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Conserved domains on  [gi|386768875|ref|NP_001245818|]
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kismet, isoform D [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
2029-2606 5.60e-156

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: 515.12  E-value: 5.60e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2029 LRPYQLEGLNWLKFSWYNTHNCILADEMGLGKTIQSLTFVHSVYEY-GIRGPFLVIAPLSTIPNWQREFEGWTDM-NVVV 2106
Cdd:PLN03142  170 MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYrGITGPHMVVAPKSTLGNWMNEIRRFCPVlRAVK 249
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2107 YHGSVTSKQMIQDYeyyyktesgkvLKEPIKFNVLITTFEMIVTDYMDLKAFNWRLCVIDEAHRLKNRNCKLLEGLRQLN 2186
Cdd:PLN03142  250 FHGNPEERAHQREE-----------LLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFS 318
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2187 LEHRVLLSGTPLQNNISELFSLLNFLEPSQFSSQEEFMSEF---GSLRTEEEVNKLQALLKPMMLRRLKDDVEKSLAPKE 2263
Cdd:PLN03142  319 TNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFqisGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKK 398
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2264 ETIIEVELTNIQKKYYRGILEQNFSFLKKGttsANIPNLMNTMMELRKCCIHPYLLNGAEEQIQYdFKSQHgedpesyyk 2343
Cdd:PLN03142  399 ETILKVGMSQMQKQYYKALLQKDLDVVNAG---GERKRLLNIAMQLRKCCNHPYLFQGAEPGPPY-TTGEH--------- 465
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2344 nLILSAGKMVLIDKLLPKLKANGHRVLIFSQMVRCLDILEDYLVYRKYPFERIDGRIRGNLRQEAIDRYSKPGSDRFVFL 2423
Cdd:PLN03142  466 -LVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFL 544
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2424 LCTKAGGLGINLTAADTVIIYDSDWNPQNDLQAQARCHRIGQRKMVKIYRLLCRNTYEREMFDKASMKLGLDKAVLQsmn 2503
Cdd:PLN03142  545 LSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQ--- 621
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2504 tQGsKDGNNKQLSKkeiEDLLKKGAYGAVMDDDNAGDKFCEEDIDSILKRRTQVITMESEKGSTFSKAS--FAASGNRSD 2581
Cdd:PLN03142  622 -QG-RLAEQKTVNK---DELLQMVRYGAEMVFSSKDSTITDEDIDRIIAKGEEATAELDAKMKKFTEDAikFKMDDTAEL 696
                         570       580       590
                  ....*....|....*....|....*....|....
gi 386768875 2582 ITIDDPDfwTKWAKKVD---------IDPDACER 2606
Cdd:PLN03142  697 YDFDDED--DKDENKLDfkkivsdnwIDPPKRER 728
CD2_tandem_CHD5-9_like cd18663
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
1937-1995 6.43e-33

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


:

Pssm-ID: 349310 [Multi-domain]  Cd Length: 59  Bit Score: 123.17  E-value: 6.43e-33
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 386768875 1937 QDFTEVDRVLDMSVHTDETSGETTKHYLVKWKSLPYEDCTWELEEDVDNDKIEQYLRFN 1995
Cdd:cd18663     1 PDYVEVDRILDVSVSTDPNTGEPVTHYLVKWCSLPYEDSTWELEEDVDPAKIEEFEKLR 59
CD1_tandem_CHD5-9_like cd18668
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
1851-1918 2.09e-27

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


:

Pssm-ID: 349315 [Multi-domain]  Cd Length: 68  Bit Score: 107.81  E-value: 2.09e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386768875 1851 EGEESVKKENDEKTEADmENKPEPVFIDVEEYFVKYRNFSYLHCEWRTEEELLKGDRRVAAKIRRFQQ 1918
Cdd:cd18668     2 EDTMIIEKILASRKKKK-EKEEGAEEIEVEEYLVKYKNFSYLHCEWKTEEELEKGDKRIKQKIKRFKQ 68
BRK pfam07533
BRK domain; The function of this domain is unknown. It is often found associated with ...
4394-4437 3.09e-18

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: 81.02  E-value: 3.09e-18
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 386768875  4394 LTGEEPVPVINKQTGKRLGGNKAPQLKRLMQWLTENPNYEVDPK 4437
Cdd:pfam07533    1 LTGDERVPVVNRKTGKKLTGDKAPKLKDLEEWLEENPGYEVDPR 44
PTZ00121 super family cl31754
MAEBL; Provisional
1419-1923 6.61e-14

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 79.41  E-value: 6.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1419 EDEKEAEAgdetVDSVPDSAGDpASTPSRRDRKRSTARSRRnanSEEGGSARKNRGSLSAKALKKRRNRGRIVPESDGED 1498
Cdd:PTZ00121 1221 EDAKKAEA----VKKAEEAKKD-AEEAKKAEEERNNEEIRK---FEEARMAHFARRQAAIKAEEARKADELKKAEEKKKA 1292
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1499 DTLDRTPPPSPPPDSEMDSNKRRSSRNTQRK-----KYIDDVMLRFSDDENSLLVASPVKKDKKPSANASNSNAGSDVEK 1573
Cdd:PTZ00121 1293 DEAKKAEEKKKADEAKKKAEEAKKADEAKKKaeeakKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKK 1372
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1574 TEpQSGAEGDAAQEVGEEKSNLPLDESSQLEASSSTSAV--AEKERQISTDAANAAMSSKPNYVYINTGDEDSMVVQLVL 1651
Cdd:PTZ00121 1373 KE-EAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELkkAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKK 1451
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1652 AMRMGKRELILDKPKE---KAPEPKQD-EEKSELDE----ATTDKPEGDEKFKTEGESKK--DLTDSEETKlesSAMEVD 1721
Cdd:PTZ00121 1452 KAEEAKKAEEAKKKAEeakKADEAKKKaEEAKKADEakkkAEEAKKKADEAKKAAEAKKKadEAKKAEEAK---KADEAK 1528
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1722 SKEESEPDDSKKSDEDNKDKDKMEVDDEVGKSDKESKPEE-------------------QSETVKTEENSKAIEEDKSST 1782
Cdd:PTZ00121 1529 KAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEakkaeedknmalrkaeeakKAEEARIEEVMKLYEEEKKMK 1608
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1783 VLTADHAKEPETVLEKMEVDEKANDDQSAVSKAEGSDEKSTDDSNPEEATTEKNKESLEIEGEKERvKEGEESVKKENDE 1862
Cdd:PTZ00121 1609 AEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK-KKAEEAKKAEEDE 1687
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386768875 1863 KTEADMENKPEPVFIDVEEYFVKYRNfsylhcEWRTEEELLKGDRRVAAKIRRFQQKQSQQ 1923
Cdd:PTZ00121 1688 KKAAEALKKEAEEAKKAEELKKKEAE------EKKKAEELKKAEEENKIKAEEAKKEAEED 1742
PTZ00341 super family cl31759
Ring-infected erythrocyte surface antigen; Provisional
3488-3713 1.33e-06

Ring-infected erythrocyte surface antigen; Provisional


The actual alignment was detected with superfamily member PTZ00341:

Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 55.18  E-value: 1.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 3488 KNEVIDLDDELMTNESVIKKEspvtpIKEEIKSEESPEKHDTADNLEDknsDAEESTKIKGKEdfNPETTEKEALDESTN 3567
Cdd:PTZ00341  907 KKDAKDLSGNIAHEINLINKE-----LKNQNENVPEHLKEHAEANIEE---DAEENVEEDAEE--NVEENVEENVEENVE 976
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 3568 LNKDKSSTETLVPEIEDSKPSEDKMEVEElPVAENGEkEGSPEKCSDAEDKKFSEEKPSSPAVPDGKVSEMEaDEAAPNT 3647
Cdd:PTZ00341  977 ENVEENVEENVEENVEENVEENVEENIEE-NVEENVE-ENIEENVEEYDEENVEEVEENVEEYDEENVEEIE-ENAEENV 1053
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386768875 3648 EENCSGDSESPEKECEDKVVEKVEEEKGENSYEKAEEQKEETEKLEKSSIESEPSEKSETVLEPEV 3713
Cdd:PTZ00341 1054 EENIEENIEEYDEENVEEIEENIEENIEENVEENVEENVEEIEENVEENVEENAEENAEENAEENA 1119
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
221-533 5.44e-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.


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 46.68  E-value: 5.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875   221 QAPGQHPLYPGVGAPTVQAGQPPTPQAYAHSPYGSPMQHQPSRgAPQHVGYGHTGLDQ-ASAYGQHVPGGAPPGHHLSAQ 299
Cdd:pfam03154  177 QSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPN-QTQSTAAPHTLIQQtPTLHPQRLPSPHPPLQPMTQP 255
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875   300 QQQAAQQLGAhqqqqlqsqqqqqaqqqqphvslMQQQQLPGAGLPPPH-MGMPPSYGSHHQQQQQQQQTQQQQQQSAPPy 378
Cdd:pfam03154  256 PPPSQVSPQP-----------------------LPQPSLHGQMPPMPHsLQTGPSHMQHPVPPQPFPLTPQSSQSQVPP- 311
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875   379 mssSKHQQAAAQLNSSPQYRAPFPQLSPQMSPR----PPTMSPHPQMSPRPVG-VSPAKPPPPQQQQQQTQAQQPQQVVS 453
Cdd:pfam03154  312 ---GPSPAAPGQSQQRIHTPPSQSQLQSQQPPReqplPPAPLSMPHIKPPPTTpIPQLPNPQSHKHPPHLSGPSPFQMNS 388
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875   454 NQPSQHSIQGMVGLPSPRP----QPPTSGAGGAGAKGPAPVAAPVNTlqaleqmvmPSQALGLPPMDYPSAYRSAVGPRM 529
Cdd:pfam03154  389 NLPPPPALKPLSSLSTHHPpsahPPPLQLMPQSQQLPPPPAQPPVLT---------QSQSLPPPAASHPPTSGLHQVPSQ 459

                   ....
gi 386768875   530 PASP 533
Cdd:pfam03154  460 SPFP 463
Med15 super family cl26621
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
1056-1265 1.39e-03

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


The actual alignment was detected with superfamily member pfam09606:

Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 45.00  E-value: 1.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875  1056 PADPIIPVTQPPQQQMPPIGMPMHPIAPGYEAQAQGQGHMPPMMPPYGGAPGmyppypmlHQQEIAALQQQIQElycMPP 1135
Cdd:pfam09606  180 PGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPADAGAQMGQQAQANGGMNP--------QQMGGAPNQVAMQQ---QQP 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875  1136 GHELQHQDKLMRMQErLNLLTQHEVNDQCAGGPQcllfQNVPPMYGPPGnPLLNQQMVESPQVSSTTGrgrgksaNKPRK 1215
Cdd:pfam09606  249 QQQGQQSQLGMGINQ-MQQMPQGVGGGAGQGGPG----QPMGPPGQQPG-AMPNVMSIGDQNNYQQQQ-------TRQQQ 315
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 386768875  1216 PRAKKGEKAQVGQQQdlmdisgNVAMGAANAVSSIPTTQLPVSEDCVTQG 1265
Cdd:pfam09606  316 QQQGGNHPAAHQQQM-------NQSVGQGGQVVALGGLNHLETWNPGNFG 358
PRK12678 super family cl36163
transcription termination factor Rho; Provisional
1319-1500 8.36e-03

transcription termination factor Rho; Provisional


The actual alignment was detected with superfamily member PRK12678:

Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 42.58  E-value: 8.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1319 PPRDRTPKAKKPKDPNDPNSTETPA-AVKKRAGASKRRKQYGEDGAEQTGE--GSEVEDNKPLVPKAGSADGEA-----E 1390
Cdd:PRK12678  105 APAARAAAAAAAEAASAPEAAQARErRERGEAARRGAARKAGEGGEQPATEarADAAERTEEEERDERRRRGDRedrqaE 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1391 TTSGGTGVDGESPDYDDIPVSKIPRGSNEDEKEAEAGDETVDSvpDSAGDPASTPSRRDRKRSTARSRRNANSEEGGSAR 1470
Cdd:PRK12678  185 AERGERGRREERGRDGDDRDRRDRREQGDRREERGRRDGGDRR--GRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRR 262
                         170       180       190
                  ....*....|....*....|....*....|
gi 386768875 1471 KNRGslsakalKKRRNRGRIVPESDGEDDT 1500
Cdd:PRK12678  263 GRRF-------RDRDRRGRRGGDGGNEREP 285
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
2029-2606 5.60e-156

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 515.12  E-value: 5.60e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2029 LRPYQLEGLNWLKFSWYNTHNCILADEMGLGKTIQSLTFVHSVYEY-GIRGPFLVIAPLSTIPNWQREFEGWTDM-NVVV 2106
Cdd:PLN03142  170 MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYrGITGPHMVVAPKSTLGNWMNEIRRFCPVlRAVK 249
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2107 YHGSVTSKQMIQDYeyyyktesgkvLKEPIKFNVLITTFEMIVTDYMDLKAFNWRLCVIDEAHRLKNRNCKLLEGLRQLN 2186
Cdd:PLN03142  250 FHGNPEERAHQREE-----------LLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFS 318
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2187 LEHRVLLSGTPLQNNISELFSLLNFLEPSQFSSQEEFMSEF---GSLRTEEEVNKLQALLKPMMLRRLKDDVEKSLAPKE 2263
Cdd:PLN03142  319 TNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFqisGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKK 398
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2264 ETIIEVELTNIQKKYYRGILEQNFSFLKKGttsANIPNLMNTMMELRKCCIHPYLLNGAEEQIQYdFKSQHgedpesyyk 2343
Cdd:PLN03142  399 ETILKVGMSQMQKQYYKALLQKDLDVVNAG---GERKRLLNIAMQLRKCCNHPYLFQGAEPGPPY-TTGEH--------- 465
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2344 nLILSAGKMVLIDKLLPKLKANGHRVLIFSQMVRCLDILEDYLVYRKYPFERIDGRIRGNLRQEAIDRYSKPGSDRFVFL 2423
Cdd:PLN03142  466 -LVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFL 544
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2424 LCTKAGGLGINLTAADTVIIYDSDWNPQNDLQAQARCHRIGQRKMVKIYRLLCRNTYEREMFDKASMKLGLDKAVLQsmn 2503
Cdd:PLN03142  545 LSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQ--- 621
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2504 tQGsKDGNNKQLSKkeiEDLLKKGAYGAVMDDDNAGDKFCEEDIDSILKRRTQVITMESEKGSTFSKAS--FAASGNRSD 2581
Cdd:PLN03142  622 -QG-RLAEQKTVNK---DELLQMVRYGAEMVFSSKDSTITDEDIDRIIAKGEEATAELDAKMKKFTEDAikFKMDDTAEL 696
                         570       580       590
                  ....*....|....*....|....*....|....
gi 386768875 2582 ITIDDPDfwTKWAKKVD---------IDPDACER 2606
Cdd:PLN03142  697 YDFDDED--DKDENKLDfkkivsdnwIDPPKRER 728
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
2029-2250 1.51e-141

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: 440.92  E-value: 1.51e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2029 LRPYQLEGLNWLKFSWYNTHNCILADEMGLGKTIQSLTFVHSVYEY-GIRGPFLVIAPLSTIPNWQREFEGWTDMNVVVY 2107
Cdd:cd17995     1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVeGIRGPFLVIAPLSTIPNWQREFETWTDMNVVVY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2108 HGSVTSKQMIQDYEYYYKTESGKVLKEPIKFNVLITTFEMIVTDYMDLKAFNWRLCVIDEAHRLKNRNCKLLEGLRQLNL 2187
Cdd:cd17995    81 HGSGESRQIIQQYEMYFKDAQGRKKKGVYKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKLTL 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386768875 2188 EHRVLLSGTPLQNNISELFSLLNFLEPSQFSSQEEFMSEFGSLRTEEEVNKLQALLKPMMLRR 2250
Cdd:cd17995   161 EHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFGDLKTAEQVEKLQALLKPYMLRR 223
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
2028-2500 2.86e-123

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: 2.86e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2028 SLRPYQLEGLNWLKFSWYNTHNCILADEMGLGKTIQSLTFVHSVYEYGIRGPFLVIAPLSTIPNWQREFEGWT-DMNVVV 2106
Cdd:COG0553   241 TLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELAKFApGLRVLV 320
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2107 YHGSVTSKQMIQDYEyyyktesgkvlkepiKFNVLITTFEMIVTDYMDLKAFNWRLCVIDEAHRLKNRNCKLLEGLRQLN 2186
Cdd:COG0553   321 LDGTRERAKGANPFE---------------DADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALK 385
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2187 LEHRVLLSGTPLQNNISELFSLLNFLEPSQFSSQEEFMSEFGSL---RTEEEVNKLQALLKPMMLRRLKDDVEKSLAPKE 2263
Cdd:COG0553   386 ARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPiekGDEEALERLRRLLRPFLLRRTKEDVLKDLPEKT 465
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2264 ETIIEVELTNIQKKYYRGILEQnfsFLKKGTTSANIPNLMN---TMMELRKCCIHPYLLNgaEEQIQYDFKSqhgedpes 2340
Cdd:COG0553   466 EETLYVELTPEQRALYEAVLEY---LRRELEGAEGIRRRGLilaALTRLRQICSHPALLL--EEGAELSGRS-------- 532
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2341 yyknlilsaGKMVLIDKLLPKLKANGHRVLIFSQMVRCLDILEDYLVYRKYPFERIDGRIRGNLRQEAIDRYSKpGSDRF 2420
Cdd:COG0553   533 ---------AKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQE-GPEAP 602
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2421 VFLLCTKAGGLGINLTAADTVIIYDSDWNPQNDLQAQARCHRIGQRKMVKIYRLLCRNTYEREMFDKASMKLGLDKAVLQ 2500
Cdd:COG0553   603 VFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
2032-2319 7.50e-91

SNF2-related domain; This domain is found in proteins involved in a variety of processes including transcription regulation (e.g., SNF2, STH1, brahma, MOT1), DNA repair (e.g., ERCC6, RAD16, RAD5), DNA recombination (e.g., RAD54), and chromatin unwinding (e.g., ISWI) as well as a variety of other proteins with little functional information (e.g., lodestar, ETL1). SNF2 functions as the ATPase component of the SNF2/SWI multisubunit complex, which utilizes energy derived from ATP hydrolysis to disrupt histone-DNA interactions, resulting in the increased accessibility of DNA to transcription factors.


Pssm-ID: 425504 [Multi-domain]  Cd Length: 289  Bit Score: 298.44  E-value: 7.50e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875  2032 YQLEGLNWLKFSWYNT-HNCILADEMGLGKTIQSLTFVHSVYEYGI--RGPFLVIAPLSTIPNWQREFEGWT---DMNVV 2105
Cdd:pfam00176    1 YQIEGVNWMLSLENNLgRGGILADEMGLGKTLQTISLLLYLKHVDKnwGGPTLIVVPLSLLHNWMNEFERWVsppALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875  2106 VYHGsVTSKQMIQdyeyyykTESGKVLKepiKFNVLITTFEMIVTDYMDLKAFNWRLCVIDEAHRLKNRNCKLLEGLRQL 2185
Cdd:pfam00176   81 VLHG-NKRPQERW-------KNDPNFLA---DFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSL 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875  2186 NLEHRVLLSGTPLQNNISELFSLLNFLEPSQFSSQEEFMSEFG--SLRTEEE--VNKLQALLKPMMLRRLKDDVEKSLAP 2261
Cdd:pfam00176  150 KTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDrpIERGGGKkgVSRLHKLLKPFLLRRTKKDVEKSLPP 229
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875  2262 KEETIIEVELTNIQKKYY-RGILEQNFSFLKKGTTSANIP-NLMNTMMELRKCCIHPYLL 2319
Cdd:pfam00176  230 KVEYILFCRLSKLQRKLYqTFLLKKDLNAIKTGEGGREIKaSLLNILMRLRKICNHPGLI 289
CD2_tandem_CHD5-9_like cd18663
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
1937-1995 6.43e-33

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


Pssm-ID: 349310 [Multi-domain]  Cd Length: 59  Bit Score: 123.17  E-value: 6.43e-33
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 386768875 1937 QDFTEVDRVLDMSVHTDETSGETTKHYLVKWKSLPYEDCTWELEEDVDNDKIEQYLRFN 1995
Cdd:cd18663     1 PDYVEVDRILDVSVSTDPNTGEPVTHYLVKWCSLPYEDSTWELEEDVDPAKIEEFEKLR 59
DEXDc smart00487
DEAD-like helicases superfamily;
2023-2215 1.38e-27

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 113.36  E-value: 1.38e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875   2023 YKGGNSLRPYQLEGLNWLKFSWyntHNCILADEMGLGKTIQSLTFVHSVYEYGIRGPFLVIAPL-STIPNWQREFEGWTD 2101
Cdd:smart00487    3 KFGFEPLRPYQKEAIEALLSGL---RDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTrELAEQWAEELKKLGP 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875   2102 ----MNVVVYHGSVTSKQMiqdyeyyYKTESGkvlkepiKFNVLITTFEMIVTDYMD--LKAFNWRLCVIDEAHRLKN-- 2173
Cdd:smart00487   80 slglKVVGLYGGDSKREQL-------RKLESG-------KTDILVTTPGRLLDLLENdkLSLSNVDLVILDEAHRLLDgg 145
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|....*.
gi 386768875   2174 RNCKLLEGLRQLNLE-HRVLLSGTP---LQNNISELFSLLNFLEPS 2215
Cdd:smart00487  146 FGDQLEKLLKLLPKNvQLLLLSATPpeeIENLLELFLNDPVFIDVG 191
CD1_tandem_CHD5-9_like cd18668
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
1851-1918 2.09e-27

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


Pssm-ID: 349315 [Multi-domain]  Cd Length: 68  Bit Score: 107.81  E-value: 2.09e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386768875 1851 EGEESVKKENDEKTEADmENKPEPVFIDVEEYFVKYRNFSYLHCEWRTEEELLKGDRRVAAKIRRFQQ 1918
Cdd:cd18668     2 EDTMIIEKILASRKKKK-EKEEGAEEIEVEEYLVKYKNFSYLHCEWKTEEELEKGDKRIKQKIKRFKQ 68
DISARM_DrmD_b NF038318
DISARM system SNF2-like helicase DrmD, short form; DrmD, a SNF2-like helicase, is a component ...
1988-2498 6.53e-26

DISARM system SNF2-like helicase DrmD, short form; DrmD, a SNF2-like helicase, is a component of class 1 DISARM (Defence Island System Associated with Restriction Modification), which contains a DNA adenine N6 methyltransferase. This HMM describes a distinct form that is somewhat shorter than the majority of DrmD proteins.


Pssm-ID: 468472 [Multi-domain]  Cd Length: 868  Bit Score: 118.25  E-value: 6.53e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1988 IEQYLRFNKIpqrsewkskkrphpelwkKLEKTPVYKGGNS---LRPYQLEG----LNWLKfswynTHNCILADEMGLGK 2060
Cdd:NF038318    4 LEQYARYKRQ------------------ELEKSPYHCLLMAdidPNPHQINAfcaaIAALK-----TGGIILADEVGLGK 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2061 TIQSLTFVHSVYEYGIRgPFLVIAPLSTIPNWQREFEGWTDMNVVVyhgsVTSKQMIQDYEYYYKTesgkvLKEPIKFNV 2140
Cdd:NF038318   61 TIEAGLVLKYVLESGAK-KILIILPANLRKQWEIELEEKFDLESLI----LDSLTVEKDAKKWNKR-----LTDNKKVRI 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2141 LITTFemivtDY--MDLKAF---NWRLCVIDEAHRLKN--RNCKLLEGLRQLNLE-HRVLLSGTPLQNNISELFSLLNFL 2212
Cdd:NF038318  131 VITSY-----DYasKLMKRFpkvKWDFIIIDEAHNLRNvhKGGKRAKNLYELTKGiPKILLTATPLQNSLLDLYGLVSFI 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2213 EPSQFSSQEEFMSEFgsLRTEEeVNKLQALLKPMMLRRLKDDVEKSLAPKEETII---------EVEL----TNIQKKYY 2279
Cdd:NF038318  206 DPRIFGSEKVFSKRY--IKDED-YSDLKRELSPVLYRTLRKDVADYMQFKKRKCItvdfelspdEIELyvrvNNFLKRDI 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2280 --------RG----------------------ILEQNFSFLKKGTTSANIPNLMNTMMElrkccihpYLlngAEEQIQYD 2329
Cdd:NF038318  283 lysiptsnRTliilvirkllasssfalaetfeVLKKRLEKLKEGTRSANAQEGFDLFWS--------FV---EDEIDESG 351
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2330 FKSQHGED---------------------PESYYKNLILSAGKMVlIDKLLPKLKANG--HRVLIFSQMVRCLDILEDYL 2386
Cdd:NF038318  352 FEEKQDELytrqkefiqheidevdaiidvAKRIKTNAKVTALKTA-LEIAFEYQREEGiaQKVVVFTESKRTQKYIAEEL 430
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2387 VYRKYPFERI---DGRIRGNLRQE-----------------------AIDRYSKpgsDRFVFLLCTKAGGLGINLTAADT 2440
Cdd:NF038318  431 RKSGYEGEDIllfNGDFDDAMTKEiyrawqvknygkanygrsveykhAIVDYFK---NNAKILIVTDAGSEGLNLQFCNT 507
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 386768875 2441 VIIYDSDWNPQNDLQAQARCHRIGQRKMVKIYRLL-CRNTYEREMFDKASMKLGLDKAV 2498
Cdd:NF038318  508 VINYDLPWNPQKIEQRIGRCHRYGQKNDVVAINLLnTQNVADKRVYEILSEKFELFEGV 566
BRK pfam07533
BRK domain; The function of this domain is unknown. It is often found associated with ...
4394-4437 3.09e-18

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: 81.02  E-value: 3.09e-18
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 386768875  4394 LTGEEPVPVINKQTGKRLGGNKAPQLKRLMQWLTENPNYEVDPK 4437
Cdd:pfam07533    1 LTGDERVPVVNRKTGKKLTGDKAPKLKDLEEWLEENPGYEVDPR 44
BRK smart00592
domain in transcription and CHROMO domain helicases;
4395-4439 3.22e-17

domain in transcription and CHROMO domain helicases;


Pssm-ID: 197800  Cd Length: 45  Bit Score: 78.16  E-value: 3.22e-17
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 386768875   4395 TGEEPVPVINKQTGKRLGGNKAPQLKRLMQWLTENPNYEVDPKWL 4439
Cdd:smart00592    1 DGEERVPVINRETGKKLTGDDAPKAKDLERWLEENPEYEVAPRSA 45
PTZ00121 PTZ00121
MAEBL; Provisional
1419-1923 6.61e-14

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 79.41  E-value: 6.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1419 EDEKEAEAgdetVDSVPDSAGDpASTPSRRDRKRSTARSRRnanSEEGGSARKNRGSLSAKALKKRRNRGRIVPESDGED 1498
Cdd:PTZ00121 1221 EDAKKAEA----VKKAEEAKKD-AEEAKKAEEERNNEEIRK---FEEARMAHFARRQAAIKAEEARKADELKKAEEKKKA 1292
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1499 DTLDRTPPPSPPPDSEMDSNKRRSSRNTQRK-----KYIDDVMLRFSDDENSLLVASPVKKDKKPSANASNSNAGSDVEK 1573
Cdd:PTZ00121 1293 DEAKKAEEKKKADEAKKKAEEAKKADEAKKKaeeakKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKK 1372
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1574 TEpQSGAEGDAAQEVGEEKSNLPLDESSQLEASSSTSAV--AEKERQISTDAANAAMSSKPNYVYINTGDEDSMVVQLVL 1651
Cdd:PTZ00121 1373 KE-EAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELkkAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKK 1451
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1652 AMRMGKRELILDKPKE---KAPEPKQD-EEKSELDE----ATTDKPEGDEKFKTEGESKK--DLTDSEETKlesSAMEVD 1721
Cdd:PTZ00121 1452 KAEEAKKAEEAKKKAEeakKADEAKKKaEEAKKADEakkkAEEAKKKADEAKKAAEAKKKadEAKKAEEAK---KADEAK 1528
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1722 SKEESEPDDSKKSDEDNKDKDKMEVDDEVGKSDKESKPEE-------------------QSETVKTEENSKAIEEDKSST 1782
Cdd:PTZ00121 1529 KAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEakkaeedknmalrkaeeakKAEEARIEEVMKLYEEEKKMK 1608
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1783 VLTADHAKEPETVLEKMEVDEKANDDQSAVSKAEGSDEKSTDDSNPEEATTEKNKESLEIEGEKERvKEGEESVKKENDE 1862
Cdd:PTZ00121 1609 AEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK-KKAEEAKKAEEDE 1687
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386768875 1863 KTEADMENKPEPVFIDVEEYFVKYRNfsylhcEWRTEEELLKGDRRVAAKIRRFQQKQSQQ 1923
Cdd:PTZ00121 1688 KKAAEALKKEAEEAKKAEELKKKEAE------EKKKAEELKKAEEENKIKAEEAKKEAEED 1742
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
1941-1993 1.61e-12

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 64.91  E-value: 1.61e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 386768875  1941 EVDRVLDMSVhtdetSGETTKHYLVKWKSLPYEDCTWELEEDVDNDK--IEQYLR 1993
Cdd:pfam00385    2 EVERILDHRK-----DKGGKEEYLVKWKGYPYDENTWEPEENLSKCPelIEEFKD 51
MDN1 COG5271
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ...
1242-1881 1.20e-11

Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444083 [Multi-domain]  Cd Length: 1028  Bit Score: 71.97  E-value: 1.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1242 GAANAVSSIPTTQLPVSEDCVTQGAGDTSVVGMLEYSEGMGDLSQDVHSANELDTSTDGSGKKKKPRKPRTPKDPNKPPR 1321
Cdd:COG5271   289 LDAELTAAQAADPESDDDADDSTLAALEGAAEDTEIATADELAAADDEDDDDSAAEDAAEEAATAEDSAAEDTQDAEDEA 368
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1322 DRTPKAKKPKDPNDPNSTETPAAVKKRAGASKRRKQYGEDGAEQTGEGSEVEDNKPLVPKAGSADGEAETTSGGTGVDGE 1401
Cdd:COG5271   369 AGEAADESEGADTDAAADEADAAADDSADDEEASADGGTSPTSDTDEEEEEADEDASAGETEDESTDVTSAEDDIATDEE 448
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1402 SPDYDDIPVSKIPRGSNEDEKEAEAGDETVDSVPDSAGDPASTPSRRDRKRSTARSRRNANSEEGGSARKNRGSLSAKAL 1481
Cdd:COG5271   449 ADSLADEEEEAEAELDTEEDTESAEEDADGDEATDEDDASDDGDEEEAEEDAEAEADSDELTAEETSADDGADTDAAADP 528
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1482 KKRRNRGR-----IVPESDGEDDTLDRTPPPSPPPDSEMDSNKRRSSRNTQRKKYIDDVMLRFSDDENsllvASPVKKDK 1556
Cdd:COG5271   529 EDSDEDALedeteGEENAPGSDQDADETDEPEATAEEDEPDEAEAETEDATENADADETEESADESEE----AEASEDEA 604
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1557 KPSANASNSNAGSDVEKTEPQSGAEGDAAQEVGEEKSN-LPLDESSQLEASSSTSAVAEKERQISTDAANAAmSSKPNY- 1634
Cdd:COG5271   605 AEEEEADDDEADADADGAADEEETEEEAAEDEAAEPETdASEAADEDADAETEAEASADESEEEAEDESETS-SEDAEEd 683
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1635 ----VYINTGDEDSMVVqlvlamRMGKRELILDKPKEKAPEPKQDEEKSELDEATTDKPEGDEKfKTEGESKKDLTDSEE 1710
Cdd:COG5271   684 adaaAAEASDDEEETEE------ADEDAETASEEADAEEADTEADGTAEEAEEAAEEAESADEE-AASLPDEADAEEEAE 756
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1711 TKLESSAMEVDSKEESEPDDSKKSDEDNKDKDKMEVDDEVGKSDKESKPEEQSETVKTEENSKAIEEDKSSTVLTADHAK 1790
Cdd:COG5271   757 EAEEAEEDDADGLEEALEEEKADAEEAATDEEAEAAAEEKEKVADEDQDTDEDALLDEAEADEEEDLDGEDEETADEALE 836
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1791 EPETVLEKMEVDEKANDDQSAVSKAEGSDEKSTDDSNPEEATTEKNKESLEIEGEKERVKEGEESVKKENDEKTEADMEN 1870
Cdd:COG5271   837 DIEAGIAEDDEEDDDAAAAKDVDADLDLDADLAADEHEAEEAQEAETDADADADAGEADSSGESSAAAEDDDAAEDADSD 916
                         650
                  ....*....|.
gi 386768875 1871 KPEPVFIDVEE 1881
Cdd:COG5271   917 DGANDEDDDDD 927
CHROMO smart00298
Chromatin organization modifier domain;
1941-1993 5.04e-09

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 55.30  E-value: 5.04e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 386768875   1941 EVDRVLDMSVHtdetsGETTKHYLVKWKSLPYEDCTWELEEDVDND--KIEQYLR 1993
Cdd:smart00298    3 EVEKILDHRWK-----KKGELEYLVKWKGYSYSEDTWEPEENLLNCskKLDNYKK 52
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
1335-1792 3.24e-07

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


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 57.23  E-value: 3.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1335 DPNSTETPAAVKKRAGASK----RRKQYGEDGAEQTGEGSEVEDNKPLVPKAGSADGEAETTSGGTGVDGESPDYDDipv 1410
Cdd:NF033609  496 DPNSKGDLALRSTLYGYNSniiwRSMSWDNEVAFNNGSGSGDGIDKPVVPEQPDEPGEIEPIPEDSDSDPGSDSGSD--- 572
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1411 skiprGSNEDEKEAEAGDETVDSVPDSAGDPASTPSRRDRKRSTARSRRNANSEEGGSARKNRGSLSAKAlkkrrnrgri 1490
Cdd:NF033609  573 -----SSNSDSGSDSGSDSTSDSGSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSA---------- 637
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1491 vPESDGEDDTlDRTPPPSPPPDSEMDSNKRRSSRNTQRKKYIDDVMLRFSDDENSllvaspvkkdKKPSANASNSNAGSD 1570
Cdd:NF033609  638 -SDSDSDSDS-DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS----------DSDSDSDSDSDSDSD 705
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1571 VEkTEPQSGAEGDAAQEvGEEKSNLPLDESSQLEASSSTSAVAEKERQISTDAANAAMSSKpnyvyintgDEDSmvvqlv 1650
Cdd:NF033609  706 SD-SDSDSDSDSDSDSD-SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS---------DSDS------ 768
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1651 lamrmgkrelilDKPKEKAPEPKQDEEkSELDEATTDKPEGDEKFKTEGESKKDlTDSEETKLESSAMEVDSKEESEPDD 1730
Cdd:NF033609  769 ------------DSDSDSDSDSDSDSD-SDSDSDSDSDSDSDSDSDSDSDSDSD-SDSDSDSDSDSDSDSDSDSDSDSDS 834
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386768875 1731 SKKSDEDN-KDKDKMEVDDEVGKSDKESKPEEQSETVKTEENSKAiEEDKSSTVLTADHAKEP 1792
Cdd:NF033609  835 DSDSDSDSdSDSDSDSDSDSDSESDSNSDSESGSNNNVVPPNSPK-NGTNASNKNEAKDSKEP 896
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
3488-3713 1.33e-06

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 55.18  E-value: 1.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 3488 KNEVIDLDDELMTNESVIKKEspvtpIKEEIKSEESPEKHDTADNLEDknsDAEESTKIKGKEdfNPETTEKEALDESTN 3567
Cdd:PTZ00341  907 KKDAKDLSGNIAHEINLINKE-----LKNQNENVPEHLKEHAEANIEE---DAEENVEEDAEE--NVEENVEENVEENVE 976
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 3568 LNKDKSSTETLVPEIEDSKPSEDKMEVEElPVAENGEkEGSPEKCSDAEDKKFSEEKPSSPAVPDGKVSEMEaDEAAPNT 3647
Cdd:PTZ00341  977 ENVEENVEENVEENVEENVEENVEENIEE-NVEENVE-ENIEENVEEYDEENVEEVEENVEEYDEENVEEIE-ENAEENV 1053
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386768875 3648 EENCSGDSESPEKECEDKVVEKVEEEKGENSYEKAEEQKEETEKLEKSSIESEPSEKSETVLEPEV 3713
Cdd:PTZ00341 1054 EENIEENIEEYDEENVEEIEENIEENIEENVEENVEENVEEIEENVEENVEENAEENAEENAEENA 1119
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
1532-1867 1.40e-06

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


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 55.30  E-value: 1.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1532 IDDVMLRFSDDENSLLVASPVKKDKKPSanasnSNAGSDVEKTEPQSGAEGDAAQEVGEEKSNLPLDESSQLEASSSTSA 1611
Cdd:NF033609  539 IDKPVVPEQPDEPGEIEPIPEDSDSDPG-----SDSGSDSSNSDSGSDSGSDSTSDSGSDSASDSDSASDSDSASDSDSA 613
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1612 VAEKERQISTDAANAAMSSKPNYVYINTGDEDSMVVQLVLAMRMGKRELILDKPKEKAPEPKQDEEKSELDEATTDKpEG 1691
Cdd:NF033609  614 SDSDSASDSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS-DS 692
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1692 DEKFKTEGESKKDlTDSEETKLESSAMEVDSKEESEPDDSKKSDEDNkDKDKMEVDDEVGKSDKESKPEEQSETvKTEEN 1771
Cdd:NF033609  693 DSDSDSDSDSDSD-SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS-DSDSDSDSDSDSDSDSDSDSDSDSDS-DSDSD 769
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1772 SKAIEEDKSSTVLTADHAKEPETVLEKMEVDEKANDDQSAVSKAEGSDEKSTDDSNPEEATTEKNKESLEIEGEKERVKE 1851
Cdd:NF033609  770 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 849
                         330
                  ....*....|....*.
gi 386768875 1852 GEESVKKENDEKTEAD 1867
Cdd:NF033609  850 SDSDSDSESDSNSDSE 865
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
1572-1859 5.01e-06

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 53.46  E-value: 5.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875  1572 EKTEPQSGAEGDAAQEVGEEKSNlplDESSQLEASSSTSAVAEKERQISTDAANAAMSSKPNYvyinTGDEDSMVVQLVl 1651
Cdd:TIGR00927  647 EEGERPTEAEGENGEESGGEAEQ---EGETETKGENESEGEIPAERKGEQEGEGEIEAKEADH----KGETEAEEVEHE- 718
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875  1652 amrmgkrelilDKPKEKAPEPKQDEEKSELDEATTDKPEGDEKFKTEGESKKDLTDSEETKLESSAMEVDSKE---ESEP 1728
Cdd:TIGR00927  719 -----------GETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEgeiQAGE 787
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875  1729 DDSKKSDEDNKDKDKMEvddEVGKSDKESKPEEQSETVKTEENSKAIEEDKSSTVLTADHAKEpetvlekmevDEKANDD 1808
Cdd:TIGR00927  788 DGEMKGDEGAEGKVEHE---GETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQ----------DEKGVDG 854
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 386768875  1809 QSAVSKAEGSDEKSTDDSNPEEATTEKNKESLEIEGEKERVKEGEESVKKE 1859
Cdd:TIGR00927  855 GGGSDGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENEEPLSLEWPETRQKQ 905
DMP1 pfam07263
Dentin matrix protein 1 (DMP1); This family consists of several mammalian dentin matrix ...
1359-1747 7.78e-06

Dentin matrix protein 1 (DMP1); This family consists of several mammalian dentin matrix protein 1 (DMP1) sequences. The dentin matrix acidic phosphoprotein 1 (DMP1) gene has been mapped to human chromosome 4q21. DMP1 is a bone and teeth specific protein initially identified from mineralized dentin. DMP1 is primarily localized in the nuclear compartment of undifferentiated osteoblasts. In the nucleus, DMP1 acts as a transcriptional component for activation of osteoblast-specific genes like osteocalcin. During the early phase of osteoblast maturation, Ca(2+) surges into the nucleus from the cytoplasm, triggering the phosphorylation of DMP1 by a nuclear isoform of casein kinase II. This phosphorylated DMP1 is then exported out into the extracellular matrix, where it regulates nucleation of hydroxyapatite. DMP1 is a unique molecule that initiates osteoblast differentiation by transcription in the nucleus and orchestrates mineralized matrix formation extracellularly, at later stages of osteoblast maturation. The DMP1 gene has been found to be ectopically expressed in lung cancer although the reason for this is unknown.


Pssm-ID: 462128 [Multi-domain]  Cd Length: 519  Bit Score: 52.24  E-value: 7.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875  1359 GEDGAEQTGEGSEVEDNKPLV---PKAGSADGEAETTSG--GTGVDGESPDYDdipvskiprgSNEDEKEAEAGDetvds 1433
Cdd:pfam07263  153 GEDSAQDTTSESRDLDNEDEVssrPESGDSTQDSESEEHwvGGGSEGDSSHGD----------GSEFDDEGMQSD----- 217
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875  1434 vpdsagDPASTPSRRDRKR---STARSRRNANSEEGGSARKNRGSLSAKALKKRRNRGRIVPESDGEDDTLDRTPPPSPP 1510
Cdd:pfam07263  218 ------DPDSIRSERGNSRmssASVKSKESKGDSEQASTQDSGDSQSVEYPSRKFFRKSRISEEDDRGELDDSNTMEEVK 291
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875  1511 PDSEMDSNKRrssrntqrkkyiddvmlrfsddensllvaspvkkDKKPSANASNSNAGSDVEKTEPQSGAEGDAAQEVGE 1590
Cdd:pfam07263  292 SDSTESTSSK----------------------------------EAGLSQSREDSKSESQEDSEESQSQEDSQNSQDPSS 337
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875  1591 EKSNlPLDESSQLEASSSTSAVAEKERQISTDAANAAMSSKPNYvyiNTGDEDSmvvqlvlamrmgkreliLDKPKEKAP 1670
Cdd:pfam07263  338 ESSQ-EADLPSQESSSESQEEVVSESRGDNPDNTSSSEEDQEDS---DSSEEDS-----------------LSTFSSSES 396
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875  1671 EPKQDEEKSELDEATTDKPEGDEKFKTEGESKKDLTDSEETKLESSAMEVD--------------------SKEESEPDD 1730
Cdd:pfam07263  397 ESREEQADSESNESLRSSEESPESSEDENSSSQEGLQSHSASTESQSEESQseqdsqseeddesdsqdssrSKEDSNSTE 476
                          410
                   ....*....|....*..
gi 386768875  1731 SKKSDEDNKDKDKMEVD 1747
Cdd:pfam07263  477 STSSSEEDGQSKNMEIE 493
CHROMO smart00298
Chromatin organization modifier domain;
1879-1921 3.66e-05

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 44.13  E-value: 3.66e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 386768875   1879 VEEYFVKYRNFSYLHCEWRTEEELLKGDRrvaaKIRRFQQKQS 1921
Cdd:smart00298   17 ELEYLVKWKGYSYSEDTWEPEENLLNCSK----KLDNYKKKER 55
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
1879-1919 8.39e-05

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 42.95  E-value: 8.39e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 386768875  1879 VEEYFVKYRNFSYLHCEWRTEEELLKGDRrvaaKIRRFQQK 1919
Cdd:pfam00385   16 KEEYLVKWKGYPYDENTWEPEENLSKCPE----LIEEFKDR 52
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
221-533 5.44e-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: 46.68  E-value: 5.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875   221 QAPGQHPLYPGVGAPTVQAGQPPTPQAYAHSPYGSPMQHQPSRgAPQHVGYGHTGLDQ-ASAYGQHVPGGAPPGHHLSAQ 299
Cdd:pfam03154  177 QSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPN-QTQSTAAPHTLIQQtPTLHPQRLPSPHPPLQPMTQP 255
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875   300 QQQAAQQLGAhqqqqlqsqqqqqaqqqqphvslMQQQQLPGAGLPPPH-MGMPPSYGSHHQQQQQQQQTQQQQQQSAPPy 378
Cdd:pfam03154  256 PPPSQVSPQP-----------------------LPQPSLHGQMPPMPHsLQTGPSHMQHPVPPQPFPLTPQSSQSQVPP- 311
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875   379 mssSKHQQAAAQLNSSPQYRAPFPQLSPQMSPR----PPTMSPHPQMSPRPVG-VSPAKPPPPQQQQQQTQAQQPQQVVS 453
Cdd:pfam03154  312 ---GPSPAAPGQSQQRIHTPPSQSQLQSQQPPReqplPPAPLSMPHIKPPPTTpIPQLPNPQSHKHPPHLSGPSPFQMNS 388
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875   454 NQPSQHSIQGMVGLPSPRP----QPPTSGAGGAGAKGPAPVAAPVNTlqaleqmvmPSQALGLPPMDYPSAYRSAVGPRM 529
Cdd:pfam03154  389 NLPPPPALKPLSSLSTHHPpsahPPPLQLMPQSQQLPPPPAQPPVLT---------QSQSLPPPAASHPPTSGLHQVPSQ 459

                   ....
gi 386768875   530 PASP 533
Cdd:pfam03154  460 SPFP 463
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
1334-1673 5.47e-04

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


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 46.44  E-value: 5.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1334 NDPNSTETPAAVKKRAGASKRRKQYGEDGAEQTGEGSEVE---DNKPLVPKAGSADGEAETTSGGTGVDGESPDYDDIPV 1410
Cdd:NF033609  602 SDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDsdsDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 681
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1411 SKIPRGSNEDEKEAEAGDETVDSVPDSAGDPASTPSRRDRKRSTARSRRNANSEEGGSARKNRGSLSAKALKKrrnrgri 1490
Cdd:NF033609  682 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS------- 754
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1491 vpESDGEDDTlDRTPPPSPPPDSEMDSNKRRSSRNTQRKKYIDDVMLRFSDDENSLLVASPVKKDKKPSANASNSNAGSD 1570
Cdd:NF033609  755 --DSDSDSDS-DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 831
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1571 VEKTEPQSGAEGDAAQEVGEEKSNLPLDESSQLEASSSTSAVAEKERQISTDAANAAMSSKPNYVYINTGDEDSMVVQLV 1650
Cdd:NF033609  832 SDSDSDSDSDSDSDSDSDSDSDSDSESDSNSDSESGSNNNVVPPNSPKNGTNASNKNEAKDSKEPLPDTGSEDEANTSLI 911
                         330       340
                  ....*....|....*....|...
gi 386768875 1651 LAMRMGKRELILDKPKEKAPEPK 1673
Cdd:NF033609  912 WGLLASLGSLLLFRRKKENKDKK 934
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
1056-1265 1.39e-03

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


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 45.00  E-value: 1.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875  1056 PADPIIPVTQPPQQQMPPIGMPMHPIAPGYEAQAQGQGHMPPMMPPYGGAPGmyppypmlHQQEIAALQQQIQElycMPP 1135
Cdd:pfam09606  180 PGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPADAGAQMGQQAQANGGMNP--------QQMGGAPNQVAMQQ---QQP 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875  1136 GHELQHQDKLMRMQErLNLLTQHEVNDQCAGGPQcllfQNVPPMYGPPGnPLLNQQMVESPQVSSTTGrgrgksaNKPRK 1215
Cdd:pfam09606  249 QQQGQQSQLGMGINQ-MQQMPQGVGGGAGQGGPG----QPMGPPGQQPG-AMPNVMSIGDQNNYQQQQ-------TRQQQ 315
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 386768875  1216 PRAKKGEKAQVGQQQdlmdisgNVAMGAANAVSSIPTTQLPVSEDCVTQG 1265
Cdd:pfam09606  316 QQQGGNHPAAHQQQM-------NQSVGQGGQVVALGGLNHLETWNPGNFG 358
PRK12678 PRK12678
transcription termination factor Rho; Provisional
1319-1500 8.36e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 42.58  E-value: 8.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1319 PPRDRTPKAKKPKDPNDPNSTETPA-AVKKRAGASKRRKQYGEDGAEQTGE--GSEVEDNKPLVPKAGSADGEA-----E 1390
Cdd:PRK12678  105 APAARAAAAAAAEAASAPEAAQARErRERGEAARRGAARKAGEGGEQPATEarADAAERTEEEERDERRRRGDRedrqaE 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1391 TTSGGTGVDGESPDYDDIPVSKIPRGSNEDEKEAEAGDETVDSvpDSAGDPASTPSRRDRKRSTARSRRNANSEEGGSAR 1470
Cdd:PRK12678  185 AERGERGRREERGRDGDDRDRRDRREQGDRREERGRRDGGDRR--GRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRR 262
                         170       180       190
                  ....*....|....*....|....*....|
gi 386768875 1471 KNRGslsakalKKRRNRGRIVPESDGEDDT 1500
Cdd:PRK12678  263 GRRF-------RDRDRRGRRGGDGGNEREP 285
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
2029-2606 5.60e-156

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 515.12  E-value: 5.60e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2029 LRPYQLEGLNWLKFSWYNTHNCILADEMGLGKTIQSLTFVHSVYEY-GIRGPFLVIAPLSTIPNWQREFEGWTDM-NVVV 2106
Cdd:PLN03142  170 MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYrGITGPHMVVAPKSTLGNWMNEIRRFCPVlRAVK 249
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2107 YHGSVTSKQMIQDYeyyyktesgkvLKEPIKFNVLITTFEMIVTDYMDLKAFNWRLCVIDEAHRLKNRNCKLLEGLRQLN 2186
Cdd:PLN03142  250 FHGNPEERAHQREE-----------LLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFS 318
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2187 LEHRVLLSGTPLQNNISELFSLLNFLEPSQFSSQEEFMSEF---GSLRTEEEVNKLQALLKPMMLRRLKDDVEKSLAPKE 2263
Cdd:PLN03142  319 TNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFqisGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKK 398
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2264 ETIIEVELTNIQKKYYRGILEQNFSFLKKGttsANIPNLMNTMMELRKCCIHPYLLNGAEEQIQYdFKSQHgedpesyyk 2343
Cdd:PLN03142  399 ETILKVGMSQMQKQYYKALLQKDLDVVNAG---GERKRLLNIAMQLRKCCNHPYLFQGAEPGPPY-TTGEH--------- 465
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2344 nLILSAGKMVLIDKLLPKLKANGHRVLIFSQMVRCLDILEDYLVYRKYPFERIDGRIRGNLRQEAIDRYSKPGSDRFVFL 2423
Cdd:PLN03142  466 -LVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFL 544
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2424 LCTKAGGLGINLTAADTVIIYDSDWNPQNDLQAQARCHRIGQRKMVKIYRLLCRNTYEREMFDKASMKLGLDKAVLQsmn 2503
Cdd:PLN03142  545 LSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQ--- 621
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2504 tQGsKDGNNKQLSKkeiEDLLKKGAYGAVMDDDNAGDKFCEEDIDSILKRRTQVITMESEKGSTFSKAS--FAASGNRSD 2581
Cdd:PLN03142  622 -QG-RLAEQKTVNK---DELLQMVRYGAEMVFSSKDSTITDEDIDRIIAKGEEATAELDAKMKKFTEDAikFKMDDTAEL 696
                         570       580       590
                  ....*....|....*....|....*....|....
gi 386768875 2582 ITIDDPDfwTKWAKKVD---------IDPDACER 2606
Cdd:PLN03142  697 YDFDDED--DKDENKLDfkkivsdnwIDPPKRER 728
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
2029-2250 1.51e-141

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: 440.92  E-value: 1.51e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2029 LRPYQLEGLNWLKFSWYNTHNCILADEMGLGKTIQSLTFVHSVYEY-GIRGPFLVIAPLSTIPNWQREFEGWTDMNVVVY 2107
Cdd:cd17995     1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVeGIRGPFLVIAPLSTIPNWQREFETWTDMNVVVY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2108 HGSVTSKQMIQDYEYYYKTESGKVLKEPIKFNVLITTFEMIVTDYMDLKAFNWRLCVIDEAHRLKNRNCKLLEGLRQLNL 2187
Cdd:cd17995    81 HGSGESRQIIQQYEMYFKDAQGRKKKGVYKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKLTL 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386768875 2188 EHRVLLSGTPLQNNISELFSLLNFLEPSQFSSQEEFMSEFGSLRTEEEVNKLQALLKPMMLRR 2250
Cdd:cd17995   161 EHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFGDLKTAEQVEKLQALLKPYMLRR 223
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
2028-2500 2.86e-123

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: 2.86e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2028 SLRPYQLEGLNWLKFSWYNTHNCILADEMGLGKTIQSLTFVHSVYEYGIRGPFLVIAPLSTIPNWQREFEGWT-DMNVVV 2106
Cdd:COG0553   241 TLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELAKFApGLRVLV 320
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2107 YHGSVTSKQMIQDYEyyyktesgkvlkepiKFNVLITTFEMIVTDYMDLKAFNWRLCVIDEAHRLKNRNCKLLEGLRQLN 2186
Cdd:COG0553   321 LDGTRERAKGANPFE---------------DADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALK 385
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2187 LEHRVLLSGTPLQNNISELFSLLNFLEPSQFSSQEEFMSEFGSL---RTEEEVNKLQALLKPMMLRRLKDDVEKSLAPKE 2263
Cdd:COG0553   386 ARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPiekGDEEALERLRRLLRPFLLRRTKEDVLKDLPEKT 465
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2264 ETIIEVELTNIQKKYYRGILEQnfsFLKKGTTSANIPNLMN---TMMELRKCCIHPYLLNgaEEQIQYDFKSqhgedpes 2340
Cdd:COG0553   466 EETLYVELTPEQRALYEAVLEY---LRRELEGAEGIRRRGLilaALTRLRQICSHPALLL--EEGAELSGRS-------- 532
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2341 yyknlilsaGKMVLIDKLLPKLKANGHRVLIFSQMVRCLDILEDYLVYRKYPFERIDGRIRGNLRQEAIDRYSKpGSDRF 2420
Cdd:COG0553   533 ---------AKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQE-GPEAP 602
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2421 VFLLCTKAGGLGINLTAADTVIIYDSDWNPQNDLQAQARCHRIGQRKMVKIYRLLCRNTYEREMFDKASMKLGLDKAVLQ 2500
Cdd:COG0553   603 VFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
2029-2250 6.84e-112

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: 355.89  E-value: 6.84e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2029 LRPYQLEGLNWLKFSWYNTHNCILADEMGLGKTIQSLTFVHSVYEYGIRGPFLVIAPLSTIPNWQREFEGWTDMNVVVYH 2108
Cdd:cd18058     1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLMGIRGPFLIIAPLSTITNWEREFRTWTEMNAIVYH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2109 GSVTSKQMIQDYEYYYKTESGKVLKEPIKFNVLITTFEMIVTDYMDLKAFNWRLCVIDEAHRLKNRNCKLLEGLRQLNLE 2188
Cdd:cd18058    81 GSQISRQMIQQYEMYYRDEQGNPLSGIFKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMALE 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386768875 2189 HRVLLSGTPLQNNISELFSLLNFLEPSQFSSQEEFMSEFGSLRTEEEVNKLQALLKPMMLRR 2250
Cdd:cd18058   161 HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFGDLKTEEQVKKLQSILKPMMLRR 222
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
2029-2250 5.07e-110

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: 350.51  E-value: 5.07e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2029 LRPYQLEGLNWLKFSWYNTHNCILADEMGLGKTIQSLTFVHSVYEYGIRGPFLVIAPLSTIPNWQREFEGWTDMNVVVYH 2108
Cdd:cd18060     1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWTEMNTIVYH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2109 GSVTSKQMIQDYEYYYKTESGKVLKEPIKFNVLITTFEMIVTDYMDLKAFNWRLCVIDEAHRLKNRNCKLLEGLRQLNLE 2188
Cdd:cd18060    81 GSLASRQMIQQYEMYCKDSRGRLIPGAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDLE 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386768875 2189 HRVLLSGTPLQNNISELFSLLNFLEPSQFSSQEEFMSEFGSLRTEEEVNKLQALLKPMMLRR 2250
Cdd:cd18060   161 HKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKTEEQVQKLQAILKPMMLRR 222
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
2029-2250 1.30e-107

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: 343.55  E-value: 1.30e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2029 LRPYQLEGLNWLKFSWYNTHNCILADEMGLGKTIQSLTFVHSVYEYGIRGPFLVIAPLSTIPNWQREFEGWTDMNVVVYH 2108
Cdd:cd18059     1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFLYEIYLKGIHGPFLVIAPLSTIPNWEREFRTWTELNVVVYH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2109 GSVTSKQMIQDYEYYYKTESGKVLKEPIKFNVLITTFEMIVTDYMDLKAFNWRLCVIDEAHRLKNRNCKLLEGLRQLNLE 2188
Cdd:cd18059    81 GSQASRRTIQLYEMYFKDPQGRVIKGSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMDLE 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386768875 2189 HRVLLSGTPLQNNISELFSLLNFLEPSQFSSQEEFMSEFGSLRTEEEVNKLQALLKPMMLRR 2250
Cdd:cd18059   161 HKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGDLKTEEQVQKLQAILKPMMLRR 222
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
2029-2250 9.72e-106

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: 338.52  E-value: 9.72e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2029 LRPYQLEGLNWLKFSWYNTHNCILADEMGLGKTIQSLTFVHSVYEYGIRGPFLVIAPLSTIPNWQREFEGWTDMNVVVYH 2108
Cdd:cd18061     1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIANWEREFRTWTDLNVVVYH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2109 GSVTSKQMIQDYEYYYKTESGKVLKEPIKFNVLITTFEMIVTDYMDLKAFNWRLCVIDEAHRLKNRNCKLLEGLRQLNLE 2188
Cdd:cd18061    81 GSLISRQMIQQYEMYFRDSQGRIIRGAYRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMNLE 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386768875 2189 HRVLLSGTPLQNNISELFSLLNFLEPSQFSSQEEFMSEFGSLRTEEEVNKLQALLKPMMLRR 2250
Cdd:cd18061   161 HKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKTEEQVQKLQAILKPMMLRR 222
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
2032-2319 7.50e-91

SNF2-related domain; This domain is found in proteins involved in a variety of processes including transcription regulation (e.g., SNF2, STH1, brahma, MOT1), DNA repair (e.g., ERCC6, RAD16, RAD5), DNA recombination (e.g., RAD54), and chromatin unwinding (e.g., ISWI) as well as a variety of other proteins with little functional information (e.g., lodestar, ETL1). SNF2 functions as the ATPase component of the SNF2/SWI multisubunit complex, which utilizes energy derived from ATP hydrolysis to disrupt histone-DNA interactions, resulting in the increased accessibility of DNA to transcription factors.


Pssm-ID: 425504 [Multi-domain]  Cd Length: 289  Bit Score: 298.44  E-value: 7.50e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875  2032 YQLEGLNWLKFSWYNT-HNCILADEMGLGKTIQSLTFVHSVYEYGI--RGPFLVIAPLSTIPNWQREFEGWT---DMNVV 2105
Cdd:pfam00176    1 YQIEGVNWMLSLENNLgRGGILADEMGLGKTLQTISLLLYLKHVDKnwGGPTLIVVPLSLLHNWMNEFERWVsppALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875  2106 VYHGsVTSKQMIQdyeyyykTESGKVLKepiKFNVLITTFEMIVTDYMDLKAFNWRLCVIDEAHRLKNRNCKLLEGLRQL 2185
Cdd:pfam00176   81 VLHG-NKRPQERW-------KNDPNFLA---DFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSL 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875  2186 NLEHRVLLSGTPLQNNISELFSLLNFLEPSQFSSQEEFMSEFG--SLRTEEE--VNKLQALLKPMMLRRLKDDVEKSLAP 2261
Cdd:pfam00176  150 KTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDrpIERGGGKkgVSRLHKLLKPFLLRRTKKDVEKSLPP 229
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875  2262 KEETIIEVELTNIQKKYY-RGILEQNFSFLKKGTTSANIP-NLMNTMMELRKCCIHPYLL 2319
Cdd:pfam00176  230 KVEYILFCRLSKLQRKLYqTFLLKKDLNAIKTGEGGREIKaSLLNILMRLRKICNHPGLI 289
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
2029-2250 7.81e-84

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: 275.39  E-value: 7.81e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2029 LRPYQLEGLNWLKFSWYNTHNCILADEMGLGKTIQSLTFVHSVY-EYGIRGPFLVIAPLSTIPNWQREFEGWT-DMNVVV 2106
Cdd:cd17993     2 LRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFhSQQQYGPFLVVVPLSTMPAWQREFAKWApDMNVIV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2107 YHGSVTSKQMIQDYEYYykTESGKvlkePIKFNVLITTFEMIVTDYMDLKAFNWRLCVIDEAHRLKNRNCKLLEGLRQLN 2186
Cdd:cd17993    82 YLGDIKSRDTIREYEFY--FSQTK----KLKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFK 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386768875 2187 LEHRVLLSGTPLQNNISELFSLLNFLEPSQFSSQEEFMSEFGSLRtEEEVNKLQALLKPMMLRR 2250
Cdd:cd17993   156 TNNRLLITGTPLQNSLKELWALLHFLMPGKFDIWEEFEEEHDEEQ-EKGIADLHKELEPFILRR 218
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
2029-2214 2.43e-77

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: 255.18  E-value: 2.43e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2029 LRPYQLEGLNWLKFSWYNTHNCILADEMGLGKTIQSLTFVHSV-YEYGIRGPFLVIAPLSTIPNWQREFEGWT-DMNVVV 2106
Cdd:cd17919     1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLlKEGKERGPVLVVCPLSVLENWEREFEKWTpDLRVVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2107 YHGSVTSKQMIQDYEyyyktesgkvlkEPIKFNVLITTFEMIVTDYMDLKAFNWRLCVIDEAHRLKNRNCKLLEGLRQLN 2186
Cdd:cd17919    81 YHGSQRERAQIRAKE------------KLDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALR 148
                         170       180
                  ....*....|....*....|....*...
gi 386768875 2187 LEHRVLLSGTPLQNNISELFSLLNFLEP 2214
Cdd:cd17919   149 AKRRLLLTGTPLQNNLEELWALLDFLDP 176
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
2026-2252 2.05e-74

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: 249.23  E-value: 2.05e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2026 GNSLRPYQLEGLNWLKFSWYNTHNCILADEMGLGKTIQSLTFVHSVYEYGIRGPFLVIAPLSTIPNWQREFEGWT-DMNV 2104
Cdd:cd18009     1 GGVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRERGVWGPFLVIAPLSTLPNWVNEFARFTpSVPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2105 VVYHGSVTSKQMIQDyEYYYKTESGKvlkepiKFNVLITTFEMIVTDYMDLKAFNWRLCVIDEAHRLKNRNCKLLEGLRQ 2184
Cdd:cd18009    81 LLYHGTKEERERLRK-KIMKREGTLQ------DFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2185 LNLEHRVLLSGTPLQNNISELFSLLNFLEPSQFSSQEEFMSEFG----SLRTEEE-----------VNKLQALLKPMMLR 2249
Cdd:cd18009   154 FNSDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDfsslSDNAADIsnlseereqniVHMLHAILKPFLLR 233

                  ...
gi 386768875 2250 RLK 2252
Cdd:cd18009   234 RLK 236
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
2029-2250 8.39e-74

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: 245.81  E-value: 8.39e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2029 LRPYQLEGLNWLKFSWYNTHNCILADEMGLGKTIQSLTFVHSVYEYG-IRGPFLVIAPLSTIPNWQREFEGWT-DMNVVV 2106
Cdd:cd17994     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGhSKGPFLVSAPLSTIINWEREFEMWApDFYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2107 YHGSvtskqmiqdyeyyyktesgkvlkepikfNVLITTFEMIVTDYMDLKAFNWRLCVIDEAHRLKNRNCKLLEGLRQLN 2186
Cdd:cd17994    81 YVGD----------------------------HVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYK 132
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386768875 2187 LEHRVLLSGTPLQNNISELFSLLNFLEPSQFSSQEEFMSEFGSLRTEEEVNKLQALLKPMMLRR 2250
Cdd:cd17994   133 IGYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLQGFLEEFADISKEDQIKKLHDLLGPHMLRR 196
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
2026-2252 1.34e-70

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: 237.60  E-value: 1.34e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2026 GNSLRPYQLEGLNWLKFSWYNTHNCILADEMGLGKTIQSLTFVHSVYEY-GIRGPFLVIAPLSTIPNWQREFEGWT-DMN 2103
Cdd:cd17997     1 GGTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHYkNINGPHLIIVPKSTLDNWMREFKRWCpSLR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2104 VVVYHGSvtskqmiqdyeyyyKTESGKVLKE---PIKFNVLITTFEMIVTDYMDLKAFNWRLCVIDEAHRLKNRNCKLLE 2180
Cdd:cd17997    81 VVVLIGD--------------KEERADIIRDvllPGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQ 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386768875 2181 GLRQLNLEHRVLLSGTPLQNNISELFSLLNFLEPSQFSSQEEFMSEFGSLRTEEE----VNKLQALLKPMMLRRLK 2252
Cdd:cd17997   147 IVRLFNSRNRLLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFNVNNCDDDnqevVQRLHKVLRPFLLRRIK 222
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
2017-2250 2.58e-70

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: 237.60  E-value: 2.58e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2017 LEKTPVYKGGNSL--RPYQLEGLNWLKFSWYNTHNCILADEMGLGKTIQSLTFVHSVY-EYGIRGPFLVIAPLSTIPNWQ 2093
Cdd:cd18054     7 LKKQPSYIGGENLelRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFhQHQLYGPFLLVVPLSTLTSWQ 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2094 REFEGWT-DMNVVVYHGSVTSKQMIQDYEYYYKTesgkvlKEPIKFNVLITTFEMIVTDYMDLKAFNWRLCVIDEAHRLK 2172
Cdd:cd18054    87 REFEIWApEINVVVYIGDLMSRNTIREYEWIHSQ------TKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLK 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386768875 2173 NRNCKLLEGLRQLNLEHRVLLSGTPLQNNISELFSLLNFLEPSQFSSQEEFMSEFGSLRtEEEVNKLQALLKPMMLRR 2250
Cdd:cd18054   161 NDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGR-ENGYQSLHKVLEPFLLRR 237
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
2029-2250 6.78e-69

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: 232.98  E-value: 6.78e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2029 LRPYQLEGLNWLKFSWYNTHNCILADEMGLGKTIQSLTFVHSVYEYG-IRGPFLVIAPLSTIPNWQREFEGWT-DMNVVV 2106
Cdd:cd18055     1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGhTKGPFLVSAPLSTIINWEREFQMWApDFYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2107 YHGSVTSKQMIQDYEYYYKTESGKVLKE--------PIKFNVLITTFEMIVTDYMDLKAFNWRLCVIDEAHRLKNRNCKL 2178
Cdd:cd18055    81 YTGDKDSRAIIRENEFSFDDNAVKGGKKafkmkreaQVKFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKF 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386768875 2179 LEGLRQLNLEHRVLLSGTPLQNNISELFSLLNFLEPSQFSSQEEFMSEFGSLRTEEEVNKLQALLKPMMLRR 2250
Cdd:cd18055   161 FRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQIKKLHDLLGPHMLRR 232
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
2029-2250 2.70e-67

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: 228.41  E-value: 2.70e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2029 LRPYQLEGLNWLKFSWYNTHNCILADEMGLGKTIQSLTFVHSVYEYG-IRGPFLVIAPLSTIPNWQREFEGWT-DMNVVV 2106
Cdd:cd18057     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGhSKGPYLVSAPLSTIINWEREFEMWApDFYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2107 YHGSVTSKQMIQDYEYYYK---TESGKVL-----KEPIKFNVLITTFEMIVTDYMDLKAFNWRLCVIDEAHRLKNRNCKL 2178
Cdd:cd18057    81 YTGDKESRSVIRENEFSFEdnaIRSGKKVfrmkkEAQIKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386768875 2179 LEGLRQLNLEHRVLLSGTPLQNNISELFSLLNFLEPSQFSSQEEFMSEFGSLRTEEEVNKLQALLKPMMLRR 2250
Cdd:cd18057   161 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQIKKLHDLLGPHMLRR 232
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
2029-2250 4.01e-67

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: 228.03  E-value: 4.01e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2029 LRPYQLEGLNWLKFSWYNTHNCILADEMGLGKTIQSLTFVHSVYEYG-IRGPFLVIAPLSTIPNWQREFEGWT-DMNVVV 2106
Cdd:cd18056     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGhSKGPFLVSAPLSTIINWEREFEMWApDMYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2107 YHGSVTSKQMIQDYEYYYK-------TESGKVLKEP-IKFNVLITTFEMIVTDYMDLKAFNWRLCVIDEAHRLKNRNCKL 2178
Cdd:cd18056    81 YVGDKDSRAIIRENEFSFEdnairggKKASRMKKEAsVKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386768875 2179 LEGLRQLNLEHRVLLSGTPLQNNISELFSLLNFLEPSQFSSQEEFMSEFGSLRTEEEVNKLQALLKPMMLRR 2250
Cdd:cd18056   161 FRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFADIAKEDQIKKLHDMLGPHMLRR 232
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
2026-2252 1.72e-65

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: 223.40  E-value: 1.72e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2026 GNSLRPYQLEGLNWLkFSWYNTH-NCILADEMGLGKTIQSLTFVHSVYEY-GIRGPFLVIAPLSTIPNWQREFEGWT-DM 2102
Cdd:cd17996     1 GGTLKEYQLKGLQWM-VSLYNNNlNGILADEMGLGKTIQTISLITYLMEKkKNNGPYLVIVPLSTLSNWVSEFEKWApSV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2103 NVVVYHGSVTSKQMIQDYEyyyktesgkvlkEPIKFNVLITTFEMIVTDYMDLKAFNWRLCVIDEAHRLKNRNCKLLEGL 2182
Cdd:cd17996    80 SKIVYKGTPDVRKKLQSQI------------RAGKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2183 -RQLNLEHRVLLSGTPLQNNISELFSLLNFLEPSQFSSQEEFMSEFGS-----------LRTEEE----VNKLQALLKPM 2246
Cdd:cd17996   148 nTYYHARYRLLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTpfantgeqvkiELNEEEtlliIRRLHKVLRPF 227

                  ....*.
gi 386768875 2247 MLRRLK 2252
Cdd:cd17996   228 LLRRLK 233
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
2027-2252 4.49e-61

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: 210.11  E-value: 4.49e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2027 NSLRPYQLEGLNWLKFSWYNTHNCILADEMGLGKTIQSLTFVHSVYEYGIRGPFLVIAPLSTIPNWQREFEGWT-DMNVV 2105
Cdd:cd18012     3 ATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKEEGRKGPSLVVAPTSLIYNWEEEAAKFApELKVL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2106 VYHGSVTSKQMIQDYEyyyktesgkvlkepiKFNVLITTFEMIVTDYMDLKAFNWRLCVIDEAHRLKNRNCKLLEGLRQL 2185
Cdd:cd18012    83 VIHGTKRKREKLRALE---------------DYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKAL 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386768875 2186 NLEHRVLLSGTPLQNNISELFSLLNFLEPSQFSSQEEFMSEFGSL----RTEEEVNKLQALLKPMMLRRLK 2252
Cdd:cd18012   148 KADHRLALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKPiekdGDEEALEELKKLISPFILRRLK 218
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
2017-2250 1.82e-60

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: 209.14  E-value: 1.82e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2017 LEKTPVYKGGNS---LRPYQLEGLNWLKFSWYNTHNCILADEMGLGKTIQSLTFVHSVY-EYGIRGPFLVIAPLSTIPNW 2092
Cdd:cd18053     6 LKKQPSYIGGHEgleLRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFhEHQLYGPFLLVVPLSTLTSW 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2093 QREFEGWTD-MNVVVYHGSVTSKQMIQDYEYYYKTesgkvlKEPIKFNVLITTFEMIVTDYMDLKAFNWRLCVIDEAHRL 2171
Cdd:cd18053    86 QREIQTWAPqMNAVVYLGDINSRNMIRTHEWMHPQ------TKRLKFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRL 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386768875 2172 KNRNCKLLEGLRQLNLEHRVLLSGTPLQNNISELFSLLNFLEPSQFSSQEEFMSEFGSLRtEEEVNKLQALLKPMMLRR 2250
Cdd:cd18053   160 KNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEEHGKGR-EYGYASLHKELEPFLLRR 237
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
2350-2475 2.70e-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: 193.08  E-value: 2.70e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2350 GKMVLIDKLLPKLKANGHRVLIFSQMVRCLDILEDYLVYRKYPFERIDGRIRGNLRQEAIDRYSKPGSDrFVFLLCTKAG 2429
Cdd:cd18793    11 GKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDI-RVFLLSTKAG 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 386768875 2430 GLGINLTAADTVIIYDSDWNPQNDLQAQARCHRIGQRKMVKIYRLL 2475
Cdd:cd18793    90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
2029-2250 3.11e-55

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: 193.42  E-value: 3.11e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2029 LRPYQLEGLNWLKFSWYNTHNCILADEMGLGKTIQSLTFV-HSVYEYGIRGPFLVIAPLSTIPNWQREFEGWT-DMNVVV 2106
Cdd:cd18006     1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLwYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFApDLSVIT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2107 YHGsvtskqmiqdyEYYYKTESGKVLKEPIKFNVLITTFEMIVTDYMDLKAFNWRLCVIDEAHRLKNRNCKLLEGLRQLN 2186
Cdd:cd18006    81 YMG-----------DKEKRLDLQQDIKSTNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFS 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386768875 2187 LEHRVLLSGTPLQNNISELFSLLNFLEPSQFSSQ--EEFMSEFGSLRTEEE-VNKLQALLKPMMLRR 2250
Cdd:cd18006   150 VDFRLLLTGTPIQNSLQELYALLSFIEPNVFPKDklDDFIKAYSETDDESEtVEELHLLLQPFLLRR 216
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
2016-2263 5.33e-55

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: 193.73  E-value: 5.33e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2016 KLEKTPVYKGGNSLRPYQLEGLNWLKFSWYNTHNCILADEMGLGKTIQSLTFVHSVYEY-GIRGPFLVIAPLSTIPNWQR 2094
Cdd:cd18064     3 RFEDSPSYVKWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYrNIPGPHMVLVPKSTLHNWMA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2095 EFEGWTDmnvvvyhgSVTSKQMIQDYEYYYKTESGKVLkePIKFNVLITTFEMIVTDYMDLKAFNWRLCVIDEAHRLKNR 2174
Cdd:cd18064    83 EFKRWVP--------TLRAVCLIGDKDQRAAFVRDVLL--PGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2175 NCKLLEGLRQLNLEHRVLLSGTPLQNNISELFSLLNFLEPSQFSSQEEFMSEFGS---LRTEEEVNKLQALLKPMMLRRL 2251
Cdd:cd18064   153 KSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTnncLGDQKLVERLHMVLRPFLLRRI 232
                         250
                  ....*....|..
gi 386768875 2252 KDDVEKSLAPKE 2263
Cdd:cd18064   233 KADVEKSLPPKK 244
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
2029-2217 1.30e-53

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


Pssm-ID: 350756 [Multi-domain]  Cd Length: 187  Bit Score: 187.59  E-value: 1.30e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2029 LRPYQLEGLNWLKFSWYNTHNCILADEMGLGKTIQSLTFVHSVYEYGIRGPFLVIAPLSTIPNWQREFEGWT-DMNVVVY 2107
Cdd:cd17998     1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKEIGIPGPHLVVVPSSTLDNWLREFKRWCpSLKVEPY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2108 HGSVTSKQMIQDyeyyyktesgKVLKEPIKFNVLITTFEMIVTDYMD---LKAFNWRLCVIDEAHRLKNRNCKLLEGLRQ 2184
Cdd:cd17998    81 YGSQEERKHLRY----------DILKGLEDFDVIVTTYNLATSNPDDrsfFKRLKLNYVVYDEGHMLKNMTSERYRHLMT 150
                         170       180       190
                  ....*....|....*....|....*....|...
gi 386768875 2185 LNLEHRVLLSGTPLQNNISELFSLLNFLEPSQF 2217
Cdd:cd17998   151 INANFRLLLTGTPLQNNLLELMSLLNFIMPKPF 183
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
2029-2250 1.29e-52

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: 186.02  E-value: 1.29e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2029 LRPYQLEGLNWLKFSWYNTHNCILADEMGLGKTIQSLTFV-HSVYEYGIRGPFLVIAPLSTIPNWQREFEGWTD-MNVVV 2106
Cdd:cd18003     1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLaHLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPgFKILT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2107 YHGSVTSKqmiqdyeyyYKTESGkvLKEPIKFNVLITTFEMIVTDYMDLKAFNWRLCVIDEAHRLKNRNCKLLEGLRQLN 2186
Cdd:cd18003    81 YYGSAKER---------KLKRQG--WMKPNSFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFN 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386768875 2187 LEHRVLLSGTPLQNNISELFSLLNFLEPSQFSSQEEF----------MSEFGSLRTEEEVNKLQALLKPMMLRR 2250
Cdd:cd18003   150 TQRRLLLTGTPLQNSLMELWSLMHFLMPHIFQSHQEFkewfsnpltaMSEGSQEENEELVRRLHKVLRPFLLRR 223
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
2016-2252 3.22e-51

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: 182.52  E-value: 3.22e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2016 KLEKTPVYKGGNSLRPYQLEGLNWLKFSWYNTHNCILADEMGLGKTIQSLTFVHSVYEY-GIRGPFLVIAPLSTIPNWQR 2094
Cdd:cd18065     3 RFEESPSYVKGGTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYrNIPGPHMVLVPKSTLHNWMN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2095 EFEGWT-DMNVVVYHGSVTSKQ-MIQDyeyyyktesgkvLKEPIKFNVLITTFEMIVTDYMDLKAFNWRLCVIDEAHRLK 2172
Cdd:cd18065    83 EFKRWVpSLRAVCLIGDKDARAaFIRD------------VMMPGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2173 NRNCKLLEGLRQLNLEHRVLLSGTPLQNNISELFSLLNFLEPSQFSSQEEFMSEFGS---LRTEEEVNKLQALLKPMMLR 2249
Cdd:cd18065   151 NEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTkncLGDQKLVERLHAVLKPFLLR 230

                  ...
gi 386768875 2250 RLK 2252
Cdd:cd18065   231 RIK 233
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
2029-2250 3.79e-51

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: 181.93  E-value: 3.79e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2029 LRPYQLEGLNWLKFSWYNTHNCILADEMGLGKTIQSLTFV-HSVYEYGIRGPFLVIAPLSTIPNWQREFEGWT-DMNVVV 2106
Cdd:cd18002     1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLaHLAEEHNIWGPFLVIAPASTLHNWQQEISRFVpQFKVLP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2107 YHGSVTSKQMIQDY----EYYYKTESgkvlkepikFNVLITTFEMIVTDYMDLKAFNWRLCVIDEAHRLKNRNCKLLEGL 2182
Cdd:cd18002    81 YWGNPKDRKVLRKFwdrkNLYTRDAP---------FHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTL 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386768875 2183 RQLNLEHRVLLSGTPLQNNISELFSLLNFLEPSQFSSQEEF----------MSEFGSLRTEEEVNKLQALLKPMMLRR 2250
Cdd:cd18002   152 LSFHCRNRLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFnewfskdiesHAENKTGLNEHQLKRLHMILKPFMLRR 229
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
2015-2252 9.22e-47

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: 170.23  E-value: 9.22e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2015 KKLEKTPVYKGGNSLRPYQLEGLNWLKFSWYNTHNCILADEMGLGKTIQSLTFVHSVYEYG-IRGPFLVIAPLSTIPNWQ 2093
Cdd:cd18062    10 EKVEKQSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKrINGPFLIIVPLSTLSNWV 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2094 REFEGWTDMNV-VVYHGSVTSKQmiqdyEYYYKTESGKvlkepikFNVLITTFEMIVTDYMDLKAFNWRLCVIDEAHRLK 2172
Cdd:cd18062    90 YEFDKWAPSVVkVSYKGSPAARR-----AFVPQLRSGK-------FNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2173 NRNCKLLEGLRQLNLE-HRVLLSGTPLQNNISELFSLLNFLEPSQFSSQEEFMSEFGS----------LRTEEE---VNK 2238
Cdd:cd18062   158 NHHCKLTQVLNTHYVApRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNApfamtgekvdLNEEETiliIRR 237
                         250
                  ....*....|....
gi 386768875 2239 LQALLKPMMLRRLK 2252
Cdd:cd18062   238 LHKVLRPFLLRRLK 251
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
2029-2250 1.33e-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: 166.79  E-value: 1.33e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2029 LRPYQLEGLNWLkFSWY-NTHNCILADEMGLGKTIQSLTFVHSVYE--------YGIR-------------GPFLVIAPL 2086
Cdd:cd18005     1 LRDYQREGVEFM-YDLYkNGRGGILGDDMGLGKTVQVIAFLAAVLGktgtrrdrENNRprfkkkppassakKPVLIVAPL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2087 STIPNWQREFEGWTDMNVVVYHGSVTSKQMIQDYEyyykteSGKVlkepikfNVLITTFEMIVTDYMDLKAFNWRLCVID 2166
Cdd:cd18005    80 SVLYNWKDELDTWGHFEVGVYHGSRKDDELEGRLK------AGRL-------EVVVTTYDTLRRCIDSLNSINWSAVIAD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2167 EAHRLKNRNCKLLEGLRQLNLEHRVLLSGTPLQNNISELFSLLNFLEPSQFSSQEEFMSEF------GSLRT-------- 2232
Cdd:cd18005   147 EAHRIKNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFsepikrGQRHTatarelrl 226
                         250
                  ....*....|....*....
gi 386768875 2233 -EEEVNKLQALLKPMMLRR 2250
Cdd:cd18005   227 gRKRKQELAVKLSKFFLRR 245
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
2015-2252 2.94e-45

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: 166.01  E-value: 2.94e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2015 KKLEKTPVYKGGNSLRPYQLEGLNWLKFSWYNTHNCILADEMGLGKTIQSLTFVHSVYEYG-IRGPFLVIAPLSTIPNWQ 2093
Cdd:cd18063    10 ERVEKQSSLLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKrLNGPYLIIVPLSTLSNWT 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2094 REFEGWTDMNV-VVYHGSVTSKQMIQDyeyyyKTESGKvlkepikFNVLITTFEMIVTDYMDLKAFNWRLCVIDEAHRLK 2172
Cdd:cd18063    90 YEFDKWAPSVVkISYKGTPAMRRSLVP-----QLRSGK-------FNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2173 NRNCKLLEGLRQLNLE-HRVLLSGTPLQNNISELFSLLNFLEPSQFSSQEEFMSEFGS----------LRTEEE---VNK 2238
Cdd:cd18063   158 NHHCKLTQVLNTHYVApRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNApfamtgervdLNEEETiliIRR 237
                         250
                  ....*....|....
gi 386768875 2239 LQALLKPMMLRRLK 2252
Cdd:cd18063   238 LHKVLRPFLLRRLK 251
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
2029-2250 6.89e-45

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: 164.08  E-value: 6.89e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2029 LRPYQLEGLNWLKFSWYNTHNCILADEMGLGKTIQSLTFVHSVYEYGIRGPFLVIAPLSTIPNWQREFEGWT-DMNVVVY 2107
Cdd:cd18001     1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKSVLVVMPTSLIPHWVKEFAKWTpGLRVKVF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2108 HG-SVTSKQMIQDYeyyyktesgkVLKEpikFNVLITTFEMIVTDYMDLKA-----FNWRLCVIDEAHRLKNRNCKLLEG 2181
Cdd:cd18001    81 HGtSKKERERNLER----------IQRG---GGVLLTTYGMVLSNTEQLSAddhdeFKWDYVILDEGHKIKNSKTKSAKS 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2182 LRQLNLEHRVLLSGTPLQNNISELFSLLNFLEPSQ-FSSQEEFMSEF--------------GSLRTEEEVNK-LQALLKP 2245
Cdd:cd18001   148 LREIPAKNRIILTGTPIQNNLKELWALFDFACNGSlLGTRKTFKMEFenpitrgrdkdatqGEKALGSEVAEnLRQIIKP 227

                  ....*
gi 386768875 2246 MMLRR 2250
Cdd:cd18001   228 YFLRR 232
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
2029-2250 2.04e-43

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: 159.82  E-value: 2.04e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2029 LRPYQLEGLNWLKF-SWYNTHNcILADEMGLGKTIQSLTFV-----HSVYEYGIRG-PFLVIAPLSTIPNWQREFEGWTD 2101
Cdd:cd17999     1 LRPYQQEGINWLAFlNKYNLHG-ILCDDMGLGKTLQTLCILasdhhKRANSFNSENlPSLVVCPPTLVGHWVAEIKKYFP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2102 ---MNVVVYHGSvtskqmiqdyeyyyKTESGKVLKEPIKFNVLITTFEMIVTDYMDLKAFNWRLCVIDEAHRLKNRNCKL 2178
Cdd:cd17999    80 nafLKPLAYVGP--------------PQERRRLREQGEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKL 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2179 LEGLRQLNLEHRVLLSGTPLQNNISELFSLLNFLEPSQFSSQEEFMSEFG------------SLRTEEEVNKLQALLK-- 2244
Cdd:cd17999   146 SKAVKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLkpilasrdskasAKEQEAGALALEALHKqv 225

                  ....*..
gi 386768875 2245 -PMMLRR 2250
Cdd:cd17999   226 lPFLLRR 232
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
2029-2250 2.05e-43

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: 160.15  E-value: 2.05e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2029 LRPYQLEGLNWLKFswyntHNCILADEMGLGKTIQSLTFVHS--------VYEYGIRGPF----------LVIAPLSTIP 2090
Cdd:cd18008     1 LLPYQKQGLAWMLP-----RGGILADEMGLGKTIQALALILAtrpqdpkiPEELEENSSDpkklylskttLIVVPLSLLS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2091 NWQREFE---GWTDMNVVVYHGSvtskqmiqdyeyyyktESGKVLKEPIKFNVLITTFEMIVTDYMD------------- 2154
Cdd:cd18008    76 QWKDEIEkhtKPGSLKVYVYHGS----------------KRIKSIEELSDYDIVITTYGTLASEFPKnkkgggrdskeke 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2155 ---LKAFNWRLCVIDEAHRLKNRNCKLLEGLRQLNLEHRVLLSGTPLQNNISELFSLLNFL--EP-SQFSSQEEFMSEFG 2228
Cdd:cd18008   140 aspLHRIRWYRVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLrvEPfGDYPWFNSDISKPF 219
                         250       260
                  ....*....|....*....|..
gi 386768875 2229 SLRTEEEVNKLQALLKPMMLRR 2250
Cdd:cd18008   220 SKNDRKALERLQALLKPILLRR 241
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
2029-2250 3.86e-40

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: 150.90  E-value: 3.86e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2029 LRPYQLEGLNWL-----KFSWYNTHNCILADEMGLGKTIQSLTFVHSVYEygiRGPF--------LVIAPLSTIPNWQRE 2095
Cdd:cd18004     1 LRPHQREGVQFLydcltGRRGYGGGGAILADEMGLGKTLQAIALVWTLLK---QGPYgkptakkaLIVCPSSLVGNWKAE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2096 FEGW---TDMNVVVYHGSVTSKQMIQDYEYYYKTesgkvlkepikFNVLIT---TFEMIVTDYMDLKAFNwrLCVIDEAH 2169
Cdd:cd18004    78 FDKWlglRRIKVVTADGNAKDVKASLDFFSSAST-----------YPVLIIsyeTLRRHAEKLSKKISID--LLICDEGH 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2170 RLKNRNCKLLEGLRQLNLEHRVLLSGTPLQNNISELFSLLNFLEPSQFSSQEEFMSEF-------------------GSL 2230
Cdd:cd18004   145 RLKNSESKTTKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFeepilrsrdpdaseedkelGAE 224
                         250       260
                  ....*....|....*....|
gi 386768875 2231 RTEEevnkLQALLKPMMLRR 2250
Cdd:cd18004   225 RSQE----LSELTSRFILRR 240
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
2029-2227 6.99e-37

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: 141.27  E-value: 6.99e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2029 LRPYQLEGLnwlKFSWYN----------THNCILADEMGLGKTIQSLTFVHSVYEYGIRGP-FLVIAPLSTIPNWQREFE 2097
Cdd:cd18007     1 LKPHQVEGV---RFLWSNlvgtdvgsdeGGGCILAHTMGLGKTLQVITFLHTYLAAAPRRSrPLVLCPASTLYNWEDEFK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2098 GWTDMNVVVYHGSVTSKQmiqdyeyyykteSGKVLKEPIKFN-------VLITTFEMIV-------TDYMDLKAFNWRLC 2163
Cdd:cd18007    78 KWLPPDLRPLLVLVSLSA------------SKRADARLRKINkwhkeggVLLIGYELFRnlasnatTDPRLKQEFIAALL 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386768875 2164 -------VIDEAHRLKNRNCKLLEGLRQLNLEHRVLLSGTPLQNNISELFSLLNFLEPSQFSSQEEFMSEF 2227
Cdd:cd18007   146 dpgpdllVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKF 216
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
2029-2214 6.84e-36

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: 136.68  E-value: 6.84e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2029 LRPYQLEGLNWLkfSWYNTHNC--ILADEMGLGKTIQSLTFVHSVYEYGI-RGPFLVIAPLSTIPNWQREFEGW-TDMNV 2104
Cdd:cd18000     1 LFKYQQTGVQWL--WELHCQRVggILGDEMGLGKTIQIIAFLAALHHSKLgLGPSLIVCPATVLKQWVKEFHRWwPPFRV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2105 VVYHGSVtSKQMIQDYEYYYKTESGKVLKEPIKFNVLITTFEMIVTDYMDLKAFNWRLCVIDEAHRLKNRNCKLLEGLRQ 2184
Cdd:cd18000    79 VVLHSSG-SGTGSEEKLGSIERKSQLIRKVVGDGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLACKQ 157
                         170       180       190
                  ....*....|....*....|....*....|
gi 386768875 2185 LNLEHRVLLSGTPLQNNISELFSLLNFLEP 2214
Cdd:cd18000   158 LRTPHRLILSGTPIQNNLKELWSLFDFVFP 187
CD2_tandem_CHD5-9_like cd18663
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
1937-1995 6.43e-33

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


Pssm-ID: 349310 [Multi-domain]  Cd Length: 59  Bit Score: 123.17  E-value: 6.43e-33
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 386768875 1937 QDFTEVDRVLDMSVHTDETSGETTKHYLVKWKSLPYEDCTWELEEDVDNDKIEQYLRFN 1995
Cdd:cd18663     1 PDYVEVDRILDVSVSTDPNTGEPVTHYLVKWCSLPYEDSTWELEEDVDPAKIEEFEKLR 59
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
2029-2244 2.56e-30

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: 122.58  E-value: 2.56e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2029 LRPYQLEGLnwlKFSWY--------NTHNCILADEMGLGKTIQSLTFVHSVYEYGIRGP-----FLVIAPLSTIPNWQRE 2095
Cdd:cd18067     1 LRPHQREGV---KFLYRcvtgrrirGSHGCIMADEMGLGKTLQCITLMWTLLRQSPQCKpeidkAIVVSPSSLVKNWANE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2096 FEGWTDMNVVVYHGSVTSKQMIQDYEYYYKTESGKVLKEPikfnVLITTFEMIVTDYMDLKAFNWRLCVIDEAHRLKNRN 2175
Cdd:cd18067    78 LGKWLGGRLQPLAIDGGSKKEIDRKLVQWASQQGRRVSTP----VLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSD 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386768875 2176 CKLLEGLRQLNLEHRVLLSGTPLQNNISELFSLLNFLEPSQFSSQEEFMSEFGS--LR------TEEEVNKLQALLK 2244
Cdd:cd18067   154 NQTYQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELpiLKgrdadaSEKERQLGEEKLQ 230
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
2029-2223 1.66e-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: 119.95  E-value: 1.66e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2029 LRPYQLEGLNWLKFSWYNT-HN----CILADEMGLGKTIQSLTFVHSVYEYGIRGP------FLVIAPLSTIPNWQREFE 2097
Cdd:cd18066     1 LRPHQREGIEFLYECVMGMrVNerfgAILADEMGLGKTLQCISLIWTLLRQGPYGGkpvikrALIVTPGSLVKNWKKEFQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2098 GWTdmnvvvyhGSVTSKQMIQDYEYyyKTEsgKVLKEPIkFNVLITTFEMIVTDYMDLKAFNWRLCVIDEAHRLKNRNCK 2177
Cdd:cd18066    81 KWL--------GSERIKVFTVDQDH--KVE--EFIASPL-YSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIK 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 386768875 2178 LLEGLRQLNLEHRVLLSGTPLQNNISELFSLLNFLEPSQFSSQEEF 2223
Cdd:cd18066   148 TTTALTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTY 193
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
2029-2250 3.98e-29

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


Pssm-ID: 350768 [Multi-domain]  Cd Length: 213  Bit Score: 118.08  E-value: 3.98e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2029 LRPYQLEGLNW-LKFSwyntHNCILADEMGLGKTIQSLTFVHSVYEYgirGPFLVIAPLSTIPNWQREFEGW----TDMN 2103
Cdd:cd18010     1 LLPFQREGVCFaLRRG----GRVLIADEMGLGKTVQAIAIAAYYREE---WPLLIVCPSSLRLTWADEIERWlpslPPDD 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2104 VVVYHGSvtskqmiQDYEYyykTESGKvlkepikfnVLITTFEMIVTDYMDLKAFNWRLCVIDEAHRLKNRNCK----LL 2179
Cdd:cd18010    74 IQVIVKS-------KDGLR---DGDAK---------VVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKrtkaAL 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2180 EGLRQLNleHRVLLSGTPLQNNISELFSLLNFLEPSQFSSQEEF--------MSEF-----GSLRTEEEVNklqALLKPM 2246
Cdd:cd18010   135 PLLKRAK--RVILLSGTPALSRPIELFTQLDALDPKLFGRFHDFgrrycaakQGGFgwdysGSSNLEELHL---LLLATI 209

                  ....
gi 386768875 2247 MLRR 2250
Cdd:cd18010   210 MIRR 213
DEXDc smart00487
DEAD-like helicases superfamily;
2023-2215 1.38e-27

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 113.36  E-value: 1.38e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875   2023 YKGGNSLRPYQLEGLNWLKFSWyntHNCILADEMGLGKTIQSLTFVHSVYEYGIRGPFLVIAPL-STIPNWQREFEGWTD 2101
Cdd:smart00487    3 KFGFEPLRPYQKEAIEALLSGL---RDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTrELAEQWAEELKKLGP 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875   2102 ----MNVVVYHGSVTSKQMiqdyeyyYKTESGkvlkepiKFNVLITTFEMIVTDYMD--LKAFNWRLCVIDEAHRLKN-- 2173
Cdd:smart00487   80 slglKVVGLYGGDSKREQL-------RKLESG-------KTDILVTTPGRLLDLLENdkLSLSNVDLVILDEAHRLLDgg 145
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|....*.
gi 386768875   2174 RNCKLLEGLRQLNLE-HRVLLSGTP---LQNNISELFSLLNFLEPS 2215
Cdd:smart00487  146 FGDQLEKLLKLLPKNvQLLLLSATPpeeIENLLELFLNDPVFIDVG 191
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
2029-2250 1.97e-27

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


Pssm-ID: 350829 [Multi-domain]  Cd Length: 239  Bit Score: 114.10  E-value: 1.97e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2029 LRPYQLEGLNWL----------------KFSWYNT-------------HNCILADEMGLGKTIQSLTFVHSvyeygirGP 2079
Cdd:cd18071     1 LLPHQKQALAWMvsrensqdlppfweeaVGLFLNTitnfsqkkrpelvRGGILADDMGLGKTLTTISLILA-------NF 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2080 FLVIAPLSTIPNWQREFEGWTD---MNVVVYHGSvtskqmiqdyeyyyktESGKVLKEPIKFNVLITTFEMIVTDY---- 2152
Cdd:cd18071    74 TLIVCPLSVLSNWETQFEEHVKpgqLKVYTYHGG----------------ERNRDPKLLSKYDIVLTTYNTLASDFgakg 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2153 -MDLKAFNWRLCVIDEAHRLKNRNCKLLEGLRQLNLEHRVLLSGTPLQNNISELFSLLNFLEPSQFSSQEEFMSEFG--- 2228
Cdd:cd18071   138 dSPLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLGSLLSFLHLKPFSNPEYWRRLIQrpl 217
                         250       260
                  ....*....|....*....|..
gi 386768875 2229 SLRTEEEVNKLQALLKPMMLRR 2250
Cdd:cd18071   218 TMGDPTGLKRLQVLMKQITLRR 239
CD1_tandem_CHD5-9_like cd18668
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
1851-1918 2.09e-27

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


Pssm-ID: 349315 [Multi-domain]  Cd Length: 68  Bit Score: 107.81  E-value: 2.09e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386768875 1851 EGEESVKKENDEKTEADmENKPEPVFIDVEEYFVKYRNFSYLHCEWRTEEELLKGDRRVAAKIRRFQQ 1918
Cdd:cd18668     2 EDTMIIEKILASRKKKK-EKEEGAEEIEVEEYLVKYKNFSYLHCEWKTEEELEKGDKRIKQKIKRFKQ 68
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
2350-2464 1.55e-26

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: 106.91  E-value: 1.55e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875  2350 GKMVLIDKLLPKlkANGHRVLIFSQMVRCLDIlEDYLVYRKYPFERIDGRIRGNLRQEAIDRYSKpgsDRFVFLLCTKAG 2429
Cdd:pfam00271    1 EKLEALLELLKK--ERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRK---GKIDVLVATDVA 74
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 386768875  2430 GLGINLTAADTVIIYDSDWNPQNDLQAQARCHRIG 2464
Cdd:pfam00271   75 ERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DISARM_DrmD_b NF038318
DISARM system SNF2-like helicase DrmD, short form; DrmD, a SNF2-like helicase, is a component ...
1988-2498 6.53e-26

DISARM system SNF2-like helicase DrmD, short form; DrmD, a SNF2-like helicase, is a component of class 1 DISARM (Defence Island System Associated with Restriction Modification), which contains a DNA adenine N6 methyltransferase. This HMM describes a distinct form that is somewhat shorter than the majority of DrmD proteins.


Pssm-ID: 468472 [Multi-domain]  Cd Length: 868  Bit Score: 118.25  E-value: 6.53e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1988 IEQYLRFNKIpqrsewkskkrphpelwkKLEKTPVYKGGNS---LRPYQLEG----LNWLKfswynTHNCILADEMGLGK 2060
Cdd:NF038318    4 LEQYARYKRQ------------------ELEKSPYHCLLMAdidPNPHQINAfcaaIAALK-----TGGIILADEVGLGK 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2061 TIQSLTFVHSVYEYGIRgPFLVIAPLSTIPNWQREFEGWTDMNVVVyhgsVTSKQMIQDYEYYYKTesgkvLKEPIKFNV 2140
Cdd:NF038318   61 TIEAGLVLKYVLESGAK-KILIILPANLRKQWEIELEEKFDLESLI----LDSLTVEKDAKKWNKR-----LTDNKKVRI 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2141 LITTFemivtDY--MDLKAF---NWRLCVIDEAHRLKN--RNCKLLEGLRQLNLE-HRVLLSGTPLQNNISELFSLLNFL 2212
Cdd:NF038318  131 VITSY-----DYasKLMKRFpkvKWDFIIIDEAHNLRNvhKGGKRAKNLYELTKGiPKILLTATPLQNSLLDLYGLVSFI 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2213 EPSQFSSQEEFMSEFgsLRTEEeVNKLQALLKPMMLRRLKDDVEKSLAPKEETII---------EVEL----TNIQKKYY 2279
Cdd:NF038318  206 DPRIFGSEKVFSKRY--IKDED-YSDLKRELSPVLYRTLRKDVADYMQFKKRKCItvdfelspdEIELyvrvNNFLKRDI 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2280 --------RG----------------------ILEQNFSFLKKGTTSANIPNLMNTMMElrkccihpYLlngAEEQIQYD 2329
Cdd:NF038318  283 lysiptsnRTliilvirkllasssfalaetfeVLKKRLEKLKEGTRSANAQEGFDLFWS--------FV---EDEIDESG 351
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2330 FKSQHGED---------------------PESYYKNLILSAGKMVlIDKLLPKLKANG--HRVLIFSQMVRCLDILEDYL 2386
Cdd:NF038318  352 FEEKQDELytrqkefiqheidevdaiidvAKRIKTNAKVTALKTA-LEIAFEYQREEGiaQKVVVFTESKRTQKYIAEEL 430
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2387 VYRKYPFERI---DGRIRGNLRQE-----------------------AIDRYSKpgsDRFVFLLCTKAGGLGINLTAADT 2440
Cdd:NF038318  431 RKSGYEGEDIllfNGDFDDAMTKEiyrawqvknygkanygrsveykhAIVDYFK---NNAKILIVTDAGSEGLNLQFCNT 507
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 386768875 2441 VIIYDSDWNPQNDLQAQARCHRIGQRKMVKIYRLL-CRNTYEREMFDKASMKLGLDKAV 2498
Cdd:NF038318  508 VINYDLPWNPQKIEQRIGRCHRYGQKNDVVAINLLnTQNVADKRVYEILSEKFELFEGV 566
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
2029-2227 6.68e-25

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: 106.90  E-value: 6.68e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2029 LRPYQLEGLnwlKFSW------------YNTHNCILADEMGLGKTIQSLTFVHSVYEYGIRGPF---LVIAPLSTIPNWQ 2093
Cdd:cd18068     1 LKPHQVDGV---QFMWdccceslkktkkSPGSGCILAHCMGLGKTLQVVTFLHTVLLCEKLENFsrvLVVCPLNTVLNWL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2094 REFEGWTDMNvvvyhgsvTSKQMIQDYEY-YYKTESGKVLKEPIKFN---VLITTFEM--IVTDYMDLKA-------FNW 2160
Cdd:cd18068    78 NEFEKWQEGL--------KDEEKIEVNELaTYKRPQERSYKLQRWQEeggVMIIGYDMyrILAQERNVKSreklkeiFNK 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386768875 2161 RL-------CVIDEAHRLKNRNCKLLEGLRQLNLEHRVLLSGTPLQNNISELFSLLNFLEPSQFSSQEEFMSEF 2227
Cdd:cd18068   150 ALvdpgpdfVVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRF 223
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
2029-2250 1.13e-21

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: 96.59  E-value: 1.13e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2029 LRPYQLEGLN--WLKFSwyntHNCILADEMGLGKTIQSLTFVHsvyEYGIRG---PFLVIAPLSTIPNWQREFegWTDMN 2103
Cdd:cd18011     1 PLPHQIDAVLraLRKPP----VRLLLADEVGLGKTIEAGLIIK---ELLLRGdakRVLILCPASLVEQWQDEL--QDKFG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2104 VvvyhgsvtsKQMIQDYEYYYKTESGKVlKEPIKFNVLITTFEMIVTD---YMDLKAFNWRLCVIDEAHRLKNRNC---- 2176
Cdd:cd18011    72 L---------PFLILDRETAAQLRRLIG-NPFEEFPIVIVSLDLLKRSeerRGLLLSEEWDLVVVDEAHKLRNSGGgket 141
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386768875 2177 ---KLLEGLRQLNlEHRVLLSGTPLQNNISELFSLLNFLEPSQFSSQEefmsEFGSLRTEEEVnklqalLKPMMLRR 2250
Cdd:cd18011   142 kryKLGRLLAKRA-RHVLLLTATPHNGKEEDFRALLSLLDPGRFAVLG----RFLRLDGLREV------LAKVLLRR 207
HELICc smart00490
helicase superfamily c-terminal domain;
2380-2464 2.23e-21

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 91.12  E-value: 2.23e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875   2380 DILEDYLVYRKYPFERIDGRIRGNLRQEAIDRYSKpgsDRFVFLLCTKAGGLGINLTAADTVIIYDSDWNPQNDLQAQAR 2459
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNN---GKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77

                    ....*
gi 386768875   2460 CHRIG 2464
Cdd:smart00490   78 AGRAG 82
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
2029-2227 2.29e-21

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: 96.04  E-value: 2.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2029 LRPYQLEGLnwlKFSWYNT------------HNCILADEMGLGKTIQSLTFVHSVYEYGIRGPFLVIAPLSTIPNWQREF 2096
Cdd:cd18069     1 LKPHQIGGI---RFLYDNIieslerykgssgFGCILAHSMGLGKTLQVISFLDVLLRHTGAKTVLAIVPVNTLQNWLSEF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2097 EGWtdMNVVVYHGSVTSKQ----MIQDYEYYYKTESGKVLKEPIKFNVLITTFEMivtdymdlkaFNWR----LCVIDEA 2168
Cdd:cd18069    78 NKW--LPPPEALPNVRPRPfkvfILNDEHKTTAARAKVIEDWVKDGGVLLMGYEM----------FRLRpgpdVVICDEG 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 386768875 2169 HRLKNRNCKLLEGLRQLNLEHRVLLSGTPLQNNISELFSLLNFLEPSQFSSQEEFMSEF 2227
Cdd:cd18069   146 HRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMF 204
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
2029-2250 1.20e-18

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: 88.69  E-value: 1.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2029 LRPYQLEGLNWLkfSWYNTHNC---ILADEMGLGKTIQSLTFV--------------HSVYEYGI---------RGPFLV 2082
Cdd:cd18072     1 LLLHQKQALAWL--LWRERQKPrggILADDMGLGKTLTMIALIlaqkntqnrkeeekEKALTEWEskkdstlvpSAGTLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2083 IAPLSTIPNWQREFEGWTDMN---VVVYHGSvtskqmiqdyeyyYKTESGKVLKEpikFNVLITTFEMIVTDYMDLK--- 2156
Cdd:cd18072    79 VCPASLVHQWKNEVESRVASNklrVCLYHGP-------------NRERIGEVLRD---YDIVITTYSLVAKEIPTYKees 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2157 ------AFNWRLCVIDEAHRLKNRNCKLLEGLRQLNLEHRVLLSGTPLQNNISELFSLLNFLEPSQFSSQEEFMSEFGSl 2230
Cdd:cd18072   143 rssplfRIAWARIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQVDN- 221
                         250       260
                  ....*....|....*....|
gi 386768875 2231 RTEEEVNKLQALLKPMMLRR 2250
Cdd:cd18072   222 KSRKGGERLNILTKSLLLRR 241
BRK pfam07533
BRK domain; The function of this domain is unknown. It is often found associated with ...
4394-4437 3.09e-18

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: 81.02  E-value: 3.09e-18
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 386768875  4394 LTGEEPVPVINKQTGKRLGGNKAPQLKRLMQWLTENPNYEVDPK 4437
Cdd:pfam07533    1 LTGDERVPVVNRKTGKKLTGDKAPKLKDLEEWLEENPGYEVDPR 44
CD2_tandem cd18659
repeat 2 of paired tandem chromodomains; Repeat 2 of tandem CHRomatin Organization Modifier ...
1938-1993 2.06e-17

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


Pssm-ID: 349306 [Multi-domain]  Cd Length: 54  Bit Score: 78.77  E-value: 2.06e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 386768875 1938 DFTEVDRVLDMSvhtdeTSGETTKHYLVKWKSLPYEDCTWELEEDVDN---DKIEQYLR 1993
Cdd:cd18659     1 EYTIVERIIAHR-----EDDEGVTEYLVKWKGLPYDECTWESEEDISDifqEAIDEYKK 54
BRK smart00592
domain in transcription and CHROMO domain helicases;
4395-4439 3.22e-17

domain in transcription and CHROMO domain helicases;


Pssm-ID: 197800  Cd Length: 45  Bit Score: 78.16  E-value: 3.22e-17
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 386768875   4395 TGEEPVPVINKQTGKRLGGNKAPQLKRLMQWLTENPNYEVDPKWL 4439
Cdd:smart00592    1 DGEERVPVINRETGKKLTGDDAPKAKDLERWLEENPEYEVAPRSA 45
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
2029-2218 6.90e-15

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: 78.15  E-value: 6.90e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2029 LRPYQLEGLNWLKfswynTHNCILADEMGLGKTIQSL----------------TFVHSVYEYGIR----------GPFLV 2082
Cdd:cd18070     1 LLPYQRRAVNWML-----VPGGILADEMGLGKTVEVLalillhprpdndldaaDDDSDEMVCCPDclvaetpvssKATLI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2083 IAPLSTIPNWQREFEGWTDMNVVVYHgsvtskqmiqdYEYYYKtESGKVLKEPIKFN---VLITTFEMIVTD-------- 2151
Cdd:cd18070    76 VCPSAILAQWLDEINRHVPSSLKVLT-----------YQGVKK-DGALASPAPEILAeydIVVTTYDVLRTElhyaeanr 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2152 ----------YMDLKA-----FNWRLCViDEAHRLKNRNCKLLEGLRQLNLEHRVLLSGTPLQNNISELFSLLNFLEPSQ 2216
Cdd:cd18070   144 snrrrrrqkrYEAPPSplvlvEWWRVCL-DEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGVEP 222

                  ..
gi 386768875 2217 FS 2218
Cdd:cd18070   223 FC 224
PTZ00121 PTZ00121
MAEBL; Provisional
1419-1923 6.61e-14

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 79.41  E-value: 6.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1419 EDEKEAEAgdetVDSVPDSAGDpASTPSRRDRKRSTARSRRnanSEEGGSARKNRGSLSAKALKKRRNRGRIVPESDGED 1498
Cdd:PTZ00121 1221 EDAKKAEA----VKKAEEAKKD-AEEAKKAEEERNNEEIRK---FEEARMAHFARRQAAIKAEEARKADELKKAEEKKKA 1292
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1499 DTLDRTPPPSPPPDSEMDSNKRRSSRNTQRK-----KYIDDVMLRFSDDENSLLVASPVKKDKKPSANASNSNAGSDVEK 1573
Cdd:PTZ00121 1293 DEAKKAEEKKKADEAKKKAEEAKKADEAKKKaeeakKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKK 1372
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1574 TEpQSGAEGDAAQEVGEEKSNLPLDESSQLEASSSTSAV--AEKERQISTDAANAAMSSKPNYVYINTGDEDSMVVQLVL 1651
Cdd:PTZ00121 1373 KE-EAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELkkAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKK 1451
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1652 AMRMGKRELILDKPKE---KAPEPKQD-EEKSELDE----ATTDKPEGDEKFKTEGESKK--DLTDSEETKlesSAMEVD 1721
Cdd:PTZ00121 1452 KAEEAKKAEEAKKKAEeakKADEAKKKaEEAKKADEakkkAEEAKKKADEAKKAAEAKKKadEAKKAEEAK---KADEAK 1528
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1722 SKEESEPDDSKKSDEDNKDKDKMEVDDEVGKSDKESKPEE-------------------QSETVKTEENSKAIEEDKSST 1782
Cdd:PTZ00121 1529 KAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEakkaeedknmalrkaeeakKAEEARIEEVMKLYEEEKKMK 1608
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1783 VLTADHAKEPETVLEKMEVDEKANDDQSAVSKAEGSDEKSTDDSNPEEATTEKNKESLEIEGEKERvKEGEESVKKENDE 1862
Cdd:PTZ00121 1609 AEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK-KKAEEAKKAEEDE 1687
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386768875 1863 KTEADMENKPEPVFIDVEEYFVKYRNfsylhcEWRTEEELLKGDRRVAAKIRRFQQKQSQQ 1923
Cdd:PTZ00121 1688 KKAAEALKKEAEEAKKAEELKKKEAE------EKKKAEELKKAEEENKIKAEEAKKEAEED 1742
PTZ00121 PTZ00121
MAEBL; Provisional
1330-1923 2.51e-13

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 77.49  E-value: 2.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1330 PKDPNDPNSTETPAAVKKRAGASKRRKQYGEDGAEQTGEGSEVEDNKPLVPKAGSAD-GEAETTSGGTGVDGESPDYDDI 1408
Cdd:PTZ00121 1051 DIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTEtGKAEEARKAEEAKKKAEDARKA 1130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1409 PVSKIPRGSNEDEKEAEAGDETVDSVPDSAGDP--ASTPSRRDRKRSTARSRRNANSEEGGSARKNRGSLSAKALKKRRN 1486
Cdd:PTZ00121 1131 EEARKAEDARKAEEARKAEDAKRVEIARKAEDArkAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEE 1210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1487 RGRIVPESDGEDDT-LDRTPPPSPPPDSEMDSNKRRSSRNTQR-KKYIDDVMLRFSDDENSLLV-----ASPVKK--DKK 1557
Cdd:PTZ00121 1211 ERKAEEARKAEDAKkAEAVKKAEEAKKDAEEAKKAEEERNNEEiRKFEEARMAHFARRQAAIKAeearkADELKKaeEKK 1290
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1558 PSANASNSNAGSDVE--KTEPQSGAEGDAAQEVGEEKSNLPLDESSQLEASSSTSAVAEKERQISTDAANAAmSSKPNYV 1635
Cdd:PTZ00121 1291 KADEAKKAEEKKKADeaKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAA-EEKAEAA 1369
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1636 YINTGDEDSMVVQLVLAMRMGKRElilDKPKEKAPEPKQ--------DEEKSELDEA---TTDKPEGDEKFKTEGESKK- 1703
Cdd:PTZ00121 1370 EKKKEEAKKKADAAKKKAEEKKKA---DEAKKKAEEDKKkadelkkaAAAKKKADEAkkkAEEKKKADEAKKKAEEAKKa 1446
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1704 -DLTDSEETKLESSAMEVDSKEESEPDDSKKSDEDNKDKD--KMEVDDEVGKSDKESKPEEQ----SETVKTEENSKAIE 1776
Cdd:PTZ00121 1447 dEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADeaKKKAEEAKKKADEAKKAAEAkkkaDEAKKAEEAKKADE 1526
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1777 EDKSSTVLTADHAKEPETV-----LEKMEVDEKANDDQSAVSKAEGSDEKSTDDSNPEEA-TTEKNKESLEIEGEKERVK 1850
Cdd:PTZ00121 1527 AKKAEEAKKADEAKKAEEKkkadeLKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAkKAEEARIEEVMKLYEEEKK 1606
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386768875 1851 EGEESVKKENDEKTEADMENKPEPVFIDVEEYFVKYRNfsylhcEWRTEEELLKGDRRvaAKIRRFQQKQSQQ 1923
Cdd:PTZ00121 1607 MKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAE------EKKKAEELKKAEEE--NKIKAAEEAKKAE 1671
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
1941-1993 1.61e-12

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 64.91  E-value: 1.61e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 386768875  1941 EVDRVLDMSVhtdetSGETTKHYLVKWKSLPYEDCTWELEEDVDNDK--IEQYLR 1993
Cdd:pfam00385    2 EVERILDHRK-----DKGGKEEYLVKWKGYPYDENTWEPEENLSKCPelIEEFKD 51
PTZ00121 PTZ00121
MAEBL; Provisional
1415-1999 5.78e-12

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 73.25  E-value: 5.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1415 RGSNEDEKEAEAGDETVDSVPDSAgDPASTPSRRDRKRSTARSRRNANSEEGGSARKNRGSLS---AKALKKRRNRGRIV 1491
Cdd:PTZ00121 1315 KKADEAKKKAEEAKKKADAAKKKA-EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAkkkADAAKKKAEEKKKA 1393
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1492 PESDGEDDTlDRTPPPSPPPDSEMDSNKRRSSRNTQRKKYIDDVMLRFSDDENsllvASPVKKDKKPSANASNSNAGSDV 1571
Cdd:PTZ00121 1394 DEAKKKAEE-DKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKK----ADEAKKKAEEAKKAEEAKKKAEE 1468
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1572 EKTEPQSGAEGDAAQEVGEEKSnlpldESSQLEASSSTSAVAEKERQISTDAANAAMSSKPNYvyINTGDEDSMVVQLVL 1651
Cdd:PTZ00121 1469 AKKADEAKKKAEEAKKADEAKK-----KAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE--AKKAEEAKKADEAKK 1541
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1652 AMRMGKRELIldkpkEKAPEPKQDEEKSELDEATTDKPEGDEKFKTEGESKKdltdSEETKLESSAMEVDSKEESEPDDS 1731
Cdd:PTZ00121 1542 AEEKKKADEL-----KKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKK----AEEARIEEVMKLYEEEKKMKAEEA 1612
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1732 KKSDEDNKDKDKMEVDDEVGKSDKESKPEEQSETVKTEENSKAIEEDKsstVLTADHAKEPETVLEKMEVDEKANDDQSA 1811
Cdd:PTZ00121 1613 KKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENK---IKAAEEAKKAEEDKKKAEEAKKAEEDEKK 1689
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1812 VSKA---EGSDEKSTDDSNPEEATTEKNKESLEIEgEKERVKEGEESVKKENDEKTEA-----DMENKPEPVFIDVEEYf 1883
Cdd:PTZ00121 1690 AAEAlkkEAEEAKKAEELKKKEAEEKKKAEELKKA-EEENKIKAEEAKKEAEEDKKKAeeakkDEEEKKKIAHLKKEEE- 1767
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1884 vKYRNFSYLHCEWRTEEELLKGDRRVAAKI-RRFQQKQSQQLNIFE-NIEDEPFNQDF-----TEVDRVLDMSVHTDETS 1956
Cdd:PTZ00121 1768 -KKAEEIRKEKEAVIEEELDEEDEKRRMEVdKKIKDIFDNFANIIEgGKEGNLVINDSkemedSAIKEVADSKNMQLEEA 1846
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*..
gi 386768875 1957 GETTKHYLVKwKSLPYEDCTWEL----EEDVDNDKIEQYLRFNKIPQ 1999
Cdd:PTZ00121 1847 DAFEKHKFNK-NNENGEDGNKEAdfnkEKDLKEDDEEEIEEADEIEK 1892
MDN1 COG5271
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ...
1242-1881 1.20e-11

Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444083 [Multi-domain]  Cd Length: 1028  Bit Score: 71.97  E-value: 1.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1242 GAANAVSSIPTTQLPVSEDCVTQGAGDTSVVGMLEYSEGMGDLSQDVHSANELDTSTDGSGKKKKPRKPRTPKDPNKPPR 1321
Cdd:COG5271   289 LDAELTAAQAADPESDDDADDSTLAALEGAAEDTEIATADELAAADDEDDDDSAAEDAAEEAATAEDSAAEDTQDAEDEA 368
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1322 DRTPKAKKPKDPNDPNSTETPAAVKKRAGASKRRKQYGEDGAEQTGEGSEVEDNKPLVPKAGSADGEAETTSGGTGVDGE 1401
Cdd:COG5271   369 AGEAADESEGADTDAAADEADAAADDSADDEEASADGGTSPTSDTDEEEEEADEDASAGETEDESTDVTSAEDDIATDEE 448
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1402 SPDYDDIPVSKIPRGSNEDEKEAEAGDETVDSVPDSAGDPASTPSRRDRKRSTARSRRNANSEEGGSARKNRGSLSAKAL 1481
Cdd:COG5271   449 ADSLADEEEEAEAELDTEEDTESAEEDADGDEATDEDDASDDGDEEEAEEDAEAEADSDELTAEETSADDGADTDAAADP 528
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1482 KKRRNRGR-----IVPESDGEDDTLDRTPPPSPPPDSEMDSNKRRSSRNTQRKKYIDDVMLRFSDDENsllvASPVKKDK 1556
Cdd:COG5271   529 EDSDEDALedeteGEENAPGSDQDADETDEPEATAEEDEPDEAEAETEDATENADADETEESADESEE----AEASEDEA 604
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1557 KPSANASNSNAGSDVEKTEPQSGAEGDAAQEVGEEKSN-LPLDESSQLEASSSTSAVAEKERQISTDAANAAmSSKPNY- 1634
Cdd:COG5271   605 AEEEEADDDEADADADGAADEEETEEEAAEDEAAEPETdASEAADEDADAETEAEASADESEEEAEDESETS-SEDAEEd 683
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1635 ----VYINTGDEDSMVVqlvlamRMGKRELILDKPKEKAPEPKQDEEKSELDEATTDKPEGDEKfKTEGESKKDLTDSEE 1710
Cdd:COG5271   684 adaaAAEASDDEEETEE------ADEDAETASEEADAEEADTEADGTAEEAEEAAEEAESADEE-AASLPDEADAEEEAE 756
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1711 TKLESSAMEVDSKEESEPDDSKKSDEDNKDKDKMEVDDEVGKSDKESKPEEQSETVKTEENSKAIEEDKSSTVLTADHAK 1790
Cdd:COG5271   757 EAEEAEEDDADGLEEALEEEKADAEEAATDEEAEAAAEEKEKVADEDQDTDEDALLDEAEADEEEDLDGEDEETADEALE 836
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1791 EPETVLEKMEVDEKANDDQSAVSKAEGSDEKSTDDSNPEEATTEKNKESLEIEGEKERVKEGEESVKKENDEKTEADMEN 1870
Cdd:COG5271   837 DIEAGIAEDDEEDDDAAAAKDVDADLDLDADLAADEHEAEEAQEAETDADADADAGEADSSGESSAAAEDDDAAEDADSD 916
                         650
                  ....*....|.
gi 386768875 1871 KPEPVFIDVEE 1881
Cdd:COG5271   917 DGANDEDDDDD 927
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
2029-2227 8.36e-11

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: 65.06  E-value: 8.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2029 LRPYQLEGLNWLKFSWYNthnCILADeMGLGKTIQSLTFVHSVYEYGIRGPFLVIAPLSTIPN-WQREFEGWTDMNVVVY 2107
Cdd:cd18013     1 PHPYQKVAINFIIEHPYC---GLFLD-MGLGKTVTTLTALSDLQLDDFTRRVLVIAPLRVARStWPDEVEKWNHLRNLTV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2108 HGSVTSkqmiqdyeyyyKTESGKVLKEPIkfNVLITTFEMIV-TDYMDLKAFNWRLCVIDEAHRLKNRNCKLLEGLRQLN 2186
Cdd:cd18013    77 SVAVGT-----------ERQRSKAANTPA--DLYVINRENLKwLVNKSGDPWPFDMVVIDELSSFKSPRSKRFKALRKVR 143
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 386768875 2187 --LEHRVLLSGTPLQNNISELFSLLNFLEPSQfsSQEEFMSEF 2227
Cdd:cd18013   144 pvIKRLIGLTGTPSPNGLMDLWAQIALLDQGE--RLGRSITAY 184
PTZ00121 PTZ00121
MAEBL; Provisional
1326-1867 3.08e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 67.47  E-value: 3.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1326 KAKKPKDPNDPNSTETPAAVKKRAGASKRRKQYGEDGAEQTGEGSEVEDNKPLVPKAGSADGEAEttsggtgvdgespdy 1405
Cdd:PTZ00121 1337 KAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAE--------------- 1401
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1406 DDIPVSKIPRGSNEDEKEAEAGDETVDSV--PDSAGDPASTPSRRDRKRSTARSRRNANSEEGGSARKNRgslsAKALKK 1483
Cdd:PTZ00121 1402 EDKKKADELKKAAAAKKKADEAKKKAEEKkkADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK----ADEAKK 1477
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1484 RRNRGRIVPESDGEDDTLDRTPPPSPPPDSEmdSNKRRSSRNTQRKKYIDDvmLRFSDDENSLLVASPVKKDKKpsanAS 1563
Cdd:PTZ00121 1478 KAEEAKKADEAKKKAEEAKKKADEAKKAAEA--KKKADEAKKAEEAKKADE--AKKAEEAKKADEAKKAEEKKK----AD 1549
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1564 NSNAGSDVEKTEPQSGAEgDAAQEvgEEKSNLPL---DESSQLEAS--SSTSAVAEKERQISTDAANAAMSSKPNYVYIN 1638
Cdd:PTZ00121 1550 ELKKAEELKKAEEKKKAE-EAKKA--EEDKNMALrkaEEAKKAEEAriEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK 1626
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1639 TGDEDSMVVQlvlamRMGKRElilDKPKEKAPEPKQDEEKSELDEATTDKPEGDEKFKTEgESKKdltDSEETKLESSAM 1718
Cdd:PTZ00121 1627 KAEEEKKKVE-----QLKKKE---AEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAE-EAKK---AEEDEKKAAEAL 1694
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1719 EVDSKEESEPDDSKKSDEDNKDK-DKMEVDDEVGKSD-KESKPEEQSETVKTEENSKAIEEDKSSTVLTADHAKEPETVL 1796
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEAEEKKKaEELKKAEEENKIKaEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIR 1774
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386768875 1797 EKMEVDEKANDDQSAVSKAEGSDEKSTDDSNPEEATTEKNKE-SLEIEGEKE-RVKEGEESVKKENDEKTEAD 1867
Cdd:PTZ00121 1775 KEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEgNLVINDSKEmEDSAIKEVADSKNMQLEEAD 1847
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
2048-2196 7.98e-10

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: 60.49  E-value: 7.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2048 HNCILADEMGLGKTIQSLTFVHSVYEYGiRGPFLVIAPLSTI-PNWQREFEGWTDMNVVVyhgsvtskQMIQDYEYYYKT 2126
Cdd:cd00046     2 ENVLITAPTGSGKTLAALLAALLLLLKK-GKKVLVLVPTKALaLQTAERLRELFGPGIRV--------AVLVGGSSAEER 72
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386768875 2127 ESGKVLKEPIkfnvLITTFEMIVTDYMDLKAF---NWRLCVIDEAHRLKN-----RNCKLLEGLRQLNLEHRVLLSGT 2196
Cdd:cd00046    73 EKNKLGDADI----IIATPDMLLNLLLREDRLflkDLKLIIVDEAHALLIdsrgaLILDLAVRKAGLKNAQVILLSAT 146
CD1_tandem cd18660
repeat 1 of paired tandem chromodomains; Repeat 1 of tandem CHRomatin Organization Modifier ...
1861-1917 8.94e-10

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


Pssm-ID: 349307 [Multi-domain]  Cd Length: 70  Bit Score: 57.76  E-value: 8.94e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 386768875 1861 DEKTEADMENKPEP-VFIDVEEYFVKYRNFSYLHCEWRTEEELLKgdRRVAAKIRRFQ 1917
Cdd:cd18660    14 KGPVEEASLDLTDPdEPWDEREFLVKWKGKSYLHCTWVTEETLEQ--LRGKKKLKNYI 69
CHROMO smart00298
Chromatin organization modifier domain;
1941-1993 5.04e-09

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 55.30  E-value: 5.04e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 386768875   1941 EVDRVLDMSVHtdetsGETTKHYLVKWKSLPYEDCTWELEEDVDND--KIEQYLR 1993
Cdd:smart00298    3 EVEKILDHRWK-----KKGELEYLVKWKGYSYSEDTWEPEENLLNCskKLDNYKK 52
CD2_tandem_CHD3-4_like cd18662
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 3 and ...
1942-1991 1.15e-08

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


Pssm-ID: 349309 [Multi-domain]  Cd Length: 55  Bit Score: 54.19  E-value: 1.15e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 386768875 1942 VDRVLDMSVHTDetsGETtkHYLVKWKSLPYEDCTWElEEDVD----NDKIEQY 1991
Cdd:cd18662     6 IHRIINHRVDKD---GNT--WYLVKWRDLPYDQSTWE-SEDDDipdyEKHIQEY 53
PTZ00121 PTZ00121
MAEBL; Provisional
1326-1904 1.74e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 61.70  E-value: 1.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1326 KAKKPKDPNDPNSTETPAAVKKRA------GASKRRKQYGEDGAEQTGEGSEVEDNKPLVPKAGSADGEAETTSGGTGVD 1399
Cdd:PTZ00121 1397 KKKAEEDKKKADELKKAAAAKKKAdeakkkAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAK 1476
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1400 GESPDyddipvskiPRGSNEDEKEAEAGDETVDSV--PDSAGDPASTPSRRDRKRSTARSRRNANSEEGGSARKNRGSLS 1477
Cdd:PTZ00121 1477 KKAEE---------AKKADEAKKKAEEAKKKADEAkkAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKK 1547
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1478 AKALKKrrnrgriVPESDGEDDTLDRTPPPSPPPDSEMDSNKRRSSRNTQRKKyIDDVMLRFsdDENSLLVASPVKKDKK 1557
Cdd:PTZ00121 1548 ADELKK-------AEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR-IEEVMKLY--EEEKKMKAEEAKKAEE 1617
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1558 PSANASNSNAGSDVEKTEPQsgAEGDAAQEVGEEKSNLPLDESSQLEASSSTSAvAEKERQISTDAANAAMSSKPnyvyi 1637
Cdd:PTZ00121 1618 AKIKAEELKKAEEEKKKVEQ--LKKKEAEEKKKAEELKKAEEENKIKAAEEAKK-AEEDKKKAEEAKKAEEDEKK----- 1689
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1638 ntgdedsmvvqlvlAMRMGKRElilDKPKEKAPEPKQDEEKSELDEATTDKPEGDEKFKTEgESKKdltDSEETKLESSA 1717
Cdd:PTZ00121 1690 --------------AAEALKKE---AEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAE-EAKK---EAEEDKKKAEE 1748
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1718 MEVDSKEESEPDDSKKSDEDNKDKDKME----VDDEVGKSDKESKPEEQSETVKTEENSKAIEEDKSSTVLTADHAKEPE 1793
Cdd:PTZ00121 1749 AKKDEEEKKKIAHLKKEEEKKAEEIRKEkeavIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEME 1828
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1794 TVLEKMEVDEKANDDQSAVSKAEGSDEKSTDDSNPEEATTEKNKESLEIEGEKERVKEGEESVKKENDEKTEADMENKPE 1873
Cdd:PTZ00121 1829 DSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMA 1908
                         570       580       590
                  ....*....|....*....|....*....|....*...
gi 386768875 1874 P-------VFIDVEEYfvKYRNFSylhcewRTEEELLK 1904
Cdd:PTZ00121 1909 GknndiidDKLDKDEY--IKRDAE------ETREEIIK 1938
CD_CSD cd00024
CHROMO (CHRromatin Organization Modifier) domains and chromo shadow domains; Members of this ...
1941-1993 1.84e-08

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


Pssm-ID: 349274 [Multi-domain]  Cd Length: 50  Bit Score: 53.25  E-value: 1.84e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 386768875 1941 EVDRVLDMSVHTDETsgettkHYLVKWKSLPYEDCTWELEEDVDNDK--IEQYLR 1993
Cdd:cd00024     2 EVEKILDHRVRKGKL------EYLVKWKGYPPEENTWEPEENLTNAPelIKEYEK 50
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
1968-2590 1.28e-07

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 58.11  E-value: 1.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1968 KSLPYEDCTWELEEDVDNDKIEQYLRFNKIPQRSEWKSKKRPHPELWKKL--EKTPVYKGGNSLRPYQLEGLN-WLKFSW 2044
Cdd:COG1061    18 LLLLDLERLELSLLRNLVEARRLAIKEGTREDGRRLPEEDTERELAEAEAleAGDEASGTSFELRPYQQEALEaLLAALE 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2045 YNTHNCILADEMGLGKTIqslTFVHSVYEYGIRGPFLVIAPLSTIPN-WQREFEGWTDmnvvvyhgsvtskqmiqdyeyy 2123
Cdd:COG1061    98 RGGGRGLVVAPTGTGKTV---LALALAAELLRGKRVLVLVPRRELLEqWAEELRRFLG---------------------- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2124 ykTESGKVLKEPIKFNVLITTFEMIVTDyMDLKAF--NWRLCVIDEAHRLKNRncKLLEGLRQLNLEHRVLLSGTPLQNN 2201
Cdd:COG1061   153 --DPLAGGGKKDSDAPITVATYQSLARR-AHLDELgdRFGLVIIDEAHHAGAP--SYRRILEAFPAAYRLGLTATPFRSD 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2202 iselfsllnflepsqfsSQEEFMSEFGSLRTEEEVNKLQAllkpmmlrrlkddvEKSLAPKEETIIEVELTNIQKKYyrg 2281
Cdd:COG1061   228 -----------------GREILLFLFDGIVYEYSLKEAIE--------------DGYLAPPEYYGIRVDLTDERAEY--- 273
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2282 ileqnfsflkkgttsanipnlmntmmelrkccihpyllngaeeqiqydfksqhgEDPESYYKNLILSAGKMVL--IDKLL 2359
Cdd:COG1061   274 ------------------------------------------------------DALSERLREALAADAERKDkiLRELL 299
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2360 PKLkANGHRVLIFSQMVRCLDILEDYLVYRKYPFERIDGRIRGNLRQEAIDRYSkpgSDRFVFLLCTKAGGLGINLTAAD 2439
Cdd:COG1061   300 REH-PDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFR---DGELRILVTVDVLNEGVDVPRLD 375
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2440 TVIIYDSDWNPQNDLQAQARCHRIGQRK-MVKIYRLLCRNT-YEREMFDKASMKLGLDKAVLQSMNTQGSKDGNNKQLSK 2517
Cdd:COG1061   376 VAILLRPTGSPREFIQRLGRGLRPAPGKeDALVYDFVGNDVpVLEELAKDLRDLAGYRVEFLDEEESEELALLIAVKPAL 455
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386768875 2518 KEIEDLLKKGAYGAVMDDDNAGDKFCEEDIDSILKRRTQVITMESEKGSTFSKASFAASGNRSDITIDDPDFW 2590
Cdd:COG1061   456 EVKGELEEELLEELELLEDALLLVLAELLLLELLALALELLELAKAEGKAEEEEEEKELLLLLALAKLLKLLL 528
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
1335-1792 3.24e-07

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


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 57.23  E-value: 3.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1335 DPNSTETPAAVKKRAGASK----RRKQYGEDGAEQTGEGSEVEDNKPLVPKAGSADGEAETTSGGTGVDGESPDYDDipv 1410
Cdd:NF033609  496 DPNSKGDLALRSTLYGYNSniiwRSMSWDNEVAFNNGSGSGDGIDKPVVPEQPDEPGEIEPIPEDSDSDPGSDSGSD--- 572
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1411 skiprGSNEDEKEAEAGDETVDSVPDSAGDPASTPSRRDRKRSTARSRRNANSEEGGSARKNRGSLSAKAlkkrrnrgri 1490
Cdd:NF033609  573 -----SSNSDSGSDSGSDSTSDSGSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSA---------- 637
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1491 vPESDGEDDTlDRTPPPSPPPDSEMDSNKRRSSRNTQRKKYIDDVMLRFSDDENSllvaspvkkdKKPSANASNSNAGSD 1570
Cdd:NF033609  638 -SDSDSDSDS-DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS----------DSDSDSDSDSDSDSD 705
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1571 VEkTEPQSGAEGDAAQEvGEEKSNLPLDESSQLEASSSTSAVAEKERQISTDAANAAMSSKpnyvyintgDEDSmvvqlv 1650
Cdd:NF033609  706 SD-SDSDSDSDSDSDSD-SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS---------DSDS------ 768
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1651 lamrmgkrelilDKPKEKAPEPKQDEEkSELDEATTDKPEGDEKFKTEGESKKDlTDSEETKLESSAMEVDSKEESEPDD 1730
Cdd:NF033609  769 ------------DSDSDSDSDSDSDSD-SDSDSDSDSDSDSDSDSDSDSDSDSD-SDSDSDSDSDSDSDSDSDSDSDSDS 834
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386768875 1731 SKKSDEDN-KDKDKMEVDDEVGKSDKESKPEEQSETVKTEENSKAiEEDKSSTVLTADHAKEP 1792
Cdd:NF033609  835 DSDSDSDSdSDSDSDSDSDSDSESDSNSDSESGSNNNVVPPNSPK-NGTNASNKNEAKDSKEP 896
PRK05901 PRK05901
RNA polymerase sigma factor; Provisional
1663-1869 8.49e-07

RNA polymerase sigma factor; Provisional


Pssm-ID: 235640 [Multi-domain]  Cd Length: 509  Bit Score: 55.39  E-value: 8.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1663 DKPKEKAPEPKQDEEKSELDEATTDKPEGDEKFKTEGESKKDLTDSEETKLESSAMEVDSKEESEPDDSKKSDEDNKDKD 1742
Cdd:PRK05901    6 TKAELAAEEEAKKKLKKLAAKSKSKGFITKEEIKEALESKKKTPEQIDQVLIFLSGMVKDTDDATESDIPKKKTKTAAKA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1743 KMEVDDEVGKSDKESKPEEQSETVKTEENSKAIEEDKSSTVLTADHAKEPETVLEKMEvDEKANDDQSAVSKAEGSDEKS 1822
Cdd:PRK05901   86 AAAKAPAKKKLKDELDSSKKAEKKNALDKDDDLNYVKDIDVLNQADDDDDDDDDDDLD-DDDIDDDDDDEDDDEDDDDDD 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 386768875 1823 TDDSNpeeattEKNKESLEIEGEKERVKEGEESVKKENDEKTEADME 1869
Cdd:PRK05901  165 VDDED------EEKKEAKELEKLSDDDDFVWDEDDSEALRQARKDAK 205
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
1591-1882 8.96e-07

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 55.95  E-value: 8.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1591 EKSNLPLDESSQLEASSSTSAVAEK---ERQIS-------TDAANAAMSSKPNYVYINTGDEDSMV--VQLVLAMRMGKR 1658
Cdd:PTZ00341  814 ENINLNEDNENGSKKILDLNHKDQKeifEEIISyivdislSDIENTAKNAAEQILSDEGLDEKKLKkrAESLKKLANAIE 893
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1659 ELILDKPKEKAPEPKQDEEKS------------ELDEATTDKPEgDEKFKTEGESKKDLTDSEETKLESSAMEvdSKEES 1726
Cdd:PTZ00341  894 KYAGGGKKDKKAKKKDAKDLSgniaheinlinkELKNQNENVPE-HLKEHAEANIEEDAEENVEEDAEENVEE--NVEEN 970
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1727 EPDDSKKSDEDNKDKDKME-VDDEVGKSDKESKPEEQSETVK--TEENSKAIEEDKSSTVLTADHAKEPETVlEKMEVDE 1803
Cdd:PTZ00341  971 VEENVEENVEENVEENVEEnVEENVEENVEENIEENVEENVEenIEENVEEYDEENVEEVEENVEEYDEENV-EEIEENA 1049
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386768875 1804 KANDDQSAVSKAEGSDEKSTDdsNPEEATTEKNKESLEiEGEKERVKEGEESVKKENDEKTEadmENKPEPVFIDVEEY 1882
Cdd:PTZ00341 1050 EENVEENIEENIEEYDEENVE--EIEENIEENIEENVE-ENVEENVEEIEENVEENVEENAE---ENAEENAEENAEEY 1122
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
1682-1963 1.23e-06

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 55.56  E-value: 1.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1682 DEATTDKPEGDEKFKTEGESKKDLTDSEET-KLESSAMEvdskeesEPDDSKKSDEDNKDKDKMEVD----DEVGKSDKE 1756
Cdd:PTZ00341  855 DIENTAKNAAEQILSDEGLDEKKLKKRAESlKKLANAIE-------KYAGGGKKDKKAKKKDAKDLSgniaHEINLINKE 927
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1757 SKPEEQSETVKTEENSKA-IEEDKSSTVLTADHAKEPETVLEKMEVDEKANDDQSAVSKAEGSDEKSTDDS---NPEEAT 1832
Cdd:PTZ00341  928 LKNQNENVPEHLKEHAEAnIEEDAEENVEEDAEENVEENVEENVEENVEENVEENVEENVEENVEENVEENveeNIEENV 1007
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1833 TEKNKESLE---IEGEKERVKEGEESVKKENDEKTEADMENKPEPVFIDVEEYFVKYRNFSYLHCEWRTEEELLKG-DRR 1908
Cdd:PTZ00341 1008 EENVEENIEenvEEYDEENVEEVEENVEEYDEENVEEIEENAEENVEENIEENIEEYDEENVEEIEENIEENIEENvEEN 1087
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 386768875 1909 VAAKIRRFQQKQSQqlNIFENIE---DEPFNQDFTEVDrvldmsvhtDETSGETTKHY 1963
Cdd:PTZ00341 1088 VEENVEEIEENVEE--NVEENAEenaEENAEENAEEYD---------DENPEEHNEEY 1134
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
3488-3713 1.33e-06

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 55.18  E-value: 1.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 3488 KNEVIDLDDELMTNESVIKKEspvtpIKEEIKSEESPEKHDTADNLEDknsDAEESTKIKGKEdfNPETTEKEALDESTN 3567
Cdd:PTZ00341  907 KKDAKDLSGNIAHEINLINKE-----LKNQNENVPEHLKEHAEANIEE---DAEENVEEDAEE--NVEENVEENVEENVE 976
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 3568 LNKDKSSTETLVPEIEDSKPSEDKMEVEElPVAENGEkEGSPEKCSDAEDKKFSEEKPSSPAVPDGKVSEMEaDEAAPNT 3647
Cdd:PTZ00341  977 ENVEENVEENVEENVEENVEENVEENIEE-NVEENVE-ENIEENVEEYDEENVEEVEENVEEYDEENVEEIE-ENAEENV 1053
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386768875 3648 EENCSGDSESPEKECEDKVVEKVEEEKGENSYEKAEEQKEETEKLEKSSIESEPSEKSETVLEPEV 3713
Cdd:PTZ00341 1054 EENIEENIEEYDEENVEEIEENIEENIEENVEENVEENVEEIEENVEENVEENAEENAEENAEENA 1119
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
1532-1867 1.40e-06

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


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 55.30  E-value: 1.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1532 IDDVMLRFSDDENSLLVASPVKKDKKPSanasnSNAGSDVEKTEPQSGAEGDAAQEVGEEKSNLPLDESSQLEASSSTSA 1611
Cdd:NF033609  539 IDKPVVPEQPDEPGEIEPIPEDSDSDPG-----SDSGSDSSNSDSGSDSGSDSTSDSGSDSASDSDSASDSDSASDSDSA 613
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1612 VAEKERQISTDAANAAMSSKPNYVYINTGDEDSMVVQLVLAMRMGKRELILDKPKEKAPEPKQDEEKSELDEATTDKpEG 1691
Cdd:NF033609  614 SDSDSASDSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS-DS 692
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1692 DEKFKTEGESKKDlTDSEETKLESSAMEVDSKEESEPDDSKKSDEDNkDKDKMEVDDEVGKSDKESKPEEQSETvKTEEN 1771
Cdd:NF033609  693 DSDSDSDSDSDSD-SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS-DSDSDSDSDSDSDSDSDSDSDSDSDS-DSDSD 769
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1772 SKAIEEDKSSTVLTADHAKEPETVLEKMEVDEKANDDQSAVSKAEGSDEKSTDDSNPEEATTEKNKESLEIEGEKERVKE 1851
Cdd:NF033609  770 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 849
                         330
                  ....*....|....*.
gi 386768875 1852 GEESVKKENDEKTEAD 1867
Cdd:NF033609  850 SDSDSDSESDSNSDSE 865
PRK12678 PRK12678
transcription termination factor Rho; Provisional
1338-1541 2.32e-06

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 54.14  E-value: 2.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1338 STETPAAVKKRAGASKRRKQYGEDGAEQTGEGSEVEDNKPLVPKAGSADGEAETTSGGTGVDGESPDYDDIPVSKIPRGS 1417
Cdd:PRK12678   69 TPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEG 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1418 NEDEKEAEAGDETVDSVPDSAGDPASTPSRRDRKRSTARSRRNANSEEGGSARKNRGSLSAKALKKRRNRGRivpeSDGE 1497
Cdd:PRK12678  149 GEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREERGR----RDGG 224
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 386768875 1498 DDTLDRTPPPSPPPDSEMDSNKRRSSRNTQRKKYIDDVMLRFSD 1541
Cdd:PRK12678  225 DRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRFRD 268
MDN1 COG5271
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ...
1363-1874 4.92e-06

Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444083 [Multi-domain]  Cd Length: 1028  Bit Score: 53.48  E-value: 4.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1363 AEQTGEGSEVEDNKPLVPKAGSADGEAETTSGGtgvdgESPDYDDIPVSKIPRGSNEDEKEAEAGDETVDSVPDSAGDPA 1442
Cdd:COG5271   478 GDEATDEDDASDDGDEEEAEEDAEAEADSDELT-----AEETSADDGADTDAAADPEDSDEDALEDETEGEENAPGSDQD 552
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1443 STPSRRDRKRSTARSRRNANSEEGGSARKNRGSLSAKALKKRRNRGRIVPESDGEDDTLDRTPPPSPppDSEMDSNKRRS 1522
Cdd:COG5271   553 ADETDEPEATAEEDEPDEAEAETEDATENADADETEESADESEEAEASEDEAAEEEEADDDEADADA--DGAADEEETEE 630
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1523 SRNTQRKKYIDDVMLRFSDDENSLLVASPVKKDKKPSANASNSnagsDVEKTEPQSGAEGDAAQEVGEEKSNLPLDE--S 1600
Cdd:COG5271   631 EAAEDEAAEPETDASEAADEDADAETEAEASADESEEEAEDES----ETSSEDAEEDADAAAAEASDDEEETEEADEdaE 706
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1601 SQLEASSSTSAVAEKERQISTDAANAAMSskpnyvyiNTGDEDSmvvqlvlamrmgkrelildkpkeKAPEPKQDEEKSE 1680
Cdd:COG5271   707 TASEEADAEEADTEADGTAEEAEEAAEEA--------ESADEEA-----------------------ASLPDEADAEEEA 755
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1681 LDEATTDKPEGDEkfkTEGESKKDLTDSEETKLESSAMEVDSKEESEPDDSKKSDEDNKDKDKMEVDDEVGKSDKESKPE 1760
Cdd:COG5271   756 EEAEEAEEDDADG---LEEALEEEKADAEEAATDEEAEAAAEEKEKVADEDQDTDEDALLDEAEADEEEDLDGEDEETAD 832
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1761 EQSETVKtEENSKAIEEDKSSTVLTADHAKEPETVLEKMEVDEKANDDQSAVSKAEGSDEKSTDDSNPEEATTEKNKESL 1840
Cdd:COG5271   833 EALEDIE-AGIAEDDEEDDDAAAAKDVDADLDLDADLAADEHEAEEAQEAETDADADADAGEADSSGESSAAAEDDDAAE 911
                         490       500       510
                  ....*....|....*....|....*....|....
gi 386768875 1841 EIEGEKERVKEGEESVKKENDEKTEADMENKPEP 1874
Cdd:COG5271   912 DADSDDGANDEDDDDDAEEERKDAEEDELGAAED 945
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
1572-1859 5.01e-06

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 53.46  E-value: 5.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875  1572 EKTEPQSGAEGDAAQEVGEEKSNlplDESSQLEASSSTSAVAEKERQISTDAANAAMSSKPNYvyinTGDEDSMVVQLVl 1651
Cdd:TIGR00927  647 EEGERPTEAEGENGEESGGEAEQ---EGETETKGENESEGEIPAERKGEQEGEGEIEAKEADH----KGETEAEEVEHE- 718
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875  1652 amrmgkrelilDKPKEKAPEPKQDEEKSELDEATTDKPEGDEKFKTEGESKKDLTDSEETKLESSAMEVDSKE---ESEP 1728
Cdd:TIGR00927  719 -----------GETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEgeiQAGE 787
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875  1729 DDSKKSDEDNKDKDKMEvddEVGKSDKESKPEEQSETVKTEENSKAIEEDKSSTVLTADHAKEpetvlekmevDEKANDD 1808
Cdd:TIGR00927  788 DGEMKGDEGAEGKVEHE---GETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQ----------DEKGVDG 854
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 386768875  1809 QSAVSKAEGSDEKSTDDSNPEEATTEKNKESLEIEGEKERVKEGEESVKKE 1859
Cdd:TIGR00927  855 GGGSDGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENEEPLSLEWPETRQKQ 905
DMP1 pfam07263
Dentin matrix protein 1 (DMP1); This family consists of several mammalian dentin matrix ...
1359-1747 7.78e-06

Dentin matrix protein 1 (DMP1); This family consists of several mammalian dentin matrix protein 1 (DMP1) sequences. The dentin matrix acidic phosphoprotein 1 (DMP1) gene has been mapped to human chromosome 4q21. DMP1 is a bone and teeth specific protein initially identified from mineralized dentin. DMP1 is primarily localized in the nuclear compartment of undifferentiated osteoblasts. In the nucleus, DMP1 acts as a transcriptional component for activation of osteoblast-specific genes like osteocalcin. During the early phase of osteoblast maturation, Ca(2+) surges into the nucleus from the cytoplasm, triggering the phosphorylation of DMP1 by a nuclear isoform of casein kinase II. This phosphorylated DMP1 is then exported out into the extracellular matrix, where it regulates nucleation of hydroxyapatite. DMP1 is a unique molecule that initiates osteoblast differentiation by transcription in the nucleus and orchestrates mineralized matrix formation extracellularly, at later stages of osteoblast maturation. The DMP1 gene has been found to be ectopically expressed in lung cancer although the reason for this is unknown.


Pssm-ID: 462128 [Multi-domain]  Cd Length: 519  Bit Score: 52.24  E-value: 7.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875  1359 GEDGAEQTGEGSEVEDNKPLV---PKAGSADGEAETTSG--GTGVDGESPDYDdipvskiprgSNEDEKEAEAGDetvds 1433
Cdd:pfam07263  153 GEDSAQDTTSESRDLDNEDEVssrPESGDSTQDSESEEHwvGGGSEGDSSHGD----------GSEFDDEGMQSD----- 217
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875  1434 vpdsagDPASTPSRRDRKR---STARSRRNANSEEGGSARKNRGSLSAKALKKRRNRGRIVPESDGEDDTLDRTPPPSPP 1510
Cdd:pfam07263  218 ------DPDSIRSERGNSRmssASVKSKESKGDSEQASTQDSGDSQSVEYPSRKFFRKSRISEEDDRGELDDSNTMEEVK 291
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875  1511 PDSEMDSNKRrssrntqrkkyiddvmlrfsddensllvaspvkkDKKPSANASNSNAGSDVEKTEPQSGAEGDAAQEVGE 1590
Cdd:pfam07263  292 SDSTESTSSK----------------------------------EAGLSQSREDSKSESQEDSEESQSQEDSQNSQDPSS 337
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875  1591 EKSNlPLDESSQLEASSSTSAVAEKERQISTDAANAAMSSKPNYvyiNTGDEDSmvvqlvlamrmgkreliLDKPKEKAP 1670
Cdd:pfam07263  338 ESSQ-EADLPSQESSSESQEEVVSESRGDNPDNTSSSEEDQEDS---DSSEEDS-----------------LSTFSSSES 396
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875  1671 EPKQDEEKSELDEATTDKPEGDEKFKTEGESKKDLTDSEETKLESSAMEVD--------------------SKEESEPDD 1730
Cdd:pfam07263  397 ESREEQADSESNESLRSSEESPESSEDENSSSQEGLQSHSASTESQSEESQseqdsqseeddesdsqdssrSKEDSNSTE 476
                          410
                   ....*....|....*..
gi 386768875  1731 SKKSDEDNKDKDKMEVD 1747
Cdd:pfam07263  477 STSSSEEDGQSKNMEIE 493
CD1_tandem_CHD3-4_like cd18667
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 3 and ...
1853-1902 7.88e-06

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


Pssm-ID: 349314 [Multi-domain]  Cd Length: 79  Bit Score: 46.95  E-value: 7.88e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 386768875 1853 EESVKKENDEKTEADMENKPEpvfidvEEYFVKYRNFSYLHCEWRTEEEL 1902
Cdd:cd18667    23 PEKPDEDPYPPPPRKLQPRPE------REFFVKWHGMSYWHCEWVSELQL 66
PRK05901 PRK05901
RNA polymerase sigma factor; Provisional
1591-1786 8.13e-06

RNA polymerase sigma factor; Provisional


Pssm-ID: 235640 [Multi-domain]  Cd Length: 509  Bit Score: 52.30  E-value: 8.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1591 EKSNLPLDESSQLEASSSTSAVAEKERQISTDAANAA-MSSKPNYVYINTGDEDSMVVQLVLAMRMGKRELILDKPKEKA 1669
Cdd:PRK05901    6 TKAELAAEEEAKKKLKKLAAKSKSKGFITKEEIKEALeSKKKTPEQIDQVLIFLSGMVKDTDDATESDIPKKKTKTAAKA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1670 PEPKQDEEKSELDEATTDKPE------GDEKFKTEGESKKDLTDSEETKLESSAMEVDSKEESEPDDSKKSDEDNKDKDK 1743
Cdd:PRK05901   86 AAAKAPAKKKLKDELDSSKKAekknalDKDDDLNYVKDIDVLNQADDDDDDDDDDDLDDDDIDDDDDDEDDDEDDDDDDV 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 386768875 1744 MEVDDEVGKSDKESKPEEQSETVKTEENSKAIEEDKSSTVLTA 1786
Cdd:PRK05901  166 DDEDEEKKEAKELEKLSDDDDFVWDEDDSEALRQARKDAKLTA 208
ResIII pfam04851
Type III restriction enzyme, res subunit;
2028-2171 9.73e-06

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 48.82  E-value: 9.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875  2028 SLRPYQLEGL-NWLKFSWYNTHNCILADEMGLGKTIQSLTFVHSVYEYGIRGPFLVIAP-LSTIPNWQREFEGWTDmnvv 2105
Cdd:pfam04851    3 ELRPYQIEAIeNLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFKKGPIKKVLFLVPrKDLLEQALEEFKKFLP---- 78
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386768875  2106 vyhgsvtskqmiqdyEYYYKTESGKVLKEPIKFN---VLITTFEMI----VTDYMDLKAFNWRLCVIDEAHRL 2171
Cdd:pfam04851   79 ---------------NYVEIGEIISGDKKDESVDdnkIVVTTIQSLykalELASLELLPDFFDVIIIDEAHRS 136
PTZ00121 PTZ00121
MAEBL; Provisional
3496-3790 1.47e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.07  E-value: 1.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 3496 DELMTNESVIKKESPVTPIKEEIKSEESPEKHDTADNLEDKNSDAEESTKikGKEDFNPETTEKEALDESTNLNKDKSST 3575
Cdd:PTZ00121 1369 AEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKK--KADEAKKKAEEKKKADEAKKKAEEAKKA 1446
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 3576 ETLVPEIEDSKPSED-KMEVEELPVAENGEKEGSPEKCSDAEDKKFSEEKPSSPAVPDGKVSEMEADEAAPNTEENCSGD 3654
Cdd:PTZ00121 1447 DEAKKKAEEAKKAEEaKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE 1526
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 3655 SESPEKECEDKVVEKVEEEKGENSYEKAEEQK--EETEKLEKSSIESEpsEKSETVLEPEVAVPKKSTGDQDILDLVAGP 3732
Cdd:PTZ00121 1527 AKKAEEAKKADEAKKAEEKKKADELKKAEELKkaEEKKKAEEAKKAEE--DKNMALRKAEEAKKAEEARIEEVMKLYEEE 1604
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 386768875 3733 SDPDDDEVMKEKEKAVEEECKKQAAELKARFPDLEVIQPATVKQQKLEKPKLEMCMIR 3790
Cdd:PTZ00121 1605 KKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIK 1662
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
1668-1865 1.51e-05

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 51.92  E-value: 1.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875  1668 KAPEPKQDEEKSELDEATTDKPEGDEKFKTEGESKKDltDSEETKLESSAMEVDSKEESEPDDSKKSDEDNKDKDKMEVD 1747
Cdd:TIGR00927  656 EGENGEESGGEAEQEGETETKGENESEGEIPAERKGE--QEGEGEIEAKEADHKGETEAEEVEHEGETEAEGTEDEGEIE 733
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875  1748 DEVGKSDKESKPEEQSE-----TVKTEENSKAIEEDKSSTVLTADH--------------------AKEPETVLEKMEVD 1802
Cdd:TIGR00927  734 TGEEGEEVEDEGEGEAEgkhevETEGDRKETEHEGETEAEGKEDEDegeiqagedgemkgdegaegKVEHEGETEAGEKD 813
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386768875  1803 EKANDDQSAVSKAEGSDEKSTDDSNPEEATTEKNKE-------------SLEIEGEKERVKEGEESVKKENDEKTE 1865
Cdd:TIGR00927  814 EHEGQSETQADDTEVKDETGEQELNAENQGEAKQDEkgvdggggsdggdSEEEEEEEEEEEEEEEEEEEEEEEEEE 889
CD2_tandem_ScCHD1_like cd18664
repeat 2 of the paired tandem chromodomains of yeast chromodomain helicase DNA-binding protein ...
1938-1983 1.62e-05

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


Pssm-ID: 349311  Cd Length: 59  Bit Score: 45.34  E-value: 1.62e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 386768875 1938 DFTEVDRVLDMSVHTDEtSGETTKHYLVKWKSLPYEDCTWELEEDV 1983
Cdd:cd18664     1 EFHVVERIIASQRASLE-DGTSQLQYLVKWRRLNYDECTWEDATLI 45
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
1655-1874 2.57e-05

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 51.20  E-value: 2.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1655 MGKRELilDKPKEKAPEPKQDEEKSeldEATTDKPEGDEKFKTEGESKKDLTDSEETKLESSAMEVDSKEESEPDDSKKS 1734
Cdd:PTZ00108 1129 MWLEDL--DKFEEALEEQEEVEEKE---IAKEQRLKSKTKGKASKLRKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDS 1203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1735 DEDNKDKDKMEVDDEVGKSDKESKPEEQSETVKTEENSKAIEEDKSSTVLTADhakEPETVLEKMEVDEKANDDQSAVSK 1814
Cdd:PTZ00108 1204 DEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSED---NDEFSSDDLSKEGKPKNAPKRVSA 1280
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386768875 1815 AEGSDEKSTDDSNPEEATTEK-NKESLEIEGEKERVKEGEESVKKENDEKTEADMENKPEP 1874
Cdd:PTZ00108 1281 VQYSPPPPSKRPDGESNGGSKpSSPTKKKVKKRLEGSLAALKKKKKSEKKTARKKKSKTRV 1341
PTZ00121 PTZ00121
MAEBL; Provisional
3516-3724 2.73e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.91  E-value: 2.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 3516 EEIKSEESPEKHDTADNLEDKNSDAEESTKIKGKEDFNPETTEKEALDESTNLNKDKSSTETLVPEIEDS---------K 3586
Cdd:PTZ00121 1590 EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENkikaaeeakK 1669
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 3587 PSEDKMEVEELPVAENGEKEGSPEKCSDAEDKKFSEEKPSSPAVPDGKVSEMEADEaapntEENCSGDSESPEKEcedkv 3666
Cdd:PTZ00121 1670 AEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAE-----EENKIKAEEAKKEA----- 1739
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 386768875 3667 vekveeekgENSYEKAEE-QKEETEKLEKSSIESEPSEKSETVLEPEVAVPKKSTGDQD 3724
Cdd:PTZ00121 1740 ---------EEDKKKAEEaKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEED 1789
chromodomain cd18966
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
1941-1986 2.87e-05

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


Pssm-ID: 349322  Cd Length: 49  Bit Score: 44.20  E-value: 2.87e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 386768875 1941 EVDRVLDmsvhtdETSGETTKHYLVKWKSLPYEDCTWELEEDVDND 1986
Cdd:cd18966     2 EVERILA------ERRDDGGKRYLVKWEGYPLEEATWEPEENIGDE 41
TFIIF_alpha pfam05793
Transcription initiation factor IIF, alpha subunit (TFIIF-alpha); Transcription initiation ...
1664-1856 2.99e-05

Transcription initiation factor IIF, alpha subunit (TFIIF-alpha); Transcription initiation factor IIF, alpha subunit (TFIIF-alpha) or RNA polymerase II-associating protein 74 (RAP74) is the large subunit of transcription factor IIF (TFIIF), which is essential for accurate initiation and stimulates elongation by RNA polymerase II.


Pssm-ID: 310411 [Multi-domain]  Cd Length: 528  Bit Score: 50.33  E-value: 2.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875  1664 KPKEKAPEPKQDEEKSELDEATTDKPEGDE-----KFKTEGESKKDLTDSEETKlessameVDSKEESEPDDSKKSDEDN 1738
Cdd:pfam05793  208 RGKDLKIKDLEGDDEDDGDESDKGGEDGDEekkkkKKKKLAKNKKKLDDDKKKK-------RGGDDDAFEYDSDDGDDEG 280
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875  1739 KDKDKMevDDEvgkSDKESKPEEQSETVKTEENSKAIEEDKSSTVLTADHAKEPETVLEKMEvdEKANDDQSAVSKAEGS 1818
Cdd:pfam05793  281 REEDYI--SDS---SASGNDPEEREDKLSPEEPAKGEIEQSDDSEESEEEKNEEEGKLSKKG--KKAKKLKGKKNGKDKS 353
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 386768875  1819 DEKSTDDSnpEEATTEKNKESLEIEGEKERVKEGEESV 1856
Cdd:pfam05793  354 ESSDGDDS--DDSDIDDEDSVPLFTAKKKKEPKKEEPV 389
CHROMO smart00298
Chromatin organization modifier domain;
1879-1921 3.66e-05

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 44.13  E-value: 3.66e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 386768875   1879 VEEYFVKYRNFSYLHCEWRTEEELLKGDRrvaaKIRRFQQKQS 1921
Cdd:smart00298   17 ELEYLVKWKGYSYSEDTWEPEENLLNCSK----KLDNYKKKER 55
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
1662-1873 3.83e-05

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 50.56  E-value: 3.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1662 LDKPKEKAPEPKQDEEKSELDEATTDKPEGDEKFKTEGESKKDLTDSEETKLESSAME--VDSKEESEPDDSKKSDEDNK 1739
Cdd:PTZ00341  928 LKNQNENVPEHLKEHAEANIEEDAEENVEEDAEENVEENVEENVEENVEENVEENVEEnvEENVEENVEENVEENIEENV 1007
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1740 DKDKMEVDDEVGKSDKESKPEEQSETVKT--EENSKAIEEDKSSTVltadhakePETVLEKMEVDEKANDDQSAVSKAEG 1817
Cdd:PTZ00341 1008 EENVEENIEENVEEYDEENVEEVEENVEEydEENVEEIEENAEENV--------EENIEENIEEYDEENVEEIEENIEEN 1079
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 386768875 1818 SDEKSTDDSNPEEATTEKNKESLEIEGEKERVKEG-EESVKKENDEKTEADMENKPE 1873
Cdd:PTZ00341 1080 IEENVEENVEENVEEIEENVEENVEENAEENAEENaEENAEEYDDENPEEHNEEYDE 1136
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
1553-1839 5.14e-05

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 50.17  E-value: 5.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1553 KKDKKPSANASNSNA-----GSDVEKTEPQsgaEGDAAQEVGEEKSNLPLDESSQLEASSSTSAvaekerqistdaanaa 1627
Cdd:PTZ00341  328 KRAEKPKKKKSKRRGwlccgGGDIETVEPQ---QEEPVQDVGEHQINEYGDILPSLKASINNSA---------------- 388
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1628 msskpnyvyINTGDedsmvvqlvlAMRMGKRelildkpkekapepkqdeekseLDEATTDKPEGDEK--FKTEGESKKDL 1705
Cdd:PTZ00341  389 ---------INYYD----------AVKDGKY----------------------LDDDSSDALYTDEDllFDLEKQKYMDM 427
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1706 TD-SEETKLESSAME--VDSKEESEPDDSKKSDEDNKDKDKMEVDDEVGKSDKESK-PEEQSETVKTEENSKAieeDKSS 1781
Cdd:PTZ00341  428 LDgSEDESVEDNEEEhsGDANEEELSVDEHVEEHNADDSGEQQSDDESGEHQSVNEiVEEQSVNEHVEEPTVA---DIVE 504
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1782 TVLTADHAKEP--ETVLEKMEVDEkaNDDQSAVSKAEGSDEKSTDDSNPEEATTEKNKES 1839
Cdd:PTZ00341  505 QETVDEHVEEPavDENEEQQTADE--HVEEPTIAEEHVEEEISTAEEHIEEPASDVQQDS 562
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
1879-1919 8.39e-05

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 42.95  E-value: 8.39e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 386768875  1879 VEEYFVKYRNFSYLHCEWRTEEELLKGDRrvaaKIRRFQQK 1919
Cdd:pfam00385   16 KEEYLVKWKGYPYDENTWEPEENLSKCPE----LIEEFKDR 52
PTZ00121 PTZ00121
MAEBL; Provisional
1657-1865 9.05e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.37  E-value: 9.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1657 KRELILDKPKEKAPEPKQdEEKSELDEATTDKPEGDE-KFKTEGESKKDLTDSEETKLESSAMEVDS---KEESEPDDSK 1732
Cdd:PTZ00121 1043 KEKDIIDEDIDGNHEGKA-EAKAHVGQDEGLKPSYKDfDFDAKEDNRADEATEEAFGKAEEAKKTETgkaEEARKAEEAK 1121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1733 KSDEDNKDKDKMEVDDEVGKSDKESKPEEQ---------------------SETVKTEENSKAIEEDKSSTVLTADHAKE 1791
Cdd:PTZ00121 1122 KKAEDARKAEEARKAEDARKAEEARKAEDAkrveiarkaedarkaeearkaEDAKKAEAARKAEEVRKAEELRKAEDARK 1201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1792 PETV-----LEKMEVDEKANDDQ--SAVSKAEgsdEKSTDDSNPEEATTEKNKESLE----------------IEGEKER 1848
Cdd:PTZ00121 1202 AEAArkaeeERKAEEARKAEDAKkaEAVKKAE---EAKKDAEEAKKAEEERNNEEIRkfeearmahfarrqaaIKAEEAR 1278
                         250       260
                  ....*....|....*....|.
gi 386768875 1849 ----VKEGEESVKKENDEKTE 1865
Cdd:PTZ00121 1279 kadeLKKAEEKKKADEAKKAE 1299
Mpp10 COG5384
U3 small nucleolar ribonucleoprotein component [Translation, ribosomal structure and ...
1660-1891 9.82e-05

U3 small nucleolar ribonucleoprotein component [Translation, ribosomal structure and biogenesis];


Pssm-ID: 227674 [Multi-domain]  Cd Length: 569  Bit Score: 48.92  E-value: 9.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1660 LILDKPKEKAPEPKQDEEKSELDEATTDKPEGDEKFKTEGES-----KKDLTDSEETKLESSAMEVDSKEESEPDDSKKS 1734
Cdd:COG5384    61 LVLDSIDGDLIQGIQELKDPSLDGSTLNSSSGEESELEEAESvfkekQMLSADVSEIEEQSNDSLSENDEEPSMDDEKTS 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1735 DEDNKDKDKME--VDDEVGKSDKESKPEE-QSETVKTEENSKAIEEDKSSTVltaDHAKEPETVLEKME--VDEKANDDQ 1809
Cdd:COG5384   141 AEAAREEFAEEkrIPDPYGINDKFFDLEKfNRDTLAAEDSNEASEGSEDEDI---DYFQDMPSDDEEEEaiYYEDFFDKP 217
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1810 SAVSKAEGSDEKstDDSNPEEATTEKNKESLEIE-GEKERVKEGEESVKKEND---------EKTEADMENKPEpvfiDV 1879
Cdd:COG5384   218 TKEPVKKHSDVK--DPKEDEELDEEEHDSAMDKVkLDLFADEEDEPNAEGVGEasdknlssfEKQQIEMDEQIE----EL 291
                         250
                  ....*....|..
gi 386768875 1880 EEYFVKYRNFSY 1891
Cdd:COG5384   292 EKELVAPKEWKY 303
PTZ00121 PTZ00121
MAEBL; Provisional
3496-3706 1.30e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 3496 DELMTNESViKKESPVTPIKEEIKSEESPEKHDTADNLEDKNSDAEESTKikGKEDFNPETTEKEALDESTNLNKDKSST 3575
Cdd:PTZ00121 1281 DELKKAEEK-KKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKK--KADAAKKKAEEAKKAAEAAKAEAEAAAD 1357
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 3576 EtlvpeiedSKPSEDKMEVEELPVAEngEKEGSPEKCSDAEDKKFSEE--------KPSSPAVPDGKVSEMEADEAAPNT 3647
Cdd:PTZ00121 1358 E--------AEAAEEKAEAAEKKKEE--AKKKADAAKKKAEEKKKADEakkkaeedKKKADELKKAAAAKKKADEAKKKA 1427
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 386768875 3648 EENCSGDSESPEKECEDKVVEKVEEEKGENSYEKAEEQKEETEKLEKSSIESEPSEKSE 3706
Cdd:PTZ00121 1428 EEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD 1486
PTZ00121 PTZ00121
MAEBL; Provisional
3516-3717 1.34e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 1.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 3516 EEIKSEESPEKHDTADNLEDKNSDAEESTKIKgKEDFNPETTEKEALDESTNLNKDKSSTETLVPEIEDSKPSEDKMEVE 3595
Cdd:PTZ00121 1215 EEARKAEDAKKAEAVKKAEEAKKDAEEAKKAE-EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD 1293
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 3596 ELPVAEngEKEGSPEKCSDAEDKKFSEEKPSSPAVPDGKVSEME--------ADEAAPNTEENCSGDSESPEKECEDKVV 3667
Cdd:PTZ00121 1294 EAKKAE--EKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKkkaeeakkAAEAAKAEAEAAADEAEAAEEKAEAAEK 1371
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 386768875 3668 EKVEEEKGENSYEKAEEQKEETEKLEKSSieSEPSEKSETVLEPEVAVPK 3717
Cdd:PTZ00121 1372 KKEEAKKKADAAKKKAEEKKKADEAKKKA--EEDKKKADELKKAAAAKKK 1419
rad2 TIGR00600
DNA excision repair protein (rad2); All proteins in this family for which functions are known ...
1394-1864 1.63e-04

DNA excision repair protein (rad2); All proteins in this family for which functions are known are flap endonucleases that generate the 3' incision next to DNA damage as part of nucleotide excision repair. This family is related to many other flap endonuclease families including the fen1 family. 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: 273166 [Multi-domain]  Cd Length: 1034  Bit Score: 48.36  E-value: 1.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875  1394 GGTGVDGESPDYD-DIPVSKIPRGSNEDEKEAEAGDetvdSVPDSAGDPASTPSRRDRKRS--TARSRRNANSEEGGS-- 1468
Cdd:TIGR00600  293 LIKGIQGKTAVKAvDSDDESLPSLSSQLDSNSEDLK----SSPWEKLKPESESIVEAEPPSprTLLAKQAAMSESSSEds 368
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875  1469 --ARKNR-------------GSLSAK---ALKKRRNRGRIVPESDGEDDTLDrtpppspppdSEMDSNKRRSSRNTQrkk 1530
Cdd:TIGR00600  369 deSEWERqelkrnnvafvddGSLSPRtlqAIGQALDDDEDKKVSASSDDQAS----------PSKKTKMLLISRIEV--- 435
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875  1531 yiDDVMLRFSDDENSLLVASPVKKDKKPSANASNSNAGSDVEKTEPQSGAEGDAAQEVGEEKSN-LPLDESSQLEASSST 1609
Cdd:TIGR00600  436 --EDDDLDYLDQGEGIPLMAALQLSSVNSKPEAVASTKIAREVTSSGHEAVPKAVQSLLLGATNdSPIPSEFTILDRKSE 513
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875  1610 SAVAE-KERQISTDAANAAMSSKP----------NYVYINTGDEDSMVVQLVLAMRMGKRELILDKPKEKAPEPKQDEEK 1678
Cdd:TIGR00600  514 LSIERtVKPVSSEFGLPSQREDKLaiptegtqnlQGISDHPEQFEFQNELSPLETKNNESNLSSDAETEGSPNPEMPSWS 593
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875  1679 S------ELDEATTDKPEGDEKFKTEGESK---KDLTDSEETKLESSAMEVDSKEEsepdDSKKSDEDNKDkDKMEVDDE 1749
Cdd:TIGR00600  594 SvtvpseALDNYETTNPSNAKEVRNFAETGiqtTNVGESADLLLISNPMEVEPMES----EKEESESDGSF-IEVDSVSS 668
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875  1750 VGKSDKESKPEEQSETVKTEENSKA-IEEDKSSTVLTADHAKEPETVLEKMEVDEKANDDQSavskaegsdeKSTDDSNP 1828
Cdd:TIGR00600  669 TLELQVPSKSQPTDESEENAENKVAsIEGEHRKEIEDLLFDESEEDNIVGMIEEEKDADDFK----------NEWQDISL 738
                          490       500       510
                   ....*....|....*....|....*....|....*.
gi 386768875  1829 EEATTEKNKEsleiEGEKERVKEGEESVKKENDEKT 1864
Cdd:TIGR00600  739 EELEALEANL----LAEQNSLKAQKQQQKRIAAEVT 770
COG5177 COG5177
Uncharacterized conserved protein [Function unknown];
1667-1900 1.64e-04

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 227504 [Multi-domain]  Cd Length: 769  Bit Score: 48.15  E-value: 1.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1667 EKAPEPKQDEEKSELDEATtdkpegdekfktegeskkDLTDSEETkLESSAMEVDSKEESEP----DDSKKSDEDNKDKD 1742
Cdd:COG5177   298 IVNGQYEQTIREIFADRAT------------------KLELDLQT-VFESNMNRDTLDEYAPegedLRSDYDEDFEYDGL 358
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1743 KMEVDDEVGKSDKEskpeeqsetvktEENSKAIEEDKSSTVLTADHAKEPEtvlekmEVDEKANDDQSAVSKAEGSDEKS 1822
Cdd:COG5177   359 TTVRIDDHGFLPGR------------EQTSKKAAVPKGTSFYQAKWAEDEE------EEDGQCNDEESTMSAIDDDDPKE 420
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1823 TDDSNP---EEATTEKNKESLEIEGEKERVKEGEESVKKENDEKTEADMENKPEPVFIdveEYFVKYRNFSYLH-CEWRT 1898
Cdd:COG5177   421 NDNEEVagdEESAIDDNEGFEELSPEEEERQLREFRDMEKEDREFPDEAELQPSESAI---ERYKEYRGLRNLYtCSWRS 497

                  ..
gi 386768875 1899 EE 1900
Cdd:COG5177   498 DE 499
BMS1 COG5192
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ...
1542-1871 2.25e-04

GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and biogenesis];


Pssm-ID: 227519 [Multi-domain]  Cd Length: 1077  Bit Score: 47.81  E-value: 2.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1542 DENSLLVASP------VKKDKK------PSANAS---NSNAGSDVEKTEPQSGAEGDAAQEVGEEK--SNLPLDESSQLE 1604
Cdd:COG5192   319 SLKSKLIYSPmsdiggILKDKDrvyievPTSNFSkdeNSEAGEGEKMKMQLQEIEQDPGVDGVGLQlfSNSDAIDTVDRE 398
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1605 ASSSTSAVAEKERQISTDAANAAMSSKPNyvyINTGDEDSMVVQLVLAMRMGKRELILDKPKEKAPEPKQDEEKSELDEA 1684
Cdd:COG5192   399 SSEIDNVGRKTRRQPTGKAIAEETSREDE---LSFDDSDVSTSDENEDVDFTGKKGAINNEDESDNEEVAFDSDSQFDES 475
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1685 ttdkpEGDEKFKTEGESKKDLTDSEETKLESSA---MEVDSKEE------SEPDDSKKSDEDNKDKDK-----MEVDDEV 1750
Cdd:COG5192   476 -----EGNLRWKEGLASKLAYSQSGKRGRNIQKifyDESLSPEEcieeykGESAKSSESDLVVQDEPEdffdvSKVANES 550
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1751 GKSDKESKPEEQSETVKTEENSKAIEEDKSSTVLTADHAKEPEtvlEKMEVDEKANDDQSAVSKAEGSDEKSTDDSNPEE 1830
Cdd:COG5192   551 ISSNHEKLMESEFEELKKKWSSLAQLKSRFQKDATLDSIEGEE---ELIQDDEKGNFEDLEDEENSSDNEMEESRGSSVT 627
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 386768875 1831 ATTEKNKESLEIEGEKERVKEGEESVKKENDEKTEADMENK 1871
Cdd:COG5192   628 AENEESADEVDYETEREENARKKEELRGNFELEERGDPEKK 668
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
1663-1873 2.37e-04

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 47.68  E-value: 2.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875  1663 DKPKEKAPEPKQDEEKSELDEATTDKPEGDEKfKTEGESKKDLTDSEETKLESsamEVDSKEESEPDDSKKSDEDNKDKD 1742
Cdd:TIGR00927  636 AEAEHTGERTGEEGERPTEAEGENGEESGGEA-EQEGETETKGENESEGEIPA---ERKGEQEGEGEIEAKEADHKGETE 711
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875  1743 KMEVDDEVGKSDKESKPEEQSETvkteENSKAIEEDKSSTVLTADHAKEPE------TVLEKMEVDEKANDDQSAVSKAE 1816
Cdd:TIGR00927  712 AEEVEHEGETEAEGTEDEGEIET----GEEGEEVEDEGEGEAEGKHEVETEgdrketEHEGETEAEGKEDEDEGEIQAGE 787
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 386768875  1817 GSDEKSTDDSNPEEATTEKNKESLEIEGEKERVKEGEESVKKENDEKTEADMENKPE 1873
Cdd:TIGR00927  788 DGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGE 844
Caldesmon pfam02029
Caldesmon;
1666-1871 2.38e-04

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 47.55  E-value: 2.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875  1666 KEKAPEPKQDEEKSELDEATTDKPEGDEKFK-----------------TEGESKKDLTDSEETKLESSAMEVDSKEESEP 1728
Cdd:pfam02029   35 SVEPNEHNSYEEDSELKPSGQGGLDEEEAFLdrtakreerrqkrlqeaLERQKEFDPTIADEKESVAERKENNEEEENSS 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875  1729 DDSKKSDEDNKDKDKMEVDDEVGKSDKESKPEEQSETVKTEENSKAIEEDKSSTVLTADHAKEPETVLEKMEVDEKANDD 1808
Cdd:pfam02029  115 WEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYES 194
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386768875  1809 QSAV--------SKAEGSDEKSTDDSNPEEATTEKNKESLEIEGEKERVKEGE---ESVKKENDEKTEADMENK 1871
Cdd:pfam02029  195 KVFLdqkrghpeVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEqklEELRRRRQEKESEEFEKL 268
PHA03169 PHA03169
hypothetical protein; Provisional
3515-3708 2.64e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 47.27  E-value: 2.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 3515 KEEIKSEESPEKHDTADNLEDKNSDAEESTKIKGKEDFNPETTEKEALDESTNLNKDKSSTETlvpEIEDSKPSEDKMEV 3594
Cdd:PHA03169   68 QTESDTETAEESRHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPES---PASHSPPPSPPSHP 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 3595 EELPVAENGEKEGSPEKCSDAEDKKFSEEKPSSPAVPDGKvSEMEADEAAPNTEENCSGDSESPEKECEDKVVEKVEEEK 3674
Cdd:PHA03169  145 GPHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSE-PEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAP 223
                         170       180       190
                  ....*....|....*....|....*....|....
gi 386768875 3675 GENSYEKAEEQKEETEKLEKSSIESEPSEKSETV 3708
Cdd:PHA03169  224 SPNTQQAVEHEDEPTEPEREGPPFPGHRSHSYTV 257
CD_MarY1_POL_like cd18975
chromodomain of Tricholoma matsutake polyprotein, and similar proteins; This subgroup includes ...
1941-1988 2.74e-04

chromodomain of Tricholoma matsutake polyprotein, and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in the polyprotein from the MarY1 Ty3/Gypsy long terminal repeat (LTR) retroelement from the from the Ectomycorrhizal Basidiomycete Tricholoma matsutake. The pol gene in TY3/gypsy elements generally encodes domains in the following order: prt-reverse transcriptase-RNase H-integrase, in marY1 POL the chromodomain is found at the C-terminus of the integrase domain. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349331  Cd Length: 49  Bit Score: 41.76  E-value: 2.74e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 386768875 1941 EVDRVLDMSVHTDETsgettkHYLVKWKSLPYEDCTWELEEDVDNDKI 1988
Cdd:cd18975     2 EVESILNSRLHRGKL------QYLIQWKGYPLEEASWELEDNIKNPRL 43
CD2_tandem_CHD1-2_like cd18661
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 1 and ...
1942-1978 2.82e-04

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


Pssm-ID: 349308  Cd Length: 58  Bit Score: 41.90  E-value: 2.82e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 386768875 1942 VDRVLDMSVHTDETSGETtkHYLVKWKSLPYEDCTWE 1978
Cdd:cd18661     5 VERIIAHSPQKSAASGYP--DYLCKWQGLPYSECTWE 39
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1633-1882 3.00e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.37  E-value: 3.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1633 NYVYINTGDEDSMVVQLVLAMRMGKRELILDKpKEKAPEpKQDEEKSELDEattdKPEGDEKFKTEGESKKDLTDSEETK 1712
Cdd:PRK03918  128 NAIYIRQGEIDAILESDESREKVVRQILGLDD-YENAYK-NLGEVIKEIKR----RIERLEKFIKRTENIEELIKEKEKE 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1713 LESSAMEVDSKEESEPDDSKKSDEDNKDKDKMEvddevgkSDKESKPEEQSETVKTEENSKAIEEDKSStvlTADHAKEP 1792
Cdd:PRK03918  202 LEEVLREINEISSELPELREELEKLEKEVKELE-------ELKEEIEELEKELESLEGSKRKLEEKIRE---LEERIEEL 271
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1793 ETVLEKMEvdEKANDDQSAVSKAEGSDE--KSTDDSNPEEATTEKNKESLE--IEGEKERVKEGEESVKKEND-EKTEAD 1867
Cdd:PRK03918  272 KKEIEELE--EKVKELKELKEKAEEYIKlsEFYEEYLDELREIEKRLSRLEeeINGIEERIKELEEKEERLEElKKKLKE 349
                         250
                  ....*....|....*
gi 386768875 1868 MENKPEPVFIDVEEY 1882
Cdd:PRK03918  350 LEKRLEELEERHELY 364
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
2029-2197 3.26e-04

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: 44.22  E-value: 3.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2029 LRPYQLEGL-NWLKFSWYNTHNCILAdeMGLGKTIQSLTFvhSVYEYgiRGPFLVIAPLSTIPN-WQREFEGWTDMNVVv 2106
Cdd:cd17926     1 LRPYQEEALeAWLAHKNNRRGILVLP--TGSGKTLTALAL--IAYLK--ELRTLIVVPTDALLDqWKERFEDFLGDSSI- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 2107 yhgsvtskqmiqdyeyyyKTESGKVLKEPIKFNVLITTF---EMIVTDYMDLKAFNWrLCVIDEAHRLknrNCKLLEGLR 2183
Cdd:cd17926    74 ------------------GLIGGGKKKDFDDANVVVATYqslSNLAEEEKDLFDQFG-LLIVDEAHHL---PAKTFSEIL 131
                         170
                  ....*....|....*
gi 386768875 2184 QLNLEHRVL-LSGTP 2197
Cdd:cd17926   132 KELNAKYRLgLTATP 146
COG5137 COG5137
Histone chaperone involved in gene silencing [Transcription / Chromatin structure and dynamics] ...
1663-1777 3.60e-04

Histone chaperone involved in gene silencing [Transcription / Chromatin structure and dynamics];


Pssm-ID: 227466 [Multi-domain]  Cd Length: 279  Bit Score: 46.14  E-value: 3.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1663 DKPKE-KAPEPKQ----DEEKSELDEATTDKPEGDEKFKTE--GESKKDLTDSEETklessamEVDSKEESEPD-DSKKS 1734
Cdd:COG5137   159 DNDEDnDEAPPAQpdvdNEEEERLEESDGREEEEDEEVGSDsyGEGNRELNEEEEE-------EAEGSDDGEDVvDYEGE 231
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 386768875 1735 DEDNKDKDKMEVDDEVGKSDKeskpEEQSETVKTEENSKAIEE 1777
Cdd:COG5137   232 RIDKKQGEEEEMEEEVINLFE----IEWEEESPSEEVPRNNEE 270
CD_POL_like cd18974
chromodomain of Penicillium solitum protein PENSOL_c198G03123; This subgroup includes the ...
1941-1993 3.79e-04

chromodomain of Penicillium solitum protein PENSOL_c198G03123; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in Penicillium solitum protein PENSOL_c198G03123 a putative polyprotein from a Ty3/Gypsy long terminal repeat (LTR) retroelement. The pol gene in TY3/gypsy elements generally encodes domains in the following order: an aspartyl protease, a reverse transcriptase, RNase H, and an integrase, here the chromodomain is found at the C-terminus of the integrase domain. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349330  Cd Length: 50  Bit Score: 41.31  E-value: 3.79e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 386768875 1941 EVDRVLDMSVHTDETsgettkHYLVKWKSLPYEDCTWELEEDVDNDK--IEQYLR 1993
Cdd:cd18974     2 EVEEIVDEKMIDDEL------HYLVKWKGWPAEYNQWEPEDDMENAPkaIQSYEK 50
CD1_tandem cd18660
repeat 1 of paired tandem chromodomains; Repeat 1 of tandem CHRomatin Organization Modifier ...
1938-1993 4.84e-04

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


Pssm-ID: 349307 [Multi-domain]  Cd Length: 70  Bit Score: 41.58  E-value: 4.84e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1938 DFTEVDRVLDMSVHTDETSGET----------TKHYLVKWKSLPYEDCTWELEEDVDND----KIEQYLR 1993
Cdd:cd18660     1 DEDKIEKILDHRPKGPVEEASLdltdpdepwdEREFLVKWKGKSYLHCTWVTEETLEQLrgkkKLKNYIK 70
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
221-533 5.44e-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: 46.68  E-value: 5.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875   221 QAPGQHPLYPGVGAPTVQAGQPPTPQAYAHSPYGSPMQHQPSRgAPQHVGYGHTGLDQ-ASAYGQHVPGGAPPGHHLSAQ 299
Cdd:pfam03154  177 QSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPN-QTQSTAAPHTLIQQtPTLHPQRLPSPHPPLQPMTQP 255
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875   300 QQQAAQQLGAhqqqqlqsqqqqqaqqqqphvslMQQQQLPGAGLPPPH-MGMPPSYGSHHQQQQQQQQTQQQQQQSAPPy 378
Cdd:pfam03154  256 PPPSQVSPQP-----------------------LPQPSLHGQMPPMPHsLQTGPSHMQHPVPPQPFPLTPQSSQSQVPP- 311
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875   379 mssSKHQQAAAQLNSSPQYRAPFPQLSPQMSPR----PPTMSPHPQMSPRPVG-VSPAKPPPPQQQQQQTQAQQPQQVVS 453
Cdd:pfam03154  312 ---GPSPAAPGQSQQRIHTPPSQSQLQSQQPPReqplPPAPLSMPHIKPPPTTpIPQLPNPQSHKHPPHLSGPSPFQMNS 388
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875   454 NQPSQHSIQGMVGLPSPRP----QPPTSGAGGAGAKGPAPVAAPVNTlqaleqmvmPSQALGLPPMDYPSAYRSAVGPRM 529
Cdd:pfam03154  389 NLPPPPALKPLSSLSTHHPpsahPPPLQLMPQSQQLPPPPAQPPVLT---------QSQSLPPPAASHPPTSGLHQVPSQ 459

                   ....
gi 386768875   530 PASP 533
Cdd:pfam03154  460 SPFP 463
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
1334-1673 5.47e-04

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


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 46.44  E-value: 5.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1334 NDPNSTETPAAVKKRAGASKRRKQYGEDGAEQTGEGSEVE---DNKPLVPKAGSADGEAETTSGGTGVDGESPDYDDIPV 1410
Cdd:NF033609  602 SDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDsdsDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 681
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1411 SKIPRGSNEDEKEAEAGDETVDSVPDSAGDPASTPSRRDRKRSTARSRRNANSEEGGSARKNRGSLSAKALKKrrnrgri 1490
Cdd:NF033609  682 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS------- 754
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1491 vpESDGEDDTlDRTPPPSPPPDSEMDSNKRRSSRNTQRKKYIDDVMLRFSDDENSLLVASPVKKDKKPSANASNSNAGSD 1570
Cdd:NF033609  755 --DSDSDSDS-DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 831
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1571 VEKTEPQSGAEGDAAQEVGEEKSNLPLDESSQLEASSSTSAVAEKERQISTDAANAAMSSKPNYVYINTGDEDSMVVQLV 1650
Cdd:NF033609  832 SDSDSDSDSDSDSDSDSDSDSDSDSESDSNSDSESGSNNNVVPPNSPKNGTNASNKNEAKDSKEPLPDTGSEDEANTSLI 911
                         330       340
                  ....*....|....*....|...
gi 386768875 1651 LAMRMGKRELILDKPKEKAPEPK 1673
Cdd:NF033609  912 WGLLASLGSLLLFRRKKENKDKK 934
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
3487-3706 5.52e-04

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 46.70  E-value: 5.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 3487 VKNEVIDLDDELMT-NESVIK--KESPVTPIKEEIksEESPEkHDTADNLEDK-NSDAEESTKIKGKEDF--NPETTEKE 3560
Cdd:PTZ00341  917 IAHEINLINKELKNqNENVPEhlKEHAEANIEEDA--EENVE-EDAEENVEENvEENVEENVEENVEENVeeNVEENVEE 993
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 3561 ALDESTNLNKDKSSTETLVPEIEDSKPSEDKMEVEELPVAENGEKEGSPEKCSDAEDKKFSEEKPSSPAVPDGKVSEMEA 3640
Cdd:PTZ00341  994 NVEENVEENIEENVEENVEENIEENVEEYDEENVEEVEENVEEYDEENVEEIEENAEENVEENIEENIEEYDEENVEEIE 1073
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386768875 3641 DEAAPNTEENCSGDSESPEKECEDKVVEKVEEEKGENSYEKAEEQKEETEklekssiESEPSEKSE 3706
Cdd:PTZ00341 1074 ENIEENIEENVEENVEENVEEIEENVEENVEENAEENAEENAEENAEEYD-------DENPEEHNE 1132
PRK05901 PRK05901
RNA polymerase sigma factor; Provisional
1694-1878 5.68e-04

RNA polymerase sigma factor; Provisional


Pssm-ID: 235640 [Multi-domain]  Cd Length: 509  Bit Score: 46.14  E-value: 5.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1694 KFKTEGESKKDLTDSEETKLESSAMEVDSKEESEPDDSKKSDEDNKDKDKMEVDDEVGKSDKESKPEEQSETVKTEE-NS 1772
Cdd:PRK05901    9 ELAAEEEAKKKLKKLAAKSKSKGFITKEEIKEALESKKKTPEQIDQVLIFLSGMVKDTDDATESDIPKKKTKTAAKAaAA 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1773 KAIEEDKSSTVLTADHAKEPETVLEKMEVDEKANDDQSAVSKAEGSDEKSTDDSNPEEATTEKNKESLEIEGEKERVKEG 1852
Cdd:PRK05901   89 KAPAKKKLKDELDSSKKAEKKNALDKDDDLNYVKDIDVLNQADDDDDDDDDDDLDDDDIDDDDDDEDDDEDDDDDDVDDE 168
                         170       180
                  ....*....|....*....|....*.
gi 386768875 1853 EESVKKENDEKTEADMENKPEPVFID 1878
Cdd:PRK05901  169 DEEKKEAKELEKLSDDDDFVWDEDDS 194
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
2030-2197 6.35e-04

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


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 43.77  E-value: 6.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875  2030 RPYQLEGLNWLkfswYNTHNCILADEMGLGKT-IQSLTFVHSVYEYGIRGPFLVIAPLSTIpNWQ-----REFEGWTDMN 2103
Cdd:pfam00270    1 TPIQAEAIPAI----LEGRDVLVQAPTGSGKTlAFLLPALEALDKLDNGPQALVLAPTREL-AEQiyeelKKLGKGLGLK 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875  2104 VVVYHGSVTSKQMIQDyeyyyktesgkvLKEPikfNVLITTFEMIVTDYMDLKAF-NWRLCVIDEAHRL--KNRNCKLLE 2180
Cdd:pfam00270   76 VASLLGGDSRKEQLEK------------LKGP---DILVGTPGRLLDLLQERKLLkNLKLLVLDEAHRLldMGFGPDLEE 140
                          170
                   ....*....|....*...
gi 386768875  2181 GLRQLNLEHR-VLLSGTP 2197
Cdd:pfam00270  141 ILRRLPKKRQiLLLSATL 158
PRK05901 PRK05901
RNA polymerase sigma factor; Provisional
1600-1793 6.35e-04

RNA polymerase sigma factor; Provisional


Pssm-ID: 235640 [Multi-domain]  Cd Length: 509  Bit Score: 46.14  E-value: 6.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1600 SSQLEASSSTSAVAEKER---QISTDAANAAMSSKPNYVYINTGDEDSMVVqLVLAMRMGKRELILDKPKEKAPEPKQDE 1676
Cdd:PRK05901   11 AAEEEAKKKLKKLAAKSKskgFITKEEIKEALESKKKTPEQIDQVLIFLSG-MVKDTDDATESDIPKKKTKTAAKAAAAK 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1677 EKSELdeATTDKPEGDEKFKTEGESKKDLTDSEETKLESSAMEVDSKEESEPDDSKksDEDNKDKDKMEVDDEvgKSDKE 1756
Cdd:PRK05901   90 APAKK--KLKDELDSSKKAEKKNALDKDDDLNYVKDIDVLNQADDDDDDDDDDDLD--DDDIDDDDDDEDDDE--DDDDD 163
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 386768875 1757 SKPEEQSETVKTEENSKAIEEDKSSTVLTADHAKEPE 1793
Cdd:PRK05901  164 DVDDEDEEKKEAKELEKLSDDDDFVWDEDDSEALRQA 200
COG5593 COG5593
Nucleic-acid-binding protein possibly involved in ribosomal biogenesis [Translation, ribosomal ...
1664-1807 7.53e-04

Nucleic-acid-binding protein possibly involved in ribosomal biogenesis [Translation, ribosomal structure and biogenesis];


Pssm-ID: 227880 [Multi-domain]  Cd Length: 821  Bit Score: 46.19  E-value: 7.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1664 KPKEKAPEPKQDEEKSELDEattdkpegDEKFKTEGESKKDLT-DSEETKLESSAMEV-DSKEESEPDDSKKSDEDNKDK 1741
Cdd:COG5593   668 DGKGKKSNKASFDSDDEMDE--------NEIWSALVKSRPDVEdDSDDSELDFAEDDFsDSTSDDEPKLDAIDDEDAKSE 739
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1742 DKMEVDDEVGKSD----------------KESKPEEQSETVKTEENSKAIEEDKSstvltadHAKEPETVLEKMEVDEKA 1805
Cdd:COG5593   740 GSQESDQEEGLDEifysfdgeqdnsdsfaESSEEDESSEEEKEEEENKEVSAKRA-------KKKQRKNMLKSLPVFASA 812

                  ..
gi 386768875 1806 ND 1807
Cdd:COG5593   813 DD 814
CD_CMT3_like cd18635
chromodomain of chromomethylase 3, and similar proteins; CHRomatin Organization Modifier ...
1941-1993 7.57e-04

chromodomain of chromomethylase 3, and similar proteins; CHRomatin Organization Modifier (chromo) domain of DNA (cytosine-5)-methyltransferase chromomethylase 3 (CMT3, EC:2.1.1.37), and similar proteins. CMT3 is primarily a CHG (where H is either A, T or C) methyltransferase and is predominantly expressed in actively replicating cells. The protein is involved in preferentially methylating transposon-related sequences, reducing their mobility. Studies suggest that in order to target DNA methylation, CMT3 associates with H3K9me2-containing nucleosomes through binding of its BAH- and chromo-domains to H3K9me2. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349285  Cd Length: 57  Bit Score: 40.76  E-value: 7.57e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 386768875 1941 EVDRVLDMSVHTDETSGETTKHYLVKWKSLPYEDCTWELEEDVDN--DKIEQYLR 1993
Cdd:cd18635     3 EVEKLVGICYGDPKKTGERGLYFKVRWKGYGPEEDTWEPIEGLSNcpEKIKEFVQ 57
PRK05901 PRK05901
RNA polymerase sigma factor; Provisional
1657-1858 7.72e-04

RNA polymerase sigma factor; Provisional


Pssm-ID: 235640 [Multi-domain]  Cd Length: 509  Bit Score: 45.76  E-value: 7.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1657 KRELILDKPKEKAPEPKQDEEKSELDEATTDKPEGDEKFKTEGESKKDLTDSEETKLESSAMEVDSKE-ESEPDDSKKSD 1735
Cdd:PRK05901   11 AAEEEAKKKLKKLAAKSKSKGFITKEEIKEALESKKKTPEQIDQVLIFLSGMVKDTDDATESDIPKKKtKTAAKAAAAKA 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1736 EDNKDKDkmevddevgKSDKESKPEEQSETVKTEENSKAIEEDKSSTVLTADHAKEPETVLEKMEVDEKANDDQSAvSKA 1815
Cdd:PRK05901   91 PAKKKLK---------DELDSSKKAEKKNALDKDDDLNYVKDIDVLNQADDDDDDDDDDDLDDDDIDDDDDDEDDD-EDD 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 386768875 1816 EGSDEKSTDDSNPEEATTEKNKESLEIEGEKERVKEGEESVKK 1858
Cdd:PRK05901  161 DDDDVDDEDEEKKEAKELEKLSDDDDFVWDEDDSEALRQARKD 203
MAK16 COG5129
Nuclear protein with HMG-like acidic region [General function prediction only];
1671-1780 8.70e-04

Nuclear protein with HMG-like acidic region [General function prediction only];


Pssm-ID: 227458 [Multi-domain]  Cd Length: 303  Bit Score: 45.04  E-value: 8.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1671 EPKQDEEKSELDEATTDKPEGDEKFKTEGESKKDLTDSEE-----TKLESSAMEVDSKEESEPDDSkkSDEDNKDKDKME 1745
Cdd:COG5129   194 EKRQDEKERYVEEEEESDTELEAVTDDSEKEKTKKKDLEKwlgsdQSMETSESEEEESSESESDED--EDEDNKGKIRKR 271
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 386768875 1746 vddEVGKSDKESKPEEQSETVKTEENSKAIEEDKS 1780
Cdd:COG5129   272 ---KTDDAKKSRKPHIHIEYEQERENEKIPAVQHS 303
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
2417-2467 1.16e-03

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: 40.77  E-value: 1.16e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 386768875 2417 SDRFVFLLCTKAGGLGINLTAADTVIIYDSDWNPQNDLQAQARCHRIGQRK 2467
Cdd:cd18785    20 ASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDE 70
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
1056-1265 1.39e-03

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


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 45.00  E-value: 1.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875  1056 PADPIIPVTQPPQQQMPPIGMPMHPIAPGYEAQAQGQGHMPPMMPPYGGAPGmyppypmlHQQEIAALQQQIQElycMPP 1135
Cdd:pfam09606  180 PGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPADAGAQMGQQAQANGGMNP--------QQMGGAPNQVAMQQ---QQP 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875  1136 GHELQHQDKLMRMQErLNLLTQHEVNDQCAGGPQcllfQNVPPMYGPPGnPLLNQQMVESPQVSSTTGrgrgksaNKPRK 1215
Cdd:pfam09606  249 QQQGQQSQLGMGINQ-MQQMPQGVGGGAGQGGPG----QPMGPPGQQPG-AMPNVMSIGDQNNYQQQQ-------TRQQQ 315
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 386768875  1216 PRAKKGEKAQVGQQQdlmdisgNVAMGAANAVSSIPTTQLPVSEDCVTQG 1265
Cdd:pfam09606  316 QQQGGNHPAAHQQQM-------NQSVGQGGQVVALGGLNHLETWNPGNFG 358
MAK16 COG5129
Nuclear protein with HMG-like acidic region [General function prediction only];
1651-1809 1.71e-03

Nuclear protein with HMG-like acidic region [General function prediction only];


Pssm-ID: 227458 [Multi-domain]  Cd Length: 303  Bit Score: 44.27  E-value: 1.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1651 LAMRMGKRELILDKPKEKAPEpkQDEEKSELDEATTDKPEGDE---KFKTEGESKKDLTDSEET-KLESSAMEVDSKEES 1726
Cdd:COG5129   124 LALFKEHGEYMVRKPKMNRRE--KLRERKALNAAKFEKNIEKElmlRLKSGIYGDTPLNVREHLwNKAATEREKRQDEKE 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1727 EPDDSKKSDE-------DNKDKDKMEVDDE---VGKSDKESKPEEQSET-VKTEENSKAIEEDKSST----VLTADHAKE 1791
Cdd:COG5129   202 RYVEEEEESDteleavtDDSEKEKTKKKDLekwLGSDQSMETSESEEEEsSESESDEDEDEDNKGKIrkrkTDDAKKSRK 281
                         170
                  ....*....|....*...
gi 386768875 1792 PETVLEKMEVDEKANDDQ 1809
Cdd:COG5129   282 PHIHIEYEQERENEKIPA 299
COG5137 COG5137
Histone chaperone involved in gene silencing [Transcription / Chromatin structure and dynamics] ...
1663-1765 1.84e-03

Histone chaperone involved in gene silencing [Transcription / Chromatin structure and dynamics];


Pssm-ID: 227466 [Multi-domain]  Cd Length: 279  Bit Score: 43.83  E-value: 1.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1663 DKPKEKAPEPKQDEEKSELDEATTDKPEGDEKFKTEGESKKDLTDSEETKLESSAMEVDSKEESEPDDSKKSDEDNKDKD 1742
Cdd:COG5137   176 NEEEERLEESDGREEEEDEEVGSDSYGEGNRELNEEEEEEAEGSDDGEDVVDYEGERIDKKQGEEEEMEEEVINLFEIEW 255
                          90       100
                  ....*....|....*....|...
gi 386768875 1743 KMEVDDEVGKSDKESKPEEQSET 1765
Cdd:COG5137   256 EEESPSEEVPRNNEESPAKKQKV 278
PTZ00121 PTZ00121
MAEBL; Provisional
1683-1866 2.79e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 2.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1683 EATTDKPEGDEKFKTEGESKKDLTDSEETKLESSAmEVDSKEESEPDDSKKSDEDNKDKDKMEVDDEVGKSDKESKpeeQ 1762
Cdd:PTZ00121 1030 EELTEYGNNDDVLKEKDIIDEDIDGNHEGKAEAKA-HVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAK---K 1105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1763 SETVKTEENSKAIE-EDKSSTVLTADHAKEPETVlEKMEVDEKANDDqsavsKAEGSDEKSTDDSNPEEATTEKNKESLE 1841
Cdd:PTZ00121 1106 TETGKAEEARKAEEaKKKAEDARKAEEARKAEDA-RKAEEARKAEDA-----KRVEIARKAEDARKAEEARKAEDAKKAE 1179
                         170       180
                  ....*....|....*....|....*
gi 386768875 1842 IEGEKERVKEGEESVKKENDEKTEA 1866
Cdd:PTZ00121 1180 AARKAEEVRKAEELRKAEDARKAEA 1204
chromodomain cd18968
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
1941-1987 2.90e-03

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


Pssm-ID: 349324  Cd Length: 57  Bit Score: 38.87  E-value: 2.90e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 386768875 1941 EVDRVLDMSVHTDETSGETTKHYLVKWKSLPYEDCTWELEEDVDNDK 1987
Cdd:cd18968     3 EVEVILAARVVKDAESRKKGWKYLVKWAGYPDEENTWEPEESFDGCD 49
CD3_cpSRP43_like cd18628
chromodomain 3 of chloroplast signal recognition particle 43 kDa protein, and similar proteins; ...
1945-1991 3.22e-03

chromodomain 3 of chloroplast signal recognition particle 43 kDa protein, and similar proteins; This subgroup includes the chromodomain 3 of chloroplast SRP43 (cpSRP43), and similar proteins. CpSRP43 is a component of the chloroplast signal recognition particle (SRP) pathway. It forms a stable complex with cpSRP54 (cpSRP complex) which is required for the efficient posttranslational transport of members of the nuclearly encoded light harvesting chlorophyll-a/b-binding proteins (LHCPs) to the thylakoid membrane. Chromatin organization modifier (chromo) domain is a conserved region of around 50 amino acids found in a variety of chromosomal proteins, which appear to play a role in the functional organization of the eukaryotic nucleus. Experimental evidence implicates the chromodomain in the binding activity of these proteins to methylated histone tails and maybe RNA. May occur as single instance, in a tandem arrangement or followed by a related chromo shadow domain.


Pssm-ID: 349278  Cd Length: 51  Bit Score: 38.52  E-value: 3.22e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 386768875 1945 VLDMSVHTDETSGETTKHYLVKWksLPYEDCTWELEEDVDNDKIEQY 1991
Cdd:cd18628     5 VAESVIGKRVGDDGKTIEYLVKW--TDMSDATWEPQDNVDSTLVLLY 49
COG5137 COG5137
Histone chaperone involved in gene silencing [Transcription / Chromatin structure and dynamics] ...
1658-1781 3.64e-03

Histone chaperone involved in gene silencing [Transcription / Chromatin structure and dynamics];


Pssm-ID: 227466 [Multi-domain]  Cd Length: 279  Bit Score: 43.06  E-value: 3.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1658 RELILDKPKEKAPEPKQDEEKsELDEATTDKPEGDEKFKTEGESKKDLTDSEETKLES-SAMEVD---SKEESEPDDSKK 1733
Cdd:COG5137   142 REILAEKPRVTRFNIVWDNDE-DNDEAPPAQPDVDNEEEERLEESDGREEEEDEEVGSdSYGEGNrelNEEEEEEAEGSD 220
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 386768875 1734 SDEDNKDKDKMEVDDEVGkSDKESKPEEQSETVKTEENSKAIEEDKSS 1781
Cdd:COG5137   221 DGEDVVDYEGERIDKKQG-EEEEMEEEVINLFEIEWEEESPSEEVPRN 267
Granin pfam01271
Granin (chromogranin or secretogranin);
1595-1866 4.00e-03

Granin (chromogranin or secretogranin);


Pssm-ID: 279595 [Multi-domain]  Cd Length: 584  Bit Score: 43.48  E-value: 4.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875  1595 LPLDESSQLEA----SSSTSAVAEKERQISTDAANAAMSSKPNYVyiNTGDEDSMVVQLVLAMRMGKRELILDKPKEKAP 1670
Cdd:pfam01271   60 LLRDLADQSEAshlsSRSRDGLSDEDMQIITEALRQAENEPGGHS--RENQPYALQVEKEFKTDHSDDYETQQWEEEKLK 137
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875  1671 EPKQDEEKSELDEattdkpegDEKFKTEGE-SKKDLTDSEETKLESSAMEVDSKEESEPDDSKKSDEdnKDKDKMEVDDE 1749
Cdd:pfam01271  138 HMRFPLRYEENSE--------EKHSEREGElSEVFENPRSQATLKKVFEEVSRLDTPSKQKREKSDE--REKSSQESGED 207
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875  1750 VGKSdkESKPEEQSETVKTEENSKAIEEDKSSTVL--TADHAKEPETVLEKMEVDEKANDDQSAVSKAEGSDEKSTDDSn 1827
Cdd:pfam01271  208 TYRQ--ENIPQEDQVGPEDQEPSEEGEEDATQEEVkrSRPRTHHGRSLPDESSRGGQLGLEEEASEEEEEYGEESRGLS- 284
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 386768875  1828 pEEATTEKNKESLEIEGEKERVKEGEESVKKENDEKTEA 1866
Cdd:pfam01271  285 -AVQTYLLRLVNARGRGRSEKRAERERSEESEEEELKRA 322
PRK08581 PRK08581
amidase domain-containing protein;
1558-1837 4.65e-03

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 43.24  E-value: 4.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1558 PSANASNSNAGSDVEKTEPQSGAEGDAAQEVGEEKSnlplDESSQLEASSSTSAVAEKERqiSTDAANAAMSSkpnyvyi 1637
Cdd:PRK08581   18 PTLTSPTAYADDPQKDSTAKTTSHDSKKSNDDETSK----DTSSKDTDKADNNNTSNQDN--NDKKFSTIDSS------- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1638 nTGDEDSMVVQLVlamrmgKRELILDKPKEKAPEPKQDEEKSELDEATTDKPEGDEKFKTEGESKKDLTDSEETKLESSA 1717
Cdd:PRK08581   85 -TSDSNNIIDFIY------KNLPQTNINQLLTKNKYDDNYSLTTLIQNLFNLNSDISDYEQPRNSEKSTNDSNKNSDSSI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1718 MEVDSKEESEPDDSKKSDEDNKDKDKMEVDDEVGKSDK---ESKPEEQSETVKTEENSKAIEEDKSSTVLTADhakepeT 1794
Cdd:PRK08581  158 KNDTDTQSSKQDKADNQKAPSSNNTKPSTSNKQPNSPKptqPNQSNSQPASDDTANQKSSSKDNQSMSDSALD------S 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 386768875 1795 VLEKMEVDEKANDDQSAVSKaEGSDEKSTDDSNPEEATTEKNK 1837
Cdd:PRK08581  232 ILDQYSEDAKKTQKDYASQS-KKDKTETSNTKNPQLPTQDELK 273
PRK05901 PRK05901
RNA polymerase sigma factor; Provisional
1663-1826 4.67e-03

RNA polymerase sigma factor; Provisional


Pssm-ID: 235640 [Multi-domain]  Cd Length: 509  Bit Score: 43.44  E-value: 4.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1663 DKPKEKAPEPKQDEEKSELDEATTDKPEGDEKFKTEGESKKDLTDSEETKLESSAMEVDSKEESEPDDSKKSDEDNKDKD 1742
Cdd:PRK05901   55 VLIFLSGMVKDTDDATESDIPKKKTKTAAKAAAAKAPAKKKLKDELDSSKKAEKKNALDKDDDLNYVKDIDVLNQADDDD 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1743 KMEVDDEVGKSDKESKPEEQSETVKTEENSKAIEEDKsstvltADHAKEPETVLEKMEVDEKANDDQSAVSKAEGSDEKS 1822
Cdd:PRK05901  135 DDDDDDDLDDDDIDDDDDDEDDDEDDDDDDVDDEDEE------KKEAKELEKLSDDDDFVWDEDDSEALRQARKDAKLTA 208

                  ....
gi 386768875 1823 TDDS 1826
Cdd:PRK05901  209 TADP 212
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
1517-1749 4.71e-03

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 43.50  E-value: 4.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1517 SNKRRSSRNTQRKKYIDDVMlrfsDDENSLLVASPVKKDKKPSANASNSNAGSDVEKtePQSGAEGDAAQEVGEEKSNLP 1596
Cdd:PTZ00108 1160 SKTKGKASKLRKPKLKKKEK----KKKKSSADKSKKASVVGNSKRVDSDEKRKLDDK--PDNKKSNSSGSDQEDDEEQKT 1233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1597 LDESSQLEASSSTSAVAEKERQISTDAANAAMSSKPNyvyintGDEDSMVVQLVLAM------RMGKRELILDKPKEKAP 1670
Cdd:PTZ00108 1234 KPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGK------PKNAPKRVSAVQYSppppskRPDGESNGGSKPSSPTK 1307
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1671 EPKQDEEKSELDEATTDKPEGDEKF--KTEGESKKDLTDSEETKLESSAMEVDSKEESEPDDSKKSDEDNKDKDKMEVDD 1748
Cdd:PTZ00108 1308 KKVKKRLEGSLAALKKKKKSEKKTArkKKSKTRVKQASASQSSRLLRRPRKKKSDSSSEDDDDSEVDDSEDEDDEDDEDD 1387

                  .
gi 386768875 1749 E 1749
Cdd:PTZ00108 1388 D 1388
chromodomain cd18969
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; for most members ...
1941-1991 5.89e-03

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


Pssm-ID: 349325  Cd Length: 56  Bit Score: 37.89  E-value: 5.89e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 386768875 1941 EVDRVLDmsvHTDETSGETTKHYLVKWKSLPYEDCTWELEEDVDN--DKIEQY 1991
Cdd:cd18969     5 EIEEILD---VKKGGFEDGKLAYFVKWKGYPSSENSWVTEEDAANaqEMIEEY 54
PRK12678 PRK12678
transcription termination factor Rho; Provisional
1319-1500 8.36e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 42.58  E-value: 8.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1319 PPRDRTPKAKKPKDPNDPNSTETPA-AVKKRAGASKRRKQYGEDGAEQTGE--GSEVEDNKPLVPKAGSADGEA-----E 1390
Cdd:PRK12678  105 APAARAAAAAAAEAASAPEAAQARErRERGEAARRGAARKAGEGGEQPATEarADAAERTEEEERDERRRRGDRedrqaE 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768875 1391 TTSGGTGVDGESPDYDDIPVSKIPRGSNEDEKEAEAGDETVDSvpDSAGDPASTPSRRDRKRSTARSRRNANSEEGGSAR 1470
Cdd:PRK12678  185 AERGERGRREERGRDGDDRDRRDRREQGDRREERGRRDGGDRR--GRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRR 262
                         170       180       190
                  ....*....|....*....|....*....|
gi 386768875 1471 KNRGslsakalKKRRNRGRIVPESDGEDDT 1500
Cdd:PRK12678  263 GRRF-------RDRDRRGRRGGDGGNEREP 285
 
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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