|
Name |
Accession |
Description |
Interval |
E-value |
| SEN1_N |
pfam12726 |
SEN1 N terminal; This domain is found at the N terminal of the helicase SEN1. SEN1 is a Pol II ... |
75-784 |
6.03e-133 |
|
SEN1 N terminal; This domain is found at the N terminal of the helicase SEN1. SEN1 is a Pol II termination factor for noncoding RNA genes. The N terminal of SEN1, unlike the C terminal, is not required for growth.
Pssm-ID: 432746 Cd Length: 744 Bit Score: 434.83 E-value: 6.03e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 75 FKKHLNERLQLCPKCIVKYHQSLDDFKSLCLniFHFDPNTLEIVMEKIYSWDIFRLQEVLKT----------VPKIDTSS 144
Cdd:pfam12726 1 LKERLNACLSSCDKCVRNFHRGKKELRQTFA--ERFPEETVAQFLDKLDEWDIERILPGLDKakeilekrgiFSKSSLSS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 145 ASKPILCAFYEILYSPRIL-HNKEIFPLFRNRF----LESGFLRLSKnLVPGVISLLFSRDDELRRWACSILSDVKT-IS 218
Cdd:pfam12726 79 HLKEVLLALYEALCCPPYLrSDPELRALFDYVFkllqTKKKPLRLGT-LLPGMTYFLFDGDPEERRWARRQLERLKRsLT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 219 DNEFKILEGPLLQE-IRSLDQKKENENEMQIFLKGLSLLLKHVDH----LYFRGLTGK--NFNVADFILSGLQSDHTNLC 291
Cdd:pfam12726 158 PEEFDWAVHDLLEEaIVHLSNIQLDPSFIERFWSGFSLILRLLDKdlitHRLRALEVNppIEDIYRLLLNHLSSTLDPPL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 292 PSFLVCLHSLLYCYGRNFWT--PEISPSEVIDKIFNGNAYKRWTEENTSNFSNDQKAEN---PFEWATSLLKTISIIDEV 366
Cdd:pfam12726 238 PDLLRALSLLLEKSGKAFWDamGPISPQVVLDQIFDNPAFAKLLAQSLEEEMDPPDDDSlsdLLSWIPPFLRSLSPSQRI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 367 ELINKILINYTMQYKKELEVGFKNVQLLQSLADIFSVLFSEYFMIFPHSDQSLQ--NKVFELH-STLAIKFDELFRLLNL 443
Cdd:pfam12726 318 DACRKLLHFLLERLQHDRYSDPARPARAACLRAGLTALLRTLLTFLDPERSLLYstSLDFVNElLNVVLKHADLIVDLAL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 444 ENEE-----SVEWRLIKKVFEYRLNLDLYILKQFYCHYLDRNRKPPLniksVSESFKNFWVYLQNVFREEKFFMVRIVFR 518
Cdd:pfam12726 398 KLKPgdkawSEVSKSARDVIEKALALDIKSLAEESYALLSGKPPQHG----VSRSSPNLWKALLDSLRPGDLDLAKAILI 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 519 ACSTVCLIDKLPPKKVDI-----PFKSDFENALNGFVATFSEMLIQTQC-WHLSAQTQLVSNPLTFRGIFSLVFSPILEI 592
Cdd:pfam12726 474 SLAPLAGLEKFKPKSKKQldqldAAKSQFNKALGQLRDLISRLLERLSDfSLPSDLKELLSDPEAAQGLWSLLFSPDDEL 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 593 STGSISIIKSISLSDSVVDTIGELLRSQFSNTLNSSCYVLLQWLKVRNFGGAKHIVYFNKLIINTIFDSVDGLTSKDATF 672
Cdd:pfam12726 554 YQAALNLLKQAFDVDGRLEAIRALLESNLTTTLSAINDALRQLTKLKTFEPAPRLVRCLMDILDVLCDPSDGLLRSRSLT 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 673 AKQVekKESLKNFWESLWKFFTHFFIVLPTWPV-HDKDNLVDLMRDTLDFCDMLINIFEEVNGFIFGLSDNDIKIVSAND 751
Cdd:pfam12726 634 SEGE--AAALKKFWSLMWQFLDMIFKRTESWASkYEKSEMEEFCRDTLEFADLLLDQYRLFASALSGASGSDSGGKSSSS 711
|
730 740 750
....*....|....*....|....*....|...
gi 19112847 752 KGSALAMCIADSLVTVSYWLKLTDSSLLTSVVK 784
Cdd:pfam12726 712 AGKKLLKSPQKAFKGLVKWLRLRDEYLLSSCVS 744
|
|
| AAA_12 |
pfam13087 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1560-1756 |
7.92e-80 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.
Pssm-ID: 463780 [Multi-domain] Cd Length: 196 Bit Score: 261.71 E-value: 7.92e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1560 YSQSLYVRMFKQHNESACLLSIQYRMNPEISRFPSKFFYNSKLLDGPNMSAVT-SRPWHEDPQLGIYRFFNVHGTEAFSN 1638
Cdd:pfam13087 1 LDRSLFERLQELGPSAVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAERPlPDDFHLPDPLGPLVFIDVDGSEEEES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1639 --SKSLYNVEEASFILLLYERLIQCYlnIDFEGKIGVVTPYRSQVQQLRSQFQRKYGsiIFKHLDIHTVDGFQGQEKDII 1716
Cdd:pfam13087 81 dgGTSYSNEAEAELVVQLVEKLIKSG--PEEPSDIGVITPYRAQVRLIRKLLKRKLG--GKLEIEVNTVDGFQGREKDVI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 19112847 1717 IFSCVRSSMSGGIGFLQDLRRLNVALTRAKSSLYIVGNSK 1756
Cdd:pfam13087 157 IFSCVRSNEKGGIGFLSDPRRLNVALTRAKRGLIIVGNAK 196
|
|
| TIGR00376 |
TIGR00376 |
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ... |
1219-1780 |
8.33e-78 |
|
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of this family have been characterized as binding certain single-stranded G-rich DNA sequences (GGGGT and GGGCT). A number of related proteins are characterized as helicases. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273041 [Multi-domain] Cd Length: 636 Bit Score: 272.07 E-value: 8.33e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1219 KLFNATTSLREFAALKSLR--HLPLSQRILDANVtrlPSNFTDDKKQKIMKSyGVNEPQAYAIYASSVNDGFTLIQGPPG 1296
Cdd:TIGR00376 108 LYANDVTFKRMKEALRALTenHSRLLEFLLGREA---PSKASEIHDFQFFDP-NLNESQKEAVLFALSSKDLFLIHGPPG 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1297 TGKTKTILGMIgavltssSQGLQFNvpgqtrktskNKILICAPSNAAIDEILLRIkagvydhegIKFFPKVIRVGFGDSI 1376
Cdd:TIGR00376 184 TGKTRTVVELI-------RQLVKRG----------LRVLVTAPSNIAVDNLLERL---------ALCDQKIVRLGHPARL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1377 SVHAKEFTLEEQmikqmeltnLKKDQEANNSSDTRKKYDSIIKKRDSLREDLEKFRSTGKNSSILEAQLREitKQKNMLE 1456
Cdd:TIGR00376 238 LKSNKQHSLDYL---------IENHPKYQIVADIREKIDELIEERNKKTKPSPQKRRGLSDIKILRKALKK--REARGIE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1457 ----QSLDDMRERQRSTNRNLDVLKK---QIQNQLLQEADivcATLSASGHELLLnaGLTFRTVIIDEAAQAVELSSIIP 1529
Cdd:TIGR00376 307 slkiASMAEWIETNKSIDRLLKLLPEseeRIMNEILAESD---ATNSMAGSEILN--GQYFDVAVIDEASQAMEPSCLIP 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1530 LKYGcESCVMVGDPNQLPPTVLSKTSAKFgySQSLYVRMFKQHNESACLLSIQYRMNPEISRFPSKFFYNSKLLDGPNMS 1609
Cdd:TIGR00376 382 LLKA-RKLILAGDHKQLPPTILSHDAEEL--SLTLFERLIKEYPERSRTLNVQYRMNQKIMEFPSREFYNGKLTAHESVA 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1610 AVTSR--------PWHEDPQLGI-YRFFNVHGTEAFS----NSKSLYNVEEASFILLLYERLIQCYLNidfEGKIGVVTP 1676
Cdd:TIGR00376 459 NILLRdlpkveatESEDDLETGIpLLFIDTSGCELFElkeaDSTSKYNPGEAELVSEIIQALVKMGVP---ANDIGVITP 535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1677 YRSQVQQLRSQFQRKYGSIifkhlDIHTVDGFQGQEKDIIIFSCVRSSMSGGIGFLQDLRRLNVALTRAKSSLYIVGNSK 1756
Cdd:TIGR00376 536 YDAQVDLLRQLLEHRHIDI-----EVSSVDGFQGREKEVIIISFVRSNRKGEVGFLKDLRRLNVALTRARRKLIVIGDSR 610
|
570 580
....*....|....*....|....
gi 19112847 1757 PLMQEDIFYSLIEDAKTRGVWRDL 1780
Cdd:TIGR00376 611 TLSNHKFYKRLIEWCKQHGEVREA 634
|
|
| DEXXQc_SETX |
cd18042 |
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in ... |
1272-1584 |
5.34e-76 |
|
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in transcription, neurogenesis, and antiviral response. SEXT is an R-loop-associated protein that is thought to function as an RNA/DNA helicase. R-loops consist of RNA/DNA hybrids, formed during transcription when nascent RNA hybridizes to the DNA template strand, displacing the non-template DNA strand. Mutations in SETX are linked to two neurodegenerative disorders: ataxia with oculomotor apraxia type 2 (AOA2) and amyotrophic lateral sclerosis type 4 (ALS4). S. cerevisiae homolog splicing endonuclease 1 (Sen1) is an exclusively nuclear protein, important for nucleolar organization. S. cerevisiae Sen1 and its ortholog, the Schizosaccharomyces pombe Sen1, share conserved domains and belong to the family I class of helicases. Both proteins translocate 5' to 3' and unwind both DNA and RNA duplexes and also RNA/DNA hybrids in vitro. SETX 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: 438712 [Multi-domain] Cd Length: 218 Bit Score: 251.75 E-value: 5.34e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1272 NEPQAYAIYAS-SVNDGFTLIQGPPGTGKTKTILGMIGAVLTSSSQ--------GLQFNVPGQTRKTSKNKILICAPSNA 1342
Cdd:cd18042 2 NESQLEAIASAlQNSPGITLIQGPPGTGKTKTIVGILSVLLAGKYRkyyekvkkKLRKLQRNLNNKKKKNRILVCAPSNA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1343 AIDEILLRIKA-GVYDHEGIKFFPKVIRVGfgdsisvhakeftleeqmikqmeltnlkkdqeannssdtrkkydsiikkr 1421
Cdd:cd18042 82 AVDEIVLRLLSeGFLDGDGRSYKPNVVRVG-------------------------------------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1422 dslredlekfrstgknssileaqlreitkqknmleqslddmrerqrstnrnldvlKKQIQNQLLQEADIVCATLSASGHE 1501
Cdd:cd18042 112 -------------------------------------------------------RQELRASILNEADIVCTTLSSSGSD 136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1502 LLLNAGLTFRTVIIDEAAQAVELSSIIPLKYGCESCVMVGDPNQLPPTVLSKTSAKFGYSQSLYVRMFKqHNESACLLSI 1581
Cdd:cd18042 137 LLESLPRGFDTVIIDEAAQAVELSTLIPLRLGCKRLILVGDPKQLPATVFSKVAQKLGYDRSLFERLQL-AGYPVLMLTT 215
|
...
gi 19112847 1582 QYR 1584
Cdd:cd18042 216 QYR 218
|
|
| AAA_11 |
pfam13086 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1274-1553 |
6.95e-73 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.
Pssm-ID: 404072 [Multi-domain] Cd Length: 248 Bit Score: 243.79 E-value: 6.95e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1274 PQAYAIYASSVNDGFTLIQGPPGTGKTKTILGMIGavltsssqglQFNVPGQTRKTSKNKILICAPSNAAIDEILLRIKA 1353
Cdd:pfam13086 1 SQREAIRSALSSSHFTLIQGPPGTGKTTTIVELIR----------QLLSYPATSAAAGPRILVCAPSNAAVDNILERLLR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1354 gvydhEGIKFFPKVIRVGFGDSISVHAKEFTLEEQMIKQMEltnlkkdqeannssdtRKKYDSIIKKRDSLREDLEKFRS 1433
Cdd:pfam13086 71 -----KGQKYGPKIVRIGHPAAISEAVLPVSLDYLVESKLN----------------NEEDAQIVKDISKELEKLAKALR 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1434 TGKNSSILEAQLREITKQKNMLEQSLDDMRERQRSTNRNLDVLKKQIQNQLLQEADIVCATLSASGHELLLNAGLtFRTV 1513
Cdd:pfam13086 130 AFEKEIIVEKLLKSRNKDKSKLEQERRKLRSERKELRKELRRREQSLEREILDEAQIVCSTLSGAGSRLLSSLAN-FDVV 208
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 19112847 1514 IIDEAAQAVELSSIIPLKYGCESCVMVGDPNQLPPTVLSK 1553
Cdd:pfam13086 209 IIDEAAQALEPSTLIPLLRGPKKVVLVGDPKQLPPTVISK 248
|
|
| DNA2 |
COG1112 |
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair]; |
1421-1774 |
6.08e-69 |
|
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
Pssm-ID: 440729 [Multi-domain] Cd Length: 819 Bit Score: 250.43 E-value: 6.08e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1421 RDSLREDLEKFRSTGKNSSILEAQLREITKQKNMLEQSLDDMRERQRSTNRNLDV---LKKQIQNQLLQEADIVCATLSA 1497
Cdd:COG1112 465 LLLLLAAAAALLALALLESLLEELIEEHPEELEKLIAELREAARLRRALRRELKKrreLRKLLWDALLELAPVVGMTPAS 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1498 SGHELLLNAGLtFRTVIIDEAAQAVELSSIIPLkYGCESCVMVGDPNQLPPTVLS---KTSAKFGYSQSLYVRMFKQHNE 1574
Cdd:COG1112 545 VARLLPLGEGS-FDLVIIDEASQATLAEALGAL-ARAKRVVLVGDPKQLPPVVFGeeaEEVAEEGLDESLLDRLLARLPE 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1575 SACLLSIQYRMNPEISRFPSKFFYNSKLLDGPNmsaVTSRPWhEDPQLGIyRFFNVHGTEAfSNSKSLYNVEEASFILLL 1654
Cdd:COG1112 623 RGVMLREHYRMHPEIIAFSNRLFYDGKLVPLPS---PKARRL-ADPDSPL-VFIDVDGVYE-RRGGSRTNPEEAEAVVEL 696
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1655 YERLIQCYLNidfEGKIGVVTPYRSQVQQLRSQFqRKYGSIIFKHLDIHTVDGFQGQEKDIIIFSCVRSS---MSGGIGF 1731
Cdd:COG1112 697 VRELLEDGPD---GESIGVITPYRAQVALIRELL-REALGDGLEPVFVGTVDRFQGDERDVIIFSLVYSNdedVPRNFGF 772
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 19112847 1732 LQ-DLRRLNVALTRAKSSLYIVGNSKPLMQEDI---FYSLIEDAKTR 1774
Cdd:COG1112 773 LNgGPRRLNVAVSRARRKLIVVGSRELLDSDPStpaLKRLLEYLERA 819
|
|
| SF1_C_Upf1 |
cd18808 |
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ... |
1585-1772 |
2.88e-63 |
|
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family includes UPF1, HELZ, Mov10L1, Aquarius, IGHMBP2 (SMUBP2), and similar proteins. They are DEAD-like helicases belonging to superfamily (SF)1, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF2 helicases, SF1 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: 350195 [Multi-domain] Cd Length: 184 Bit Score: 213.64 E-value: 2.88e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1585 MNPEISRFPSKFFYNSKLLDGPNMSAVTSRPWHEDPQlGIYRFFNVHGTEA-FSNSKSLYNVEEASFILLLYERLIQCYL 1663
Cdd:cd18808 1 MHPEISEFPSKLFYEGKLKAGVSVAARLNPPPLPGPS-KPLVFVDVSGGEErEESGTSKSNEAEAELVVELVKYLLKSGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1664 NidfEGKIGVVTPYRSQVQQLRSQFQRKYGsiIFKHLDIHTVDGFQGQEKDIIIFSCVRSSMSGG-IGFLQDLRRLNVAL 1742
Cdd:cd18808 80 K---PSSIGVITPYRAQVALIRELLRKRGG--LLEDVEVGTVDNFQGREKDVIILSLVRSNESGGsIGFLSDPRRLNVAL 154
|
170 180 190
....*....|....*....|....*....|
gi 19112847 1743 TRAKSSLYIVGNSKPLMQEDIFYSLIEDAK 1772
Cdd:cd18808 155 TRAKRGLIIVGNPDTLSKDPLWKKLLEYLE 184
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1391-1484 |
8.57e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 8.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1391 KQMELTNLKKDQEAnnssdTRKKYDSIIKKRDSLREDLEKFRstgKNSSILEAQLREITKQKNMLEQSLDDMRERQRSTN 1470
Cdd:COG4942 25 AEAELEQLQQEIAE-----LEKELAALKKEEKALLKQLAALE---RRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90
....*....|....
gi 19112847 1471 RNLDVLKKQIQNQL 1484
Cdd:COG4942 97 AELEAQKEELAELL 110
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| SEN1_N |
pfam12726 |
SEN1 N terminal; This domain is found at the N terminal of the helicase SEN1. SEN1 is a Pol II ... |
75-784 |
6.03e-133 |
|
SEN1 N terminal; This domain is found at the N terminal of the helicase SEN1. SEN1 is a Pol II termination factor for noncoding RNA genes. The N terminal of SEN1, unlike the C terminal, is not required for growth.
Pssm-ID: 432746 Cd Length: 744 Bit Score: 434.83 E-value: 6.03e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 75 FKKHLNERLQLCPKCIVKYHQSLDDFKSLCLniFHFDPNTLEIVMEKIYSWDIFRLQEVLKT----------VPKIDTSS 144
Cdd:pfam12726 1 LKERLNACLSSCDKCVRNFHRGKKELRQTFA--ERFPEETVAQFLDKLDEWDIERILPGLDKakeilekrgiFSKSSLSS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 145 ASKPILCAFYEILYSPRIL-HNKEIFPLFRNRF----LESGFLRLSKnLVPGVISLLFSRDDELRRWACSILSDVKT-IS 218
Cdd:pfam12726 79 HLKEVLLALYEALCCPPYLrSDPELRALFDYVFkllqTKKKPLRLGT-LLPGMTYFLFDGDPEERRWARRQLERLKRsLT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 219 DNEFKILEGPLLQE-IRSLDQKKENENEMQIFLKGLSLLLKHVDH----LYFRGLTGK--NFNVADFILSGLQSDHTNLC 291
Cdd:pfam12726 158 PEEFDWAVHDLLEEaIVHLSNIQLDPSFIERFWSGFSLILRLLDKdlitHRLRALEVNppIEDIYRLLLNHLSSTLDPPL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 292 PSFLVCLHSLLYCYGRNFWT--PEISPSEVIDKIFNGNAYKRWTEENTSNFSNDQKAEN---PFEWATSLLKTISIIDEV 366
Cdd:pfam12726 238 PDLLRALSLLLEKSGKAFWDamGPISPQVVLDQIFDNPAFAKLLAQSLEEEMDPPDDDSlsdLLSWIPPFLRSLSPSQRI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 367 ELINKILINYTMQYKKELEVGFKNVQLLQSLADIFSVLFSEYFMIFPHSDQSLQ--NKVFELH-STLAIKFDELFRLLNL 443
Cdd:pfam12726 318 DACRKLLHFLLERLQHDRYSDPARPARAACLRAGLTALLRTLLTFLDPERSLLYstSLDFVNElLNVVLKHADLIVDLAL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 444 ENEE-----SVEWRLIKKVFEYRLNLDLYILKQFYCHYLDRNRKPPLniksVSESFKNFWVYLQNVFREEKFFMVRIVFR 518
Cdd:pfam12726 398 KLKPgdkawSEVSKSARDVIEKALALDIKSLAEESYALLSGKPPQHG----VSRSSPNLWKALLDSLRPGDLDLAKAILI 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 519 ACSTVCLIDKLPPKKVDI-----PFKSDFENALNGFVATFSEMLIQTQC-WHLSAQTQLVSNPLTFRGIFSLVFSPILEI 592
Cdd:pfam12726 474 SLAPLAGLEKFKPKSKKQldqldAAKSQFNKALGQLRDLISRLLERLSDfSLPSDLKELLSDPEAAQGLWSLLFSPDDEL 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 593 STGSISIIKSISLSDSVVDTIGELLRSQFSNTLNSSCYVLLQWLKVRNFGGAKHIVYFNKLIINTIFDSVDGLTSKDATF 672
Cdd:pfam12726 554 YQAALNLLKQAFDVDGRLEAIRALLESNLTTTLSAINDALRQLTKLKTFEPAPRLVRCLMDILDVLCDPSDGLLRSRSLT 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 673 AKQVekKESLKNFWESLWKFFTHFFIVLPTWPV-HDKDNLVDLMRDTLDFCDMLINIFEEVNGFIFGLSDNDIKIVSAND 751
Cdd:pfam12726 634 SEGE--AAALKKFWSLMWQFLDMIFKRTESWASkYEKSEMEEFCRDTLEFADLLLDQYRLFASALSGASGSDSGGKSSSS 711
|
730 740 750
....*....|....*....|....*....|...
gi 19112847 752 KGSALAMCIADSLVTVSYWLKLTDSSLLTSVVK 784
Cdd:pfam12726 712 AGKKLLKSPQKAFKGLVKWLRLRDEYLLSSCVS 744
|
|
| AAA_12 |
pfam13087 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1560-1756 |
7.92e-80 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.
Pssm-ID: 463780 [Multi-domain] Cd Length: 196 Bit Score: 261.71 E-value: 7.92e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1560 YSQSLYVRMFKQHNESACLLSIQYRMNPEISRFPSKFFYNSKLLDGPNMSAVT-SRPWHEDPQLGIYRFFNVHGTEAFSN 1638
Cdd:pfam13087 1 LDRSLFERLQELGPSAVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAERPlPDDFHLPDPLGPLVFIDVDGSEEEES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1639 --SKSLYNVEEASFILLLYERLIQCYlnIDFEGKIGVVTPYRSQVQQLRSQFQRKYGsiIFKHLDIHTVDGFQGQEKDII 1716
Cdd:pfam13087 81 dgGTSYSNEAEAELVVQLVEKLIKSG--PEEPSDIGVITPYRAQVRLIRKLLKRKLG--GKLEIEVNTVDGFQGREKDVI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 19112847 1717 IFSCVRSSMSGGIGFLQDLRRLNVALTRAKSSLYIVGNSK 1756
Cdd:pfam13087 157 IFSCVRSNEKGGIGFLSDPRRLNVALTRAKRGLIIVGNAK 196
|
|
| TIGR00376 |
TIGR00376 |
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ... |
1219-1780 |
8.33e-78 |
|
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of this family have been characterized as binding certain single-stranded G-rich DNA sequences (GGGGT and GGGCT). A number of related proteins are characterized as helicases. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273041 [Multi-domain] Cd Length: 636 Bit Score: 272.07 E-value: 8.33e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1219 KLFNATTSLREFAALKSLR--HLPLSQRILDANVtrlPSNFTDDKKQKIMKSyGVNEPQAYAIYASSVNDGFTLIQGPPG 1296
Cdd:TIGR00376 108 LYANDVTFKRMKEALRALTenHSRLLEFLLGREA---PSKASEIHDFQFFDP-NLNESQKEAVLFALSSKDLFLIHGPPG 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1297 TGKTKTILGMIgavltssSQGLQFNvpgqtrktskNKILICAPSNAAIDEILLRIkagvydhegIKFFPKVIRVGFGDSI 1376
Cdd:TIGR00376 184 TGKTRTVVELI-------RQLVKRG----------LRVLVTAPSNIAVDNLLERL---------ALCDQKIVRLGHPARL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1377 SVHAKEFTLEEQmikqmeltnLKKDQEANNSSDTRKKYDSIIKKRDSLREDLEKFRSTGKNSSILEAQLREitKQKNMLE 1456
Cdd:TIGR00376 238 LKSNKQHSLDYL---------IENHPKYQIVADIREKIDELIEERNKKTKPSPQKRRGLSDIKILRKALKK--REARGIE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1457 ----QSLDDMRERQRSTNRNLDVLKK---QIQNQLLQEADivcATLSASGHELLLnaGLTFRTVIIDEAAQAVELSSIIP 1529
Cdd:TIGR00376 307 slkiASMAEWIETNKSIDRLLKLLPEseeRIMNEILAESD---ATNSMAGSEILN--GQYFDVAVIDEASQAMEPSCLIP 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1530 LKYGcESCVMVGDPNQLPPTVLSKTSAKFgySQSLYVRMFKQHNESACLLSIQYRMNPEISRFPSKFFYNSKLLDGPNMS 1609
Cdd:TIGR00376 382 LLKA-RKLILAGDHKQLPPTILSHDAEEL--SLTLFERLIKEYPERSRTLNVQYRMNQKIMEFPSREFYNGKLTAHESVA 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1610 AVTSR--------PWHEDPQLGI-YRFFNVHGTEAFS----NSKSLYNVEEASFILLLYERLIQCYLNidfEGKIGVVTP 1676
Cdd:TIGR00376 459 NILLRdlpkveatESEDDLETGIpLLFIDTSGCELFElkeaDSTSKYNPGEAELVSEIIQALVKMGVP---ANDIGVITP 535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1677 YRSQVQQLRSQFQRKYGSIifkhlDIHTVDGFQGQEKDIIIFSCVRSSMSGGIGFLQDLRRLNVALTRAKSSLYIVGNSK 1756
Cdd:TIGR00376 536 YDAQVDLLRQLLEHRHIDI-----EVSSVDGFQGREKEVIIISFVRSNRKGEVGFLKDLRRLNVALTRARRKLIVIGDSR 610
|
570 580
....*....|....*....|....
gi 19112847 1757 PLMQEDIFYSLIEDAKTRGVWRDL 1780
Cdd:TIGR00376 611 TLSNHKFYKRLIEWCKQHGEVREA 634
|
|
| DEXXQc_SETX |
cd18042 |
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in ... |
1272-1584 |
5.34e-76 |
|
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in transcription, neurogenesis, and antiviral response. SEXT is an R-loop-associated protein that is thought to function as an RNA/DNA helicase. R-loops consist of RNA/DNA hybrids, formed during transcription when nascent RNA hybridizes to the DNA template strand, displacing the non-template DNA strand. Mutations in SETX are linked to two neurodegenerative disorders: ataxia with oculomotor apraxia type 2 (AOA2) and amyotrophic lateral sclerosis type 4 (ALS4). S. cerevisiae homolog splicing endonuclease 1 (Sen1) is an exclusively nuclear protein, important for nucleolar organization. S. cerevisiae Sen1 and its ortholog, the Schizosaccharomyces pombe Sen1, share conserved domains and belong to the family I class of helicases. Both proteins translocate 5' to 3' and unwind both DNA and RNA duplexes and also RNA/DNA hybrids in vitro. SETX 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: 438712 [Multi-domain] Cd Length: 218 Bit Score: 251.75 E-value: 5.34e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1272 NEPQAYAIYAS-SVNDGFTLIQGPPGTGKTKTILGMIGAVLTSSSQ--------GLQFNVPGQTRKTSKNKILICAPSNA 1342
Cdd:cd18042 2 NESQLEAIASAlQNSPGITLIQGPPGTGKTKTIVGILSVLLAGKYRkyyekvkkKLRKLQRNLNNKKKKNRILVCAPSNA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1343 AIDEILLRIKA-GVYDHEGIKFFPKVIRVGfgdsisvhakeftleeqmikqmeltnlkkdqeannssdtrkkydsiikkr 1421
Cdd:cd18042 82 AVDEIVLRLLSeGFLDGDGRSYKPNVVRVG-------------------------------------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1422 dslredlekfrstgknssileaqlreitkqknmleqslddmrerqrstnrnldvlKKQIQNQLLQEADIVCATLSASGHE 1501
Cdd:cd18042 112 -------------------------------------------------------RQELRASILNEADIVCTTLSSSGSD 136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1502 LLLNAGLTFRTVIIDEAAQAVELSSIIPLKYGCESCVMVGDPNQLPPTVLSKTSAKFGYSQSLYVRMFKqHNESACLLSI 1581
Cdd:cd18042 137 LLESLPRGFDTVIIDEAAQAVELSTLIPLRLGCKRLILVGDPKQLPATVFSKVAQKLGYDRSLFERLQL-AGYPVLMLTT 215
|
...
gi 19112847 1582 QYR 1584
Cdd:cd18042 216 QYR 218
|
|
| AAA_11 |
pfam13086 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1274-1553 |
6.95e-73 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.
Pssm-ID: 404072 [Multi-domain] Cd Length: 248 Bit Score: 243.79 E-value: 6.95e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1274 PQAYAIYASSVNDGFTLIQGPPGTGKTKTILGMIGavltsssqglQFNVPGQTRKTSKNKILICAPSNAAIDEILLRIKA 1353
Cdd:pfam13086 1 SQREAIRSALSSSHFTLIQGPPGTGKTTTIVELIR----------QLLSYPATSAAAGPRILVCAPSNAAVDNILERLLR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1354 gvydhEGIKFFPKVIRVGFGDSISVHAKEFTLEEQMIKQMEltnlkkdqeannssdtRKKYDSIIKKRDSLREDLEKFRS 1433
Cdd:pfam13086 71 -----KGQKYGPKIVRIGHPAAISEAVLPVSLDYLVESKLN----------------NEEDAQIVKDISKELEKLAKALR 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1434 TGKNSSILEAQLREITKQKNMLEQSLDDMRERQRSTNRNLDVLKKQIQNQLLQEADIVCATLSASGHELLLNAGLtFRTV 1513
Cdd:pfam13086 130 AFEKEIIVEKLLKSRNKDKSKLEQERRKLRSERKELRKELRRREQSLEREILDEAQIVCSTLSGAGSRLLSSLAN-FDVV 208
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 19112847 1514 IIDEAAQAVELSSIIPLKYGCESCVMVGDPNQLPPTVLSK 1553
Cdd:pfam13086 209 IIDEAAQALEPSTLIPLLRGPKKVVLVGDPKQLPPTVISK 248
|
|
| DNA2 |
COG1112 |
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair]; |
1421-1774 |
6.08e-69 |
|
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
Pssm-ID: 440729 [Multi-domain] Cd Length: 819 Bit Score: 250.43 E-value: 6.08e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1421 RDSLREDLEKFRSTGKNSSILEAQLREITKQKNMLEQSLDDMRERQRSTNRNLDV---LKKQIQNQLLQEADIVCATLSA 1497
Cdd:COG1112 465 LLLLLAAAAALLALALLESLLEELIEEHPEELEKLIAELREAARLRRALRRELKKrreLRKLLWDALLELAPVVGMTPAS 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1498 SGHELLLNAGLtFRTVIIDEAAQAVELSSIIPLkYGCESCVMVGDPNQLPPTVLS---KTSAKFGYSQSLYVRMFKQHNE 1574
Cdd:COG1112 545 VARLLPLGEGS-FDLVIIDEASQATLAEALGAL-ARAKRVVLVGDPKQLPPVVFGeeaEEVAEEGLDESLLDRLLARLPE 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1575 SACLLSIQYRMNPEISRFPSKFFYNSKLLDGPNmsaVTSRPWhEDPQLGIyRFFNVHGTEAfSNSKSLYNVEEASFILLL 1654
Cdd:COG1112 623 RGVMLREHYRMHPEIIAFSNRLFYDGKLVPLPS---PKARRL-ADPDSPL-VFIDVDGVYE-RRGGSRTNPEEAEAVVEL 696
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1655 YERLIQCYLNidfEGKIGVVTPYRSQVQQLRSQFqRKYGSIIFKHLDIHTVDGFQGQEKDIIIFSCVRSS---MSGGIGF 1731
Cdd:COG1112 697 VRELLEDGPD---GESIGVITPYRAQVALIRELL-REALGDGLEPVFVGTVDRFQGDERDVIIFSLVYSNdedVPRNFGF 772
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 19112847 1732 LQ-DLRRLNVALTRAKSSLYIVGNSKPLMQEDI---FYSLIEDAKTR 1774
Cdd:COG1112 773 LNgGPRRLNVAVSRARRKLIVVGSRELLDSDPStpaLKRLLEYLERA 819
|
|
| SF1_C_Upf1 |
cd18808 |
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ... |
1585-1772 |
2.88e-63 |
|
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family includes UPF1, HELZ, Mov10L1, Aquarius, IGHMBP2 (SMUBP2), and similar proteins. They are DEAD-like helicases belonging to superfamily (SF)1, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF2 helicases, SF1 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: 350195 [Multi-domain] Cd Length: 184 Bit Score: 213.64 E-value: 2.88e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1585 MNPEISRFPSKFFYNSKLLDGPNMSAVTSRPWHEDPQlGIYRFFNVHGTEA-FSNSKSLYNVEEASFILLLYERLIQCYL 1663
Cdd:cd18808 1 MHPEISEFPSKLFYEGKLKAGVSVAARLNPPPLPGPS-KPLVFVDVSGGEErEESGTSKSNEAEAELVVELVKYLLKSGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1664 NidfEGKIGVVTPYRSQVQQLRSQFQRKYGsiIFKHLDIHTVDGFQGQEKDIIIFSCVRSSMSGG-IGFLQDLRRLNVAL 1742
Cdd:cd18808 80 K---PSSIGVITPYRAQVALIRELLRKRGG--LLEDVEVGTVDNFQGREKDVIILSLVRSNESGGsIGFLSDPRRLNVAL 154
|
170 180 190
....*....|....*....|....*....|
gi 19112847 1743 TRAKSSLYIVGNSKPLMQEDIFYSLIEDAK 1772
Cdd:cd18808 155 TRAKRGLIIVGNPDTLSKDPLWKKLLEYLE 184
|
|
| DEXXQc_UPF1 |
cd18039 |
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ... |
1272-1584 |
7.78e-44 |
|
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of Nonsense Transcripts, or ATP-Dependent Helicase RENT1) is an RNA-dependent helicase and ATPase required for nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. It is recruited to mRNAs upon translation termination and undergoes a cycle of phosphorylation and dephosphorylation; its phosphorylation appears to be a key step in NMD. It is recruited by release factors to stalled ribosomes together with the SMG1C protein kinase complex to form the transient SURF (SMG1-UPF1-eRF1-eRF3) complex. In EJC-dependent NMD, the SURF complex associates with the exon junction complex (EJC) located downstream from the termination codon through UPF2 and allows the formation of an UPF1-UPF2-UPF3 surveillance complex which is believed to activate NMD. Diseases associated with UPF1 include juvenile amyotrophic lateral sclerosis and epidermolysis bullosa, junctional, non-Herlitz type. UPF1 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: 350797 [Multi-domain] Cd Length: 234 Bit Score: 159.72 E-value: 7.78e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1272 NEPQAYAIyASSVNDGFTLIQGPPGTGKTktilgmigavLTSSSQGLQFnvpgqtRKTSKNKILICAPSNAAIDEILLRI 1351
Cdd:cd18039 3 NHSQVDAV-KTALQRPLSLIQGPPGTGKT----------VTSATIVYHL------VKQGNGPVLVCAPSNVAVDQLTEKI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1352 -KAGVydhegikffpKVIRVgfgdsisvhakeftleeqmikqmeltnLKKDQEANNSSDtrkkydsiikkrdslrEDLek 1430
Cdd:cd18039 66 hQTGL----------KVVRL---------------------------CAKSREAVESPV----------------SFL-- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1431 frstgknssILEAQLRE-ITKQKNMLEQSL-DDMRERQRSTNRNLDVLKKQIQNQLLQEADIVCATLSASGHELLlnAGL 1508
Cdd:cd18039 91 ---------ALHNQVRNlDSAEKLELLKLLkLETGELSSADEKRYRKLKRKAERELLRNADVICCTCVGAGDPRL--SKM 159
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19112847 1509 TFRTVIIDEAAQAVELSSIIPLKYGCESCVMVGDPNQLPPTVLSKTSAKFGYSQSLYVRMFkQHNESACLLSIQYR 1584
Cdd:cd18039 160 KFRTVLIDEATQATEPECLIPLVHGAKQVILVGDHCQLGPVVMCKKAAKAGLSQSLFERLV-QLGIRPIRLQVQYR 234
|
|
| DEXXQc_SMUBP2 |
cd18044 |
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ... |
1272-1584 |
1.72e-29 |
|
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, or IGHMBP2) is a 5' to 3' helicase that unwinds RNA and DNA duplexes in an ATP-dependent reaction. It is a DNA-binding protein specific to 5'-phosphorylated single-stranded guanine-rich sequence (5'-GGGCT-3') related to the immunoglobulin mu chain switch region. The IGHMBP2 gene is responsible for Charcot-Marie-Tooth disease (CMT) type 2S and spinal muscular atrophy with respiratory distress type 1 (SMARD1). It is also thought to play a role in frontotemporal dementia (FTD) with amyotrophic lateral sclerosis (ALS) and major depressive disorder (MDD). SMUBP2 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: 350802 [Multi-domain] Cd Length: 191 Bit Score: 116.94 E-value: 1.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1272 NEPQAYAI-YASSVNDgFTLIQGPPGTGKTKTILGMIgavltsssqgLQFNVPGQtrktsknKILICAPSNAAIDEILLR 1350
Cdd:cd18044 3 NDSQKEAVkFALSQKD-VALIHGPPGTGKTTTVVEII----------LQAVKRGE-------KVLACAPSNIAVDNLVER 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1351 IkagvydhegIKFFPKVIRVGfgdsisvHAkeftleeqmikqmeltnlkkdqeannssdtrkkydsiikkrdslredlek 1430
Cdd:cd18044 65 L---------VALKVKVVRIG-------HP-------------------------------------------------- 78
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1431 frstgknssileAQLreitkQKNMLEQSLDdmrerqrstnrnldvlkkqiqnqLLQEADIVCATLSASGHELLLNaGLTF 1510
Cdd:cd18044 79 ------------ARL-----LESVLDHSLD-----------------------ALVAAQVVLATNTGAGSRQLLP-NELF 117
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19112847 1511 RTVIIDEAAQAVELSSIIPLKYGcESCVMVGDPNQLPPTVLSKTSAKFGYSQSLYVRMFKQHNESA-CLLSIQYR 1584
Cdd:cd18044 118 DVVVIDEAAQALEASCWIPLLKA-RRCILAGDHKQLPPTILSDKAARGGLGVTLFERLVNLYGESVvRMLTVQYR 191
|
|
| DEXXQc_DNA2 |
cd18041 |
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ... |
1270-1584 |
6.39e-24 |
|
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses different enzymatic activities, such as single-stranded DNA (ssDNA)-dependent ATPase, 5-3 helicase, and endonuclease activities, and is involved in DNA replication and DNA repair in the nucleus and mitochondrion. It is involved in Okazaki fragment processing by cleaving long flaps that escape FEN1: flaps that are longer than 27 nucleotides are coated by replication protein A complex (RPA), leading to recruit DNA2 which cleaves the flap until it is too short to bind RPA and becomes a substrate for FEN1. It is also involved in 5-end resection of DNA during double-strand break (DSB) repair; it is recruited by BLM and mediates the cleavage of 5-ssDNA, while the 3-ssDNA cleavage is prevented by the presence of RPA. DNA2 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: 350799 [Multi-domain] Cd Length: 203 Bit Score: 101.54 E-value: 6.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1270 GVNEPQAYAIYASSVNDGFTLIQGPPGTGKTKTILGMIGAVLtssSQGlqfnvpgqtrktskNKILICAPSNAAIDEILL 1349
Cdd:cd18041 1 GLNKDQRQAIKKVLNAKDYALILGMPGTGKTTTIAALVRILV---ALG--------------KSVLLTSYTHSAVDNILL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1350 RIKAGVYDhegikffpkVIRVGFGDSISVHAKEFTLEEqmikqmeltnlkkdqeannssdtrkkydsIIKKRDSLrEDLE 1429
Cdd:cd18041 64 KLKKFGVN---------FLRLGRLKKIHPDVQEFTLEA-----------------------------ILKSCKSV-EELE 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1430 KFrstgknssileaqlreitkqknmleqslddmrerqrstnrnldvlkkqiqnqlLQEADIVCATLSASGHELLLNAglT 1509
Cdd:cd18041 105 SK-----------------------------------------------------YESVSVVATTCLGINHPIFRRR--T 129
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19112847 1510 FRTVIIDEAAQAVELSSIIPLKYgCESCVMVGDPNQLPPTVLSKTSAKFGYSQSLYVRMFKQHNESACLLSIQYR 1584
Cdd:cd18041 130 FDYCIVDEASQITLPICLGPLRL-AKKFVLVGDHYQLPPLVKSREARELGMDESLFKRLSEAHPDAVVQLTIQYR 203
|
|
| DEXXc_HELZ2-C |
cd18040 |
C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ... |
1270-1584 |
7.28e-21 |
|
C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known as PPAR-alpha-interacting complex protein 285 or PRIC285 and PPAR-gamma DBD-interacting protein 1 or PDIP1) acts as a transcriptional coactivator for a number of nuclear receptors including PPARA, PPARG, THRA, THRB and RXRA. It 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: 350798 [Multi-domain] Cd Length: 271 Bit Score: 94.51 E-value: 7.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1270 GVNEPQAYAIyASSVNDGFTLIQGPPGTGKTKTILGMIGAVLTSSSQGLQFNVPGQtrktSKNKILICAPSNAAID---E 1346
Cdd:cd18040 1 KLNPSQNHAV-RTALTKPFTLIQGPPGTGKTVTGVHIAYWFAKQNREIQSVSGEGD----GGPCVLYCGPSNKSVDvvaE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1347 ILLRIKagvydheGIKffpkVIRVgfgdsisvhakeftleeqMIKQMELTnlkkdqeannssdtrkKYDSIIKKRDSLRE 1426
Cdd:cd18040 76 LLLKVP-------GLK----ILRV------------------YSEQIETT----------------EYPIPNEPRHPNKK 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1427 DLEKFRSTGKNSSILEAQLreITKQKNMLEQSLDDMRERQRSTNRNLDVlKKQIQN---------QLLQEADIVCATLSA 1497
Cdd:cd18040 111 SERESKPNSELSSITLHHR--IRQPSNPHSQQIKAFEARFERTQEKITE-EDIKTYkiliwearfEELETVDVILCTCSE 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1498 SGHELLLNAgLTFRTVIIDEAAQAVELSSIIPL--KYGCESCVMVGDPNQLPPTVLSKTSAKFGYSQSLyvrmFKQHNES 1575
Cdd:cd18040 188 AASQKMRTH-ANVKQCIVDECGMCTEPESLIPIvsAPRAEQVVLIGDHKQLRPVVQNKEAQKLGLGRSL----FERYAEK 262
|
....*....
gi 19112847 1576 ACLLSIQYR 1584
Cdd:cd18040 263 ACMLDTQYR 271
|
|
| DEXXQc_Helz-like |
cd18038 |
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ... |
1290-1571 |
7.28e-20 |
|
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and similar proteins. Helicase with zinc finger (HELZ) acts as a helicase that plays a role in RNA metabolism during development. Moloney leukemia virus 10-like protein 1 (Mov10L1) binds Piwi-interacting RNA (piRNA) precursors to initiate piRNA processing. All 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: 350796 [Multi-domain] Cd Length: 229 Bit Score: 90.37 E-value: 7.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1290 LIQGPPGTGKTKTILGMIGAVLtsssqglqfnvpgqtRKTSKNKILICAPSNAAIDEILLRIkagvydhegIKFFPkvir 1369
Cdd:cd18038 24 IIFGPPGTGKTVTLVEAILQVL---------------RQPPEARILVCAPSNSAADLLAERL---------LNALV---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1370 vgfgdsisvhakeftlEEQMIKQMeltnlkkdqeaNNSSDTRKKYDSiikkrdslredlekfrstgknssileaqlREIT 1449
Cdd:cd18038 76 ----------------TKREILRL-----------NAPSRDRASVPP-----------------------------ELLP 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1450 KQKNMLEQslddmrerqrstNRNLDVLKKqiqnqlLQEADIVCATLSASGHelLLNAGLT---FRTVIIDEAAQAVELSS 1526
Cdd:cd18038 100 YCNSKAEG------------TFRLPSLEE------LKKYRIVVCTLMTAGR--LVQAGVPnghFTHIFIDEAGQATEPEA 159
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 19112847 1527 IIPLKYGCE---SCVMVGDPNQLPPTVLSKTSAKFGYSQSLYVRMFKQ 1571
Cdd:cd18038 160 LIPLSELASkntQIVLAGDPKQLGPVVRSPLARKYGLGKSLLERLMER 207
|
|
| DEXXQc_Upf1-like |
cd17934 |
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ... |
1510-1584 |
7.94e-16 |
|
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, HELZ, Mov10L1, Aquarius, IGHMBP2 (SMUBP2), coronavirus Nsp13, and similar proteins. They belong 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: 438708 [Multi-domain] Cd Length: 121 Bit Score: 75.35 E-value: 7.94e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19112847 1510 FRTVIIDEAAQAVELSSIIPLKyGCESCVMVGDPNQLPPTVLSKTSAKFGYSQSLYVRMFKQH---NESACLLSIQYR 1584
Cdd:cd17934 45 VDVVIIDEASQITEPELLIALI-RAKKVVLVGDPKQLPPVVQEDHAALLGLSFILSLLLLFRLllpGSPKVMLDTQYR 121
|
|
| DEXXQc_Mov10L1 |
cd18078 |
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds ... |
1265-1603 |
1.22e-15 |
|
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds Piwi-interacting RNA (piRNA) precursors to initiate piRNA processing. Mov10L1 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: 350836 [Multi-domain] Cd Length: 230 Bit Score: 78.18 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1265 IMKsyGVNEPQAYAIYassvndgftliqGPPGTGKTKTIlgmIGAVLTsssqgLQFNVPgqtrktsKNKILICAPSNAAI 1344
Cdd:cd18078 13 ILG--GECRPLPYILF------------GPPGTGKTVTI---IEAILQ-----VVYNLP-------RSRILVCAPSNSAA 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1345 DEILLRIkagvydHEGikffpKVIRVGfgdsisvhakeftleeqmikqmeltnlkkdqeannssdtrkkydsiikkrdsl 1424
Cdd:cd18078 64 DLVTSRL------HES-----KVLKPG----------------------------------------------------- 79
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1425 reDLEKFRSTgknssileaqlreitkqkNMLEQSLDDMRerqrstnrnLDVLKKQIQNQLLQEADIVCATLSASGheLLL 1504
Cdd:cd18078 80 --DMVRLNAV------------------NRFESTVIDAR---------KLYCRLGEDLSKASRHRIVISTCSTAG--LLY 128
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1505 NAGL---TFRTVIIDEAAQAVELSSIIPL---KYGCESCVMVGDPNQLPPTVLSKTSAKFGYSQSLYVRMfkqhnesacL 1578
Cdd:cd18078 129 QMGLpvgHFTHVFVDEAGQATEPESLIPLgliSSRDGQIILAGDPMQLGPVIKSRLASAYGLGVSFLERL---------M 199
|
330 340
....*....|....*....|....*
gi 19112847 1579 LSIQYRMNPEisRFPSKFFYNSKLL 1603
Cdd:cd18078 200 NRPLYLRDPN--RFGESGGYNPLLV 222
|
|
| SF1_C |
cd18786 |
C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family ... |
1670-1753 |
1.23e-12 |
|
C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family members include UvrD/Rep, Pif1-like, and Upf-1-like proteins. Similar to SF2 helicases, they do not form toroidal, predominantly hexameric structures like SF3-6. SF1 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: 350173 [Multi-domain] Cd Length: 89 Bit Score: 65.15 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1670 KIGVVTPYRSQVQQLRSQFQRKYGSIIFKHLDIH-TVDGFQGQEKDIIIFSCVRSsmsggigFLQDLRRLNVALTRAKSS 1748
Cdd:cd18786 12 KGVVLTPYHRDRAYLNQYLQGLSLDEFDLQLVGAiTIDSSQGLTFDVVTLYLPTA-------NSLTPRRLYVALTRARKR 84
|
....*
gi 19112847 1749 LYIVG 1753
Cdd:cd18786 85 LVIYD 89
|
|
| CoV_Nsp13-helicase |
cd21718 |
helicase domain of coronavirus non-structural protein 13; This model represents the helicase ... |
1513-1767 |
3.72e-08 |
|
helicase domain of coronavirus non-structural protein 13; This model represents the helicase domain of non-structural protein 13 (Nsp13) from alpha-, beta-, gamma-, and deltacoronavirus, including pathogenic human viruses such as Severe acute respiratory syndrome coronavirus (SARS-CoV), SARS-CoV2 (also called 2019 novel CoV or 2019-nCoV), and Middle East respiratory syndrome-related (MERS) CoV. Helicases catalyze NTP-dependent unwinding of nucleic acid duplexes into single strands and are classified based on the arrangement of conserved motifs into six superfamilies. CoV Nsp13 is a member of the helicase superfamily 1 (SF1); SF1 and SF2 helicases do not form toroidal structures, while SF3-6 helicases do. Nsp13 is a component of the viral RNA synthesis replication and transcription complex (RTC). It is a multidomain protein containing a Cys/His rich zinc-binding domain (CH/ZBD), a stalk domain, a 1B domain involved in nucleic acid substrate binding, and a SF1 helicase core.
Pssm-ID: 409652 [Multi-domain] Cd Length: 341 Bit Score: 57.54 E-value: 3.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1513 VIIDEAAQAV--ELSSI-IPLKYgcESCVMVGDPNQLPP--TVLSKTSAKFGYSQSLYVRMfkQHNESACLLSIQYRMNP 1587
Cdd:cd21718 121 VVVDEVSMCTnyDLSVVnARLKY--KHIVYVGDPAQLPAprTLLTEGSLEPKDYNVVTRLM--VGSGPDVFLSKCYRCPK 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1588 EISRFPSKFFYNSKLldgpnmsavtsRPWHEDPQLGIYRFFNvhGTEAFSNSkSLYNVEEASFILLLYERliqcylNIDF 1667
Cdd:cd21718 197 EIVDTVSKLVYDNKL-----------KAIKPKSRQCFKTFGK--GDVRHDNG-SAINRPQLEFVKRFLDR------NPRW 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1668 EgKIGVVTPYRSQVQQLrsqfQRKYGsiifkhLDIHTVDGFQGQEKDIIIFsCVRSSMSGGIgflqDLRRLNVALTRAKS 1747
Cdd:cd21718 257 R-KAVFISPYNAMNNRA----SRLLG------LSTQTVDSSQGSEYDYVIF-CQTTDTAHAL----NINRFNVAITRAKH 320
|
250 260
....*....|....*....|
gi 19112847 1748 SLYIVGNSkplmQEDIFYSL 1767
Cdd:cd21718 321 GILVIMRD----ENDLYNAL 336
|
|
| EEXXQc_AQR |
cd17935 |
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds ... |
1484-1591 |
7.30e-08 |
|
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds precursor-mRNA introns at a defined position and is part of a pentameric intron-binding complex (IBC). 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: 350693 [Multi-domain] Cd Length: 207 Bit Score: 54.74 E-value: 7.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1484 LLQEADIV---CATLSASGHELLlNAGLTFRTVIIDEAAQAVELSSIIPLKY--------GCESCVMVGDPNQLPPTVLS 1552
Cdd:cd17935 83 LGHGAKIIamtCTHAALKRGELV-ELGFKYDNILMEEAAQILEIETFIPLLLqnpedgpnRLKRLIMIGDHHQLPPVIKN 161
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 19112847 1553 KTSAKFGYS-QSLYVRmFKQHNESACLLSIQYRMNPEISR 1591
Cdd:cd17935 162 MAFQKYSNMeQSLFTR-LVRLGVPTVDLDAQGRARASISS 200
|
|
| EEXXEc_NFX1 |
cd17936 |
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ... |
1469-1583 |
8.19e-08 |
|
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that represses class II MHC (major histocompatibility complex) gene expression. NFX1 binds a conserved cis-acting element, termed the X-box, in promoters of human class II MHC genes. The Cys-rich region contains several NFX1-type zinc finger domains. Frequently, a R3H domain is present in the C-terminus, and a RING finger domain and a PAM2 motif are present in the N-terminus. The lack of R3H and PAM2 motifs in the plant proteins indicates functional differences. Plant NFX1-like proteins are proposed to modulate growth and survival by coordinating reactive oxygen species, salicylic acid, further biotic stress and abscisic acid responses. A common feature of all members may be E3 ubiquitin ligase, due to the presence of a RING finger domain, as well as DNA binding. NFX1 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: 350694 [Multi-domain] Cd Length: 178 Bit Score: 54.09 E-value: 8.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1469 TNRNLD-----VLKKQIQNQLLQEADIVCATLS--ASGHELLlnAGLTFRTVIIDEAAQAVE---LSSIIPlkyGCESCV 1538
Cdd:cd17936 58 TNHALDqflegLLDFGPTKIVRLGARVIGMTTTgaAKYRELL--QALGPKVVIVEEAAEVLEahiLAALTP---STEHLI 132
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 19112847 1539 MVGDPNQLPPTV--LSKTSAKFGYSQSLYVRMFKQHNESAClLSIQY 1583
Cdd:cd17936 133 LIGDHKQLRPKVnvYELTAKKYNLDVSLFERLVKNGLPFVT-LNVQR 178
|
|
| DEXXQc_HELZ |
cd18077 |
DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that ... |
1485-1584 |
2.99e-07 |
|
DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that plays a role in RNA metabolism during development. HELZ is a member of the family I class of RNA helicases 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: 350835 [Multi-domain] Cd Length: 226 Bit Score: 53.26 E-value: 2.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1485 LQEADIVCATLSASGH--ELLLNAGlTFRTVIIDEAAQAVELSSIIPLKYGCESC--VMVGDPNQLPPTVLSKTSAKFGY 1560
Cdd:cd18077 121 VMRHRVVVVTLSTSQYlcQLDLEPG-FFTHILLDEAAQAMECEAIMPLALATKSTriVLAGDHMQLSPEVYSEFARERNL 199
|
90 100
....*....|....*....|....*..
gi 19112847 1561 SQSLYVRMFKQH-NESAC--LLSIQYR 1584
Cdd:cd18077 200 HISLLERLYEHYpSEHPCriLLCENYR 226
|
|
| deltaCoV_Nsp13-helicase |
cd21721 |
helicase domain of deltacoronavirus non-structural protein 13; This model represents the ... |
1513-1752 |
5.87e-07 |
|
helicase domain of deltacoronavirus non-structural protein 13; This model represents the helicase domain of non-structural protein 13 (Nsp13) from deltacoronavirus, including Bulbul coronavirus (CoV) HKU11 and Common moorhen CoV HKU21. Helicases catalyze NTP-dependent unwinding of nucleic acid duplexes into single strands and are classified based on the arrangement of conserved motifs into six superfamilies. CoV Nsp13 is a member of the helicase superfamily 1 (SF1); SF1 and SF2 helicases do not form toroidal structures, while SF3-6 helicases do. Nsp13 is a component of the viral RNA synthesis replication and transcription complex (RTC). It is a multidomain protein containing a Cys/His rich zinc-binding domain (CH/ZBD), a stalk domain, a 1B domain involved in nucleic acid substrate binding, and a SF1 helicase core.
Pssm-ID: 409654 [Multi-domain] Cd Length: 342 Bit Score: 53.77 E-value: 5.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1513 VIIDEAAQAV--ELSSI-IPLKYgcESCVMVGDPNQLPPTVLSKTSAKFGYSQSLYVRMFKQHNESACLLSIQYRMNPEI 1589
Cdd:cd21721 121 VVVDEVSMLTnyELSSVnARLVY--NHIVYVGDPYQLPSPRTMLTTGQLSPADYNVVTDIMVHAGADVMLDMCYRCPREI 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1590 SRFPSKFFYNSKLLdgpnmsavTSRPwhedPQLGIYRFFNVHGTEAFS-NSKSLYNVEEASFILLLyeRLIQCYLNIDFe 1668
Cdd:cd21721 199 VDTVSKLVYDNKLK--------AAKP----NSRQCYKTIINNGNNDIAhEGQSAYNEPQLRFALAF--RQYKRWDNVTF- 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1669 gkigvVTPYRS-QVQQLRSQFQRKygsiifkhldihTVDGFQGQEKDIIIFsCVRSSMsggiGFLQDLRRLNVALTRAKS 1747
Cdd:cd21721 264 -----ISPYNAmNVKAAMAGFSTQ------------TVDSSQGSEYDYVIF-CVTTDS----AHALNMSRLNVALTRAKI 321
|
....*
gi 19112847 1748 SLYIV 1752
Cdd:cd21721 322 GILVV 326
|
|
| DEXXQc_SF1 |
cd18043 |
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are ... |
1272-1311 |
2.46e-06 |
|
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are nucleic acid motor proteins that couple ATP hydrolysis to translocation along with the concomitant unwinding of DNA or RNA. This is central to many aspects of cellular DNA and RNA metabolism and accordingly, they are implicated in a wide range of nucleic acid processing events including DNA replication, recombination, and repair as well as many aspects of RNA metabolism. Superfamily 1 helicases 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: 350801 [Multi-domain] Cd Length: 127 Bit Score: 48.35 E-value: 2.46e-06
10 20 30 40
....*....|....*....|....*....|....*....|
gi 19112847 1272 NEPQAYAIYaSSVNDGFTLIQGPPGTGKTKTILGMIGAVL 1311
Cdd:cd18043 1 DSSQEAAII-SARNGKNVVIQGPPGTGKSQTIANIIANAL 39
|
|
| DExxQc_SF1-N |
cd17914 |
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ... |
1506-1583 |
2.67e-06 |
|
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members include UvrD/Rep, Pif1-like, and Upf-1-like proteins. Like SF2, they do not form toroidal, predominantly hexameric structures like SF3-6. 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. SF1 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: 438706 [Multi-domain] Cd Length: 121 Bit Score: 48.25 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1506 AGLTFRTVIIDEAAQA--VELSSIIPLKYGCESCVMVGDPNQLPPTVLSKTSAKFGYSQSLYVRmFKQHNESACLLSIQY 1583
Cdd:cd17914 43 AAAQLDNILVDEAAQIlePETSRLIDLALDQGRVILVGDHDQLGPVWRGAVLAKICNEQSLFTR-LVRLGVSLIRLQVQY 121
|
|
| EEXXEc_NFX1 |
cd17936 |
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ... |
1270-1372 |
2.83e-06 |
|
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that represses class II MHC (major histocompatibility complex) gene expression. NFX1 binds a conserved cis-acting element, termed the X-box, in promoters of human class II MHC genes. The Cys-rich region contains several NFX1-type zinc finger domains. Frequently, a R3H domain is present in the C-terminus, and a RING finger domain and a PAM2 motif are present in the N-terminus. The lack of R3H and PAM2 motifs in the plant proteins indicates functional differences. Plant NFX1-like proteins are proposed to modulate growth and survival by coordinating reactive oxygen species, salicylic acid, further biotic stress and abscisic acid responses. A common feature of all members may be E3 ubiquitin ligase, due to the presence of a RING finger domain, as well as DNA binding. NFX1 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: 350694 [Multi-domain] Cd Length: 178 Bit Score: 49.46 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1270 GVNEPQAYAIYASSVNDgFTLIQGPPGTGKTktilgMIGAVLTsssQGLQFNvpgqTRKTSKNKILICAPSNAAIDEILL 1349
Cdd:cd17936 1 TLDPSQLEALKHALTSE-LALIQGPPGTGKT-----FLGVKLV---RALLQN----QDLSITGPILVVCYTNHALDQFLE 67
|
90 100
....*....|....*....|....
gi 19112847 1350 RIkagvydhegIKFFP-KVIRVGF 1372
Cdd:cd17936 68 GL---------LDFGPtKIVRLGA 82
|
|
| DEXXQc_SF1 |
cd18043 |
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are ... |
1473-1551 |
3.47e-05 |
|
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are nucleic acid motor proteins that couple ATP hydrolysis to translocation along with the concomitant unwinding of DNA or RNA. This is central to many aspects of cellular DNA and RNA metabolism and accordingly, they are implicated in a wide range of nucleic acid processing events including DNA replication, recombination, and repair as well as many aspects of RNA metabolism. Superfamily 1 helicases 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: 350801 [Multi-domain] Cd Length: 127 Bit Score: 45.27 E-value: 3.47e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19112847 1473 LDVLKKQIqnqllqeadIVCATLSASgHELLLNAGLtFRTVIIDEAAQaVELSSIIPLKYGCESCVMVGDPNQLPPTVL 1551
Cdd:cd18043 55 LDVVRFPC---------WIMSPLSVS-QYLPLNRNL-FDLVIFDEASQ-IPIEEALPALFRGKQVVVVGDDKQLPPSIL 121
|
|
| DExxQc_SF1-N |
cd17914 |
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ... |
1289-1346 |
6.30e-05 |
|
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members include UvrD/Rep, Pif1-like, and Upf-1-like proteins. Like SF2, they do not form toroidal, predominantly hexameric structures like SF3-6. 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. SF1 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: 438706 [Multi-domain] Cd Length: 121 Bit Score: 44.40 E-value: 6.30e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 19112847 1289 TLIQGPPGTGKTKTILGMIGAVLtsssqglqfnvpgQTRKTSKNKILICAPSNAAIDE 1346
Cdd:cd17914 2 SLIQGPPGTGKTRVLVKIVAALM-------------QNKNGEPGRILLVTPTNKAAAQ 46
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
1385-1487 |
1.24e-04 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 43.83 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1385 LEEQMiKQMELTNLKKDQEANnssdtrkkydSIIKKRDSLREDLEKfrstgknssiLEAQLREitkQKNMLEQSlddmrE 1464
Cdd:pfam12718 19 LEEKV-KELEQENLEKEQEIK----------SLTHKNQQLEEEVEK----------LEEQLKE---AKEKAEES-----E 69
|
90 100
....*....|....*....|...
gi 19112847 1465 RQRSTNRNLdvlkkQIQNQLLQE 1487
Cdd:pfam12718 70 KLKTNNENL-----TRKIQLLEE 87
|
|
| recD |
TIGR01447 |
exodeoxyribonuclease V, alpha subunit; This family describes the exodeoxyribonuclease V alpha ... |
1177-1343 |
3.94e-04 |
|
exodeoxyribonuclease V, alpha subunit; This family describes the exodeoxyribonuclease V alpha subunit, RecD. RecD is part of a RecBCD complex. A related family in the Gram-positive bacteria separates in a phylogenetic tree, has an additional N-terminal extension of about 200 residues, and is not supported as a member of a RecBCD complex by neighboring genes. The related family is consequently described by a different model. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273631 [Multi-domain] Cd Length: 582 Bit Score: 45.52 E-value: 3.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1177 SFQLCKIQsISRKKESLELCLRMNIESIDLQEYAPNIRFTAQKLFNATTSLREFAALKSLRHLPLSQRILDANVTRLPSN 1256
Cdd:TIGR01447 49 CLDLEKAA-KSPGLTGISEPDLGEKLNFDWLAALPASVLVGLPGETAPPLVLCDGRLYLRRYWREEEKLAAKLRTLLEAR 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1257 FTDDKKQKIMKSYGVNEPQAYAIYASSV--NDGFTLIQGPPGTGKTKTILGMIGAVLTsssqglqfnvpgQTRKTSKNKI 1334
Cdd:TIGR01447 128 KRTAPSAILENLFPLLNEQNWRKTAVALalKSNFSLITGGPGTGKTTTVARLLLALVK------------QSPKQGKLRI 195
|
....*....
gi 19112847 1335 LICAPSNAA 1343
Cdd:TIGR01447 196 ALAAPTGKA 204
|
|
| gammaCoV_Nsp13-helicase |
cd21720 |
helicase domain of gammacoronavirus non-structural protein 13; This model represents the ... |
1674-1766 |
5.46e-04 |
|
helicase domain of gammacoronavirus non-structural protein 13; This model represents the helicase domain of non-structural protein 13 (Nsp13) from gammacoronavirus, including Avian infectious bronchitis virus. Helicases catalyze NTP-dependent unwinding of nucleic acid duplexes into single strands and are classified based on the arrangement of conserved motifs into six superfamilies. Coronavirus (CoV) Nsp13 is a member of the helicase superfamily 1 (SF1); SF1 and SF2 helicases do not form toroidal structures, while SF3-6 helicases do. Nsp13 is a component of the viral RNA synthesis replication and transcription complex (RTC). It is a multidomain protein containing a Cys/His rich zinc-binding domain (CH/ZBD), a stalk domain, a 1B domain involved in nucleic acid substrate binding, and a SF1 helicase core.
Pssm-ID: 409653 [Multi-domain] Cd Length: 343 Bit Score: 44.52 E-value: 5.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1674 VTPYRSQVQQLRsqfqRKYGsiifkhLDIHTVDGFQGQEKDIIIFsCVRSSMSGGIgflqDLRRLNVALTRAKSSLYIVg 1753
Cdd:cd21720 264 ISPYNAMNQRAY----RMLG------LNVQTVDSSQGSEYDYVIF-CVTADSQHAL----NINRFNVALTRAKRGILVV- 327
|
90
....*....|...
gi 19112847 1754 nskpLMQEDIFYS 1766
Cdd:cd21720 328 ----MRQRDELYS 336
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1391-1484 |
8.57e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 8.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1391 KQMELTNLKKDQEAnnssdTRKKYDSIIKKRDSLREDLEKFRstgKNSSILEAQLREITKQKNMLEQSLDDMRERQRSTN 1470
Cdd:COG4942 25 AEAELEQLQQEIAE-----LEKELAALKKEEKALLKQLAALE---RRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90
....*....|....
gi 19112847 1471 RNLDVLKKQIQNQL 1484
Cdd:COG4942 97 AELEAQKEELAELL 110
|
|
| DEXSc_RecD-like |
cd17933 |
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ... |
1275-1343 |
2.98e-03 |
|
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD 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: 350691 [Multi-domain] Cd Length: 155 Bit Score: 40.23 E-value: 2.98e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19112847 1275 QAYAIYASsVNDGFTLIQGPPGTGKTKTILGMIGAvltsssqglqFNVPGQtrktsknKILICAPSNAA 1343
Cdd:cd17933 2 QKAAVRLV-LRNRVSVLTGGAGTGKTTTLKALLAA----------LEAEGK-------RVVLAAPTGKA 52
|
|
| RecD |
COG0507 |
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
1231-1343 |
3.33e-03 |
|
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];
Pssm-ID: 440273 [Multi-domain] Cd Length: 514 Bit Score: 42.27 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1231 AALKSLRHLPLSQRILDANVTRL--PSNFTDDKKQKImksygvnepqayAIYASSVNDGFTLIQGPPGTGKTkTILGMIG 1308
Cdd:COG0507 95 RRLRRLARPALDEADVEAALAALepRAGITLSDEQRE------------AVALALTTRRVSVLTGGAGTGKT-TTLRALL 161
|
90 100 110
....*....|....*....|....*....|....*
gi 19112847 1309 AVLtsSSQGLqfnvpgqtrktsknKILICAPSNAA 1343
Cdd:COG0507 162 AAL--EALGL--------------RVALAAPTGKA 180
|
|
| DEXXQc_HELZ2-N |
cd18076 |
N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ... |
1491-1585 |
3.43e-03 |
|
N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known as PPAR-alpha-interacting complex protein 285 or PRIC285 and PPAR-gamma DBD-interacting protein 1 or PDIP1) acts as a transcriptional coactivator for a number of nuclear receptors including PPARA, PPARG, THRA, THRB, and RXRA. It 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: 350834 [Multi-domain] Cd Length: 230 Bit Score: 41.03 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112847 1491 VCATLSASGHELLLNAGLtFRTVIIDEAAQAVELSSIIPLKYGCESC--VMVGDPNQLPPTVLSKTSAKFGYsQSLYVRM 1568
Cdd:cd18076 129 IVITTTAMAFNLHVLSGF-FTHIFIDEAAQMLECEALIPLSYAGPKTrvVLAGDHMQMTPKLFSVADYNRAN-HTLLNRL 206
|
90
....*....|....*..
gi 19112847 1569 FKQHNESACLLSIQYRM 1585
Cdd:cd18076 207 FHYYQGEKHEVAVKSRV 223
|
|
| |
