|
Name |
Accession |
Description |
Interval |
E-value |
| DEXXQc_Mov10L1 |
cd18078 |
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds ... |
218-447 |
1.35e-161 |
|
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: 465.31 E-value: 1.35e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 218 VLNENQKLAVKRILSGDCRPLPYILFGPPGTGKTVTIIEAVLQVHFALPDSRILVCAPSNSAADLVCLRLHESKVLQPAT 297
Cdd:cd18078 1 DLNELQKEAVKRILGGECRPLPYILFGPPGTGKTVTIIEAILQVVYNLPRSRILVCAPSNSAADLVTSRLHESKVLKPGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 298 MVRVNATCRFEEIVIDAVKPYCRDGEDIWKASRFRIIITTCSSSGLFYQIGVRVGHFTHVFVDEAGQASEPECLIPLGLM 377
Cdd:cd18078 81 MVRLNAVNRFESTVIDARKLYCRLGEDLSKASRHRIVISTCSTAGLLYQMGLPVGHFTHVFVDEAGQATEPESLIPLGLI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 378 SDISGQIVLAGDPMQLGPVIKSRLAMAYGLNVSFLERLMSRPAYQRDENAFGACGAHNPLLVTKLVKNYR 447
Cdd:cd18078 161 SSRDGQIILAGDPMQLGPVIKSRLASAYGLGVSFLERLMNRPLYLRDPNRFGESGGYNPLLVTKLVDNYR 230
|
|
| SF1_C_Upf1 |
cd18808 |
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ... |
448-683 |
4.92e-55 |
|
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: 186.67 E-value: 4.92e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 448 SHEALLMLPSRLFYHRELEVCADptvVTSLLGWEKLPKKGFPLIFHGVRGSEAREGKSPSWFNPAEAVQVLRYCCLLahs 527
Cdd:cd18808 1 MHPEISEFPSKLFYEGKLKAGVS---VAARLNPPPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYL--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 528 ISSQVSASDIGVITPYRKQwlwssggdtgashaehqvsfmkhvslwcshhqaelgknpqnteekVEKIRILLRNV--DLM 605
Cdd:cd18808 75 LKSGVKPSSIGVITPYRAQ---------------------------------------------VALIRELLRKRggLLE 109
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034629103 606 DIKVGSVEEFQGQEYLVIIISTVRSNEDRFEddryfLGFLSNSKRFNVAITRPKALLIVLGNPHVLVRDPCFGALLEY 683
Cdd:cd18808 110 DVEVGTVDNFQGREKDVIILSLVRSNESGGS-----IGFLSDPRRLNVALTRAKRGLIIVGNPDTLSKDPLWKKLLEY 182
|
|
| DNA2 |
COG1112 |
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair]; |
328-683 |
3.44e-52 |
|
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
Pssm-ID: 440729 [Multi-domain] Cd Length: 819 Bit Score: 194.58 E-value: 3.44e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 328 ASRFRIIITTCSSSGLFyqIGVRVGHFTHVFVDEAGQASEPECLIPLGLmsdiSGQIVLAGDPMQLGPviksrlamaygl 407
Cdd:COG1112 532 LELAPVVGMTPASVARL--LPLGEGSFDLVIIDEASQATLAEALGALAR----AKRVVLVGDPKQLPP------------ 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 408 nVSFLERLMSRPAYQRDENAFGACGAHNPLLVTKLVKNYRSHEALLMLPSRLFYHRELEVCADPTVvtsllgwEKLPKKG 487
Cdd:COG1112 594 -VVFGEEAEEVAEEGLDESLLDRLLARLPERGVMLREHYRMHPEIIAFSNRLFYDGKLVPLPSPKA-------RRLADPD 665
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 488 FPLIFHGVRGSEAREGKspSWFNPAEAVQVLRyccLLAHSISSQVSASDIGVITPYRKQwlwssggdtgashaehqvsfm 567
Cdd:COG1112 666 SPLVFIDVDGVYERRGG--SRTNPEEAEAVVE---LVRELLEDGPDGESIGVITPYRAQ--------------------- 719
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 568 khvslwcshhqaelgknpqnteekVEKIRILLRN---VDLMDIKVGSVEEFQGQEYLVIIISTVRSNEdrfEDDRYFLGF 644
Cdd:COG1112 720 ------------------------VALIRELLREalgDGLEPVFVGTVDRFQGDERDVIIFSLVYSND---EDVPRNFGF 772
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1034629103 645 LSNS-KRFNVAITRPKALLIVLGNPHVLVRDP---CFGALLEY 683
Cdd:COG1112 773 LNGGpRRLNVAVSRARRKLIVVGSRELLDSDPstpALKRLLEY 815
|
|
| TIGR00376 |
TIGR00376 |
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ... |
211-690 |
8.42e-52 |
|
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: 190.80 E-value: 8.42e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 211 KMEFFNPVLNENQKLAVKRILSGDCRplpYILFGPPGTGKTVTIIEAVLQVhfALPDSRILVCAPSNSAAD--------- 281
Cdd:TIGR00376 150 DFQFFDPNLNESQKEAVLFALSSKDL---FLIHGPPGTGKTRTVVELIRQL--VKRGLRVLVTAPSNIAVDnllerlalc 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 282 -LVCLRL-HESKVLQ-------PATMVRVNATCRFEEIV--IDAV----------KPYCRDG------------------ 322
Cdd:TIGR00376 225 dQKIVRLgHPARLLKsnkqhslDYLIENHPKYQIVADIRekIDELieernkktkpSPQKRRGlsdikilrkalkkrearg 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 323 -EDIWKASRFRIIITTCSSSGLF---YQIGVRVGH----------------------FTHVFVDEAGQASEPECLIPLgl 376
Cdd:TIGR00376 305 iESLKIASMAEWIETNKSIDRLLkllPESEERIMNeilaesdatnsmagseilngqyFDVAVIDEASQAMEPSCLIPL-- 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 377 msdISGQ-IVLAGDPMQLGPVIKSRlaMAYGLNVSFLERLMSRpayqrdenafgacgahNPLLVTKLVKNYRSHEALLML 455
Cdd:TIGR00376 383 ---LKARkLILAGDHKQLPPTILSH--DAEELSLTLFERLIKE----------------YPERSRTLNVQYRMNQKIMEF 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 456 PSRLFYHRELEvcADPTVVTSLLgwEKLPKK-----------GFPLIF---HGVRGSEAREGKSPSWFNPAEAVQVLRYC 521
Cdd:TIGR00376 442 PSREFYNGKLT--AHESVANILL--RDLPKVeateseddletGIPLLFidtSGCELFELKEADSTSKYNPGEAELVSEII 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 522 CLLahsISSQVSASDIGVITPYrkqwlwssggdtgashaEHQVSFMKhvslwcshhqaelgknpQNTEEKvekirillrn 601
Cdd:TIGR00376 518 QAL---VKMGVPANDIGVITPY-----------------DAQVDLLR-----------------QLLEHR---------- 550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 602 vdLMDIKVGSVEEFQGQEYLVIIISTVRSNEDRfeddryFLGFLSNSKRFNVAITRPKALLIVLGNPHVLVRDPCFGALL 681
Cdd:TIGR00376 551 --HIDIEVSSVDGFQGREKEVIIISFVRSNRKG------EVGFLKDLRRLNVALTRARRKLIVIGDSRTLSNHKFYKRLI 622
|
....*....
gi 1034629103 682 EYSITNGVY 690
Cdd:TIGR00376 623 EWCKQHGEV 631
|
|
| AAA_12 |
pfam13087 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
407-668 |
6.19e-48 |
|
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: 167.73 E-value: 6.19e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 407 LNVSFLERLMSrpayqrdenafgacgaHNPLLVTKLVKNYRSHEALLMLPSRLFYHRELEvCADPTVVTSLLGWEKLPKK 486
Cdd:pfam13087 1 LDRSLFERLQE----------------LGPSAVVMLDTQYRMHPEIMEFPSKLFYGGKLK-DGPSVAERPLPDDFHLPDP 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 487 GFPLIFHGVRGSEAREGKS-PSWFNPAEAVQVLRYCCLLAHSISSQvsASDIGVITPYRKQwlwssggdtgashaehqvs 565
Cdd:pfam13087 64 LGPLVFIDVDGSEEEESDGgTSYSNEAEAELVVQLVEKLIKSGPEE--PSDIGVITPYRAQ------------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 566 fmkhvslwcshhqaelgknpqnteekVEKIRILLRNVDLM--DIKVGSVEEFQGQEYLVIIISTVRSNEDRfeddryFLG 643
Cdd:pfam13087 123 --------------------------VRLIRKLLKRKLGGklEIEVNTVDGFQGREKDVIIFSCVRSNEKG------GIG 170
|
250 260
....*....|....*....|....*
gi 1034629103 644 FLSNSKRFNVAITRPKALLIVLGNP 668
Cdd:pfam13087 171 FLSDPRRLNVALTRAKRGLIIVGNA 195
|
|
| AAA_11 |
pfam13086 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
223-400 |
2.14e-24 |
|
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: 102.81 E-value: 2.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 223 QKLAVKRILSgdcRPLPYILFGPPGTGKTVTIIEAVLQVHF-----ALPDSRILVCAPSNSAADLVCLRLHESKVLQPAT 297
Cdd:pfam13086 2 QREAIRSALS---SSHFTLIQGPPGTGKTTTIVELIRQLLSypatsAAAGPRILVCAPSNAAVDNILERLLRKGQKYGPK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 298 MVRVNAtcrfEEIVIDAVKPYCRD-------------------------------------------------------- 321
Cdd:pfam13086 79 IVRIGH----PAAISEAVLPVSLDylvesklnneedaqivkdiskeleklakalrafekeiivekllksrnkdkskleqe 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 322 -----------GEDIWKASRF---------RIIITTCSSSG---LFYQIGVRVghfthVFVDEAGQASEPECLIPLglms 378
Cdd:pfam13086 155 rrklrserkelRKELRRREQSlereildeaQIVCSTLSGAGsrlLSSLANFDV-----VIIDEAAQALEPSTLIPL---- 225
|
250 260
....*....|....*....|....
gi 1034629103 379 dISG--QIVLAGDPMQLGPVIKSR 400
Cdd:pfam13086 226 -LRGpkKVVLVGDPKQLPPTVISK 248
|
|
| RecD |
COG0507 |
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
202-396 |
2.24e-10 |
|
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: 63.84 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 202 DEIQTPKARKMEFFNPVLNENQKLAVKRILSGdcRPLpYILFGPPGTGKTvTIIEAVLQVHFALPDsRILVCAPSNSAAd 281
Cdd:COG0507 108 ADVEAALAALEPRAGITLSDEQREAVALALTT--RRV-SVLTGGAGTGKT-TTLRALLAALEALGL-RVALAAPTGKAA- 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 282 lvcLRLHESKVLQPATMvrvnatCRFEEIVIDAVKPYCRDGEDIWKAsrfRIIIttcsssglfyqigvrvghfthvfVDE 361
Cdd:COG0507 182 ---KRLSESTGIEARTI------HRLLGLRPDSGRFRHNRDNPLTPA---DLLV-----------------------VDE 226
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1034629103 362 AGqasepecLIPLGLMSDI-------SGQIVLAGDPMQLGPV 396
Cdd:COG0507 227 AS-------MVDTRLMAALlealpraGARLILVGDPDQLPSV 261
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
213-362 |
5.36e-09 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 56.73 E-value: 5.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 213 EFFNPVLNENQKLAVKRILSGDCRplpYILFGPPGTGKTVTIIEAVLQVHFALPDSRILVCAPSNSAADLVCLRLheSKV 292
Cdd:smart00487 3 KFGFEPLRPYQKEAIEALLSGLRD---VILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEEL--KKL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034629103 293 LQPATMVRVNATCRFEEividavkpycRDGEDIWKASRFRIIITTCSS-SGLFYQIGVRVGHFTHVFVDEA 362
Cdd:smart00487 78 GPSLGLKVVGLYGGDSK----------REQLRKLESGKTDILVTTPGRlLDLLENDKLSLSNVDLVILDEA 138
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DEXXQc_Mov10L1 |
cd18078 |
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds ... |
218-447 |
1.35e-161 |
|
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: 465.31 E-value: 1.35e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 218 VLNENQKLAVKRILSGDCRPLPYILFGPPGTGKTVTIIEAVLQVHFALPDSRILVCAPSNSAADLVCLRLHESKVLQPAT 297
Cdd:cd18078 1 DLNELQKEAVKRILGGECRPLPYILFGPPGTGKTVTIIEAILQVVYNLPRSRILVCAPSNSAADLVTSRLHESKVLKPGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 298 MVRVNATCRFEEIVIDAVKPYCRDGEDIWKASRFRIIITTCSSSGLFYQIGVRVGHFTHVFVDEAGQASEPECLIPLGLM 377
Cdd:cd18078 81 MVRLNAVNRFESTVIDARKLYCRLGEDLSKASRHRIVISTCSTAGLLYQMGLPVGHFTHVFVDEAGQATEPESLIPLGLI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 378 SDISGQIVLAGDPMQLGPVIKSRLAMAYGLNVSFLERLMSRPAYQRDENAFGACGAHNPLLVTKLVKNYR 447
Cdd:cd18078 161 SSRDGQIILAGDPMQLGPVIKSRLASAYGLGVSFLERLMNRPLYLRDPNRFGESGGYNPLLVTKLVDNYR 230
|
|
| DEXXQc_Helz-like |
cd18038 |
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ... |
218-447 |
2.55e-116 |
|
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: 349.23 E-value: 2.55e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 218 VLNENQKLAVKRILSGDCRPLPYILFGPPGTGKTVTIIEAVLQVHFALPDSRILVCAPSNSAADLVCLRLHeSKVLQPAT 297
Cdd:cd18038 1 ELNDEQKLAVRNIVTGTSRPPPYIIFGPPGTGKTVTLVEAILQVLRQPPEARILVCAPSNSAADLLAERLL-NALVTKRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 298 MVRVNATCRFEEIVIDAVKPYCRDGED-------IWKASRFRIIITTCSSSGLFYQIGVRVGHFTHVFVDEAGQASEPEC 370
Cdd:cd18038 80 ILRLNAPSRDRASVPPELLPYCNSKAEgtfrlpsLEELKKYRIVVCTLMTAGRLVQAGVPNGHFTHIFIDEAGQATEPEA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034629103 371 LIPLGLMSDISGQIVLAGDPMQLGPVIKSRLAMAYGLNVSFLERLMSRPAYQRDenafgacGAHNPLLVTKLVKNYR 447
Cdd:cd18038 160 LIPLSELASKNTQIVLAGDPKQLGPVVRSPLARKYGLGKSLLERLMERPLYYKD-------GEYNPSYITKLLKNYR 229
|
|
| SF1_C_Upf1 |
cd18808 |
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ... |
448-683 |
4.92e-55 |
|
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: 186.67 E-value: 4.92e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 448 SHEALLMLPSRLFYHRELEVCADptvVTSLLGWEKLPKKGFPLIFHGVRGSEAREGKSPSWFNPAEAVQVLRYCCLLahs 527
Cdd:cd18808 1 MHPEISEFPSKLFYEGKLKAGVS---VAARLNPPPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYL--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 528 ISSQVSASDIGVITPYRKQwlwssggdtgashaehqvsfmkhvslwcshhqaelgknpqnteekVEKIRILLRNV--DLM 605
Cdd:cd18808 75 LKSGVKPSSIGVITPYRAQ---------------------------------------------VALIRELLRKRggLLE 109
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034629103 606 DIKVGSVEEFQGQEYLVIIISTVRSNEDRFEddryfLGFLSNSKRFNVAITRPKALLIVLGNPHVLVRDPCFGALLEY 683
Cdd:cd18808 110 DVEVGTVDNFQGREKDVIILSLVRSNESGGS-----IGFLSDPRRLNVALTRAKRGLIIVGNPDTLSKDPLWKKLLEY 182
|
|
| DNA2 |
COG1112 |
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair]; |
328-683 |
3.44e-52 |
|
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
Pssm-ID: 440729 [Multi-domain] Cd Length: 819 Bit Score: 194.58 E-value: 3.44e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 328 ASRFRIIITTCSSSGLFyqIGVRVGHFTHVFVDEAGQASEPECLIPLGLmsdiSGQIVLAGDPMQLGPviksrlamaygl 407
Cdd:COG1112 532 LELAPVVGMTPASVARL--LPLGEGSFDLVIIDEASQATLAEALGALAR----AKRVVLVGDPKQLPP------------ 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 408 nVSFLERLMSRPAYQRDENAFGACGAHNPLLVTKLVKNYRSHEALLMLPSRLFYHRELEVCADPTVvtsllgwEKLPKKG 487
Cdd:COG1112 594 -VVFGEEAEEVAEEGLDESLLDRLLARLPERGVMLREHYRMHPEIIAFSNRLFYDGKLVPLPSPKA-------RRLADPD 665
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 488 FPLIFHGVRGSEAREGKspSWFNPAEAVQVLRyccLLAHSISSQVSASDIGVITPYRKQwlwssggdtgashaehqvsfm 567
Cdd:COG1112 666 SPLVFIDVDGVYERRGG--SRTNPEEAEAVVE---LVRELLEDGPDGESIGVITPYRAQ--------------------- 719
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 568 khvslwcshhqaelgknpqnteekVEKIRILLRN---VDLMDIKVGSVEEFQGQEYLVIIISTVRSNEdrfEDDRYFLGF 644
Cdd:COG1112 720 ------------------------VALIRELLREalgDGLEPVFVGTVDRFQGDERDVIIFSLVYSND---EDVPRNFGF 772
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1034629103 645 LSNS-KRFNVAITRPKALLIVLGNPHVLVRDP---CFGALLEY 683
Cdd:COG1112 773 LNGGpRRLNVAVSRARRKLIVVGSRELLDSDPstpALKRLLEY 815
|
|
| TIGR00376 |
TIGR00376 |
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ... |
211-690 |
8.42e-52 |
|
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: 190.80 E-value: 8.42e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 211 KMEFFNPVLNENQKLAVKRILSGDCRplpYILFGPPGTGKTVTIIEAVLQVhfALPDSRILVCAPSNSAAD--------- 281
Cdd:TIGR00376 150 DFQFFDPNLNESQKEAVLFALSSKDL---FLIHGPPGTGKTRTVVELIRQL--VKRGLRVLVTAPSNIAVDnllerlalc 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 282 -LVCLRL-HESKVLQ-------PATMVRVNATCRFEEIV--IDAV----------KPYCRDG------------------ 322
Cdd:TIGR00376 225 dQKIVRLgHPARLLKsnkqhslDYLIENHPKYQIVADIRekIDELieernkktkpSPQKRRGlsdikilrkalkkrearg 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 323 -EDIWKASRFRIIITTCSSSGLF---YQIGVRVGH----------------------FTHVFVDEAGQASEPECLIPLgl 376
Cdd:TIGR00376 305 iESLKIASMAEWIETNKSIDRLLkllPESEERIMNeilaesdatnsmagseilngqyFDVAVIDEASQAMEPSCLIPL-- 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 377 msdISGQ-IVLAGDPMQLGPVIKSRlaMAYGLNVSFLERLMSRpayqrdenafgacgahNPLLVTKLVKNYRSHEALLML 455
Cdd:TIGR00376 383 ---LKARkLILAGDHKQLPPTILSH--DAEELSLTLFERLIKE----------------YPERSRTLNVQYRMNQKIMEF 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 456 PSRLFYHRELEvcADPTVVTSLLgwEKLPKK-----------GFPLIF---HGVRGSEAREGKSPSWFNPAEAVQVLRYC 521
Cdd:TIGR00376 442 PSREFYNGKLT--AHESVANILL--RDLPKVeateseddletGIPLLFidtSGCELFELKEADSTSKYNPGEAELVSEII 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 522 CLLahsISSQVSASDIGVITPYrkqwlwssggdtgashaEHQVSFMKhvslwcshhqaelgknpQNTEEKvekirillrn 601
Cdd:TIGR00376 518 QAL---VKMGVPANDIGVITPY-----------------DAQVDLLR-----------------QLLEHR---------- 550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 602 vdLMDIKVGSVEEFQGQEYLVIIISTVRSNEDRfeddryFLGFLSNSKRFNVAITRPKALLIVLGNPHVLVRDPCFGALL 681
Cdd:TIGR00376 551 --HIDIEVSSVDGFQGREKEVIIISFVRSNRKG------EVGFLKDLRRLNVALTRARRKLIVIGDSRTLSNHKFYKRLI 622
|
....*....
gi 1034629103 682 EYSITNGVY 690
Cdd:TIGR00376 623 EWCKQHGEV 631
|
|
| AAA_12 |
pfam13087 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
407-668 |
6.19e-48 |
|
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: 167.73 E-value: 6.19e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 407 LNVSFLERLMSrpayqrdenafgacgaHNPLLVTKLVKNYRSHEALLMLPSRLFYHRELEvCADPTVVTSLLGWEKLPKK 486
Cdd:pfam13087 1 LDRSLFERLQE----------------LGPSAVVMLDTQYRMHPEIMEFPSKLFYGGKLK-DGPSVAERPLPDDFHLPDP 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 487 GFPLIFHGVRGSEAREGKS-PSWFNPAEAVQVLRYCCLLAHSISSQvsASDIGVITPYRKQwlwssggdtgashaehqvs 565
Cdd:pfam13087 64 LGPLVFIDVDGSEEEESDGgTSYSNEAEAELVVQLVEKLIKSGPEE--PSDIGVITPYRAQ------------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 566 fmkhvslwcshhqaelgknpqnteekVEKIRILLRNVDLM--DIKVGSVEEFQGQEYLVIIISTVRSNEDRfeddryFLG 643
Cdd:pfam13087 123 --------------------------VRLIRKLLKRKLGGklEIEVNTVDGFQGREKDVIIFSCVRSNEKG------GIG 170
|
250 260
....*....|....*....|....*
gi 1034629103 644 FLSNSKRFNVAITRPKALLIVLGNP 668
Cdd:pfam13087 171 FLSDPRRLNVALTRAKRGLIIVGNA 195
|
|
| DEXXQc_UPF1 |
cd18039 |
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ... |
219-419 |
3.33e-40 |
|
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: 147.78 E-value: 3.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 219 LNENQKLAVKRILSgdcRPLPYILfGPPGTGKTVTIIEAVLQVHFALPdSRILVCAPSNSAADLVCLRLHES--KVlqpa 296
Cdd:cd18039 2 LNHSQVDAVKTALQ---RPLSLIQ-GPPGTGKTVTSATIVYHLVKQGN-GPVLVCAPSNVAVDQLTEKIHQTglKV---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 297 tmVRVNATCR-----------FEEIVIDAVKPYCRDGEDIWKA----------SRFR---------------IIITTCSS 340
Cdd:cd18039 73 --VRLCAKSReavespvsflaLHNQVRNLDSAEKLELLKLLKLetgelssadeKRYRklkrkaerellrnadVICCTCVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 341 SGlfyqiGVRVG--HFTHVFVDEAGQASEPECLIPLGLMSDisgQIVLAGDPMQLGPVIKSRLAMAYGLNVSFLERLMS- 417
Cdd:cd18039 151 AG-----DPRLSkmKFRTVLIDEATQATEPECLIPLVHGAK---QVILVGDHCQLGPVVMCKKAAKAGLSQSLFERLVQl 222
|
....
gi 1034629103 418 --RP 419
Cdd:cd18039 223 giRP 226
|
|
| DEXXQc_SMUBP2 |
cd18044 |
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ... |
219-447 |
1.80e-37 |
|
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: 138.51 E-value: 1.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 219 LNENQKLAVKRILSGdcRPLpYILFGPPGTGKTVTIIEAVLQVhfALPDSRILVCAPSNSAADLVCLRLheskVLQPATM 298
Cdd:cd18044 2 LNDSQKEAVKFALSQ--KDV-ALIHGPPGTGKTTTVVEIILQA--VKRGEKVLACAPSNIAVDNLVERL----VALKVKV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 299 VRVNATCRfeeiVIDAVKPYCRDgediwKASRFRIIITTCSSSGLFyqiGVRVG-HFTHVFVDEAGQASEPECLIPLGLM 377
Cdd:cd18044 73 VRIGHPAR----LLESVLDHSLD-----ALVAAQVVLATNTGAGSR---QLLPNeLFDVVVIDEAAQALEASCWIPLLKA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 378 SdisgQIVLAGDPMQLGPVIKSRLAMAYGLNVSFLERLMSRpayqrdenafgacgaHNPLLVTKLVKNYR 447
Cdd:cd18044 141 R----RCILAGDHKQLPPTILSDKAARGGLGVTLFERLVNL---------------YGESVVRMLTVQYR 191
|
|
| DEXXQc_HELZ |
cd18077 |
DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that ... |
219-415 |
1.85e-35 |
|
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: 134.15 E-value: 1.85e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 219 LNENQKLAVKRILSGDCRPLPYILF-GPPGTGKTVTIIEAVLQVhFALPDSRILVCAPSNSAADLVC---LRLHESKVLQ 294
Cdd:cd18077 2 LNAKQKEAVLAITTPLSIQLPPVLLiGPFGTGKTFTLAQAVKHI-LQQPETRILICTHSNSAADLYIkeyLHPYVETGNP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 295 PATMVRVNATCRFEEIVIDAVKPYC---RDG-------EDIWKAsrfRIIITTCSSSGLFYQIGVRVGHFTHVFVDEAGQ 364
Cdd:cd18077 81 RARPLRVYYRNRWVKTVHPVVQKYClidEHGtfrmptrEDVMRH---RVVVVTLSTSQYLCQLDLEPGFFTHILLDEAAQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1034629103 365 ASEPECLIPLGLMSDiSGQIVLAGDPMQLGPVIKSRLAMAYGLNVSFLERL 415
Cdd:cd18077 158 AMECEAIMPLALATK-STRIVLAGDHMQLSPEVYSEFARERNLHISLLERL 207
|
|
| DEXXQc_SETX |
cd18042 |
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in ... |
219-417 |
1.74e-30 |
|
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: 119.63 E-value: 1.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 219 LNENQKLAVKRILSGDcrplPYI--LFGPPGTGKTVTIIEAVLQVHFALPDS-----------------------RILVC 273
Cdd:cd18042 1 LNESQLEAIASALQNS----PGItlIQGPPGTGKTKTIVGILSVLLAGKYRKyyekvkkklrklqrnlnnkkkknRILVC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 274 APSNSAADLVCLRLHESKVLQPatmvrvNATCRFEEIVidavkpycRDGEDIWKASRFR---IIITTCSSSG-LFYQIGV 349
Cdd:cd18042 77 APSNAAVDEIVLRLLSEGFLDG------DGRSYKPNVV--------RVGRQELRASILNeadIVCTTLSSSGsDLLESLP 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034629103 350 RvgHFTHVFVDEAGQASEPECLIPLGLmsdISGQIVLAGDPMQLGPVIKSRLAMAYGLNVSFLERLMS 417
Cdd:cd18042 143 R--GFDTVIIDEAAQAVELSTLIPLRL---GCKRLILVGDPKQLPATVFSKVAQKLGYDRSLFERLQL 205
|
|
| DEXXQc_DNA2 |
cd18041 |
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ... |
219-447 |
1.40e-28 |
|
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: 113.48 E-value: 1.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 219 LNENQKLAVKRILSgdCRPLPYILfGPPGTGKTVTIIEAVLQvhFALPDSRILVCAPSNSAADLVCLRLHESKVlqpaTM 298
Cdd:cd18041 2 LNKDQRQAIKKVLN--AKDYALIL-GMPGTGKTTTIAALVRI--LVALGKSVLLTSYTHSAVDNILLKLKKFGV----NF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 299 VRVNATCR----FEEIVIDAVKPYCRDGEDIWKA-SRFRIIITTCSSsglFYQIGVRVGHFTHVFVDEAGQASEPECLIP 373
Cdd:cd18041 73 LRLGRLKKihpdVQEFTLEAILKSCKSVEELESKyESVSVVATTCLG---INHPIFRRRTFDYCIVDEASQITLPICLGP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034629103 374 LgLMSDisgQIVLAGDPMQLGPVIKSRLAMAYGLNVSFLERLmsrpayqrdenafgaCGAHnPLLVTKLVKNYR 447
Cdd:cd18041 150 L-RLAK---KFVLVGDHYQLPPLVKSREARELGMDESLFKRL---------------SEAH-PDAVVQLTIQYR 203
|
|
| DEXXQc_Upf1-like |
cd17934 |
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ... |
241-421 |
9.32e-26 |
|
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: 102.70 E-value: 9.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 241 ILFGPPGTGKTVTIIEAVLQVHFALPDSRILVCAPSNSAADlvclrlheskvlqpatmvrvnatcrfeeiVIDavkpycr 320
Cdd:cd17934 3 LIQGPPGTGKTTTIAAIVLQLLKGLRGKRVLVTAQSNVAVD-----------------------------NVD------- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 321 dgediwkasrfriiittcsssglfyqigvrvghftHVFVDEAGQASEPECLIPLGLmsdiSGQIVLAGDPMQLGPVIKSR 400
Cdd:cd17934 47 -----------------------------------VVIIDEASQITEPELLIALIR----AKKVVLVGDPKQLPPVVQED 87
|
170 180
....*....|....*....|.
gi 1034629103 401 LAMAYGLNVSFLERLMSRPAY 421
Cdd:cd17934 88 HAALLGLSFILSLLLLFRLLL 108
|
|
| DEXXQc_HELZ2-N |
cd18076 |
N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ... |
218-415 |
2.04e-24 |
|
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: 102.28 E-value: 2.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 218 VLNENQKLAVKRIL---SGDCRPLPYILFGPPGTGKTVTIIEAVLQVhFALPDSRILVCAPSNSAADLVC---LRLHESK 291
Cdd:cd18076 1 AGNNKQQLAFNFIAgkpSEARFVPPLLIYGPFGTGKTFTLAMAALEV-IREPGTKVLICTHTNSAADIYIreyFHPYVDK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 292 VLQPATMVRVNATCRFEEIVIDAVKPYCRDGEDIW--------KASRFRIIITTCSSSglfYQIGVRVGHFTHVFVDEAG 363
Cdd:cd18076 80 GHPEARPLRIKATDRPNAITDPDTITYCCLTKDRQcfrlptrdELDFHNIVITTTAMA---FNLHVLSGFFTHIFIDEAA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1034629103 364 QASEPECLIPLGLMSdISGQIVLAGDPMQLGPVIKSrLAMAYGLNVSFLERL 415
Cdd:cd18076 157 QMLECEALIPLSYAG-PKTRVVLAGDHMQMTPKLFS-VADYNRANHTLLNRL 206
|
|
| AAA_11 |
pfam13086 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
223-400 |
2.14e-24 |
|
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: 102.81 E-value: 2.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 223 QKLAVKRILSgdcRPLPYILFGPPGTGKTVTIIEAVLQVHF-----ALPDSRILVCAPSNSAADLVCLRLHESKVLQPAT 297
Cdd:pfam13086 2 QREAIRSALS---SSHFTLIQGPPGTGKTTTIVELIRQLLSypatsAAAGPRILVCAPSNAAVDNILERLLRKGQKYGPK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 298 MVRVNAtcrfEEIVIDAVKPYCRD-------------------------------------------------------- 321
Cdd:pfam13086 79 IVRIGH----PAAISEAVLPVSLDylvesklnneedaqivkdiskeleklakalrafekeiivekllksrnkdkskleqe 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 322 -----------GEDIWKASRF---------RIIITTCSSSG---LFYQIGVRVghfthVFVDEAGQASEPECLIPLglms 378
Cdd:pfam13086 155 rrklrserkelRKELRRREQSlereildeaQIVCSTLSGAGsrlLSSLANFDV-----VIIDEAAQALEPSTLIPL---- 225
|
250 260
....*....|....*....|....
gi 1034629103 379 dISG--QIVLAGDPMQLGPVIKSR 400
Cdd:pfam13086 226 -LRGpkKVVLVGDPKQLPPTVISK 248
|
|
| DEXXc_HELZ2-C |
cd18040 |
C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ... |
219-415 |
1.94e-18 |
|
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: 86.04 E-value: 1.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 219 LNENQKLAVKRILsgdCRPLpYILFGPPGTGKTVTII-----------EAVLQVHFALPDSRILVCAPSNSAADLVC--- 284
Cdd:cd18040 2 LNPSQNHAVRTAL---TKPF-TLIQGPPGTGKTVTGVhiaywfakqnrEIQSVSGEGDGGPCVLYCGPSNKSVDVVAell 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 285 LRLHESKVLQ-------------PATMVRVN-------------------------------ATCRFEEIVIDAVKPYCR 320
Cdd:cd18040 78 LKVPGLKILRvyseqietteypiPNEPRHPNkksereskpnselssitlhhrirqpsnphsqQIKAFEARFERTQEKITE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 321 DGED-----IWKASRFR-----IIITTCSSSGlfyqiGVRVGHFTHV---FVDEAGQASEPECLIPLGLMSDISgQIVLA 387
Cdd:cd18040 158 EDIKtykilIWEARFEEletvdVILCTCSEAA-----SQKMRTHANVkqcIVDECGMCTEPESLIPIVSAPRAE-QVVLI 231
|
250 260
....*....|....*....|....*...
gi 1034629103 388 GDPMQLGPVIKSRLAMAYGLNVSFLERL 415
Cdd:cd18040 232 GDHKQLRPVVQNKEAQKLGLGRSLFERY 259
|
|
| EEXXEc_NFX1 |
cd17936 |
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ... |
219-423 |
6.76e-14 |
|
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: 70.27 E-value: 6.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 219 LNENQKLAVKRILSgdcRPLPYILfGPPGTGKT---VTIIEAVLQVHFALPDSRILVCAPSNSAADLVCLRLHESkvlQP 295
Cdd:cd17936 2 LDPSQLEALKHALT---SELALIQ-GPPGTGKTflgVKLVRALLQNQDLSITGPILVVCYTNHALDQFLEGLLDF---GP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 296 ATMVRVNATcrfeeiVIdavkpycrdGEDIWKASRFRiiittcsssGLFYQIGVRVghfthVFVDEAGQASEPE---CLI 372
Cdd:cd17936 75 TKIVRLGAR------VI---------GMTTTGAAKYR---------ELLQALGPKV-----VIVEEAAEVLEAHilaALT 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034629103 373 PlglmsDISgQIVLAGDPMQLGPVIKSRL--AMAYGLNVSFLERL------MSRPAYQR 423
Cdd:cd17936 126 P-----STE-HLILIGDHKQLRPKVNVYEltAKKYNLDVSLFERLvknglpFVTLNVQR 178
|
|
| DEXXQc_SF1 |
cd18043 |
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are ... |
220-405 |
1.21e-10 |
|
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: 59.52 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 220 NENQKLAVKRILSGDCrplpYILFGPPGTGKTVTIieAVLQVHFALPDSRILVCAPSNSAADLVclrlheskvlqpatmv 299
Cdd:cd18043 1 DSSQEAAIISARNGKN----VVIQGPPGTGKSQTI--ANIIANALARGKRVLFVSEKKAALDVV---------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 300 rvnatcrfeeividavkpycrdgediwkasRFRIIITTCSSSGLFYQIGvrVGHFTHVFVDEAGQASePECLIPLGLMSD 379
Cdd:cd18043 59 ------------------------------RFPCWIMSPLSVSQYLPLN--RNLFDLVIFDEASQIP-IEEALPALFRGK 105
|
170 180
....*....|....*....|....*.
gi 1034629103 380 isgQIVLAGDPMQLGPVIksRLAMAY 405
Cdd:cd18043 106 ---QVVVVGDDKQLPPSI--LLREHY 126
|
|
| RecD |
COG0507 |
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
202-396 |
2.24e-10 |
|
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: 63.84 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 202 DEIQTPKARKMEFFNPVLNENQKLAVKRILSGdcRPLpYILFGPPGTGKTvTIIEAVLQVHFALPDsRILVCAPSNSAAd 281
Cdd:COG0507 108 ADVEAALAALEPRAGITLSDEQREAVALALTT--RRV-SVLTGGAGTGKT-TTLRALLAALEALGL-RVALAAPTGKAA- 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 282 lvcLRLHESKVLQPATMvrvnatCRFEEIVIDAVKPYCRDGEDIWKAsrfRIIIttcsssglfyqigvrvghfthvfVDE 361
Cdd:COG0507 182 ---KRLSESTGIEARTI------HRLLGLRPDSGRFRHNRDNPLTPA---DLLV-----------------------VDE 226
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1034629103 362 AGqasepecLIPLGLMSDI-------SGQIVLAGDPMQLGPV 396
Cdd:COG0507 227 AS-------MVDTRLMAALlealpraGARLILVGDPDQLPSV 261
|
|
| EEXXQc_AQR |
cd17935 |
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds ... |
227-415 |
6.19e-10 |
|
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: 59.75 E-value: 6.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 227 VKRILSGdCRPLPYILFGPPGTGKTVTIIEAVLQVHFALPDSRILVCAPSNSAADLVclrlheskvlqpatmvrvnatcr 306
Cdd:cd17935 11 IEAIRSG-MQPGLTMVVGPPGTGKTDVAVQIISNLYHNFPNQRTLIVTHSNQALNQL----------------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 307 FEEIVidavKPYCRDGEDIWKASRFRIIITTCSSSGLFYQIGVRVG-HFTHVFVDEAGQASEPECLIPLGLMSDISG--- 382
Cdd:cd17935 67 FEKIM----ALDIDERHLLRLGHGAKIIAMTCTHAALKRGELVELGfKYDNILMEEAAQILEIETFIPLLLQNPEDGpnr 142
|
170 180 190
....*....|....*....|....*....|....*.
gi 1034629103 383 --QIVLAGDPMQLGPVIKSRLAMAYG-LNVSFLERL 415
Cdd:cd17935 143 lkRLIMIGDHHQLPPVIKNMAFQKYSnMEQSLFTRL 178
|
|
| AAA_30 |
pfam13604 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
219-396 |
4.47e-09 |
|
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. There is a Walker A and Walker B.
Pssm-ID: 433343 [Multi-domain] Cd Length: 191 Bit Score: 56.80 E-value: 4.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 219 LNENQKLAVKRILSGDCRPLpyILFGPPGTGKTvTIIEAVLQVHFALPdSRILVCAPSNSAAdlvclrlhesKVLQpatm 298
Cdd:pfam13604 2 LNAEQAAAVRALLTSGDRVA--VLVGPAGTGKT-TALKALREAWEAAG-YRVIGLAPTGRAA----------KVLG---- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 299 vrvnatcrfEEIVIDAVkpycrdgediwkasrfriiiTTcssSGLFYQIGVRVGHFTH--VFVDEAGQASEPECLIPLGL 376
Cdd:pfam13604 64 ---------EELGIPAD--------------------TI---AKLLHRLGGRAGLDPGtlLIVDEAGMVGTRQMARLLKL 111
|
170 180
....*....|....*....|
gi 1034629103 377 MSDISGQIVLAGDPMQLGPV 396
Cdd:pfam13604 112 AEDAGARVILVGDPRQLPSV 131
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
213-362 |
5.36e-09 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 56.73 E-value: 5.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 213 EFFNPVLNENQKLAVKRILSGDCRplpYILFGPPGTGKTVTIIEAVLQVHFALPDSRILVCAPSNSAADLVCLRLheSKV 292
Cdd:smart00487 3 KFGFEPLRPYQKEAIEALLSGLRD---VILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEEL--KKL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034629103 293 LQPATMVRVNATCRFEEividavkpycRDGEDIWKASRFRIIITTCSS-SGLFYQIGVRVGHFTHVFVDEA 362
Cdd:smart00487 78 GPSLGLKVVGLYGGDSK----------REQLRKLESGKTDILVTTPGRlLDLLENDKLSLSNVDLVILDEA 138
|
|
| DExxQc_SF1-N |
cd17914 |
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ... |
244-417 |
3.48e-08 |
|
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: 52.49 E-value: 3.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 244 GPPGTGKT---VTIIEAVLQVHfALPDSRILVCAPSNSAADlvclrlheskvlqpatmvrvnatcrfeeividavkpycr 320
Cdd:cd17914 6 GPPGTGKTrvlVKIVAALMQNK-NGEPGRILLVTPTNKAAA--------------------------------------- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 321 dgediwkasRFRIIittcsssglfyqigvrvghfthvFVDEAGQASEPECLIPLGLMSDiSGQIVLAGDPMQLGPVIKSR 400
Cdd:cd17914 46 ---------QLDNI-----------------------LVDEAAQILEPETSRLIDLALD-QGRVILVGDHDQLGPVWRGA 92
|
170
....*....|....*..
gi 1034629103 401 LAMAYGLNVSFLERLMS 417
Cdd:cd17914 93 VLAKICNEQSLFTRLVR 109
|
|
| DEXSc_RecD-like |
cd17933 |
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ... |
223-396 |
6.99e-08 |
|
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: 52.56 E-value: 6.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 223 QKLAVKRILSGdcrplPYILF-GPPGTGKTvTIIEAVLQVhFALPDSRILVCAPSNSAADlvclRLHESKVLQPATMvrv 301
Cdd:cd17933 2 QKAAVRLVLRN-----RVSVLtGGAGTGKT-TTLKALLAA-LEAEGKRVVLAAPTGKAAK----RLSESTGIEASTI--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 302 natCRFEEIVIDAVKPYcRDGEDIwkaSRFRIIIttcsssglfyqigvrvghfthvfVDEAGqasepecLIPLGLMSDI- 380
Cdd:cd17933 68 ---HRLLGINPGGGGFY-YNEENP---LDADLLI-----------------------VDEAS-------MVDTRLMAALl 110
|
170 180
....*....|....*....|.
gi 1034629103 381 -----SGQIVLAGDPMQLGPV 396
Cdd:cd17933 111 saipaGARLILVGDPDQLPSV 131
|
|
| AAA_19 |
pfam13245 |
AAA domain; |
223-297 |
2.75e-04 |
|
AAA domain;
Pssm-ID: 433059 [Multi-domain] Cd Length: 136 Bit Score: 41.43 E-value: 2.75e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034629103 223 QKLAVKRILSGDcrplPYILFGPPGTGKT---VTIIEAVLQVHFAlpDSRILVCAPSNSAADlvclRLHESkVLQPAT 297
Cdd:pfam13245 1 QREAVRTALPSK----VVLLTGGPGTGKTttiRHIVALLVALGGV--SFPILLAAPTGRAAK----RLSER-TGLPAS 67
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
218-260 |
2.86e-03 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 39.05 E-value: 2.86e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1034629103 218 VLNENQKLAVKRILSGDcRPLPYILFGPPGTGKTvTIIEAVLQ 260
Cdd:cd00009 1 VGQEEAIEALREALELP-PPKNLLLYGPPGTGKT-TLARAIAN 41
|
|
| DEXQc_bact_SNF2 |
cd18013 |
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ... |
223-281 |
3.76e-03 |
|
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: 39.64 E-value: 3.76e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034629103 223 QKLAVKRILSGDcrplPYILFGPPGTGKTVTIIEAVLQVHFALPDSRILVCAPSNSAAD 281
Cdd:cd18013 5 QKVAINFIIEHP----YCGLFLDMGLGKTVTTLTALSDLQLDDFTRRVLVIAPLRVARS 59
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
216-278 |
4.90e-03 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 38.42 E-value: 4.90e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034629103 216 NPVLNENQKLAVKRIL-SGDCRPLPYILFGPPGTGKTVTIIEAVLQVHFALPDSRILVCAPSNS 278
Cdd:pfam04851 1 KLELRPYQIEAIENLLeSIKNGQKRGLIVMATGSGKTLTAAKLIARLFKKGPIKKVLFLVPRKD 64
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
177-263 |
5.50e-03 |
|
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 440232 [Multi-domain] Cd Length: 397 Bit Score: 39.89 E-value: 5.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629103 177 TEERRVGDKDLPVLAPFTAEMSDWVDEIQTPKARKMEFFNPVLNENQKLAVKRILS------------GDCRPLPYILFG 244
Cdd:COG0464 119 LELLRESAEALALAAPLVTYEDIGGLEEELLELREAILDDLGGLEEVKEELRELVAlplkrpelreeyGLPPPRGLLLYG 198
|
90 100
....*....|....*....|..
gi 1034629103 245 PPGTGKTvTIIEAV---LQVHF 263
Cdd:COG0464 199 PPGTGKT-LLARALageLGLPL 219
|
|
| |
