|
Name |
Accession |
Description |
Interval |
E-value |
| DEXXQc_SETX |
cd18042 |
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in ... |
258-557 |
4.41e-97 |
|
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: 301.44 E-value: 4.41e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 258 LNKSQKEAIDVGLSRKS-FVLIQGPPGTGKTQTILSILGAIMHATPARVQSKGTDHEVKRGIQmtiqekynhwgraspwi 336
Cdd:cd18042 1 LNESQLEAIASALQNSPgITLIQGPPGTGKTKTIVGILSVLLAGKYRKYYEKVKKKLRKLQRN----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 337 lgvnprdaimpedgddgffptsgnelkpevvNASRKYRLRVLVCAPSNSALDEIVLRLLSSGLRDENAQTYTPKIVRIGl 416
Cdd:cd18042 64 -------------------------------LNNKKKKNRILVCAPSNAAVDEIVLRLLSEGFLDGDGRSYKPNVVRVG- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 417 kahhsvasvsldhlvaqkrgsaidkpkqgttgtdIDSIRTAILEEAAIVFATLSFSGSALLAKSNRGFDVVIIDEAAQAV 496
Cdd:cd18042 112 ----------------------------------RQELRASILNEADIVCTTLSSSGSDLLESLPRGFDTVIIDEAAQAV 157
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063722804 497 EPATLIPLATRCKQVFLVGDPKQLPATVISTVAQDSGYGTSMFERLQKAGYPVKMLKTQYR 557
Cdd:cd18042 158 ELSTLIPLRLGCKRLILVGDPKQLPATVFSKVAQKLGYDRSLFERLQLAGYPVLMLTTQYR 218
|
|
| AAA_12 |
pfam13087 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
534-731 |
3.44e-83 |
|
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: 264.02 E-value: 3.44e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 534 YGTSMFERLQKAG-YPVKMLKTQYRMHPEIRSFPSKQFYEGALEDGSDIEAQTTRD-WHKYRCFGPFCFFDIHEGKESQH 611
Cdd:pfam13087 1 LDRSLFERLQELGpSAVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAERPLPDdFHLPDPLGPLVFIDVDGSEEEES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 612 PGaTGSRVNLDEVEFVLLIYHRLVTMYPELKSssQLAIISPYNYQVKTFKDRFKEMFGTEAEkvVDINTVDGFQGREKDV 691
Cdd:pfam13087 81 DG-GTSYSNEAEAELVVQLVEKLIKSGPEEPS--DIGVITPYRAQVRLIRKLLKRKLGGKLE--IEVNTVDGFQGREKDV 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1063722804 692 AIFSCVRANENGQIGFLSNSRRMNVGITRAKSSVLVVGSA 731
Cdd:pfam13087 156 IIFSCVRSNEKGGIGFLSDPRRLNVALTRAKRGLIIVGNA 195
|
|
| DNA2 |
COG1112 |
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair]; |
457-750 |
1.16e-71 |
|
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
Pssm-ID: 440729 [Multi-domain] Cd Length: 819 Bit Score: 251.59 E-value: 1.16e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 457 AILEEAAIVFATLSFSGSALLAKSNRgFDVVIIDEAAQAVEPATLIPLAtRCKQVFLVGDPKQLPATVISTVAQDS---G 533
Cdd:COG1112 530 ALLELAPVVGMTPASVARLLPLGEGS-FDLVIIDEASQATLAEALGALA-RAKRVVLVGDPKQLPPVVFGEEAEEVaeeG 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 534 YGTSMFERLQKA-GYPVKMLKTQYRMHPEIRSFPSKQFYEGALEDGSDIEAQTTRDWHKyrcfgPFCFFDIHEGKESQHp 612
Cdd:COG1112 608 LDESLLDRLLARlPERGVMLREHYRMHPEIIAFSNRLFYDGKLVPLPSPKARRLADPDS-----PLVFIDVDGVYERRG- 681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 613 gatGSRVNLDEVEFVLLIYHRLVTMYPELKSssqLAIISPYNYQVKTFKDRFKEMFGTEAEKVVdINTVDGFQGREKDVA 692
Cdd:COG1112 682 ---GSRTNPEEAEAVVELVRELLEDGPDGES---IGVITPYRAQVALIRELLREALGDGLEPVF-VGTVDRFQGDERDVI 754
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063722804 693 IFSCVRANEN---GQIGFLSNS-RRMNVGITRAKSSVLVVGSAATLKSDP---LWKNLIESAEQR 750
Cdd:COG1112 755 IFSLVYSNDEdvpRNFGFLNGGpRRLNVAVSRARRKLIVVGSRELLDSDPstpALKRLLEYLERA 819
|
|
| TIGR00376 |
TIGR00376 |
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ... |
252-750 |
3.18e-70 |
|
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: 243.57 E-value: 3.18e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 252 EFFNENLNKSQKEAIDVGLSRKSFVLIQGPPGTGKTQTILSILgaimhatparVQskgtdhEVKRGiqmtiqekynhwgr 331
Cdd:TIGR00376 152 QFFDPNLNESQKEAVLFALSSKDLFLIHGPPGTGKTRTVVELI----------RQ------LVKRG-------------- 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 332 aspwilgvnprdaimpedgddgffptsgnelkpevvnasrkyrLRVLVCAPSNSALDEIVLRLLSSGLrdenaqtytpKI 411
Cdd:TIGR00376 202 -------------------------------------------LRVLVTAPSNIAVDNLLERLALCDQ----------KI 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 412 VRIGLKA-------HHSVASVSLDHLVAQ-----------------------------------------KRGSAIDKPK 443
Cdd:TIGR00376 229 VRLGHPArllksnkQHSLDYLIENHPKYQivadirekidelieernkktkpspqkrrglsdikilrkalkKREARGIESL 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 444 QG-------TTGTDID-----------SIRTAILEEAAivfATLSFSGSALLAKSNrgFDVVIIDEAAQAVEPATLIPLA 505
Cdd:TIGR00376 309 KIasmaewiETNKSIDrllkllpeseeRIMNEILAESD---ATNSMAGSEILNGQY--FDVAVIDEASQAMEPSCLIPLL 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 506 tRCKQVFLVGDPKQLPATVISTVAqdSGYGTSMFERLQKAgYP--VKMLKTQYRMHPEIRSFPSKQFYEGALEDGSDIEA 583
Cdd:TIGR00376 384 -KARKLILAGDHKQLPPTILSHDA--EELSLTLFERLIKE-YPerSRTLNVQYRMNQKIMEFPSREFYNGKLTAHESVAN 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 584 QTTRDWHK-----YRCFG----PFCFFDIH--EGKESQHPGATgSRVNLDEVEFVLLIYHRLVTM-YPElkssSQLAIIS 651
Cdd:TIGR00376 460 ILLRDLPKveateSEDDLetgiPLLFIDTSgcELFELKEADST-SKYNPGEAELVSEIIQALVKMgVPA----NDIGVIT 534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 652 PYNYQVKTFKDRFkemfgtEAEKV-VDINTVDGFQGREKDVAIFSCVRANENGQIGFLSNSRRMNVGITRAKSSVLVVGS 730
Cdd:TIGR00376 535 PYDAQVDLLRQLL------EHRHIdIEVSSVDGFQGREKEVIIISFVRSNRKGEVGFLKDLRRLNVALTRARRKLIVIGD 608
|
570 580
....*....|....*....|
gi 1063722804 731 AATLKSDPLWKNLIESAEQR 750
Cdd:TIGR00376 609 SRTLSNHKFYKRLIEWCKQH 628
|
|
| SF1_C_Upf1 |
cd18808 |
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ... |
558-748 |
9.22e-61 |
|
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: 203.23 E-value: 9.22e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 558 MHPEIRSFPSKQFYEGALEDGSDiEAQTTRDWHKYRCFGPFCFFDIHEGKESQHPGatGSRVNLDEVEFVLLIYHRLVTM 637
Cdd:cd18808 1 MHPEISEFPSKLFYEGKLKAGVS-VAARLNPPPLPGPSKPLVFVDVSGGEEREESG--TSKSNEAEAELVVELVKYLLKS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 638 YpelKSSSQLAIISPYNYQVKTFKDRFKEMFGTEAEkvVDINTVDGFQGREKDVAIFSCVRANE-NGQIGFLSNSRRMNV 716
Cdd:cd18808 78 G---VKPSSIGVITPYRAQVALIRELLRKRGGLLED--VEVGTVDNFQGREKDVIILSLVRSNEsGGSIGFLSDPRRLNV 152
|
170 180 190
....*....|....*....|....*....|..
gi 1063722804 717 GITRAKSSVLVVGSAATLKSDPLWKNLIESAE 748
Cdd:cd18808 153 ALTRAKRGLIIVGNPDTLSKDPLWKKLLEYLE 184
|
|
| AAA_11 |
pfam13086 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
261-526 |
4.18e-53 |
|
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: 184.85 E-value: 4.18e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 261 SQKEAIDVGLSRKSFVLIQGPPGTGKTQTILSILGAIMHATPARVQSKGtdhevkrgiqmtiqekynhwgraspwilgvn 340
Cdd:pfam13086 1 SQREAIRSALSSSHFTLIQGPPGTGKTTTIVELIRQLLSYPATSAAAGP------------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 341 prdaimpedgddgffptsgnelkpevvnasrkyrlRVLVCAPSNSALDEIVLRLLSSGlrdenaQTYTPKIVRIGLKA-- 418
Cdd:pfam13086 50 -----------------------------------RILVCAPSNAAVDNILERLLRKG------QKYGPKIVRIGHPAai 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 419 HHSVASVSLDHLVAQKRGSAID-------------------------------------KPKQGTTGTDIDSIRTA---- 457
Cdd:pfam13086 89 SEAVLPVSLDYLVESKLNNEEDaqivkdiskeleklakalrafekeiivekllksrnkdKSKLEQERRKLRSERKElrke 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 458 -----------ILEEAAIVFATLSFSGSALLAKSnRGFDVVIIDEAAQAVEPATLIPLATRCKQVFLVGDPKQLPATVIS 526
Cdd:pfam13086 169 lrrreqslereILDEAQIVCSTLSGAGSRLLSSL-ANFDVVIIDEAAQALEPSTLIPLLRGPKKVVLVGDPKQLPPTVIS 247
|
|
| RecD |
COG0507 |
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
250-305 |
3.43e-06 |
|
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: 50.36 E-value: 3.43e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063722804 250 LNEFFNEN---LNKSQKEAIDVGLSRKSFVLIQGPPGTGKTQTILSILgAIMHATPARV 305
Cdd:COG0507 114 LAALEPRAgitLSDEQREAVALALTTRRVSVLTGGAGTGKTTTLRALL-AALEALGLRV 171
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
250-305 |
4.72e-04 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 42.09 E-value: 4.72e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063722804 250 LNEFFNENLNKSQKEAIDVGLSRKSFVLIQGPPGTGKT-QTILSILGAIMHATPARV 305
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTlAALLPALEALKRGKGGRV 57
|
|
| McrB |
COG1401 |
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ... |
95-306 |
4.40e-03 |
|
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];
Pssm-ID: 441011 [Multi-domain] Cd Length: 477 Bit Score: 40.52 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 95 ECNEGEGFHFLLVTYEHEEDEYLAQNDLLLLSKEEVKGNSFPSSYGFAVVEHRqnNLLRLRMYLAEDIVQITKNTKSSRT 174
Cdd:COG1401 50 LSEELLRADRAARATELVEELSAALEVVVLLLDLEKVELNEKLALSEAAVAIE--ELYELEADSEIEAVGLLLELAERSD 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 175 KSFIQALSNMRSLITSSASPIDKRVFSLKLCGLSTIIREYIALRSVSSLPFKDLIFTAAEKSCGFGDEAwkisgPLNEFF 254
Cdd:COG1401 128 ALEALERARLLLELADLEERAALETEVLEALEAELEELLAAPEDLSADALAAELSAAEELYSEDLESED-----DYLKDL 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1063722804 255 NENLNKSQKEAIDVGLSRKSFVLIQGPPGTGKTQTILSILGAIMHATPARVQ 306
Cdd:COG1401 203 LREKFEETLEAFLAALKTKKNVILAGPPGTGKTYLARRLAEALGGEDNGRIE 254
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DEXXQc_SETX |
cd18042 |
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in ... |
258-557 |
4.41e-97 |
|
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: 301.44 E-value: 4.41e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 258 LNKSQKEAIDVGLSRKS-FVLIQGPPGTGKTQTILSILGAIMHATPARVQSKGTDHEVKRGIQmtiqekynhwgraspwi 336
Cdd:cd18042 1 LNESQLEAIASALQNSPgITLIQGPPGTGKTKTIVGILSVLLAGKYRKYYEKVKKKLRKLQRN----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 337 lgvnprdaimpedgddgffptsgnelkpevvNASRKYRLRVLVCAPSNSALDEIVLRLLSSGLRDENAQTYTPKIVRIGl 416
Cdd:cd18042 64 -------------------------------LNNKKKKNRILVCAPSNAAVDEIVLRLLSEGFLDGDGRSYKPNVVRVG- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 417 kahhsvasvsldhlvaqkrgsaidkpkqgttgtdIDSIRTAILEEAAIVFATLSFSGSALLAKSNRGFDVVIIDEAAQAV 496
Cdd:cd18042 112 ----------------------------------RQELRASILNEADIVCTTLSSSGSDLLESLPRGFDTVIIDEAAQAV 157
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063722804 497 EPATLIPLATRCKQVFLVGDPKQLPATVISTVAQDSGYGTSMFERLQKAGYPVKMLKTQYR 557
Cdd:cd18042 158 ELSTLIPLRLGCKRLILVGDPKQLPATVFSKVAQKLGYDRSLFERLQLAGYPVLMLTTQYR 218
|
|
| AAA_12 |
pfam13087 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
534-731 |
3.44e-83 |
|
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: 264.02 E-value: 3.44e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 534 YGTSMFERLQKAG-YPVKMLKTQYRMHPEIRSFPSKQFYEGALEDGSDIEAQTTRD-WHKYRCFGPFCFFDIHEGKESQH 611
Cdd:pfam13087 1 LDRSLFERLQELGpSAVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAERPLPDdFHLPDPLGPLVFIDVDGSEEEES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 612 PGaTGSRVNLDEVEFVLLIYHRLVTMYPELKSssQLAIISPYNYQVKTFKDRFKEMFGTEAEkvVDINTVDGFQGREKDV 691
Cdd:pfam13087 81 DG-GTSYSNEAEAELVVQLVEKLIKSGPEEPS--DIGVITPYRAQVRLIRKLLKRKLGGKLE--IEVNTVDGFQGREKDV 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1063722804 692 AIFSCVRANENGQIGFLSNSRRMNVGITRAKSSVLVVGSA 731
Cdd:pfam13087 156 IIFSCVRSNEKGGIGFLSDPRRLNVALTRAKRGLIIVGNA 195
|
|
| DNA2 |
COG1112 |
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair]; |
457-750 |
1.16e-71 |
|
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
Pssm-ID: 440729 [Multi-domain] Cd Length: 819 Bit Score: 251.59 E-value: 1.16e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 457 AILEEAAIVFATLSFSGSALLAKSNRgFDVVIIDEAAQAVEPATLIPLAtRCKQVFLVGDPKQLPATVISTVAQDS---G 533
Cdd:COG1112 530 ALLELAPVVGMTPASVARLLPLGEGS-FDLVIIDEASQATLAEALGALA-RAKRVVLVGDPKQLPPVVFGEEAEEVaeeG 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 534 YGTSMFERLQKA-GYPVKMLKTQYRMHPEIRSFPSKQFYEGALEDGSDIEAQTTRDWHKyrcfgPFCFFDIHEGKESQHp 612
Cdd:COG1112 608 LDESLLDRLLARlPERGVMLREHYRMHPEIIAFSNRLFYDGKLVPLPSPKARRLADPDS-----PLVFIDVDGVYERRG- 681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 613 gatGSRVNLDEVEFVLLIYHRLVTMYPELKSssqLAIISPYNYQVKTFKDRFKEMFGTEAEKVVdINTVDGFQGREKDVA 692
Cdd:COG1112 682 ---GSRTNPEEAEAVVELVRELLEDGPDGES---IGVITPYRAQVALIRELLREALGDGLEPVF-VGTVDRFQGDERDVI 754
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063722804 693 IFSCVRANEN---GQIGFLSNS-RRMNVGITRAKSSVLVVGSAATLKSDP---LWKNLIESAEQR 750
Cdd:COG1112 755 IFSLVYSNDEdvpRNFGFLNGGpRRLNVAVSRARRKLIVVGSRELLDSDPstpALKRLLEYLERA 819
|
|
| TIGR00376 |
TIGR00376 |
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ... |
252-750 |
3.18e-70 |
|
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: 243.57 E-value: 3.18e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 252 EFFNENLNKSQKEAIDVGLSRKSFVLIQGPPGTGKTQTILSILgaimhatparVQskgtdhEVKRGiqmtiqekynhwgr 331
Cdd:TIGR00376 152 QFFDPNLNESQKEAVLFALSSKDLFLIHGPPGTGKTRTVVELI----------RQ------LVKRG-------------- 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 332 aspwilgvnprdaimpedgddgffptsgnelkpevvnasrkyrLRVLVCAPSNSALDEIVLRLLSSGLrdenaqtytpKI 411
Cdd:TIGR00376 202 -------------------------------------------LRVLVTAPSNIAVDNLLERLALCDQ----------KI 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 412 VRIGLKA-------HHSVASVSLDHLVAQ-----------------------------------------KRGSAIDKPK 443
Cdd:TIGR00376 229 VRLGHPArllksnkQHSLDYLIENHPKYQivadirekidelieernkktkpspqkrrglsdikilrkalkKREARGIESL 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 444 QG-------TTGTDID-----------SIRTAILEEAAivfATLSFSGSALLAKSNrgFDVVIIDEAAQAVEPATLIPLA 505
Cdd:TIGR00376 309 KIasmaewiETNKSIDrllkllpeseeRIMNEILAESD---ATNSMAGSEILNGQY--FDVAVIDEASQAMEPSCLIPLL 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 506 tRCKQVFLVGDPKQLPATVISTVAqdSGYGTSMFERLQKAgYP--VKMLKTQYRMHPEIRSFPSKQFYEGALEDGSDIEA 583
Cdd:TIGR00376 384 -KARKLILAGDHKQLPPTILSHDA--EELSLTLFERLIKE-YPerSRTLNVQYRMNQKIMEFPSREFYNGKLTAHESVAN 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 584 QTTRDWHK-----YRCFG----PFCFFDIH--EGKESQHPGATgSRVNLDEVEFVLLIYHRLVTM-YPElkssSQLAIIS 651
Cdd:TIGR00376 460 ILLRDLPKveateSEDDLetgiPLLFIDTSgcELFELKEADST-SKYNPGEAELVSEIIQALVKMgVPA----NDIGVIT 534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 652 PYNYQVKTFKDRFkemfgtEAEKV-VDINTVDGFQGREKDVAIFSCVRANENGQIGFLSNSRRMNVGITRAKSSVLVVGS 730
Cdd:TIGR00376 535 PYDAQVDLLRQLL------EHRHIdIEVSSVDGFQGREKEVIIISFVRSNRKGEVGFLKDLRRLNVALTRARRKLIVIGD 608
|
570 580
....*....|....*....|
gi 1063722804 731 AATLKSDPLWKNLIESAEQR 750
Cdd:TIGR00376 609 SRTLSNHKFYKRLIEWCKQH 628
|
|
| SF1_C_Upf1 |
cd18808 |
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ... |
558-748 |
9.22e-61 |
|
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: 203.23 E-value: 9.22e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 558 MHPEIRSFPSKQFYEGALEDGSDiEAQTTRDWHKYRCFGPFCFFDIHEGKESQHPGatGSRVNLDEVEFVLLIYHRLVTM 637
Cdd:cd18808 1 MHPEISEFPSKLFYEGKLKAGVS-VAARLNPPPLPGPSKPLVFVDVSGGEEREESG--TSKSNEAEAELVVELVKYLLKS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 638 YpelKSSSQLAIISPYNYQVKTFKDRFKEMFGTEAEkvVDINTVDGFQGREKDVAIFSCVRANE-NGQIGFLSNSRRMNV 716
Cdd:cd18808 78 G---VKPSSIGVITPYRAQVALIRELLRKRGGLLED--VEVGTVDNFQGREKDVIILSLVRSNEsGGSIGFLSDPRRLNV 152
|
170 180 190
....*....|....*....|....*....|..
gi 1063722804 717 GITRAKSSVLVVGSAATLKSDPLWKNLIESAE 748
Cdd:cd18808 153 ALTRAKRGLIIVGNPDTLSKDPLWKKLLEYLE 184
|
|
| AAA_11 |
pfam13086 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
261-526 |
4.18e-53 |
|
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: 184.85 E-value: 4.18e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 261 SQKEAIDVGLSRKSFVLIQGPPGTGKTQTILSILGAIMHATPARVQSKGtdhevkrgiqmtiqekynhwgraspwilgvn 340
Cdd:pfam13086 1 SQREAIRSALSSSHFTLIQGPPGTGKTTTIVELIRQLLSYPATSAAAGP------------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 341 prdaimpedgddgffptsgnelkpevvnasrkyrlRVLVCAPSNSALDEIVLRLLSSGlrdenaQTYTPKIVRIGLKA-- 418
Cdd:pfam13086 50 -----------------------------------RILVCAPSNAAVDNILERLLRKG------QKYGPKIVRIGHPAai 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 419 HHSVASVSLDHLVAQKRGSAID-------------------------------------KPKQGTTGTDIDSIRTA---- 457
Cdd:pfam13086 89 SEAVLPVSLDYLVESKLNNEEDaqivkdiskeleklakalrafekeiivekllksrnkdKSKLEQERRKLRSERKElrke 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 458 -----------ILEEAAIVFATLSFSGSALLAKSnRGFDVVIIDEAAQAVEPATLIPLATRCKQVFLVGDPKQLPATVIS 526
Cdd:pfam13086 169 lrrreqslereILDEAQIVCSTLSGAGSRLLSSL-ANFDVVIIDEAAQALEPSTLIPLLRGPKKVVLVGDPKQLPPTVIS 247
|
|
| DEXXQc_SMUBP2 |
cd18044 |
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ... |
257-557 |
3.71e-48 |
|
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: 168.94 E-value: 3.71e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 257 NLNKSQKEAIDVGLSRKSFVLIQGPPGTGKTQTILSILgaimhatparVQskgtdhEVKRGiqmtiqekynhwgraspwi 336
Cdd:cd18044 1 NLNDSQKEAVKFALSQKDVALIHGPPGTGKTTTVVEII----------LQ------AVKRG------------------- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 337 lgvnprdaimpedgddgffptsgnelkpevvnasrkyrLRVLVCAPSNSALDEIVLRLLSSGLrdenaqtytpKIVRIGL 416
Cdd:cd18044 46 --------------------------------------EKVLACAPSNIAVDNLVERLVALKV----------KVVRIGH 77
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 417 KAH--HSVASVSLDHLVaqkrgsaidkpkqgttgtdidsirtaileEAAIVFATLSFSGSALLaKSNRGFDVVIIDEAAQ 494
Cdd:cd18044 78 PARllESVLDHSLDALV-----------------------------AAQVVLATNTGAGSRQL-LPNELFDVVVIDEAAQ 127
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063722804 495 AVEPATLIPLaTRCKQVFLVGDPKQLPATVISTVAQDSGYGTSMFERL--QKAGYPVKMLKTQYR 557
Cdd:cd18044 128 ALEASCWIPL-LKARRCILAGDHKQLPPTILSDKAARGGLGVTLFERLvnLYGESVVRMLTVQYR 191
|
|
| DEXXQc_UPF1 |
cd18039 |
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ... |
257-557 |
4.30e-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: 4.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 257 NLNKSQKEAIDVGLSRKsFVLIQGPPGTGKTQTILSIlgaimhatparvqskgtdhevkrgiqmtiqekynhwgraspwi 336
Cdd:cd18039 1 ELNHSQVDAVKTALQRP-LSLIQGPPGTGKTVTSATI------------------------------------------- 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 337 lgvnprdaimpedgddgffptsgnelkpeVVNASRKYRLRVLVCAPSNSALDEIVLRLLSSGLrdenaqtytpKIVRIGL 416
Cdd:cd18039 37 -----------------------------VYHLVKQGNGPVLVCAPSNVAVDQLTEKIHQTGL----------KVVRLCA 77
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 417 KAHHSVAS----VSLDHLVAQKRGSAIDKPKQGT-----------TGTDIDSIRTA---ILEEAAIVFATLSFSGSALLA 478
Cdd:cd18039 78 KSREAVESpvsfLALHNQVRNLDSAEKLELLKLLkletgelssadEKRYRKLKRKAereLLRNADVICCTCVGAGDPRLS 157
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063722804 479 KSNrgFDVVIIDEAAQAVEPATLIPLATRCKQVFLVGDPKQLPATVISTVAQDSGYGTSMFERLQKAGYPVKMLKTQYR 557
Cdd:cd18039 158 KMK--FRTVLIDEATQATEPECLIPLVHGAKQVILVGDHCQLGPVVMCKKAAKAGLSQSLFERLVQLGIRPIRLQVQYR 234
|
|
| DEXXQc_DNA2 |
cd18041 |
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ... |
257-557 |
1.01e-30 |
|
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: 119.65 E-value: 1.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 257 NLNKSQKEAIDVGLSRKSFVLIQGPPGTGKTQTILSIlgaimhatparvqskgtdhevkrgiqmtiqekynhwgraspwi 336
Cdd:cd18041 1 GLNKDQRQAIKKVLNAKDYALILGMPGTGKTTTIAAL------------------------------------------- 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 337 lgvnprdaimpedgddgffptsgnelkpevVNASRKYRLRVLVCAPSNSALDEIVLRLLSSGLRdenaqtytpkIVRIGl 416
Cdd:cd18041 38 ------------------------------VRILVALGKSVLLTSYTHSAVDNILLKLKKFGVN----------FLRLG- 76
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 417 kahhsvaSVSLDH-LVAQKRGSAIdkpkqGTTGTDIDSIRTaILEEAAIVFAT-LSFsGSALLAKsnRGFDVVIIDEAAQ 494
Cdd:cd18041 77 -------RLKKIHpDVQEFTLEAI-----LKSCKSVEELES-KYESVSVVATTcLGI-NHPIFRR--RTFDYCIVDEASQ 140
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063722804 495 AVEPATLIPLAtRCKQVFLVGDPKQLPATVISTVAQDSGYGTSMFERLQKAgYP--VKMLKTQYR 557
Cdd:cd18041 141 ITLPICLGPLR-LAKKFVLVGDHYQLPPLVKSREARELGMDESLFKRLSEA-HPdaVVQLTIQYR 203
|
|
| DEXXQc_Helz-like |
cd18038 |
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ... |
258-561 |
1.19e-26 |
|
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: 108.86 E-value: 1.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 258 LNKSQKEAIDVGLSRKSFV---LIQGPPGTGKTQTILSILGAIMHATParvqskgtdhevkrgiqmtiqekyNHwgrasp 334
Cdd:cd18038 2 LNDEQKLAVRNIVTGTSRPppyIIFGPPGTGKTVTLVEAILQVLRQPP------------------------EA------ 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 335 wilgvnprdaimpedgddgffptsgnelkpevvnasrkyrlRVLVCAPSNSALDEIVLRLLSSGLRDE-----NAQTYTP 409
Cdd:cd18038 52 -----------------------------------------RILVCAPSNSAADLLAERLLNALVTKReilrlNAPSRDR 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 410 KIVRIGLKAHHSVASvsldhlvaqKRGSAIDKPKQgttgtdidsirtaiLEEAAIVFATLSFSGsaLLAKSNRG---FDV 486
Cdd:cd18038 91 ASVPPELLPYCNSKA---------EGTFRLPSLEE--------------LKKYRIVVCTLMTAG--RLVQAGVPnghFTH 145
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063722804 487 VIIDEAAQAVEPATLIPLATRCK---QVFLVGDPKQLPATVISTVAQDSGYGTSMFERLqkagypvkMLKTQYRMHPE 561
Cdd:cd18038 146 IFIDEAGQATEPEALIPLSELASkntQIVLAGDPKQLGPVVRSPLARKYGLGKSLLERL--------MERPLYYKDGE 215
|
|
| DEXXc_HELZ2-C |
cd18040 |
C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ... |
257-557 |
1.76e-23 |
|
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: 101.06 E-value: 1.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 257 NLNKSQKEAIDVGLSrKSFVLIQGPPGTGKTQTILSIlgaimhatparvqskgtdhevkrgiqmtiqekynhwgraSPWI 336
Cdd:cd18040 1 KLNPSQNHAVRTALT-KPFTLIQGPPGTGKTVTGVHI---------------------------------------AYWF 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 337 LGVNpRDAIMPEDGDDGffptsgnelKPEVvnasrkyrlrvLVCAPSNSALD---EIVLRLlsSGLR-----DENAQTYT 408
Cdd:cd18040 41 AKQN-REIQSVSGEGDG---------GPCV-----------LYCGPSNKSVDvvaELLLKV--PGLKilrvySEQIETTE 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 409 PKIVRIGL----------KAHHSVASVSLDHLVAQKRG----------SAIDKPKQGTTGTDIDSIRTAILEEAA----- 463
Cdd:cd18040 98 YPIPNEPRhpnkkseresKPNSELSSITLHHRIRQPSNphsqqikafeARFERTQEKITEEDIKTYKILIWEARFeelet 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 464 --IVFATLSFSGSALLaKSNRGFDVVIIDEAAQAVEPATLIPLAT--RCKQVFLVGDPKQLPATVISTVAQDSGYGTSMF 539
Cdd:cd18040 178 vdVILCTCSEAASQKM-RTHANVKQCIVDECGMCTEPESLIPIVSapRAEQVVLIGDHKQLRPVVQNKEAQKLGLGRSLF 256
|
330
....*....|....*...
gi 1063722804 540 ERLQKAGYpvkMLKTQYR 557
Cdd:cd18040 257 ERYAEKAC---MLDTQYR 271
|
|
| DEXXQc_Mov10L1 |
cd18078 |
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds ... |
258-542 |
5.78e-22 |
|
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: 95.51 E-value: 5.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 258 LNKSQKEA---IDVGLSRKSFVLIQGPPGTGKTQTIlsilgaimhatparvqskgtdhevkrgIQMTIQEKYNHwgrasp 334
Cdd:cd18078 2 LNELQKEAvkrILGGECRPLPYILFGPPGTGKTVTI---------------------------IEAILQVVYNL------ 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 335 wilgvnprdaimpedgddgffptsgnelkPevvnasrkyRLRVLVCAPSNSALDEIVLRLLSSGLRDENAqtytpkIVRi 414
Cdd:cd18078 49 -----------------------------P---------RSRILVCAPSNSAADLVTSRLHESKVLKPGD------MVR- 83
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 415 gLKAHHSVASVSLDhlvaqkrgsaIDKPKQGTTgtdiDSIRTAIleEAAIVFATLSFSGSALLAKSNRG-FDVVIIDEAA 493
Cdd:cd18078 84 -LNAVNRFESTVID----------ARKLYCRLG----EDLSKAS--RHRIVISTCSTAGLLYQMGLPVGhFTHVFVDEAG 146
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1063722804 494 QAVEPATLIPL---ATRCKQVFLVGDPKQLPATVISTVAQDSGYGTSMFERL 542
Cdd:cd18078 147 QATEPESLIPLgliSSRDGQIILAGDPMQLGPVIKSRLASAYGLGVSFLERL 198
|
|
| DEXXQc_Upf1-like |
cd17934 |
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ... |
456-557 |
7.06e-20 |
|
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: 85.75 E-value: 7.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 456 TAILEEAAIVFATLSFSGSALLAKSNR---GFDVVIIDEAAQAVEPATLIPLAtRCKQVFLVGDPKQLPATV----ISTV 528
Cdd:cd17934 14 TTIAAIVLQLLKGLRGKRVLVTAQSNVavdNVDVVIIDEASQITEPELLIALI-RAKKVVLVGDPKQLPPVVqedhAALL 92
|
90 100
....*....|....*....|....*....
gi 1063722804 529 AQDSGYGTSMFERLQKAGYPVKMLKTQYR 557
Cdd:cd17934 93 GLSFILSLLLLFRLLLPGSPKVMLDTQYR 121
|
|
| EEXXEc_NFX1 |
cd17936 |
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ... |
258-556 |
6.04e-19 |
|
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: 85.29 E-value: 6.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 258 LNKSQKEAIDVGLSRKsFVLIQGPPGTGKTQTILSILGAImhatparvqskgtdhevkrgiqmtiqekynhwgraspwil 337
Cdd:cd17936 2 LDPSQLEALKHALTSE-LALIQGPPGTGKTFLGVKLVRAL---------------------------------------- 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 338 gvnprdaimpedgddgffptsgnelkpeVVNASRKYRLRVLVCAPSNSALDEIVLRLLSSGlrdenaqtyTPKIVRIGlk 417
Cdd:cd17936 41 ----------------------------LQNQDLSITGPILVVCYTNHALDQFLEGLLDFG---------PTKIVRLG-- 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 418 ahhsvasvsldhlvaqkrgsaidkpkqgttgtdidsirtaileeAAIVFATLSfsGSA----LLAKSNrgFDVVIIDEAA 493
Cdd:cd17936 82 --------------------------------------------ARVIGMTTT--GAAkyreLLQALG--PKVVIVEEAA 113
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063722804 494 QAVEPATLIPLATRCKQVFLVGDPKQLPATVISTVAQDSGYG--TSMFERLQKAGYPVKMLKTQY 556
Cdd:cd17936 114 EVLEAHILAALTPSTEHLILIGDHKQLRPKVNVYELTAKKYNldVSLFERLVKNGLPFVTLNVQR 178
|
|
| CoV_Nsp13-helicase |
cd21718 |
helicase domain of coronavirus non-structural protein 13; This model represents the helicase ... |
485-728 |
1.22e-15 |
|
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: 79.11 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 485 DVVIIDEAAQAVE-PATLIPLATRCKQVFLVGDPKQLPA--TVISTVAQDSGYGTSMfERLQKAGYPVKMLKTQYRMHPE 561
Cdd:cd21718 119 DIVVVDEVSMCTNyDLSVVNARLKYKHIVYVGDPAQLPAprTLLTEGSLEPKDYNVV-TRLMVGSGPDVFLSKCYRCPKE 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 562 IRSFPSKQFYEGALEDGSDIEAQttrdwhkyrCFGPFCFFDI-HEGkesqhpgatGSRVNLDEVEFVLliyhRLVTMYPE 640
Cdd:cd21718 198 IVDTVSKLVYDNKLKAIKPKSRQ---------CFKTFGKGDVrHDN---------GSAINRPQLEFVK----RFLDRNPR 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 641 LkssSQLAIISPYNYQvktfKDRFKEMFGteaekvVDINTVDGFQGREKDVAIFsCVRANENGQigflSNSRRMNVGITR 720
Cdd:cd21718 256 W---RKAVFISPYNAM----NNRASRLLG------LSTQTVDSSQGSEYDYVIF-CQTTDTAHA----LNINRFNVAITR 317
|
....*...
gi 1063722804 721 AKSSVLVV 728
Cdd:cd21718 318 AKHGILVI 325
|
|
| betaCoV_Nsp13-helicase |
cd21722 |
helicase domain of betacoronavirus non-structural protein 13; This model represents the ... |
485-734 |
1.44e-10 |
|
helicase domain of betacoronavirus non-structural protein 13; This model represents the helicase domain of non-structural protein 13 (Nsp13) from betacoronavirus, 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: 409655 [Multi-domain] Cd Length: 340 Bit Score: 63.67 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 485 DVVIIDEAAQAVE-PATLIPLATRCKQVFLVGDPKQLPA--TVISTVAQDSGYGTSMfERLQKAGYPVKMLKTQYRMHPE 561
Cdd:cd21722 119 DILVVDEVSMCTNyDLSVINARVRAKHIVYIGDPAQLPAprTLLTKGTLEPEYFNSV-TRLMCCLGPDIFLGTCYRCPKE 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 562 IRSFPSKQFYEGALEDGSDIEAQttrdwhkyrCFGpfCFFDIHEGKESQhpgatgSRVNLDEVEFVlliyHRLVTMYPEL 641
Cdd:cd21722 198 IVDTVSALVYDNKLKAKKDNSGQ---------CFK--VYYKGSVTHDSS------SAINRPQIYLV----KKFLKANPAW 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 642 KSSsqlAIISPYNYQVKTFKdrfkEMFGTEAEkvvdinTVDGFQGREKDVAIFScvranENGQIGFLSNSRRMNVGITRA 721
Cdd:cd21722 257 SKA---VFISPYNSQNAVAR----RVLGLQTQ------TVDSSQGSEYDYVIYC-----QTAETAHSVNVNRFNVAITRA 318
|
250
....*....|...
gi 1063722804 722 KSSVLVVGSAATL 734
Cdd:cd21722 319 KKGILCVMSSMQL 331
|
|
| DEXXQc_HELZ |
cd18077 |
DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that ... |
376-557 |
5.21e-10 |
|
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: 60.19 E-value: 5.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 376 RVLVCAPSNSALDEIVLRLLSSGLRDENAQTytpKIVRIGLKaHHSVASVsldHLVAQKRgSAIDkpkqgTTGTDIDSIR 455
Cdd:cd18077 52 RILICTHSNSAADLYIKEYLHPYVETGNPRA---RPLRVYYR-NRWVKTV---HPVVQKY-CLID-----EHGTFRMPTR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 456 TAILeEAAIVFATLSFSGSALLAKSNRG-FDVVIIDEAAQAVEPATLIP--LATRCKQVFLVGDPKQLPATVISTVAQDS 532
Cdd:cd18077 119 EDVM-RHRVVVVTLSTSQYLCQLDLEPGfFTHILLDEAAQAMECEAIMPlaLATKSTRIVLAGDHMQLSPEVYSEFARER 197
|
170 180
....*....|....*....|....*....
gi 1063722804 533 GYGTSMFERL---QKAGYPVKMLKTQ-YR 557
Cdd:cd18077 198 NLHISLLERLyehYPSEHPCRILLCEnYR 226
|
|
| DExxQc_SF1-N |
cd17914 |
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ... |
473-556 |
8.00e-10 |
|
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: 57.11 E-value: 8.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 473 GSALLA----KSNRGFDVVIIDEAAQAVEPAT--LIPLATRCKQVFLVGDPKQLPATVISTVAQDSGYGTSMFERLQKAG 546
Cdd:cd17914 32 GRILLVtptnKAAAQLDNILVDEAAQILEPETsrLIDLALDQGRVILVGDHDQLGPVWRGAVLAKICNEQSLFTRLVRLG 111
|
90
....*....|
gi 1063722804 547 YPVKMLKTQY 556
Cdd:cd17914 112 VSLIRLQVQY 121
|
|
| DEXXQc_SF1 |
cd18043 |
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are ... |
484-521 |
1.57e-09 |
|
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: 56.44 E-value: 1.57e-09
10 20 30
....*....|....*....|....*....|....*...
gi 1063722804 484 FDVVIIDEAAQaVEPATLIPLATRCKQVFLVGDPKQLP 521
Cdd:cd18043 81 FDLVIFDEASQ-IPIEEALPALFRGKQVVVVGDDKQLP 117
|
|
| EEXXQc_AQR |
cd17935 |
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds ... |
477-564 |
4.54e-09 |
|
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: 57.05 E-value: 4.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 477 LAKSNRGFDVVIIDEAAQAVEPATLIPLA--------TRCKQVFLVGDPKQLPATV-ISTVAQDSGYGTSMFERLQKAGY 547
Cdd:cd17935 104 LVELGFKYDNILMEEAAQILEIETFIPLLlqnpedgpNRLKRLIMIGDHHQLPPVIkNMAFQKYSNMEQSLFTRLVRLGV 183
|
90
....*....|....*..
gi 1063722804 548 PVKMLKTQYRMHPEIRS 564
Cdd:cd17935 184 PTVDLDAQGRARASISS 200
|
|
| gammaCoV_Nsp13-helicase |
cd21720 |
helicase domain of gammacoronavirus non-structural protein 13; This model represents the ... |
511-728 |
4.94e-09 |
|
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: 58.78 E-value: 4.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 511 VFLVGDPKQLPA--TVISTVAQDSGYgtSMFERLQKAGYPVKMLKTQYRMHPEIRSFPSKQFYEGaledgsDIEAQTTRD 588
Cdd:cd21720 146 VVYVGDPAQLPAprTLLNGSLSPKDY--NVVTNLMVCVKPDIFLAKCYRCPKEIVDTVSTLVYDG------KFIANNPES 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 589 WHKYRCFGPFCFFDIheGKESqhpgatGSRVNLDEVEFVlliyHRLVTMYPELKSSSqlaIISPYNyqvkTFKDRFKEMF 668
Cdd:cd21720 218 RQCFKVIVNNGNSDV--GHES------GSAYNTTQLEFV----KDFVCRNKEWREAT---FISPYN----AMNQRAYRML 278
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 669 GteaekvVDINTVDGFQGREKDVAIFsCVRANENGQIgflsNSRRMNVGITRAKSSVLVV 728
Cdd:cd21720 279 G------LNVQTVDSSQGSEYDYVIF-CVTADSQHAL----NINRFNVALTRAKRGILVV 327
|
|
| SF1_C |
cd18786 |
C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family ... |
646-729 |
1.35e-08 |
|
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: 52.82 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 646 QLAIISPYNYQVKTFKDRFKEMFGTEAEK-VVDINTVDGFQGREKDVAIFSCVRANENgqigflsNSRRMNVGITRAKSS 724
Cdd:cd18786 12 KGVVLTPYHRDRAYLNQYLQGLSLDEFDLqLVGAITIDSSQGLTFDVVTLYLPTANSL-------TPRRLYVALTRARKR 84
|
....*
gi 1063722804 725 VLVVG 729
Cdd:cd18786 85 LVIYD 89
|
|
| alphaCoV_Nsp13-helicase |
cd21723 |
helicase domain of alphacoronavirus non-structural protein 13; This model represents the ... |
485-734 |
2.86e-07 |
|
helicase domain of alphacoronavirus non-structural protein 13; This model represents the helicase domain of non-structural protein 13 (Nsp13) from alphacoronavirus, including Porcine epidemic diarrhea virus and Human coronavirus (CoV) NL63. 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: 409656 [Multi-domain] Cd Length: 340 Bit Score: 53.20 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 485 DVVIIDEAAQAVE-PATLIPLATRCKQVFLVGDPKQLPA--TVIST-VAQDSGYGTsMFERLQKAGyPVKMLKTQYRMHP 560
Cdd:cd21723 119 DIVVVDEVSMCTNyDLSVINQRVSYKHIVYVGDPQQLPAprTMITRgVLEPKDYNV-VTQRMCALG-PDVFLHKCYRCPA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 561 EIRSFPSKQFYEGALEDGSDIEAQttrdwhkyrCFGPFCFFDIHEGkesqhpgaTGSRVNLDEVEFVLLIYHRLvtmype 640
Cdd:cd21723 197 EIVNTVSELVYENKFKPVHPESKQ---------CFKIFCKGNVQVD--------NGSSINRRQLDVVKMFLAKN------ 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 641 lKSSSQLAIISPYNYQVKTFKdrfkEMFGTEaekvvdINTVDGFQGREKDVAIFScvranENGQIGFLSNSRRMNVGITR 720
Cdd:cd21723 254 -PKWSKAVFISPYNSQNYVAS----RVLGLQ------IQTVDSSQGSEYDYVIYT-----QTSDTAHACNVNRFNVAITR 317
|
250
....*....|....
gi 1063722804 721 AKSSVLVVGSAATL 734
Cdd:cd21723 318 AKKGILCVMCDKEL 331
|
|
| deltaCoV_Nsp13-helicase |
cd21721 |
helicase domain of deltacoronavirus non-structural protein 13; This model represents the ... |
485-728 |
5.31e-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: 52.62 E-value: 5.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 485 DVVIIDEAAQAVEpATLIPLATRC--KQVFLVGDPKQLPA--TVIST---VAQDSGYGTSMferLQKAGYPVkMLKTQYR 557
Cdd:cd21721 119 DIVVVDEVSMLTN-YELSSVNARLvyNHIVYVGDPYQLPSprTMLTTgqlSPADYNVVTDI---MVHAGADV-MLDMCYR 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 558 MHPEIRSFPSKQFYEGALEDGSDIEAQTtrdwhkYRCFGPFCFFDI-HEGKesqhpgatgSRVNLDEVEFVLliyhrlvt 636
Cdd:cd21721 194 CPREIVDTVSKLVYDNKLKAAKPNSRQC------YKTIINNGNNDIaHEGQ---------SAYNEPQLRFAL-------- 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 637 MYPELKSSSQLAIISPYNyqvktfkdrfkEMFGTEAEKVVDINTVDGFQGREKDVAIFsCVRANEngqiGFLSNSRRMNV 716
Cdd:cd21721 251 AFRQYKRWDNVTFISPYN-----------AMNVKAAMAGFSTQTVDSSQGSEYDYVIF-CVTTDS----AHALNMSRLNV 314
|
250
....*....|..
gi 1063722804 717 GITRAKSSVLVV 728
Cdd:cd21721 315 ALTRAKIGILVV 326
|
|
| RecD |
COG0507 |
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
250-305 |
3.43e-06 |
|
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: 50.36 E-value: 3.43e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063722804 250 LNEFFNEN---LNKSQKEAIDVGLSRKSFVLIQGPPGTGKTQTILSILgAIMHATPARV 305
Cdd:COG0507 114 LAALEPRAgitLSDEQREAVALALTTRRVSVLTGGAGTGKTTTLRALL-AALEALGLRV 171
|
|
| DEXSc_RecD-like |
cd17933 |
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ... |
262-305 |
1.70e-04 |
|
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: 42.54 E-value: 1.70e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1063722804 262 QKEAIDVGLSRKsFVLIQGPPGTGKTQTILSILGAImHATPARV 305
Cdd:cd17933 2 QKAAVRLVLRNR-VSVLTGGAGTGKTTTLKALLAAL-EAEGKRV 43
|
|
| AAA_30 |
pfam13604 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
485-589 |
2.01e-04 |
|
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: 43.32 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 485 DVVIIDEAAQAVEP--ATLIPLATRCK-QVFLVGDPKQLPATvistvaqdsGYGtSMFERLQKAGYPVKMLKTQYRM-HP 560
Cdd:pfam13604 90 TLLIVDEAGMVGTRqmARLLKLAEDAGaRVILVGDPRQLPSV---------EAG-GAFRDLLAAGIGTAELTEIVRQrDP 159
|
90 100
....*....|....*....|....*....
gi 1063722804 561 EIRSFpSKQFYEGALEDGsdIEAQTTRDW 589
Cdd:pfam13604 160 WQRAA-SLALRDGDPAEA--LDALADRGR 185
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
250-305 |
4.72e-04 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 42.09 E-value: 4.72e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063722804 250 LNEFFNENLNKSQKEAIDVGLSRKSFVLIQGPPGTGKT-QTILSILGAIMHATPARV 305
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTlAALLPALEALKRGKGGRV 57
|
|
| AAA_30 |
pfam13604 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
258-305 |
2.77e-03 |
|
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: 39.85 E-value: 2.77e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1063722804 258 LNKSQKEAID-VGLSRKSFVLIQGPPGTGKTqTILSILGAIMHATPARV 305
Cdd:pfam13604 2 LNAEQAAAVRaLLTSGDRVAVLVGPAGTGKT-TALKALREAWEAAGYRV 49
|
|
| DExxQc_SF1-N |
cd17914 |
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ... |
277-299 |
3.16e-03 |
|
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: 38.24 E-value: 3.16e-03
|
| McrB |
COG1401 |
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ... |
95-306 |
4.40e-03 |
|
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];
Pssm-ID: 441011 [Multi-domain] Cd Length: 477 Bit Score: 40.52 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 95 ECNEGEGFHFLLVTYEHEEDEYLAQNDLLLLSKEEVKGNSFPSSYGFAVVEHRqnNLLRLRMYLAEDIVQITKNTKSSRT 174
Cdd:COG1401 50 LSEELLRADRAARATELVEELSAALEVVVLLLDLEKVELNEKLALSEAAVAIE--ELYELEADSEIEAVGLLLELAERSD 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722804 175 KSFIQALSNMRSLITSSASPIDKRVFSLKLCGLSTIIREYIALRSVSSLPFKDLIFTAAEKSCGFGDEAwkisgPLNEFF 254
Cdd:COG1401 128 ALEALERARLLLELADLEERAALETEVLEALEAELEELLAAPEDLSADALAAELSAAEELYSEDLESED-----DYLKDL 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1063722804 255 NENLNKSQKEAIDVGLSRKSFVLIQGPPGTGKTQTILSILGAIMHATPARVQ 306
Cdd:COG1401 203 LREKFEETLEAFLAALKTKKNVILAGPPGTGKTYLARRLAEALGGEDNGRIE 254
|
|
| AAA_19 |
pfam13245 |
AAA domain; |
262-295 |
7.76e-03 |
|
AAA domain;
Pssm-ID: 433059 [Multi-domain] Cd Length: 136 Bit Score: 37.58 E-value: 7.76e-03
10 20 30
....*....|....*....|....*....|....
gi 1063722804 262 QKEAIDVGLSRKSFVLIqGPPGTGKTQTILSILG 295
Cdd:pfam13245 1 QREAVRTALPSKVVLLT-GGPGTGKTTTIRHIVA 33
|
|
| recD |
TIGR01447 |
exodeoxyribonuclease V, alpha subunit; This family describes the exodeoxyribonuclease V alpha ... |
251-309 |
9.27e-03 |
|
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: 39.36 E-value: 9.27e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063722804 251 NEFFNENLNKSQKEAIDVGLSRkSFVLIQGPPGTGKTQTILSILGAImhATPARVQSKG 309
Cdd:TIGR01447 138 NLFPLLNEQNWRKTAVALALKS-NFSLITGGPGTGKTTTVARLLLAL--VKQSPKQGKL 193
|
|
| |
