|
Name |
Accession |
Description |
Interval |
E-value |
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
20-1010 |
0e+00 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 922.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 20 TLLYSFRQEISFELDGFQIEACKELESGRGVLVAAPTGAGKTVVGEFAVYLALQRDGKCFYTTPIKALSNQKFQEFSEKY 99
Cdd:COG4581 13 EALADFAEERGFELDPFQEEAILALEAGRSVLVAAPTGSGKTLVAEFAIFLALARGRRSFYTAPIKALSNQKFFDLVERF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 100 GPERVGLLTGDTSINPEAEIVVMTTEVLRNMLYADSNTLRGLSFVVMDEVHYLADKFRGAVWEEVIIHLPDSVQVVSLSA 179
Cdd:COG4581 93 GAENVGLLTGDASVNPDAPIVVMTTEILRNMLYREGADLEDVGVVVMDEFHYLADPDRGWVWEEPIIHLPARVQLVLLSA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 180 TVSNAEEFGGWLDAVRGDTAIIVSEHRPIPLFQHVMVGGRIVDLFAeevsfdeagteqrrealtVNPELLRIArhdratt 259
Cdd:COG4581 173 TVGNAEEFAEWLTRVRGETAVVVSEERPVPLEFHYLVTPRLFPLFR------------------VNPELLRPP------- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 260 ltrsgrggssrrdreefrasrggkahggagrgkgdrrfnnrdgsgtwdgsksrdgagkrdssskweateeaprfnvSRPH 339
Cdd:COG4581 228 ----------------------------------------------------------------------------SRHE 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 340 MIRALEAAGLLPAIVFIFSRKGCDAAVSQCVRSglKLTNDAESREIAAIVDDAAkdlnpSDLDVLGFWSWRDGLINGFAA 419
Cdd:COG4581 232 VIEELDRGGLLPAIVFIFSRRGCDEAAQQLLSA--RLTTKEERAEIREAIDEFA-----EDFSVLFGKTLSRLLRRGIAV 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 420 HHAGMLPVFKEVVEKLFAEGYVHAVFATETLALGVNMPARSVVLEKLVKFNGEEHVQISPGEYTQLTGRAGRRGIDVEGH 499
Cdd:COG4581 305 HHAGMLPKYRRLVEELFQAGLLKVVFATDTLAVGINMPARTVVFTKLSKFDGERHRPLTAREFHQIAGRAGRRGIDTEGH 384
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 500 GVVLWQPGTDPAAVAGLASKRTYPLNSSFRPTYNMSLNLTAQFGRERGRGILESSFAQFQADRSVVGLARKVRGREESLA 579
Cdd:COG4581 385 VVVLAPEHDDPKKFARLASARPEPLRSSFRPSYNMVLNLLARPGLERARELLEDSFAQFQADRSVVGLARRARELERALA 464
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 580 GYAESMKCHLGDFSEYAKLRRELSQAEKEASSSERRMRrgaaaaslegisrgDVLLAKGPRgvtrcvvletsrsLRDPSP 659
Cdd:COG4581 465 GVVERLACDLGDLQEYFALRQPLSPLEALERESPAYAL--------------DVVSVPEAT-------------LEDPRP 517
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 660 TILTEDGkikrlnpleldspvvvherlripnhftgrtpRERRDLASSLRNLLQDkrppkhfsrafsyegsdriEAEITRL 739
Cdd:COG4581 518 VLLAQDR-------------------------------RARGEAAAAMKAAIEY-------------------DERMERL 547
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 740 RKELRHHPCHGCSdreeharwADRWWSLRKETDQLKAQIGGRTNTIAKIYDRVCAVLNHYGYLKLDEemasiadgshary 819
Cdd:COG4581 548 EEVLRPHPLHECP--------LERAFELYRETHPWVRDIELRPKSVARDFDRFCELLREYGYLDDLT------------- 606
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 820 ssagqvpesgtdladpaldaagidgsalISQAGQRLRRIYGerdmlTSLVLESGVMENLDPEELAAFITTLVFQAKREER 899
Cdd:COG4581 607 ----------------------------LTSEGLLLRYLYD-----AAEALRQGVPDDLDPEELAALISWLVEEVRRVDS 653
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 900 MLDVKLPSPGIHDAWDVAVREWSELTDLEEEHHLPQtaaPELGLVWpmfHWARGKDLGDAIKGTDLAAGDFVRWAKQVID 979
Cdd:COG4581 654 SEWERLPSPANRRAFVLVNALFRRLELLERRHGLPE---LDPGLAG---AWASGADLAEVLDATDLDAGDFVRWVRQVID 727
|
970 980 990
....*....|....*....|....*....|.
gi 1110665004 980 SldqlakvqgiSPKFAKNCRRAVDLVRRGVV 1010
Cdd:COG4581 728 P----------DPELRRTARAAVDLIRRGVV 748
|
|
| DEXHc_Mtr4-like |
cd18024 |
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or ... |
27-191 |
7.79e-65 |
|
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or SKIV2L2) is a type II DEAD box helicase that plays a role in the processing of structured RNAs, including the maturation of 5.8S ribosomal RNA (rRNA)and is part of the TRAMP complex that is involved in exosome-mediated degradation of aberrant RNAs. Mtr4 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350782 [Multi-domain] Cd Length: 205 Bit Score: 217.31 E-value: 7.79e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 27 QEISFELDGFQIEACKELESGRGVLVAAPTGAGKTVVGEFAVYLALQRDGKCFYTTPIKALSNQKFQEFSEKYGpeRVGL 106
Cdd:cd18024 27 RTYPFTLDPFQKTAIACIERNESVLVSAHTSAGKTVVAEYAIAQSLRDKQRVIYTSPIKALSNQKYRELQEEFG--DVGL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 107 LTGDTSINPEAEIVVMTTEVLRNMLYADSNTLRGLSFVVMDEVHYLADKFRGAVWEEVIIHLPDSVQVVSLSATVSNAEE 186
Cdd:cd18024 105 MTGDVTINPNASCLVMTTEILRSMLYRGSEIMREVAWVIFDEIHYMRDKERGVVWEETIILLPDKVRYVFLSATIPNARQ 184
|
....*
gi 1110665004 187 FGGWL 191
Cdd:cd18024 185 FAEWI 189
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
31-503 |
1.69e-64 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 227.47 E-value: 1.69e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 31 FELDGFQIEA-CKELESGRGVLVAAPTGAGKTVVGEFAVYLALQRDGKCFYTTPIKALSNQKFQEFSEKYGPE--RVGLL 107
Cdd:COG1204 21 EELYPPQAEAlEAGLLEGKNLVVSAPTASGKTLIAELAILKALLNGGKALYIVPLRALASEKYREFKRDFEELgiKVGVS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 108 TGDTSINPE----AEIVVMTTEVLRNMLYADSNTLRGLSFVVMDEVHYLADKFRGAVWEEVIIHL---PDSVQVVSLSAT 180
Cdd:COG1204 101 TGDYDSDDEwlgrYDILVATPEKLDSLLRNGPSWLRDVDLVVVDEAHLIDDESRGPTLEVLLARLrrlNPEAQIVALSAT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 181 VSNAEEFGGWLDAvrgdtAIIVSEHRPIPLFQHVMVGGRIvdlfaeevSFDEAGTEQRREALTVnpellriarhdrattl 260
Cdd:COG1204 181 IGNAEEIAEWLDA-----ELVKSDWRPVPLNEGVLYDGVL--------RFDDGSRRSKDPTLAL---------------- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 261 trsgrggssrrdreefrasrggkahggagrgkgdrrfnnrdgsgtwdgsksrdgagkrdssskweateeaprfnvsrphM 340
Cdd:COG1204 232 -------------------------------------------------------------------------------A 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 341 IRALEAAGllPAIVFIFSRKGC-DAA--VSQCVRSGLKLTNDAESREIAAIVDDAAKDLNPSdlDVLgfwswRDGLINGF 417
Cdd:COG1204 233 LDLLEEGG--QVLVFVSSRRDAeSLAkkLADELKRRLTPEEREELEELAEELLEVSEETHTN--EKL-----ADCLEKGV 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 418 AAHHAGMLPVFKEVVEKLFAEGYVHAVFATETLALGVNMPARSVVLEKlVKFNGEehVQISPGEYTQLTGRAGRRGIDVE 497
Cdd:COG1204 304 AFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIRD-TKRGGM--VPIPVLEFKQMAGRAGRPGYDPY 380
|
....*.
gi 1110665004 498 GHGVVL 503
Cdd:COG1204 381 GEAILV 386
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
31-203 |
4.53e-60 |
|
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also called SKI2 or DHX13) plays a role in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. SKIV2L belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350785 [Multi-domain] Cd Length: 179 Bit Score: 203.27 E-value: 4.53e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 31 FELDGFQIEACKELESGRGVLVAAPTGAGKTVVGEFAVYLALQRDGKCFYTTPIKALSNQKFQEFSEKYGpeRVGLLTGD 110
Cdd:cd18027 7 FELDVFQKQAILHLEAGDSVFVAAHTSAGKTVVAEYAIALAQKHMTRTIYTSPIKALSNQKFRDFKNTFG--DVGLITGD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 111 TSINPEAEIVVMTTEVLRNMLYADSNTLRGLSFVVMDEVHYLADKFRGAVWEEVIIHLPDSVQVVSLSATVSNAEEFGGW 190
Cdd:cd18027 85 VQLNPEASCLIMTTEILRSMLYNGSDVIRDLEWVIFDEVHYINDAERGVVWEEVLIMLPDHVSIILLSATVPNTVEFADW 164
|
170
....*....|...
gi 1110665004 191 LDAVRGDTAIIVS 203
Cdd:cd18027 165 IGRIKKKNIYVIS 177
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
32-192 |
1.13e-50 |
|
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350679 [Multi-domain] Cd Length: 181 Bit Score: 176.68 E-value: 1.13e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 32 ELDGFQIEACKEL-ESGRGVLVAAPTGAGKTVVGEFAVYLAL-QRDGKCFYTTPIKALSNQKFQEFSEKYGPE--RVGLL 107
Cdd:cd17921 1 LLNPIQREALRALyLSGDSVLVSAPTSSGKTLIAELAILRALaTSGGKAVYIAPTRALVNQKEADLRERFGPLgkNVGLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 108 TGDTSIN----PEAEIVVMTTEVLRNMLYADSNT-LRGLSFVVMDEVHYLADKFRGAVWEEVIIHLP---DSVQVVSLSA 179
Cdd:cd17921 81 TGDPSVNklllAEADILVATPEKLDLLLRNGGERlIQDVRLVVVDEAHLIGDGERGVVLELLLSRLLrinKNARFVGLSA 160
|
170
....*....|...
gi 1110665004 180 TVSNAEEFGGWLD 192
Cdd:cd17921 161 TLPNAEDLAEWLG 173
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
37-503 |
1.55e-43 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 170.14 E-value: 1.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 37 QIEACKE-LESGRGVLVAAPTGAGKTVVGEFAVYLALQRDGKCFYTTPIKALSNQKFQEFS--EKYGPeRVGLLTGDTSI 113
Cdd:PRK02362 28 QAEAVEAgLLDGKNLLAAIPTASGKTLIAELAMLKAIARGGKALYIVPLRALASEKFEEFErfEELGV-RVGISTGDYDS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 114 NPEA----EIVVMTTE----VLRNmlyaDSNTLRGLSFVVMDEVHYLADKFRGAVWEEVIIHL----PDsVQVVSLSATV 181
Cdd:PRK02362 107 RDEWlgdnDIIVATSEkvdsLLRN----GAPWLDDITCVVVDEVHLIDSANRGPTLEVTLAKLrrlnPD-LQVVALSATI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 182 SNAEEFGGWLDAvrgdtAIIVSEHRPIPLFQHVMVGGRIVdlfaeevsFDEagteqrrealtvnpellriarhdrattlt 261
Cdd:PRK02362 182 GNADELADWLDA-----ELVDSEWRPIDLREGVFYGGAIH--------FDD----------------------------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 262 rsgrggssrrdreefrasrggkahggagrgkGDRRFNNRdgsgtwdgSKSRDGAGKRDssskweateeaprfnvsrphmi 341
Cdd:PRK02362 220 -------------------------------SQREVEVP--------SKDDTLNLVLD---------------------- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 342 rALEAAGllPAIVFIFSRKGCDAAVSQCVRSGLKLTNDAESREIAAIVDDAAKDLNPSDLDVLGfwswrDGLINGFAAHH 421
Cdd:PRK02362 239 -TLEEGG--QCLVFVSSRRNAEGFAKRAASALKKTLTAAERAELAELAEEIREVSDTETSKDLA-----DCVAKGAAFHH 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 422 AGMLPVFKEVVEKLFAEGYVHAVFATETLALGVNMPARSVVLEKLVKFNGEEHVQ-ISPGEYTQLTGRAGRRGIDVEGHG 500
Cdd:PRK02362 311 AGLSREHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIRDYRRYDGGAGMQpIPVLEYHQMAGRAGRPGLDPYGEA 390
|
...
gi 1110665004 501 VVL 503
Cdd:PRK02362 391 VLL 393
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
344-505 |
4.00e-41 |
|
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350182 [Multi-domain] Cd Length: 154 Bit Score: 148.08 E-value: 4.00e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 344 LEAAGLLPAIVFIFSRKGCDAAvsqcvrsglkltndaesreiaaivddaAKDLNpsdldvlgfwswrdglinGFAAHHAG 423
Cdd:cd18795 38 ETVSEGKPVLVFCSSRKECEKT---------------------------AKDLA------------------GIAFHHAG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 424 MLPVFKEVVEKLFAEGYVHAVFATETLALGVNMPARSVVLEKLVKFNGEEHVQISPGEYTQLTGRAGRRGIDVEGHGVVL 503
Cdd:cd18795 73 LTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYDGKGYRELSPLEYLQMIGRAGRPGFDTRGEAIIM 152
|
..
gi 1110665004 504 WQ 505
Cdd:cd18795 153 TK 154
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
37-193 |
5.47e-39 |
|
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350786 [Multi-domain] Cd Length: 177 Bit Score: 142.86 E-value: 5.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 37 QIEACKE-LESGRGVLVAAPTGAGKTVVGEFAVYLALQRDGKCFYTTPIKALSNQKFQEFSEKYGPE-RVGLLTGDTSIN 114
Cdd:cd18028 6 QAEAVRAgLLKGENLLISIPTASGKTLIAEMAMVNTLLEGGKALYLVPLRALASEKYEEFKKLEEIGlKVGISTGDYDED 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 115 PE----AEIVVMTTEVLRNMLYADSNTLRGLSFVVMDEVHYLADKFRGAVWEEVII---HLPDSVQVVSLSATVSNAEEF 187
Cdd:cd18028 86 DEwlgdYDIIVATYEKFDSLLRHSPSWLRDVGVVVVDEIHLISDEERGPTLESIVArlrRLNPNTQIIGLSATIGNPDEL 165
|
....*.
gi 1110665004 188 GGWLDA 193
Cdd:cd18028 166 AEWLNA 171
|
|
| DSHCT |
pfam08148 |
DSHCT (NUC185) domain; This C terminal domain is found in DOB1/SK12/helY-like DEAD box ... |
852-1010 |
6.01e-39 |
|
DSHCT (NUC185) domain; This C terminal domain is found in DOB1/SK12/helY-like DEAD box helicases.
Pssm-ID: 462374 Cd Length: 154 Bit Score: 141.82 E-value: 6.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 852 GQRLRRIYGERDMLTSLVLESGVMENLDPEELAAFITTLVFQAKREErmldVKLPSPGIHDAWDvavrewsELTdlEEEH 931
Cdd:pfam08148 7 GRVACEIRSENELLLTELLFSGVFDDLDPEELAALLSAFVFEEKRRE----PYLPSPELAEALR-------LLE--EIAH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 932 HLPQTAAPELGLVWPMFHWARGKDLGDAIKGTDLAAGDFVRWAKQVIDSLDQLAKVQGI--SPKFAKNCRRAVDLVRRGV 1009
Cdd:pfam08148 74 RIAVSRFLDFGLMEVVYAWARGASFAEICKLTDLDEGDIVRLIRRLDELLRQIANAAKIigDPELREKAEEAIELIKRDI 153
|
.
gi 1110665004 1010 V 1010
Cdd:pfam08148 154 V 154
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
37-187 |
7.39e-35 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 130.83 E-value: 7.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 37 QIEACKELESGRGVLVAAPTGAGKTVVGEFAVYLAL---QRDGKCFYTTPIKALSNQKFQEFSEKYGPE--RVGLLTGDT 111
Cdd:pfam00270 4 QAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALdklDNGPQALVLAPTRELAEQIYEELKKLGKGLglKVASLLGGD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 112 SINPEAE------IVVMTTEVLRNMLYaDSNTLRGLSFVVMDEVHYLADKFRGAVWEEVIIHLPDSVQVVSLSATVS-NA 184
Cdd:pfam00270 84 SRKEQLEklkgpdILVGTPGRLLDLLQ-ERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSATLPrNL 162
|
...
gi 1110665004 185 EEF 187
Cdd:pfam00270 163 EDL 165
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
37-503 |
9.41e-35 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 142.65 E-value: 9.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 37 QIEACK-ELESGRGVLVAAPTGAGKTVVGEFA-VYLALQRDGKCFYTTPIKALSNQKFQEFS--EKYGPeRVGLLTGDTS 112
Cdd:PRK00254 28 QAEALKsGVLEGKNLVLAIPTASGKTLVAEIVmVNKLLREGGKAVYLVPLKALAEEKYREFKdwEKLGL-RVAMTTGDYD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 113 INPE----AEIVVMTTEVLRNMLYADSNTLRGLSFVVMDEVHYLADKFRGAVWEEVIIHLPDSVQVVSLSATVSNAEEFG 188
Cdd:PRK00254 107 STDEwlgkYDIIIATAEKFDSLLRHGSSWIKDVKLVVADEIHLIGSYDRGATLEMILTHMLGRAQILGLSATVGNAEELA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 189 GWLDAvrgdtAIIVSEHRPIPLFQHVMVGGrivdlfaeEVSFDEAGTEQrrealtvnpellriarhdrattltrsgrggs 268
Cdd:PRK00254 187 EWLNA-----ELVVSDWRPVKLRKGVFYQG--------FLFWEDGKIER------------------------------- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 269 srrdreeFRASRGGKAHGGAGRGKGDRRFNNrdgsgtwdgsksrdgagKRDSSSKweateeaprfnvsrphmiRALEAAG 348
Cdd:PRK00254 223 -------FPNSWESLVYDAVKKGKGALVFVN-----------------TRRSAEK------------------EALELAK 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 349 LlpaivfifsrkgcdaavsqcVRSGLKLTNDAESREIAAIVDDaakdlNPSDLDVlgfwswRDGLINGFAAHHAGMLPVF 428
Cdd:PRK00254 261 K--------------------IKRFLTKPELRALKELADSLEE-----NPTNEKL------KKALRGGVAFHHAGLGRTE 309
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1110665004 429 KEVVEKLFAEGYVHAVFATETLALGVNMPARSVVLEKLVKFNGEEHVQISPGEYTQLTGRAGRRGIDVEGHGVVL 503
Cdd:PRK00254 310 RVLIEDAFREGLIKVITATPTLSAGINLPAFRVIIRDTKRYSNFGWEDIPVLEIQQMMGRAGRPKYDEVGEAIIV 384
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
31-502 |
7.69e-33 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 136.17 E-value: 7.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 31 FELDGFQIEACKELESGRGVLVAAPTGAGKTVVGEFAVYLALQRDGKCFYTTPIKALSNQKFQEFSE-KYGPERVGLLTG 109
Cdd:PRK01172 21 FELYDHQRMAIEQLRKGENVIVSVPTAAGKTLIAYSAIYETFLAGLKSIYIVPLRSLAMEKYEELSRlRSLGMRVKISIG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 110 DTSINPE----AEIVVMTTEVLRNMLYADSNTLRGLSFVVMDEVHYLADKFRGAVWEEVIIHL----PDsVQVVSLSATV 181
Cdd:PRK01172 101 DYDDPPDfikrYDVVILTSEKADSLIHHDPYIINDVGLIVADEIHIIGDEDRGPTLETVLSSAryvnPD-ARILALSATV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 182 SNAEEFGGWLDAvrgdtAIIVSEHRPIPLFQHVMVGGRivdLFAEevsfdeagtEQRREALTVNpELLRIARHDrattlt 261
Cdd:PRK01172 180 SNANELAQWLNA-----SLIKSNFRPVPLKLGILYRKR---LILD---------GYERSQVDIN-SLIKETVND------ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 262 rsgrggssrrdreefrasrGGKahggagrgkgdrrfnnrdgsgtwdgsksrdgagkrdssskweateeaprfnvsrphmi 341
Cdd:PRK01172 236 -------------------GGQ---------------------------------------------------------- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 342 raleaagllpAIVFIFSRKGCDAAVSQCVRSGLKLTNDAESREIAAIVDDAAKDLNPsdldvlgfwswrdgliNGFAAHH 421
Cdd:PRK01172 239 ----------VLVFVSSRKNAEDYAEMLIQHFPEFNDFKVSSENNNVYDDSLNEMLP----------------HGVAFHH 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 422 AGMLPVFKEVVEKLFAEGYVHAVFATETLALGVNMPARSVVLEKLVKFNGEEHVQISPGEYTQLTGRAGRRGIDVEGHGV 501
Cdd:PRK01172 293 AGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVNLPARLVIVRDITRYGNGGIRYLSNMEIKQMIGRAGRPGYDQYGIGY 372
|
.
gi 1110665004 502 V 502
Cdd:PRK01172 373 I 373
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
31-191 |
1.48e-30 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 119.52 E-value: 1.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 31 FELDGFQIEACKELESG-RGVLVAAPTGAGKTVVGEFAVYLALQRD--GKCFYTTPIKALSNQKFQEFSEKYGP---ERV 104
Cdd:smart00487 7 EPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGkgGRVLVLVPTRELAEQWAEELKKLGPSlglKVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 105 GLLTGDTS-------INPEAEIVVMTTEVLRNMLYADSNTLRGLSFVVMDEVHYLADKFRGAVWEEVIIHLPDSVQVVSL 177
Cdd:smart00487 87 GLYGGDSKreqlrklESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPKNVQLLLL 166
|
170
....*....|....
gi 1110665004 178 SATVSNAEEFGGWL 191
Cdd:smart00487 167 SATPPEEIENLLEL 180
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
47-507 |
1.22e-25 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 114.22 E-value: 1.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 47 GRGVLVAAPTGAGKTVVGEFA-VYLALQRDGKCFYTTPIKALSNQKFQEFSEKYGPE-----RVG---LLTGDTSINPEA 117
Cdd:COG1202 225 GKDQLVVSATATGKTLIGELAgIKNALEGKGKMLFLVPLVALANQKYEDFKDRYGDGldvsiRVGasrIRDDGTRFDPNA 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 118 EIVVMTTEVLRNMLYAdSNTLRGLSFVVMDEVHYLADKFRGAVWEEVIIHL----PDSvQVVSLSATVSNAEEFGGWLDA 193
Cdd:COG1202 305 DIIVGTYEGIDHALRT-GRDLGDIGTVVIDEVHMLEDPERGHRLDGLIARLkyycPGA-QWIYLSATVGNPEELAKKLGA 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 194 vrgdtAIIVSEHRPIPLFQHVmvggrivdLFAEEvsfdeagteqrREALtvnpellriarhDRATTLTrsgrggssrrdR 273
Cdd:COG1202 383 -----KLVEYEERPVPLERHL--------TFADG-----------REKI------------RIINKLV-----------K 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 274 EEFrASRGGKAHggagRGKgdrrfnnrdgsgtwdgsksrdgagkrdssskweateeaprfnvsrphmiraleaagllpAI 353
Cdd:COG1202 416 REF-DTKSSKGY----RGQ-----------------------------------------------------------TI 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 354 VFIFSRKGCdaavsqcvrsglkltndaesREIAaivddaakdlnpsdlDVLGFWSwrdglingfAAHHAGMLPVFKEVVE 433
Cdd:COG1202 432 IFTNSRRRC--------------------HEIA---------------RALGYKA---------APYHAGLDYGERKKVE 467
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1110665004 434 KLFAEGYVHAVFATETLALGVNMPARSVVLEKLVKfnGEEhvQISPGEYTQLTGRAGRRGIDVEGHGVVLWQPG 507
Cdd:COG1202 468 RRFADQELAAVVTTAALAAGVDFPASQVIFDSLAM--GIE--WLSVQEFHQMLGRAGRPDYHDRGKVYLLVEPG 537
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
44-207 |
2.51e-24 |
|
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350781 [Multi-domain] Cd Length: 206 Bit Score: 101.66 E-value: 2.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 44 LESGRGVLVAAPTGAGKTVVGEFAVYLALQR-------DGKCFYTTPIKALSNQKFQEFSEKYGPE--RVGLLTGDTSIN 114
Cdd:cd18023 14 LYSDKNFVVSAPTGSGKTVLFELAILRLLKErnplpwgNRKVVYIAPIKALCSEKYDDWKEKFGPLglSCAELTGDTEMD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 115 PEAEI----VVMTT-EVLRNM--LYADSNTL-RGLSFVVMDEVHYLADkFRGAVWEEVI-----IHLP--------DSVQ 173
Cdd:cd18023 94 DTFEIqdadIILTTpEKWDSMtrRWRDNGNLvQLVALVLIDEVHIIKE-NRGATLEVVVsrmktLSSSselrgstvRPMR 172
|
170 180 190
....*....|....*....|....*....|....
gi 1110665004 174 VVSLSATVSNAEEFGGWLDAVRGDTAIIVSEHRP 207
Cdd:cd18023 173 FVAVSATIPNIEDLAEWLGDNPAGCFSFGESFRP 206
|
|
| DEXHc_DDX60 |
cd18025 |
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ... |
34-206 |
5.11e-22 |
|
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an IFN-inducible cytoplasmic helicase that plays a role in RIG-I-mediated type I interferon (IFN) nuclease-mediated viral RNA degradation. DDX60 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350783 [Multi-domain] Cd Length: 192 Bit Score: 94.74 E-value: 5.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 34 DGFQIEACKELESGRGVLVAAPTGAGKTVVGEFAVYLALQR--DGKCFYTTPIKALSNQKFQE----FSEKYGPER---V 104
Cdd:cd18025 3 DAWQRELLDIVDRRESALIVAPTSSGKTFISYYCMEKVLREsdDGVVVYVAPTKALVNQVVAEvyarFSKKYPPSGkslW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 105 GLLTGDTSINP--EAEIVVMTTEVLRNMLYADSNT--LRGLSFVVMDEVHYLADKFRGAVWEEVIIHLPdsVQVVSLSAT 180
Cdd:cd18025 83 GVFTRDYRHNNpmNCQVLITVPECLEILLLSPHNAswVPRIKYVIFDEIHSIGQSEDGAVWEQLLLLIP--CPFLALSAT 160
|
170 180 190
....*....|....*....|....*....|
gi 1110665004 181 VSNAEEFGGWLDAVR----GDTAIIVSEHR 206
Cdd:cd18025 161 IGNPQKFHEWLQSVQrarkAELKKIEHNHR 190
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
47-180 |
1.77e-20 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 89.00 E-value: 1.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 47 GRGVLVAAPTGAGKTVVGE-FAVYLALQRDGKCFYTTPIKALSNQKFQEFSEKYGP-ERVGLLTGDTS-------INPEA 117
Cdd:cd00046 1 GENVLITAPTGSGKTLAALlAALLLLLKKGKKVLVLVPTKALALQTAERLRELFGPgIRVAVLVGGSSaeereknKLGDA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1110665004 118 EIVVMTTEVLRN-MLYADSNTLRGLSFVVMDEVHYLADKFRGAVWEEVIIH--LPDSVQVVSLSAT 180
Cdd:cd00046 81 DIIIATPDMLLNlLLREDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRkaGLKNAQVILLSAT 146
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
47-191 |
1.52e-19 |
|
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from 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: 350680 [Multi-domain] Cd Length: 166 Bit Score: 86.87 E-value: 1.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 47 GRGVLVAAPTGAGKTVVGEFAVYLALQRDG----KCFYTTPIKALSNQKF---QEFSEKYGPE-RVGLLTGDTS------ 112
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPekgvQVLYISPLKALINDQErrlEEPLDEIDLEiPVAVRHGDTSqsekak 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 113 --INPEaEIVVMTTEVLRNMLY--ADSNTLRGLSFVVMDEVHYLADKFRGAVWE---EVIIHLPD-SVQVVSLSATVSNA 184
Cdd:cd17922 81 qlKNPP-GILITTPESLELLLVnkKLRELFAGLRYVVVDEIHALLGSKRGVQLElllERLRKLTGrPLRRIGLSATLGNL 159
|
....*..
gi 1110665004 185 EEFGGWL 191
Cdd:cd17922 160 EEAAAFL 166
|
|
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
50-191 |
2.29e-18 |
|
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; Activating signal cointegrator 1 complex subunit 3 (ASCC3) is a type II DEAD box helicase that plays a role in the repair of N-alkylated nucleotides. ASCC3 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350780 [Multi-domain] Cd Length: 189 Bit Score: 83.96 E-value: 2.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 50 VLVAAPTGAGKTVVGEFAVYLALQR--DGKCFYTTPIKALSNQKFQE----FSEKYGpERVGLLTGDTSINPE----AEI 119
Cdd:cd18022 20 VLLGAPTGSGKTIAAELAMFRAFNKypGSKVVYIAPLKALVRERVDDwkkrFEEKLG-KKVVELTGDVTPDMKaladADI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 120 VVMTTE----VLRNmlYADSNTLRGLSFVVMDEVHYLADKfRGAVWeEVII--------HLPDSVQVVSLSATVSNAEEF 187
Cdd:cd18022 99 IITTPEkwdgISRS--WQTREYVQQVSLIIIDEIHLLGSD-RGPVL-EVIVsrmnyissQTEKPVRLVGLSTALANAGDL 174
|
....
gi 1110665004 188 GGWL 191
Cdd:cd18022 175 ANWL 178
|
|
| DEXH_lig_assoc |
TIGR04121 |
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ... |
36-207 |
2.46e-17 |
|
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box helicases found associated with a bacterial ATP-dependent DNA ligase, part of a four-gene system that occurs in about 12 % of prokaryotic reference genomes. The actual motif in this family is DE[VILW]H.
Pssm-ID: 274994 [Multi-domain] Cd Length: 804 Bit Score: 87.22 E-value: 2.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 36 FQIEACKELESGRGVLVAAPTGAGKTVVGEFAVYLALQRDG-------KCFYTTPIKALSN---QKFQEFSEKYG-PERV 104
Cdd:TIGR04121 17 FQLEMWAAALEGRSGLLIAPTGSGKTLAGFLPSLIDLAGPEapkekglHTLYITPLRALAVdiaRNLQAPIEELGlPIRV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 105 GLLTGDTSINPEA-------EIVVMTTEVLRNML-YADSNTL-RGLSFVVMDEVHYLADKFRGAVWEEVIIHL----PDs 171
Cdd:TIGR04121 97 ETRTGDTSSSERArqrkkppDILLTTPESLALLLsYPDAARLfKDLRCVVVDEWHELAGSKRGDQLELALARLrrlaPG- 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 1110665004 172 VQVVSLSATVSNAEEFGGWLDAVRGDTAIIVSEHRP 207
Cdd:TIGR04121 176 LRRWGLSATIGNLEEARRVLLGVGGAPAVLVRGKLP 211
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
50-193 |
5.76e-17 |
|
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350779 [Multi-domain] Cd Length: 191 Bit Score: 79.99 E-value: 5.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 50 VLVAAPTGAGKTVVGEFAVYLALQR--DGKCFYTTPIKALSNQKFQEFSEKYGP---ERVGLLTGDTSINPE----AEIV 120
Cdd:cd18021 22 VFVGAPTGSGKTVCAELALLRHWRQnpKGRAVYIAPMQELVDARYKDWRAKFGPllgKKVVKLTGETSTDLKllakSDVI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 121 VMTTE---VL------RNMlyadsntLRGLSFVVMDEVHYLADkFRGAVWEEVI-------IHLPDSVQVVSLSATVSNA 184
Cdd:cd18021 102 LATPEqwdVLsrrwkqRKN-------VQSVELFIADELHLIGG-ENGPVYEVVVsrmryisSQLEKPIRIVGLSSSLANA 173
|
....*....
gi 1110665004 185 EEFGGWLDA 193
Cdd:cd18021 174 RDVGEWLGA 182
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
37-188 |
1.68e-15 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350681 [Multi-domain] Cd Length: 182 Bit Score: 75.70 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 37 QIEACKELESGRGVLVAAPTGAGKTVVGEFAVYLALQRD--GKCFYTTPIKALSN---QKFQEFSEKYGPE-RVGLLTGD 110
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDpgSRALYLYPTKALAQdqlRSLRELLEQLGLGiRVATYDGD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 111 TSINP-------EAEIVVMTTEVLRNML----YADSNTLRGLSFVVMDEVHYladkFRGAVWEEV---------IIHLPD 170
Cdd:cd17923 85 TPREErraiirnPPRILLTNPDMLHYALlphhDRWARFLRNLRYVVLDEAHT----YRGVFGSHValllrrlrrLCRRYG 160
|
170
....*....|....*....
gi 1110665004 171 S-VQVVSLSATVSNAEEFG 188
Cdd:cd17923 161 AdPQFILTSATIGNPAEHA 179
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
36-207 |
2.75e-15 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 80.92 E-value: 2.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 36 FQIEACKELESGRGVLVAAPTGAGKTvvgeFAVYL-ALQR-----------DG-KCFYTTPIKALSN-------QKFQEF 95
Cdd:COG1201 28 PQREAWPAIAAGESTLLIAPTGSGKT----LAAFLpALDElarrprpgelpDGlRVLYISPLKALANdiernlrAPLEEI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 96 SEKYGPE----RVGLLTGDTSI--------NPeAEIVVMTTEVLRNML-YADS-NTLRGLSFVVMDEVHYLADKFRGAvw 161
Cdd:COG1201 104 GEAAGLPlpeiRVGVRTGDTPAserqrqrrRP-PHILITTPESLALLLtSPDArELLRGVRTVIVDEIHALAGSKRGV-- 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1110665004 162 eeviiHL-----------PDSVQVVSLSATVSNAEEFGGWL--DAVRGDTAIIVSEHRP 207
Cdd:COG1201 181 -----HLalslerlralaPRPLQRIGLSATVGPLEEVARFLvgYEDPRPVTIVDAGAGK 234
|
|
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
44-207 |
2.36e-14 |
|
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in the repair of genomic double-strand breaks (DSBs). POLQ contains an N-terminal type II DEAD box helicase domain which contains the ATP-binding region.
Pssm-ID: 350784 [Multi-domain] Cd Length: 202 Bit Score: 73.02 E-value: 2.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 44 LESGRGVLVAAPTGAGKTVVGE-FAVYLALQRDGKCFYTTPIKALSNQK---FQEFSEKYGpERVGLLTGDTSINP---- 115
Cdd:cd18026 30 LLEGRNLVYSLPTSGGKTLVAEiLMLKRLLERRKKALFVLPYVSIVQEKvdaLSPLFEELG-FRVEGYAGNKGRSPpkrr 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 116 -EAEIVVMTTE---VLRNMLYADsNTLRGLSFVVMDEVHYLADKFRGAVWEEVIIHL----PDSVQVVSLSATVSNAEEF 187
Cdd:cd18026 109 kSLSVAVCTIEkanSLVNSLIEE-GRLDELGLVVVDELHMLGDGHRGALLELLLTKLlyaaQKNIQIVGMSATLPNLEEL 187
|
170 180
....*....|....*....|
gi 1110665004 188 GGWLDAvrgdtAIIVSEHRP 207
Cdd:cd18026 188 ASWLRA-----ELYTTNFRP 202
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
36-199 |
7.46e-13 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 72.95 E-value: 7.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 36 FQIEACKELESGRGVLVAAPTGAGKTVvgefaVYL--ALQ-----RDGKCFYTTPIKALSN---QKFQEFSEKYGPE-RV 104
Cdd:COG1205 60 HQAEAIEAARAGKNVVIATPTASGKSL-----AYLlpVLEalledPGATALYLYPTKALARdqlRRLRELAEALGLGvRV 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 105 GLLTGDTS------INPEAEIVVMTTEVL-RNMLYAD---SNTLRGLSFVVMDEVHYladkFRGavweeV-------II- 166
Cdd:COG1205 135 ATYDGDTPpeerrwIREHPDIVLTNPDMLhYGLLPHHtrwARFFRNLRYVVIDEAHT----YRG-----VfgshvanVLr 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1110665004 167 -------HLPDSVQVVSLSATVSNAEEFGGWL-----DAVRGDTA 199
Cdd:COG1205 206 rlrricrHYGSDPQFILASATIGNPAEHAERLtgrpvTVVDEDGS 250
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
26-180 |
1.43e-12 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 71.59 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 26 RQEISFELDGFQIEACKEL------ESGRGVLVAaPTGAGKTVVGEFAVYlALQRDGKCFYTTPIKALSNQKFQEFSEKY 99
Cdd:COG1061 74 ASGTSFELRPYQQEALEALlaalerGGGRGLVVA-PTGTGKTVLALALAA-ELLRGKRVLVLVPRRELLEQWAEELRRFL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 100 GPERVglltGDTSINPEAEIVVMTTEVLRNMLYADsNTLRGLSFVVMDEVHYLAdkfrGAVWEEVIIHLPDSVqVVSLSA 179
Cdd:COG1061 152 GDPLA----GGGKKDSDAPITVATYQSLARRAHLD-ELGDRFGLVIIDEAHHAG----APSYRRILEAFPAAY-RLGLTA 221
|
.
gi 1110665004 180 T 180
Cdd:COG1061 222 T 222
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
37-180 |
1.83e-11 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 63.46 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 37 QIEACKELESG-----RGVLVAAPTGAGKTVVGEFAVYLALQRDG--KCFYTTPIKALSNQ---KFQEFSEKYgPERVGL 106
Cdd:pfam04851 8 QIEAIENLLESikngqKRGLIVMATGSGKTLTAAKLIARLFKKGPikKVLFLVPRKDLLEQaleEFKKFLPNY-VEIGEI 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1110665004 107 LTGDT--SINPEAEIVVMTTEVLRNMLYADSNTLRGLSF--VVMDEVHYLADKFrgavWEEVIIHLPDSVQvVSLSAT 180
Cdd:pfam04851 87 ISGDKkdESVDDNKIVVTTIQSLYKALELASLELLPDFFdvIIIDEAHRSGASS----YRNILEYFKPAFL-LGLTAT 159
|
|
| DEXHc_Brr2_1 |
cd18019 |
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ... |
44-191 |
3.60e-11 |
|
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350777 [Multi-domain] Cd Length: 214 Bit Score: 63.93 E-value: 3.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 44 LESGRGVLVAAPTGAGKTVVGEFAVYLALQ----RDG-------KCFYTTPIKALSNQKFQEFSEKYGPE--RVGLLTGD 110
Cdd:cd18019 30 FETDENLLLCAPTGAGKTNVALLTILREIGkhrnPDGtinldafKIVYIAPMKALVQEMVGNFSKRLAPYgiTVAELTGD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 111 TSINPE----AEIVVMTTE----VLRNMLYADSNTLRGLsfVVMDEVHYLADKfRGAVWEEVIIHL-------PDSVQVV 175
Cdd:cd18019 110 QQLTKEqiseTQIIVTTPEkwdiITRKSGDRTYTQLVRL--IIIDEIHLLHDD-RGPVLESIVARTirqieqtQEYVRLV 186
|
170
....*....|....*.
gi 1110665004 176 SLSATVSNAEEFGGWL 191
Cdd:cd18019 187 GLSATLPNYEDVATFL 202
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
37-186 |
2.04e-10 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 64.91 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 37 QIEACKELESGRGVLVAAPTGAGKTVvgefAVYLA-------LQRDGK------CFYTTPIKALSN----------QKFQ 93
Cdd:PRK13767 37 QRYAIPLIHEGKNVLISSPTGSGKTL----AAFLAiidelfrLGREGEledkvyCLYVSPLRALNNdihrnleeplTEIR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 94 EFSEKYGPE----RVGLLTGDTSINPEAE-------IVVMTTEVLRNMLYAD--SNTLRGLSFVVMDEVHYLADKFRGAv 160
Cdd:PRK13767 113 EIAKERGEElpeiRVAIRTGDTSSYEKQKmlkkpphILITTPESLAILLNSPkfREKLRTVKWVIVDEIHSLAENKRGV- 191
|
170 180 190
....*....|....*....|....*....|....*..
gi 1110665004 161 weeviiHLPDSV-----------QVVSLSATVSNAEE 186
Cdd:PRK13767 192 ------HLSLSLerleelaggefVRIGLSATIEPLEE 222
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
36-180 |
7.51e-10 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 58.47 E-value: 7.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 36 FQIEACKEL----ESGRGVLVAaPTGAGKTVVGefavyLALQRD---GKCFYTTPIKALSNQKFQEFSEKYGPERVGLLT 108
Cdd:cd17926 4 YQEEALEAWlahkNNRRGILVL-PTGSGKTLTA-----LALIAYlkeLRTLIVVPTDALLDQWKERFEDFLGDSSIGLIG 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1110665004 109 GDTSI-NPEAEIVVMTTEVLRNMLYADSNTLRGLSFVVMDEVHYLADKFrgavWEEVIIHLPDSVQvVSLSAT 180
Cdd:cd17926 78 GGKKKdFDDANVVVATYQSLSNLAEEEKDLFDQFGLLIVDEAHHLPAKT----FSEILKELNAKYR-LGLTAT 145
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
50-183 |
7.69e-10 |
|
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; Activating signal cointegrator 1 complex subunit 3 (ASCC3) is a type II DEAD box helicase that plays a role in the repair of N-alkylated nucleotides. ASCC3 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350778 [Multi-domain] Cd Length: 199 Bit Score: 59.75 E-value: 7.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 50 VLVAAPTGAGKTVVGEFAV----------YLALQRDG-KCFYTTPIKALSNQKFQEFSEKYGP--ERVGLLTGDTSINP- 115
Cdd:cd18020 20 MLICAPTGAGKTNIAMLTIlheirqhvnqGGVIKKDDfKIVYIAPMKALAAEMVEKFSKRLAPlgIKVKELTGDMQLTKk 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 116 ---EAEIVVMTTE---VLRNMLYADSNTLRGLSFVVMDEVHYLADKfRGAVWEEVIIHLPDSVQ-------VVSLSATVS 182
Cdd:cd18020 100 eiaETQIIVTTPEkwdVVTRKSSGDVALSQLVRLLIIDEVHLLHDD-RGPVIESLVARTLRQVEstqsmirIVGLSATLP 178
|
.
gi 1110665004 183 N 183
Cdd:cd18020 179 N 179
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
37-184 |
8.52e-10 |
|
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350669 [Multi-domain] Cd Length: 196 Bit Score: 59.38 E-value: 8.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 37 QIEACKELESGRGVLVAAPTGAGKTvvgefAVYL--ALQR--DGKCFYTTPIKA--------LSNQKFQEFSE--KYGPE 102
Cdd:cd00268 17 QAQAIPLILSGRDVIGQAQTGSGKT-----LAFLlpILEKllPEPKKKGRGPQAlvlaptreLAMQIAEVARKlgKGTGL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 103 RVGLLTGDTSINPEAE-------IVVMTTEVLRNMLYADSNTLRGLSFVVMDEvhylADK-----FRGAVwEEVIIHLPD 170
Cdd:cd00268 92 KVAAIYGGAPIKKQIEalkkgpdIVVGTPGRLLDLIERGKLDLSNVKYLVLDE----ADRmldmgFEEDV-EKILSALPK 166
|
170
....*....|....
gi 1110665004 171 SVQVVSLSATVSNA 184
Cdd:cd00268 167 DRQTLLFSATLPEE 180
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
31-183 |
8.41e-09 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350685 [Multi-domain] Cd Length: 201 Bit Score: 56.67 E-value: 8.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 31 FELDGFQIEACKELESGRGVLVAAPTGAGKTVVgefAVYLA--------LQRDGKCFYTTPIKALSNQKFQEFSEKYG-- 100
Cdd:cd17927 1 FKPRNYQLELAQPALKGKNTIICLPTGSGKTFV---AVLICehhlkkfpAGRKGKVVFLANKVPLVEQQKEVFRKHFErp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 101 PERVGLLTGDTSINPEAE-------IVVMTTEVLRNMLYADSNT-LRGLSFVVMDEVH--------------YLADKFRG 158
Cdd:cd17927 78 GYKVTGLSGDTSENVSVEqivessdVIIVTPQILVNDLKSGTIVsLSDFSLLVFDECHnttknhpyneimfrYLDQKLGS 157
|
170 180
....*....|....*....|....*
gi 1110665004 159 AvweeviIHLPdsvQVVSLSATVSN 183
Cdd:cd17927 158 S------GPLP---QILGLTASPGV 173
|
|
| SF2_C_suv3 |
cd18805 |
C-terminal helicase domain of ATP-dependent RNA helicase; The SUV3 (suppressor of Var 3) gene ... |
446-502 |
1.38e-08 |
|
C-terminal helicase domain of ATP-dependent RNA helicase; The SUV3 (suppressor of Var 3) gene encodes a DNA and RNA helicase, which is localized in mitochondria and is a subunit of the degradosome complex involved in regulation of RNA surveillance and turnover. SUV3 exhibits DNA and RNA-dependent ATPase, DNA and RNA-binding and DNA and RNA unwinding activities. SUV3 is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350192 [Multi-domain] Cd Length: 135 Bit Score: 54.49 E-value: 1.38e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1110665004 446 ATETLALGVNMPARSVVLEKLVKFNGEEHVQISPGEYTQLTGRAGRRGIDVEgHGVV 502
Cdd:cd18805 76 ASDAIGMGLNLNIRRVIFSSLSKFDGNEMRPLSPSEVKQIAGRAGRFGSHFP-EGEV 131
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
52-200 |
1.64e-08 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 58.78 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 52 VAAPTGAGKTVVGEFAVYLALQRDG-------------KCFYTTPIKALSNQKFQEFS---EKYGPER-----------V 104
Cdd:PRK09751 1 VIAPTGSGKTLAAFLYALDRLFREGgedtreahkrktsRILYISPIKALGTDVQRNLQiplKGIADERrrrgetevnlrV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 105 GLLTGDTSINPEA-------EIVVMTTEVLRNMLYADS-NTLRGLSFVVMDEVHYLADKFRGA----VWEEVIIHLPDSV 172
Cdd:PRK09751 81 GIRTGDTPAQERSkltrnppDILITTPESLYLMLTSRArETLRGVETVIIDEVHAVAGSKRGAhlalSLERLDALLHTSA 160
|
170 180
....*....|....*....|....*...
gi 1110665004 173 QVVSLSATVSNAEEFGGWLDAVRGDTAI 200
Cdd:PRK09751 161 QRIGLSATVRSASDVAAFLGGDRPVTVV 188
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
416-493 |
2.37e-08 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 52.21 E-value: 2.37e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1110665004 416 GFAAHHAGMLPVFKEVVEKLFAEGYVHAVFATETLALGVNMP-ARSVVLeklvkfngeEHVQISPGEYTQLTGRAGRRG 493
Cdd:smart00490 13 KVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVII---------YDLPWSPASYIQRIGRAGRAG 82
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
51-156 |
1.39e-07 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 55.51 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 51 LVAAPTGAGKTVVGEFAVYLALQR-DGKCFYTTPIKALSNQKFQEFSE--KYGPERVGLLTGDTSINP------EAEIVV 121
Cdd:COG1111 21 LVVLPTGLGKTAVALLVIAERLHKkGGKVLFLAPTKPLVEQHAEFFKEalNIPEDEIVVFTGEVSPEKrkelweKARIIV 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1110665004 122 MTTEVLRNMLYADSNTLRGLSFVVMDEVH---------YLADKF 156
Cdd:COG1111 101 ATPQVIENDLIAGRIDLDDVSLLIFDEAHravgnyayvYIAERY 144
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
36-171 |
1.92e-07 |
|
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef 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: 350793 [Multi-domain] Cd Length: 181 Bit Score: 52.13 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 36 FQIEACKELESGRgVLVAAPTGAGKTVVGEFAVYLALQR-DGKCFYTTPIKALSNQKFQEFSEKYG-PERVGLLTGDTSI 113
Cdd:cd18035 6 YQVLIAAVALNGN-TLIVLPTGLGKTIIAILVAADRLTKkGGKVLILAPSRPLVEQHAENLKRVLNiPDKITSLTGEVKP 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1110665004 114 NPEAE------IVVMTTEVLRNMLYADSNTLRGLSFVVMDEVH---------YLADKFRGAVWEEVIIHLPDS 171
Cdd:cd18035 85 EERAErwdaskIIVATPQVIENDLLAGRITLDDVSLLIFDEAHhavgnyayvYIAHRYKREANNPLILGLTAS 157
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
50-180 |
5.37e-07 |
|
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase responsible for degradation of dsDNA. The two enzymatic units of Cas3, a histidine-aspartate (HD) nuclease and a Superfamily 2 (SF2) helicase, may be expressed from separate genes as Cas3' (SF2 helicase) and Cas3'' (HD nuclease) or may be fused as a single HD-SF2 polypeptide. The nucleolytic activity of most Cas3 enzymes is transition metal ion-dependent. Cas3 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: 350688 [Multi-domain] Cd Length: 186 Bit Score: 51.14 E-value: 5.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 50 VLVAAPTGAGKTvvgEFAVYLALQ-----RDGKCFYTTPIKALSNQKFQEFSEKYGPER----VGLLTGDTSINPE---- 116
Cdd:cd17930 4 VILEAPTGSGKT---EAALLWALKlaargGKRRIIYALPTRATINQMYERIREILGRLDdedkVLLLHSKAALELLesde 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 117 ---------------------AEIVVMTT-EVLRNMLYADSNTLRGL----SFVVMDEVHYLADKFrgavWEEVIIHLPD 170
Cdd:cd17930 81 epdddpveavdwalllkrswlAPIVVTTIdQLLESLLKYKHFERRLHglanSVVVLDEVQAYDPEY----MALLLKALLE 156
|
170
....*....|....*
gi 1110665004 171 -----SVQVVSLSAT 180
Cdd:cd17930 157 llgelGGPVVLMTAT 171
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
31-182 |
9.21e-07 |
|
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) 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: 350794 [Multi-domain] Cd Length: 204 Bit Score: 50.55 E-value: 9.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 31 FELDGFQIEACKELESGRGVLVAAPTGAGKTVVgefAVYLALQ---------RDGK-CFYTTPIKALSNQKFQEFSEKYG 100
Cdd:cd18036 1 LELRNYQLELVLPALRGKNTIICAPTGSGKTRV---AVYICRHhlekrrsagEKGRvVVLVNKVPLVEQQLEKFFKYFRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 101 PERVGLLTGDTSIN----PEAE---IVVMTTEVLRNMLYA----DSNTLRGLSFVVMDEVHYLA-----DKFRGAVWEEV 164
Cdd:cd18036 78 GYKVTGLSGDSSHKvsfgQIVKasdVIICTPQILINNLLSgreeERVYLSDFSLLIFDECHHTQkehpyNKIMRMYLDKK 157
|
170
....*....|....*...
gi 1110665004 165 IIHLPDSVQVVSLSATVS 182
Cdd:cd18036 158 LSSQGPLPQILGLTASPG 175
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
31-150 |
1.03e-06 |
|
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350676 [Multi-domain] Cd Length: 180 Bit Score: 50.11 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 31 FELDGFQIEACKELESG------RGVLVAAPTGAGKTVVGEFAVYLALQRDGKCFYTTPIKALSNQKFQEFSEKYGPERV 104
Cdd:cd17918 14 FSLTKDQAQAIKDIEKDlhspepMDRLLSGDVGSGKTLVALGAALLAYKNGKQVAILVPTEILAHQHYEEARKFLPFINV 93
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1110665004 105 GLLTGDT--SINPEAEIVVMTTEVlrnmLYADSNTLRgLSFVVMDEVH 150
Cdd:cd17918 94 ELVTGGTkaQILSGISLLVGTHAL----LHLDVKFKN-LDLVIVDEQH 136
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
5-150 |
3.39e-06 |
|
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 440816 [Multi-domain] Cd Length: 535 Bit Score: 50.85 E-value: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 5 AERYAAAKIRAAEAKTLLYSFRQEISfeldgfqiEACKEL--ESGRGVLVAAPTGAGKTvvgEFAVYLAL-----QRDGK 77
Cdd:COG1203 111 AERLERLLPKKSKPRTPINPLQNEAL--------ELALEAaeEEPGLFILTAPTGGGKT---EAALLFALrlaakHGGRR 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 78 CFYTTPIKALSNQKFQEFSEKYGPErVGLLTGDTSINPE---------------------AEIVVMTTEVLRNMLYAD-- 134
Cdd:COG1203 180 IIYALPFTSIINQTYDRLRDLFGED-VLLHHSLADLDLLeeeeeyesearwlkllkelwdAPVVVTTIDQLFESLFSNrk 258
|
170 180
....*....|....*....|
gi 1110665004 135 SNTLRGL----SFVVMDEVH 150
Cdd:COG1203 259 GQERRLHnlanSVIILDEVQ 278
|
|
| DEXHc_RIG-I_DDX58 |
cd18073 |
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called ... |
31-186 |
6.25e-06 |
|
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called DEAD box protein 58 (DDX58), is a pathogen-recognition receptor that recognizes viral 5'-triphosphates carrying double-stranded RNA. Upon binding to these microbe-associated molecular patterns (MAMPs), RIG-I forms oligomers and promotes downstream processes that result in type I interferon production and induction of an antiviral state. The optimal ligand for RIG-I has been found to be base-paired or double-stranded RNA (dsRNA) molecules containing a 5' triphosphate (5'-ppp-dsRNA). RIG-I contains two N-terminal caspase activation and recruitment domains (CARDs), which are required for interaction with IPS-1, a superfamily 2 helicase/translocase/ATPase (SF2) domain and a C-terminal regulatory/repressor domain (RD). RIG-I 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: 350831 [Multi-domain] Cd Length: 202 Bit Score: 48.28 E-value: 6.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 31 FELDGFQIEACKELESGRGVLVAAPTGAGKTVVGEFAVYLALQ-----RDGK-CFYTTPIKALSNQK--FQEFSEKYGpE 102
Cdd:cd18073 1 FKPRNYQLELALPAMKGKNTIICAPTGCGKTFVSLLICEHHLKkfpqgQKGKvVFFATKVPVYEQQKsvFSKYFERHG-Y 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 103 RVGLLTGDTSIN-------PEAEIVVMTTEVLRNMLyaDSNTLRGLS-FVVM--DEVH--------------YLADKFRG 158
Cdd:cd18073 80 RVTGISGATAENvpveqiiENNDIIILTPQILVNNL--KKGTIPSLSiFTLMifDECHntsgnhpynmimfrYLDQKLGG 157
|
170 180 190
....*....|....*....|....*....|...
gi 1110665004 159 AVweeviIHLPdsvQVVSLSATV-----SNAEE 186
Cdd:cd18073 158 SS-----GPLP---QIIGLTASVgvgdaKNTDE 182
|
|
| rRNA_proc-arch |
pfam13234 |
rRNA-processing arch domain; Mtr4 is the essential RNA helicase, and is an exosome-activating ... |
550-778 |
7.89e-06 |
|
rRNA-processing arch domain; Mtr4 is the essential RNA helicase, and is an exosome-activating cofactor. This arch domain is carried in Mtr4 and Ski2 (the cytosolic homolog of Mtr4). The arch domain is required for proper 5.8S rRNA processing, and appears to function independently of canonical helicase activity.
Pssm-ID: 463813 Cd Length: 267 Bit Score: 48.82 E-value: 7.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 550 ILESSFAQFQADRSVVGLARKVRGREESLAgyaeSMKC-HLGDFSEYAKLRRELSQAEKEASS----------------- 611
Cdd:pfam13234 3 MLKRSFSQFQNQASLPELEKKLKELEKELA----SIKIpDEEDIKEYYDLRQQLEKLNEDIREvilhppyglpflqpgrl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 612 -----------------SERRMRRGAAAASLEGISRGDVLLakgprgvtrCVVLETSRSLRDPSPTILTEDgkIKRLNPL 674
Cdd:pfam13234 79 vvvkdngdqdfgwgvvvNFKKRKKNGKAEPPQESYIVDVLL---------VLALVSSPEDLDKFNDVNPEG--FRPAPPG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 675 ELDSPVVV-----------HERLRIPNhfTGRTPRERRDLASSLRNLLqdKR---------PPKHFS-RAFSY-EGSDRI 732
Cdd:pfam13234 148 EKGEMEVVpvplsdieaisSVRLKLPK--DLRPAEAREAVLKALQELK--RRfpdgiplldPIEDMKiKDDEFkELLRKI 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1110665004 733 EAEITRLRKelrhHPCHGCSDREEHARWADRWWSLRKETDQLKAQI 778
Cdd:pfam13234 224 EVLESRLES----HPLHKSPRLEELYALYHEKVELQEEIKELKKEI 265
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
51-157 |
1.18e-05 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 49.49 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 51 LVAAPTGAGKTVVGEF-AVYLALQRDGKCFYTTPIKALSNQKFQEFSE--KYGPERVGLLTGDTSinPE--------AEI 119
Cdd:PRK13766 33 LVVLPTGLGKTAIALLvIAERLHKKGGKVLILAPTKPLVEQHAEFFRKflNIPEEKIVVFTGEVS--PEkraelwekAKV 110
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1110665004 120 VVMTTEVLRNMLYADSNTLRGLSFVVMDEVH---------YLADKFR 157
Cdd:PRK13766 111 IVATPQVIENDLIAGRISLEDVSLLIFDEAHravgnyayvYIAERYH 157
|
|
| DEXHc_RE_I_III_res |
cd18032 |
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ... |
36-180 |
1.29e-05 |
|
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs 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: 350790 [Multi-domain] Cd Length: 163 Bit Score: 46.40 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 36 FQIEA----CKELESG-RGVLVAAPTGAGKTVVGEFAVY--LALQRDGKCFYTTPIKALSNQKFQEFSEKYGPERVGLLT 108
Cdd:cd18032 4 YQQEAiealEEAREKGqRRALLVMATGTGKTYTAAFLIKrlLEANRKKRILFLAHREELLEQAERSFKEVLPDGSFGNLK 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1110665004 109 GDTSINPEAEIVVMTTE-VLRNMLYADSNTLRgLSFVVMDEVHY-LADKFRgavweEVIIHLPDSVQvVSLSAT 180
Cdd:cd18032 84 GGKKKPDDARVVFATVQtLNKRKRLEKFPPDY-FDLIIIDEAHHaIASSYR-----KILEYFEPAFL-LGLTAT 150
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
37-186 |
1.30e-05 |
|
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ubiquitously expressed in testis, endometrium, and other tissues in humans. DDX52 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350715 [Multi-domain] Cd Length: 198 Bit Score: 47.20 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 37 QIEACKELESGRGVLVAAPTGAGKTVVGEFAVYLALQRDGK-----CFYTTPIKALSNQKFQEFsEKYG---PERVGLLT 108
Cdd:cd17957 17 QMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKkkglrALILAPTRELASQIYREL-LKLSkgtGLRIVLLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 109 GDTSINPE--------AEIVVMTTEVLRNMLYADSNTLRGLSFVVMDEVHYLADK-FRGAVwEEVIIHLPDSVQVVSL-S 178
Cdd:cd17957 96 KSLEAKAKdgpksitkYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPgFREQT-DEILAACTNPNLQRSLfS 174
|
....*....
gi 1110665004 179 ATV-SNAEE 186
Cdd:cd17957 175 ATIpSEVEE 183
|
|
| DEXHc_RecG |
cd17992 |
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in ... |
19-150 |
1.98e-05 |
|
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. It is a member of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350750 [Multi-domain] Cd Length: 225 Bit Score: 47.14 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 19 KTLLYSFRQEISFELDGFQIEACKELESG--RGV----LVAAPTGAGKTVVGEFAVYLALQRDGKCFYTTPIKALSNQKF 92
Cdd:cd17992 32 GELLKKFLEALPFELTGAQKRVIDEILRDlaSEKpmnrLLQGDVGSGKTVVAALAMLAAVENGYQVALMAPTEILAEQHY 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1110665004 93 QEFS---EKYGPeRVGLLTGDTS-----------INPEAEIVVMTtevlrNMLYADSNTLRGLSFVVMDEVH 150
Cdd:cd17992 112 DSLKkllEPLGI-RVALLTGSTKakekreilekiASGEIDIVIGT-----HALIQEDVEFHNLGLVIIDEQH 177
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
31-150 |
4.05e-05 |
|
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer 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: 350792 [Multi-domain] Cd Length: 200 Bit Score: 45.72 E-value: 4.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 31 FELDGFQIEACKELeSGRGVLVAAPTGAGKTVVgefAVYL---------ALQRDGK-CFYTTPIKALSNQKFqEFSEKYG 100
Cdd:cd18034 1 FTPRSYQLELFEAA-LKRNTIVVLPTGSGKTLI---AVMLikemgelnrKEKNPKKrAVFLVPTVPLVAQQA-EAIRSHT 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1110665004 101 PERVGLLTGDTSINPEA-----------EIVVMTTEVLRNMLyadSN---TLRGLSFVVMDEVH 150
Cdd:cd18034 76 DLKVGEYSGEMGVDKWTkerwkeelekyDVLVMTAQILLDAL---RHgflSLSDINLLIFDECH 136
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
417-493 |
1.25e-04 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 42.20 E-value: 1.25e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1110665004 417 FAAHHAGMLPVFKEVVEKLFAEGYVHAVFATETLALGVNMPARSVVleklVKFNGEEhvqiSPGEYTQLTGRAGRRG 493
Cdd:pfam00271 41 VARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDLV----INYDLPW----NPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
37-192 |
1.68e-04 |
|
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. It possesses 5' single-stranded RNA overhang nuclease activity as well as ATPase activity on various RNA, but not DNA polynucleotides. DDX1 may play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. It may also be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. DDX1 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350696 [Multi-domain] Cd Length: 204 Bit Score: 43.85 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 37 QIEACKELESGRGVLVAAPTGAGKTvvGEFAvyLALQRDGKCFYTTPIKALSNQKFQEFS--EKY--GPE-RVGLLTGDT 111
Cdd:cd17938 26 QAEAIPLILGGGDVLMAAETGSGKT--GAFC--LPVLQIVVALILEPSRELAEQTYNCIEnfKKYldNPKlRVALLIGGV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 112 SINP-------EAEIVVMTTEVLRNMLYADSNTLRGLSFVVMDEVHYLADKFRGAVWEEVIIHLP------DSVQVVSLS 178
Cdd:cd17938 102 KAREqlkrlesGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQGNLETINRIYNRIPkitsdgKRLQVIVCS 181
|
170 180
....*....|....*....|...
gi 1110665004 179 ATVSNAE---------EFGGWLD 192
Cdd:cd17938 182 ATLHSFEvkkladkimHFPTWVD 204
|
|
| DEXHc_HrpB |
cd17990 |
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ... |
44-184 |
1.77e-04 |
|
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA two-partner secretion (TPS) system, a secretion pathway important to the secretion of large virulence-associated proteins. HrpB 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: 438711 [Multi-domain] Cd Length: 174 Bit Score: 43.47 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 44 LESGRGVLVAAPTGAGKTVvgefAVYLAL-----QRDGKCFYTTP----IKALSNQKFQEFSEKYGpERVGL-LTGDTSI 113
Cdd:cd17990 14 LDAGGQVVLEAPPGAGKTT----RVPLALlaelwIAGGKIIVLEPrrvaARAAARRLATLLGEAPG-ETVGYrVRGESRV 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1110665004 114 NPEAEIVVMTTEVLRNMLYADSNtLRGLSFVVMDEVH--YLADKFRGAVWEEVIIHLPDSVQVVSLSATVSNA 184
Cdd:cd17990 89 GRRTRVEVVTEGVLLRRLQRDPE-LSGVGAVILDEFHerSLDADLALALLLEVQQLLRDDLRLLAMSATLDGD 160
|
|
| cas3_core |
TIGR01587 |
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ... |
50-183 |
1.90e-04 |
|
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an alignment of Cas3, a protein found in association with CRISPR repeat elements in a broad range of bacteria and archaea. Cas3 appears to be a helicase, with regions found by pfam00270 (DEAD/DEAH box helicase) and pfam00271 (Helicase conserved C-terminal domain). Some but not all members have an N-terminal HD domain region (pfam01966) that is not included within this model.
Pssm-ID: 273707 [Multi-domain] Cd Length: 359 Bit Score: 44.75 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 50 VLVAAPTGAGKTvvgEFAVYLAL-----QRDGKCFYTTPIKALSNQKFQEFSEKYGPERVGLLTGDTSINPEAEIVVMTT 124
Cdd:TIGR01587 2 LVIEAPTGYGKT---EAALLWALhsiksQKADRVIIALPTRATINAMYRRAKELFGSELVGLHHSSSFSRIKEMGDSEEF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 125 EVLRNMLYADSNTLR------------------------------GLSFVVMDEVHYLADKFRGAVwEEVIIHLPD-SVQ 173
Cdd:TIGR01587 79 EHLFPLYIHSNDKLFldpitvctidqvlksvfgefghyeftlasiANSLLIFDEVHFYDEYTLALI-LAVLEVLKDnDVP 157
|
170
....*....|
gi 1110665004 174 VVSLSATVSN 183
Cdd:TIGR01587 158 ILLMSATLPK 167
|
|
| DEXHc_RHA-like |
cd17917 |
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ... |
50-187 |
2.10e-04 |
|
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family 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: 438707 [Multi-domain] Cd Length: 159 Bit Score: 42.83 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 50 VLVAAPTGAGKTV-VGEFAVYLALQRDGKC--FYTTP--IKALSNQKF--QEFSEKYGpERVGLLT-GDTSINPEAEIVV 121
Cdd:cd17917 4 VVIVGETGSGKTTqVPQFLLEDGLAKGGKGriVCTQPrrIAAISVAERvaEERGEKLG-EEVGYQIrFESKTSSKTRIKF 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1110665004 122 MTTEVLRNMLYADSNtLRGLSFVVMDEVH---YLADKFRGAVweEVIIHLPDSVQVVSLSATVsNAEEF 187
Cdd:cd17917 83 CTDGILLRELLSDPL-LSGYSHVILDEAHersLDTDFLLGLL--KDLLRKRPDLKVILMSATL-DAEKF 147
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
25-149 |
2.35e-04 |
|
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350682 [Multi-domain] Cd Length: 189 Bit Score: 43.08 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 25 FRQEISFELDGFQIEACKELESGRGVLVAAPTGAGKTVVGEF-AVYLALQRdGKCFYTTPIKALSNQ---KFQEFSEKYG 100
Cdd:cd17924 10 FKKKTGFPPWGAQRTWAKRLLRGKSFAIIAPTGVGKTTFGLAtSLYLASKG-KRSYLIFPTKSLVKQayeRLSKYAEKAG 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1110665004 101 pERVGLLTGDTSINPEA-------------EIVVMTTEVLRNmlYADSNTLRGLSFVVMDEV 149
Cdd:cd17924 89 -VEVKILVYHSRLKKKEkeellekiekgdfDILVTTNQFLSK--NFDLLSNKKFDFVFVDDV 147
|
|
| DEXHc_RLR-3 |
cd18075 |
DEXH-box helicase domain of RLR-3; RIG-I-like receptor 3 (RLR-3, also known as laboratory of ... |
32-151 |
3.40e-04 |
|
DEXH-box helicase domain of RLR-3; RIG-I-like receptor 3 (RLR-3, also known as laboratory of genetics and physiology 2 or LGP2 and DHX58) appears to positively and negatively regulate MDA5 and RIG-I signaling, respectively. RLR-3 resembles a chimera combining a MDA5-like helicase domain and RIG-I like CTD supporting both stem and end binding. RNA binding is required for RLR-3-mediated enhancement of MDA5 activation. RLR-3 end-binding may promote nucleation of MDA5 oligomerization on dsRNA. RLR-3 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: 350833 [Multi-domain] Cd Length: 200 Bit Score: 42.92 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 32 ELDGFQIEACKELESGRGVLVAAPTGAGKTvvgEFAVYLALQ-----RDGKCFYTTPIKALSNQKFQEFSEKY-GPERVG 105
Cdd:cd18075 2 ELHGYQWEVVAPALRGKNSIIWLPTGAGKT---RAAVYVARRhletkRGAKVAVLVNKVHLVDQHLEKEFHVLlDKYTVT 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1110665004 106 LLTGDTS-------INPEAEIVVMTTEVLRNMLYADSN----TLRGLSFVVMDEVHY 151
Cdd:cd18075 79 AISGDSShkcffgqLARGSDVVICTAQILQNALLSGEEeahvELTDFSLLVIDECHH 135
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
44-182 |
4.08e-04 |
|
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for mitochondrial group I and II intron splicing, translational activation, and RNA end processing. Mss116 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350722 [Multi-domain] Cd Length: 211 Bit Score: 42.96 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 44 LESGRGVLVAAPTGAGKTVVgeFAV---------YLALQRDG-KCFYTTPIKALSNQKFQEFSE--KYGPE-RVGLLTGD 110
Cdd:cd17964 29 LSTGDDVLARAKTGTGKTLA--FLLpaiqsllntKPAGRRSGvSALIISPTRELALQIAAEAKKllQGLRKlRVQSAVGG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 111 TSINPE--------AEIVVMT----TEVLRNMLYAdsNTLRGLSFVVMDEVHYLADK-FRGAVwEEVIIHLPDSV----Q 173
Cdd:cd17964 107 TSRRAElnrlrrgrPDILVATpgrlIDHLENPGVA--KAFTDLDYLVLDEADRLLDMgFRPDL-EQILRHLPEKNadprQ 183
|
....*....
gi 1110665004 174 VVSLSATVS 182
Cdd:cd17964 184 TLLFSATVP 192
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
28-180 |
6.49e-04 |
|
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein and is activated by Myc protein. DDX18 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350700 [Multi-domain] Cd Length: 198 Bit Score: 41.96 E-value: 6.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 28 EISFE-LDGFQIEACKELESGRGVLVAAPTGAGKTV-----VGEFAVYLA-LQRDGK-CFYTTPIKALSNQKFQEFSE-- 97
Cdd:cd17942 7 EMGFTkMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLaflipAIELLYKLKfKPRNGTgVIIISPTRELALQIYGVAKEll 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 98 KYGPERVGLLTGDTSINPEAE-------IVVMTTEVLRNMLYADSN-TLRGLSFVVMDEvhylADKFRGAVWEE----VI 165
Cdd:cd17942 87 KYHSQTFGIVIGGANRKAEAEklgkgvnILVATPGRLLDHLQNTKGfLYKNLQCLIIDE----ADRILEIGFEEemrqII 162
|
170
....*....|....*
gi 1110665004 166 IHLPDSVQVVSLSAT 180
Cdd:cd17942 163 KLLPKRRQTMLFSAT 177
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
37-186 |
1.12e-03 |
|
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) is a component of the 17S U2 snRNP complex. It plays an important role in pre-mRNA splicing and has a role in antiviral innate immunity. DDX46 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350711 [Multi-domain] Cd Length: 222 Bit Score: 41.59 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 37 QIEACKELESGRGVLVAAPTGAGKTVvgefAVYLALQR-----------DGKC-FYTTPIKALSNQKFQE---FSEKYGP 101
Cdd:cd17953 39 QAQALPAIMSGRDVIGIAKTGSGKTL----AFLLPMFRhikdqrpvkpgEGPIgLIMAPTRELALQIYVEckkFSKALGL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 102 eRVGLLTGDTSINPE-------AEIVVMTTEVLRNMLYADSN---TLRGLSFVVMDEvhylADKFRGAVWEEVIIHLPDS 171
Cdd:cd17953 115 -RVVCVYGGSGISEQiaelkrgAEIVVCTPGRMIDILTANNGrvtNLRRVTYVVLDE----ADRMFDMGFEPQIMKIVNN 189
|
170
....*....|....*....
gi 1110665004 172 V----QVVSLSATVSNAEE 186
Cdd:cd17953 190 IrpdrQTVLFSATFPRKVE 208
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
46-155 |
1.14e-03 |
|
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor 3B-Associated 125 kDa Protein, RHELP, or RNAHP) is an NTPase with a preference for ATP, the hydrolysis of which is enhanced by various RNA substrates. It acts as a non-processive RNA helicase with protein displacement and RNA annealing activities. DDX42 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350710 [Multi-domain] Cd Length: 197 Bit Score: 41.25 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 46 SGRGVLVAAPTGAGKTV--VGEFAVYLALQRDGK------CFYTTPIKALSNQKFQE---FSEKYGPERVGLLTGDT--- 111
Cdd:cd17952 26 SGRDMIGIAKTGSGKTAafIWPMLVHIMDQRELEkgegpiAVIVAPTRELAQQIYLEakkFGKAYNLRVVAVYGGGSkwe 105
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1110665004 112 ---SINPEAEIVVMTTEVLRNMLYADSNTLRGLSFVVMDEvhylADK 155
Cdd:cd17952 106 qakALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDE----ADR 148
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
46-211 |
1.26e-03 |
|
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ribosomal subunits protein 1 homolog, and probable ATP-dependent RNA helicase DDX27) is involved in the processing of 5.8S and 28S ribosomal RNAs. More specifically, the encoded protein localizes to the nucleolus, where it interacts with the PeBoW complex to ensure proper 3' end formation of 47S rRNA. DDX27 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350705 [Multi-domain] Cd Length: 196 Bit Score: 41.09 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 46 SGRGVLVAAPTGAGKTvvgefAVYLA------LQRDGKCFYT-----TPIKALSNQKFQEFSE--KYGPERVGLLTGDTS 112
Cdd:cd17947 26 LGKDICASAVTGSGKT-----AAFLLpilerlLYRPKKKAATrvlvlVPTRELAMQCFSVLQQlaQFTDITFALAVGGLS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 113 INP-EAE------IVVMTT-EVLRNMLYADSNTLRGLSFVVMDEvhylADK-----FRGAVwEEVIIHLPDSVQVVSLSA 179
Cdd:cd17947 101 LKAqEAAlrarpdIVIATPgRLIDHLRNSPSFDLDSIEILVLDE----ADRmleegFADEL-KEILRLCPRTRQTMLFSA 175
|
170 180 190
....*....|....*....|....*....|..
gi 1110665004 180 TVSnaeefggwlDAVrgDTAIIVSEHRPIPLF 211
Cdd:cd17947 176 TMT---------DEV--KDLAKLSLNKPVRVF 196
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
31-180 |
1.30e-03 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 40.98 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 31 FELDGF---QIEACKELESGRGVLVAAPTGAGKTVVgeFAVYlALQRDGKCFYTTPIKALSNQKFQEFSEKygPERVGLL 107
Cdd:cd17920 8 FGYDEFrpgQLEAINAVLAGRDVLVVMPTGGGKSLC--YQLP-ALLLDGVTLVVSPLISLMQDQVDRLQQL--GIRAAAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 108 TGDTS-----------INPEAEIVVMTTEVLRN----MLYADSNTLRGLSFVVMDEVHYLA----DkFRGAVWE--EVII 166
Cdd:cd17920 83 NSTLSpeekrevllriKNGQYKLLYVTPERLLSpdflELLQRLPERKRLALIVVDEAHCVSqwghD-FRPDYLRlgRLRR 161
|
170
....*....|....
gi 1110665004 167 HLPDsVQVVSLSAT 180
Cdd:cd17920 162 ALPG-VPILALTAT 174
|
|
| DEXDc_FANCM |
cd18033 |
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ... |
50-180 |
1.34e-03 |
|
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. In complex with CENPS and CENPX, it binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA), and Holliday junction substrates. Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX. In complex with FAAP24, it efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates. In vitro, on its own, it strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA. FANCM 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: 350791 [Multi-domain] Cd Length: 182 Bit Score: 40.77 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 50 VLVAAPTGAGKTVVGefAV----YLALQRDGKCFYTTPIKALSNQKFQEFSEKYG--PERVGLLTGDTSINPEAE----- 118
Cdd:cd18033 19 TLVALPTGLGKTFIA--AVvmlnYYRWFPKGKIVFMAPTKPLVSQQIEACYKITGipSSQTAELTGSVPPTKRAElwask 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1110665004 119 -IVVMTTEVLRNMLYADSNTLRGLSFVVMDEVHyladKFRG-AVWEEVIIHL---PDSVQVVSLSAT 180
Cdd:cd18033 97 rVFFLTPQTLENDLKEGDCDPKSIVCLVIDEAH----RATGnYAYCQVVRELmryNSHFRILALTAT 159
|
|
| DEXHc_RLR-2 |
cd18074 |
DEXH-box helicase domain of RLR-2; RIG-I-like receptor 2 (RLR-2, also known as melanoma ... |
33-167 |
1.38e-03 |
|
DEXH-box helicase domain of RLR-2; RIG-I-like receptor 2 (RLR-2, also known as melanoma differentiation-associated protein 5 or Mda5 and IFIH1) is a viral double-stranded RNA (dsRNA) receptor that shares sequence similarity and signaling pathways with RIG-I, yet plays essential functions in antiviral immunity through distinct specificity for viral RNA. RLR-2 recognizes the internal duplex structure, whereas RIG-I recognizes the terminus of dsRNA. RLR-2 uses direct protein-protein contacts to stack along dsRNA in a head-to-tail arrangement. The signaling domain (tandem CARD), which decorates the outside of the core RLR-2 filament, also has an intrinsic propensity to oligomerize into an elongated structure that activates the signaling adaptor, MAVS. RLR-2 uses long dsRNA as a signaling platform to cooperatively assemble the core filament, which in turn promotes stochastic assembly of the tandem CARD oligomers for signaling. LGP2 appears to positively and negatively regulate RLR-2 and RIG-I signaling, respectively. RLR-2 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: 350832 [Multi-domain] Cd Length: 216 Bit Score: 41.38 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 33 LDGFQIEACKELESGRGVLVAAPTGAGKTVVgefAVYLALQR-DGKCFYTTPIKA--LSNQKF---QEFSEKYGP----- 101
Cdd:cd18074 3 LRDYQMEVAKPALEGKNIIICLPTGSGKTRV---AVYITKDHlDKKRKASEPGKVivLVNKVPlveQHYRKEFNPflkhw 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1110665004 102 ERVGLLTGDTSIN---PEA----EIVVMTTEVLRNMLYADSN------TLRGLSFVVMDEVHYLAdkfRGAVWEEVIIH 167
Cdd:cd18074 80 YQVIGLSGDSQLKisfPEVvkryDVIICTAQILENSLLNATEeedegvQLSDFSLIIIDECHHTQ---KEAVYNNIMRR 155
|
|
| DEXHc_XPB |
cd18029 |
DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription ... |
47-157 |
1.64e-03 |
|
DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription factor complex helicase XPB subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB 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: 350787 [Multi-domain] Cd Length: 169 Bit Score: 40.36 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 47 GRGVLVAaPTGAGKTVVGEFAVYLaLQRDGKCFYTTPIKALsnQKFQEFSEK--YGPERVGLLTGDT-SINPEAEIVVMT 123
Cdd:cd18029 27 RSGVIVL-PCGAGKTLVGITAACT-IKKSTLVLCTSAVSVE--QWRRQFLDWttIDDEQIGRFTSDKkEIFPEAGVTVST 102
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1110665004 124 TEVLRN--------MLYADSNTLRGLSFVVMDEVHYL-ADKFR 157
Cdd:cd18029 103 YSMLANtrkrspesEKFMEFITEREWGLIILDEVHVVpAPMFR 145
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
37-183 |
1.87e-03 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation factor-4A (eIF4A) family consists of 3 proteins EIF4A1, EIF4A2, and EIF4A3. These factors are required for the binding of mRNA to 40S ribosomal subunits. In addition these proteins are helicases that function to unwind double-stranded RNA. EIF4A proteins are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350697 [Multi-domain] Cd Length: 199 Bit Score: 40.77 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 37 QIEACKELESGRGVLVAAPTGAGKTvvGEFAVyLALQR----DGKC--FYTTPIKALSNQKFQEFSE--KYGPERVGLLT 108
Cdd:cd17939 24 QQRAIVPIIKGRDVIAQAQSGTGKT--ATFSI-GALQRidttVRETqaLVLAPTRELAQQIQKVVKAlgDYMGVKVHACI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 109 GDTSINPEAE-------IVVMTTEVLRNMLYADSNTLRGLSFVVMDEVHYLADK-FRGAVWeEVIIHLPDSVQVVSLSAT 180
Cdd:cd17939 101 GGTSVREDRRklqygphIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRgFKDQIY-DIFQFLPPETQVVLFSAT 179
|
...
gi 1110665004 181 VSN 183
Cdd:cd17939 180 MPH 182
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
46-180 |
2.68e-03 |
|
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, Component Of Gems 3, Gemin-3, and SMN-Interacting Protein) interacts directly with SMN (survival of motor neurons), the spinal muscular atrophy gene product, and may play a catalytic role in the function of the SMN complex on ribonucleoproteins. Diseases associated with DDX20 include spinal muscular atrophy and muscular atrophy. DDX20 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350701 [Multi-domain] Cd Length: 192 Bit Score: 39.94 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 46 SGRGVLVAAPTGAGKTVVgeFAVyLALQR-DGKCFYT-----TPIKALSNQ---KFQEFSEKYGPERVGLLTGDTSIN-- 114
Cdd:cd17943 26 AGHDLIVQAKSGTGKTLV--FVV-IALESlDLERRHPqvlilAPTREIAVQihdVFKKIGKKLEGLKCEVFIGGTPVKed 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1110665004 115 ----PEAEIVVMTTEVLRNMLYADSNTLRGLSFVVMDEvhylADKFRGAVWEE----VIIHLPDSVQVVSLSAT 180
Cdd:cd17943 103 kkklKGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDE----ADKLMEGSFQKdvnwIFSSLPKNKQVIAFSAT 172
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
47-191 |
2.72e-03 |
|
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer development by promoting DNA replication. DDX59 knockdown mice showed reduced cell proliferation, anchorage-independent cell growth, and reduction of tumor formation. Recent work shows that EGFR and Ras regulate DDX59 during lung cancer development. Diseases associated with DDX59 (also called zinc finger HIT domain-containing protein 5) include orofaciodigital syndrome V and orofaciodigital syndrome. DDX59 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350720 [Multi-domain] Cd Length: 193 Bit Score: 40.22 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 47 GRGVLVAAPTGAGKTVVGEFAVY---LALQRDGKCFYTTPIKALSNQ---KFQEFSEKYGPERVGLLTGDTSINPE---- 116
Cdd:cd17962 27 GRDILASADTGSGKTAAFLLPVIircLTEHRNPSALILTPTRELAVQiedQAKELMKGLPPMKTALLVGGLPLPPQlyrl 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 117 ---AEIVVMTTEVLRNMLYADSNTLRGLSFVVMDEVH-YLADKFRGAVWeEVIIHLPDSVQVVSLSATVSNA-EEFGGWL 191
Cdd:cd17962 107 qqgVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADtMLKMGFQQQVL-DILENISHDHQTILVSATIPRGiEQLAGQL 185
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
46-154 |
2.80e-03 |
|
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and nucleolar RNA helicase 2) is an RNA helicase that acts as a sensor of the transcriptional status of both RNA polymerase (Pol) I and II. It promotes ribosomal RNA (rRNA) processing and transcription from polymerase II (Pol II) and binds various RNAs, such as rRNAs, snoRNAs, 7SK and, at lower extent, mRNAs. DDX50 (also called Gu-Beta, Nucleolar Protein Gu2, and malignant cell derived RNA helicase). DDX21 and DDX50 have similar genomic structures and are in tandem orientation on chromosome 10, suggesting that the two genes arose by gene duplication in evolution. Diseases associated with DDX21 include stomach disease and cerebral creatine deficiency syndrome 3. Diseases associated with DDX50 include rectal disease. Both are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. Their name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region.
Pssm-ID: 350702 [Multi-domain] Cd Length: 202 Bit Score: 40.22 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 46 SGRGVLVAAPTGAGKTVvgEFAVYLA--LQRDG---------KCFYTTPIKALSNQKFQEFSEKYGPERVGLLTGDTSIN 114
Cdd:cd17944 26 SGKDLIAQARTGTGKTF--SFAIPLIekLQEDQqprkrgrapKVLVLAPTRELANQVTKDFKDITRKLSVACFYGGTPYQ 103
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1110665004 115 PEAE-------IVVMTTEVLRNMLYADSNTLRGLSFVVMDEVHYLAD 154
Cdd:cd17944 104 QQIFairngidILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLD 150
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
46-184 |
2.87e-03 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 41.29 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 46 SGRGVLVAAPTGAGKTvvgefAVYL--ALQR--DGKCFYT-----TPIKALSNQKFQEFsEKYGPE---RVGLLTGDTSI 113
Cdd:COG0513 38 AGRDVLGQAQTGTGKT-----AAFLlpLLQRldPSRPRAPqalilAPTRELALQVAEEL-RKLAKYlglRVATVYGGVSI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 114 NPE-------AEIVVMTTEVLRNMLYADSNTLRGLSFVVMDEvhylADK-----FRGAVwEEVIIHLPDSVQVVSLSATV 181
Cdd:COG0513 112 GRQiralkrgVDIVVATPGRLLDLIERGALDLSGVETLVLDE----ADRmldmgFIEDI-ERILKLLPKERQTLLFSATM 186
|
...
gi 1110665004 182 SNA 184
Cdd:COG0513 187 PPE 189
|
|
| DEXHc_DHX9 |
cd17972 |
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ... |
36-181 |
3.14e-03 |
|
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ATP-dependent RNA helicase A or RHA and leukophysin or LKP) plays an important role in many cellular processes, including regulation of DNA replication, transcription, translation, microRNA biogenesis, RNA processing and transport, and maintenance of genomic stability. DHX9 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: 350730 [Multi-domain] Cd Length: 234 Bit Score: 40.20 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 36 FQIEACKELESGRGVLVAAPTGAGKTV-VGEFAV--YLALQRDGKC--FYTTP--IKALSnqkfqeFSEKYGPERvGLLT 108
Cdd:cd17972 64 FREEILEAISNNPVVIIRGATGCGKTTqVPQYILddFIQNDRAAECniVVTQPrrISAVS------VAERVAFER-GEEV 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 109 GDT--------SI--NPEAEIVVMTTEVLRNMLyadSNTLRGLSFVVMDEVHY--LADKFRGAVWEEVIIHLPDsVQVVS 176
Cdd:cd17972 137 GKScgysvrfeSVlpRPHASILFCTVGVLLRKL---EAGIRGISHVIVDEIHErdINTDFLLVVLRDVVQAYPD-LRVIL 212
|
....*
gi 1110665004 177 LSATV 181
Cdd:cd17972 213 MSATI 217
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
47-184 |
4.15e-03 |
|
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350713 [Multi-domain] Cd Length: 204 Bit Score: 39.52 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110665004 47 GRGVLVAAPTGAGKTVVgeFAVYLaLQR---DGKCFYT---TPIKALSNQ---KFQEFSEKYGPeRVGLLTGDTSINPEA 117
Cdd:cd17955 36 GRDVIGGAKTGSGKTAA--FALPI-LQRlseDPYGIFAlvlTPTRELAYQiaeQFRALGAPLGL-RCCVIVGGMDMVKQA 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1110665004 118 E-------IVVMTTEVLRNMLYADSNTLRGLS---FVVMDEV-HYLADKFRGAVwEEVIIHLPDSVQVVSLSATVSNA 184
Cdd:cd17955 112 LelskrphIVVATPGRLADHLRSSDDTTKVLSrvkFLVLDEAdRLLTGSFEDDL-ATILSALPPKRQTLLFSATLTDA 188
|
|
| |
