|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
28-440 |
1.57e-102 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 316.32 E-value: 1.57e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 28 LDKEIHKAITRMEFPGLTPVQQKTIKPILssEDHDVIARAKTGTGKTFAFLIPIFQHLintKFDSQYMVKAVIVAPTRDL 107
Cdd:COG0513 9 LSPPLLKALAELGYTTPTPIQAQAIPLIL--AGRDVLGQAQTGTGKTAAFLLPLLQRL---DPSRPRAPQALILAPTREL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 108 ALQIEAEVKKIHDmNYGLKkyaCVSLVGGTDFRAAMNKMNKlRPNIVIATPGRLIDVLEKysnKFFRF--VDYKVLDEAD 185
Cdd:COG0513 84 ALQVAEELRKLAK-YLGLR---VATVYGGVSIGRQIRALKR-GVDIVVATPGRLLDLIER---GALDLsgVETLVLDEAD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 186 RLLEIGFRDDLETISGILNEKnsksadnIKTLLFSATLDDKVQKLANNIMNKKEclfldTVD-KNEPEAHERIDQSVVIS 264
Cdd:COG0513 156 RMLDMGFIEDIERILKLLPKE-------RQTLLFSATMPPEIRKLAKRYLKNPV-----RIEvAPENATAETIEQRYYLV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 265 EKfaNSIFAAVEHIkkqIKERDsNYKAIIFAPTVKFTSFLCSILKnefKKDLPILEFHGKITQNKRTSLVKRFKKDESGI 344
Cdd:COG0513 224 DK--RDKLELLRRL---LRDED-PERAIVFCNTKRGADRLAEKLQ---KRGISAAALHGDLSQGQRERALDAFRNGKIRV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 345 LVCTDVGARGMDFPNVHEVLQIGVPSELANYIHRIGRTARSGKEGSSVLFICKDELPFVRELEDAKNIVIAKQE--KYEP 422
Cdd:COG0513 295 LVATDVAARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEElpGFEP 374
|
410
....*....|....*...
gi 350610602 423 SEEIKSEVLEAVTEEPED 440
Cdd:COG0513 375 VEEKRLERLKPKIKEKLK 392
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
28-244 |
2.19e-101 |
|
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: 305.66 E-value: 2.19e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 28 LDKEIHKAITRMEFPGLTPVQQKTIKPILSSEdHDVIARAKTGTGKTFAFLIPIFQHLINTKFD-SQYMVKAVIVAPTRD 106
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILSTG-DDVLARAKTGTGKTLAFLLPAIQSLLNTKPAgRRSGVSALIISPTRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 107 LALQIEAEVKKIHdmnYGLKKYACVSLVGGTDFRAAMNKMNKLRPNIVIATPGRLIDVLEKYSN-KFFRFVDYKVLDEAD 185
Cdd:cd17964 80 LALQIAAEAKKLL---QGLRKLRVQSAVGGTSRRAELNRLRRGRPDILVATPGRLIDHLENPGVaKAFTDLDYLVLDEAD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 350610602 186 RLLEIGFRDDLETISGILNEKNSksaDNIKTLLFSATLDDKVQKLANNIMnKKECLFLD 244
Cdd:cd17964 157 RLLDMGFRPDLEQILRHLPEKNA---DPRQTLLFSATVPDEVQQIARLTL-KKDYKFID 211
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
32-236 |
3.65e-70 |
|
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: 224.24 E-value: 3.65e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 32 IHKAITRMEFPGLTPVQQKTIKPILSseDHDVIARAKTGTGKTFAFLIPIFQHLINTKFDSQYMVKAVIVAPTRDLALQI 111
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILS--GRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGRGPQALVLAPTRELAMQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 112 EAEVKKIHDmNYGLKkyaCVSLVGGTDFRAAMNKMNKlRPNIVIATPGRLIDVLEKYsNKFFRFVDYKVLDEADRLLEIG 191
Cdd:cd00268 79 AEVARKLGK-GTGLK---VAAIYGGAPIKKQIEALKK-GPDIVVGTPGRLLDLIERG-KLDLSNVKYLVLDEADRMLDMG 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 350610602 192 FRDDLETISGILNEKnsksadnIKTLLFSATLDDKVQKLANNIMN 236
Cdd:cd00268 153 FEEDVEKILSALPKD-------RQTLLFSATLPEEVKELAKKFLK 190
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
24-440 |
2.43e-54 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 190.15 E-value: 2.43e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 24 EEGVLDKEIHKAITRMEFPGLTPVQQKTIKPILssEDHDVIARAKTGTGKTFAFLIPIFQHLIN--TKFDSQYMVkaVIV 101
Cdd:PRK11192 4 SELELDESLLEALQDKGYTRPTAIQAEAIPPAL--DGRDVLGSAPTGTGKTAAFLLPALQHLLDfpRRKSGPPRI--LIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 102 APTRDLALQIeaevkkiHDMNYGLKKYA---CVSLVGGTdfrAAMNKMNKLRPN--IVIATPGRLIDVLEKysNKF-FRF 175
Cdd:PRK11192 80 TPTRELAMQV-------ADQARELAKHThldIATITGGV---AYMNHAEVFSENqdIVVATPGRLLQYIKE--ENFdCRA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 176 VDYKVLDEADRLLEIGFRDDLETISGilNEKNSKsadniKTLLFSATLD-DKVQKLANNIMNkkECLFLDTvdknEPEAH 254
Cdd:PRK11192 148 VETLILDEADRMLDMGFAQDIETIAA--ETRWRK-----QTLLFSATLEgDAVQDFAERLLN--DPVEVEA----EPSRR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 255 ER--IDQSVVISEKFANSiFAAVEHIKKQikerDSNYKAIIFAPTVKFTSFLCSILKnefKKDLPILEFHGKITQNKRTS 332
Cdd:PRK11192 215 ERkkIHQWYYRADDLEHK-TALLCHLLKQ----PEVTRSIVFVRTRERVHELAGWLR---KAGINCCYLEGEMVQAKRNE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 333 LVKRFKKDESGILVCTDVGARGMDFPNVHEVLQIGVPSELANYIHRIGRTARSGKEGSSVLFIckdelpfvrELEDAKni 412
Cdd:PRK11192 287 AIKRLTDGRVNVLVATDVAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISLV---------EAHDHL-- 355
|
410 420 430
....*....|....*....|....*....|.
gi 350610602 413 VIAKQEKYePSEEIKSEV---LEAVTEEPED 440
Cdd:PRK11192 356 LLGKIERY-IEEPLKARVideLRPKTKAPSE 385
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
28-406 |
1.09e-53 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 189.74 E-value: 1.09e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 28 LDKEIHKAITRMEFPGLTPVQQKTIKPILSSedHDVIARAKTGTGKTFAFLIPIFQHLINTKFDSQ-YM--VKAVIVAPT 104
Cdd:PRK01297 94 LAPELMHAIHDLGFPYCTPIQAQVLGYTLAG--HDAIGRAQTGTGKTAAFLISIINQLLQTPPPKErYMgePRALIIAPT 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 105 RDLALQIEAEVKKihdmnygLKKYA---CVSLVGGTDFRAAMNKMNKLRPNIVIATPGRLIDVLEKySNKFFRFVDYKVL 181
Cdd:PRK01297 172 RELVVQIAKDAAA-------LTKYTglnVMTFVGGMDFDKQLKQLEARFCDILVATPGRLLDFNQR-GEVHLDMVEVMVL 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 182 DEADRLLEIGFrddLETISGILNEKNSKSADniKTLLFSATLDDKVQKLAnnimnkKECLFLDTVDKNEPEAheridqsv 261
Cdd:PRK01297 244 DEADRMLDMGF---IPQVRQIIRQTPRKEER--QTLLFSATFTDDVMNLA------KQWTTDPAIVEIEPEN-------- 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 262 VISEKFANSIFAAVEHIKKQIKE---RDSNY-KAIIFA---PTVKFtsflcsiLKNEFKKD-LPILEFHGKITQNKRTSL 333
Cdd:PRK01297 305 VASDTVEQHVYAVAGSDKYKLLYnlvTQNPWeRVMVFAnrkDEVRR-------IEERLVKDgINAAQLSGDVPQHKRIKT 377
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 350610602 334 VKRFKKDESGILVCTDVGARGMDFPNVHEVLQIGVPSELANYIHRIGRTARSGKEGSSVLFICKDE---LPFVREL 406
Cdd:PRK01297 378 LEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDafqLPEIEEL 453
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
31-438 |
1.50e-49 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 180.53 E-value: 1.50e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 31 EIHKAI----TRMEFPGLTPVQQKTIKPILSSEDhdVIARAKTGTGKTFAFLIPIFQHLINTKFDSQYMV---KAVIVAP 103
Cdd:PRK04537 15 DLHPALlaglESAGFTRCTPIQALTLPVALPGGD--VAGQAQTGTGKTLAFLVAVMNRLLSRPALADRKPedpRALILAP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 104 TRDLALQIEAEVKKIhDMNYGLKkYACVslVGGTDFRAAMNKMNKlRPNIVIATPGRLIDVLEKYSNKFFRFVDYKVLDE 183
Cdd:PRK04537 93 TRELAIQIHKDAVKF-GADLGLR-FALV--YGGVDYDKQRELLQQ-GVDVIIATPGRLIDYVKQHKVVSLHACEICVLDE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 184 ADRLLEIGFRDDLETISGILNEKNSKsadniKTLLFSATLDDKVQKLANNIMNKKECLFLDTVDKNEPEAHERIdqsvvi 263
Cdd:PRK04537 168 ADRMFDLGFIKDIRFLLRRMPERGTR-----QTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRI------ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 264 sekfansIFAAVEhiKKQ-----IKERDSNYKAIIFAPTVKFTSFLCSIL-KNEFKKDLpileFHGKITQNKRTSLVKRF 337
Cdd:PRK04537 237 -------YFPADE--EKQtlllgLLSRSEGARTMVFVNTKAFVERVARTLeRHGYRVGV----LSGDVPQKKRESLLNRF 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 338 KKDESGILVCTDVGARGMDFPNVHEVLQIGVPSELANYIHRIGRTARSGKEGSSVLFICKDelpFVRELEDAKniviAKQ 417
Cdd:PRK04537 304 QKGQLEILVATDVAARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACER---YAMSLPDIE----AYI 376
|
410 420
....*....|....*....|.
gi 350610602 418 EKYEPSEEIKSEVLEAVTEEP 438
Cdd:PRK04537 377 EQKIPVEPVTAELLTPLPRPP 397
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
44-415 |
1.45e-48 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 175.37 E-value: 1.45e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 44 LTPVQQKTIKPILssEDHDVIARAKTGTGKTFAFLIPIFQHLINTKFDSQYMVkaviVAPTRDLALQIEAEVKK----IH 119
Cdd:PRK11776 27 MTPIQAQSLPAIL--AGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALV----LCPTRELADQVAKEIRRlarfIP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 120 dmnyGLKkyaCVSLVGGTDFRAamnKMNKLR--PNIVIATPGRLIDVLEKYSNKfFRFVDYKVLDEADRLLEIGFRDDLE 197
Cdd:PRK11776 101 ----NIK---VLTLCGGVPMGP---QIDSLEhgAHIIVGTPGRILDHLRKGTLD-LDALNTLVLDEADRMLDMGFQDAID 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 198 TISGILNEKNsksadniKTLLFSATLDDKVQKLANNIMNKKEclfldTVDKNEPEAHERIDQsvvisekfansIFAAVEH 277
Cdd:PRK11776 170 AIIRQAPARR-------QTLLFSATYPEGIAAISQRFQRDPV-----EVKVESTHDLPAIEQ-----------RFYEVSP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 278 IKKQIKERD--SNYK---AIIFAPTVKFTSFLCSILKNefkKDLPILEFHGKITQNKRTSLVKRFKKDESGILVCTDVGA 352
Cdd:PRK11776 227 DERLPALQRllLHHQpesCVVFCNTKKECQEVADALNA---QGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAA 303
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 350610602 353 RGMDFPNVHEVLQIGVPSELANYIHRIGRTARSGKEGSSVLFICKDELPFVRELEDAKNIVIA 415
Cdd:PRK11776 304 RGLDIKALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLN 366
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
45-230 |
1.73e-47 |
|
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: 163.57 E-value: 1.73e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 45 TPVQQKTIKPILssEDHDVIARAKTGTGKTFAFLIPIFQHLINTKFDSQymvkAVIVAPTRDLALQIEAEVKKIHDmNYG 124
Cdd:pfam00270 1 TPIQAEAIPAIL--EGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQ----ALVLAPTRELAEQIYEELKKLGK-GLG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 125 LKkyaCVSLVGGTDFRAAMNKMNKlrPNIVIATPGRLIDVLEKysNKFFRFVDYKVLDEADRLLEIGFRDDLETISGILN 204
Cdd:pfam00270 74 LK---VASLLGGDSRKEQLEKLKG--PDILVGTPGRLLDLLQE--RKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLP 146
|
170 180
....*....|....*....|....*.
gi 350610602 205 EKnsksadnIKTLLFSATLDDKVQKL 230
Cdd:pfam00270 147 KK-------RQILLLSATLPRNLEDL 165
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
32-231 |
1.67e-46 |
|
DEAD-box helicase domain of DEAD box protein 55; DDX55 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: 350718 [Multi-domain] Cd Length: 202 Bit Score: 161.97 E-value: 1.67e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 32 IHKAITRMEFPGLTPVQQKTIKPILSSEDhdVIARAKTGTGKTFAFLIPIFQHLINTKFDSQYM-VKAVIVAPTRDLALQ 110
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKD--VVVEAVTGSGKTLAFLIPVLEILLKRKANLKKGqVGALIISPTRELATQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 111 IEAEVKKIhdMNYGLKKYACVSLVGGTDFRAAMNKMNKLRPNIVIATPGRLIDVLEKYSNKF-FRFVDYKVLDEADRLLE 189
Cdd:cd17960 79 IYEVLQSF--LEHHLPKLKCQLLIGGTNVEEDVKKFKRNGPNILVGTPGRLEELLSRKADKVkVKSLEVLVLDEADRLLD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 350610602 190 IGFRDDLETISGILnEKNSksadniKTLLFSATLDDKVQKLA 231
Cdd:cd17960 157 LGFEADLNRILSKL-PKQR------RTGLFSATQTDAVEELI 191
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
32-406 |
3.32e-46 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 170.72 E-value: 3.32e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 32 IHKAITRMEFPGLTPVQQKTIKPILSSedHDVIARAKTGTGKTFAFLIPIFQHlINtkfdSQYMVK------AVIVAPTR 105
Cdd:PTZ00110 141 ILKSLKNAGFTEPTPIQVQGWPIALSG--RDMIGIAETGSGKTLAFLLPAIVH-IN----AQPLLRygdgpiVLVLAPTR 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 106 DLALQIEAEVKKI-------HDMNYG--LKKYACVSLVGGTDfraamnkmnklrpnIVIATPGRLIDVLEK-YSNkfFRF 175
Cdd:PTZ00110 214 ELAEQIREQCNKFgasskirNTVAYGgvPKRGQIYALRRGVE--------------ILIACPGRLIDFLESnVTN--LRR 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 176 VDYKVLDEADRLLEIGFRDDLETISGILNEKNsksadniKTLLFSATLDDKVQKLANNIMnKKECLFLDtVDKNEPEAHE 255
Cdd:PTZ00110 278 VTYLVLDEADRMLDMGFEPQIRKIVSQIRPDR-------QTLMWSATWPKEVQSLARDLC-KEEPVHVN-VGSLDLTACH 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 256 RIDQSVVISEkfansifaavEHIKK-QIKE-----RDSNYKAIIFAPTVKFTSFLCSILKNEfkkDLPILEFHGKITQNK 329
Cdd:PTZ00110 349 NIKQEVFVVE----------EHEKRgKLKMllqriMRDGDKILIFVETKKGADFLTKELRLD---GWPALCIHGDKKQEE 415
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 350610602 330 RTSLVKRFKKDESGILVCTDVGARGMDFPNVHEVLQIGVPSELANYIHRIGRTARSGKEGSSVLFICKDELPFVREL 406
Cdd:PTZ00110 416 RTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDL 492
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
34-237 |
1.93e-45 |
|
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: 159.31 E-value: 1.93e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 34 KAITRMEFPGLTPVQQKTIKPILSSEDhdVIARAKTGTGKTFAFLIPIFQHLintkfdSQ--YMVKAVIVAPTRDLALQI 111
Cdd:cd17955 12 KQCASLGIKEPTPIQKLCIPEILAGRD--VIGGAKTGSGKTAAFALPILQRL------SEdpYGIFALVLTPTRELAYQI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 112 eAEVKKIHDMNYGLKkyaCVSLVGGTDFRAAMNKMNKlRPNIVIATPGRLIDVLEKYSN--KFFRFVDYKVLDEADRLLE 189
Cdd:cd17955 84 -AEQFRALGAPLGLR---CCVIVGGMDMVKQALELSK-RPHIVVATPGRLADHLRSSDDttKVLSRVKFLVLDEADRLLT 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 350610602 190 IGFRDDLETISGILNEKNsksadniKTLLFSATLDDKVQKLANNIMNK 237
Cdd:cd17955 159 GSFEDDLATILSALPPKR-------QTLLFSATLTDALKALKELFGNK 199
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
28-429 |
3.33e-45 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 166.14 E-value: 3.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 28 LDKEIHKAITRMEFPGLTPVQQKTIKPILssEDHDVIARAKTGTGKTFAFLIPIFQHLINTKFDSQ--YMVKAVIVAPTR 105
Cdd:PRK10590 8 LSPDILRAVAEQGYREPTPIQQQAIPAVL--EGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKgrRPVRALILTPTR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 106 DLALQIEAEVKkihdmNYglKKYACV-SLV--GGTDFRAamnKMNKLRP--NIVIATPGRLIDVLEKYSNKFFRfVDYKV 180
Cdd:PRK10590 86 ELAAQIGENVR-----DY--SKYLNIrSLVvfGGVSINP---QMMKLRGgvDVLVATPGRLLDLEHQNAVKLDQ-VEILV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 181 LDEADRLLEIGFRDDLETISGILNEKNsksadniKTLLFSATLDDKVQKLANNIMNKKEClfLDTVDKNepEAHERIDQS 260
Cdd:PRK10590 155 LDEADRMLDMGFIHDIRRVLAKLPAKR-------QNLLFSATFSDDIKALAEKLLHNPLE--IEVARRN--TASEQVTQH 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 261 VVISEKFANSifaavEHIKKQIKERDSNyKAIIFAPTVKFTSFLCSILKnefKKDLPILEFHGKITQNKRTSLVKRFKKD 340
Cdd:PRK10590 224 VHFVDKKRKR-----ELLSQMIGKGNWQ-QVLVFTRTKHGANHLAEQLN---KDGIRSAAIHGNKSQGARTRALADFKSG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 341 ESGILVCTDVGARGMDFPNVHEVLQIGVPSELANYIHRIGRTARSGKEGSSVLFICKDELPFVRELED--AKNIVIAKQE 418
Cdd:PRK10590 295 DIRVLVATDIAARGLDIEELPHVVNYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKllKKEIPRIAIP 374
|
410
....*....|.
gi 350610602 419 KYEPSEEIKSE 429
Cdd:PRK10590 375 GYEPDPSIKAE 385
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
28-414 |
3.59e-45 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 164.61 E-value: 3.59e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 28 LDKEIHKAITRMEFPGLTPVQQKTIKPILssEDHDVIARAKTGTGKTFAFLIPIFQhLINTKFDSqymVKAVIVAPTRDL 107
Cdd:PTZ00424 35 LNEDLLRGIYSYGFEKPSAIQQRGIKPIL--DGYDTIGQAQSGTGKTATFVIAALQ-LIDYDLNA---CQALILAPTREL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 108 ALQIEAEVKKIHDMnYGLKKYACVslvGGTDFRAAMNKMnKLRPNIVIATPGRLIDVLEKysnKFFRFVDYK--VLDEAD 185
Cdd:PTZ00424 109 AQQIQKVVLALGDY-LKVRCHACV---GGTVVRDDINKL-KAGVHMVVGTPGRVYDMIDK---RHLRVDDLKlfILDEAD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 186 RLLEIGFRDDLETISgilneknSKSADNIKTLLFSATLDDKVQKLANNIMNKKECLFLdtvdKNEPEAHERIDQSVVISE 265
Cdd:PTZ00424 181 EMLSRGFKGQIYDVF-------KKLPPDVQVALFSATMPNEILELTTKFMRDPKRILV----KKDELTLEGIRQFYVAVE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 266 KfansifaavEHIK----KQIKERDSNYKAIIFAPTVKFTSFLCSILKNefkKDLPILEFHGKITQNKRTSLVKRFKKDE 341
Cdd:PTZ00424 250 K---------EEWKfdtlCDLYETLTITQAIIYCNTRRKVDYLTKKMHE---RDFTVSCMHGDMDQKDRDLIMREFRSGS 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 350610602 342 SGILVCTDVGARGMDFPNVHEVLQIGVPSELANYIHRIGRTARSGKEGSSVLFICKDELPFVRELEDAKNIVI 414
Cdd:PTZ00424 318 TRVLITTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQI 390
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
28-398 |
8.86e-45 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 163.99 E-value: 8.86e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 28 LDKEIHKAITRMEFPGLTPVQQKTIKPILSSedHDVIARAKTGTGKTFAFLIPIFQHLINTKFDSQYMV---KAVIVAPT 104
Cdd:PRK04837 15 LHPQVVEALEKKGFHNCTPIQALALPLTLAG--RDVAGQAQTGTGKTMAFLTATFHYLLSHPAPEDRKVnqpRALIMAPT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 105 RDLALQIEAEVKKIHDMNyGLKkyacVSLV-GGTDFRAAMNKMNKlRPNIVIATPGRLIDVlekYSNKFFRF--VDYKVL 181
Cdd:PRK04837 93 RELAVQIHADAEPLAQAT-GLK----LGLAyGGDGYDKQLKVLES-GVDILIGTTGRLIDY---AKQNHINLgaIQVVVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 182 DEADRLLEIGFRDDLETISGILNEKNSKsadniKTLLFSATLDDKVQKLANNIMNKKECLfldTVDKNEPEAHeRIDQsv 261
Cdd:PRK04837 164 DEADRMFDLGFIKDIRWLFRRMPPANQR-----LNMLFSATLSYRVRELAFEHMNNPEYV---EVEPEQKTGH-RIKE-- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 262 visEKFANSIFAAVEHIKKQIKErDSNYKAIIFAPTvKFTsflCSILKNEFKKD---LPILEfhGKITQNKRTSLVKRFK 338
Cdd:PRK04837 233 ---ELFYPSNEEKMRLLQTLIEE-EWPDRAIIFANT-KHR---CEEIWGHLAADghrVGLLT--GDVAQKKRLRILEEFT 302
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 339 KDESGILVCTDVGARGMDFPNVHEVLQIGVPSELANYIHRIGRTARSGKEGSSVLFICKD 398
Cdd:PRK04837 303 RGDLDILVATDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEE 362
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
34-244 |
3.56e-44 |
|
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: 155.60 E-value: 3.56e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 34 KAITRMEFPGLTPVQQKTIKPILssEDHDVIARAKTGTGKTFAFLIPIFQHLINTKFDSQYMVKAVIVAPTRDLALQIEA 113
Cdd:cd17942 3 KAIEEMGFTKMTEIQAKSIPPLL--EGRDVLGAAKTGSGKTLAFLIPAIELLYKLKFKPRNGTGVIIISPTRELALQIYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 114 EVKKIhdMNYGLKKYACVslVGGTDFRAAMNKMNKlRPNIVIATPGRLIDVLEKYSNKFFRFVDYKVLDEADRLLEIGFR 193
Cdd:cd17942 81 VAKEL--LKYHSQTFGIV--IGGANRKAEAEKLGK-GVNILVATPGRLLDHLQNTKGFLYKNLQCLIIDEADRILEIGFE 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 350610602 194 DDLETISGILNEKNsksadniKTLLFSATLDDKVQKLAnNIMNKKECLFLD 244
Cdd:cd17942 156 EEMRQIIKLLPKRR-------QTMLFSATQTRKVEDLA-RISLKKKPLYVG 198
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
36-236 |
8.65e-43 |
|
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes Drosophila melanogaster Vasa, which is essential for development. DEAD box protein 3 (DDX3) has been reported to display a high level of RNA-independent ATPase activity stimulated by both RNA and DNA. DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DDX3 and DDX4 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: 350725 [Multi-domain] Cd Length: 221 Bit Score: 152.64 E-value: 8.65e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 36 ITRMEFPGLTPVQQKTIkPILSSeDHDVIARAKTGTGKTFAFLIPIFQHLINTKFDSQYMVK------AVIVAPTRDLAL 109
Cdd:cd17967 15 IKRAGYTKPTPVQKYAI-PIILA-GRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVGRGRrkaypsALILAPTRELAI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 110 QIEAEVKKihdMNY--GLKkyaCVSLVGGTDFRAAMNKMnkLRP-NIVIATPGRLIDVLEKysNKF-FRFVDYKVLDEAD 185
Cdd:cd17967 93 QIYEEARK---FSYrsGVR---SVVVYGGADVVHQQLQL--LRGcDILVATPGRLVDFIER--GRIsLSSIKFLVLDEAD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 350610602 186 RLLEIGFRDDLETisgILNEKNSKSADNIKTLLFSATLDDKVQKLANNIMN 236
Cdd:cd17967 163 RMLDMGFEPQIRK---IVEHPDMPPKGERQTLMFSATFPREIQRLAADFLK 210
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
28-230 |
1.46e-42 |
|
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can shuttle between the nucleus and the cytoplasm, and has an RNA-independent ATPase activity. DX47 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: 350712 [Multi-domain] Cd Length: 203 Bit Score: 151.32 E-value: 1.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 28 LDKEIHKAITRMEFPGLTPVQQKTIKPILssEDHDVIARAKTGTGKTFAFLIPIFQHLINTKfdsQYMVkAVIVAPTRDL 107
Cdd:cd17954 7 VCEELCEACEKLGWKKPTKIQEEAIPVAL--QGRDIIGLAETGSGKTAAFALPILQALLENP---QRFF-ALVLAPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 108 ALQIEAEVKKIhDMNYGLKkyaCVSLVGGTDFRAAMNKMNKlRPNIVIATPGRLIDVLEKYSNKFFRFVDYKVLDEADRL 187
Cdd:cd17954 81 AQQISEQFEAL-GSSIGLK---SAVLVGGMDMMAQAIALAK-KPHVIVATPGRLVDHLENTKGFSLKSLKFLVMDEADRL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 350610602 188 LEIGFRDDLETISGIL-NEKNsksadnikTLLFSATLDDKVQKL 230
Cdd:cd17954 156 LNMDFEPEIDKILKVIpRERT--------TYLFSATMTTKVAKL 191
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
28-223 |
8.11e-42 |
|
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner with nuclear receptors, and represses their transcriptional activity. DDX54 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: 350717 [Multi-domain] Cd Length: 205 Bit Score: 149.38 E-value: 8.11e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 28 LDKEIHKAITRMEFPGLTPVQQKTIKPILSSedHDVIARAKTGTGKTFAFLIPIFQHLINTKfdSQYMVKAVIVAPTRDL 107
Cdd:cd17959 8 LSPPLLRAIKKKGYKVPTPIQRKTIPLILDG--RDVVAMARTGSGKTAAFLIPMIEKLKAHS--PTVGARALILSPTREL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 108 ALQIEAEVKKIHDMNyGLKkyaCVSLVGGTDFRAAMNKMNKlRPNIVIATPGRLIDVLEKYSNKFFRfVDYKVLDEADRL 187
Cdd:cd17959 84 ALQTLKVTKELGKFT-DLR---TALLVGGDSLEEQFEALAS-NPDIIIATPGRLLHLLVEMNLKLSS-VEYVVFDEADRL 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 350610602 188 LEIGFRDDLETISgilneknSKSADNIKTLLFSATL 223
Cdd:cd17959 158 FEMGFAEQLHEIL-------SRLPENRQTLLFSATL 186
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
34-237 |
1.30e-41 |
|
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: 148.56 E-value: 1.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 34 KAITRMEFPGLTPVQQKTIKPILSSEDhdVIARAKTGTGKTFAFLIPIFQHLINTKFDSQYmVKAVIVAPTRDLALQIEA 113
Cdd:cd17947 3 RALSSLGFTKPTPIQAAAIPLALLGKD--ICASAVTGSGKTAAFLLPILERLLYRPKKKAA-TRVLVLVPTRELAMQCFS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 114 EVKKIH---DMNYGLkkyacvsLVGGTDFRAAMNKMnKLRPNIVIATPGRLIDVLEKYSNKFFRFVDYKVLDEADRLLEI 190
Cdd:cd17947 80 VLQQLAqftDITFAL-------AVGGLSLKAQEAAL-RARPDIVIATPGRLIDHLRNSPSFDLDSIEILVLDEADRMLEE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 350610602 191 GFRDDLETISGILNEknsksadNIKTLLFSATLDDKVQKLANNIMNK 237
Cdd:cd17947 152 GFADELKEILRLCPR-------TRQTMLFSATMTDEVKDLAKLSLNK 191
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
34-231 |
1.82e-41 |
|
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin gene, NUP98, by inversion 11 (p15q22) chromosome translocation is found in the patients with de novo or therapy-related myeloid malignancies. Diseases associated with DDX10 (also known as DDX10-NUP98 Fusion Protein Type 2) include myelodysplastic syndrome and leukemia, acute myeloid. DDX10 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: 350699 [Multi-domain] Cd Length: 198 Bit Score: 148.21 E-value: 1.82e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 34 KAITRMEFPGLTPVQQKTIKPILssEDHDVIARAKTGTGKTFAFLIPIFQHLINTKFDSQYMVKAVIVAPTRDLALQIEA 113
Cdd:cd17941 3 KGLKEAGFIKMTEIQRDSIPHAL--QGRDILGAAKTGSGKTLAFLVPLLEKLYRERWTPEDGLGALIISPTRELAMQIFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 114 EVKKI---HDMNYGLkkyacvsLVGGTDFRAAMNKMNklRPNIVIATPGRLIDVLEkySNKFFRFVDYK--VLDEADRLL 188
Cdd:cd17941 81 VLRKVgkyHSFSAGL-------IIGGKDVKEEKERIN--RMNILVCTPGRLLQHMD--ETPGFDTSNLQmlVLDEADRIL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 350610602 189 EIGFRddlETISGILNEKNSKSadniKTLLFSATLDDKVQKLA 231
Cdd:cd17941 150 DMGFK---ETLDAIVENLPKSR----QTLLFSATQTKSVKDLA 185
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
36-259 |
2.84e-41 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 148.02 E-value: 2.84e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 36 ITRMEFPGLTPVQQKTIKPILSSEdHDVIARAKTGTGKTFAFLIPIFQHLINTKFdsqymVKAVIVAPTRDLALQIEAEV 115
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGL-RDVILAAPTGSGKTLAALLPALEALKRGKG-----GRVLVLVPTRELAEQWAEEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 116 KKIHDMNYGLkkyaCVSLVGGTDFRAAMNKMNKLRPNIVIATPGRLIDVLEKySNKFFRFVDYKVLDEADRLLEIGFRDD 195
Cdd:smart00487 75 KKLGPSLGLK----VVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLEN-DKLSLSNVDLVILDEAHRLLDGGFGDQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 350610602 196 LETISGILNEknsksadNIKTLLFSATLDDKVQKLANNIMNkkECLFLDtvdkNEPEAHERIDQ 259
Cdd:smart00487 150 LEKLLKLLPK-------NVQLLLLSATPPEEIENLLELFLN--DPVFID----VGFTPLEPIEQ 200
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
34-237 |
6.58e-41 |
|
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and PRP28 homolog) is involved in pre-mRNA splicing and its phosphorylated form (by SRPK2) is required for spliceosomal B complex formation. Diseases associated with DDX23 include distal hereditary motor neuropathy, type II. DDX23 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: 350703 [Multi-domain] Cd Length: 220 Bit Score: 147.47 E-value: 6.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 34 KAITRMEFPGLTPVQQKTIkPIlSSEDHDVIARAKTGTGKTFAFLIPIFQHLIN----TKFDSQYMVKAVIVAPTRDLAL 109
Cdd:cd17945 3 RVIRKLGYKEPTPIQRQAI-PI-GLQNRDIIGIAETGSGKTAAFLIPLLVYISRlpplDEETKDDGPYALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 110 QIEAEVKKIHDMnYGLKkyaCVSLVGGtdfRAAMNKMNKLRP--NIVIATPGRLIDVLEkysNKFFRF--VDYKVLDEAD 185
Cdd:cd17945 81 QIEEETQKFAKP-LGIR---VVSIVGG---HSIEEQAFSLRNgcEILIATPGRLLDCLE---RRLLVLnqCTYVVLDEAD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 350610602 186 RLLEIGFRDDL--------------ETISGILNEKNSKSAdNIKTLLFSATLDDKVQKLANNIMNK 237
Cdd:cd17945 151 RMIDMGFEPQVtkildampvsnkkpDTEEAEKLAASGKHR-YRQTMMFTATMPPAVEKIAKGYLRR 215
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
45-235 |
1.53e-40 |
|
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: 145.81 E-value: 1.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 45 TPVQQKTIkPILSSEdHDVIARAKTGTGKTFAFLIPIFQHLINTKfdSQYMVKAVIVAPTRDLALQIEAEVKKIHDmNYG 124
Cdd:cd17957 14 TPIQMQAI-PILLHG-RDLLACAPTGSGKTLAFLIPILQKLGKPR--KKKGLRALILAPTRELASQIYRELLKLSK-GTG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 125 LKkyaCVSLVGGTDFRAAMNKMNKLRPNIVIATPGRLIDVLEKySNKFFRFVDYKVLDEADRLLEIGFRDDLETISGILN 204
Cdd:cd17957 89 LR---IVLLSKSLEAKAKDGPKSITKYDILVSTPLRLVFLLKQ-GPIDLSSVEYLVLDEADKLFEPGFREQTDEILAACT 164
|
170 180 190
....*....|....*....|....*....|.
gi 350610602 205 EKnsksadNIKTLLFSATLDDKVQKLANNIM 235
Cdd:cd17957 165 NP------NLQRSLFSATIPSEVEELARSVM 189
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
37-232 |
7.21e-40 |
|
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) plays a role in ribosome biogenesis and TP53/p53 regulation through its interaction with NPM1. DDX31 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: 350707 [Multi-domain] Cd Length: 214 Bit Score: 144.65 E-value: 7.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 37 TRMEFPGLTPVQQKTIKPILSseDHDVIARAKTGTGKTFAFLIPIFQHLIN--TKFDSQYMVKAVIVAPTRDLALQIEAE 114
Cdd:cd17949 7 SKMGIEKPTAIQKLAIPVLLQ--GRDVLVRSQTGSGKTLAYLLPIIQRLLSlePRVDRSDGTLALVLVPTRELALQIYEV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 115 VKKIhdmnygLKKYA-CV--SLVGGTdfRAAMNKMnKLRP--NIVIATPGRLIDVLEKYSNkfFRF--VDYKVLDEADRL 187
Cdd:cd17949 85 LEKL------LKPFHwIVpgYLIGGE--KRKSEKA-RLRKgvNILIATPGRLLDHLKNTQS--FDVsnLRWLVLDEADRL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 350610602 188 LEIGFRDDLETISGILNEKNSKSAD------NIKTLLFSATLDDKVQKLAN 232
Cdd:cd17949 154 LDMGFEKDITKILELLDDKRSKAGGekskpsRRQTVLVSATLTDGVKRLAG 204
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
24-246 |
1.51e-39 |
|
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DEAD-box helicases are 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: 350810 [Multi-domain] Cd Length: 264 Bit Score: 145.11 E-value: 1.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 24 EEGVLDKEIHKAITRMEFPGLTPVQQKTIkPILSSeDHDVIARAKTGTGKTFAFLIPIFQHLIN-----TKFDSQYMVKA 98
Cdd:cd18052 46 EEANLCETLLKNIRKAGYEKPTPVQKYAI-PIILA-GRDLMACAQTGSGKTAAFLLPVLTGMMKegltaSSFSEVQEPQA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 99 VIVAPTRDLALQIEAEVKKihdMNYGLKKYACVsLVGGTdfrAAMNKMNKLRP--NIVIATPGRLIDVLEKySNKFFRFV 176
Cdd:cd18052 124 LIVAPTRELANQIFLEARK---FSYGTCIRPVV-VYGGV---SVGHQIRQIEKgcHILVATPGRLLDFIGR-GKISLSKL 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 177 DYKVLDEADRLLEIGFRDDletISGILNEKNSKSADNIKTLLFSATLDDKVQKLANNIMNkKECLFLdTV 246
Cdd:cd18052 196 KYLILDEADRMLDMGFGPE---IRKLVSEPGMPSKEDRQTLMFSATFPEEIQRLAAEFLK-EDYLFL-TV 260
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
28-230 |
3.99e-38 |
|
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of infectious West Nile virus particles. New research suggests that DDX56 relocalizes to the site of virus assembly during WNV infection and that its interaction with WNV capsid in the cytoplasm may occur transiently during virion morphogenesis. DDX56 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: 350719 [Multi-domain] Cd Length: 206 Bit Score: 139.64 E-value: 3.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 28 LDKEIHKAITRMEFPGLTPVQQKTIKPILssEDHDVIARAKTGTGKTFAFLIPIFQHLINTKFDS--QYMVKAVIVAPTR 105
Cdd:cd17961 1 LDPRLLKAIAKLGWEKPTLIQSKAIPLAL--EGKDILARARTGSGKTAAYALPIIQKILKAKAESgeEQGTRALILVPTR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 106 DLALQIEAEVKKIhdMNYGLKKYACVSLVGGTDFRAAMNKMNKLrPNIVIATPGRLIDVLEKYSNKFFRFVDYKVLDEAD 185
Cdd:cd17961 79 ELAQQVSKVLEQL--TAYCRKDVRVVNLSASSSDSVQRALLAEK-PDIVVSTPARLLSHLESGSLLLLSTLKYLVIDEAD 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 350610602 186 RLLEIGFRDDLETISGILneknsksADNIKTLLFSATLDDKVQKL 230
Cdd:cd17961 156 LVLSYGYEEDLKSLLSYL-------PKNYQTFLMSATLSEDVEAL 193
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
28-429 |
7.83e-38 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 148.07 E-value: 7.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 28 LDKEIHKAITRMEFPGLTPVQQKTIKPILSSEDhdVIARAKTGTGKTFAFLIPIFQHLINTKFDSQYMVkaviVAPTRDL 107
Cdd:PRK11634 13 LKAPILEALNDLGYEKPSPIQAECIPHLLNGRD--VLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILV----LAPTREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 108 ALQIeAEVkkIHDMNYGLKKYACVSLVGGTDFRAamnKMNKLR--PNIVIATPGRLIDVLEK----YSNkffrfVDYKVL 181
Cdd:PRK11634 87 AVQV-AEA--MTDFSKHMRGVNVVALYGGQRYDV---QLRALRqgPQIVVGTPGRLLDHLKRgtldLSK-----LSGLVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 182 DEADRLLEIGFRDDLETISgilneknSKSADNIKTLLFSATLDDKVQKLANNIMNkkeclfldtvdknEPEaHERIDQSV 261
Cdd:PRK11634 156 DEADEMLRMGFIEDVETIM-------AQIPEGHQTALFSATMPEAIRRITRRFMK-------------EPQ-EVRIQSSV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 262 VISEKFANSiFAAVEHIKK-----QIKERDSNYKAIIFAPTVKFTSFLCSILKnefKKDLPILEFHGKITQNKRTSLVKR 336
Cdd:PRK11634 215 TTRPDISQS-YWTVWGMRKnealvRFLEAEDFDAAIIFVRTKNATLEVAEALE---RNGYNSAALNGDMNQALREQTLER 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 337 FKKDESGILVCTDVGARGMDFPNVHEVLQIGVPSELANYIHRIGRTARSGKEGSSVLFICKDELPFVRELEDAKNIVIAK 416
Cdd:PRK11634 291 LKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPE 370
|
410
....*....|...
gi 350610602 417 QEKyePSEEIKSE 429
Cdd:PRK11634 371 VEL--PNAELLGK 381
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
34-235 |
1.47e-37 |
|
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: 137.55 E-value: 1.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 34 KAITRMEFPGLTPVQQKTIKPILSSEDhdVIARAKTGTGKTFAFLIPIFQHLIntkfDSQYMVK-----AVIVAPTRDLA 108
Cdd:cd17952 3 NAIRKQEYEQPTPIQAQALPVALSGRD--MIGIAKTGSGKTAAFIWPMLVHIM----DQRELEKgegpiAVIVAPTRELA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 109 LQIEAEVKKIHDMnYGLKkyaCVSLVGGTDfRAAMNKMNKLRPNIVIATPGRLIDVLEKYSNKFFRfVDYKVLDEADRLL 188
Cdd:cd17952 77 QQIYLEAKKFGKA-YNLR---VVAVYGGGS-KWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQR-VTYLVLDEADRMF 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 350610602 189 EIGFRDDLETISGILNEKNsksadniKTLLFSATLDDKVQKLANNIM 235
Cdd:cd17952 151 DMGFEYQVRSIVGHVRPDR-------QTLLFSATFKKKIEQLARDIL 190
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
257-395 |
1.49e-37 |
|
C-terminal helicase domain of the 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. They are superfamily (SF)2 helicases that, similar to SF1, 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: 350174 [Multi-domain] Cd Length: 131 Bit Score: 135.33 E-value: 1.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 257 IDQSVVISEKFANsifaaVEHIKKQIKERDSNYKAIIFAPTVKFTSFLCSILKnefKKDLPILEFHGKITQNKRTSLVKR 336
Cdd:cd18787 1 IKQLYVVVEEEEK-----KLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLE---ELGIKVAALHGDLSQEERERALKK 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 350610602 337 FKKDESGILVCTDVGARGMDFPNVHEVLQIGVPSELANYIHRIGRTARSGKEGSSVLFI 395
Cdd:cd18787 73 FRSGKVRVLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
32-239 |
2.09e-37 |
|
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box protein, which shows little similarity to any of the other known human DEAD box proteins, but shows a high similarity to mouse Ddx24 at the amino acid level. MDM2 mediates nonproteolytic polyubiquitylation of the DEAD-Box RNA helicase DDX24. DDX24 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: 350704 [Multi-domain] Cd Length: 235 Bit Score: 138.53 E-value: 2.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 32 IHKAITRMEFPGLTPVQQKTIKPILSSEdHDVIARAKTGTGKTFAFLIPIFQHLI-----NTKFDSQYMVKAVIVAPTRD 106
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAAIRDG-KDVIGAAETGSGKTLAFGIPILERLLsqkssNGVGGKQKPLRALILTPTRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 107 LALQIEAEVKKIhdmnyglKKYA---CVSLVGGTdfraAMNKMNKL---RPNIVIATPGRLIDVLEKySNKF---FRFVD 177
Cdd:cd17946 80 LAVQVKDHLKAI-------AKYTnikIASIVGGL----AVQKQERLlkkRPEIVVATPGRLWELIQE-GNEHlanLKSLR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 350610602 178 YKVLDEADRLLEIGFRDDLETISGILNEKNSKSADNIKTLLFSATLD-DKVQKLANNIMNKKE 239
Cdd:cd17946 148 FLVLDEADRMLEKGHFAELEKILELLNKDRAGKKRKRQTFVFSATLTlDHQLPLKLNSKKKKK 210
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
28-237 |
3.20e-36 |
|
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: 134.81 E-value: 3.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 28 LDKEIHKAITRMEFPGLTPVQQKTIKPILSSEDhdVIARAKTGTGKTFAFLIPIFQHLINTKF--DSQYMVkAVIVAPTR 105
Cdd:cd17953 19 LSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRD--VIGIAKTGSGKTLAFLLPMFRHIKDQRPvkPGEGPI-GLIMAPTR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 106 DLALQIEAEVKKIHDMnYGLKkyaCVSLVGGTDFRAAMNKMnKLRPNIVIATPGRLIDVLEKYSNKF--FRFVDYKVLDE 183
Cdd:cd17953 96 ELALQIYVECKKFSKA-LGLR---VVCVYGGSGISEQIAEL-KRGAEIVVCTPGRMIDILTANNGRVtnLRRVTYVVLDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 350610602 184 ADRLLEIGFRDDLETIsgilneknsksADNIK----TLLFSATLDDKVQKLANNIMNK 237
Cdd:cd17953 171 ADRMFDMGFEPQIMKI-----------VNNIRpdrqTVLFSATFPRKVEALARKVLHK 217
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
40-406 |
3.22e-34 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 136.07 E-value: 3.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 40 EFPglTPVQQKTIKPILSSEDhdVIARAKTGTGKTFAFLIPIFQHLinTKFDSQYMVK-----AVIVAPTRDLALQIEAE 114
Cdd:PLN00206 142 EFP--TPIQMQAIPAALSGRS--LLVSADTGSGKTASFLVPIISRC--CTIRSGHPSEqrnplAMVLTPTRELCVQVEDQ 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 115 VKKihdMNYGLK-KYACVslVGGTdfrAAMNKMNKLRPNI--VIATPGRLIDVLEKYsNKFFRFVDYKVLDEADRLLEIG 191
Cdd:PLN00206 216 AKV---LGKGLPfKTALV--VGGD---AMPQQLYRIQQGVelIVGTPGRLIDLLSKH-DIELDNVSVLVLDEVDCMLERG 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 192 FRDDLETISGILNEKnsksadniKTLLFSATLDDKVQKLANNIMnkKECLFLDTVDKNEPeaheridqsvvisEKFANSI 271
Cdd:PLN00206 287 FRDQVMQIFQALSQP--------QVLLFSATVSPEVEKFASSLA--KDIILISIGNPNRP-------------NKAVKQL 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 272 FAAVEHIKKQIKERDSNYKAIIFAPTVkfTSFLCSILKNEFKKD-------LPILEFHGKITQNKRTSLVKRFKKDESGI 344
Cdd:PLN00206 344 AIWVETKQKKQKLFDILKSKQHFKPPA--VVFVSSRLGADLLANaitvvtgLKALSIHGEKSMKERREVMKSFLVGEVPV 421
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 350610602 345 LVCTDVGARGMDFPNVHEVLQIGVPSELANYIHRIGRTARSGKEGSSVLFICKDELPFVREL 406
Cdd:PLN00206 422 IVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPEL 483
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
47-237 |
1.56e-33 |
|
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: 126.67 E-value: 1.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 47 VQQKTIKPILSSedHDVIARAKTGTGKTFAFLIPIFQHLINTKFDSQymvkAVIVAPTRDLALQIEAEVKKIHDMnYGLK 126
Cdd:cd17939 23 IQQRAIVPIIKG--RDVIAQAQSGTGKTATFSIGALQRIDTTVRETQ----ALVLAPTRELAQQIQKVVKALGDY-MGVK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 127 KYACvslVGGTDFRAAMNKMNKlRPNIVIATPGRLIDVLEKYSnKFFRFVDYKVLDEADRLLEIGFRDDLETISGILNEK 206
Cdd:cd17939 96 VHAC---IGGTSVREDRRKLQY-GPHIVVGTPGRVFDMLQRRS-LRTDKIKMFVLDEADEMLSRGFKDQIYDIFQFLPPE 170
|
170 180 190
....*....|....*....|....*....|.
gi 350610602 207 nsksadnIKTLLFSATLDDKVQKLANNIMNK 237
Cdd:cd17939 171 -------TQVVLFSATMPHEVLEVTKKFMRD 194
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
24-235 |
1.41e-32 |
|
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: 123.97 E-value: 1.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 24 EEGVLDkEIHKAITRMEFPGLTPVQQKTIKPILSSedHDVIARAKTGTGKTFAFLIPIFQhlintkfdsqyMVKAVIVAP 103
Cdd:cd17938 3 ELGVMP-ELIKAVEELDWLLPTDIQAEAIPLILGG--GDVLMAAETGSGKTGAFCLPVLQ-----------IVVALILEP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 104 TRDLALQIEAEVKKihdmnygLKKY------ACVSLVGGTDFRAAMnKMNKLRPNIVIATPGRLIDVLEKYSNKfFRFVD 177
Cdd:cd17938 69 SRELAEQTYNCIEN-------FKKYldnpklRVALLIGGVKAREQL-KRLESGVDIVVGTPGRLEDLIKTGKLD-LSSVR 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 350610602 178 YKVLDEADRLLEigfRDDLETISGILNE--KNSKSADNIKTLLFSATL-DDKVQKLANNIM 235
Cdd:cd17938 140 FFVLDEADRLLS---QGNLETINRIYNRipKITSDGKRLQVIVCSATLhSFEVKKLADKIM 197
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
32-235 |
4.09e-32 |
|
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis antigen 13 or helical antigen) displays tumor-specific expression. Diseases associated with DDX43 include rheumatoid lung disease. DDX53 is also called cancer/testis antigen 26 or DEAD-Box Protein CAGE. Both DDX46 and DDX53 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: 350716 [Multi-domain] Cd Length: 197 Bit Score: 122.57 E-value: 4.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 32 IHKAITRMEFPGLTPVQQKTIKPILSSedHDVIARAKTGTGKTFAFLIPIFQHLIN--TKFDSQYMVKAVIVAPTRDLAL 109
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQG--IDLIGVAQTGTGKTLAYLLPGFIHLDLqpIPREQRNGPGVLVLTPTRELAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 110 QIEAEVKKihdmnYGLKKYACVSLVGGTDFRAAMNKMNKlRPNIVIATPGRLIDVLEKYSNKfFRFVDYKVLDEADRLLE 189
Cdd:cd17958 79 QIEAECSK-----YSYKGLKSVCVYGGGNRNEQIEDLSK-GVDIIIATPGRLNDLQMNNVIN-LKSITYLVLDEADRMLD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 350610602 190 IGFRDDLETIsgILNEKNSKsadniKTLLFSATLDDKVQKLANNIM 235
Cdd:cd17958 152 MGFEPQIRKI--LLDIRPDR-----QTIMTSATWPDGVRRLAQSYL 190
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
32-236 |
7.40e-32 |
|
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 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: 350724 [Multi-domain] Cd Length: 197 Bit Score: 121.71 E-value: 7.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 32 IHKAITRMEFPGLTPVQQKTIKPILSSedHDVIARAKTGTGKTFAFLIPIFQHlINtkfDSQYMV-----KAVIVAPTRD 106
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSG--RDMVGIAQTGSGKTLAFLLPAIVH-IN---AQPPLErgdgpIVLVLAPTRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 107 LALQIEAEVKKIHDMNYglKKYACVslVGGTDfraamnKMNKLR-----PNIVIATPGRLIDVLEKYSNKFFRfVDYKVL 181
Cdd:cd17966 75 LAQQIQQEANKFGGSSR--LRNTCV--YGGAP------KGPQIRdlrrgVEICIATPGRLIDFLDQGKTNLRR-VTYLVL 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 350610602 182 DEADRLLEIGFRDDLETISGILNEknsksadNIKTLLFSATLDDKVQKLANNIMN 236
Cdd:cd17966 144 DEADRMLDMGFEPQIRKIVDQIRP-------DRQTLMWSATWPKEVRRLAEDFLK 191
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
28-235 |
8.81e-32 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation factor 4A-I (DDX2A) and eukaryotic initiation factor 4A-II (DDX2B) are involved in cap recognition and are required for mRNA binding to ribosome. They are 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: 350804 [Multi-domain] Cd Length: 201 Bit Score: 121.78 E-value: 8.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 28 LDKEIHKAITRMEFPGLTPVQQKTIKPILssEDHDVIARAKTGTGKTFAFLIPIFQHlINTKFDSqymVKAVIVAPTRDL 107
Cdd:cd18046 6 LKESLLRGIYAYGFEKPSAIQQRAIMPCI--KGYDVIAQAQSGTGKTATFSISILQQ-IDTSLKA---TQALVLAPTREL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 108 ALQIEAEVKKIHDMnYGLKKYACvslVGGTDFRAAMNKMnKLRPNIVIATPGRLIDVLEKysnKFFRFVDYK--VLDEAD 185
Cdd:cd18046 80 AQQIQKVVMALGDY-MGIKCHAC---IGGTSVRDDAQKL-QAGPHIVVGTPGRVFDMINR---RYLRTDYIKmfVLDEAD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 350610602 186 RLLEIGFRDDLETISGILNEknsksadNIKTLLFSATLDDKVQKLANNIM 235
Cdd:cd18046 152 EMLSRGFKDQIYDIFQKLPP-------DTQVVLLSATMPNDVLEVTTKFM 194
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
24-237 |
7.67e-31 |
|
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or p54) participates in mRNA regulation mediated by miRNA-mediated silencing. It also plays a role in global and transcript-specific messenger RNA (mRNA) storage, translational repression, and decay. It is a member of the DEAD-box helicase family, 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: 350698 [Multi-domain] Cd Length: 201 Bit Score: 119.32 E-value: 7.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 24 EEGVLDKEIHKAITRMEFPGLTPVQQKTIKPILSSedHDVIARAKTGTGKTFAFLIPIFQHlINTKFDSqymVKAVIVAP 103
Cdd:cd17940 2 EDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSG--RDILARAKNGTGKTGAYLIPILEK-IDPKKDV---IQALILVP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 104 TRDLALQIEAEVKKihdmnygLKKYA---CVSLVGGTDFRAAMNKMNKlRPNIVIATPGRLIDVLEKYSNKFFRfVDYKV 180
Cdd:cd17940 76 TRELALQTSQVCKE-------LGKHMgvkVMVTTGGTSLRDDIMRLYQ-TVHVLVGTPGRILDLAKKGVADLSH-CKTLV 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 350610602 181 LDEADRLLEIGFRDDLETISGILNEKNsksadniKTLLFSATLDDKVQKLANNIMNK 237
Cdd:cd17940 147 LDEADKLLSQDFQPIIEKILNFLPKER-------QILLFSATFPLTVKNFMDRHMHN 196
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
45-243 |
2.98e-29 |
|
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD box, X isoform, or DDX14) has been reported to display a high level of RNA-independent ATPase activity stimulated by both RNA and DNA. This protein has multiple conserved domains and is thought to play roles in both the nucleus and cytoplasm. Nuclear roles include transcriptional regulation, mRNP assembly, pre-mRNA splicing, and mRNA export. In the cytoplasm, this protein is thought to be involved in translation, cellular signaling, and viral replication. Misregulation of this gene has been implicated in tumorigenesis. Diseases associated with DDX3 include mental retardation, X-linked 102 and agenesis of the corpus callosum, with facial anomalies and robin sequence. DDX3 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: 350809 [Multi-domain] Cd Length: 249 Bit Score: 116.29 E-value: 2.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 45 TPVQQKTIkPILSSEdHDVIARAKTGTGKTFAFLIPIFQHLI-----------NTKFDS--QYMVkAVIVAPTRDLALQI 111
Cdd:cd18051 45 TPVQKHAI-PIIKSK-RDLMACAQTGSGKTAAFLLPILSQIYeqgpgeslpseSGYYGRrkQYPL-ALVLAPTRELASQI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 112 EAEVKKihdMNYGLKKYACVsLVGGTDFRAAMNKMNKlRPNIVIATPGRLIDVLE--KYSNKFFRFVdykVLDEADRLLE 189
Cdd:cd18051 122 YDEARK---FAYRSRVRPCV-VYGGADIGQQMRDLER-GCHLLVATPGRLVDMLErgKIGLDYCKYL---VLDEADRMLD 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 350610602 190 IGFRddlETISGILNEKNSKSADNIKTLLFSATLDDKVQKLANNIMNkkECLFL 243
Cdd:cd18051 194 MGFE---PQIRRIVEQDTMPPTGERQTLMFSATFPKEIQMLARDFLD--NYIFL 242
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
32-231 |
4.15e-29 |
|
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by regulating multiple signalling pathways. Mammalian DEAD box protein Ddx51 acts in 3' end maturation of 28S rRNA by promoting the release of U8 snoRNA.It 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: 350714 [Multi-domain] Cd Length: 231 Bit Score: 115.42 E-value: 4.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 32 IHKAITRMEFPGLTPVQQKTIKPILSSEDH-------DVIARAKTGTGKTFAFLIPIFQhLINTKFDSQymVKAVIVAPT 104
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLPSSKStppyrpgDLCVSAPTGSGKTLAYVLPIVQ-ALSKRVVPR--LRALIVVPT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 105 RDLALQIEAEVKKIHDmNYGLKKyacVSLVGGTDFRAAMNKMNKL-------RPNIVIATPGRLIDVLEKYSNKFFRFVD 177
Cdd:cd17956 78 KELVQQVYKVFESLCK-GTGLKV---VSLSGQKSFKKEQKLLLVDtsgrylsRVDILVATPGRLVDHLNSTPGFTLKHLR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 350610602 178 YKVLDEADRLLEIGFRDDLETI--------SGILNEKNSKSADNIKT-----LLFSATLDDKVQKLA 231
Cdd:cd17956 154 FLVIDEADRLLNQSFQDWLETVmkalgrptAPDLGSFGDANLLERSVrplqkLLFSATLTRDPEKLS 220
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
44-238 |
1.60e-27 |
|
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: 109.94 E-value: 1.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 44 LTPVQQKTIKPILSSEDhdVIARAKTGTGKTFAFLIPIFQHLintKFDSQYMV-----KAVIVAPTRDLALQIEAEVKKI 118
Cdd:cd17944 13 LFPIQVKTFHPVYSGKD--LIAQARTGTGKTFSFAIPLIEKL---QEDQQPRKrgrapKVLVLAPTRELANQVTKDFKDI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 119 hdmnygLKKYACVSLVGGTDFRAAMNKMnKLRPNIVIATPGRLIDVLEKYSNKFFRfVDYKVLDEADRLLEIGFRDDLET 198
Cdd:cd17944 88 ------TRKLSVACFYGGTPYQQQIFAI-RNGIDILVGTPGRIKDHLQNGRLDLTK-LKHVVLDEVDQMLDMGFAEQVEE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 350610602 199 ISGILNEKNSKsaDNIKTLLFSATLDDKVQKLANNIMNKK 238
Cdd:cd17944 160 ILSVSYKKDSE--DNPQTLLFSATCPDWVYNVAKKYMKSQ 197
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
34-233 |
6.08e-27 |
|
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: 107.74 E-value: 6.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 34 KAITRMEFPGLTPVQQKTIKPILSSedHDVIARAKTGTGKTFAFLIPIFQHLINtkfdSQYMVKAVIVAPTRDLALQIEA 113
Cdd:cd17943 3 EGLKAAGFQRPSPIQLAAIPLGLAG--HDLIVQAKSGTGKTLVFVVIALESLDL----ERRHPQVLILAPTREIAVQIHD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 114 EVKKIHDMNYGLKkyaCVSLVGGTDFRAAMNKMNklRPNIVIATPGRLIDVLEKYSNKFFRfVDYKVLDEADRLLEIGFR 193
Cdd:cd17943 77 VFKKIGKKLEGLK---CEVFIGGTPVKEDKKKLK--GCHIAVGTPGRIKQLIELGALNVSH-VRLFVLDEADKLMEGSFQ 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 350610602 194 DDLETISGILNEknsksadNIKTLLFSAT----LDDKVQKLANN 233
Cdd:cd17943 151 KDVNWIFSSLPK-------NKQVIAFSATypknLDNLLARYMRK 187
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
28-235 |
6.43e-27 |
|
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called DEAD box RNA helicase DEAD5) and DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH)) 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: 350721 [Multi-domain] Cd Length: 196 Bit Score: 108.05 E-value: 6.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 28 LDKEIHKAITRMEFPGLTPVQQKTIKPILSSEDHDVIARAKTGTGKTFAFLIPIFQHLINTKFDSQymvkAVIVAPTRDL 107
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPLILSDPPENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQ----ALCLAPTREL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 108 ALQIEAEVKKIhdMNY-GLKKYACVSlvgGTDFRAAmnkmNKLRPNIVIATPGRLIDVLEKysnkffRFVDYK-----VL 181
Cdd:cd17963 77 ARQIGEVVEKM--GKFtGVKVALAVP---GNDVPRG----KKITAQIVIGTPGTVLDWLKK------RQLDLKkikilVL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 350610602 182 DEADRLLEI-GFRDDLETISGILNeknsksaDNIKTLLFSATLDDKVQKLANNIM 235
Cdd:cd17963 142 DEADVMLDTqGHGDQSIRIKRMLP-------RNCQILLFSATFPDSVRKFAEKIA 189
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
45-233 |
5.83e-25 |
|
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts with several spliceosomal proteins and may recognize the bacterial second messengers cyclic di-GMP and cyclic di-AMP, resulting in the induction of genes involved in the innate immune response. Diseases associated with DDX41 include "myeloproliferative/lymphoproliferative neoplasms, familial" and "Ddx41-related susceptibility to familial myeloproliferative/lymphoproliferative neoplasms". DDX41 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: 350709 [Multi-domain] Cd Length: 206 Bit Score: 102.80 E-value: 5.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 45 TPVQQKTIKPILSSEDhdVIARAKTGTGKTFAFLIPifqhLINTKFDSQYMVK--------AVIVAPTRDLALQ----IE 112
Cdd:cd17951 14 TPIQMQGLPTILSGRD--MIGIAFTGSGKTLVFTLP----LIMFALEQEKKLPfikgegpyGLIVCPSRELARQthevIE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 113 AEVKKIHDMnyGLKKYACVSLVGGTDFRAAMNKMNKlRPNIVIATPGRLIDVLEKysNKF-FRFVDYKVLDEADRLLEIG 191
Cdd:cd17951 88 YYCKALQEG--GYPQLRCLLCIGGMSVKEQLEVIRK-GVHIVVATPGRLMDMLNK--KKInLDICRYLCLDEADRMIDMG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 350610602 192 FRDDLETIsgILNEKNSKsadniKTLLFSATLDDKVQKLANN 233
Cdd:cd17951 163 FEEDIRTI--FSYFKGQR-----QTLLFSATMPKKIQNFAKS 197
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
40-235 |
3.21e-24 |
|
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: 100.32 E-value: 3.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 40 EFPglTPVQQKTIKPILSSEDhdVIARAKTGTGKTFAFLIPIFQHLInTKFDSQymvKAVIVAPTRDLALQIEAEVKkih 119
Cdd:cd17962 11 EVP--TPIQMQMIPVGLLGRD--ILASADTGSGKTAAFLLPVIIRCL-TEHRNP---SALILTPTRELAVQIEDQAK--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 120 DMNYGLKKYACVSLVGGTDFRAAMNKMnKLRPNIVIATPGRLIDVLEKYSNKFFRfVDYKVLDEADRLLEIGFRDD---- 195
Cdd:cd17962 80 ELMKGLPPMKTALLVGGLPLPPQLYRL-QQGVKVIIATPGRLLDILKQSSVELDN-IKIVVVDEADTMLKMGFQQQvldi 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 350610602 196 LETISgilneknsksaDNIKTLLFSATLDDKVQKLANNIM 235
Cdd:cd17962 158 LENIS-----------HDHQTILVSATIPRGIEQLAGQLL 186
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
275-386 |
6.93e-24 |
|
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: 96.51 E-value: 6.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 275 VEHIKKQIKERdSNYKAIIFAPTVKFTSflCSILKNefKKDLPILEFHGKITQNKRTSLVKRFKKDESGILVCTDVGARG 354
Cdd:pfam00271 3 LEALLELLKKE-RGGKVLIFSQTKKTLE--AELLLE--KEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERG 77
|
90 100 110
....*....|....*....|....*....|..
gi 350610602 355 MDFPNVHEVLQIGVPSELANYIHRIGRTARSG 386
Cdd:pfam00271 78 LDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
28-243 |
6.61e-23 |
|
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and is required for the export of mRNA out of the nucleus. DDX39B is an essential splicing factor required for association of U2 small nuclear ribonucleoprotein with pre-mRNA, and it also plays an important role in mRNA export from the nucleus to the cytoplasm. Diseases associated with DDX39A (also called UAP56-Related Helicase, 49 kDa) include gastrointestinal stromal tumor and inflammatory bowel disease 6, while diseases associated with DDX39B (also called 56 kDa U2AF65-Associated Protein) include Plasmodium vivax malaria. DDX39 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: 350708 [Multi-domain] Cd Length: 208 Bit Score: 97.03 E-value: 6.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 28 LDKEIHKAITRMEFPGLTPVQQKTI-KPILSsedHDVIARAKTGTGKTFAFLIPIFQHLinTKFDSQymVKAVIVAPTRD 106
Cdd:cd17950 9 LKPELLRAIVDCGFEHPSEVQHECIpQAILG---MDVLCQAKSGMGKTAVFVLSTLQQL--EPVDGQ--VSVLVICHTRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 107 LALQIEAEVKKihdmnygLKKY------ACVslVGGTDFRAAMNKMNKLRPNIVIATPGRLIDVLEKYSNKFFRfVDYKV 180
Cdd:cd17950 82 LAFQISNEYER-------FSKYmpnvktAVF--FGGVPIKKDIEVLKNKCPHIVVGTPGRILALVREKKLKLSH-VKHFV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 350610602 181 LDEADRLLE-IGFRDDLETIsgILNEKNSKsadniKTLLFSATLDDKVQKLANNIMNKKECLFL 243
Cdd:cd17950 152 LDECDKMLEqLDMRRDVQEI--FRATPHDK-----QVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
303-386 |
4.77e-21 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 87.27 E-value: 4.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 303 FLCSILKnefKKDLPILEFHGKITQNKRTSLVKRFKKDESGILVCTDVGARGMDFPNVHEVLQIGVPSELANYIHRIGRT 382
Cdd:smart00490 2 ELAELLK---ELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78
|
....
gi 350610602 383 ARSG 386
Cdd:smart00490 79 GRAG 82
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
14-235 |
6.03e-20 |
|
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, G17P1, or HUMP68) is involved in pathways that include the alteration of RNA structures, plays a role as a coregulator of transcription, a regulator of splicing, and in the processing of small noncoding RNAs. It synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. Dysregulation of this gene may play a role in cancer development. DDX5 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: 350807 [Multi-domain] Cd Length: 234 Bit Score: 89.30 E-value: 6.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 14 SKEVTLDSL--------LEEGVLDKEIHKAITRMEFPGLTPVQQKTIKPILSSEDhdVIARAKTGTGKTFAFLIPIFQHL 85
Cdd:cd18049 9 SKEITVRGHncpkpvlnFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLD--MVGVAQTGSGKTLSYLLPAIVHI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 86 INTKF----DSQYMVkavIVAPTRDLALQIE---AEVKKIHDMnyglkKYACVslVGGTDFRAAMNKMNKlRPNIVIATP 158
Cdd:cd18049 87 NHQPFlergDGPICL---VLAPTRELAQQVQqvaAEYGRACRL-----KSTCI--YGGAPKGPQIRDLER-GVEICIATP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 159 GRLIDVLEKYSNKFFRfVDYKVLDEADRLLEIGFRDDLETIsgilneknsksADNIK----TLLFSATLDDKVQKLANNI 234
Cdd:cd18049 156 GRLIDFLEAGKTNLRR-CTYLVLDEADRMLDMGFEPQIRKI-----------VDQIRpdrqTLMWSATWPKEVRQLAEDF 223
|
.
gi 350610602 235 M 235
Cdd:cd18049 224 L 224
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
28-237 |
1.88e-19 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor 4A-III (EIF4AIII, also known as DDX48) is part of the exon junction complex (EJC) that plays a major role in posttranscriptional regulation of mRNA. EJC consists of four proteins (eIF4AIII, Barentsz [Btz], Mago, and Y14), mRNA, and ATP. DDX48 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: 350803 [Multi-domain] Cd Length: 201 Bit Score: 86.75 E-value: 1.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 28 LDKEIHKAITRMEFPGLTPVQQKTIKPILSSEDhdVIARAKTGTGKTFAFLIPIFQHLINTKFDSQymvkAVIVAPTRDL 107
Cdd:cd18045 6 LREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRD--VIAQSQSGTGKTATFSISVLQCLDIQVRETQ----ALILSPTREL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 108 ALQIEAEVKKIHD-MNygLKKYACvslVGGTDFRAAMNKMNKlRPNIVIATPGRLIDVLEKYSNKfFRFVDYKVLDEADR 186
Cdd:cd18045 80 AVQIQKVLLALGDyMN--VQCHAC---IGGTSVGDDIRKLDY-GQHIVSGTPGRVFDMIRRRSLR-TRHIKMLVLDEADE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 350610602 187 LLEIGFRDDLETISGILNEKnsksadnIKTLLFSATLDDKVQKLANNIMNK 237
Cdd:cd18045 153 MLNKGFKEQIYDVYRYLPPA-------TQVVLVSATLPQDILEMTNKFMTD 196
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
35-236 |
1.63e-18 |
|
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 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: 350706 [Multi-domain] Cd Length: 231 Bit Score: 84.73 E-value: 1.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 35 AITRMEFPGLTPVQQKTIKPILSSEdHDVIArAKTGTGKTFAFLIPIFQ------HLINTKFDSqymVKAVIVAPTRDLA 108
Cdd:cd17948 4 ILQRQGITKPTTVQKQGIPSILRGR-NTLCA-AETGSGKTLTYLLPIIQrllrykLLAEGPFNA---PRGLVITPSRELA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 109 LQIEAEVKKIHDmNYGLKkyacVSLVGGTDFRAAMNKMNKLRPNIVIATPGRLIDVLEK--YSNKFFRFVdykVLDEADR 186
Cdd:cd17948 79 EQIGSVAQSLTE-GLGLK----VKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSriYSLEQLRHL---VLDEADT 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 350610602 187 LLEIGFRDDLETI------SGILNEKNSKSADNIKTLLFSATLDDKVQKLANNIMN 236
Cdd:cd17948 151 LLDDSFNEKLSHFlrrfplASRRSENTDGLDPGTQLVLVSATMPSGVGEVLSKVID 206
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
61-222 |
5.99e-18 |
|
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: 80.91 E-value: 5.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 61 HDVIARAKTGTGKTFAFLIPIFQHLINTKFdsqymvKAVIVAPTRDLALQIEAEVKKIHDMNyglkkYACVSLVGGTDFR 140
Cdd:cd00046 2 ENVLITAPTGSGKTLAALLAALLLLLKKGK------KVLVLVPTKALALQTAERLRELFGPG-----IRVAVLVGGSSAE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 141 AamNKMNKLRPN-IVIATPGRLIDVLEKYSNKFFRFVDYKVLDEADRLLEIGFRDDLETISGILneknsKSADNIKTLLF 219
Cdd:cd00046 71 E--REKNKLGDAdIIIATPDMLLNLLLREDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRK-----AGLKNAQVILL 143
|
...
gi 350610602 220 SAT 222
Cdd:cd00046 144 SAT 146
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
45-235 |
1.22e-17 |
|
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or DEAD Box Protein P82) has a wide variety of functions including regulating the alternative splicing of exons exhibiting specific features such as the inclusion of AC-rich alternative exons in CD44 transcripts, playing a role in innate immunity, and promoting mRNA degradation mediated by the antiviral zinc-finger protein ZC3HAV1 in an ATPase-dependent manner. DDX17 synergizes with DDX5 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. DDX17 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: 350808 [Multi-domain] Cd Length: 271 Bit Score: 83.14 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 45 TPVQQKTIKPILSSEDhdVIARAKTGTGKTFAFLIPIFQHlINTKfdsQYMVKA-----VIVAPTRDLALQieaeVKKIH 119
Cdd:cd18050 86 TPIQCQGFPLALSGRD--MVGIAQTGSGKTLAYLLPAIVH-INHQ---PYLERGdgpicLVLAPTRELAQQ----VQQVA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 120 DmNYGLK---KYACVslVGGTDFRAAMNKMNKlRPNIVIATPGRLIDVLEKYSNKfFRFVDYKVLDEADRLLEIGFRDDL 196
Cdd:cd18050 156 D-DYGKSsrlKSTCI--YGGAPKGPQIRDLER-GVEICIATPGRLIDFLEAGKTN-LRRCTYLVLDEADRMLDMGFEPQI 230
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 350610602 197 ETIsgilneknsksADNIK----TLLFSATLDDKVQKLANNIM 235
Cdd:cd18050 231 RKI-----------VDQIRpdrqTLMWSATWPKEVRQLAEDFL 262
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
42-512 |
3.03e-14 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 75.45 E-value: 3.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 42 PGLTPVQQK---TIKPILSSEDHDVIARAKTGTGKTFAFLIpIFQHLINTKfdsqymvKAVIVAPTRDLALQIEAEvkki 118
Cdd:COG1061 79 FELRPYQQEaleALLAALERGGGRGLVVAPTGTGKTVLALA-LAAELLRGK-------RVLVLVPRRELLEQWAEE---- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 119 hdmnygLKKYACVSLVGGTDfraamnkmNKLRPNIVIATPGRLIdvLEKYSNKFFRFVDYKVLDEADRLLEIGFRDdlet 198
Cdd:COG1061 147 ------LRRFLGDPLAGGGK--------KDSDAPITVATYQSLA--RRAHLDELGDRFGLVIIDEAHHAGAPSYRR---- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 199 isgILNEKNSKsadniKTLLFSATL--DDKVQKLANNIMNK---------------KECLFLDTVDKNEPEAHERIDQSV 261
Cdd:COG1061 207 ---ILEAFPAA-----YRLGLTATPfrSDGREILLFLFDGIvyeyslkeaiedgylAPPEYYGIRVDLTDERAEYDALSE 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 262 VISEKFANSIFAAVEHIKKQIKERDSNYKAIIFAPTVKFTSFLCSILKnefKKDLPILEFHGKITQNKRTSLVKRFKKDE 341
Cdd:COG1061 279 RLREALAADAERKDKILRELLREHPDDRKTLVFCSSVDHAEALAELLN---EAGIRAAVVTGDTPKKEREEILEAFRDGE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 342 SGILVCTDVGARGMDFPNVhEVLQIGVPSE-LANYIHRIGRTAR--SGKEGSSVLFICKDELPFVRELedAKNIVIAKQE 418
Cdd:COG1061 356 LRILVTVDVLNEGVDVPRL-DVAILLRPTGsPREFIQRLGRGLRpaPGKEDALVYDFVGNDVPVLEEL--AKDLRDLAGY 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 419 KYEPSEEIKSEVLEAVTEEPEDISDiVISLISSYRSCIKEYRFSERRILPEIASTYGVLLNDPQLKIPVSRRFLDKLGLS 498
Cdd:COG1061 433 RVEFLDEEESEELALLIAVKPALEV-KGELEEELLEELELLEDALLLVLAELLLLELLALALELLELAKAEGKAEEEEEE 511
|
490
....*....|....
gi 350610602 499 RSPIGKAMFEIRDY 512
Cdd:COG1061 512 KELLLLLALAKLLK 525
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
45-234 |
1.82e-13 |
|
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 (MRH4) plays an essential role during the late stages of mitochondrial ribosome or mitoribosome assembly by promoting remodeling of the 21S rRNA-protein interactions. MRH4 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: 350723 [Multi-domain] Cd Length: 251 Bit Score: 70.48 E-value: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 45 TPVQQKTIKPILSSE---------DHD------VIArAKTGTGKTFAFLIPIFQHL----INTKFDSQY---------MV 96
Cdd:cd17965 32 SPIQTLAIKKLLKTLmrkvtkqtsNEEpklevfLLA-AETGSGKTLAYLAPLLDYLkrqeQEPFEEAEEeyesakdtgRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 97 KAVIVAPTRDLALQIEAEVKKI-HDMNYGLKKYAcvslVGGTDFRAAMNKMNKLRPNIVIATPGRLIDvLEKYSNKFFRF 175
Cdd:cd17965 111 RSVILVPTHELVEQVYSVLKKLsHTVKLGIKTFS----SGFGPSYQRLQLAFKGRIDILVTTPGKLAS-LAKSRPKILSR 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 350610602 176 VDYKVLDEADRLLEIGFRDDleTISGIlneknsKSADNIKTLLF-SAT----LDDKVQKLANNI 234
Cdd:cd17965 186 VTHLVVDEADTLFDRSFLQD--TTSII------KRAPKLKHLILcSATipkeFDKTLRKLFPDV 241
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
23-235 |
7.03e-13 |
|
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both mRNA (mRNA) export from the nucleus into the cytoplasm and in mRNA translation. DDX19 functions in the nucleus in resolving RNA:DNA hybrids (R-loops). Activation of a DNA damage response pathway dependent upon the ATR kinase, a major regulator of replication fork progression, stimulates translocation of DDX19 from the cytoplasm into the nucleus. Only nuclear Ddx19 is competent to resolve R-loops. DDX19 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: 350805 [Multi-domain] Cd Length: 205 Bit Score: 67.82 E-value: 7.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 23 LEEGVLDKEIHKAITRMEFPGLTPVQQKTIKPILSSEDHDVIARAKTGTGKTFAFLIPIFQHLINTKFDSQymvkAVIVA 102
Cdd:cd18047 3 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEPPQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQ----CLCLS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 103 PTRDLALQIEaevKKIHDMNyglKKYACVSLVGGTDFRaAMNKMNKLRPNIVIATPGRLIDVLEKysnkfFRFVDYK--- 179
Cdd:cd18047 79 PTYELALQTG---KVIEQMG---KFYPELKLAYAVRGN-KLERGQKISEQIVIGTPGTVLDWCSK-----LKFIDPKkik 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 350610602 180 --VLDEADRLLEI-GFRDDLETISGILNEknsksadNIKTLLFSATLDDKVQKLANNIM 235
Cdd:cd18047 147 vfVLDEADVMIATqGHQDQSIRIQRMLPR-------NCQMLLFSATFEDSVWKFAQKVV 198
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
6-235 |
1.07e-12 |
|
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH) is a testis-specific protein essential for completion of spermatogenesis. DDX25 is also a novel negative regulator of IFN pathway and facilitates RNA virus infection. Diseases associated with DDX25 include hydrolethalus syndrome, an autosomal recessive lethal malformation syndrome characterized by multiple developmental defects of fetus.. DDX25 (also called gonadotropin-regulated testicular RNA helicase) 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: 350806 [Multi-domain] Cd Length: 229 Bit Score: 67.74 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 6 IHVPKEDNSKEVTLDSLLEEGVLDKEIHKAITRMEFPGLTPVQQKTIKPILSSEDHDVIARAKTGTGKTFAFLIPIFQHL 85
Cdd:cd18048 3 VEVLQRDPTSPLFSVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADPPQNLIAQSQSGTGKTAAFVLAMLSRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 86 INTKFDSQYMVkaviVAPTRDLALQIEAEVKKIHDMNYGLK-KYAcvslVGGTdfraAMNKMNKLRPNIVIATPGRLIDV 164
Cdd:cd18048 83 DALKLYPQCLC----LSPTFELALQTGKVVEEMGKFCVGIQvIYA----IRGN----RPGKGTDIEAQIVIGTPGTVLDW 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 350610602 165 LEKysnkfFRFVDYK-----VLDEADRLLEI-GFRDDLETISGILneknsksADNIKTLLFSATLDDKVQKLANNIM 235
Cdd:cd18048 151 CFK-----LRLIDVTnisvfVLDEADVMINVqGHSDHSVRVKRSM-------PKECQMLLFSATFEDSVWAFAERIV 215
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
44-225 |
3.69e-12 |
|
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: 64.98 E-value: 3.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 44 LTPVQQKTIKPILSSEDHDVIArAKTGTGKTFAFLIPIFQHLINTKFdsqymvKAVIVAPTRDLALQIEAEVKKIHDMNY 123
Cdd:cd17921 2 LNPIQREALRALYLSGDSVLVS-APTSSGKTLIAELAILRALATSGG------KAVYIAPTRALVNQKEADLRERFGPLG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 124 GLkkyaCVSLVGGTDfraaMNKMNKLRPNIVIATPGRLIDVLEKYSNKFFRFVDYKVLDEAdRLLEIGFR-DDLE-TISG 201
Cdd:cd17921 75 KN----VGLLTGDPS----VNKLLLAEADILVATPEKLDLLLRNGGERLIQDVRLVVVDEA-HLIGDGERgVVLElLLSR 145
|
170 180
....*....|....*....|....
gi 350610602 202 ILNEknsksADNIKTLLFSATLDD 225
Cdd:cd17921 146 LLRI-----NKNARFVGLSATLPN 164
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
25-393 |
1.12e-09 |
|
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: 61.39 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 25 EGVLDKEIHKAITRMEFPGLTPVQQKTIKPILssEDHDVIARAKTGTGKTFAFLIPIFQHLINtkfDSQymVKAVIVAPT 104
Cdd:COG1205 38 PDWLPPELRAALKKRGIERLYSHQAEAIEAAR--AGKNVVIATPTASGKSLAYLLPVLEALLE---DPG--ATALYLYPT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 105 RDLAL-QieaeVKKIHDMNYGLkkyacvslvgGTDFRAA-------MNKMNKLR--PNIVIATPgrliDVL--------E 166
Cdd:COG1205 111 KALARdQ----LRRLRELAEAL----------GLGVRVAtydgdtpPEERRWIRehPDIVLTNP----DMLhygllphhT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 167 KYSnKFFRFVDYKVLDEA---------------DRLLEIgfrddletisgilneknsksADNIKT----LLFSATLDDKV 227
Cdd:COG1205 173 RWA-RFFRNLRYVVIDEAhtyrgvfgshvanvlRRLRRI--------------------CRHYGSdpqfILASATIGNPA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 228 QkLANNIMNKKeclfLDTVDKNEPEAHER----IDQSVVISEKFANSIFAAVEHIKKQIKErdsNYKAIIFAPTVKFTSF 303
Cdd:COG1205 232 E-HAERLTGRP----VTVVDEDGSPRGERtfvlWNPPLVDDGIRRSALAEAARLLADLVRE---GLRTLVFTRSRRGAEL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 304 LCSILKNEFKK-DLP--ILEFHGKITQNKRTSLVKRFKKDESGILVCT-------DVGarGMDFpnvheVLQIGVPSELA 373
Cdd:COG1205 304 LARYARRALREpDLAdrVAAYRAGYLPEERREIERGLRSGELLGVVSTnalelgiDIG--GLDA-----VVLAGYPGTRA 376
|
410 420
....*....|....*....|
gi 350610602 374 NYIHRIGRTARSGKEGSSVL 393
Cdd:COG1205 377 SFWQQAGRAGRRGQDSLVVL 396
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
270-395 |
1.35e-09 |
|
C-terminal helicase domain of LHR family helicases; 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. LHR family 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: 350183 [Multi-domain] Cd Length: 150 Bit Score: 56.89 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 270 SIFAAVEHIKKQIKERDSNykaIIFAPTVKFTSFLCSILKNEFKKDLPILEF---HGKITQNKRTSLVKRFKKDESGILV 346
Cdd:cd18796 23 SGADAYAEVIFLLERHKST---LVFTNTRSQAERLAQRLRELCPDRVPPDFIalhHGSLSRELREEVEAALKRGDLKVVV 99
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 350610602 347 CTDVGARGMDFPNVHEVLQIGVPSELANYIHRIGRTARSGKEGSSVLFI 395
Cdd:cd18796 100 ATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGHRPGAASKGRLV 148
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
56-184 |
3.41e-09 |
|
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: 56.44 E-value: 3.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 56 LSSEDHDVIARAKTGTGKTFAFLIPIFQHLIntkfdSQYMVKAVIVAPTRDLALQIEAEVKKIhdMNYGLKKYACVSLVG 135
Cdd:cd17923 11 AARAGRSVVVTTGTASGKSLCYQLPILEALL-----RDPGSRALYLYPTKALAQDQLRSLREL--LEQLGLGIRVATYDG 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 350610602 136 GTDfRAAMNKMNKLRPNIVIATPgrliDVLE-------KYSNKFFRFVDYKVLDEA 184
Cdd:cd17923 84 DTP-REERRAIIRNPPRILLTNP----DMLHyallphhDRWARFLRNLRYVVLDEA 134
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
275-447 |
1.04e-08 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 58.20 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 275 VEHIKKQIKERDSNyKAIIFaptvkfTSF--LCSILKNEFKKD-LPILEFHGK--------ITQNKRTSLVKRFKKDESG 343
Cdd:COG1111 341 REILKEQLGTNPDS-RIIVF------TQYrdTAEMIVEFLSEPgIKAGRFVGQaskegdkgLTQKEQIEILERFRAGEFN 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 344 ILVCTDVGARGMDFPNVHEVLQI-GVPSELaNYIHRIGRTARSGkEGSSVLFICK---DELPF---VRELEDAKNIV--- 413
Cdd:COG1111 414 VLVATSVAEEGLDIPEVDLVIFYePVPSEI-RSIQRKGRTGRKR-EGRVVVLIAKgtrDEAYYwssRRKEKKMKSILkkl 491
|
170 180 190
....*....|....*....|....*....|....*..
gi 350610602 414 ---IAKQEKYEPSEEIKSEVLEAVTEEPEDISDIVIS 447
Cdd:COG1111 492 kklLDKQEKEKLKESAQATLDEFESIKELAEDEINEK 528
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
344-395 |
3.95e-06 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350172 [Multi-domain] Cd Length: 77 Bit Score: 45.00 E-value: 3.95e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 350610602 344 ILVCTDVGARGMDFPNVHEVLQIGVPSELANYIHRIGRTAR-SGKEGSSVLFI 395
Cdd:cd18785 25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRgGKDEGEVILFV 77
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
273-429 |
6.47e-06 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 49.10 E-value: 6.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 273 AAVEHIKKQIKERDSNyKAIIFAP---TVKF-TSFLcsiLKNEFKkdlpILEFHGK--------ITQNKRTSLVKRFKKD 340
Cdd:PRK13766 351 KLREIVKEQLGKNPDS-RIIVFTQyrdTAEKiVDLL---EKEGIK----AVRFVGQaskdgdkgMSQKEQIEILDKFRAG 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 341 ESGILVCTDVGARGMDFPNVHEVLQI-GVPSELaNYIHRIGRTARsGKEGSSVLFICK---DELPF----------VREL 406
Cdd:PRK13766 423 EFNVLVSTSVAEEGLDIPSVDLVIFYePVPSEI-RSIQRKGRTGR-QEEGRVVVLIAKgtrDEAYYwssrrkekkmKEEL 500
|
170 180
....*....|....*....|...
gi 350610602 407 EDAKNIVIAKQEKYEPSEEIKSE 429
Cdd:PRK13766 501 KNLKGILNKKLQELDEEQKGEEE 523
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
62-401 |
6.50e-06 |
|
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DEAD/DEAH box helicase DNA helicase cas3'; Often but not always is fused to HD nuclease domain; signature gene for Type I
Pssm-ID: 187770 [Multi-domain] Cd Length: 353 Bit Score: 48.58 E-value: 6.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 62 DVIARAKTGTGKTFAFLIPIFQHLINTKFDsqymvKAVIVAPTRDLALQIEAEVKKIHDMNYGLKKYACVS---LVGGTD 138
Cdd:cd09639 1 LLVIEAPTGYGKTEAALLWALHSLKSQKAD-----RVIIALPTRATINAMYRRAKEAFGETGLYHSSILSSrikEMGDSE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 139 FRAAMNKMNKLRPNIVIATPGRL--IDVLEKYSNKFFRFVDYK---------VLDEADrLLEIGFRDDLETISGILNEKN 207
Cdd:cd09639 76 EFEHLFPLYIHSNDTLFLDPITVctIDQVLKSVFGEFGHYEFTlasiansllIFDEVH-FYDEYTLALILAVLEVLKDND 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 208 sksadnIKTLLFSATLDDKVQKLANNIMNKKECLFLDTVD-KNEPEAHerIDQSVVISEKFANSIfaavehikkqIKERD 286
Cdd:cd09639 155 ------VPILLMSATLPKFLKEYAEKIGYVEENEPLDLKPnERAPFIK--IESDKVGEISSLERL----------LEFIK 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 287 SNYKAIIFAPTVKfTSFLCSILKNEFKKDLPILEFHGKITQN----KRTSLVKRFKKDESGILVCTDVGARGMDFPNVHE 362
Cdd:cd09639 217 KGGSVAIIVNTVD-RAQEFYQQLKEKGPEEEIMLIHSRFTEKdrakKEAELLLEFKKSEKFVIVATQVIEASLDISVDVM 295
|
330 340 350
....*....|....*....|....*....|....*....
gi 350610602 363 VLQIGVPSELanyIHRIGRTARSGKEGSSVLFICKDELP 401
Cdd:cd09639 296 ITELAPIDSL---IQRLGRLHRYGEKNGEEVYIITDAPD 331
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
251-354 |
1.77e-05 |
|
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350180 [Multi-domain] Cd Length: 135 Bit Score: 44.77 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 251 PEAHERidqsvVISEKFAnsifAAVEHIKKQIKERDsnyKAIIFAptvKFTSFLcSILKNEFKK-DLPILEFHGKITQNK 329
Cdd:cd18793 2 PPKIEE-----VVSGKLE----ALLELLEELREPGE---KVLIFS---QFTDTL-DILEEALRErGIKYLRLDGSTSSKE 65
|
90 100
....*....|....*....|....*..
gi 350610602 330 RTSLVKRFKKDESG--ILVCTDVGARG 354
Cdd:cd18793 66 RQKLVDRFNEDPDIrvFLLSTKAGGVG 92
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
280-394 |
4.30e-05 |
|
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350181 [Multi-domain] Cd Length: 134 Bit Score: 43.35 E-value: 4.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 280 KQIKERDSNYKAIIFAPTVKFTSFLCSILKnefKKDLPILEFHGKITQNKRTSLVKRFKKDESGILVCTDvgARGM--DF 357
Cdd:cd18794 22 KRIKVEHLGGSGIIYCLSRKECEQVAARLQ---SKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATV--AFGMgiDK 96
|
90 100 110
....*....|....*....|....*....|....*..
gi 350610602 358 PNVHEVLQIGVPSELANYIHRIGRTARSGKEGSSVLF 394
Cdd:cd18794 97 PDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILF 133
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
275-395 |
5.81e-05 |
|
C-terminal helicase domain of Fanconi anemia group M family helicases; 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. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef 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: 350188 [Multi-domain] Cd Length: 143 Bit Score: 43.50 E-value: 5.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 275 VEHIKKqiKERDSNYKAIIFaptvkfTSFLCSILK--NEFKKDLPIL---EFHGK--------ITQNKRTSLVKRFKKDE 341
Cdd:cd18801 19 KEHFKK--KQEGSDTRVIIF------SEFRDSAEEivNFLSKIRPGIratRFIGQasgksskgMSQKEQKEVIEQFRKGG 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 350610602 342 SGILVCTDVGARGMDFPNVHEVLQI-GVPSELANyIHRIGRTARsGKEGSSVLFI 395
Cdd:cd18801 91 YNVLVATSIGEEGLDIGEVDLIICYdASPSPIRM-IQRMGRTGR-KRQGRVVVLL 143
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
275-382 |
5.89e-05 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 45.99 E-value: 5.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 275 VEHIKKQIKE-RDSNYKAIIFAptvKFTSFLcSILKNEF-KKDLPILEFHGKITQNKRTSLVKRFKKDESG--ILVCTDV 350
Cdd:COG0553 535 LEALLELLEElLAEGEKVLVFS---QFTDTL-DLLEERLeERGIEYAYLHGGTSAEERDELVDRFQEGPEApvFLISLKA 610
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 350610602 351 GARGMDF--------------PNVHEvlQ-IGvpselanYIHRIGRT 382
Cdd:COG0553 611 GGEGLNLtaadhvihydlwwnPAVEE--QaID-------RAHRIGQT 648
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
31-226 |
9.22e-05 |
|
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: 43.47 E-value: 9.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 31 EIHKAITRMEFPGLtpvqQKT-IKPILSSEDHDVIAraKTGTGKT-FAFLIPIFqhlintkFDSQYMvKAVIVAPTRDLA 108
Cdd:cd17924 8 EFFKKKTGFPPWGA----QRTwAKRLLRGKSFAIIA--PTGVGKTtFGLATSLY-------LASKGK-RSYLIFPTKSLV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 109 LQIEAEVKKihdmnYGLKKYACVSLV---GGTDFRAAMNKMNKLRP---NIVIATPGRLIDVLEKYSNKFFRFVdykVLD 182
Cdd:cd17924 74 KQAYERLSK-----YAEKAGVEVKILvyhSRLKKKEKEELLEKIEKgdfDILVTTNQFLSKNFDLLSNKKFDFV---FVD 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 350610602 183 EADRLLeigfrddletisgilneKNSKSAD------NIKTLLF-SATLDDK 226
Cdd:cd17924 146 DVDAVL-----------------KSSKNIDrllkllGFGQLVVsSATGRPR 179
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
69-223 |
1.61e-04 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 42.29 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 69 TGTGKTFaFLIPIFQHLINTKFdsqymvkaVIVAPTRDLALQIEAEVKkihdmNYGLKKYacVSLVGGTDFRAAMNKmnk 148
Cdd:cd17926 27 TGSGKTL-TALALIAYLKELRT--------LIVVPTDALLDQWKERFE-----DFLGDSS--IGLIGGGKKKDFDDA--- 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 350610602 149 lrpNIVIATPgRLIDVLEKYSNKFFRFVDYKVLDEADRLleigfrdDLETISGILNEKNSKsadniKTLLFSATL 223
Cdd:cd17926 88 ---NVVVATY-QSLSNLAEEEKDLFDQFGLLIVDEAHHL-------PAKTFSEILKELNAK-----YRLGLTATP 146
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
60-183 |
3.22e-04 |
|
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: 41.41 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 60 DHDVIARAKTGTGKTFAFLIPIFQHLINTKFDSqymVKAVIVAPTRDLALQIEAEVKK-IHDMNYGLKkyacVSLVGGTD 138
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEKG---VQVLYISPLKALINDQERRLEEpLDEIDLEIP----VAVRHGDT 73
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 350610602 139 FRAAMNKMNKLRPNIVIATPGRL--IDVLEKYSNKfFRFVDYKVLDE 183
Cdd:cd17922 74 SQSEKAKQLKNPPGILITTPESLelLLVNKKLREL-FAGLRYVVVDE 119
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
60-184 |
4.32e-04 |
|
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: 41.87 E-value: 4.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 60 DHDVIARAKTGTGKTF--AFLIPIFQHLINtKFDSQYMVkAVIVAPTRDLALQiEAEVKKIHdmnYGLKKYACVSLVGGT 137
Cdd:cd18034 16 KRNTIVVLPTGSGKTLiaVMLIKEMGELNR-KEKNPKKR-AVFLVPTVPLVAQ-QAEAIRSH---TDLKVGEYSGEMGVD 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 350610602 138 DFRAAMNKMNKLRPNIVIATPGRLIDVLekySNKFFRFVDYKVL--DEA 184
Cdd:cd18034 90 KWTKERWKEELEKYDVLVMTAQILLDAL---RHGFLSLSDINLLifDEC 135
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
304-393 |
6.11e-04 |
|
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It 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: 350198 [Multi-domain] Cd Length: 159 Bit Score: 40.79 E-value: 6.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 304 LCSILKNEFKKDLPILEFHGKITQNKRTSLVKRFKKDESGILVCTDVGARGMDFPNVhEVLQIGVPSELA-NYIHRI-GR 381
Cdd:cd18811 50 MYEYLKERFRPELNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNA-TVMVIEDAERFGlSQLHQLrGR 128
|
90
....*....|..
gi 350610602 382 TARSGKEGSSVL 393
Cdd:cd18811 129 VGRGDHQSYCLL 140
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
275-394 |
1.04e-03 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 41.67 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 275 VEHIKKQikERDSnykAIIFAPTVKFTSFLCSILKnefKKDLPILEFHGKITQNKRTSLVKRFKKDESGILVCTDvgARG 354
Cdd:COG0514 222 LDFLKEH--PGGS---GIVYCLSRKKVEELAEWLR---EAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATI--AFG 291
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 350610602 355 M--DFPNVHEVLQIGVPSELANYIHRIGRTARSGKEGSSVLF 394
Cdd:COG0514 292 MgiDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLL 333
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
321-394 |
1.43e-03 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 41.81 E-value: 1.43e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 350610602 321 FHGKITQNKRTSLVKRFKKDESGILVCTDVGARGMDFPNVHEVLQIGVPSELANYIHRIGRTARSGKEGSSVLF 394
Cdd:PLN03137 710 YHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQECGRAGRDGQRSSCVLY 783
|
|
| DinG |
COG1199 |
Rad3-related DNA helicase DinG [Replication, recombination and repair]; |
41-196 |
1.60e-03 |
|
Rad3-related DNA helicase DinG [Replication, recombination and repair];
Pssm-ID: 440812 [Multi-domain] Cd Length: 629 Bit Score: 41.45 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 41 FPGLTP--VQQKTIKPILSS--EDHDVIARAKTGTGKTFAFLIPIFQHLINTKfdsqymvKAVIVApTRDLALQ---IEA 113
Cdd:COG1199 10 FPGFEPrpGQREMAEAVARAlaEGRHLLIEAGTGTGKTLAYLVPALLAARETG-------KKVVIS-TATKALQeqlVEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 114 EVKKIHDmnyglkkyacvslVGGTDFRAAM--NKMNKLRPNiviatpgRLIDVLEKYSNKFFRFVDYKVLDEADRLLEIG 191
Cdd:COG1199 82 DLPLLRK-------------ALGLPLRVALlkGRSNYLCLR-------RLEQALQEGDDLDDEELLLARILAWASETWTG 141
|
....*
gi 350610602 192 FRDDL 196
Cdd:COG1199 142 DRDEL 146
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
322-389 |
1.96e-03 |
|
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF 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: 350197 [Multi-domain] Cd Length: 151 Bit Score: 38.86 E-value: 1.96e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 350610602 322 HGKITQNKRTSLVKRFKKDESGILVCTDVGARGMDFPN-----VHEVLQIGvpseLANYIHRIGRTARSGKEG 389
Cdd:cd18810 58 HGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNantiiIERADKFG----LAQLYQLRGRVGRSKERA 126
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
44-222 |
2.01e-03 |
|
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: 39.32 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 44 LTPVQQKTIKPIL----SSEDHDVIARAKTGTGKTFAFLIPIFQHLINTKfdsqymvKAVIVAPTRDLALQIEAEVKKIH 119
Cdd:cd17918 16 LTKDQAQAIKDIEkdlhSPEPMDRLLSGDVGSGKTLVALGAALLAYKNGK-------QVAILVPTEILAHQHYEEARKFL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 120 -DMNyglkkyacVSLVGGtDFRAAMnkmnKLRPNIVIATPGrLIDVLEKYSNkffrfVDYKVLDEADRLleigfrddlet 198
Cdd:cd17918 89 pFIN--------VELVTG-GTKAQI----LSGISLLVGTHA-LLHLDVKFKN-----LDLVIVDEQHRF----------- 138
|
170 180
....*....|....*....|....
gi 350610602 199 isGILNEKNSKSADNIKTLLFSAT 222
Cdd:cd17918 139 --GVAQREALYNLGATHFLEATAT 160
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
44-445 |
2.24e-03 |
|
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: 40.84 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 44 LTPVQQK---TIKPILSSEDHDVIARAKTGTGKTFAFLIPIFQHLINTKFDsqymvKAVIVAPTRDLALQIEAEVKKI-- 118
Cdd:COG1203 128 INPLQNEaleLALEAAEEEPGLFILTAPTGGGKTEAALLFALRLAAKHGGR-----RIIYALPFTSIINQTYDRLRDLfg 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 119 -----HDMNYGLKKYACVSLVGGTDFRAAMNKMNKLRPnIVIATPGRLIDVLEKYSN----KFFRFVdYKV--LDEADrL 187
Cdd:COG1203 203 edvllHHSLADLDLLEEEEEYESEARWLKLLKELWDAP-VVVTTIDQLFESLFSNRKgqerRLHNLA-NSViiLDEVQ-A 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 188 LEIgfrDDLETISGILNE-KNSksadNIKTLLFSATL-DDKVQKLANNImnkkeCLFLDTVDKNEPEAHERIDQSVVISE 265
Cdd:COG1203 280 YPP---YMLALLLRLLEWlKNL----GGSVILMTATLpPLLREELLEAY-----ELIPDEPEELPEYFRAFVRKRVELKE 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 266 KFANSifaavEHIKKQIKERDSNYK--AIIFApTVKFTSFLCSILKNEFKKDlPILEFHGKITQNKRT----SLVKRFKK 339
Cdd:COG1203 348 GPLSD-----EELAELILEALHKGKsvLVIVN-TVKDAQELYEALKEKLPDE-EVYLLHSRFCPADRSeiekEIKERLER 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 340 DESGILVCT-------DVgargmDFPNVHevlqigvpSELANY---IHRIGRTARSGK-EGSSVLFICKdelpfvreLED 408
Cdd:COG1203 421 GKPCILVSTqvveagvDI-----DFDVVI--------RDLAPLdslIQRAGRCNRHGRkEEEGNVYVFD--------PED 479
|
410 420 430
....*....|....*....|....*....|....*..
gi 350610602 409 AKNIVIAKQEKYEPSEEIKSEVLEAVTEEPEDISDIV 445
Cdd:COG1203 480 EGGGYVYDKPLLERTRELLREHDEILPEDKRELIEEY 516
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
44-193 |
2.53e-03 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 38.81 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350610602 44 LTPVQQKTIKPIL---SSEDHDVIARAKTGTGKTFaflipIFQHLINTKFDSQYMVKAVIVAPTRDLALQIEAEVKKihd 120
Cdd:pfam04851 4 LRPYQIEAIENLLesiKNGQKRGLIVMATGSGKTL-----TAAKLIARLFKKGPIKKVLFLVPRKDLLEQALEEFKK--- 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 350610602 121 mnYGLKKY-ACVSLVGGTDFRAAMNKmnklrpNIVIATPGRLIDVLEKYSNKFFR-FVDYKVLDEADRLLEIGFR 193
Cdd:pfam04851 76 --FLPNYVeIGEIISGDKKDESVDDN------KIVVTTIQSLYKALELASLELLPdFFDVIIIDEAHRSGASSYR 142
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
322-393 |
7.37e-03 |
|
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350179 [Multi-domain] Cd Length: 160 Bit Score: 37.63 E-value: 7.37e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 350610602 322 HGKITQNKRTSLVKRFKKDESGILVCTDVGARGMDFPN-----VHEVLQIGVpSELanyiHRI-GRTARSGKEGSSVL 393
Cdd:cd18792 67 HGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNantmiIEDADRFGL-SQL----HQLrGRVGRGKHQSYCYL 139
|
|
| mfd |
TIGR00580 |
transcription-repair coupling factor (mfd); All proteins in this family for which functions ... |
322-389 |
8.65e-03 |
|
transcription-repair coupling factor (mfd); All proteins in this family for which functions are known are DNA-dependent ATPases that function in the process of transcription-coupled DNA repair in which the repair of the transcribed strand of actively transcribed genes is repaired at a higher rate than the repair of non-transcribed regions of the genome and than the non-transcribed strand of the same gene. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). This family is closely related to the RecG and UvrB families. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273152 [Multi-domain] Cd Length: 926 Bit Score: 39.26 E-value: 8.65e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 350610602 322 HGKITQNKRTSLVKRFKKDESGILVCTDVGARGMDFPNVHEVL-----QIGVpSELanYIHRiGRTARSGKEG 389
Cdd:TIGR00580 693 HGQMTENELEEVMLEFYKGEFQVLVCTTIIETGIDIPNANTIIieradKFGL-AQL--YQLR-GRVGRSKKKA 761
|
|
| |
