|
Name |
Accession |
Description |
Interval |
E-value |
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
96-300 |
5.14e-147 |
|
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: 431.73 E-value: 5.14e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 96 GGFQSMGLSYPVFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKTHSAQTGARALILSPT 175
Cdd:cd17959 1 GGFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTVGARALILSPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 176 RELALQTLKFTKELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLVHVAVEMSLKLQSVEYVVFDEADRLFEM 255
Cdd:cd17959 81 RELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEM 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 164419743 256 GFAEQLQEIIARLPGGHQTVLFSATLPKLLVEFARAGLTEPVLIR 300
Cdd:cd17959 161 GFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLIR 205
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
98-462 |
6.23e-128 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 391.05 E-value: 6.23e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 98 FQSMGLSYPVFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKTHSAQtGARALILSPTRE 177
Cdd:COG0513 4 FADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPR-APQALILAPTRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 178 LALQTLKFTKELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLVHVAVEMSLKLQSVEYVVFDEADRLFEMGF 257
Cdd:COG0513 83 LALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMGF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 258 AEQLQEIIARLPGGHQTVLFSATLPKLLVEFARAGLTEPVLIRLDVDTKLNEQLKTSFFLVREDTKAAVLLHLLHnvVRP 337
Cdd:COG0513 163 IEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLR--DED 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 338 QDQTVVFVATKHHAEYLTELLTTQRVSCAHIYSALDPTARKINLAKFTLGKCSTLIVTDLAARGLDIPLLDNVINYSFPA 417
Cdd:COG0513 241 PERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPE 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 164419743 418 KGKLFLHRVGRVARAGRSGTAYSLVAPDEIPYLLDLHLFLGRSLT 462
Cdd:COG0513 321 DPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIE 365
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
109-300 |
4.82e-84 |
|
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: 267.39 E-value: 4.82e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 109 KGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKTHSAQTGA--RALILSPTRELALQTLKFT 186
Cdd:cd00268 3 KALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGRgpQALVLAPTRELAMQIAEVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 187 KELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLVHVAVEMSLKLQSVEYVVFDEADRLFEMGFAEQLQEIIA 266
Cdd:cd00268 83 RKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKILS 162
|
170 180 190
....*....|....*....|....*....|....
gi 164419743 267 RLPGGHQTVLFSATLPKLLVEFARAGLTEPVLIR 300
Cdd:cd00268 163 ALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
109-470 |
1.33e-79 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 264.11 E-value: 1.33e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 109 KGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERL----KTHSAQtgARALILSPTRELALQTLK 184
Cdd:PRK11192 14 EALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLldfpRRKSGP--PRILILTPTRELAMQVAD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 185 FTKELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLVHVAVEMSLKLQSVEYVVFDEADRLFEMGFAEQLQEI 264
Cdd:PRK11192 92 QARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRMLDMGFAQDIETI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 265 IARLPGGHQTVLFSATLP-KLLVEFARAGLTEPVLIrlDVDTKLNEQLKTSFFLVREDT---KAAVLLHLLHN--VVRpq 338
Cdd:PRK11192 172 AAETRWRKQTLLFSATLEgDAVQDFAERLLNDPVEV--EAEPSRRERKKIHQWYYRADDlehKTALLCHLLKQpeVTR-- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 339 dqTVVFVATKHHAEYLTELLTTQRVSCAHIYSALDPTARKINLAKFTLGKCSTLIVTDLAARGLDIPLLDNVINYSFPAK 418
Cdd:PRK11192 248 --SIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINFDMPRS 325
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 164419743 419 GKLFLHRVGRVARAGRSGTAYSLV-APDeipylldlHLFLGRsltLARPLKEP 470
Cdd:PRK11192 326 ADTYLHRIGRTGRAGRKGTAISLVeAHD--------HLLLGK---IERYIEEP 367
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
98-470 |
1.42e-72 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 245.87 E-value: 1.42e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 98 FQSMGLSYPVFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKTHSAQTGAR----ALILS 173
Cdd:PRK10590 3 FDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGRrpvrALILT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 174 PTRELALQTLKFTKELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLVHVAVEMSLKLQSVEYVVFDEADRLF 253
Cdd:PRK10590 83 PTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRML 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 254 EMGFAEQLQEIIARLPGGHQTVLFSATLPKLLVEFARAGLTEPVLIRLDVDTKLNEQLKTSFFLVREDTKAAVLLHLLHN 333
Cdd:PRK10590 163 DMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKRELLSQMIGK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 334 vvRPQDQTVVFVATKHHAEYLTELLTTQRVSCAHIYSALDPTARKINLAKFTLGKCSTLIVTDLAARGLDIPLLDNVINY 413
Cdd:PRK10590 243 --GNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNY 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 164419743 414 SFPAKGKLFLHRVGRVARAGRSGTAYSLVAPDEIPYLLDLHLFLGRSLT-LARPLKEP 470
Cdd:PRK10590 321 ELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEIPrIAIPGYEP 378
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
98-476 |
9.26e-72 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 243.94 E-value: 9.26e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 98 FQSMGLSYPVFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKThsAQTGARALILSPTRE 177
Cdd:PRK11776 6 FSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDV--KRFRVQALVLCPTRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 178 LALQTLKFTKELGKFT-GLKTALILGGDRMEDQFAALHENPDIIIATPGRLV-HVAVEmSLKLQSVEYVVFDEADRLFEM 255
Cdd:PRK11776 84 LADQVAKEIRRLARFIpNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILdHLRKG-TLDLDALNTLVLDEADRMLDM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 256 GFAEQLQEIIARLPGGHQTVLFSATLPKLLVEFARAGLTEPVLIRLDVDTKLN--EQLktsFFLVREDTK-AAVLLHLLH 332
Cdd:PRK11776 163 GFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDLPaiEQR---FYEVSPDERlPALQRLLLH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 333 NvvRPQdQTVVFVATKHHAEYLTELLTTQRVSCAHIYSALDPTARKINLAKFTLGKCSTLIVTDLAARGLDIPLLDNVIN 412
Cdd:PRK11776 240 H--QPE-SCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVIN 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164419743 413 YSFPAKGKLFLHRVGRVARAGRSGTAYSLVAPDEIPYLLDLHLFLGRSLTLArPLKEPSGVAGV 476
Cdd:PRK11776 317 YELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWE-PLPSLSPLSGV 379
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
107-300 |
6.09e-66 |
|
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: 218.66 E-value: 6.09e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 107 VFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKTHSAQTGA-RALILSPTRELALQTLKF 185
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRPKKKAAtRVLVLVPTRELAMQCFSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 186 TKELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLV-HVAVEMSLKLQSVEYVVFDEADRLFEMGFAEQLQEI 264
Cdd:cd17947 81 LQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIdHLRNSPSFDLDSIEILVLDEADRMLEEGFADELKEI 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 164419743 265 IARLPGGHQTVLFSATLPKLLVEFARAGLTEPVLIR 300
Cdd:cd17947 161 LRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRVF 196
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
98-441 |
4.14e-64 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 221.77 E-value: 4.14e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 98 FQSMGLSYPVFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKTHSAQTG-----ARALIL 172
Cdd:PRK04837 10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPAPEDrkvnqPRALIM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 173 SPTRELALQTLKFTKELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLVHVAVEMSLKLQSVEYVVFDEADRL 252
Cdd:PRK04837 90 APTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 253 FEMGFAEQLQEIIARLPGGHQ--TVLFSATLPKLLVEFARAGLTEPVLIRLDVDTKLNEQLKTSFFLVREDTKAAVLLHL 330
Cdd:PRK04837 170 FDLGFIKDIRWLFRRMPPANQrlNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEELFYPSNEEKMRLLQTL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 331 LHNvvRPQDQTVVFVATKHhaeyltellttqrvSCAHIYSALD-------------PTARKIN-LAKFTLGKCSTLIVTD 396
Cdd:PRK04837 250 IEE--EWPDRAIIFANTKH--------------RCEEIWGHLAadghrvglltgdvAQKKRLRiLEEFTRGDLDILVATD 313
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 164419743 397 LAARGLDIPLLDNVINYSFPAKGKLFLHRVGRVARAGRSGTAYSL 441
Cdd:PRK04837 314 VAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
120-288 |
1.47e-62 |
|
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: 208.25 E-value: 1.47e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 120 TPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKTHsaQTGARALILSPTRELALQTLKFTKELGKFTGLKTAL 199
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKL--DNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVAS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 200 ILGGDRMEDQFAALHeNPDIIIATPGRLVHVAVEMSlKLQSVEYVVFDEADRLFEMGFAEQLQEIIARLPGGHQTVLFSA 279
Cdd:pfam00270 79 LLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSA 156
|
....*....
gi 164419743 280 TLPKLLVEF 288
Cdd:pfam00270 157 TLPRNLEDL 165
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
104-446 |
3.12e-61 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 217.33 E-value: 3.12e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 104 SYP--VFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLkthSAQT------GARALILSPT 175
Cdd:PTZ00110 136 SFPdyILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHI---NAQPllrygdGPIVLVLAPT 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 176 RELALQTLKFTKELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLVHVAVEMSLKLQSVEYVVFDEADRLFEM 255
Cdd:PTZ00110 213 RELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDM 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 256 GFAEQLQEIIARLPGGHQTVLFSATLPKLLVEFARAGLTE-PVLIRL-DVDTKLNEQLKTSFFLVREDTKAAVLLHLLHN 333
Cdd:PTZ00110 293 GFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEePVHVNVgSLDLTACHNIKQEVFVVEEHEKRGKLKMLLQR 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 334 VVRPQDQTVVFVATKHHAEYLTELLTTQRVSCAHIYSALDPTARKINLAKFTLGKCSTLIVTDLAARGLDIPLLDNVINY 413
Cdd:PTZ00110 373 IMRDGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINF 452
|
330 340 350
....*....|....*....|....*....|...
gi 164419743 414 SFPAKGKLFLHRVGRVARAGRSGTAYSLVAPDE 446
Cdd:PTZ00110 453 DFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDK 485
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
1-469 |
1.75e-60 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 213.24 E-value: 1.75e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 1 MAADKGPAAGPRSRAAMAQWRKKKGLRKRRGAASQARGSDSEDGEfeiqaEDDARARKLGPGRPLPTFPTSECTsdVEPd 80
Cdd:PRK01297 11 KGEAEQPAPAPPSPAAAPAPPPPAKTAAPATKAAAPAAAAPRAEK-----PKKDKPRRERKPKPASLWKLEDFV--VEP- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 81 tremvraqnkkKKKSGGFQSMGLSYPVFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKT 160
Cdd:PRK01297 83 -----------QEGKTRFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 161 HSAQTG-----ARALILSPTRELALQTLKFTKELGKFTGLKTALILGGDRMEDQFAALHEN-PDIIIATPGRLVHVAVEM 234
Cdd:PRK01297 152 TPPPKErymgePRALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEARfCDILVATPGRLLDFNQRG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 235 SLKLQSVEYVVFDEADRLFEMGFAEQLQEIIARLP--GGHQTVLFSATLPKLLVEFARAGLTEPVLIRLDVDTKLNEQLK 312
Cdd:PRK01297 232 EVHLDMVEVMVLDEADRMLDMGFIPQVRQIIRQTPrkEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 313 TSFFLVREDTKaavlLHLLHNVVR--PQDQTVVFVATKHHAEYLTELLTTQRVSCAHIYSALDPTARKINLAKFTLGKCS 390
Cdd:PRK01297 312 QHVYAVAGSDK----YKLLYNLVTqnPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIR 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164419743 391 TLIVTDLAARGLDIPLLDNVINYSFPAKGKLFLHRVGRVARAGRSGTAYSLVAPDEIPYLLDLHLFLGRSLTLARPLKE 469
Cdd:PRK01297 388 VLVATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKISCEMPPAE 466
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
111-299 |
7.53e-60 |
|
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: 202.05 E-value: 7.53e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 111 IMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKTHSAQTGARALILSPTRELALQTLKFTKELG 190
Cdd:cd17957 5 LEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKKGLRALILAPTRELASQIYRELLKLS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 191 KFTGLKTALILGGDR-MEDQFAALHENPDIIIATPGRLVHVAVEMSLKLQSVEYVVFDEADRLFEMGFAEQLQEIIARLP 269
Cdd:cd17957 85 KGTGLRIVLLSKSLEaKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDEILAACT 164
|
170 180 190
....*....|....*....|....*....|.
gi 164419743 270 GGH-QTVLFSATLPKLLVEFARAGLTEPVLI 299
Cdd:cd17957 165 NPNlQRSLFSATIPSEVEELARSVMKDPIRI 195
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
98-442 |
1.22e-58 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 212.02 E-value: 1.22e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 98 FQSMGLSYPVFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKthSAQTGARALILSPTRE 177
Cdd:PRK11634 8 FADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLD--PELKAPQILVLAPTRE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 178 LALQTLKFTKELGK-FTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLVHVAVEMSLKLQSVEYVVFDEADRLFEMG 256
Cdd:PRK11634 86 LAVQVAEAMTDFSKhMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 257 FAEQLQEIIARLPGGHQTVLFSATLPKLLVEFARAGLTEPVLIRLDVDTKLNEQLKTSFFLVREDTKAAVLLHLLHnvVR 336
Cdd:PRK11634 166 FIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKNEALVRFLE--AE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 337 PQDQTVVFVATKHHAEYLTELLTTQRVSCAHIYSALDPTARKINLAKFTLGKCSTLIVTDLAARGLDIPLLDNVINYSFP 416
Cdd:PRK11634 244 DFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIP 323
|
330 340
....*....|....*....|....*.
gi 164419743 417 AKGKLFLHRVGRVARAGRSGTAYSLV 442
Cdd:PRK11634 324 MDSESYVHRIGRTGRAGRAGRALLFV 349
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
98-299 |
1.72e-58 |
|
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: 198.69 E-value: 1.72e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 98 FQSMGLSYPVFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKTHsaQTGARALILSPTRE 177
Cdd:cd17954 2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLEN--PQRFFALVLAPTRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 178 LALQTLKFTKELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLV-HVAVEMSLKLQSVEYVVFDEADRLFEMG 256
Cdd:cd17954 80 LAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVdHLENTKGFSLKSLKFLVMDEADRLLNMD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 164419743 257 FAEQLQEIIARLPGGHQTVLFSATLPKLLVEFARAGLTEPVLI 299
Cdd:cd17954 160 FEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKI 202
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
98-524 |
8.21e-55 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 199.79 E-value: 8.21e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 98 FQSMGLSYPVFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKTHSAQTG-----ARALIL 172
Cdd:PRK04537 11 FSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALADrkpedPRALIL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 173 SPTRELALQTLKFTKELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLV-HVAVEMSLKLQSVEYVVFDEADR 251
Cdd:PRK04537 91 APTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIdYVKQHKVVSLHACEICVLDEADR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 252 LFEMGFAEQLQEIIARLP--GGHQTVLFSATLPKLLVEFARAGLTEPVLIRLDVDTKLNEQLKTSFFLVREDTKAAVLLH 329
Cdd:PRK04537 171 MFDLGFIKDIRFLLRRMPerGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRIYFPADEEKQTLLLG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 330 LLHnvvRPQD-QTVVFVATKHHAEYLTELLTTQRVSCAHIYSALDPTARKINLAKFTLGKCSTLIVTDLAARGLDIPLLD 408
Cdd:PRK04537 251 LLS---RSEGaRTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVK 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 409 NVINYSFPAKGKLFLHRVGRVARAGRSGTAYSLVAPDEIPYLLDLHLFLGRSL-------TLARPLKEPSgvagvdgmlg 481
Cdd:PRK04537 328 YVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYIEQKIpvepvtaELLTPLPRPP---------- 397
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 164419743 482 RVPQSVVDEEDSGLQSTLEASLELRGlARVADNAQQQYVRSRP 524
Cdd:PRK04537 398 RVPVEGEEADDEAGDSVGTIFREARE-QRAAEEQRRGGGRSGP 439
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
102-299 |
1.13e-54 |
|
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: 188.74 E-value: 1.13e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 102 GLSYPVFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKTH---SAQTGARALILSPTREL 178
Cdd:cd17953 18 GLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQrpvKPGEGPIGLIMAPTREL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 179 ALQTLKFTKELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLVHVAVEMSLK---LQSVEYVVFDEADRLFEM 255
Cdd:cd17953 98 ALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTANNGRvtnLRRVTYVVLDEADRMFDM 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 164419743 256 GFAEQLQEIIARLPGGHQTVLFSATLPKLLVEFARAGLTEPVLI 299
Cdd:cd17953 178 GFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
98-299 |
3.52e-54 |
|
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: 186.66 E-value: 3.52e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 98 FQSMGLSYPVFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKTHSaqTGARALILSPTRE 177
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDP--YGIFALVLTPTRE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 178 LALQTLKFTKELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLV-HV--AVEMSLKLQSVEYVVFDEADRLFE 254
Cdd:cd17955 79 LAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLAdHLrsSDDTTKVLSRVKFLVLDEADRLLT 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 164419743 255 MGFAEQLQEIIARLPGGHQTVLFSATLPKLLVEFARAGLTEPVLI 299
Cdd:cd17955 159 GSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPFFW 203
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
66-453 |
4.82e-54 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 193.12 E-value: 4.82e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 66 PTFPTSECTSDVEPDTREMVRAqnkkkkksggFQSMGLSYPVFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSG 145
Cdd:PTZ00424 8 NQSEQVASTGTIESNYDEIVDS----------FDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 146 KTACFLLPMFERL--KTHSAQtgarALILSPTRELALQTLKFTKELGKFTGLKTALILGGDRMEDQFAALHENPDIIIAT 223
Cdd:PTZ00424 78 KTATFVIAALQLIdyDLNACQ----ALILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 224 PGRLVHVAVEMSLKLQSVEYVVFDEADRLFEMGFAEQLQEIIARLPGGHQTVLFSATLPKLLVEFARAGLTEPVLIRLDV 303
Cdd:PTZ00424 154 PGRVYDMIDKRHLRVDDLKLFILDEADEMLSRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 304 DTKLNEQLKTSFFLV-REDTKAAVLLHLLHNVVrpQDQTVVFVATKHHAEYLTELLTTQRVSCAHIYSALDPTARKINLA 382
Cdd:PTZ00424 234 DELTLEGIRQFYVAVeKEEWKFDTLCDLYETLT--ITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMR 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164419743 383 KFTLGKCSTLIVTDLAARGLDIPLLDNVINYSFPAKGKLFLHRVGRVARAGRSGTAYSLVAPDEIPYLLDL 453
Cdd:PTZ00424 312 EFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEI 382
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
111-299 |
3.65e-53 |
|
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: 183.77 E-value: 3.65e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 111 IMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERL---KTHSAQTGARALILSPTRELALQTLKFTK 187
Cdd:cd17952 5 IRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHImdqRELEKGEGPIAVIVAPTRELAQQIYLEAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 188 ELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLVHVAVEMSLKLQSVEYVVFDEADRLFEMGFAEQLQEIIAR 267
Cdd:cd17952 85 KFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRSIVGH 164
|
170 180 190
....*....|....*....|....*....|..
gi 164419743 268 LPGGHQTVLFSATLPKLLVEFARAGLTEPVLI 299
Cdd:cd17952 165 VRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
109-299 |
1.26e-52 |
|
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: 182.10 E-value: 1.26e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 109 KGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERL--KTHSAQTGARALILSPTRELALQTLKFT 186
Cdd:cd17941 3 KGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLyrERWTPEDGLGALIISPTRELAMQIFEVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 187 KELGKFTGLKTALILGGDRMEDQFAALHENpDIIIATPGRLV-HVAVEMSLKLQSVEYVVFDEADRLFEMGFAEQLQEII 265
Cdd:cd17941 83 RKVGKYHSFSAGLIIGGKDVKEEKERINRM-NILVCTPGRLLqHMDETPGFDTSNLQMLVLDEADRILDMGFKETLDAIV 161
|
170 180 190
....*....|....*....|....*....|....
gi 164419743 266 ARLPGGHQTVLFSATLPKLLVEFARAGLTEPVLI 299
Cdd:cd17941 162 ENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYI 195
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
115-300 |
1.44e-52 |
|
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: 182.01 E-value: 1.44e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 115 GYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERL---KTHSAQTGARALILSPTRELALQTLKFTKELGK 191
Cdd:cd17960 9 GFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILlkrKANLKKGQVGALIISPTRELATQIYEVLQSFLE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 192 FTG--LKTALILGGDRMEDQFAALHEN-PDIIIATPGRLVH--VAVEMSLKLQSVEYVVFDEADRLFEMGFAEQLQEIIA 266
Cdd:cd17960 89 HHLpkLKCQLLIGGTNVEEDVKKFKRNgPNILVGTPGRLEEllSRKADKVKVKSLEVLVLDEADRLLDLGFEADLNRILS 168
|
170 180 190
....*....|....*....|....*....|....
gi 164419743 267 RLPGGHQTVLFSATLPKLLVEFARAGLTEPVLIR 300
Cdd:cd17960 169 KLPKQRRTGLFSATQTDAVEELIKAGLRNPVRVV 202
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
107-299 |
2.55e-52 |
|
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: 182.13 E-value: 2.55e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 107 VFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKTHSAQT------GARALILSPTRELAL 180
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDeetkddGPYALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 181 QTLKFTKELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLVHVAVEMSLKLQSVEYVVFDEADRLFEMGFAEQ 260
Cdd:cd17945 81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 164419743 261 LQEIIARLP-----------------GGH---QTVLFSATLPKLLVEFARAGLTEPVLI 299
Cdd:cd17945 161 VTKILDAMPvsnkkpdteeaeklaasGKHryrQTMMFTATMPPAVEKIAKGYLRRPVVV 219
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
109-281 |
5.72e-52 |
|
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: 180.47 E-value: 5.72e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 109 KGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKTHSAQT----GARALILSPTRELALQTLK 184
Cdd:cd17961 7 KAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAESgeeqGTRALILVPTRELAQQVSK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 185 FTKELGKFTG--LKTALILGGDRMEDQFAALHENPDIIIATPGRLVHVAVEMSLKLQS-VEYVVFDEADRLFEMGFAEQL 261
Cdd:cd17961 87 VLEQLTAYCRkdVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLLStLKYLVIDEADLVLSYGYEEDL 166
|
170 180
....*....|....*....|
gi 164419743 262 QEIIARLPGGHQTVLFSATL 281
Cdd:cd17961 167 KSLLSYLPKNYQTFLMSATL 186
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
98-283 |
8.05e-52 |
|
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: 180.76 E-value: 8.05e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 98 FQSMGLSYPVFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERL--------KTHSAQTGARA 169
Cdd:cd17967 2 FEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLledgppsvGRGRRKAYPSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 170 LILSPTRELALQ----TLKFTKElgkfTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLVHVaVEMS-LKLQSVEYV 244
Cdd:cd17967 82 LILAPTRELAIQiyeeARKFSYR----SGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDF-IERGrISLSSIKFL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 164419743 245 VFDEADRLFEMGFAEQLQEIIAR----LPGGHQTVLFSATLPK 283
Cdd:cd17967 157 VLDEADRMLDMGFEPQIRKIVEHpdmpPKGERQTLMFSATFPR 199
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
98-442 |
1.02e-51 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 189.61 E-value: 1.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 98 FQSMGLSYPVFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKTH-----SAQTGARALIL 172
Cdd:PLN00206 123 FSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCTIrsghpSEQRNPLAMVL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 173 SPTRELALQTLKFTKELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLVHVAVEMSLKLQSVEYVVFDEADRL 252
Cdd:PLN00206 203 TPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCM 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 253 FEMGFAEQLQEIIARLPGGhQTVLFSATLPKLLVEFARAGLTEPVLIRLDVDTKLNEQLKTSFFLVREDTKAAVLLHLLH 332
Cdd:PLN00206 283 LERGFRDQVMQIFQALSQP-QVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKKQKLFDILK 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 333 NVVRPQDQTVVFVATKHHAEYLTELLT-TQRVSCAHIYSALDPTARKINLAKFTLGKCSTLIVTDLAARGLDIPLLDNVI 411
Cdd:PLN00206 362 SKQHFKPPAVVFVSSRLGADLLANAITvVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVI 441
|
330 340 350
....*....|....*....|....*....|.
gi 164419743 412 NYSFPAKGKLFLHRVGRVARAGRSGTAYSLV 442
Cdd:PLN00206 442 IFDMPNTIKEYIHQIGRASRMGEKGTAIVFV 472
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
113-312 |
1.14e-51 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 179.61 E-value: 1.14e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 113 KKGYKVPTPIQRKTIPVILDG-KDVVAMARTGSGKTACFLLPMFERLKTHSaqtGARALILSPTRELALQTLKFTKELGK 191
Cdd:smart00487 3 KFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGK---GGRVLVLVPTRELAEQWAEELKKLGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 192 FTGLKTALILGGDRMEDQFAAL-HENPDIIIATPGRLVHVAVEMSLKLQSVEYVVFDEADRLFEMGFAEQLQEIIARLPG 270
Cdd:smart00487 80 SLGLKVVGLYGGDSKREQLRKLeSGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 164419743 271 GHQTVLFSATLPKLLVEFARAGLTEPvlIRLDVDTKLNEQLK 312
Cdd:smart00487 160 NVQLLLLSATPPEEIENLLELFLNDP--VFIDVGFTPLEPIE 199
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
98-299 |
9.24e-51 |
|
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: 177.10 E-value: 9.24e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 98 FQSMGLSYPVFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKTHSAQTgaRALILSPTRE 177
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVI--QALILVPTRE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 178 LALQTLKFTKELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLVHVAVEMSLKLQSVEYVVFDEADRLFEMGF 257
Cdd:cd17940 79 LALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDF 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 164419743 258 AEQLQEIIARLPGGHQTVLFSATLPKLLVEFARAGLTEPVLI 299
Cdd:cd17940 159 QPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
101-299 |
5.90e-50 |
|
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: 174.82 E-value: 5.90e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 101 MGLSYPVFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKTHSAQTgaRALILSPTRELAL 180
Cdd:cd17939 2 MGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRET--QALVLAPTRELAQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 181 QTLKFTKELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLVHVAVEMSLKLQSVEYVVFDEADRLFEMGFAEQ 260
Cdd:cd17939 80 QIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQ 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 164419743 261 LQEIIARLPGGHQTVLFSATLPKLLVEFARAGLTEPVLI 299
Cdd:cd17939 160 IYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
111-299 |
5.43e-49 |
|
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: 171.96 E-value: 5.43e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 111 IMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKTHSAQTGAraLILSPTRELALQTLKFTKELG 190
Cdd:cd17962 5 LKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSA--LILTPTRELAVQIEDQAKELM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 191 K-FTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLVHVAVEMSLKLQSVEYVVFDEADRLFEMGFAEQLQEIIARLP 269
Cdd:cd17962 83 KgLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILENIS 162
|
170 180 190
....*....|....*....|....*....|
gi 164419743 270 GGHQTVLFSATLPKLLVEFARAGLTEPVLI 299
Cdd:cd17962 163 HDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
103-293 |
7.81e-49 |
|
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: 172.00 E-value: 7.81e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 103 LSYPVFKGIMKKGYKVPTPIQRKTIPVIL-DGKDVVAMARTGSGKTACFLLPMFER-LKTHSAQTGAR--ALILSPTREL 178
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILsTGDDVLARAKTGTGKTLAFLLPAIQSlLNTKPAGRRSGvsALIISPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 179 ALQTLK-FTKELGKFTGLKTALILGG-DRMEDQFAALHENPDIIIATPGRLV-HVAVEMSLK-LQSVEYVVFDEADRLFE 254
Cdd:cd17964 81 ALQIAAeAKKLLQGLRKLRVQSAVGGtSRRAELNRLRRGRPDILVATPGRLIdHLENPGVAKaFTDLDYLVLDEADRLLD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 164419743 255 MGFAEQLQEIIARLP----GGHQTVLFSATLPKLLVEFARAGL 293
Cdd:cd17964 161 MGFRPDLEQILRHLPeknaDPRQTLLFSATVPDEVQQIARLTL 203
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
107-299 |
6.42e-46 |
|
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: 163.66 E-value: 6.42e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 107 VFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMF------ERLKTHSAQTGARALILSPTRELAL 180
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLImfaleqEKKLPFIKGEGPYGLIVCPSRELAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 181 QTLK----FTKEL--GKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLVHVAVEMSLKLQSVEYVVFDEADRLFE 254
Cdd:cd17951 81 QTHEvieyYCKALqeGGYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 164419743 255 MGFAEQLQEIIARLPGGHQTVLFSATLPKLLVEFARAGLTEPVLI 299
Cdd:cd17951 161 MGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
107-281 |
8.23e-45 |
|
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: 161.64 E-value: 8.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 107 VFKGIMKKGYKVPTPIQRKTIPV-ILDGKDVVAMARTGSGKTACFLLPMFERL-------KTHSAQTGARALILSPTREL 178
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAaIRDGKDVIGAAETGSGKTLAFGIPILERLlsqkssnGVGGKQKPLRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 179 ALQTLKFTKELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLVHV---AVEMSLKLQSVEYVVFDEADRLFEM 255
Cdd:cd17946 81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELiqeGNEHLANLKSLRFLVLDEADRMLEK 160
|
170 180 190
....*....|....*....|....*....|...
gi 164419743 256 GFAEQLQEIIARLPGGH-------QTVLFSATL 281
Cdd:cd17946 161 GHFAELEKILELLNKDRagkkrkrQTFVFSATL 193
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
107-299 |
6.57e-44 |
|
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: 157.53 E-value: 6.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 107 VFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKthsAQT------GARALILSPTRELAL 180
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHIN---AQPplergdGPIVLVLAPTRELAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 181 QTLKFTKELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLVHVAVEMSLKLQSVEYVVFDEADRLFEMGFAEQ 260
Cdd:cd17966 78 QIQQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQ 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 164419743 261 LQEIIARLPGGHQTVLFSATLPKLLVEFARAGLTEPVLI 299
Cdd:cd17966 158 IRKIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
115-300 |
1.35e-43 |
|
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: 157.36 E-value: 1.35e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 115 GYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERL----KTHSAQTGARALILSPTRELALQTLK-FTKEL 189
Cdd:cd17949 10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLlslePRVDRSDGTLALVLVPTRELALQIYEvLEKLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 190 GKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLV-HVAVEMSLKLQSVEYVVFDEADRLFEMGFAEQLQEII--- 265
Cdd:cd17949 90 KPFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLdHLKNTQSFDVSNLRWLVLDEADRLLDMGFEKDITKILell 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 164419743 266 ----------ARLPGGHQTVLFSATLPKLLVEFARAGLTEPVLIR 300
Cdd:cd17949 170 ddkrskaggeKSKPSRRQTVLVSATLTDGVKRLAGLSLKDPVYID 214
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
107-299 |
1.66e-43 |
|
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: 156.47 E-value: 1.66e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 107 VFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKTHSAQTGAR----ALILSPTRELALQT 182
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIPREQRngpgVLVLTPTRELALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 183 LKFTKELgKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLVHVAVEMSLKLQSVEYVVFDEADRLFEMGFAEQLQ 262
Cdd:cd17958 81 EAECSKY-SYKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIR 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 164419743 263 EIIARLPGGHQTVLFSATLPKLLVEFARAGLTEPVLI 299
Cdd:cd17958 160 KILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
98-281 |
2.81e-41 |
|
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: 150.16 E-value: 2.81e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 98 FQSMGLSYPVFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLkthsaqtgaRALILSPTRE 177
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIV---------VALILEPSRE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 178 LALQTLKFTKELGKFT---GLKTALILGGDRMEDQFAALHENPDIIIATPGRLVHVAVEMSLKLQSVEYVVFDEADRLFE 254
Cdd:cd17938 72 LAEQTYNCIENFKKYLdnpKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLS 151
|
170 180 190
....*....|....*....|....*....|...
gi 164419743 255 MGFAEQLQEIIARLPGGH------QTVLFSATL 281
Cdd:cd17938 152 QGNLETINRIYNRIPKITsdgkrlQVIVCSATL 184
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
311-442 |
5.09e-41 |
|
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: 146.88 E-value: 5.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 311 LKTSFFLVREDTKAAVLLHLLHNVvRPQDQTVVFVATKHHAEYLTELLTTQRVSCAHIYSALDPTARKINLAKFTLGKCS 390
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLLLLLLEK-LKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVR 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 164419743 391 TLIVTDLAARGLDIPLLDNVINYSFPAKGKLFLHRVGRVARAGRSGTAYSLV 442
Cdd:cd18787 80 VLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
109-299 |
9.28e-41 |
|
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: 148.66 E-value: 9.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 109 KGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKT--HSAQTGARALILSPTRELALQTLKFT 186
Cdd:cd17942 3 KAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKlkFKPRNGTGVIIISPTRELALQIYGVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 187 KELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLV-HVAVEMSLKLQSVEYVVFDEADRLFEMGFAEQLQEII 265
Cdd:cd17942 83 KELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLdHLQNTKGFLYKNLQCLIIDEADRILEIGFEEEMRQII 162
|
170 180 190
....*....|....*....|....*....|....*
gi 164419743 266 ARLPGGHQTVLFSATLPKLLVEFARAGL-TEPVLI 299
Cdd:cd17942 163 KLLPKRRQTMLFSATQTRKVEDLARISLkKKPLYV 197
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
107-300 |
1.93e-40 |
|
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: 147.41 E-value: 1.93e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 107 VFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKTHSAQTgaRALILSPTRELALQTLKFT 186
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHP--QVLILAPTREIAVQIHDVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 187 KELG-KFTGLKTALILGGDRMEDQFAALhENPDIIIATPGRLVHVAVEMSLKLQSVEYVVFDEADRLFEMGFAEQLQEII 265
Cdd:cd17943 79 KKIGkKLEGLKCEVFIGGTPVKEDKKKL-KGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIF 157
|
170 180 190
....*....|....*....|....*....|....*
gi 164419743 266 ARLPGGHQTVLFSATLPKLLVEFARAGLTEPVLIR 300
Cdd:cd17943 158 SSLPKNKQVIAFSATYPKNLDNLLARYMRKPVLVR 192
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
98-288 |
1.03e-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: 147.81 E-value: 1.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 98 FQSMGLSYPVFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKTH----SAQTGAR---AL 170
Cdd:cd18052 45 FEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEgltaSSFSEVQepqAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 171 ILSPTRELALQTLkftKELGKF---TGLKTALILGGDRMEDQFAALHENPDIIIATPGRLVHVAVEMSLKLQSVEYVVFD 247
Cdd:cd18052 125 IVAPTRELANQIF---LEARKFsygTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILD 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 164419743 248 EADRLFEMGFAEQLQEIIARL----PGGHQTVLFSATLP----KLLVEF 288
Cdd:cd18052 202 EADRMLDMGFGPEIRKLVSEPgmpsKEDRQTLMFSATFPeeiqRLAAEF 250
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
103-300 |
1.23e-39 |
|
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: 145.41 E-value: 1.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 103 LSYPVFKGIMKKGYKVPTPIQRKTIPVILDG--KDVVAMARTGSGKTACFLLPMFERLKTHSAQTgaRALILSPTRELAL 180
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSP--QALCLAPTRELAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 181 QTLKFTKELGKFTGLKTALIL------GGDRMEDQfaalhenpdIIIATPGRLVHVAVEMSLKLQSVEYVVFDEADRLFE 254
Cdd:cd17963 79 QIGEVVEKMGKFTGVKVALAVpgndvpRGKKITAQ---------IVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLD 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 164419743 255 M-GFAEQLQEIIARLPGGHQTVLFSATLPKLLVEFARAGLTEPVLIR 300
Cdd:cd17963 150 TqGHGDQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTIK 196
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
98-299 |
2.81e-38 |
|
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: 141.45 E-value: 2.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 98 FQSMGLSYPVFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKTHSAQTgaRALILSPTRE 177
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRET--QALILSPTRE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 178 LALQTLKFTKELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLVHVAVEMSLKLQSVEYVVFDEADRLFEMGF 257
Cdd:cd18045 79 LAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGF 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 164419743 258 AEQLQEIIARLPGGHQTVLFSATLPKLLVEFARAGLTEPVLI 299
Cdd:cd18045 159 KEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
116-290 |
8.37e-38 |
|
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: 141.72 E-value: 8.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 116 YKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPM---------FERLKTHSAQTGAR-----ALILSPTRELALQ 181
Cdd:cd18051 41 YTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPIlsqiyeqgpGESLPSESGYYGRRkqyplALVLAPTRELASQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 182 TLKFTKELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLVHVAVEMSLKLQSVEYVVFDEADRLFEMGFAEQL 261
Cdd:cd18051 121 IYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQI 200
|
170 180 190
....*....|....*....|....*....|...
gi 164419743 262 QEIIAR--LP--GGHQTVLFSATLPKLLVEFAR 290
Cdd:cd18051 201 RRIVEQdtMPptGERQTLMFSATFPKEIQMLAR 233
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
98-299 |
4.89e-37 |
|
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: 137.96 E-value: 4.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 98 FQSMGLSYPVFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKTHSAQTgaRALILSPTRE 177
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKAT--QALVLAPTRE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 178 LALQTLKFTKELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLVHVAVEMSLKLQSVEYVVFDEADRLFEMGF 257
Cdd:cd18046 79 LAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGF 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 164419743 258 AEQLQEIIARLPGGHQTVLFSATLPKLLVEFARAGLTEPVLI 299
Cdd:cd18046 159 KDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
104-301 |
7.25e-35 |
|
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: 132.83 E-value: 7.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 104 SYP--VFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKTH---SAQTGARALILSPTREL 178
Cdd:cd18049 30 NFPanVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQpflERGDGPICLVLAPTREL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 179 ALQTLKFTKELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLVHVAVEMSLKLQSVEYVVFDEADRLFEMGFA 258
Cdd:cd18049 110 AQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFE 189
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 164419743 259 EQLQEIIARLPGGHQTVLFSATLPKLLVEFARAGLTEPVLIRL 301
Cdd:cd18049 190 PQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINI 232
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
113-283 |
3.40e-34 |
|
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: 130.95 E-value: 3.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 113 KKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKTHSAQTGA-----RALILSPTRELALQTLKFTK 187
Cdd:cd17948 7 RQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGpfnapRGLVITPSRELAEQIGSVAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 188 ELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLVHVAVEMSLKLQSVEYVVFDEADRLFEMGFAEQLQEIIAR 267
Cdd:cd17948 87 SLTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKLSHFLRR 166
|
170 180
....*....|....*....|....*....
gi 164419743 268 LP-------------GGHQTVLFSATLPK 283
Cdd:cd17948 167 FPlasrrsentdgldPGTQLVLVSATMPS 195
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
95-283 |
5.58e-33 |
|
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: 126.69 E-value: 5.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 95 SGGFQSMGLSYPVFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKTHSAQTgaRALILSP 174
Cdd:cd17950 1 SSGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQV--SVLVICH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 175 TRELALQTLKFTKELGKF-TGLKTALILGGDRMEDQFAALHEN-PDIIIATPGRLVHVAVEMSLKLQSVEYVVFDEADRL 252
Cdd:cd17950 79 TRELAFQISNEYERFSKYmPNVKTAVFFGGVPIKKDIEVLKNKcPHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKM 158
|
170 180 190
....*....|....*....|....*....|..
gi 164419743 253 FE-MGFAEQLQEIIARLPGGHQTVLFSATLPK 283
Cdd:cd17950 159 LEqLDMRRDVQEIFRATPHDKQVMMFSATLSK 190
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
97-301 |
9.96e-33 |
|
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: 127.82 E-value: 9.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 97 GFQSMGLSYPVFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKTH---SAQTGARALILS 173
Cdd:cd18050 63 AFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQpylERGDGPICLVLA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 174 PTRELALQTLKFTKELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLVHVAVEMSLKLQSVEYVVFDEADRLF 253
Cdd:cd18050 143 PTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRML 222
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 164419743 254 EMGFAEQLQEIIARLPGGHQTVLFSATLPKLLVEFARAGLTEPVLIRL 301
Cdd:cd18050 223 DMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQINI 270
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
121-290 |
4.60e-32 |
|
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: 123.80 E-value: 4.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 121 PIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKTHSaQTGARA-----LILSPTRELALQTLKFTKELGKftGL 195
Cdd:cd17944 15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQ-QPRKRGrapkvLVLAPTRELANQVTKDFKDITR--KL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 196 KTALILGGDRMEDQFAALHENPDIIIATPGRLVHVAVEMSLKLQSVEYVVFDEADRLFEMGFAEQLQEII-----ARLPG 270
Cdd:cd17944 92 SVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILsvsykKDSED 171
|
170 180
....*....|....*....|
gi 164419743 271 GHQTVLFSATLPKLLVEFAR 290
Cdd:cd17944 172 NPQTLLFSATCPDWVYNVAK 191
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
113-281 |
6.69e-28 |
|
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: 112.73 E-value: 6.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 113 KKGYKVPTPIQRKTIPVILDG---------KDVVAMARTGSGKTACFLLPMFERLKTHSAqTGARALILSPTRELALQTL 183
Cdd:cd17956 7 NNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQALSKRVV-PRLRALIVVPTKELVQQVY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 184 KFTKELGKFTGLKTALiLGGDR---------MEDQFAALHENPDIIIATPGRLV-HVAVEMSLKLQSVEYVVFDEADRLF 253
Cdd:cd17956 86 KVFESLCKGTGLKVVS-LSGQKsfkkeqkllLVDTSGRYLSRVDILVATPGRLVdHLNSTPGFTLKHLRFLVIDEADRLL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 164419743 254 EMGFAE--------------------QLQEIIARLPGGHQTVLFSATL 281
Cdd:cd17956 165 NQSFQDwletvmkalgrptapdlgsfGDANLLERSVRPLQKLLFSATL 212
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
98-301 |
1.12e-24 |
|
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: 103.56 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 98 FQSMGLSYPVFKGIMKKGYKVPTPIQRKTIPVILDG--KDVVAMARTGSGKTACFLLPMFERLktHSAQTGARALILSPT 175
Cdd:cd18048 20 FEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRV--DALKLYPQCLCLSPT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 176 RELALQTLKFTKELGKF-TGLKTALILGGDR------MEDQfaalhenpdIIIATPGRLVHVAVEMSL-KLQSVEYVVFD 247
Cdd:cd18048 98 FELALQTGKVVEEMGKFcVGIQVIYAIRGNRpgkgtdIEAQ---------IVIGTPGTVLDWCFKLRLiDVTNISVFVLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 164419743 248 EADRLFEM-GFAEQLQEIIARLPGGHQTVLFSATLPKLLVEFARAGLTEPVLIRL 301
Cdd:cd18048 169 EADVMINVqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKL 223
|
|
| DBP10CT |
pfam08147 |
DBP10CT (NUC160) domain; This C terminal domain is found in the Dbp10p subfamily of ... |
714-774 |
5.51e-23 |
|
DBP10CT (NUC160) domain; This C terminal domain is found in the Dbp10p subfamily of hypothetical RNA helicases.
Pssm-ID: 462373 [Multi-domain] Cd Length: 66 Bit Score: 93.12 E-value: 5.51e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164419743 714 DLMGDEAQNLTRGRQ---QLKWDRKKKRFVGQSGQED--KKKIKTESGRYISSSYKRDLYQKWKQK 774
Cdd:pfam08147 1 DLTGDDGQELNQQKQvqkKMRWDKKKKKFVKRSGNDEdgKKKIRTESGVKIPASYKSGRYDEWKKK 66
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
115-283 |
2.54e-22 |
|
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: 97.06 E-value: 2.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 115 GYKVPTPIQRKTIPVIL------------DGKD-----VVAmARTGSGKTACFLLPMFERLKTHSAQTG----------- 166
Cdd:cd17965 27 EEIKPSPIQTLAIKKLLktlmrkvtkqtsNEEPklevfLLA-AETGSGKTLAYLAPLLDYLKRQEQEPFeeaeeeyesak 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 167 ----ARALILSPTRELALQTLKFTKELGKFTGLKTALILG--GDRMEDQFAALHENPDIIIATPGRLVHVAVEMSLKLQS 240
Cdd:cd17965 106 dtgrPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSgfGPSYQRLQLAFKGRIDILVTTPGKLASLAKSRPKILSR 185
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 164419743 241 VEYVVFDEADRLFEMGFAEQLQEIIARLPGGHQTVLFSATLPK 283
Cdd:cd17965 186 VTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPK 228
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
98-300 |
4.93e-22 |
|
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: 95.17 E-value: 4.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 98 FQSMGLSYPVFKGIMKKGYKVPTPIQRKTIPVIL--DGKDVVAMARTGSGKTACFLLPMFERLKthSAQTGARALILSPT 175
Cdd:cd18047 3 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLaePPQNLIAQSQSGTGKTAAFVLAMLSQVE--PANKYPQCLCLSPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 176 RELALQTLKFTKELGKF-TGLKTALILGGDRMEdqfAALHENPDIIIATPGRLVHVAVEMSL-KLQSVEYVVFDEADRLF 253
Cdd:cd18047 81 YELALQTGKVIEQMGKFyPELKLAYAVRGNKLE---RGQKISEQIVIGTPGTVLDWCSKLKFiDPKKIKVFVLDEADVMI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 164419743 254 -EMGFAEQLQEIIARLPGGHQTVLFSATLPKLLVEFARAGLTEPVLIR 300
Cdd:cd18047 158 aTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 205
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
323-433 |
1.03e-21 |
|
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: 90.73 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 323 KAAVLLHLLHNvvRPQDQTVVFVATKHHAEyLTELLTTQRVSCAHIYSALDPTARKINLAKFTLGKCSTLIVTDLAARGL 402
Cdd:pfam00271 2 KLEALLELLKK--ERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78
|
90 100 110
....*....|....*....|....*....|.
gi 164419743 403 DIPLLDNVINYSFPAKGKLFLHRVGRVARAG 433
Cdd:pfam00271 79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
136-437 |
7.46e-19 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 91.24 E-value: 7.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 136 VVAMArTGSGKTACFLLPMFErlkthsAQTGARALILSPTRELALQTLKftkELGKFTGLKtalILGGDRMEDQFaalhe 215
Cdd:COG1061 104 LVVAP-TGTGKTVLALALAAE------LLRGKRVLVLVPRRELLEQWAE---ELRRFLGDP---LAGGGKKDSDA----- 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 216 npDIIIATPGRLVHVAVEMSLKlQSVEYVVFDEADRLFemgfAEQLQEIIARLPGGHqTVLFSAT------LPKLLVEF- 288
Cdd:COG1061 166 --PITVATYQSLARRAHLDELG-DRFGLVIIDEAHHAG----APSYRRILEAFPAAY-RLGLTATpfrsdgREILLFLFd 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 289 -----------ARAG-LTEPVLIRLDVD--------TKLNEQLKTSFfLVREDTKAAVLLHLLHNVVRpQDQTVVFVATK 348
Cdd:COG1061 238 givyeyslkeaIEDGyLAPPEYYGIRVDltderaeyDALSERLREAL-AADAERKDKILRELLREHPD-DRKTLVFCSSV 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 349 HHAEYLTELLTTQRVSCAHIYSALDPTARKINLAKFTLGKCSTLIVTDLAARGLDIPLLDNVINYSfPAKGK-LFLHRVG 427
Cdd:COG1061 316 DHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLR-PTGSPrEFIQRLG 394
|
330
....*....|
gi 164419743 428 RVARAGRSGT 437
Cdd:COG1061 395 RGLRPAPGKE 404
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
123-445 |
2.30e-17 |
|
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: 87.20 E-value: 2.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 123 QRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKTHSaqtGARALILSPTRELA---LQTL-KFTKELGkfTGLKTA 198
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDP---GATALYLYPTKALArdqLRRLrELAEALG--LGVRVA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 199 lILGGDRMEDQFAALHENPDIIIATPGrLVHVAVemsLK--------LQSVEYVVFDEA---------------DRLFEm 255
Cdd:COG1205 136 -TYDGDTPPEERRWIREHPDIVLTNPD-MLHYGL---LPhhtrwarfFRNLRYVVIDEAhtyrgvfgshvanvlRRLRR- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 256 gfaeqlqeiIARLPGGHQTVLF-SATL--PKllvEFARAgLT-EPVLIrldVDTKLNEQLKTSFFL----VREDTK---- 323
Cdd:COG1205 210 ---------ICRHYGSDPQFILaSATIgnPA---EHAER-LTgRPVTV---VDEDGSPRGERTFVLwnppLVDDGIrrsa 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 324 ----AAVLLHLLHNVVrpqdQTVVFVATKHHAE----YLTELLTTQRV-SCAHIYSA-LDPTARKINLAKFTLGKCSTLI 393
Cdd:COG1205 274 laeaARLLADLVREGL----RTLVFTRSRRGAEllarYARRALREPDLaDRVAAYRAgYLPEERREIERGLRSGELLGVV 349
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 164419743 394 VT---DLaarGLDIPLLDNVINYSFPakGKL--FLHRVGRVARAGRSGTAYsLVAPD 445
Cdd:COG1205 350 STnalEL---GIDIGGLDAVVLAGYP--GTRasFWQQAGRAGRRGQDSLVV-LVAGD 400
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
133-280 |
3.44e-17 |
|
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: 79.37 E-value: 3.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 133 GKDVVAMARTGSGKTACFLLPMFERLkthsAQTGARALILSPTRELALQTLKFTKELGKfTGLKTALILGGDRMEDQFAA 212
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLL----LKKGKKVLVLVPTKALALQTAERLRELFG-PGIRVAVLVGGSSAEEREKN 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164419743 213 LHENPDIIIATPGRLVH-VAVEMSLKLQSVEYVVFDEADRLFEMGFAEQL--QEIIARLPGGHQTVLFSAT 280
Cdd:cd00046 76 KLGDADIIIATPDMLLNlLLREDRLFLKDLKLIIVDEAHALLIDSRGALIldLAVRKAGLKNAQVILLSAT 146
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
352-433 |
4.76e-16 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 73.79 E-value: 4.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 352 EYLTELLTTQRVSCAHIYSALDPTARKINLAKFTLGKCSTLIVTDLAARGLDIPLLDNVINYSFPAKGKLFLHRVGRVAR 431
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 164419743 432 AG 433
Cdd:smart00490 81 AG 82
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
123-290 |
8.47e-16 |
|
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: 76.08 E-value: 8.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 123 QRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKThsaQTGARALILSPTRELA---LQTL-KFTKELGkfTGLKTA 198
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLR---DPGSRALYLYPTKALAqdqLRSLrELLEQLG--LGIRVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 199 LILGGDRMEDQFAALHENPDIIIATPGRLvHVAVemsLK--------LQSVEYVVFDEADRlFEMGFAEQLQEIIARL-- 268
Cdd:cd17923 80 TYDGDTPREERRAIIRNPPRILLTNPDML-HYAL---LPhhdrwarfLRNLRYVVLDEAHT-YRGVFGSHVALLLRRLrr 154
|
170 180
....*....|....*....|....*..
gi 164419743 269 ----PGGH-QTVLFSATLpKLLVEFAR 290
Cdd:cd17923 155 lcrrYGADpQFILTSATI-GNPAEHAR 180
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
120-282 |
8.24e-15 |
|
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: 73.45 E-value: 8.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 120 TPIQRKTI-PVILDGKDVVAMARTGSGKTACFLLPMFERLKTHsaqtGARALILSPTRELALQTLKFTKELGKFTGLKTA 198
Cdd:cd17921 3 NPIQREALrALYLSGDSVLVSAPTSSGKTLIAELAILRALATS----GGKAVYIAPTRALVNQKEADLRERFGPLGKNVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 199 LILGGDRMEDQFAAlheNPDIIIATPGRLvhvavEM------SLKLQSVEYVVFDEADRLFEMGFAEQLQEIIARLP--- 269
Cdd:cd17921 79 LLTGDPSVNKLLLA---EADILVATPEKL-----DLllrnggERLIQDVRLVVVDEAHLIGDGERGVVLELLLSRLLrin 150
|
170
....*....|...
gi 164419743 270 GGHQTVLFSATLP 282
Cdd:cd17921 151 KNARFVGLSATLP 163
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
113-401 |
9.34e-12 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 68.38 E-value: 9.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 113 KKGYKVPTPIQRKTIP-VILDGKDVVAMARTGSGKTACFLLPMFERLKthsaqTGARALILSPTRELALQ-TLKFTKELG 190
Cdd:COG1204 17 ERGIEELYPPQAEALEaGLLEGKNLVVSAPTASGKTLIAELAILKALL-----NGGKALYIVPLRALASEkYREFKRDFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 191 KFtGLKTAlILGGDRMEDqfAALHENPDIIIATPGRLvhvaveMSLK------LQSVEYVVFDEA------DRlfemGFa 258
Cdd:COG1204 92 EL-GIKVG-VSTGDYDSD--DEWLGRYDILVATPEKL------DSLLrngpswLRDVDLVVVDEAhliddeSR----GP- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 259 eQLQEIIARL---PGGHQTVLFSATLPKlLVEFAR---AGLTE----PVliRLDVDTKLNEQLKtsfFLVREDTKAAVLL 328
Cdd:COG1204 157 -TLEVLLARLrrlNPEAQIVALSATIGN-AEEIAEwldAELVKsdwrPV--PLNEGVLYDGVLR---FDDGSRRSKDPTL 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164419743 329 HLLHNVVRPQDQTVVFVATKHHAE----YLTELLTtqRVSCAHIYSALDPTARKINLAKFTLGKCSTLIvtDLAARG 401
Cdd:COG1204 230 ALALDLLEEGGQVLVFVSSRRDAEslakKLADELK--RRLTPEEREELEELAEELLEVSEETHTNEKLA--DCLEKG 302
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
142-251 |
2.51e-09 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 60.90 E-value: 2.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 142 TGSGKTACFLLPMFERLKTHsaqtGARALILSPTRELALQTLKFTKELGKFTGLKTALILGGDRMEDQfAALHENPDIII 221
Cdd:COG1111 26 TGLGKTAVALLVIAERLHKK----GGKVLFLAPTKPLVEQHAEFFKEALNIPEDEIVVFTGEVSPEKR-KELWEKARIIV 100
|
90 100 110
....*....|....*....|....*....|
gi 164419743 222 ATPGRLVHVAVEMSLKLQSVEYVVFDEADR 251
Cdd:COG1111 101 ATPQVIENDLIAGRIDLDDVSLLIFDEAHR 130
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
136-281 |
3.91e-09 |
|
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: 56.16 E-value: 3.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 136 VVAMArTGSGKTACFLLPMFERLKThsaqtgaRALILSPTRELALQTLKftkELGKFTGLKTALILGGDRMEDQFAAlhe 215
Cdd:cd17926 22 ILVLP-TGSGKTLTALALIAYLKEL-------RTLIVVPTDALLDQWKE---RFEDFLGDSSIGLIGGGKKKDFDDA--- 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164419743 216 npDIIIATPGRLVHVAVEMSLKLQSVEYVVFDEADRLfemgFAEQLQEIIARLPGGHQtVLFSATL 281
Cdd:cd17926 88 --NVVVATYQSLSNLAEEEKDLFDQFGLLIVDEAHHL----PAKTFSEILKELNAKYR-LGLTATP 146
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
122-224 |
7.68e-09 |
|
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350781 [Multi-domain] Cd Length: 206 Bit Score: 56.60 E-value: 7.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 122 IQRKTIPVILDG-KDVVAMARTGSGKTACFLLPMFERLK--THSAQTGARALILSPTRELALQTLKFTKElgKF--TGLK 196
Cdd:cd18023 5 IQSEVFPDLLYSdKNFVVSAPTGSGKTVLFELAILRLLKerNPLPWGNRKVVYIAPIKALCSEKYDDWKE--KFgpLGLS 82
|
90 100
....*....|....*....|....*...
gi 164419743 197 TALILGGDRMEDQFAAlhENPDIIIATP 224
Cdd:cd18023 83 CAELTGDTEMDDTFEI--QDADIILTTP 108
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
142-251 |
8.42e-09 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 59.50 E-value: 8.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 142 TGSGKTACFLLPMFERLKTHsaqtGARALILSPTRELALQTLKFTKELGKFTGLKTALILGGDRMEDQfAALHENPDIII 221
Cdd:PRK13766 38 TGLGKTAIALLVIAERLHKK----GGKVLILAPTKPLVEQHAEFFRKFLNIPEEKIVVFTGEVSPEKR-AELWEKAKVIV 112
|
90 100 110
....*....|....*....|....*....|....*....
gi 164419743 222 ATP---------GRlvhvavemsLKLQSVEYVVFDEADR 251
Cdd:PRK13766 113 ATPqviendliaGR---------ISLEDVSLLIFDEAHR 142
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
113-428 |
1.45e-08 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 58.74 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 113 KKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKT-ACFLL---PMFERLKTHSAQTGARALILSPTRELA-------LQ 181
Cdd:PRK13767 27 KEKFGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAFLAiidELFRLGREGELEDKVYCLYVSPLRALNndihrnlEE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 182 TLKFTKELGKFTGLKTALILGGDRMEDQFAA-----LHENPDIIIATPGRL--VHVAVEMSLKLQSVEYVVFDEADRLFE 254
Cdd:PRK13767 107 PLTEIREIAKERGEELPEIRVAIRTGDTSSYekqkmLKKPPHILITTPESLaiLLNSPKFREKLRTVKWVIVDEIHSLAE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 255 -------MGFAEQLQEIIARLPgghQTVLFSATL-P-----KLLVEFARAGLTEPVLIrldVDTKLNEQLKTSFFLVRED 321
Cdd:PRK13767 187 nkrgvhlSLSLERLEELAGGEF---VRIGLSATIePleevaKFLVGYEDDGEPRDCEI---VDARFVKPFDIKVISPVDD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 322 ---TKAAV----LLHLLHNVVRPQDQTVVFVATKHHAE----YLTELLTTQ----RVSCAHiySALDPTAR---KINLAK 383
Cdd:PRK13767 261 lihTPAEEiseaLYETLHELIKEHRTTLIFTNTRSGAErvlyNLRKRFPEEydedNIGAHH--SSLSREVRlevEEKLKR 338
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 164419743 384 FTLgKCstlIVT----DLaarGLDIPLLDNVINYSFPAKGKLFLHRVGR 428
Cdd:PRK13767 339 GEL-KV---VVSstslEL---GIDIGYIDLVVLLGSPKSVSRLLQRIGR 380
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
109-304 |
1.88e-07 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 52.54 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 109 KGIMKK--GYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLP--MFERLkthsaqtgarALILSPTreLAL---Q 181
Cdd:cd17920 1 EQILKEvfGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPalLLDGV----------TLVVSPL--ISLmqdQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 182 TLKFTKelgkfTGLKTALILGG----DRMEDQFAALHENPDIIIATPGRLVHVAVEMSL-KLQS---VEYVVFDEA---- 249
Cdd:cd17920 69 VDRLQQ-----LGIRAAALNSTlspeEKREVLLRIKNGQYKLLYVTPERLLSPDFLELLqRLPErkrLALIVVDEAhcvs 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164419743 250 ----DrlF--EMGfaeQLQEIIARLPgGHQTVLFSATLPKLLVE--FARAGLTEPVLIRLDVD 304
Cdd:cd17920 144 qwghD--FrpDYL---RLGRLRRALP-GVPILALTATATPEVREdiLKRLGLRNPVIFRASFD 200
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
121-282 |
8.80e-07 |
|
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350786 [Multi-domain] Cd Length: 177 Bit Score: 50.03 E-value: 8.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 121 PIQRKTI-PVILDGKDVVAMARTGSGKTACFLLPMFerlktHSAQTGARALILSPTRELALQTLKFTKELGKFtGLKTAL 199
Cdd:cd18028 4 PPQAEAVrAGLLKGENLLISIPTASGKTLIAEMAMV-----NTLLEGGKALYLVPLRALASEKYEEFKKLEEI-GLKVGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 200 ILGGDRMEDQFaaLHENpDIIIATPGRLVHVAVEMSLKLQSVEYVVFDEADRLFEMGFAEQLQEIIAR---LPGGHQTVL 276
Cdd:cd18028 78 STGDYDEDDEW--LGDY-DIIVATYEKFDSLLRHSPSWLRDVGVVVVDEIHLISDEERGPTLESIVARlrrLNPNTQIIG 154
|
....*.
gi 164419743 277 FSATLP 282
Cdd:cd18028 155 LSATIG 160
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
130-352 |
1.78e-06 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 51.74 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 130 ILDGKDVVAMARTGSGKTACFLLPMFERLkthsAQTGARALILSPTRELALQTLKFTKELGKFtGLKTALILGGDRMEDQ 209
Cdd:PRK00254 36 VLEGKNLVLAIPTASGKTLVAEIVMVNKL----LREGGKAVYLVPLKALAEEKYREFKDWEKL-GLRVAMTTGDYDSTDE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 210 FAALHenpDIIIATPGRLVHVAVEMSLKLQSVEYVVFDEADRLFEMGFAEQLQEIIARLPGGHQTVLFSATL--PKLLVE 287
Cdd:PRK00254 111 WLGKY---DIIIATAEKFDSLLRHGSSWIKDVKLVVADEIHLIGSYDRGATLEMILTHMLGRAQILGLSATVgnAEELAE 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164419743 288 FARAGLT----EPVLIRLDVdtklneqlktsF---FLVREDTKAAVLLH----LLHNVVRPQDQTVVFVATKHHAE 352
Cdd:PRK00254 188 WLNAELVvsdwRPVKLRKGV-----------FyqgFLFWEDGKIERFPNswesLVYDAVKKGKGALVFVNTRRSAE 252
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
129-251 |
2.96e-06 |
|
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350793 [Multi-domain] Cd Length: 181 Bit Score: 48.66 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 129 VILDGKDVVAMArTGSGKTACFLLPMFERLKthsaQTGARALILSPTRELALQTLKFTKELGKFTGLKTALIlgGDRMED 208
Cdd:cd18035 13 VALNGNTLIVLP-TGLGKTIIAILVAADRLT----KKGGKVLILAPSRPLVEQHAENLKRVLNIPDKITSLT--GEVKPE 85
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 164419743 209 QFAALHENPDIIIATPGRLVHVAVEMSLKLQSVEYVVFDEADR 251
Cdd:cd18035 86 ERAERWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEAHH 128
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
134-249 |
3.74e-06 |
|
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: 48.42 E-value: 3.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 134 KDVVAMARTGSGKT--ACFLLPMFERLKTHSAQTGARALILSPTRELALQTlkfTKELGKFTGLKTALILGGDRMEDQ-- 209
Cdd:cd18034 17 RNTIVVLPTGSGKTliAVMLIKEMGELNRKEKNPKKRAVFLVPTVPLVAQQ---AEAIRSHTDLKVGEYSGEMGVDKWtk 93
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 164419743 210 --FAALHENPDIIIATPGRLVHVAVEMSLKLQSVEYVVFDEA 249
Cdd:cd18034 94 erWKEELEKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
124-280 |
8.18e-06 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 46.90 E-value: 8.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 124 RKTIPVILDGKD--VVAMArTGSGKTACFLLPMFERLKTHSAQtgaRALILSPTRELALQTLK-FTKELGKFTGLKTalI 200
Cdd:pfam04851 13 ENLLESIKNGQKrgLIVMA-TGSGKTLTAAKLIARLFKKGPIK---KVLFLVPRKDLLEQALEeFKKFLPNYVEIGE--I 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 201 LGGDRMEDQFaalhENPDIIIATPGRLvHVAVEMSLKLQSVE---YVVFDEADRLfemgFAEQLQEIIARLPggHQTVL- 276
Cdd:pfam04851 87 ISGDKKDESV----DDNKIVVTTIQSL-YKALELASLELLPDffdVIIIDEAHRS----GASSYRNILEYFK--PAFLLg 155
|
....
gi 164419743 277 FSAT 280
Cdd:pfam04851 156 LTAT 159
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
131-251 |
1.47e-05 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350685 [Multi-domain] Cd Length: 201 Bit Score: 46.66 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 131 LDGKDVVAMARTGSGKTACFLLPMFERLKTHSAQTGARALILSPTRELALQTL-KFTKELGKfTGLKTALILGGDRMEDQ 209
Cdd:cd17927 15 LKGKNTIICLPTGSGKTFVAVLICEHHLKKFPAGRKGKVVFLANKVPLVEQQKeVFRKHFER-PGYKVTGLSGDTSENVS 93
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 164419743 210 FAALHENPDIIIATPGRLVHV---AVEMSLKLQSVeyVVFDEADR 251
Cdd:cd17927 94 VEQIVESSDVIIVTPQILVNDlksGTIVSLSDFSL--LVFDECHN 136
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
123-384 |
1.86e-05 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 48.21 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 123 QRKTIPVILDGKDVVAMARTGSGKTACFLLP--MFERLkthsaqtgarALILSPTreLALqtlkftkelgkftglktali 200
Cdd:COG0514 22 QEEIIEAVLAGRDALVVMPTGGGKSLCYQLPalLLPGL----------TLVVSPL--IAL-------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 201 lggdrMEDQFAALHEN---------------------------PDIIIATPGRLVHVAVEMSLKLQSVEYVVFDEA---- 249
Cdd:COG0514 70 -----MKDQVDALRAAgiraaflnsslsaeerrevlralrageLKLLYVAPERLLNPRFLELLRRLKISLFAIDEAhcis 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 250 --------DRLfemgfaeQLQEIIARLPgGHQTVLFSATlpkllvefAraglTEPVliRLDVDTKLN----EQLKTSF-- 315
Cdd:COG0514 145 qwghdfrpDYR-------RLGELRERLP-NVPVLALTAT--------A----TPRV--RADIAEQLGledpRVFVGSFdr 202
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164419743 316 ----FLVRE---DTKAAVLLHLLHNvvRPQDQTVVFVATKHHAEYLTELLTTQRVSCAHiYSA-LDPTARKINLAKF 384
Cdd:COG0514 203 pnlrLEVVPkppDDKLAQLLDFLKE--HPGGSGIVYCLSRKKVEELAEWLREAGIRAAA-YHAgLDAEEREANQDRF 276
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
121-295 |
2.60e-05 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 48.01 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 121 PIQRKTIPVILDGKDVVAMARTGSGKT--ACFLLpmFERLkthsaQTGARALILSPTRELALQtlKFtKELGKFTGLKTA 198
Cdd:COG4581 28 PFQEEAILALEAGRSVLVAAPTGSGKTlvAEFAI--FLAL-----ARGRRSFYTAPIKALSNQ--KF-FDLVERFGAENV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 199 LILGGDRmedqfaalHENPD--IIIATPGRLVHVAVEMSLKLQSVEYVVFDE----ADRlfEMGFAeqLQEIIARLPGGH 272
Cdd:COG4581 98 GLLTGDA--------SVNPDapIVVMTTEILRNMLYREGADLEDVGVVVMDEfhylADP--DRGWV--WEEPIIHLPARV 165
|
170 180
....*....|....*....|...
gi 164419743 273 QTVLFSATLPKllVEFARAGLTE 295
Cdd:COG4581 166 QLVLLSATVGN--AEEFAEWLTR 186
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
116-248 |
3.49e-05 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 47.79 E-value: 3.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 116 YKVPTPIQRKTIPVILDGKDVVAMARTGSGKT-ACFLLP---MFERLKTHSAQTGARALILSPTRELA------LQTlkF 185
Cdd:COG1201 22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAFLPAldeLARRPRPGELPDGLRVLYISPLKALAndiernLRA--P 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164419743 186 TKELGKFTGLKTALILGGDRMEDQFAA-----LHENPDIIIATPgrlvhvavEmSL-----------KLQSVEYVVFDE 248
Cdd:COG1201 100 LEEIGEAAGLPLPEIRVGVRTGDTPASerqrqRRRPPHILITTP--------E-SLallltspdareLLRGVRTVIVDE 169
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
119-280 |
5.05e-05 |
|
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: 44.71 E-value: 5.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 119 PTPIQRKTIPVIL-DGKDVVAMAR-----TGSGKTACFLLPMFERLKthsaqTGARALILSPTRELALQTLKFTKELgkF 192
Cdd:cd17918 16 LTKDQAQAIKDIEkDLHSPEPMDRllsgdVGSGKTLVALGAALLAYK-----NGKQVAILVPTEILAHQHYEEARKF--L 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 193 TGLKTALILGGDRMEDQfaalhENPDIIIATPGrLVHVAVemslKLQSVEYVVFDEADRlfemgFAEQLQEIIARLpGGH 272
Cdd:cd17918 89 PFINVELVTGGTKAQIL-----SGISLLVGTHA-LLHLDV----KFKNLDLVIVDEQHR-----FGVAQREALYNL-GAT 152
|
....*...
gi 164419743 273 QTVLFSAT 280
Cdd:cd17918 153 HFLEATAT 160
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
315-436 |
5.84e-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: 43.74 E-value: 5.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 315 FFLVREDTKAAVLLHLLHNVVR--PQDQTVVFVATKHHAEYLTELLTTQRVSCAHIYSALDPTARKINLAKFTLGKCSTL 392
Cdd:cd18794 5 FYSVRPKDKKDEKLDLLKRIKVehLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVI 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 164419743 393 IVTDLAARGLDIPLLDNVINYSFPAKGKLFLHRVGrvaRAGRSG 436
Cdd:cd18794 85 VATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESG---RAGRDG 125
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
121-224 |
8.62e-05 |
|
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350779 [Multi-domain] Cd Length: 191 Bit Score: 44.17 E-value: 8.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 121 PIQRKTIPVILDGKD-VVAMARTGSGKTACFLLPMferLKTHSAQTGARALILSPTRELALQTL-----KFTKELGkftg 194
Cdd:cd18021 6 PIQTQVFNSLYNTDDnVFVGAPTGSGKTVCAELAL---LRHWRQNPKGRAVYIAPMQELVDARYkdwraKFGPLLG---- 78
|
90 100 110
....*....|....*....|....*....|
gi 164419743 195 lKTALILGGDRMEDqfAALHENPDIIIATP 224
Cdd:cd18021 79 -KKVVKLTGETSTD--LKLLAKSDVILATP 105
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
119-289 |
9.77e-05 |
|
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also called SKI2 or DHX13) plays a role in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. SKIV2L belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350785 [Multi-domain] Cd Length: 179 Bit Score: 44.18 E-value: 9.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 119 PTPIQRKTIPVILDGKDVVAMARTGSGKT--ACFLLPMFERLKThsaqtgaRALILSPTRELALQTLKFTKELGKFTGLK 196
Cdd:cd18027 9 LDVFQKQAILHLEAGDSVFVAAHTSAGKTvvAEYAIALAQKHMT-------RTIYTSPIKALSNQKFRDFKNTFGDVGLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 197 TalilgGDrmedqfAALHENPDIIIATPGRLVHVAVEMSLKLQSVEYVVFDEADRLFEMGFAEQLQEIIARLPGGHQTVL 276
Cdd:cd18027 82 T-----GD------VQLNPEASCLIMTTEILRSMLYNGSDVIRDLEWVIFDEVHYINDAERGVVWEEVLIMLPDHVSIIL 150
|
170
....*....|...
gi 164419743 277 FSATLPKlLVEFA 289
Cdd:cd18027 151 LSATVPN-TVEFA 162
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
121-153 |
1.91e-04 |
|
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ family of highly conserved DNA repair helicases that is part of 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: 350773 [Multi-domain] Cd Length: 209 Bit Score: 43.51 E-value: 1.91e-04
10 20 30
....*....|....*....|....*....|...
gi 164419743 121 PIQRKTIPVILDGKDVVAMARTGSGKTACFLLP 153
Cdd:cd18015 21 PLQLETINATMAGRDVFLVMPTGGGKSLCYQLP 53
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
321-413 |
2.06e-04 |
|
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: 42.08 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 321 DTKAAVLLHLLHNVVRPQDQTVVFVATKHHAEYLTELLTTQRVSCAHIYSALDPTARKINLAKF--TLGKCSTLIVTDLA 398
Cdd:cd18793 10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFneDPDIRVFLLSTKAG 89
|
90
....*....|....*
gi 164419743 399 ARGLDIPLLDNVINY 413
Cdd:cd18793 90 GVGLNLTAANRVILY 104
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
135-434 |
4.65e-04 |
|
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: 43.57 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 135 DVVAMARTGSGKTACFLLPMFERLKThsaQTGARALILSPTRELALQTLKFTKELGKFTGLKTALILGGDRME----DQF 210
Cdd:cd09639 1 LLVIEAPTGYGKTEAALLWALHSLKS---QKADRVIIALPTRATINAMYRRAKEAFGETGLYHSSILSSRIKEmgdsEEF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 211 AAL-----HEN------------PDIIIATPGRLVHVAvEMSLKLQSVEYVVFDEADRL--FEMGFAEQLQEIIARLPGG 271
Cdd:cd09639 78 EHLfplyiHSNdtlfldpitvctIDQVLKSVFGEFGHY-EFTLASIANSLLIFDEVHFYdeYTLALILAVLEVLKDNDVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 272 HqtVLFSATLPKLLVEFARAglTEPVLIRLDVDTKLNEQLKTSFFLVREDTKAAVLLHLLHNVVRPQDQTVVFVATKHHA 351
Cdd:cd09639 157 I--LLMSATLPKFLKEYAEK--IGYVEENEPLDLKPNERAPFIKIESDKVGEISSLERLLEFIKKGGSVAIIVNTVDRAQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 352 EY---LTELLTTQRVSCAHIYSALDPTARKINLAKFTLGKCST--LIVTDLAARGLDIpllDNVINYSFPAKGKLFLHRV 426
Cdd:cd09639 233 EFyqqLKEKGPEEEIMLIHSRFTEKDRAKKEAELLLEFKKSEKfvIVATQVIEASLDI---SVDVMITELAPIDSLIQRL 309
|
....*...
gi 164419743 427 GRVARAGR 434
Cdd:cd09639 310 GRLHRYGE 317
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
118-248 |
1.13e-03 |
|
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350794 [Multi-domain] Cd Length: 204 Bit Score: 41.31 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 118 VPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERL-KTHSAQTGARALILSPTRELALQTL-KFTKELGKftGL 195
Cdd:cd18036 2 ELRNYQLELVLPALRGKNTIICAPTGSGKTRVAVYICRHHLeKRRSAGEKGRVVVLVNKVPLVEQQLeKFFKYFRK--GY 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 164419743 196 KTALILGGDRMEDQFAALHENPDIIIATPGRLVH----VAVEMSLKLQSVEYVVFDE 248
Cdd:cd18036 80 KVTGLSGDSSHKVSFGQIVKASDVIICTPQILINnllsGREEERVYLSDFSLLIFDE 136
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
133-248 |
1.51e-03 |
|
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: 40.26 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 133 GKDVVAMARTGSGKTACFLLPMFERLKTHSAQtGARALILSPTRELALQTLKFTKELGKFTGLK-TALILGGDRMEDQFA 211
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEK-GVQVLYISPLKALINDQERRLEEPLDEIDLEiPVAVRHGDTSQSEKA 79
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 164419743 212 ALHEN-PDIIIATPGRL--VHVAVEMSLKLQSVEYVVFDE 248
Cdd:cd17922 80 KQLKNpPGILITTPESLelLLVNKKLRELFAGLRYVVVDE 119
|
|
| DEXHc_RE_I_III_res |
cd18032 |
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ... |
137-251 |
1.71e-03 |
|
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350790 [Multi-domain] Cd Length: 163 Bit Score: 39.85 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 137 VAMArTGSGKT--ACFLLPMFerlktHSAQTGARALILSPTRELALQTLkftKELGKFTGLKTALILGGDRMEDQFAalh 214
Cdd:cd18032 25 LVMA-TGTGKTytAAFLIKRL-----LEANRKKRILFLAHREELLEQAE---RSFKEVLPDGSFGNLKGGKKKPDDA--- 92
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 164419743 215 enpDIIIATPGRLvhvaveMSLKLQS------VEYVVFDEADR 251
Cdd:cd18032 93 ---RVVFATVQTL------NKRKRLEkfppdyFDLIIIDEAHH 126
|
|
| DEXHc_Mtr4-like |
cd18024 |
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or ... |
103-290 |
2.01e-03 |
|
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or SKIV2L2) is a type II DEAD box helicase that plays a role in the processing of structured RNAs, including the maturation of 5.8S ribosomal RNA (rRNA)and is part of the TRAMP complex that is involved in exosome-mediated degradation of aberrant RNAs. Mtr4 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350782 [Multi-domain] Cd Length: 205 Bit Score: 40.50 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 103 LSYPVFKGIMKKGYK-VPTPIQRKTIPVILDGKDVVAMARTGSGKTACfllpmFERLKTHSAQTGARALILSPTRELALQ 181
Cdd:cd18024 16 ISAHKPPGNPARTYPfTLDPFQKTAIACIERNESVLVSAHTSAGKTVV-----AEYAIAQSLRDKQRVIYTSPIKALSNQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 182 TLK-FTKELGKfTGLKTalilgGDrmedqfAALHENPDIIIATPGRLVHVAVEMSLKLQSVEYVVFDEA----DRlfEMG 256
Cdd:cd18024 91 KYReLQEEFGD-VGLMT-----GD------VTINPNASCLVMTTEILRSMLYRGSEIMREVAWVIFDEIhymrDK--ERG 156
|
170 180 190
....*....|....*....|....*....|....
gi 164419743 257 FAeqLQEIIARLPGGHQTVLFSATLPKLLvEFAR 290
Cdd:cd18024 157 VV--WEETIILLPDKVRYVFLSATIPNAR-QFAE 187
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
341-411 |
5.01e-03 |
|
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins 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: 350186 [Multi-domain] Cd Length: 116 Bit Score: 37.54 E-value: 5.01e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164419743 341 TVVFVATKHHAEYLTELLTTQRVSCAHIYSALDPTAR---KINLAKFTLGKCSTLIVTDLAARGLDIPLLDNVI 411
Cdd:cd18799 9 TLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERgdeALILLFFGELKPPILVTVDLLTTGVDIPEVDNVV 82
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
121-249 |
8.64e-03 |
|
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) is part of the RecQ family of highly conserved DNA repair helicases that is part of 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. Mutations cause Rothmund-Thomson/RAPADILINO/Baller-Gerold syndrome.
Pssm-ID: 350776 [Multi-domain] Cd Length: 201 Bit Score: 38.39 E-value: 8.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419743 121 PIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERlkthSAQTGARALILSPTreLAL-----QTLKftkelgkfTGL 195
Cdd:cd18018 15 PGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLL----RRRGPGLTLVVSPL--IALmkdqvDALP--------RAI 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 164419743 196 KTALILGGDRMEDQFAALHE----NPDIIIATPGRLVHVA-VEMSLKLQSVEYVVFDEA 249
Cdd:cd18018 81 KAAALNSSLTREERRRILEKlragEVKILYVSPERLVNESfRELLRQTPPISLLVVDEA 139
|
|
| |
