|
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 ... |
100-304 |
2.20e-150 |
|
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: 440.20 E-value: 2.20e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 100 GGFQSMGLGYPVFKGIMKKGYKIPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLIPMFEKLKVHSAKTGARALILSPT 179
Cdd:cd17959 1 GGFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTVGARALILSPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 180 RELALQTLKFTKELGRYTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLMHVAIEMKLKLQSVEYVVFDEADRLFEM 259
Cdd:cd17959 81 RELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEM 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622179293 260 GFAEQLQEIISRLPENRQTVLFSATLPKLLVEFARAGLTEPVLIR 304
Cdd:cd17959 161 GFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLIR 205
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
102-465 |
7.03e-136 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 411.46 E-value: 7.03e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 102 FQSMGLGYPVFKGIMKKGYKIPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLIPMFEKLKVHSAKtGARALILSPTRE 181
Cdd:COG0513 4 FADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPR-APQALILAPTRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 182 LALQTLKFTKELGRYTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLMHVAIEMKLKLQSVEYVVFDEADRLFEMGF 261
Cdd:COG0513 83 LALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMGF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 262 AEQLQEIISRLPENRQTVLFSATLPKLLVEFARAGLTEPVLIRLDVESKLSEQLKLSFYHVRADDKPALLLYLLRtvVRP 341
Cdd:COG0513 163 IEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLR--DED 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 342 QDQTIVFVATKHHTEYLKELLTAQGVNCTHVYSSLDQTARKINVGKFIHGKCSVLIVTDLAARGIDIPLLDNVINYSFPA 421
Cdd:COG0513 241 PERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPE 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1622179293 422 KAKLFLHRVGRVARAGRSGTAYSLVAPDETPYVFDLHLFLGRPL 465
Cdd:COG0513 321 DPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKI 364
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
113-446 |
2.76e-88 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 287.22 E-value: 2.76e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 113 KGIMKKGYKIPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLIPMFEKLKVHSAKTG--ARALILSPTRELALQTLKFT 190
Cdd:PRK11192 14 EALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFPRRKSgpPRILILTPTRELAMQVADQA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 191 KELGRYTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLMHVAIEMKLKLQSVEYVVFDEADRLFEMGFAEQLQEIIS 270
Cdd:PRK11192 94 RELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRMLDMGFAQDIETIAA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 271 RLPENRQTVLFSATLP-KLLVEFARAGLTEPVLIrlDVESKLSEQLK-LSFYHvRADD---KPALLLYLLRT--VVRpqd 343
Cdd:PRK11192 174 ETRWRKQTLLFSATLEgDAVQDFAERLLNDPVEV--EAEPSRRERKKiHQWYY-RADDlehKTALLCHLLKQpeVTR--- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 344 qTIVFVATKHHTEYLKELLTAQGVNCTHVYSSLDQTARKINVGKFIHGKCSVLIVTDLAARGIDIPLLDNVINYSFPAKA 423
Cdd:PRK11192 248 -SIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINFDMPRSA 326
|
330 340
....*....|....*....|...
gi 1622179293 424 KLFLHRVGRVARAGRSGTAYSLV 446
Cdd:PRK11192 327 DTYLHRIGRTGRAGRKGTAISLV 349
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
113-304 |
5.73e-86 |
|
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: 272.39 E-value: 5.73e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 113 KGIMKKGYKIPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLIPMFEKLKVHSAKTGA--RALILSPTRELALQTLKFT 190
Cdd:cd00268 3 KALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGRgpQALVLAPTRELAMQIAEVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 191 KELGRYTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLMHVAIEMKLKLQSVEYVVFDEADRLFEMGFAEQLQEIIS 270
Cdd:cd00268 83 RKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKILS 162
|
170 180 190
....*....|....*....|....*....|....
gi 1622179293 271 RLPENRQTVLFSATLPKLLVEFARAGLTEPVLIR 304
Cdd:cd00268 163 ALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
119-465 |
4.64e-82 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 271.67 E-value: 4.64e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 119 GYKIPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLIPMFEKLKVhsAKTGARALILSPTRELALQTLKFTKELGRYT- 197
Cdd:PRK11776 23 GYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDV--KRFRVQALVLCPTRELADQVAKEIRRLARFIp 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 198 GLKTALILGGDKMEDQFAALHENPDIIIATPGRLMHVAIEMKLKLQSVEYVVFDEADRLFEMGFAEQLQEIISRLPENRQ 277
Cdd:PRK11776 101 NIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLDMGFQDAIDAIIRQAPARRQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 278 TVLFSATLPKLLVEFARAGLTEPVLIRLDVESKLS--EQLklsFYHVRADDKPALLLYLLRTVvRPQdQTIVFVATKHHT 355
Cdd:PRK11776 181 TLLFSATYPEGIAAISQRFQRDPVEVKVESTHDLPaiEQR---FYEVSPDERLPALQRLLLHH-QPE-SCVVFCNTKKEC 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 356 EYLKELLTAQGVNCTHVYSSLDQTARKINVGKFIHGKCSVLIVTDLAARGIDIPLLDNVINYSFPAKAKLFLHRVGRVAR 435
Cdd:PRK11776 256 QEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELARDPEVHVHRIGRTGR 335
|
330 340 350
....*....|....*....|....*....|
gi 1622179293 436 AGRSGTAYSLVAPDETPYVFDLHLFLGRPL 465
Cdd:PRK11776 336 AGSKGLALSLVAPEEMQRANAIEDYLGRKL 365
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
102-465 |
2.20e-73 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 248.18 E-value: 2.20e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 102 FQSMGLGYPVFKGIMKKGYKIPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLIPMFEKLKVHSAKTGAR----ALILS 177
Cdd:PRK10590 3 FDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGRrpvrALILT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 178 PTRELALQTLKFTKELGRYTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLMHVAIEMKLKLQSVEYVVFDEADRLF 257
Cdd:PRK10590 83 PTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRML 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 258 EMGFAEQLQEIISRLPENRQTVLFSATLPKLLVEFARAGLTEPVLIRLDVESKLSEQLKLSFYHVRADDKPALLLYLLRT 337
Cdd:PRK10590 163 DMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKRELLSQMIGK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 338 vvRPQDQTIVFVATKHHTEYLKELLTAQGVNCTHVYSSLDQTARKINVGKFIHGKCSVLIVTDLAARGIDIPLLDNVINY 417
Cdd:PRK10590 243 --GNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNY 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1622179293 418 SFPAKAKLFLHRVGRVARAGRSGTAYSLVAPDETPYVFDLHLFLGRPL 465
Cdd:PRK10590 321 ELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEI 368
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
102-458 |
4.16e-67 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 229.86 E-value: 4.16e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 102 FQSMGLGYPVFKGIMKKGYKIPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLIPMFEKLKVHSAKTG-----ARALIL 176
Cdd:PRK04837 10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPAPEDrkvnqPRALIM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 177 SPTRELALQTLKFTKELGRYTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLMHVAIEMKLKLQSVEYVVFDEADRL 256
Cdd:PRK04837 90 APTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 257 FEMGFAEQLQEIISRLPE--NRQTVLFSATLPKLLVEFARAGLTEPVLIRLDVESKLSEQLKLSFYHVRADDKPALLLYL 334
Cdd:PRK04837 170 FDLGFIKDIRWLFRRMPPanQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEELFYPSNEEKMRLLQTL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 335 LRTvvRPQDQTIVFVATKHHTEYLKELLTAQGVNCTHVYSSLDQTARKINVGKFIHGKCSVLIVTDLAARGIDIPLLDNV 414
Cdd:PRK04837 250 IEE--EWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHV 327
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1622179293 415 INYSFPAKAKLFLHRVGRVARAGRSGTAYSLvAPDEtpYVFDLH 458
Cdd:PRK04837 328 FNYDLPDDCEDYVHRIGRTGRAGASGHSISL-ACEE--YALNLP 368
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
111-304 |
1.77e-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: 220.20 E-value: 1.77e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 111 VFKGIMKKGYKIPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLIPMFEKLkVHSAKTGA--RALILSPTRELALQTLK 188
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERL-LYRPKKKAatRVLVLVPTRELAMQCFS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 189 FTKELGRYTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLM-HVAIEMKLKLQSVEYVVFDEADRLFEMGFAEQLQE 267
Cdd:cd17947 80 VLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIdHLRNSPSFDLDSIEILVLDEADRMLEEGFADELKE 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 1622179293 268 IISRLPENRQTVLFSATLPKLLVEFARAGLTEPVLIR 304
Cdd:cd17947 160 ILRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRVF 196
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
101-470 |
3.19e-66 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 229.03 E-value: 3.19e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 101 GFQSMGLGYPVFKGIMKKGYKIPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLIPMFEKL-----KVHSAKTGARALI 175
Cdd:PRK01297 88 RFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLlqtppPKERYMGEPRALI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 176 LSPTRELALQTLKFTKELGRYTGLKTALILGGDKMEDQFAALHEN-PDIIIATPGRLMHVAIEMKLKLQSVEYVVFDEAD 254
Cdd:PRK01297 168 IAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEARfCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEAD 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 255 RLFEMGFAEQLQEIISRLP--ENRQTVLFSATLPKLLVEFARAGLTEPVLIRLDVESKLSEQLKLSFYHVRADDKPALLL 332
Cdd:PRK01297 248 RMLDMGFIPQVRQIIRQTPrkEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAGSDKYKLLY 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 333 YLLRTvvRPQDQTIVFVATKHHTEYLKELLTAQGVNCTHVYSSLDQTARKINVGKFIHGKCSVLIVTDLAARGIDIPLLD 412
Cdd:PRK01297 328 NLVTQ--NPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGIS 405
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622179293 413 NVINYSFPAKAKLFLHRVGRVARAGRSGTAYSLVAPDETPYVFDLHLFLGRPLILANP 470
Cdd:PRK01297 406 HVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKISCEMP 463
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
124-292 |
9.47e-65 |
|
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: 214.03 E-value: 9.47e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 124 TPIQRKTIPVILDGKDVVAMARTGSGKTACFLIPMFEKLKVHsaKTGARALILSPTRELALQTLKFTKELGRYTGLKTAL 203
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKL--DNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVAS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 204 ILGGDKMEDQFAALHeNPDIIIATPGRLMHVAIEMKlKLQSVEYVVFDEADRLFEMGFAEQLQEIISRLPENRQTVLFSA 283
Cdd:pfam00270 79 LLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSA 156
|
....*....
gi 1622179293 284 TLPKLLVEF 292
Cdd:pfam00270 157 TLPRNLEDL 165
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
102-454 |
3.48e-61 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 217.90 E-value: 3.48e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 102 FQSMGLGYPVFKGIMKKGYKIPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLIPMFEKLKVHSA-----KTGARALIL 176
Cdd:PRK04537 11 FSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPAladrkPEDPRALIL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 177 SPTRELALQTLKFTKELGRYTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLMHVAIEMKL-KLQSVEYVVFDEADR 255
Cdd:PRK04537 91 APTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVvSLHACEICVLDEADR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 256 LFEMGFAEQLQEIISRLPE--NRQTVLFSATLPKLLVEFARAGLTEPVLIRLDVESKLSEQLKLSFYHVRADDKPALLLY 333
Cdd:PRK04537 171 MFDLGFIKDIRFLLRRMPErgTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRIYFPADEEKQTLLLG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 334 LLRtvvRPQD-QTIVFVATKHHTEYLKELLTAQGVNCTHVYSSLDQTARKINVGKFIHGKCSVLIVTDLAARGIDIPLLD 412
Cdd:PRK04537 251 LLS---RSEGaRTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVK 327
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1622179293 413 NVINYSFPAKAKLFLHRVGRVARAGRSGTA-------YSLVAPDETPYV 454
Cdd:PRK04537 328 YVYNYDLPFDAEDYVHRIGRTARLGEEGDAisfacerYAMSLPDIEAYI 376
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
108-450 |
4.36e-61 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 216.95 E-value: 4.36e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 108 GYP--VFKGIMKKGYKIPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLIPMFeklkVH-SAKT------GARALILSP 178
Cdd:PTZ00110 136 SFPdyILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAI----VHiNAQPllrygdGPIVLVLAP 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 179 TRELALQTLKFTKELGRYTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLMHVAIEMKLKLQSVEYVVFDEADRLFE 258
Cdd:PTZ00110 212 TRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLD 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 259 MGFAEQLQEIISRLPENRQTVLFSATLPKLLVEFARAGLTE-PVLIRL-DVESKLSEQLKLSFYHVRADDKPALLLYLLR 336
Cdd:PTZ00110 292 MGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEePVHVNVgSLDLTACHNIKQEVFVVEEHEKRGKLKMLLQ 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 337 TVVRPQDQTIVFVATKHHTEYLKELLTAQGVNCTHVYSSLDQTARKINVGKFIHGKCSVLIVTDLAARGIDIPLLDNVIN 416
Cdd:PTZ00110 372 RIMRDGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVIN 451
|
330 340 350
....*....|....*....|....*....|....
gi 1622179293 417 YSFPAKAKLFLHRVGRVARAGRSGTAYSLVAPDE 450
Cdd:PTZ00110 452 FDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDK 485
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
102-446 |
1.85e-60 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 217.02 E-value: 1.85e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 102 FQSMGLGYPVFKGIMKKGYKIPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLIPMFEKLKvhSAKTGARALILSPTRE 181
Cdd:PRK11634 8 FADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLD--PELKAPQILVLAPTRE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 182 LALQTLKFTKELGRYT-GLKTALILGGDKMEDQFAALHENPDIIIATPGRLMHVAIEMKLKLQSVEYVVFDEADRLFEMG 260
Cdd:PRK11634 86 LAVQVAEAMTDFSKHMrGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 261 FAEQLQEIISRLPENRQTVLFSATLPKLLVEFARAGLTEPVLIRLDVESKLSEQLKLSFYHVRADDKPALLLYLLRTvvR 340
Cdd:PRK11634 166 FIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKNEALVRFLEA--E 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 341 PQDQTIVFVATKHHTEYLKELLTAQGVNCTHVYSSLDQTARKINVGKFIHGKCSVLIVTDLAARGIDIPLLDNVINYSFP 420
Cdd:PRK11634 244 DFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIP 323
|
330 340
....*....|....*....|....*.
gi 1622179293 421 AKAKLFLHRVGRVARAGRSGTAYSLV 446
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 ... |
102-303 |
2.53e-60 |
|
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: 203.70 E-value: 2.53e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 102 FQSMGLGYPVFKGIMKKGYKIPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLIPMFEKLKvhSAKTGARALILSPTRE 181
Cdd:cd17954 2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALL--ENPQRFFALVLAPTRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 182 LALQTLKFTKELGRYTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLMHVAIEMK-LKLQSVEYVVFDEADRLFEMG 260
Cdd:cd17954 80 LAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKgFSLKSLKFLVMDEADRLLNMD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1622179293 261 FAEQLQEIISRLPENRQTVLFSATLPKLLVEFARAGLTEPVLI 303
Cdd:cd17954 160 FEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKI 202
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
115-303 |
5.84e-59 |
|
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: 199.74 E-value: 5.84e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 115 IMKKGYKIPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLIPMFEKLKVHSAKTGARALILSPTRELALQTLKFTKELG 194
Cdd:cd17957 5 LEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKKGLRALILAPTRELASQIYRELLKLS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 195 RYTGLKTALILGGD-KMEDQFAALHENPDIIIATPGRLMHVAIEMKLKLQSVEYVVFDEADRLFEMGFAEQLQEIISRLP 273
Cdd:cd17957 85 KGTGLRIVLLSKSLeAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDEILAACT 164
|
170 180 190
....*....|....*....|....*....|.
gi 1622179293 274 E-NRQTVLFSATLPKLLVEFARAGLTEPVLI 303
Cdd:cd17957 165 NpNLQRSLFSATIPSEVEELARSVMKDPIRI 195
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
119-304 |
1.02e-57 |
|
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: 196.26 E-value: 1.02e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 119 GYKIPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLIPMFEKL---KVHSAKTGARALILSPTRELALQTLKFTKELGR 195
Cdd:cd17960 9 GFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILlkrKANLKKGQVGALIISPTRELATQIYEVLQSFLE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 196 YTG--LKTALILGGDKMEDQFAALHEN-PDIIIATPGRL--MHVAIEMKLKLQSVEYVVFDEADRLFEMGFAEQLQEIIS 270
Cdd:cd17960 89 HHLpkLKCQLLIGGTNVEEDVKKFKRNgPNILVGTPGRLeeLLSRKADKVKVKSLEVLVLDEADRLLDLGFEADLNRILS 168
|
170 180 190
....*....|....*....|....*....|....
gi 1622179293 271 RLPENRQTVLFSATLPKLLVEFARAGLTEPVLIR 304
Cdd:cd17960 169 KLPKQRRTGLFSATQTDAVEELIKAGLRNPVRVV 202
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
102-450 |
9.49e-56 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 197.74 E-value: 9.49e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 102 FQSMGLGYPVFKGIMKKGYKIPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLIPMFEKlkVHSAKTGARALILSPTRE 181
Cdd:PTZ00424 30 FDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQL--IDYDLNACQALILAPTRE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 182 LALQTLKFTKELGRYTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLMHVAIEMKLKLQSVEYVVFDEADRLFEMGF 261
Cdd:PTZ00424 108 LAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRGF 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 262 AEQLQEIISRLPENRQTVLFSATLPKLLVEFARAGLTEPVLIRLDVESKLSEQLKLSFYHVRADD-KPALLLYLLRTVVr 340
Cdd:PTZ00424 188 KGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEwKFDTLCDLYETLT- 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 341 pQDQTIVFVATKHHTEYLKELLTAQGVNCTHVYSSLDQTARKINVGKFIHGKCSVLIVTDLAARGIDIPLLDNVINYSFP 420
Cdd:PTZ00424 267 -ITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLP 345
|
330 340 350
....*....|....*....|....*....|
gi 1622179293 421 AKAKLFLHRVGRVARAGRSGTAYSLVAPDE 450
Cdd:PTZ00424 346 ASPENYIHRIGRSGRFGRKGVAINFVTPDD 375
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
102-287 |
4.16e-55 |
|
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: 190.01 E-value: 4.16e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 102 FQSMGLGYPVFKGIMKKGYKIPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLIPMFEKL--------KVHSAKTGARA 173
Cdd:cd17967 2 FEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLledgppsvGRGRRKAYPSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 174 LILSPTRELALQTLKFTKELGRYTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLMHVaIEM-KLKLQSVEYVVFDE 252
Cdd:cd17967 82 LILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDF-IERgRISLSSIKFLVLDE 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 1622179293 253 ADRLFEMGFAEQLQEIISR----LPENRQTVLFSATLPK 287
Cdd:cd17967 161 ADRMLDMGFEPQIRKIVEHpdmpPKGERQTLMFSATFPR 199
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
113-303 |
7.18e-55 |
|
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: 188.27 E-value: 7.18e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 113 KGIMKKGYKIPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLIPMFEKLKVH--SAKTGARALILSPTRELALQTLKFT 190
Cdd:cd17941 3 KGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRErwTPEDGLGALIISPTRELAMQIFEVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 191 KELGRYTGLKTALILGGDKMEDQFAALHENpDIIIATPGRLM-HVAIEMKLKLQSVEYVVFDEADRLFEMGFAEQLQEII 269
Cdd:cd17941 83 RKVGKYHSFSAGLIIGGKDVKEEKERINRM-NILVCTPGRLLqHMDETPGFDTSNLQMLVLDEADRILDMGFKETLDAIV 161
|
170 180 190
....*....|....*....|....*....|....
gi 1622179293 270 SRLPENRQTVLFSATLPKLLVEFARAGLTEPVLI 303
Cdd:cd17941 162 ENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYI 195
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
111-303 |
1.44e-54 |
|
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: 188.30 E-value: 1.44e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 111 VFKGIMKKGYKIPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLIPMFE------KLKVHSAKTGARALILSPTRELAL 184
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVyisrlpPLDEETKDDGPYALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 185 QTLKFTKELGRYTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLMHVAIEMKLKLQSVEYVVFDEADRLFEMGFAEQ 264
Cdd:cd17945 81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622179293 265 LQEIISRLP--------------------ENRQTVLFSATLPKLLVEFARAGLTEPVLI 303
Cdd:cd17945 161 VTKILDAMPvsnkkpdteeaeklaasgkhRYRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
115-303 |
1.93e-54 |
|
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: 187.24 E-value: 1.93e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 115 IMKKGYKIPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLIPMFeklkVH-------SAKTGARALILSPTRELALQTL 187
Cdd:cd17952 5 IRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPML----VHimdqrelEKGEGPIAVIVAPTRELAQQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 188 KFTKELGRYTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLMHVaIEMK-LKLQSVEYVVFDEADRLFEMGFAEQLQ 266
Cdd:cd17952 81 LEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDM-VKKKaTNLQRVTYLVLDEADRMFDMGFEYQVR 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 1622179293 267 EIISRLPENRQTVLFSATLPKLLVEFARAGLTEPVLI 303
Cdd:cd17952 160 SIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
106-303 |
1.06e-53 |
|
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: 186.04 E-value: 1.06e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 106 GLGYPVFKGIMKKGYKIPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLIPMFEKLKVH---SAKTGARALILSPTREL 182
Cdd:cd17953 18 GLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQrpvKPGEGPIGLIMAPTREL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 183 ALQTLKFTKELGRYTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLMHV--AIEMKL-KLQSVEYVVFDEADRLFEM 259
Cdd:cd17953 98 ALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDIltANNGRVtNLRRVTYVVLDEADRMFDM 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1622179293 260 GFAEQLQEIISRLPENRQTVLFSATLPKLLVEFARAGLTEPVLI 303
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 ... |
102-303 |
2.90e-53 |
|
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: 183.96 E-value: 2.90e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 102 FQSMGLGYPVFKGIMKKGYKIPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLIPMFEKLKVHSakTGARALILSPTRE 181
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDP--YGIFALVLTPTRE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 182 LALQTLKFTKELGRYTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLM-HV--AIEMKLKLQSVEYVVFDEADRLFE 258
Cdd:cd17955 79 LAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLAdHLrsSDDTTKVLSRVKFLVLDEADRLLT 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622179293 259 MGFAEQLQEIISRLPENRQTVLFSATLPKLLVEFARAGLTEPVLI 303
Cdd:cd17955 159 GSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPFFW 203
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
102-303 |
6.78e-53 |
|
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: 182.88 E-value: 6.78e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 102 FQSMGLGYPVFKGIMKKGYKIPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLIPMFEKLKvhSAKTGARALILSPTRE 181
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKID--PKKDVIQALILVPTRE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 182 LALQTLKFTKELGRYTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLMHVAIEMKLKLQSVEYVVFDEADRLFEMGF 261
Cdd:cd17940 79 LALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDF 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622179293 262 AEQLQEIISRLPENRQTVLFSATLPKLLVEFARAGLTEPVLI 303
Cdd:cd17940 159 QPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
117-304 |
1.12e-52 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 182.31 E-value: 1.12e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 117 KKGYKIPTPIQRKTIPVILDG-KDVVAMARTGSGKTACFLIPMFEKLKVHSAKtgaRALILSPTRELALQTLKFTKELGR 195
Cdd:smart00487 3 KFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGKGG---RVLVLVPTRELAEQWAEELKKLGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 196 YTGLKTALILGGDKMEDQFAAL-HENPDIIIATPGRLMHVAIEMKLKLQSVEYVVFDEADRLFEMGFAEQLQEIISRLPE 274
Cdd:smart00487 80 SLGLKVVGLYGGDSKREQLRKLeSGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPK 159
|
170 180 190
....*....|....*....|....*....|
gi 1622179293 275 NRQTVLFSATLPKLLVEFARAGLTEPVLIR 304
Cdd:smart00487 160 NVQLLLLSATPPEEIENLLELFLNDPVFID 189
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
113-285 |
7.02e-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: 180.09 E-value: 7.02e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 113 KGIMKKGYKIPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLIPMFEKL---KVHSAKTGA-RALILSPTRELALQTLK 188
Cdd:cd17961 7 KAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKIlkaKAESGEEQGtRALILVPTRELAQQVSK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 189 FTKELGRYTG--LKTALILGGDKMEDQFAALHENPDIIIATPGRLMHVAIEMKLKLQS-VEYVVFDEADRLFEMGFAEQL 265
Cdd:cd17961 87 VLEQLTAYCRkdVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLLStLKYLVIDEADLVLSYGYEEDL 166
|
170 180
....*....|....*....|
gi 1622179293 266 QEIISRLPENRQTVLFSATL 285
Cdd:cd17961 167 KSLLSYLPKNYQTFLMSATL 186
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
111-297 |
3.52e-50 |
|
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: 175.85 E-value: 3.52e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 111 VFKGIMKKGYKIPTPIQRKTIPVIL-DGKDVVAMARTGSGKTACFLIPMFEK-LKVHSA--KTGARALILSPTRELALQT 186
Cdd:cd17964 5 LLKALTRMGFETMTPVQQKTLKPILsTGDDVLARAKTGTGKTLAFLLPAIQSlLNTKPAgrRSGVSALIISPTRELALQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 187 LK-FTKELGRYTGLKTALILGGDKMEDQFAALH-ENPDIIIATPGRLM-HVAIEMKLK-LQSVEYVVFDEADRLFEMGFA 262
Cdd:cd17964 85 AAeAKKLLQGLRKLRVQSAVGGTSRRAELNRLRrGRPDILVATPGRLIdHLENPGVAKaFTDLDYLVLDEADRLLDMGFR 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 1622179293 263 EQLQEIISRLPEN----RQTVLFSATLPKLLVEFARAGL 297
Cdd:cd17964 165 PDLEQILRHLPEKnadpRQTLLFSATVPDEVQQIARLTL 203
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
102-446 |
4.64e-50 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 184.99 E-value: 4.64e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 102 FQSMGLGYPVFKGIMKKGYKIPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLIPMFEKL-KVHSAKTGAR----ALIL 176
Cdd:PLN00206 123 FSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCcTIRSGHPSEQrnplAMVL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 177 SPTRELALQTLKFTKELGRYTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLMHVAIEMKLKLQSVEYVVFDEADRL 256
Cdd:PLN00206 203 TPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCM 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 257 FEMGFAEQLQEIISRLPENrQTVLFSATLPKLLVEFARAGLTEPVLIRLDVESKLSEQLKLSFYHVRADDKPALLLYLLR 336
Cdd:PLN00206 283 LERGFRDQVMQIFQALSQP-QVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKKQKLFDILK 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 337 TVVRPQDQTIVFVATKHHTEYLKELLT-AQGVNCTHVYSSLDQTARKINVGKFIHGKCSVLIVTDLAARGIDIPLLDNVI 415
Cdd:PLN00206 362 SKQHFKPPAVVFVSSRLGADLLANAITvVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVI 441
|
330 340 350
....*....|....*....|....*....|.
gi 1622179293 416 NYSFPAKAKLFLHRVGRVARAGRSGTAYSLV 446
Cdd:PLN00206 442 IFDMPNTIKEYIHQIGRASRMGEKGTAIVFV 472
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
111-303 |
7.43e-48 |
|
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: 169.06 E-value: 7.43e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 111 VFKGIMKKGYKIPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLIPMF------EKLKVHSAKTGARALILSPTRELAL 184
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLImfaleqEKKLPFIKGEGPYGLIVCPSRELAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 185 QTLK----FTKEL--GRYTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLMHVAIEMKLKLQSVEYVVFDEADRLFE 258
Cdd:cd17951 81 QTHEvieyYCKALqeGGYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622179293 259 MGFAEQLQEIISRLPENRQTVLFSATLPKLLVEFARAGLTEPVLI 303
Cdd:cd17951 161 MGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
105-303 |
8.81e-48 |
|
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: 168.66 E-value: 8.81e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 105 MGLGYPVFKGIMKKGYKIPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLIPMFEKLKVHSAKTgaRALILSPTRELAL 184
Cdd:cd17939 2 MGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRET--QALVLAPTRELAQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 185 QTLKFTKELGRYTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLMHVAIEMKLKLQSVEYVVFDEADRLFEMGFAEQ 264
Cdd:cd17939 80 QIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQ 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 1622179293 265 LQEIISRLPENRQTVLFSATLPKLLVEFARAGLTEPVLI 303
Cdd:cd17939 160 IYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
111-303 |
2.66e-47 |
|
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: 167.16 E-value: 2.66e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 111 VFKGIMKKGYKIPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLIPMFeklkVHSAKT-------GARALILSPTRELA 183
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAI----VHINAQpplergdGPIVLVLAPTRELA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 184 LQTLKFTKELGRYTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLMHVAIEMKLKLQSVEYVVFDEADRLFEMGFAE 263
Cdd:cd17966 77 QQIQQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1622179293 264 QLQEIISRLPENRQTVLFSATLPKLLVEFARAGLTEPVLI 303
Cdd:cd17966 157 QIRKIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
115-303 |
1.71e-46 |
|
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: 164.64 E-value: 1.71e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 115 IMKKGYKIPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLIPMFekLKVHSAKTGARALILSPTRELALQTLKFTKELG 194
Cdd:cd17962 5 LKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVI--IRCLTEHRNPSALILTPTRELAVQIEDQAKELM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 195 R-YTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLMHVAIEMKLKLQSVEYVVFDEADRLFEMGFAEQLQEIISRLP 273
Cdd:cd17962 83 KgLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILENIS 162
|
170 180 190
....*....|....*....|....*....|
gi 1622179293 274 ENRQTVLFSATLPKLLVEFARAGLTEPVLI 303
Cdd:cd17962 163 HDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
111-285 |
2.20e-46 |
|
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: 165.88 E-value: 2.20e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 111 VFKGIMKKGYKIPTPIQRKTIPV-ILDGKDVVAMARTGSGKTACFLIPMFEKL-------KVHSAKTGARALILSPTREL 182
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAaIRDGKDVIGAAETGSGKTLAFGIPILERLlsqkssnGVGGKQKPLRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 183 ALQTLKFTKELGRYTGLKTALILGGDKMEDQFAALHENPDIIIATPGRL---MHVAIEMKLKLQSVEYVVFDEADRLFEM 259
Cdd:cd17946 81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLwelIQEGNEHLANLKSLRFLVLDEADRMLEK 160
|
170 180 190
....*....|....*....|....*....|...
gi 1622179293 260 GFAEQLQEIISRLPEN-------RQTVLFSATL 285
Cdd:cd17946 161 GHFAELEKILELLNKDragkkrkRQTFVFSATL 193
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
315-446 |
2.27e-45 |
|
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: 159.21 E-value: 2.27e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 315 LKLSFYHVRADDKPALLLYLLRTVvRPQDQTIVFVATKHHTEYLKELLTAQGVNCTHVYSSLDQTARKINVGKFIHGKCS 394
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLLLLLLEK-LKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVR 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1622179293 395 VLIVTDLAARGIDIPLLDNVINYSFPAKAKLFLHRVGRVARAGRSGTAYSLV 446
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 ... |
113-303 |
1.17e-44 |
|
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein and is activated by Myc protein. DDX18 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350700 [Multi-domain] Cd Length: 198 Bit Score: 159.83 E-value: 1.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 113 KGIMKKGYKIPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLIPMFE---KLKVhSAKTGARALILSPTRELALQTLKF 189
Cdd:cd17942 3 KAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIEllyKLKF-KPRNGTGVIIISPTRELALQIYGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 190 TKELGRYTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLM-HVAIEMKLKLQSVEYVVFDEADRLFEMGFAEQLQEI 268
Cdd:cd17942 82 AKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLdHLQNTKGFLYKNLQCLIIDEADRILEIGFEEEMRQI 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 1622179293 269 ISRLPENRQTVLFSATLPKLLVEFARAGL-TEPVLI 303
Cdd:cd17942 162 IKLLPKRRQTMLFSATQTRKVEDLARISLkKKPLYV 197
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
111-303 |
2.63e-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: 155.70 E-value: 2.63e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 111 VFKGIMKKGYKIPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLIPMFEKLKVHSA----KTGARALILSPTRELALQT 186
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIpreqRNGPGVLVLTPTRELALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 187 -LKFTKELgrYTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLMHVAIEMKLKLQSVEYVVFDEADRLFEMGFAEQL 265
Cdd:cd17958 81 eAECSKYS--YKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQI 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 1622179293 266 QEIISRLPENRQTVLFSATLPKLLVEFARAGLTEPVLI 303
Cdd:cd17958 159 RKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
102-292 |
5.42e-43 |
|
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: 157.44 E-value: 5.42e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 102 FQSMGLGYPVFKGIMKKGYKIPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLIPMFEKLkVHSAKTGAR--------A 173
Cdd:cd18052 45 FEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGM-MKEGLTASSfsevqepqA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 174 LILSPTRELALQTLKFTKELGRYTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLMHVAIEMKLKLQSVEYVVFDEA 253
Cdd:cd18052 124 LIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEA 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1622179293 254 DRLFEMGFAEQLQEIISRL----PENRQTVLFSATLP----KLLVEF 292
Cdd:cd18052 204 DRMLDMGFGPEIRKLVSEPgmpsKEDRQTLMFSATFPeeiqRLAAEF 250
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
119-304 |
1.05e-42 |
|
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: 154.67 E-value: 1.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 119 GYKIPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLIPMFEKLKVHSAK----TGARALILSPTRELALQTLK-FTKEL 193
Cdd:cd17949 10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRvdrsDGTLALVLVPTRELALQIYEvLEKLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 194 GRYTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLM-HVAIEMKLKLQSVEYVVFDEADRLFEMGFAEQLQEIISRL 272
Cdd:cd17949 90 KPFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLdHLKNTQSFDVSNLRWLVLDEADRLLDMGFEKDITKILELL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622179293 273 -------------PENRQTVLFSATLPKLLVEFARAGLTEPVLIR 304
Cdd:cd17949 170 ddkrskaggekskPSRRQTVLVSATLTDGVKRLAGLSLKDPVYID 214
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
102-285 |
1.75e-42 |
|
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: 153.63 E-value: 1.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 102 FQSMGLGYPVFKGIMKKGYKIPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLIPMFEKLkvhsaktgaRALILSPTRE 181
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIV---------VALILEPSRE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 182 LALQTL----KFTKELGRYTgLKTALILGGDKMEDQFAALHENPDIIIATPGRLMHVAIEMKLKLQSVEYVVFDEADRLF 257
Cdd:cd17938 72 LAEQTYncieNFKKYLDNPK-LRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLL 150
|
170 180 190
....*....|....*....|....*....|....
gi 1622179293 258 EMGFAEQLQEIISRLP-----ENR-QTVLFSATL 285
Cdd:cd17938 151 SQGNLETINRIYNRIPkitsdGKRlQVIVCSATL 184
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
111-304 |
2.89e-41 |
|
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: 149.72 E-value: 2.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 111 VFKGIMKKGYKIPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLIPMFEKLKVHSAKTgaRALILSPTRELALQTLKFT 190
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHP--QVLILAPTREIAVQIHDVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 191 KELGRY-TGLKTALILGGDKMEDQFAALhENPDIIIATPGRLMHVAIEMKLKLQSVEYVVFDEADRLFEMGFAEQLQEII 269
Cdd:cd17943 79 KKIGKKlEGLKCEVFIGGTPVKEDKKKL-KGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIF 157
|
170 180 190
....*....|....*....|....*....|....*
gi 1622179293 270 SRLPENRQTVLFSATLPKLLVEFARAGLTEPVLIR 304
Cdd:cd17943 158 SSLPKNKQVIAFSATYPKNLDNLLARYMRKPVLVR 192
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
102-294 |
3.32e-39 |
|
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: 145.95 E-value: 3.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 102 FQSMGLGYPVFKGIMKKGYKIPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLIP----MFEKLKVHSAKTGAR----- 172
Cdd:cd18051 23 FSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPilsqIYEQGPGESLPSESGyygrr 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 173 -----ALILSPTRELALQTLKFTKELGRYTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLMHVAIEMKLKLQSVEY 247
Cdd:cd18051 103 kqyplALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLDYCKY 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622179293 248 VVFDEADRLFEMGFAEQLQEIISR--LPE--NRQTVLFSATLPKLLVEFAR 294
Cdd:cd18051 183 LVLDEADRMLDMGFEPQIRRIVEQdtMPPtgERQTLMFSATFPKEIQMLAR 233
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
102-303 |
5.41e-39 |
|
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: 143.74 E-value: 5.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 102 FQSMGLGYPVFKGIMKKGYKIPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLIPMFEKLKVHSAKTgaRALILSPTRE 181
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKAT--QALVLAPTRE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 182 LALQTLKFTKELGRYTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLMHVAIEMKLKLQSVEYVVFDEADRLFEMGF 261
Cdd:cd18046 79 LAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGF 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622179293 262 AEQLQEIISRLPENRQTVLFSATLPKLLVEFARAGLTEPVLI 303
Cdd:cd18046 159 KDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
107-304 |
1.39e-38 |
|
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: 142.33 E-value: 1.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 107 LGYPVFKGIMKKGYKIPTPIQRKTIPVILDG--KDVVAMARTGSGKTACFLIPMFEKLKVHSAKTgaRALILSPTRELAL 184
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSP--QALCLAPTRELAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 185 QTLKFTKELGRYTGLKTALIL------GGDKMEDQfaalhenpdIIIATPGRLMHVAIEMKLKLQSVEYVVFDEADRLFE 258
Cdd:cd17963 79 QIGEVVEKMGKFTGVKVALAVpgndvpRGKKITAQ---------IVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLD 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1622179293 259 M-GFAEQLQEIISRLPENRQTVLFSATLPKLLVEFARAGLTEPVLIR 304
Cdd:cd17963 150 TqGHGDQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTIK 196
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
102-303 |
9.28e-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: 139.91 E-value: 9.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 102 FQSMGLGYPVFKGIMKKGYKIPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLIPMFEKLKVHSAKTgaRALILSPTRE 181
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRET--QALILSPTRE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 182 LALQTLKFTKELGRYTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLMHVAIEMKLKLQSVEYVVFDEADRLFEMGF 261
Cdd:cd18045 79 LAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGF 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622179293 262 AEQLQEIISRLPENRQTVLFSATLPKLLVEFARAGLTEPVLI 303
Cdd:cd18045 159 KEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
115-305 |
2.81e-37 |
|
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: 139.76 E-value: 2.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 115 IMKKGYKIPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLIPMFeklkVH-------SAKTGARALILSPTRELALQTL 187
Cdd:cd18049 39 IARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAI----VHinhqpflERGDGPICLVLAPTRELAQQVQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 188 KFTKELGRYTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLMHVAIEMKLKLQSVEYVVFDEADRLFEMGFAEQLQE 267
Cdd:cd18049 115 QVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRK 194
|
170 180 190
....*....|....*....|....*....|....*...
gi 1622179293 268 IISRLPENRQTVLFSATLPKLLVEFARAGLTEPVLIRL 305
Cdd:cd18049 195 IVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINI 232
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
117-287 |
1.24e-35 |
|
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: 135.19 E-value: 1.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 117 KKGYKIPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLIPMFEKL--KVHSAKTG---ARALILSPTRELALQTLKFTK 191
Cdd:cd17948 7 RQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLlrYKLLAEGPfnaPRGLVITPSRELAEQIGSVAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 192 ELGRYTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLMHVAIEMKLKLQSVEYVVFDEADRLFEMGFAEQLQEIISR 271
Cdd:cd17948 87 SLTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKLSHFLRR 166
|
170 180
....*....|....*....|....*....
gi 1622179293 272 LP--ENR-----------QTVLFSATLPK 287
Cdd:cd17948 167 FPlaSRRsentdgldpgtQLVLVSATMPS 195
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
125-294 |
2.72e-35 |
|
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: 133.05 E-value: 2.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 125 PIQRKTIPVILDGKDVVAMARTGSGKTACFLIPMFEKLKVHSAKT----GARALILSPTRELALQTLKFTKELGRytGLK 200
Cdd:cd17944 15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRkrgrAPKVLVLAPTRELANQVTKDFKDITR--KLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 201 TALILGGDKMEDQFAALHENPDIIIATPGRLMHVAIEMKLKLQSVEYVVFDEADRLFEMGFAEQLQEIISRL-----PEN 275
Cdd:cd17944 93 VACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILSVSykkdsEDN 172
|
170
....*....|....*....
gi 1622179293 276 RQTVLFSATLPKLLVEFAR 294
Cdd:cd17944 173 PQTLLFSATCPDWVYNVAK 191
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
101-305 |
4.96e-34 |
|
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: 131.67 E-value: 4.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 101 GFQSMGLGYPVFKGIMKKGYKIPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLIPMFEKLKVH---SAKTGARALILS 177
Cdd:cd18050 63 AFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQpylERGDGPICLVLA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 178 PTRELALQTLKFTKELGRYTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLMHVAIEMKLKLQSVEYVVFDEADRLF 257
Cdd:cd18050 143 PTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRML 222
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1622179293 258 EMGFAEQLQEIISRLPENRQTVLFSATLPKLLVEFARAGLTEPVLIRL 305
Cdd:cd18050 223 DMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQINI 270
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
99-287 |
1.61e-32 |
|
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: 125.15 E-value: 1.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 99 SGGFQSMGLGYPVFKGIMKKGYKIPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLIPMFEKLKVHSAKTgaRALILSP 178
Cdd:cd17950 1 SSGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQV--SVLVICH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 179 TRELALQTLKFTKELGRY-TGLKTALILGGDKMEDQFAALHEN-PDIIIATPGRLMHVAIEMKLKLQSVEYVVFDEADRL 256
Cdd:cd17950 79 TRELAFQISNEYERFSKYmPNVKTAVFFGGVPIKKDIEVLKNKcPHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKM 158
|
170 180 190
....*....|....*....|....*....|..
gi 1622179293 257 FE-MGFAEQLQEIISRLPENRQTVLFSATLPK 287
Cdd:cd17950 159 LEqLDMRRDVQEIFRATPHDKQVMMFSATLSK 190
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
117-285 |
2.93e-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: 113.88 E-value: 2.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 117 KKGYKIPTPIQRKTIPVILDG---------KDVVAMARTGSGKTACFLIPMFEKLKvHSAKTGARALILSPTRELALQTL 187
Cdd:cd17956 7 NNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQALS-KRVVPRLRALIVVPTKELVQQVY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 188 KFTKELGRYTGLKTALiLGGDK---------MEDQFAALHENPDIIIATPGRLM-HVAIEMKLKLQSVEYVVFDEADRLF 257
Cdd:cd17956 86 KVFESLCKGTGLKVVS-LSGQKsfkkeqkllLVDTSGRYLSRVDILVATPGRLVdHLNSTPGFTLKHLRFLVIDEADRLL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1622179293 258 EMGFAE--------------------QLQEIISRLPENRQTVLFSATL 285
Cdd:cd17956 165 NQSFQDwletvmkalgrptapdlgsfGDANLLERSVRPLQKLLFSATL 212
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
326-437 |
2.18e-25 |
|
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: 101.13 E-value: 2.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 326 DKPALLLYLLRTvvRPQDQTIVFVATKHHTEyLKELLTAQGVNCTHVYSSLDQTARKINVGKFIHGKCSVLIVTDLAARG 405
Cdd:pfam00271 1 EKLEALLELLKK--ERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERG 77
|
90 100 110
....*....|....*....|....*....|..
gi 1622179293 406 IDIPLLDNVINYSFPAKAKLFLHRVGRVARAG 437
Cdd:pfam00271 78 LDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
102-308 |
2.19e-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: 102.41 E-value: 2.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 102 FQSMGLGYPVFKGIMKKGYKIPTPIQRKTIPVILDG--KDVVAMARTGSGKTACFLIPMFEKlkVHSAKTGARALILSPT 179
Cdd:cd18048 20 FEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSR--VDALKLYPQCLCLSPT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 180 RELALQTLKFTKELGRY-TGLKTALILGGDK------MEDQfaalhenpdIIIATPGRLMHVAIEMKL-KLQSVEYVVFD 251
Cdd:cd18048 98 FELALQTGKVVEEMGKFcVGIQVIYAIRGNRpgkgtdIEAQ---------IVIGTPGTVLDWCFKLRLiDVTNISVFVLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622179293 252 EADRLFEM-GFAEQLQEIISRLPENRQTVLFSATLPKLLVEFARAGLTEPVLIRLDVE 308
Cdd:cd18048 169 EADVMINVqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKE 226
|
|
| DBP10CT |
pfam08147 |
DBP10CT (NUC160) domain; This C terminal domain is found in the Dbp10p subfamily of ... |
709-769 |
7.74e-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: 92.35 E-value: 7.74e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622179293 709 DLMGDENRNMSNSKQLLK---WDRKRKRFVGQTGQE--NKKKIRTESGAYISSSYKGNLYDKWKKK 769
Cdd:pfam08147 1 DLTGDDGQELNQQKQVQKkmrWDKKKKKFVKRSGNDedGKKKIRTESGVKIPASYKSGRYDEWKKK 66
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
140-608 |
3.04e-22 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 102.03 E-value: 3.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 140 VVAMArTGSGKT--ACFLIpmfeklkvHSAKTGARALILSPTRELALQTLkftKELGRYTGLKtalILGGDKMEDQFaal 217
Cdd:COG1061 104 LVVAP-TGTGKTvlALALA--------AELLRGKRVLVLVPRRELLEQWA---EELRRFLGDP---LAGGGKKDSDA--- 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 218 henpDIIIATPGRLMHVAIEMKLKlQSVEYVVFDEADRLfemgFAEQLQEIISRLPENRqTVLFSAT------LPKLLVE 291
Cdd:COG1061 166 ----PITVATYQSLARRAHLDELG-DRFGLVIIDEAHHA----GAPSYRRILEAFPAAY-RLGLTATpfrsdgREILLFL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 292 F------------ARAG-LTEPVLIRLDVE--------SKLSEQL--KLSFYHVRADDKpalllylLRTVVR---PQDQT 345
Cdd:COG1061 236 FdgivyeyslkeaIEDGyLAPPEYYGIRVDltderaeyDALSERLreALAADAERKDKI-------LRELLRehpDDRKT 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 346 IVFVATKHHTEYLKELLTAQGVNCTHVYSSLDQTARKINVGKFIHGKCSVLIVTDLAARGIDIPLLDNVINYSfPAKAK- 424
Cdd:COG1061 309 LVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLR-PTGSPr 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 425 LFLHRVGRVARAGRSGTA---YSLVAPDetpyVFDLHLFLGRPLILANPHEKPTDtdgifgrvPQSIIDDEESLLQTDHE 501
Cdd:COG1061 388 EFIQRLGRGLRPAPGKEDalvYDFVGND----VPVLEELAKDLRDLAGYRVEFLD--------EEESEELALLIAVKPAL 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 502 RSLDLQSLRRVSDNAQKQYLKSRPAPSPESIKRVKEMDFTLLGIHPLFSLRFEGEEMERLKFVDSIKSYRSKATIFEINA 581
Cdd:COG1061 456 EVKGELEEELLEELELLEDALLLVLAELLLLELLALALELLELAKAEGKAEEEEEEKELLLLLALAKLLKLLLLLLLLLL 535
|
490 500
....*....|....*....|....*..
gi 1622179293 582 TNKTLASDVMRAKRNRDRQLIDRHQRK 608
Cdd:COG1061 536 LELLELLAALLRLEELAALLLKELLRA 562
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
119-287 |
3.21e-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: 96.68 E-value: 3.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 119 GYKIPTPIQRKTIPVIL------------DGKD-----VVAmARTGSGKTACFLIPMFEKLKVHSAKTG----------- 170
Cdd:cd17965 27 EEIKPSPIQTLAIKKLLktlmrkvtkqtsNEEPklevfLLA-AETGSGKTLAYLAPLLDYLKRQEQEPFeeaeeeyesak 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 171 ----ARALILSPTRELALQTLKFTKELGRYTGLKTALILG--GDKMEDQFAALHENPDIIIATPGRLMHVA-IEMKLkLQ 243
Cdd:cd17965 106 dtgrPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSgfGPSYQRLQLAFKGRIDILVTTPGKLASLAkSRPKI-LS 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1622179293 244 SVEYVVFDEADRLFEMGFAEQLQEIISRLPENRQTVLFSATLPK 287
Cdd:cd17965 185 RVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPK 228
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
127-502 |
1.34e-21 |
|
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: 100.68 E-value: 1.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 127 QRKTIPVILDGKDVVAMARTGSGKTACFLIPMFEKLkvhSAKTGARALILSPTRELA---LQTL-KFTKELGRytGLKTA 202
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEAL---LEDPGATALYLYPTKALArdqLRRLrELAEALGL--GVRVA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 203 lILGGDKMEDQFAALHENPDIIIATPGRLmHVAIemkLK--------LQSVEYVVFDEA---------------DRlfem 259
Cdd:COG1205 136 -TYDGDTPPEERRWIREHPDIVLTNPDML-HYGL---LPhhtrwarfFRNLRYVVIDEAhtyrgvfgshvanvlRR---- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 260 gfaeqLQEIISRLPENRQTVLFSATL--PKllvEFARAgLT-EPVLIrldVESKLSEQLKLSFYHV------RADDKPAL 330
Cdd:COG1205 207 -----LRRICRHYGSDPQFILASATIgnPA---EHAER-LTgRPVTV---VDEDGSPRGERTFVLWnpplvdDGIRRSAL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 331 LL--YLLRTVVRPQDQTIVFVATKHHTE----YLKELLTAQGV-NCTHVYSS--LDQTARKINvGKFIHGKCSVLIVT-- 399
Cdd:COG1205 275 AEaaRLLADLVREGLRTLVFTRSRRGAEllarYARRALREPDLaDRVAAYRAgyLPEERREIE-RGLRSGELLGVVSTna 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 400 -DLaarGIDIPLLDNVINYSFPAKAKLFLHRVGRVARAGRSGTAYsLVApDETP---YVFDlH--LFLGR---------- 463
Cdd:COG1205 354 lEL---GIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVV-LVA-GDDPldqYYVR-HpeELFERppeaavidpd 427
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1622179293 464 -PLILAnPH------EKP-TDTD-GIFGRVPQSIIDD--EESLLQTDHER 502
Cdd:COG1205 428 nPYVLA-PHllcaaaELPlTEGDlELFGPEARELLDAlvEEGLLRRRGDG 476
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
102-304 |
1.62e-21 |
|
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: 93.63 E-value: 1.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 102 FQSMGLGYPVFKGIMKKGYKIPTPIQRKTIPVIL--DGKDVVAMARTGSGKTACFLIPMFEKlkVHSAKTGARALILSPT 179
Cdd:cd18047 3 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLaePPQNLIAQSQSGTGKTAAFVLAMLSQ--VEPANKYPQCLCLSPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 180 RELALQTLKFTKELGR-YTGLKTALILGGDKMEdqfAALHENPDIIIATPGRLMHVAIEMKL-KLQSVEYVVFDEADRLF 257
Cdd:cd18047 81 YELALQTGKVIEQMGKfYPELKLAYAVRGNKLE---RGQKISEQIVIGTPGTVLDWCSKLKFiDPKKIKVFVLDEADVMI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1622179293 258 -EMGFAEQLQEIISRLPENRQTVLFSATLPKLLVEFARAGLTEPVLIR 304
Cdd:cd18047 158 aTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 205
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
356-437 |
6.40e-19 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 81.87 E-value: 6.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 356 EYLKELLTAQGVNCTHVYSSLDQTARKINVGKFIHGKCSVLIVTDLAARGIDIPLLDNVINYSFPAKAKLFLHRVGRVAR 435
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 1622179293 436 AG 437
Cdd:smart00490 81 AG 82
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
137-284 |
2.94e-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: 2.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 137 GKDVVAMARTGSGKTACFLIPMFEklkvHSAKTGARALILSPTRELALQTLKFTKELGRYtGLKTALILGGDKMEDQFAA 216
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALL----LLLKKGKKVLVLVPTKALALQTAERLRELFGP-GIRVAVLVGGSSAEEREKN 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622179293 217 LHENPDIIIATPGRL-MHVAIEMKLKLQSVEYVVFDEADRLFEMGFAEQL--QEIISRLPENRQTVLFSAT 284
Cdd:cd00046 76 KLGDADIIIATPDMLlNLLLREDRLFLKDLKLIIVDEAHALLIDSRGALIldLAVRKAGLKNAQVILLSAT 146
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
127-294 |
2.30e-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: 78.01 E-value: 2.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 127 QRKTIPVILDGKDVVAMARTGSGKTACFLIPMFEKLkvhSAKTGARALILSPTRELALQTLKFTKELGRYTGLK-TALIL 205
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEAL---LRDPGSRALYLYPTKALAQDQLRSLRELLEQLGLGiRVATY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 206 GGD-KMEDQFAALHENPDIIIATPGRLmHVAIemkLK--------LQSVEYVVFDEA---DRLFEMGFA---EQLQEIIS 270
Cdd:cd17923 82 DGDtPREERRAIIRNPPRILLTNPDML-HYAL---LPhhdrwarfLRNLRYVVLDEAhtyRGVFGSHVAlllRRLRRLCR 157
|
170 180
....*....|....*....|....
gi 1622179293 271 RLPENRQTVLFSATLpKLLVEFAR 294
Cdd:cd17923 158 RYGADPQFILTSATI-GNPAEHAR 180
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
124-286 |
1.61e-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: 75.38 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 124 TPIQRKTI-PVILDGKDVVAMARTGSGKTACFLIPMFEKLkvhsAKTGARALILSPTRELALQTLK-FTKELGRYtGLKT 201
Cdd:cd17921 3 NPIQREALrALYLSGDSVLVSAPTSSGKTLIAELAILRAL----ATSGGKAVYIAPTRALVNQKEAdLRERFGPL-GKNV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 202 ALILGGDKMEDQFAAlheNPDIIIATPGRLmhvaiEMKL------KLQSVEYVVFDEADRLFEMGFAEQLQEIISRLP-- 273
Cdd:cd17921 78 GLLTGDPSVNKLLLA---EADILVATPEKL-----DLLLrnggerLIQDVRLVVVDEAHLIGDGERGVVLELLLSRLLri 149
|
170
....*....|....
gi 1622179293 274 -ENRQTVLFSATLP 286
Cdd:cd17921 150 nKNARFVGLSATLP 163
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
117-406 |
6.81e-13 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 72.24 E-value: 6.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 117 KKGYKIPTPIQRKTIP-VILDGKDVVAMARTGSGKTACFLIPMfeklkVHSAKTGARALILSPTRELALQ-TLKFTKELG 194
Cdd:COG1204 17 ERGIEELYPPQAEALEaGLLEGKNLVVSAPTASGKTLIAELAI-----LKALLNGGKALYIVPLRALASEkYREFKRDFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 195 RYtGLKTALILGGDKMEDQFAalhENPDIIIATPGR---LMHVAIEMklkLQSVEYVVFDEA------DRlfemGFaeQL 265
Cdd:COG1204 92 EL-GIKVGVSTGDYDSDDEWL---GRYDILVATPEKldsLLRNGPSW---LRDVDLVVVDEAhliddeSR----GP--TL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 266 QEIISRL---PENRQTVLFSATLPKlLVEFAR---AGLTE----PVLIRLDVesklseqlklsFYH--VRADDKPAL--- 330
Cdd:COG1204 159 EVLLARLrrlNPEAQIVALSATIGN-AEEIAEwldAELVKsdwrPVPLNEGV-----------LYDgvLRFDDGSRRskd 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 331 -LLYLLRTVVRPQDQTIVFVATKHHTE-YLKELLTAQGVNCTHVYSS-LDQTARKI-NVGKFIHgKCSVLIvtDLAARGI 406
Cdd:COG1204 227 pTLALALDLLEEGGQVLVFVSSRRDAEsLAKKLADELKRRLTPEEREeLEELAEELlEVSEETH-TNEKLA--DCLEKGV 303
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
140-285 |
7.54e-10 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 58.09 E-value: 7.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 140 VVAMArTGSGKTACfLIPMFEKLKVHsaktgaRALILSPTRELALQTLKftkELGRYTGLKTALILGGDKMEDQFAAlhe 219
Cdd:cd17926 22 ILVLP-TGSGKTLT-ALALIAYLKEL------RTLIVVPTDALLDQWKE---RFEDFLGDSSIGLIGGGKKKDFDDA--- 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622179293 220 npDIIIATPGRLMHVAIEMKLKLQSVEYVVFDEADRLfemgFAEQLQEIISRLPENRQtVLFSATL 285
Cdd:cd17926 88 --NVVVATYQSLSNLAEEEKDLFDQFGLLIVDEAHHL----PAKTFSEILKELNAKYR-LGLTATP 146
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
108-399 |
8.69e-10 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 62.08 E-value: 8.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 108 GYPVFKgimkkgykiptPIQRKTIPVILDGKDVVAMARTGSGKTACFLIP--MFEKLkvhsaktgarALILSPtreL--- 182
Cdd:COG0514 14 GYDSFR-----------PGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPalLLPGL----------TLVVSP---Lial 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 183 ------ALQTLkftkelgrytGLKTALI---LGGDKMEDQFAALHEN-PDIIIATPGRLMHVAIEMKLKLQSVEYVVFDE 252
Cdd:COG0514 70 mkdqvdALRAA----------GIRAAFLnssLSAEERREVLRALRAGeLKLLYVAPERLLNPRFLELLRRLKISLFAIDE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 253 A------------DRLfemgfaeQLQEIISRLPeNRQTVLFSATlpkllvefAraglTEPVliRLDVESKLS----EQLK 316
Cdd:COG0514 140 AhcisqwghdfrpDYR-------RLGELRERLP-NVPVLALTAT--------A----TPRV--RADIAEQLGledpRVFV 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 317 LSF------YHVR---ADDKPALLLYLLRTvvRPQDQTIVFVATKHHTEYLKELLTAQGVNCTHVYSSLDQTARKINVGK 387
Cdd:COG0514 198 GSFdrpnlrLEVVpkpPDDKLAQLLDFLKE--HPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDR 275
|
330
....*....|..
gi 1622179293 388 FIHGKCSVLIVT 399
Cdd:COG0514 276 FLRDEVDVIVAT 287
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
117-432 |
1.25e-09 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 62.21 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 117 KKGYKIPTPIQRKTIPVILDGKDVVAMARTGSGKT-ACFLI---PMFEKLKVHSAKTGARALILSPTRELA-------LQ 185
Cdd:PRK13767 27 KEKFGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAFLAiidELFRLGREGELEDKVYCLYVSPLRALNndihrnlEE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 186 TLKFTKELGRYTGLKTALI----LGGD-------KMedqfaaLHENPDIIIATPGRLmhvAI-----EMKLKLQSVEYVV 249
Cdd:PRK13767 107 PLTEIREIAKERGEELPEIrvaiRTGDtssyekqKM------LKKPPHILITTPESL---AIllnspKFREKLRTVKWVI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 250 FDEADRLFE-------MGFAEQLQEIISRLPenrQTVLFSATL-P-----KLLVEFARAGLTEPVLIrldVESKLSEQLK 316
Cdd:PRK13767 178 VDEIHSLAEnkrgvhlSLSLERLEELAGGEF---VRIGLSATIePleevaKFLVGYEDDGEPRDCEI---VDARFVKPFD 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 317 LS-------FYHVRADDKPALLLYLLRTVVRPQDQTIVFVATKHHTE----YLKELL----TAQGVNCTHvySSLDQTAR 381
Cdd:PRK13767 252 IKvispvddLIHTPAEEISEALYETLHELIKEHRTTLIFTNTRSGAErvlyNLRKRFpeeyDEDNIGAHH--SSLSREVR 329
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622179293 382 -----KINVGKFihgKCsVLIVTDLAArGIDIPLLDNVINYSFPAKAKLFLHRVGR 432
Cdd:PRK13767 330 leveeKLKRGEL---KV-VVSSTSLEL-GIDIGYIDLVVLLGSPKSVSRLLQRIGR 380
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
319-440 |
1.18e-08 |
|
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: 54.14 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 319 FYHVRADDKPALLLYLLRTVVR--PQDQTIVFVATKHHTEYLKELLTAQGVNCTHVYSSLDQTARKINVGKFIHGKCSVL 396
Cdd:cd18794 5 FYSVRPKDKKDEKLDLLKRIKVehLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVI 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1622179293 397 IVTDLAARGIDIPLLDNVINYSFPAKAKLFLHRVGrvaRAGRSG 440
Cdd:cd18794 85 VATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESG---RAGRDG 125
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
125-286 |
3.53e-08 |
|
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: 53.88 E-value: 3.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 125 PIQRKTI-PVILDGKDVVAMARTGSGKTACFLIPMfeklkVHSAKTGARALILSPTRELALQTLKFTKELGRYtGLKTAL 203
Cdd:cd18028 4 PPQAEAVrAGLLKGENLLISIPTASGKTLIAEMAM-----VNTLLEGGKALYLVPLRALASEKYEEFKKLEEI-GLKVGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 204 ILGGDKMEDQFaaLHENpDIIIATPGRLMHVAIEMKLKLQSVEYVVFDEADRLFEMGFAEQLQEIISRLPE---NRQTVL 280
Cdd:cd18028 78 STGDYDEDDEW--LGDY-DIIVATYEKFDSLLRHSPSWLRDVGVVVVDEIHLISDEERGPTLESIVARLRRlnpNTQIIG 154
|
....*.
gi 1622179293 281 FSATLP 286
Cdd:cd18028 155 LSATIG 160
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
138-253 |
5.07e-08 |
|
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: 54.19 E-value: 5.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 138 KDVVAMARTGSGKT--ACFLIPMFEKLKVHSAKTGARALILSPTRELALQTlkfTKELGRYTGLKTAlILGGDKMEDQFA 215
Cdd:cd18034 17 RNTIVVLPTGSGKTliAVMLIKEMGELNRKEKNPKKRAVFLVPTVPLVAQQ---AEAIRSHTDLKVG-EYSGEMGVDKWT 92
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1622179293 216 ALH-----ENPDIIIATPGRLMHVAIEMKLKLQSVEYVVFDEA 253
Cdd:cd18034 93 KERwkeelEKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
146-255 |
9.09e-08 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 56.04 E-value: 9.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 146 TGSGKTACFLIPMFEKLKvhsaKTGARALILSPTRELALQTLKFTKELGRYTGLKTALILGGDKMEDQfAALHENPDIII 225
Cdd:PRK13766 38 TGLGKTAIALLVIAERLH----KKGGKVLILAPTKPLVEQHAEFFRKFLNIPEEKIVVFTGEVSPEKR-AELWEKAKVIV 112
|
90 100 110
....*....|....*....|....*....|....
gi 1622179293 226 ATPgrlmHVA----IEMKLKLQSVEYVVFDEADR 255
Cdd:PRK13766 113 ATP----QVIendlIAGRISLEDVSLLIFDEAHR 142
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
126-228 |
9.94e-08 |
|
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: 53.13 E-value: 9.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 126 IQRKTIPVILDG-KDVVAMARTGSGKTACFLIPMFEKLK--VHSAKTGARALILSPTRELALQTLKFTKE-LGRYtGLKT 201
Cdd:cd18023 5 IQSEVFPDLLYSdKNFVVSAPTGSGKTVLFELAILRLLKerNPLPWGNRKVVYIAPIKALCSEKYDDWKEkFGPL-GLSC 83
|
90 100
....*....|....*....|....*..
gi 1622179293 202 ALILGGDKMEDQFAAlhENPDIIIATP 228
Cdd:cd18023 84 AELTGDTEMDDTFEI--QDADIILTTP 108
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
128-284 |
3.21e-07 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 50.75 E-value: 3.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 128 RKTIPVILDGKD--VVAMArTGSGKTACFLIPMFEKLKVHSAKtgaRALILSPTRELALQTLK-FTKELGRYTGLKTalI 204
Cdd:pfam04851 13 ENLLESIKNGQKrgLIVMA-TGSGKTLTAAKLIARLFKKGPIK---KVLFLVPRKDLLEQALEeFKKFLPNYVEIGE--I 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 205 LGGDKMEDQFaalhENPDIIIATPGRLmHVAIEMKLKLQSVE---YVVFDEADRLfemgFAEQLQEIISRLPENRQtVLF 281
Cdd:pfam04851 87 ISGDKKDESV----DDNKIVVTTIQSL-YKALELASLELLPDffdVIIIDEAHRS----GASSYRNILEYFKPAFL-LGL 156
|
...
gi 1622179293 282 SAT 284
Cdd:pfam04851 157 TAT 159
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
123-255 |
4.37e-07 |
|
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350676 [Multi-domain] Cd Length: 180 Bit Score: 50.88 E-value: 4.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 123 PTPIQRKTIPVIL-DGKDVVAMAR-----TGSGKTACFLIPMFeklkvHSAKTGARALILSPTRELALQTLKFTKElgRY 196
Cdd:cd17918 16 LTKDQAQAIKDIEkDLHSPEPMDRllsgdVGSGKTLVALGAAL-----LAYKNGKQVAILVPTEILAHQHYEEARK--FL 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622179293 197 TGLKTALILGGDKMEDQfaalhENPDIIIATpgrlmHVAIEMKLKLQSVEYVVFDEADR 255
Cdd:cd17918 89 PFINVELVTGGTKAQIL-----SGISLLVGT-----HALLHLDVKFKNLDLVIVDEQHR 137
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
125-299 |
4.50e-07 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 53.79 E-value: 4.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 125 PIQRKTIPVILDGKDVVAMARTGSGKT--ACFLIpmFEKLkvhsaKTGARALILSPTRELALQtlKFtKELGRYTGLKTA 202
Cdd:COG4581 28 PFQEEAILALEAGRSVLVAAPTGSGKTlvAEFAI--FLAL-----ARGRRSFYTAPIKALSNQ--KF-FDLVERFGAENV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 203 LILGGDkmedqfaaLHENPD--IIIATPGRLMHVAIEMKLKLQSVEYVVFDE----ADRlfEMGFAeqLQEIISRLPENR 276
Cdd:COG4581 98 GLLTGD--------ASVNPDapIVVMTTEILRNMLYREGADLEDVGVVVMDEfhylADP--DRGWV--WEEPIIHLPARV 165
|
170 180
....*....|....*....|...
gi 1622179293 277 QTVLFSATLPKllVEFARAGLTE 299
Cdd:COG4581 166 QLVLLSATVGN--AEEFAEWLTR 186
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
133-255 |
5.83e-07 |
|
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350793 [Multi-domain] Cd Length: 181 Bit Score: 50.59 E-value: 5.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 133 VILDGKDVVAMArTGSGKTACFLIPMFEKLKvhsaKTGARALILSPTRELALQTLKFTKELGRYTGLKTALIlgGDKMED 212
Cdd:cd18035 13 VALNGNTLIVLP-TGLGKTIIAILVAADRLT----KKGGKVLILAPSRPLVEQHAENLKRVLNIPDKITSLT--GEVKPE 85
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1622179293 213 QFAALHENPDIIIATPGRLMHVAIEMKLKLQSVEYVVFDEADR 255
Cdd:cd18035 86 ERAERWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEAHH 128
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
113-304 |
6.07e-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: 51.00 E-value: 6.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 113 KGIMKK--GYKIPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLIP--MFEKLkvhsaktgarALILSPTreLAL---Q 185
Cdd:cd17920 1 EQILKEvfGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPalLLDGV----------TLVVSPL--ISLmqdQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 186 TLKFTKelgryTGLKTALILGG----DKMEDQFAALHENPDIIIATPGRLMHVAIEMKL-KLQS---VEYVVFDEA---- 253
Cdd:cd17920 69 VDRLQQ-----LGIRAAALNSTlspeEKREVLLRIKNGQYKLLYVTPERLLSPDFLELLqRLPErkrLALIVVDEAhcvs 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622179293 254 ----DrlF--EMGfaeQLQEIISRLPeNRQTVLFSATLPKLLVE--FARAGLTEPVLIR 304
Cdd:cd17920 144 qwghD--FrpDYL---RLGRLRRALP-GVPILALTATATPEVREdiLKRLGLRNPVIFR 196
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
120-432 |
3.43e-06 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 50.87 E-value: 3.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 120 YKIPTPIQRKTIPVILDGKDVVAMARTGSGKT-ACFLIP---MFEKLKVHSAKTGARALILSPTRELA------LQTlkF 189
Cdd:COG1201 22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAFLPAldeLARRPRPGELPDGLRVLYISPLKALAndiernLRA--P 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 190 TKELGRYTGLKTALI-LG---GDKMEDQFAALHEN-PDIIIATPGRLmhvAI-----EMKLKLQSVEYVVFDEadrLFEM 259
Cdd:COG1201 100 LEEIGEAAGLPLPEIrVGvrtGDTPASERQRQRRRpPHILITTPESL---ALlltspDARELLRGVRTVIVDE---IHAL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 260 gfAE-----QLQEIISRL----PENRQTVLFSATL--PKLLVEF-ARAGLTEPVLIrldVESKLSEQLKLSFyHVRADDK 327
Cdd:COG1201 174 --AGskrgvHLALSLERLralaPRPLQRIGLSATVgpLEEVARFlVGYEDPRPVTI---VDAGAGKKPDLEV-LVPVEDL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 328 PALL-------LYLLRTVVRPQDQ---TIVFVATKHHTE----YLKELLTAQGVN--CTHvySSLDQTARkINV-GKFIH 390
Cdd:COG1201 248 IERFpwaghlwPHLYPRVLDLIEAhrtTLVFTNTRSQAErlfqRLNELNPEDALPiaAHH--GSLSREQR-LEVeEALKA 324
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1622179293 391 GKCSVLIVT---DLaarGIDIPLLDNVINYSFPAKAKLFLHRVGR 432
Cdd:COG1201 325 GELRAVVATsslEL---GIDIGDVDLVIQVGSPKSVARLLQRIGR 366
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
345-432 |
4.32e-06 |
|
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: 46.40 E-value: 4.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 345 TIVFVATKHHTEYLKELLTAQGVNCTHVYSslDQTARKINVGK-----FIHGKCSVLIVTDLAARGIDIPLLDNVInysF 419
Cdd:cd18799 9 TLIFCVSIEHAEFMAEAFNEAGIDAVALNS--DYSDRERGDEAlillfFGELKPPILVTVDLLTTGVDIPEVDNVV---F 83
|
90
....*....|....*.
gi 1622179293 420 --PAKAK-LFLHRVGR 432
Cdd:cd18799 84 lrPTESRtLFLQMLGR 99
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
123-293 |
1.00e-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: 46.87 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 123 PTPIQRKTIPVILDGKDVVAMARTGSGKT--ACFLIPMfeklkvhSAKTGARALILSPTRELALQTLKFTKELGRYTGLK 200
Cdd:cd18027 9 LDVFQKQAILHLEAGDSVFVAAHTSAGKTvvAEYAIAL-------AQKHMTRTIYTSPIKALSNQKFRDFKNTFGDVGLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 201 TalilgGDkmedqfAALHENPDIIIATPGRLMHVAIEMKLKLQSVEYVVFDEADRLFEMGFAEQLQEIISRLPENRQTVL 280
Cdd:cd18027 82 T-----GD------VQLNPEASCLIMTTEILRSMLYNGSDVIRDLEWVIFDEVHYINDAERGVVWEEVLIMLPDHVSIIL 150
|
170
....*....|...
gi 1622179293 281 FSATLPKlLVEFA 293
Cdd:cd18027 151 LSATVPN-TVEFA 162
|
|
| DEXHc_RE_I_III_res |
cd18032 |
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ... |
141-255 |
2.45e-05 |
|
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350790 [Multi-domain] Cd Length: 163 Bit Score: 45.24 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 141 VAMArTGSGKT--ACFLIPMFeklkvHSAKTGARALILSPTRELALQTLkftKELGRYTGLKTALILGGDKMEDQFAalh 218
Cdd:cd18032 25 LVMA-TGTGKTytAAFLIKRL-----LEANRKKRILFLAHREELLEQAE---RSFKEVLPDGSFGNLKGGKKKPDDA--- 92
|
90 100 110
....*....|....*....|....*....|....*..
gi 1622179293 219 enpDIIIATPGRLMHVAIEMKLKLQSVEYVVFDEADR 255
Cdd:cd18032 93 ---RVVFATVQTLNKRKRLEKFPPDYFDLIIIDEAHH 126
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
125-272 |
7.49e-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: 44.56 E-value: 7.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 125 PIQRKTIPVILDGKD-VVAMARTGSGKTAC--FLIpmfekLKVHSAKTGARALILSPTRELALQTL-----KFTKELGry 196
Cdd:cd18021 6 PIQTQVFNSLYNTDDnVFVGAPTGSGKTVCaeLAL-----LRHWRQNPKGRAVYIAPMQELVDARYkdwraKFGPLLG-- 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622179293 197 tglKTALILGGDKMEDqfAALHENPDIIIATPGRLMHVAIEMKLK--LQSVEYVVFDEADRL-FEMGFAeqLQEIISRL 272
Cdd:cd18021 79 ---KKVVKLTGETSTD--LKLLAKSDVILATPEQWDVLSRRWKQRknVQSVELFIADELHLIgGENGPV--YEVVVSRM 150
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
135-255 |
8.20e-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: 44.73 E-value: 8.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 135 LDGKDVVAMARTGSGKTACFLIPMFEKLKVHSAKTGARALILSPTRELALQTL-KFTKELGRYtGLKTALILGGDKMEDQ 213
Cdd:cd17927 15 LKGKNTIICLPTGSGKTFVAVLICEHHLKKFPAGRKGKVVFLANKVPLVEQQKeVFRKHFERP-GYKVTGLSGDTSENVS 93
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1622179293 214 FAALHENPDIIIATPGRLMHVAIEMKL-KLQSVEYVVFDEADR 255
Cdd:cd17927 94 VEQIVESSDVIIVTPQILVNDLKSGTIvSLSDFSLLVFDECHN 136
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
394-437 |
1.04e-04 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350172 [Multi-domain] Cd Length: 77 Bit Score: 41.54 E-value: 1.04e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1622179293 394 SVLIVTDLAARGIDIPLLDNVINYSFPAKAKLFLHRVGRVARAG 437
Cdd:cd18785 24 EILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGG 67
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
134-356 |
1.15e-04 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 45.96 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 134 ILDGKDVVAMARTGSGKTACFLIPMFEKLkvhsAKTGARALILSPTRELALQTLKFTKELGRyTGLKTALILGGDKMEDQ 213
Cdd:PRK00254 36 VLEGKNLVLAIPTASGKTLVAEIVMVNKL----LREGGKAVYLVPLKALAEEKYREFKDWEK-LGLRVAMTTGDYDSTDE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 214 FAALHenpDIIIATPGRLMHVAIEMKLKLQSVEYVVFDEADRLFEMGFAEQLQEIISRLPENRQTVLFSATL--PKLLVE 291
Cdd:PRK00254 111 WLGKY---DIIIATAEKFDSLLRHGSSWIKDVKLVVADEIHLIGSYDRGATLEMILTHMLGRAQILGLSATVgnAEELAE 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622179293 292 FARAGLT----EPVLIRLDVesklseqlklsFYH-------VRADDKPALLLYLLRTVVRPQDQTIVFVATKHHTE 356
Cdd:PRK00254 188 WLNAELVvsdwRPVKLRKGV-----------FYQgflfwedGKIERFPNSWESLVYDAVKKGKGALVFVNTRRSAE 252
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
333-439 |
1.53e-04 |
|
C-terminal helicase domain of HrQ family helicases; 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. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350184 [Multi-domain] Cd Length: 146 Bit Score: 42.63 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 333 YLLRTVVRPQDQTIVFVATKHHTE----YLKELLTAQGVNCTHVYSS----LDQTARKINVGKFiHGKCSVLIVTDLAAR 404
Cdd:cd18797 26 RLFADLVRAGVKTIVFCRSRKLAElllrYLKARLVEEGPLASKVASYragyLAEDRREIEAELF-NGELLGVVATNALEL 104
|
90 100 110
....*....|....*....|....*....|....*
gi 1622179293 405 GIDIPLLDNVINYSFPAKAKLFLHRVGRVARAGRS 439
Cdd:cd18797 105 GIDIGGLDAVVLAGYPGSLASLWQQAGRAGRRGKD 139
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
146-447 |
1.75e-04 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 45.11 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 146 TGSGKTACFLIPMFEKLKvhsaKTGARALILSPTRELALQTLKFTKELGRYTGLKTALILGGDKMEDQfAALHENPDIII 225
Cdd:COG1111 26 TGLGKTAVALLVIAERLH----KKGGKVLFLAPTKPLVEQHAEFFKEALNIPEDEIVVFTGEVSPEKR-KELWEKARIIV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 226 ATPGRLMHVAIEMKLKLQSVEYVVFDE-------------ADRLFE-------MGFA-------EQLQEIISRL------ 272
Cdd:COG1111 101 ATPQVIENDLIAGRIDLDDVSLLIFDEahravgnyayvyiAERYHEdakdpliLGMTaspgsdeEKIEEVCENLgienve 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 273 --PENRQTVlfSATLPKLLVEFARAGLTEPVL-IRLDVESKLSEQLK----LSFYHVRADDKPALLLYLLRTVVRPQ--- 342
Cdd:COG1111 181 vrTEEDPDV--APYVHDTEVEWIRVELPEELKeIRDLLNEVLDDRLKklkeLGVIVSTSPDLSKKDLLALQKKLQRRire 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 343 DQTIVFVATKHHTEYLK-----ELLTAQGVNC------------------------------------------------ 369
Cdd:COG1111 259 DDSEGYRAISILAEALKlrhalELLETQGVEAllrylerleeearssggskaskrlvsdprfrkamrlaeeadiehpkls 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 370 ---------------------THVYSSLDQ-----TARKINVGKFI------------------------HGKCSVLIVT 399
Cdd:COG1111 339 klreilkeqlgtnpdsriivfTQYRDTAEMiveflSEPGIKAGRFVgqaskegdkgltqkeqieilerfrAGEFNVLVAT 418
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1622179293 400 DLAARGIDIPLLDNVINYSFPAKAKLFLHRVGRVARaGRSGTAYSLVA 447
Cdd:COG1111 419 SVAEEGLDIPEVDLVIFYEPVPSEIRSIQRKGRTGR-KREGRVVVLIA 465
|
|
| DEXHc_Mtr4-like |
cd18024 |
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or ... |
110-294 |
2.99e-04 |
|
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: 42.82 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 110 PVFKGIMKKGYKIP-TPIQRKTIPVILDGKDVVAMARTGSGKTAC--FLIPMfeklkvhSAKTGARALILSPTRELALQT 186
Cdd:cd18024 19 HKPPGNPARTYPFTlDPFQKTAIACIERNESVLVSAHTSAGKTVVaeYAIAQ-------SLRDKQRVIYTSPIKALSNQK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 187 LK-FTKELGRyTGLKTalilgGDkmedqfAALHENPDIIIATPGRLMHVAIEMKLKLQSVEYVVFDEA----DRlfEMGF 261
Cdd:cd18024 92 YReLQEEFGD-VGLMT-----GD------VTINPNASCLVMTTEILRSMLYRGSEIMREVAWVIFDEIhymrDK--ERGV 157
|
170 180 190
....*....|....*....|....*....|...
gi 1622179293 262 AeqLQEIISRLPENRQTVLFSATLPKLLvEFAR 294
Cdd:cd18024 158 V--WEETIILLPDKVRYVFLSATIPNAR-QFAE 187
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
330-417 |
5.75e-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: 40.92 E-value: 5.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 330 LLLYLLRTVVRPQDQTIVFVATKHHTEYLKELLTAQGVNCTHVYSSLDQTARKINVGKFIHGK--CSVLIVTDLAARGID 407
Cdd:cd18793 15 ALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPdiRVFLLSTKAGGVGLN 94
|
90
....*....|
gi 1622179293 408 IPLLDNVINY 417
Cdd:cd18793 95 LTAANRVILY 104
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
137-252 |
6.66e-04 |
|
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350680 [Multi-domain] Cd Length: 166 Bit Score: 41.41 E-value: 6.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 137 GKDVVAMARTGSGKTACFLIPMFEKLKVHSAKtGARALILSPTRELA------LQTLKFTKELGRYTGLKTalilgGDKM 210
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEK-GVQVLYISPLKALIndqerrLEEPLDEIDLEIPVAVRH-----GDTS 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1622179293 211 EDQFAALHEN-PDIIIATPGRL--MHVAIEMKLKLQSVEYVVFDE 252
Cdd:cd17922 75 QSEKAKQLKNpPGILITTPESLelLLVNKKLRELFAGLRYVVVDE 119
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
125-157 |
9.97e-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: 41.58 E-value: 9.97e-04
10 20 30
....*....|....*....|....*....|...
gi 1622179293 125 PIQRKTIPVILDGKDVVAMARTGSGKTACFLIP 157
Cdd:cd18015 21 PLQLETINATMAGRDVFLVMPTGGGKSLCYQLP 53
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
137-289 |
2.67e-03 |
|
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase responsible for degradation of dsDNA. The two enzymatic units of Cas3, a histidine-aspartate (HD) nuclease and a Superfamily 2 (SF2) helicase, may be expressed from separate genes as Cas3' (SF2 helicase) and Cas3'' (HD nuclease) or may be fused as a single HD-SF2 polypeptide. The nucleolytic activity of most Cas3 enzymes is transition metal ion-dependent. Cas3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350688 [Multi-domain] Cd Length: 186 Bit Score: 39.97 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 137 GKDVVAMARTGSGKTACFLIPMFEklkvHSAKTGARALILS-PTRELALQTLKFTKE-LGRYTGLKTALILGGD---KME 211
Cdd:cd17930 1 PGLVILEAPTGSGKTEAALLWALK----LAARGGKRRIIYAlPTRATINQMYERIREiLGRLDDEDKVLLLHSKaalELL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 212 DQFAALHENP----------------DIIIATPGRLMHVAI-----EMKLKLQSVEYVVFDEA----DRLFEMgFAEQLQ 266
Cdd:cd17930 77 ESDEEPDDDPveavdwalllkrswlaPIVVTTIDQLLESLLkykhfERRLHGLANSVVVLDEVqaydPEYMAL-LLKALL 155
|
170 180
....*....|....*....|...
gi 1622179293 267 EIISRLpeNRQTVLFSATLPKLL 289
Cdd:cd17930 156 ELLGEL--GGPVVLMTATLPALL 176
|
|
| VirD4 |
COG3505 |
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, ... |
146-195 |
4.46e-03 |
|
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442728 [Multi-domain] Cd Length: 402 Bit Score: 40.35 E-value: 4.46e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1622179293 146 TGSGKTACFLIPMFEKLkvhsaKTGARALILSPTRELALQTLKFTKELGR 195
Cdd:COG3505 8 TGSGKTVGLVIPNLTQL-----ARGESVVVTDPKGDLAELTAGFRRRAGY 52
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
135-252 |
5.27e-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: 39.00 E-value: 5.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 135 LDGKDVVAMARTGSGKT-ACFLIPMFEKLKVHSAKTGARALILSPTRELALQTL-KFTKELGRytGLKTALILGGDKMED 212
Cdd:cd18036 15 LRGKNTIICAPTGSGKTrVAVYICRHHLEKRRSAGEKGRVVVLVNKVPLVEQQLeKFFKYFRK--GYKVTGLSGDSSHKV 92
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1622179293 213 QFAALHENPDIIIATP----GRLMHVAIEMKLKLQSVEYVVFDE 252
Cdd:cd18036 93 SFGQIVKASDVIICTPqiliNNLLSGREEERVYLSDFSLLIFDE 136
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
123-227 |
8.22e-03 |
|
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350682 [Multi-domain] Cd Length: 189 Bit Score: 38.46 E-value: 8.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 123 PTPIQRKTIPVILDGKDVVAMARTGSGKTAcFLIPMfeklKVHSAKTGARALILSPTRELALQTLKFTKELGRYTGLKTA 202
Cdd:cd17924 18 PWGAQRTWAKRLLRGKSFAIIAPTGVGKTT-FGLAT----SLYLASKGKRSYLIFPTKSLVKQAYERLSKYAEKAGVEVK 92
|
90 100 110
....*....|....*....|....*....|.
gi 1622179293 203 LILGGDKM------EDQFAALHENPDIIIAT 227
Cdd:cd17924 93 ILVYHSRLkkkekeELLEKIEKGDFDILVTT 123
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
345-445 |
8.51e-03 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350183 [Multi-domain] Cd Length: 150 Bit Score: 37.63 E-value: 8.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 345 TIVFVATKHHTE----YLKELLTAQGVN----CTHvySSLDQTARKINVGKFIHGKCSVLIVT---DLaarGIDIPLLDN 413
Cdd:cd18796 41 TLVFTNTRSQAErlaqRLRELCPDRVPPdfiaLHH--GSLSRELREEVEAALKRGDLKVVVATsslEL---GIDIGDVDL 115
|
90 100 110
....*....|....*....|....*....|..
gi 1622179293 414 VINYSFPAKAKLFLHRVGrvaRAGRSGTAYSL 445
Cdd:cd18796 116 VIQIGSPKSVARLLQRLG---RSGHRPGAASK 144
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
125-270 |
8.96e-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: 8.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 125 PIQRKTIPVILDGKDVVAMARTGSGKTACFLIPMFeklkVHSAKTGARALILSPTreLALqtlkftkelgrytglktali 204
Cdd:cd18018 15 PGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPAL----LLRRRGPGLTLVVSPL--IAL-------------------- 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622179293 205 lggdkMEDQFAALhenPDIIIATPGRLMHVAIEMKLKLQSVEY----VVFDEADRLFEMGFAEQLQEIIS 270
Cdd:cd18018 69 -----MKDQVDAL---PRAIKAAALNSSLTREERRRILEKLRAgevkILYVSPERLVNESFRELLRQTPP 130
|
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