|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
90-461 |
5.91e-124 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 371.02 E-value: 5.91e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 90 TFDSLDLSEQTSIAIKEMGFQYMTQIQAGSIQPLLEGKDVLGAARTGSGKTLAFLIPAVE-LLFKERFSPRngtgVIVIC 168
Cdd:COG0513 3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQrLDPSRPRAPQ----ALILA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 169 PTRELAIQTKNVAEELLKHHSQTVSMVIGGNNRRSEAQRIASGSNLVIATPGRLLDHLQNtKAFIYKHLKCLVIDEADRI 248
Cdd:COG0513 79 PTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIER-GALDLSGVETLVLDEADRM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 249 LEENFEEDMNKILKILPKTRQTALFSATQTSKVKDLARVSLTSPVHVDVDdgRRKVTNEGLEQGYCVVPSKQRLILLISF 328
Cdd:COG0513 158 LDMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVA--PENATAETIEQRYYLVDKRDKLELLRRL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 329 LKKNLNKKIMVFFSTCKSVQFHTEIMKISDVDVSDIHGGMDQNRRTKTFFDFMKAKKGILLCTDVAARGLDIPSVDWIIQ 408
Cdd:COG0513 236 LRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVIN 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 15229677 409 YDPPDKPTEYIHRVGRTARGeGAKGKALLVLIPEELQFIRYL-KAAKVPVKELE 461
Cdd:COG0513 316 YDLPEDPEDYVHRIGRTGRA-GAEGTAISLVTPDERRLLRAIeKLIGQKIEEEE 368
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
100-296 |
1.07e-118 |
|
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: 348.97 E-value: 1.07e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 100 TSIAIKEMGFQYMTQIQAGSIQPLLEGKDVLGAARTGSGKTLAFLIPAVELLFKERFSPRNGTGVIVICPTRELAIQTKN 179
Cdd:cd17942 1 TLKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKFKPRNGTGVIIISPTRELALQIYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 180 VAEELLKHHSQTVSMVIGGNNRRSEAQRIASGSNLVIATPGRLLDHLQNTKAFIYKHLKCLVIDEADRILEENFEEDMNK 259
Cdd:cd17942 81 VAKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLYKNLQCLIIDEADRILEIGFEEEMRQ 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 15229677 260 ILKILPKTRQTALFSATQTSKVKDLARVSL-TSPVHVD 296
Cdd:cd17942 161 IIKLLPKRRQTMLFSATQTRKVEDLARISLkKKPLYVG 198
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
103-296 |
2.05e-80 |
|
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: 250.44 E-value: 2.05e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 103 AIKEMGFQYMTQIQAGSIQPLLEGKDVLGAARTGSGKTLAFLIPAVELLFKERFSPRNGTGVIVICPTRELAIQTKNVAE 182
Cdd:cd00268 4 ALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGRGPQALVLAPTRELAMQIAEVAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 183 ELLKHHSQTVSMVIGGNNRRSEAQRIASGSNLVIATPGRLLDHLQNtKAFIYKHLKCLVIDEADRILEENFEEDMNKILK 262
Cdd:cd00268 84 KLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIER-GKLDLSNVKYLVLDEADRMLDMGFEEDVEKILS 162
|
170 180 190
....*....|....*....|....*....|....
gi 15229677 263 ILPKTRQTALFSATQTSKVKDLARVSLTSPVHVD 296
Cdd:cd00268 163 ALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
100-297 |
9.11e-80 |
|
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: 249.13 E-value: 9.11e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 100 TSIAIKEMGFQYMTQIQAGSIQPLLEGKDVLGAARTGSGKTLAFLIPAVELLFKERFSPRNGTGVIVICPTRELAIQTKN 179
Cdd:cd17941 1 TLKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERWTPEDGLGALIISPTRELAMQIFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 180 VAEELLKHHSQTVSMVIGGNNRRSEAQRIaSGSNLVIATPGRLLDHLQNTKAFIYKHLKCLVIDEADRILEENFEEDMNK 259
Cdd:cd17941 81 VLRKVGKYHSFSAGLIIGGKDVKEEKERI-NRMNILVCTPGRLLQHMDETPGFDTSNLQMLVLDEADRILDMGFKETLDA 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 15229677 260 ILKILPKTRQTALFSATQTSKVKDLARVSLTSPVHVDV 297
Cdd:cd17941 160 IVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
103-296 |
1.24e-71 |
|
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: 227.91 E-value: 1.24e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 103 AIKEMGFQYMTQIQAGSIQPLLEGKDVLGAARTGSGKTLAFLIPAVE-LLFKERFSPrnGTGVIVICPTRELAIQTKNVA 181
Cdd:cd17947 4 ALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILErLLYRPKKKA--ATRVLVLVPTRELAMQCFSVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 182 EELLKHHSQTVSMVIGGNNRRSEAQRIASGSNLVIATPGRLLDHLQNTKAFIYKHLKCLVIDEADRILEENFEEDMNKIL 261
Cdd:cd17947 82 QQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPSFDLDSIEILVLDEADRMLEEGFADELKEIL 161
|
170 180 190
....*....|....*....|....*....|....*
gi 15229677 262 KILPKTRQTALFSATQTSKVKDLARVSLTSPVHVD 296
Cdd:cd17947 162 RLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRVF 196
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
90-435 |
1.28e-71 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 235.99 E-value: 1.28e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 90 TFDSLDLSEQTSIAIKEMGFQYMTQIQAGSIQPLLEGKDVLGAARTGSGKTLAFLIPAVELL--FKERFS--PRngtgVI 165
Cdd:PRK11192 2 TFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLldFPRRKSgpPR----IL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 166 VICPTRELAIQTKNVAEELLKHHSQTVSMVIGGNNRRSEAQRIASGSNLVIATPGRLLDHLQNTKaFIYKHLKCLVIDEA 245
Cdd:PRK11192 78 ILTPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEEN-FDCRAVETLILDEA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 246 DRILEENFEEDMNKILKILPKTRQTALFSAT-QTSKVKDLARVSLTSPVHVDVDDGRR---KVTnegleQGYCVVPSKQ- 320
Cdd:PRK11192 157 DRMLDMGFAQDIETIAAETRWRKQTLLFSATlEGDAVQDFAERLLNDPVEVEAEPSRRerkKIH-----QWYYRADDLEh 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 321 RLILLISFLKKNLNKKIMVFFSTCKSVQFHTEIMKISDVDVSDIHGGMDQNRRTKTFFDFMKAKKGILLCTDVAARGLDI 400
Cdd:PRK11192 232 KTALLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDI 311
|
330 340 350
....*....|....*....|....*....|....*
gi 15229677 401 PSVDWIIQYDPPDKPTEYIHRVGRTARGeGAKGKA 435
Cdd:PRK11192 312 DDVSHVINFDMPRSADTYLHRIGRTGRA-GRKGTA 345
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
86-445 |
1.49e-67 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 225.84 E-value: 1.49e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 86 MTNVTFDSLDLSEQTSIAIKEMGFQYMTQIQAGSIQPLLEGKDVLGAARTGSGKTLAFLIPAVELLFKERFsprnGTGVI 165
Cdd:PRK11776 1 MSMTAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRF----RVQAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 166 VICPTRELAIQtknVAEELLK----HHSQTVSMVIGGNNRRSEAQRIASGSNLVIATPGRLLDHLQNtKAFIYKHLKCLV 241
Cdd:PRK11776 77 VLCPTRELADQ---VAKEIRRlarfIPNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRK-GTLDLDALNTLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 242 IDEADRILEENFEEDMNKILKILPKTRQTALFSATQTSKVKDLARVSLTSPVHVDVDDgrrKVTNEGLEQGYCVVPSKQR 321
Cdd:PRK11776 153 LDEADRMLDMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVES---THDLPAIEQRFYEVSPDER 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 322 LILLISFLKKNLNKKIMVFFSTCKSVQFHTEIMKISDVDVSDIHGGMDQNRRTKTFFDFMKAKKGILLCTDVAARGLDIP 401
Cdd:PRK11776 230 LPALQRLLLHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIK 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 15229677 402 SVDWIIQYDPPDKPTEYIHRVGRTARGeGAKGKALLVLIPEELQ 445
Cdd:PRK11776 310 ALEAVINYELARDPEVHVHRIGRTGRA-GSKGLALSLVAPEEMQ 352
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
90-295 |
1.07e-66 |
|
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: 215.26 E-value: 1.07e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 90 TFDSLDLSEQTSIAIKEMGFQYMTQIQAGSIQPLLEGKDVLGAARTGSGKTLAFLIPAVELLF--KERFSprngtgVIVI 167
Cdd:cd17954 1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLenPQRFF------ALVL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 168 CPTRELAIQTKNVAEELLKHHSQTVSMVIGGNNRRSEAQRIASGSNLVIATPGRLLDHLQNTKAFIYKHLKCLVIDEADR 247
Cdd:cd17954 75 APTRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKGFSLKSLKFLVMDEADR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15229677 248 ILEENFEEDMNKILKILPKTRQTALFSATQTSKVKDLARVSLTSPVHV 295
Cdd:cd17954 155 LLNMDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKI 202
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
107-296 |
4.09e-66 |
|
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: 213.99 E-value: 4.09e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 107 MGFQYMTQIQAGSIQPLLEGKDVLGAARTGSGKTLAFLIPAVELL--FKERFSPRNGTGVIVICPTRELAIQTKNVAEEL 184
Cdd:cd17949 9 MGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLlsLEPRVDRSDGTLALVLVPTRELALQIYEVLEKL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 185 LKH-HSQTVSMVIGGNNRRSEAQRIASGSNLVIATPGRLLDHLQNTKAFIYKHLKCLVIDEADRILEENFEEDMNKILKI 263
Cdd:cd17949 89 LKPfHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQSFDVSNLRWLVLDEADRLLDMGFEKDITKILEL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15229677 264 L-------------PKTRQTALFSATQTSKVKDLARVSLTSPVHVD 296
Cdd:cd17949 169 LddkrskaggekskPSRRQTVLVSATLTDGVKRLAGLSLKDPVYID 214
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
103-295 |
6.51e-65 |
|
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: 210.51 E-value: 6.51e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 103 AIKEMGFQYMTQIQAGSIQPLLEGKDVLGAARTGSGKTLAFLIPAVELLFK-ERFSPRNGTGVIVICPTRELAIQTKNVA 181
Cdd:cd17960 4 VVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKrKANLKKGQVGALIISPTRELATQIYEVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 182 EELLKHHSQTVS--MVIGGNNRRSE-AQRIASGSNLVIATPGRLLDHLQN-TKAFIYKHLKCLVIDEADRILEENFEEDM 257
Cdd:cd17960 84 QSFLEHHLPKLKcqLLIGGTNVEEDvKKFKRNGPNILVGTPGRLEELLSRkADKVKVKSLEVLVLDEADRLLDLGFEADL 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 15229677 258 NKILKILPKTRQTALFSATQTSKVKDLARVSLTSPVHV 295
Cdd:cd17960 164 NRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRV 201
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
96-289 |
1.42e-64 |
|
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: 210.13 E-value: 1.42e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 96 LSEQTSIAIKEMGFQYMTQIQAGSIQPLLE-GKDVLGAARTGSGKTLAFLIPAVELLFKERFSPRNGT-GVIVICPTREL 173
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSGvSALIISPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 174 AIQTKNVAEELLKHHSQ-TVSMVIGGNNRRSEAQRIAS-GSNLVIATPGRLLDHLQNTKAFIY-KHLKCLVIDEADRILE 250
Cdd:cd17964 81 ALQIAAEAKKLLQGLRKlRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLENPGVAKAfTDLDYLVLDEADRLLD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15229677 251 ENFEEDMNKILKILPK----TRQTALFSATQTSKVKDLARVSL 289
Cdd:cd17964 161 MGFRPDLEQILRHLPEknadPRQTLLFSATVPDEVQQIARLTL 203
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
74-461 |
1.25e-61 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 212.71 E-value: 1.25e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 74 DEKNIVIV-GKGIMTNVT-FDSLDLSEQTSIAIKEMGFQYMTQIQAGSIQPLLEGKDVLGAARTGSGKTLAFLIPA-VEL 150
Cdd:PTZ00110 113 KEKEITIIaGENVPKPVVsFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAiVHI 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 151 LFKERFSPRNGTGVIVICPTRELAIQTKNVAEELLKHHSQTVSMVIGGNNRRSEAQRIASGSNLVIATPGRLLDHLQ--- 227
Cdd:PTZ00110 193 NAQPLLRYGDGPIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLEsnv 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 228 -NTKAFIYkhlkcLVIDEADRILEENFEEDMNKILKILPKTRQTALFSATQTSKVKDLARvSLTS--PVHVDVDDGRRKv 304
Cdd:PTZ00110 273 tNLRRVTY-----LVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLAR-DLCKeePVHVNVGSLDLT- 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 305 TNEGLEQGYCVVPSKQRLILLISFLKK--NLNKKIMVFFSTCKSVQFHTEIMKISDVDVSDIHGGMDQNRRTKTFFDFMK 382
Cdd:PTZ00110 346 ACHNIKQEVFVVEEHEKRGKLKMLLQRimRDGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKT 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 383 AKKGILLCTDVAARGLDIPSVDWIIQYDPPDKPTEYIHRVGRTARGeGAKGKALLVLIPEELQ----FIRYLKAAKVPVK 458
Cdd:PTZ00110 426 GKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRA-GAKGASYTFLTPDKYRlardLVKVLREAKQPVP 504
|
....
gi 15229677 459 -ELE 461
Cdd:PTZ00110 505 pELE 508
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
89-448 |
1.82e-60 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 206.97 E-value: 1.82e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 89 VTFDSLDLSEQTSIAIKEMGFQYMTQIQAGSIQPLLEGKDVLGAARTGSGKTLAFLIPAVELLFKERFSP--RNGTGVIV 166
Cdd:PRK10590 1 MSFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAkgRRPVRALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 167 ICPTRELAIQTKNVAEELLKHHSQTVSMVIGGNNRRSEAQRIASGSNLVIATPGRLLDhLQNTKAFIYKHLKCLVIDEAD 246
Cdd:PRK10590 81 LTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLD-LEHQNAVKLDQVEILVLDEAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 247 RILEENFEEDMNKILKILPKTRQTALFSATQTSKVKDLARVSLTSPVHVDVddGRRKVTNEGLEQGYCVVPSKQRLILLI 326
Cdd:PRK10590 160 RMLDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEV--ARRNTASEQVTQHVHFVDKKRKRELLS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 327 SFLKKNLNKKIMVFFSTCKSVQFHTEIMKISDVDVSDIHGGMDQNRRTKTFFDFMKAKKGILLCTDVAARGLDIPSVDWI 406
Cdd:PRK10590 238 QMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHV 317
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 15229677 407 IQYDPPDKPTEYIHRVGRTARGEgAKGKALLVLIPEELQFIR 448
Cdd:PRK10590 318 VNYELPNVPEDYVHRIGRTGRAA-ATGEALSLVCVDEHKLLR 358
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
91-433 |
3.15e-60 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 207.07 E-value: 3.15e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 91 FDSLDLSEQTSIAIKEMGFQYMTQIQAGSIQPLLEGKDVLGAARTGSGKTLAFLIPAVELLF-----KERF--SPRngtg 163
Cdd:PRK01297 89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLqtpppKERYmgEPR---- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 164 VIVICPTRELAIQTKNVAEELLKHHSQTVSMVIGGNNRRSEAQRI-ASGSNLVIATPGRLLDHLQNTKAFIyKHLKCLVI 242
Cdd:PRK01297 165 ALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLeARFCDILVATPGRLLDFNQRGEVHL-DMVEVMVL 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 243 DEADRILEENFEEDMNKILKILPKT--RQTALFSATQTSKVKDLARVSLTSPVHVDVDDgrRKVTNEGLEQGYCVVPSKQ 320
Cdd:PRK01297 244 DEADRMLDMGFIPQVRQIIRQTPRKeeRQTLLFSATFTDDVMNLAKQWTTDPAIVEIEP--ENVASDTVEQHVYAVAGSD 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 321 RLILLISFLKKNLNKKIMVFFSTCKSVQFHTEIMKISDVDVSDIHGGMDQNRRTKTFFDFMKAKKGILLCTDVAARGLDI 400
Cdd:PRK01297 322 KYKLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHI 401
|
330 340 350
....*....|....*....|....*....|...
gi 15229677 401 PSVDWIIQYDPPDKPTEYIHRVGRTARGeGAKG 433
Cdd:PRK01297 402 DGISHVINFTLPEDPDDYVHRIGRTGRA-GASG 433
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
86-436 |
2.04e-59 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 203.28 E-value: 2.04e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 86 MTNVTFDSLDLSEQTSIAIKEMGFQYMTQIQAGSIQPLLEGKDVLGAARTGSGKTLAFLI---------PAVEllFKERF 156
Cdd:PRK04837 5 LTEQKFSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTatfhyllshPAPE--DRKVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 157 SPRngtgVIVICPTRELAIQTKNVAEELLKHHSQTVSMVIGGNNRRSEAQRIASGSNLVIATPGRLLDHL-QNTkaFIYK 235
Cdd:PRK04837 83 QPR----ALIMAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAkQNH--INLG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 236 HLKCLVIDEADRILEENFEEDMNKILKILP--KTRQTALFSATQTSKVKDLARVSLTSPVHVDVDDGRRKVTNEGLEQGY 313
Cdd:PRK04837 157 AIQVVVLDEADRMFDLGFIKDIRWLFRRMPpaNQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEELFY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 314 cvvPSKQ-RLILLISFLKKNLNKKIMVFFST---CKSVQFHTEimkisdvdvSDIH------GGMDQNRRTKTFFDFMKA 383
Cdd:PRK04837 237 ---PSNEeKMRLLQTLIEEEWPDRAIIFANTkhrCEEIWGHLA---------ADGHrvglltGDVAQKKRLRILEEFTRG 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 15229677 384 KKGILLCTDVAARGLDIPSVDWIIQYDPPDKPTEYIHRVGRTARGeGAKGKAL 436
Cdd:PRK04837 305 DLDILVATDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRA-GASGHSI 356
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
113-284 |
2.94e-59 |
|
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: 194.38 E-value: 2.94e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 113 TQIQAGSIQPLLEGKDVLGAARTGSGKTLAFLIPAVELLFKERfsprNGTGVIVICPTRELAIQTKNVAEELLKHHSQTV 192
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLD----NGPQALVLAPTRELAEQIYEELKKLGKGLGLKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 193 SMVIGGNNRRSEAQRIAsGSNLVIATPGRLLDHLQNTKAFiyKHLKCLVIDEADRILEENFEEDMNKILKILPKTRQTAL 272
Cdd:pfam00270 77 ASLLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQERKLL--KNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILL 153
|
170
....*....|..
gi 15229677 273 FSATQTSKVKDL 284
Cdd:pfam00270 154 LSATLPRNLEDL 165
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
87-520 |
6.28e-59 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 207.01 E-value: 6.28e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 87 TNVTFDSLDLSEQTSIAIKEMGFQYMTQIQAGSIQPLLEGKDVLGAARTGSGKTLAFLIPAVELLFKERFSPRngtgVIV 166
Cdd:PRK11634 4 FETTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQ----ILV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 167 ICPTRELAIQTKNVAEELLKH-HSQTVSMVIGGNNRRSEAQRIASGSNLVIATPGRLLDHLQNTKAFIYKhLKCLVIDEA 245
Cdd:PRK11634 80 LAPTRELAVQVAEAMTDFSKHmRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSK-LSGLVLDEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 246 DRILEENFEEDMNKILKILPKTRQTALFSATQTSKVKDLARVSLTSPVHVDVDDGrrKVTNEGLEQGYCVVPSKQRLILL 325
Cdd:PRK11634 159 DEMLRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSS--VTTRPDISQSYWTVWGMRKNEAL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 326 ISFLKKNLNKKIMVFFSTCKSVQFHTEIMKISDVDVSDIHGGMDQNRRTKTFFDFMKAKKGILLCTDVAARGLDIPSVDW 405
Cdd:PRK11634 237 VRFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 406 IIQYDPPDKPTEYIHRVGRTARGeGAKGKALLVLIPEELQFIRYL-KAAKVPVKELEF-NEKRLSnvQSALEKCVAK-DY 482
Cdd:PRK11634 317 VVNYDIPMDSESYVHRIGRTGRA-GRAGRALLFVENRERRLLRNIeRTMKLTIPEVELpNAELLG--KRRLEKFAAKvQQ 393
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 15229677 483 NLNKLAKDAYRAYLSAYNSHSLKDIFNVHRL--DLLAVAE 520
Cdd:PRK11634 394 QLESSDLDQYRALLAKIQPTAEGEELDLETLaaALLKMAQ 433
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
86-436 |
4.40e-56 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 198.25 E-value: 4.40e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 86 MTNVTFDSLDLSEQTSIAIKEMGFQYMTQIQAGSIQPLLEGKDVLGAARTGSGKTLAFLIPAV-ELLFKERFSPRNGTG- 163
Cdd:PRK04537 6 LTDLTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMnRLLSRPALADRKPEDp 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 164 -VIVICPTRELAIQTKNVAEELLKHHSQTVSMVIGGNNRRSEAQRIASGSNLVIATPGRLLDHLQNTKAFIYKHLKCLVI 242
Cdd:PRK04537 86 rALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVVSLHACEICVL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 243 DEADRILEENFEEDMNKILKILPK--TRQTALFSATQTSKVKDLARVSLTSPVHVDVDdgRRKVTNEGLEQGYCVVPSKQ 320
Cdd:PRK04537 166 DEADRMFDLGFIKDIRFLLRRMPErgTRQTLLFSATLSHRVLELAYEHMNEPEKLVVE--TETITAARVRQRIYFPADEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 321 RLILLISFLKKNLNKKIMVFFSTCKSVQFHTEIMKISDVDVSDIHGGMDQNRRTKTFFDFMKAKKGILLCTDVAARGLDI 400
Cdd:PRK04537 244 KQTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHI 323
|
330 340 350
....*....|....*....|....*....|....*.
gi 15229677 401 PSVDWIIQYDPPDKPTEYIHRVGRTARgEGAKGKAL 436
Cdd:PRK04537 324 DGVKYVYNYDLPFDAEDYVHRIGRTAR-LGEEGDAI 358
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
90-295 |
1.15e-55 |
|
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: 186.36 E-value: 1.15e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 90 TFDSLDLSEQTSIAIKEMGFQYMTQIQAGSIQPLLEGKDVLGAARTGSGKTLAFLIPAVELLfKERfSPRNGTGVIVICP 169
Cdd:cd17959 2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKL-KAH-SPTVGARALILSP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 170 TRELAIQTKNVAEELLKHHSQTVSMVIGGNNRRSEAQRIASGSNLVIATPGRLLDHLQNTKaFIYKHLKCLVIDEADRIL 249
Cdd:cd17959 80 TRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMN-LKLSSVEYVVFDEADRLF 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15229677 250 EENFEEDMNKILKILPKTRQTALFSATQTSKVKDLARVSLTSPVHV 295
Cdd:cd17959 159 EMGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
90-448 |
1.22e-54 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 190.04 E-value: 1.22e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 90 TFDSLDLSEQTSIAIKEMGFQYMTQIQAGSIQPLLEGKDVLGAARTGSGKTLAFLIPAVELLFKERfsprNGTGVIVICP 169
Cdd:PTZ00424 29 SFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDL----NACQALILAP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 170 TRELAIQTKNVAEELLKHHSQTVSMVIGGNNRRSEAQRIASGSNLVIATPGRLLDHLqNTKAFIYKHLKCLVIDEADRIL 249
Cdd:PTZ00424 105 TRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMI-DKRHLRVDDLKLFILDEADEML 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 250 EENFEEDMNKILKILPKTRQTALFSATQTSKVKDLARVSLTSPVHVDVDdgRRKVTNEGLEQGYCVVPSKQ-RLILLISF 328
Cdd:PTZ00424 184 SRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVK--KDELTLEGIRQFYVAVEKEEwKFDTLCDL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 329 LKKNLNKKIMVFFSTCKSVQFHTEIMKISDVDVSDIHGGMDQNRRTKTFFDFMKAKKGILLCTDVAARGLDIPSVDWIIQ 408
Cdd:PTZ00424 262 YETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVIN 341
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 15229677 409 YDPPDKPTEYIHRVGRTARGeGAKGKALLVLIPEELQFIR 448
Cdd:PTZ00424 342 YDLPASPENYIHRIGRSGRF-GRKGVAINFVTPDDIEQLK 380
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
91-293 |
2.58e-52 |
|
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: 177.42 E-value: 2.58e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 91 FDSLDLSEQTSIAIKEMGFQYMTQIQAGSIQPLLEGKDVLGAARTGSGKTLAFLIPAVELLFKERFsprnGTGVIVICPT 170
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPY----GIFALVLTPT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 171 RELAIQtknVAEELL---KHHSQTVSMVIGGNNRRSEAQRIASGSNLVIATPGRLLDHLQN----TKAFiyKHLKCLVID 243
Cdd:cd17955 77 RELAYQ---IAEQFRalgAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSsddtTKVL--SRVKFLVLD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15229677 244 EADRILEENFEEDMNKILKILPKTRQTALFSATQTSKVKDLARVSLTSPV 293
Cdd:cd17955 152 EADRLLTGSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPF 201
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
309-439 |
3.47e-52 |
|
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: 174.62 E-value: 3.47e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 309 LEQGYCVVPSKQR-LILLISFLKKNLNKKIMVFFSTCKSVQFHTEIMKISDVDVSDIHGGMDQNRRTKTFFDFMKAKKGI 387
Cdd:cd18787 1 IKQLYVVVEEEEKkLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 15229677 388 LLCTDVAARGLDIPSVDWIIQYDPPDKPTEYIHRVGRTARGeGAKGKALLVL 439
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRA-GRKGTAITFV 131
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
103-293 |
1.23e-49 |
|
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: 170.46 E-value: 1.23e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 103 AIKEMGFQYMTQIQAGSIQPLLEGKDVLGAARTGSGKTLAFLIPAVE--LLFKERFSPRNGTGVIVICPTRELAIQTKNV 180
Cdd:cd17961 8 AIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQkiLKAKAESGEEQGTRALILVPTRELAQQVSKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 181 AEELLKHHSQTVSMVIGGNNRRSEAQRIASGSN--LVIATPGRLLDHLQNTKAFIYKHLKCLVIDEADRILEENFEEDMN 258
Cdd:cd17961 88 LEQLTAYCRKDVRVVNLSASSSDSVQRALLAEKpdIVVSTPARLLSHLESGSLLLLSTLKYLVIDEADLVLSYGYEEDLK 167
|
170 180 190
....*....|....*....|....*....|....*
gi 15229677 259 KILKILPKTRQTALFSATQTSKVKDLARVSLTSPV 293
Cdd:cd17961 168 SLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPA 202
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
104-311 |
3.20e-48 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 166.51 E-value: 3.20e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 104 IKEMGFQYMTQIQAGSIQPLLEG-KDVLGAARTGSGKTLAFLIPAVELLFKerfspRNGTGVIVICPTRELAIQTKNVAE 182
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKR-----GKGGRVLVLVPTRELAEQWAEELK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 183 ELLKHHSQTVSMVIGGNNRRSEAQRIASG-SNLVIATPGRLLDHLQNtKAFIYKHLKCLVIDEADRILEENFEEDMNKIL 261
Cdd:smart00487 76 KLGPSLGLKVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLDLLEN-DKLSLSNVDLVILDEAHRLLDGGFGDQLEKLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15229677 262 KILPKTRQTALFSATQTSKVKDLARVSLTSPVHVDVDDGrrkvTNEGLEQ 311
Cdd:smart00487 155 KLLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGFT----PLEPIEQ 200
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
103-295 |
5.11e-44 |
|
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: 155.94 E-value: 5.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 103 AIKEMGFQYMTQIQAGSIQPLLEGKDVLGAARTGSGKTLAFLIPAVELLFK----ERFSPRNGTGVIVICPTRELAIQTK 178
Cdd:cd17945 4 VIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRlpplDEETKDDGPYALILAPTRELAQQIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 179 NVAEELLKHHSQTVSMVIGGNNRRSEAQRIASGSNLVIATPGRLLDHLQNtKAFIYKHLKCLVIDEADRILEENFEEDMN 258
Cdd:cd17945 84 EETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLER-RLLVLNQCTYVVLDEADRMIDMGFEPQVT 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15229677 259 KILKILPKT--------------------RQTALFSATQTSKVKDLARVSLTSPVHV 295
Cdd:cd17945 163 KILDAMPVSnkkpdteeaeklaasgkhryRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
90-286 |
5.58e-44 |
|
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: 155.72 E-value: 5.58e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 90 TFDSLDLSEQTSIAIKEMGFQYMTQIQAGSIQPLLEGKDVLGAARTGSGKTLAFLIPAVELLFKERFSPRNGTG------ 163
Cdd:cd17967 1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVGRGRrkayps 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 164 VIVICPTRELAIQTKNVAEELLKHHSQTVSMVIGGNNRRSEAQRIASGSNLVIATPGRLLDHLQntKAFIY-KHLKCLVI 242
Cdd:cd17967 81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIE--RGRISlSSIKFLVL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15229677 243 DEADRILEENFEEDMNKIL--KILPKT--RQTALFSATQTSKVKDLAR 286
Cdd:cd17967 159 DEADRMLDMGFEPQIRKIVehPDMPPKgeRQTLMFSATFPREIQRLAA 206
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
103-296 |
2.08e-42 |
|
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: 150.95 E-value: 2.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 103 AIKEMGFQYMTQIQAGSIQPLLEGKDVLGAARTGSGKTLAFLIP----AVELLFKERFSPRNGTGVIVICPTRELAIQTK 178
Cdd:cd17951 4 GLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPlimfALEQEKKLPFIKGEGPYGLIVCPSRELARQTH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 179 NVAEELLKHHSQT------VSMVIGGNNRRSEAQRIASGSNLVIATPGRLLDHLqNTKAFIYKHLKCLVIDEADRILEEN 252
Cdd:cd17951 84 EVIEYYCKALQEGgypqlrCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDML-NKKKINLDICRYLCLDEADRMIDMG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15229677 253 FEEDMNKILKILPKTRQTALFSATQTSKVKDLARVSLTSPVHVD 296
Cdd:cd17951 163 FEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTVN 206
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
91-295 |
2.67e-42 |
|
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: 150.53 E-value: 2.67e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 91 FDSLDLSEQTSIAIKEMGFQYMTQIQAGSIQPLLEGKDVLGAARTGSGKTLAFLIPAVELLFKERfsprNGTGVIVICPT 170
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKK----DVIQALILVPT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 171 RELAIQTKNVAEELLKHHSQTVSMVIGGNNRRSEAQRIASGSNLVIATPGRLLDhLQNTKAFIYKHLKCLVIDEADRILE 250
Cdd:cd17940 77 RELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILD-LAKKGVADLSHCKTLVLDEADKLLS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15229677 251 ENFEEDMNKILKILPKTRQTALFSATQTSKVKDLARVSLTSPVHV 295
Cdd:cd17940 156 QDFQPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
103-278 |
5.22e-42 |
|
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: 150.85 E-value: 5.22e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 103 AIKEMGFQYMTQIQAGSIQP-LLEGKDVLGAARTGSGKTLAFLIPAVELLFKERFSPRNGTGV-----IVICPTRELAIQ 176
Cdd:cd17946 4 ALADLGFSEPTPIQALALPAaIRDGKDVIGAAETGSGKTLAFGIPILERLLSQKSSNGVGGKQkplraLILTPTRELAVQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 177 TKNVAEELLKHHSQTVSMVIGGNNRRSEAQRIASGSNLVIATPGRLLDHLQNTKAFI--YKHLKCLVIDEADRILEE-NF 253
Cdd:cd17946 84 VKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEHLanLKSLRFLVLDEADRMLEKgHF 163
|
170 180 190
....*....|....*....|....*....|..
gi 15229677 254 EEdMNKILKILPKT-------RQTALFSATQT 278
Cdd:cd17946 164 AE-LEKILELLNKDragkkrkRQTFVFSATLT 194
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
104-295 |
1.56e-40 |
|
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: 145.59 E-value: 1.56e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 104 IKEMGFQYMTQIQAGSIQPLLEGKDVLGAARTGSGKTLAFLIPA-VELLFKERFSPRNGTGVIVICPTRELAIQTKNVAE 182
Cdd:cd17966 5 LKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAiVHINAQPPLERGDGPIVLVLAPTRELAQQIQQEAN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 183 ELLKHHSQTVSMVIGGNNRRSEAQRIASGSNLVIATPGRLLDHLQNTKAFIyKHLKCLVIDEADRILEENFEEDMNKIL- 261
Cdd:cd17966 85 KFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNL-RRVTYLVLDEADRMLDMGFEPQIRKIVd 163
|
170 180 190
....*....|....*....|....*....|....
gi 15229677 262 KILPKtRQTALFSATQTSKVKDLARVSLTSPVHV 295
Cdd:cd17966 164 QIRPD-RQTLMWSATWPKEVRRLAEDFLKDYIQV 196
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
104-297 |
2.24e-40 |
|
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ubiquitously expressed in testis, endometrium, and other tissues in humans. DDX52 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350715 [Multi-domain] Cd Length: 198 Bit Score: 145.04 E-value: 2.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 104 IKEMGFQYMTQIQAGSIQPLLEGKDVLGAARTGSGKTLAFLIPAVELLFKerfsPRNGTGV--IVICPTRELAIQTKNVA 181
Cdd:cd17957 5 LEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGK----PRKKKGLraLILAPTRELASQIYREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 182 EELLKHHSQTVSMVIGGNNRRSEAQRIAS-GSNLVIATPGRLLDHLQNTKAFIyKHLKCLVIDEADRILEENFEEDMNKI 260
Cdd:cd17957 81 LKLSKGTGLRIVLLSKSLEAKAKDGPKSItKYDILVSTPLRLVFLLKQGPIDL-SSVEYLVLDEADKLFEPGFREQTDEI 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 15229677 261 LKILP-KTRQTALFSATQTSKVKDLARVSLTSPVHVDV 297
Cdd:cd17957 160 LAACTnPNLQRSLFSATIPSEVEELARSVMKDPIRIIV 197
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
103-295 |
8.84e-40 |
|
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: 143.71 E-value: 8.84e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 103 AIKEMGFQYMTQIQAGSIQPLLEGKDVLGAARTGSGKTLAFLIPA-VELLFKERFSPRNGTGVIVICPTRELAIQTKNVA 181
Cdd:cd17952 4 AIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMlVHIMDQRELEKGEGPIAVIVAPTRELAQQIYLEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 182 EELLKHHSQTVSMVIGGNNRRSEAQRIASGSNLVIATPGRLLDHLQnTKAFIYKHLKCLVIDEADRILEENFEEDMNKIL 261
Cdd:cd17952 84 KKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVK-KKATNLQRVTYLVLDEADRMFDMGFEYQVRSIV 162
|
170 180 190
....*....|....*....|....*....|....
gi 15229677 262 KILPKTRQTALFSATQTSKVKDLARVSLTSPVHV 295
Cdd:cd17952 163 GHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
96-296 |
4.98e-39 |
|
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: 141.69 E-value: 4.98e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 96 LSEQTSIAIKEMGFQYMTQIQAGSIQPLLEGKDVLGAARTGSGKTLAFLIPAVEllfkeRFSPR-NGTGVIVICPTRELA 174
Cdd:cd17939 4 LSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQ-----RIDTTvRETQALVLAPTRELA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 175 IQTKNVAEELLKHHSQTVSMVIGGNNRRSEAQRIASGSNLVIATPGRLLDHLQNtKAFIYKHLKCLVIDEADRILEENFE 254
Cdd:cd17939 79 QQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQR-RSLRTDKIKMFVLDEADEMLSRGFK 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15229677 255 EDMNKILKILPKTRQTALFSATQTSKVKDLARVSLTSPVHVD 296
Cdd:cd17939 158 DQIYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRIL 199
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
115-296 |
1.23e-38 |
|
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: 141.62 E-value: 1.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 115 IQAGSIQPLLEGKDVLGAARTGSGKTLAFLIPAVELLFKeRFSPRngTGVIVICPTRELAIQTKNVAEELLKHHSQTVSM 194
Cdd:cd17956 25 LPSSKSTPPYRPGDLCVSAPTGSGKTLAYVLPIVQALSK-RVVPR--LRALIVVPTKELVQQVYKVFESLCKGTGLKVVS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 195 VIGGNNRRSEAQRIA--------SGSNLVIATPGRLLDHLQNTKAFIYKHLKCLVIDEADRILEENFEE----------- 255
Cdd:cd17956 102 LSGQKSFKKEQKLLLvdtsgrylSRVDILVATPGRLVDHLNSTPGFTLKHLRFLVIDEADRLLNQSFQDwletvmkalgr 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15229677 256 ---------DMNKILKILPKTRQTALFSATQTSKVKDLARVSLTSPVHVD 296
Cdd:cd17956 182 ptapdlgsfGDANLLERSVRPLQKLLFSATLTRDPEKLSSLKLHRPRLFT 231
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
80-295 |
2.01e-38 |
|
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: 140.59 E-value: 2.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 80 IVGKGIMTNVTFDS-LDLSEQTSIAIKEMGFQYMTQIQAGSIQPLLEGKDVLGAARTGSGKTLAFLIPAVELLFKERFS- 157
Cdd:cd17953 2 VRGKDCPKPIQKWSqCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPVk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 158 PRNGTGVIVICPTRELAIQTKNVAEELLKHHSQTVSMVIGGNNRRSEAQRIASGSNLVIATPGRLLDHL--QNTKAFIYK 235
Cdd:cd17953 82 PGEGPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtaNNGRVTNLR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 236 HLKCLVIDEADRILEENFEEDMNKILKILPKTRQTALFSATQTSKVKDLARVSLTSPVHV 295
Cdd:cd17953 162 RVTYVVLDEADRMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
89-471 |
3.39e-38 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 147.63 E-value: 3.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 89 VTFDSLDLSEQTSIAIKEMGFQYMTQIQAGSIQPLLEGKDVLGAARTGSGKTLAFLIPAVE---LLFKERFSPRNGTGVI 165
Cdd:PLN00206 121 LSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISrccTIRSGHPSEQRNPLAM 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 166 VICPTRELAIQTKNVAEELLKHHSQTVSMVIGGNNRRSEAQRIASGSNLVIATPGRLLDHLQntkafiyKH------LKC 239
Cdd:PLN00206 201 VLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLS-------KHdieldnVSV 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 240 LVIDEADRILEENFEEDMNKILKILPkTRQTALFSATQTSKVKDLARVSLTSPVHVDVDDGRRKvtNEGLEQGYCVVPSK 319
Cdd:PLN00206 274 LVLDEVDCMLERGFRDQVMQIFQALS-QPQVLLFSATVSPEVEKFASSLAKDIILISIGNPNRP--NKAVKQLAIWVETK 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 320 QRLILLISFL--KKNLNKKIMVFFSTCKSVQFHTE-IMKISDVDVSDIHGGMDQNRRTKTFFDFMKAKKGILLCTDVAAR 396
Cdd:PLN00206 351 QKKQKLFDILksKQHFKPPAVVFVSSRLGADLLANaITVVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGR 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 397 GLDIPSVDWIIQYDPPDKPTEYIHRVGRTARgEGAKGKAlLVLIPEE-----LQFIRYLKAAKVPV-KELeFNEKRLSNV 470
Cdd:PLN00206 431 GVDLLRVRQVIIFDMPNTIKEYIHQIGRASR-MGEKGTA-IVFVNEEdrnlfPELVALLKSSGAAIpREL-ANSRYLGSG 507
|
.
gi 15229677 471 Q 471
Cdd:PLN00206 508 R 508
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
103-295 |
3.94e-37 |
|
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: 136.44 E-value: 3.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 103 AIKEMGFQYMTQIQAGSIQPLLEGKDVLGAARTGSGKTLAFLIPAV-----ELLFKERfspRNGTGVIVICPTRELAIQt 177
Cdd:cd17958 4 EIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFihldlQPIPREQ---RNGPGVLVLTPTRELALQ- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 178 knVAEELLK--HHSQTVSMVIGGNNRRSEAQRIASGSNLVIATPGRLLDhLQNTKAFIYKHLKCLVIDEADRILEENFEE 255
Cdd:cd17958 80 --IEAECSKysYKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLND-LQMNNVINLKSITYLVLDEADRMLDMGFEP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15229677 256 DMNKILKILPKTRQTALFSATQTSKVKDLARVSLTSPVHV 295
Cdd:cd17958 157 QIRKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
91-295 |
2.18e-35 |
|
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: 131.80 E-value: 2.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 91 FDSLDLSEQTSIAIKEMGFQYMTQIQAGSIQPLLEGKDVLGAARTGSGKTLAFLIPA---VELLFKErfsprngTGVIVI 167
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISIlqqIDTSLKA-------TQALVL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 168 CPTRELAIQTKNVAEELLKHHSQTVSMVIGGNNRRSEAQRIASGSNLVIATPGRLLDHLqNTKAFIYKHLKCLVIDEADR 247
Cdd:cd18046 74 APTRELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMI-NRRYLRTDYIKMFVLDEADE 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15229677 248 ILEENFEEDMNKILKILPKTRQTALFSATQTSKVKDLARVSLTSPVHV 295
Cdd:cd18046 153 MLSRGFKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
91-296 |
5.94e-35 |
|
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: 130.52 E-value: 5.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 91 FDSLDLSEQTSIAIKEMGFQYMTQIQAGSIQPLLEGKDVLGAARTGSGKTLAFLIPAVELlfkerfsprngTGVIVICPT 170
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQI-----------VVALILEPS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 171 RELAIQTKNVAEELLKHHSQ---TVSMVIGGNNRRSEAQRIASGSNLVIATPGRLLDHLQNTKAFIyKHLKCLVIDEADR 247
Cdd:cd17938 70 RELAEQTYNCIENFKKYLDNpklRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDL-SSVRFFVLDEADR 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15229677 248 ILEENFEEDMNKILKILPKTR------QTALFSATQTS-KVKDLARVSLTSPVHVD 296
Cdd:cd17938 149 LLSQGNLETINRIYNRIPKITsdgkrlQVIVCSATLHSfEVKKLADKIMHFPTWVD 204
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
103-295 |
1.09e-34 |
|
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: 129.31 E-value: 1.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 103 AIKEMGFQYMTQIQAGSIQPLLEGKDVLGAARTGSGKTLAFLIPAVELLFKERFSPRngtgVIVICPTRELAIQTKNVAE 182
Cdd:cd17943 4 GLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQ----VLILAPTREIAVQIHDVFK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 183 ELLKH-HSQTVSMVIGGNNRRSEAQRIAsGSNLVIATPGRLLdHLQNTKAFIYKHLKCLVIDEADRILEENFEEDMNKIL 261
Cdd:cd17943 80 KIGKKlEGLKCEVFIGGTPVKEDKKKLK-GCHIAVGTPGRIK-QLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIF 157
|
170 180 190
....*....|....*....|....*....|....*
gi 15229677 262 KILPKTRQTALFSAT-QTSKVKDLARVsLTSPVHV 295
Cdd:cd17943 158 SSLPKNKQVIAFSATyPKNLDNLLARY-MRKPVLV 191
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
90-286 |
1.58e-34 |
|
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: 131.24 E-value: 1.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 90 TFDSLDLSEQTSIAIKEMGFQYMTQIQAGSIQPLLEGKDVLGAARTGSGKTLAFLIPAVELLFKERFSPRNGTGV----- 164
Cdd:cd18052 44 TFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEGLTASSFSEVqepqa 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 165 IVICPTRELAIQTKNVAEELLKHHSQTVSMVIGGNNRRSEAQRIASGSNLVIATPGRLLDHLQNTKAFIYKhLKCLVIDE 244
Cdd:cd18052 124 LIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSK-LKYLILDE 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15229677 245 ADRILEENFEEDMNKILKIL---PKT-RQTALFSATQTSKVKDLAR 286
Cdd:cd18052 203 ADRMLDMGFGPEIRKLVSEPgmpSKEdRQTLMFSATFPEEIQRLAA 248
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
104-297 |
2.14e-32 |
|
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: 124.35 E-value: 2.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 104 IKEMGFQYMTQIQAGSIQPLLEGKDVLGAARTGSGKTLAFLIPAVELLFKERFSPR-NGTGVIVICPTRELAIQTKNVAE 182
Cdd:cd18049 39 IARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERgDGPICLVLAPTRELAQQVQQVAA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 183 ELLKHHSQTVSMVIGGNNRRSEAQRIASGSNLVIATPGRLLDHLQNTKAFIyKHLKCLVIDEADRILEENFEEDMNKILK 262
Cdd:cd18049 119 EYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNL-RRCTYLVLDEADRMLDMGFEPQIRKIVD 197
|
170 180 190
....*....|....*....|....*....|....*
gi 15229677 263 ILPKTRQTALFSATQTSKVKDLARVSLTSPVHVDV 297
Cdd:cd18049 198 QIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINI 232
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
91-295 |
7.71e-32 |
|
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: 121.81 E-value: 7.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 91 FDSLDLSEQTSIAIKEMGFQYMTQIQAGSIQPLLEGKDVLGAARTGSGKTLAF---LIPAVELLFKErfsprngTGVIVI 167
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFsisVLQCLDIQVRE-------TQALIL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 168 CPTRELAIQTKNVAEELLKHHSQTVSMVIGGNNRRSEAQRIASGSNLVIATPGRLLDHLQNtKAFIYKHLKCLVIDEADR 247
Cdd:cd18045 74 SPTRELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRR-RSLRTRHIKMLVLDEADE 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15229677 248 ILEENFEEDMNKILKILPKTRQTALFSATQTSKVKDLARVSLTSPVHV 295
Cdd:cd18045 153 MLNKGFKEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
104-295 |
1.10e-31 |
|
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: 121.12 E-value: 1.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 104 IKEMGFQYMTQIQAGSIQPLLEGKDVLGAARTGSGKTLAFLIPAVELLFKERFSPrngtGVIVICPTRELAIQTKNVAEE 183
Cdd:cd17962 5 LKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNP----SALILTPTRELAVQIEDQAKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 184 LLKH--HSQTVsMVIGGNNRRSEAQRIASGSNLVIATPGRLLDHLqNTKAFIYKHLKCLVIDEADRILEENFEEDMNKIL 261
Cdd:cd17962 81 LMKGlpPMKTA-LLVGGLPLPPQLYRLQQGVKVIIATPGRLLDIL-KQSSVELDNIKIVVVDEADTMLKMGFQQQVLDIL 158
|
170 180 190
....*....|....*....|....*....|....
gi 15229677 262 KILPKTRQTALFSATQTSKVKDLARVSLTSPVHV 295
Cdd:cd17962 159 ENISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
104-296 |
4.83e-31 |
|
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: 119.57 E-value: 4.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 104 IKEMGFQYMTQIQAGSIQPLLEGKDVLGAARTGSGKTLAFLIPAVELLFKERFSPRNGTG--VIVICPTRELAIQTKNVA 181
Cdd:cd17944 5 LQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRKRGRApkVLVLAPTRELANQVTKDF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 182 EELLKhhSQTVSMVIGGNNRRSEAQRIASGSNLVIATPGRLLDHLQNTKAFIYKhLKCLVIDEADRILEENFEEDMNKIL 261
Cdd:cd17944 85 KDITR--KLSVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTK-LKHVVLDEVDQMLDMGFAEQVEEIL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15229677 262 KILPKTR-----QTALFSATQTSKVKDLARVSLTSP-VHVD 296
Cdd:cd17944 162 SVSYKKDsednpQTLLFSATCPDWVYNVAKKYMKSQyEQVD 202
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
75-297 |
1.78e-30 |
|
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: 120.12 E-value: 1.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 75 EKNIVIVGKGIMTNVT-FDSLDLSEQTSIAIKEMGFQYMTQIQAGSIQPLLEGKDVLGAARTGSGKTLAFLIPAVELLFK 153
Cdd:cd18050 47 KKEITIRGVGCPKPVFaFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINH 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 154 ERFSPR-NGTGVIVICPTRELAIQTKNVAEELLKHHSQTVSMVIGGNNRRSEAQRIASGSNLVIATPGRLLDHLQNTKAF 232
Cdd:cd18050 127 QPYLERgDGPICLVLAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTN 206
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15229677 233 IyKHLKCLVIDEADRILEENFEEDMNKILKILPKTRQTALFSATQTSKVKDLARVSLTSPVHVDV 297
Cdd:cd18050 207 L-RRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQINI 270
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
107-286 |
6.97e-30 |
|
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: 116.14 E-value: 6.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 107 MGFQYMTQIQAGSIqPLLEG---KDVLGAARTGSGKTLAFLIPAVEllfkeRFSPRN-GTGVIVICPTRELAIQTKNVAE 182
Cdd:cd17963 12 MGFNKPSKIQETAL-PLILSdppENLIAQSQSGTGKTAAFVLAMLS-----RVDPTLkSPQALCLAPTRELARQIGEVVE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 183 ELLKHHSQTVSMVIGGNNRRSEAQriaSGSNLVIATPGRLLDHLQnTKAFIYKHLKCLVIDEADRILE-ENFEEDMNKIL 261
Cdd:cd17963 86 KMGKFTGVKVALAVPGNDVPRGKK---ITAQIVIGTPGTVLDWLK-KRQLDLKKIKILVLDEADVMLDtQGHGDQSIRIK 161
|
170 180
....*....|....*....|....*
gi 15229677 262 KILPKTRQTALFSATQTSKVKDLAR 286
Cdd:cd17963 162 RMLPRNCQILLFSATFPDSVRKFAE 186
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
91-297 |
9.78e-30 |
|
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: 116.29 E-value: 9.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 91 FDSLDLSEQTSIAIKEMGFQYMTQIQAGSIQPLLEGKDVLGAARTGSGKTLAFLIPAVELLFKerfsPRNGTGVIVICPT 170
Cdd:cd17950 4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEP----VDGQVSVLVICHT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 171 RELAIQTKNVAEELLKH-HSQTVSMVIGGNNRRSEAQRIASGS-NLVIATPGRLLDhLQNTKAFIYKHLKCLVIDEADRI 248
Cdd:cd17950 80 RELAFQISNEYERFSKYmPNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILA-LVREKKLKLSHVKHFVLDECDKM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15229677 249 LEE-NFEEDMNKILKILPKTRQTALFSATQTSKVKDLARVSLTSPVHVDV 297
Cdd:cd17950 159 LEQlDMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
90-286 |
1.32e-29 |
|
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD box, X isoform, or DDX14) has been reported to display a high level of RNA-independent ATPase activity stimulated by both RNA and DNA. This protein has multiple conserved domains and is thought to play roles in both the nucleus and cytoplasm. Nuclear roles include transcriptional regulation, mRNP assembly, pre-mRNA splicing, and mRNA export. In the cytoplasm, this protein is thought to be involved in translation, cellular signaling, and viral replication. Misregulation of this gene has been implicated in tumorigenesis. Diseases associated with DDX3 include mental retardation, X-linked 102 and agenesis of the corpus callosum, with facial anomalies and robin sequence. DDX3 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350809 [Multi-domain] Cd Length: 249 Bit Score: 117.06 E-value: 1.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 90 TFDSLDLSEQTSIAIKEMGFQYMTQIQAGSIQPLLEGKDVLGAARTGSGKTLAFLIPAVELLFKE---RFSPRNGTG--- 163
Cdd:cd18051 22 TFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEQgpgESLPSESGYygr 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 164 ------VIVICPTRELAIQtknVAEELLK--HHSQTVSMVI-GGNNRRSEAQRIASGSNLVIATPGRLLDHLQNTKAFIy 234
Cdd:cd18051 102 rkqyplALVLAPTRELASQ---IYDEARKfaYRSRVRPCVVyGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGL- 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15229677 235 KHLKCLVIDEADRILEENFEEDMNKILK--ILPKT--RQTALFSATQTSKVKDLAR 286
Cdd:cd18051 178 DYCKYLVLDEADRMLDMGFEPQIRRIVEqdTMPPTgeRQTLMFSATFPKEIQMLAR 233
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
320-427 |
8.21e-28 |
|
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: 107.30 E-value: 8.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 320 QRLILLISFLKKNLNKKIMVFFSTCKSVQFHtEIMKISDVDVSDIHGGMDQNRRTKTFFDFMKAKKGILLCTDVAARGLD 399
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLEAE-LLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100
....*....|....*....|....*...
gi 15229677 400 IPSVDWIIQYDPPDKPTEYIHRVGRTAR 427
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIGRAGR 107
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
103-323 |
3.55e-25 |
|
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: 103.99 E-value: 3.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 103 AIKEMGFQYMTQIQAGSIQPLLEGKDVLGAARTGSGKTLAFLIPAVELLFKERFSPRNGTG---VIVICPTRELAIQTKN 179
Cdd:cd17948 4 ILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGPFNaprGLVITPSRELAEQIGS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 180 VAEELLKHHSQTVSMVIGGNNRRSEAQRIASGSNLVIATPGRLldhLQNTKAFIYK--HLKCLVIDEADRILEENFEEDM 257
Cdd:cd17948 84 VAQSLTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPGAL---SKLLTSRIYSleQLRHLVLDEADTLLDDSFNEKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 258 NKIL--------------KILPKTrQTALFSATQTSKVKD-LARVsltspvhVDVdDGRRKVTNEGLeqgYCVVPS-KQR 321
Cdd:cd17948 161 SHFLrrfplasrrsentdGLDPGT-QLVLVSATMPSGVGEvLSKV-------IDV-DSIETVTSDKL---HRLMPHvKQK 228
|
..
gi 15229677 322 LI 323
Cdd:cd17948 229 FL 230
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
348-427 |
4.06e-22 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 90.35 E-value: 4.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 348 QFHTEIMKISDVDVSDIHGGMDQNRRTKTFFDFMKAKKGILLCTDVAARGLDIPSVDWIIQYDPPDKPTEYIHRVGRTAR 427
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
|
| DUF4217 |
pfam13959 |
Domain of unknown function (DUF4217); This short domain is found at the C-terminus of many ... |
471-529 |
1.00e-20 |
|
Domain of unknown function (DUF4217); This short domain is found at the C-terminus of many helicase proteins.
Pssm-ID: 464056 [Multi-domain] Cd Length: 59 Bit Score: 85.53 E-value: 1.00e-20
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 15229677 471 QSALEKCVAKDYNLNKLAKDAYRAYLSAYNSHSLKDIFNVHRLDLLAVAESFCFSSPPK 529
Cdd:pfam13959 1 QLQLEKLVLKDRELKELAQKAFVSYVRAYSKHLAKSIFNVKKLDLGHLAKSFGLLRAPK 59
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
126-276 |
5.04e-19 |
|
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: 83.99 E-value: 5.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 126 GKDVLGAARTGSGKTLAFLIPAVELLFKerfsprNGTGVIVICPTRELAIQTKNVAEELLKHHSqTVSMVIGGNNRRSEA 205
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLLK------KGKKVLVLVPTKALALQTAERLRELFGPGI-RVAVLVGGSSAEERE 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15229677 206 QRIASGSNLVIATPGRLLDHLQNTKAFIYKHLKCLVIDEADRILEENFEEDMNK--ILKILPKTRQTALFSAT 276
Cdd:cd00046 74 KNKLGDADIIIATPDMLLNLLLREDRLFLKDLKLIIVDEAHALLIDSRGALILDlaVRKAGLKNAQVILLSAT 146
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
90-276 |
9.57e-18 |
|
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: 82.38 E-value: 9.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 90 TFDSLDLSEQTSIAIKEMGFQYMTQIQAGSIQPLLEG--KDVLGAARTGSGKTLAFLIPAVELLFKERFSPRngtgVIVI 167
Cdd:cd18048 19 SFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQ----CLCL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 168 CPTRELAIQTKNVAEELLKHHSQTVSMVIGGNNRRSEAQRIASgsNLVIATPGRLLDHLQNTKAFIYKHLKCLVIDEADR 247
Cdd:cd18048 95 SPTFELALQTGKVVEEMGKFCVGIQVIYAIRGNRPGKGTDIEA--QIVIGTPGTVLDWCFKLRLIDVTNISVFVLDEADV 172
|
170 180 190
....*....|....*....|....*....|
gi 15229677 248 ILE-ENFEEDMNKILKILPKTRQTALFSAT 276
Cdd:cd18048 173 MINvQGHSDHSVRVKRSMPKECQMLLFSAT 202
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
90-292 |
9.72e-18 |
|
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: 82.08 E-value: 9.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 90 TFDSLDLSEQTSIAIKEMGFQYMTQIQAGSIQPLLEG--KDVLGAARTGSGKTLAFLIPAVEllfkeRFSPR-NGTGVIV 166
Cdd:cd18047 2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLS-----QVEPAnKYPQCLC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 167 ICPTRELAIQTKNVAEELLKHHSQ-TVSMVIGGNnRRSEAQRIASgsNLVIATPGRLLDHLQNTKAFIYKHLKCLVIDEA 245
Cdd:cd18047 77 LSPTYELALQTGKVIEQMGKFYPElKLAYAVRGN-KLERGQKISE--QIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15229677 246 DRILEENFEEDMN-KILKILPKTRQTALFSATQTSKVKDLARVSLTSP 292
Cdd:cd18047 154 DVMIATQGHQDQSiRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
101-276 |
1.96e-17 |
|
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: 82.04 E-value: 1.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 101 SIAIKEMGFQYMTQIQAGSIQPLLEGKDVLGAARTGSGKTLAFLIPAVELLFKERFSPRNGTG-------------VIVI 167
Cdd:cd17965 36 TLAIKKLLKTLMRKVTKQTSNEEPKLEVFLLAAETGSGKTLAYLAPLLDYLKRQEQEPFEEAEeeyesakdtgrprSVIL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 168 CPTRELAIQTKNVA---EELLKHHSQTVSMVIGGNNRRSeAQRIASGSNLVIATPGRLLDhLQNTKAFIYKHLKCLVIDE 244
Cdd:cd17965 116 VPTHELVEQVYSVLkklSHTVKLGIKTFSSGFGPSYQRL-QLAFKGRIDILVTTPGKLAS-LAKSRPKILSRVTHLVVDE 193
|
170 180 190
....*....|....*....|....*....|..
gi 15229677 245 ADRILEENFEEDMNKILKILPKTRQTALFSAT 276
Cdd:cd17965 194 ADTLFDRSFLQDTTSIIKRAPKLKHLILCSAT 225
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
135-520 |
6.33e-17 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 83.92 E-value: 6.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 135 TGSGKTLAFLIPAVELLFKERfsprngtgVIVICPTRELAIQTKNVAEELLkhhsqtvsmviggNNRRSEAQRIASGSNL 214
Cdd:COG1061 109 TGTGKTVLALALAAELLRGKR--------VLVLVPRRELLEQWAEELRRFL-------------GDPLAGGGKKDSDAPI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 215 VIATPGRL-----LDHLQNTKAFIykhlkclVIDEADRILEENFEedmnKILKILPKTRQTALfSAT------------- 276
Cdd:COG1061 168 TVATYQSLarrahLDELGDRFGLV-------IIDEAHHAGAPSYR----RILEAFPAAYRLGL-TATpfrsdgreillfl 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 277 QTSKV-----KDLARVSLTSPVH-----VDVDDGRRKVTNEGLEQGYCVVPSKQRLILLISFLKKNL--NKKIMVFFSTC 344
Cdd:COG1061 236 FDGIVyeyslKEAIEDGYLAPPEyygirVDLTDERAEYDALSERLREALAADAERKDKILRELLREHpdDRKTLVFCSSV 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 345 KSVQFHTEIMKISDVDVSDIHGGMDQNRRTKTFFDFMKAKKGILLCTDVAARGLDIPSVDWIIQYDPPDKPTEYIHRVGR 424
Cdd:COG1061 316 DHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGR 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 425 TARGEGAKGKALLV-LIPEELQFIRYLKAAKVP--VKELEFNEKRLSNVQSALEKCVAKDYNLNKLAKDAYRAYLSAYNS 501
Cdd:COG1061 396 GLRPAPGKEDALVYdFVGNDVPVLEELAKDLRDlaGYRVEFLDEEESEELALLIAVKPALEVKGELEEELLEELELLEDA 475
|
410
....*....|....*....
gi 15229677 502 HSLKDIFNVHRLDLLAVAE 520
Cdd:COG1061 476 LLLVLAELLLLELLALALE 494
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
111-286 |
3.74e-11 |
|
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: 62.28 E-value: 3.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 111 YMTQIQAGSIQPL-LEGKDVLGAARTGSGKTLAFLIPAVELLFKERFSprngtgVIVICPTRELAIQTKNVAEELLKHHS 189
Cdd:cd17921 1 LLNPIQREALRALyLSGDSVLVSAPTSSGKTLIAELAILRALATSGGK------AVYIAPTRALVNQKEADLRERFGPLG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 190 QTVSMVIGGnnrRSEAQRIASGSNLVIATPGRLLDHLQNTKAFIYKHLKCLVIDEADRILEEN----FEEDMNKILKILP 265
Cdd:cd17921 75 KNVGLLTGD---PSVNKLLLAEADILVATPEKLDLLLRNGGERLIQDVRLVVVDEAHLIGDGErgvvLELLLSRLLRINK 151
|
170 180
....*....|....*....|.
gi 15229677 266 KTRQTALfSATqTSKVKDLAR 286
Cdd:cd17921 152 NARFVGL-SAT-LPNAEDLAE 170
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
116-295 |
6.16e-11 |
|
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: 61.78 E-value: 6.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 116 QAGSIQPLLEGKDVLGAARTGSGKTLAFLIPAveLLFKerfsprnGTgVIVICPTREL------AIQTKNV-AEELlkhH 188
Cdd:cd17920 17 QLEAINAVLAGRDVLVVMPTGGGKSLCYQLPA--LLLD-------GV-TLVVSPLISLmqdqvdRLQQLGIrAAAL---N 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 189 SQTvsmviGGNNRRSEAQRIASGS-NLVIATPGRL-----LDHLQNTKAFiyKHLKCLVIDEADRILE--ENFEEDMNKI 260
Cdd:cd17920 84 STL-----SPEEKREVLLRIKNGQyKLLYVTPERLlspdfLELLQRLPER--KRLALIVVDEAHCVSQwgHDFRPDYLRL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15229677 261 ---LKILPKTrQTALFSATQTSKVKD--LARVSLTSPVHV 295
Cdd:cd17920 157 grlRRALPGV-PILALTATATPEVREdiLKRLGLRNPVIF 195
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
324-432 |
5.32e-10 |
|
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350188 [Multi-domain] Cd Length: 143 Bit Score: 57.75 E-value: 5.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 324 LLISFLKKN---LNKKIMVFFSTCKSVQfhtEIMKISDVDVSDIHG-------------GMDQNRRTKTFFDFMKAKKGI 387
Cdd:cd18801 17 IVKEHFKKKqegSDTRVIIFSEFRDSAE---EIVNFLSKIRPGIRAtrfigqasgksskGMSQKEQKEVIEQFRKGGYNV 93
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 15229677 388 LLCTDVAARGLDIPSVDWIIQYDPPDKPTEYIHRVGRTARGEGAK 432
Cdd:cd18801 94 LVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGRKRQGR 138
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
322-440 |
9.02e-10 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 61.67 E-value: 9.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 322 LILLISFLKKNLNKKIMVFFS---TCKS-VQFHTEI-MKI------SDVDVSDihgGMDQNRRTKTFFDFMKAKKGILLC 390
Cdd:COG1111 341 REILKEQLGTNPDSRIIVFTQyrdTAEMiVEFLSEPgIKAgrfvgqASKEGDK---GLTQKEQIEILERFRAGEFNVLVA 417
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 15229677 391 TDVAARGLDIPSVDWIIQYDPpdKPTE--YIHRVGRTARGEgaKGKaLLVLI 440
Cdd:COG1111 418 TSVAEEGLDIPEVDLVIFYEP--VPSEirSIQRKGRTGRKR--EGR-VVVLI 464
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
387-438 |
1.26e-09 |
|
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: 54.63 E-value: 1.26e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 15229677 387 ILLCTDVAARGLDIPSVDWIIQYDPPDKPTEYIHRVGRTARGEGAKGKALLV 438
Cdd:cd18785 25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVILF 76
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
135-276 |
2.16e-09 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 56.16 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 135 TGSGKTLaFLIPAVELLFKERfsprngtgVIVICPTRELAIQTKNVAEELLKHHSqtvSMVIGGNNRRSEAqriasGSNL 214
Cdd:cd17926 27 TGSGKTL-TALALIAYLKELR--------TLIVVPTDALLDQWKERFEDFLGDSS---IGLIGGGKKKDFD-----DANV 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15229677 215 VIATPgRLLDHLQNTKAFIYKHLKCLVIDEADRILEENFEEdmnkILKILPKTRQTAlFSAT 276
Cdd:cd17926 90 VVATY-QSLSNLAEEEKDLFDQFGLLIVDEAHHLPAKTFSE----ILKELNAKYRLG-LTAT 145
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
116-245 |
2.65e-09 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350681 [Multi-domain] Cd Length: 182 Bit Score: 56.82 E-value: 2.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 116 QAGSIQPLLEGKDVLGAARTGSGKTLAFLIPAVELLFKErfsprNGTGVIVICPTRELAIQTKNVAEELLKHHSQTVSM- 194
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRD-----PGSRALYLYPTKALAQDQLRSLRELLEQLGLGIRVa 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 15229677 195 VIGGNNRRSEAQRIA-SGSNLVIATPGRL---LDHLQNTKAFIYKHLKCLVIDEA 245
Cdd:cd17923 80 TYDGDTPREERRAIIrNPPRILLTNPDMLhyaLLPHHDRWARFLRNLRYVVLDEA 134
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
116-450 |
3.65e-09 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 59.00 E-value: 3.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 116 QAGSIQPLLEGKDVLGAARTGSGKTLAFLIPAveLLfkerfspRNGTGvIVICPtreL---------AIQTKNVAEELLk 186
Cdd:COG0514 22 QEEIIEAVLAGRDALVVMPTGGGKSLCYQLPA--LL-------LPGLT-LVVSP---LialmkdqvdALRAAGIRAAFL- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 187 HHSQTVsmviggNNRRSEAQRIASGS-NLVIATPGRL-----LDHLQNTKafiykhLKCLVIDEADRILE--ENFEED-- 256
Cdd:COG0514 88 NSSLSA------EERREVLRALRAGElKLLYVAPERLlnprfLELLRRLK------ISLFAIDEAHCISQwgHDFRPDyr 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 257 -MNKILKILPKtRQTALFSATQTSKVKD--LARVSLTSPVHV-----------DVddgRRKVTNEGLEQgycvvpskqrl 322
Cdd:COG0514 156 rLGELRERLPN-VPVLALTATATPRVRAdiAEQLGLEDPRVFvgsfdrpnlrlEV---VPKPPDDKLAQ----------- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 323 ilLISFLKKNLNKKIMVFFSTCKSVQFHTEIMKISDVDVSDIHGGMDQNRRTKTFFDFMKAKKGILLCTdVA-ARGLDIP 401
Cdd:COG0514 221 --LLDFLKEHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGIDKP 297
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 15229677 402 SVDWIIQYDPPDKPTEYIHRVGRTARGeGAKGKALLVLIPEELQFIRYL 450
Cdd:COG0514 298 DVRFVIHYDLPKSIEAYYQEIGRAGRD-GLPAEALLLYGPEDVAIQRFF 345
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
123-286 |
1.24e-08 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 57.60 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 123 LLEGKDVLGAARTGSGKTLAFLIPAVELLfkerfspRNGTGVIVICPTRELAIQtknVAEEL---LKHHSQTVSMVIGGN 199
Cdd:COG1204 35 LLEGKNLVVSAPTASGKTLIAELAILKAL-------LNGGKALYIVPLRALASE---KYREFkrdFEELGIKVGVSTGDY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 200 NRRSEAqriASGSNLVIATPGRlLDHLQNTKAFIYKHLKCLVIDEADRILEEN----FEEDMNKILKILPKTRQTALfSA 275
Cdd:COG1204 105 DSDDEW---LGRYDILVATPEK-LDSLLRNGPSWLRDVDLVVVDEAHLIDDESrgptLEVLLARLRRLNPEAQIVAL-SA 179
|
170
....*....|.
gi 15229677 276 TqTSKVKDLAR 286
Cdd:COG1204 180 T-IGNAEEIAE 189
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
95-245 |
1.59e-08 |
|
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: 57.54 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 95 DLSEQTSIAIKEMGFQ--YMTQIQAgsIQPLLEGKDVLGAARTGSGKTLAFLIPAVELLFKERfsprnGTGVIVICPTRE 172
Cdd:COG1205 40 WLPPELRAALKKRGIErlYSHQAEA--IEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDP-----GATALYLYPTKA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 173 LAIQTKNVAEELLKHHSQTVS-MVIGGNNRRSEAQRIASGSNLVIATP-----GRLLDHlqnTK-AFIYKHLKCLVIDEA 245
Cdd:COG1205 113 LARDQLRRLRELAEALGLGVRvATYDGDTPPEERRWIREHPDIVLTNPdmlhyGLLPHH---TRwARFFRNLRYVVIDEA 189
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
126-244 |
3.25e-08 |
|
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: 53.36 E-value: 3.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 126 GKDVLGAARTGSGKTLAFLIPAVELLFKErfsPRNGTGVIVICPTRELAIQTKNVAEELLKHHSQTVSMVI-GGNNRRSE 204
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADE---PEKGVQVLYISPLKALINDQERRLEEPLDEIDLEIPVAVrHGDTSQSE 77
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 15229677 205 AQRI-ASGSNLVIATPGRLLDHLQNTKAF-IYKHLKCLVIDE 244
Cdd:cd17922 78 KAKQlKNPPGILITTPESLELLLVNKKLReLFAGLRYVVVDE 119
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
135-276 |
2.50e-07 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 50.75 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 135 TGSGKTL--AFLIpavELLFKERFSPRngtgVIVICPTRELAIQTKN-VAEELLKHHSQTVsmVIGGNNRRSEAQriasG 211
Cdd:pfam04851 32 TGSGKTLtaAKLI---ARLFKKGPIKK----VLFLVPRKDLLEQALEeFKKFLPNYVEIGE--IISGDKKDESVD----D 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15229677 212 SNLVIATPGRLLDHLQNTKA-FIYKHLKCLVIDEADRILEENFEedmnKILKILPKTRQTAlFSAT 276
Cdd:pfam04851 99 NKIVVTTIQSLYKALELASLeLLPDFFDVIIIDEAHRSGASSYR----NILEYFKPAFLLG-LTAT 159
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
121-247 |
2.54e-07 |
|
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: 51.28 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 121 QPLLEGKDVLGAARTGSGKTLAFLIPAVELLFKerFSPRNGTGVIVICPTRELAIQTKNVAEELLKHHSQTVSMVIGGNN 200
Cdd:cd17927 12 QPALKGKNTIICLPTGSGKTFVAVLICEHHLKK--FPAGRKGKVVFLANKVPLVEQQKEVFRKHFERPGYKVTGLSGDTS 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 15229677 201 RRSEAQRIASGSNLVIATPGRLLDHLQNTKAFIYKHLKCLVIDEADR 247
Cdd:cd17927 90 ENVSVEQIVESSDVIIVTPQILVNDLKSGTIVSLSDFSLLVFDECHN 136
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
120-281 |
3.13e-07 |
|
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: 51.10 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 120 IQPLLEGKDVLGAARTGSGKTLAFLIPAveLLFKERfsprnGTGV-IVICPTRELAI-QTKNvAEELLK----HHSQTVS 193
Cdd:cd18018 21 IARLLSGRSTLVVLPTGAGKSLCYQLPA--LLLRRR-----GPGLtLVVSPLIALMKdQVDA-LPRAIKaaalNSSLTRE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 194 MviggnnRRSEAQRIASGS-NLVIATPGRLldhlqNTKAF--IYKHLK---CLVIDEADRILE--ENFEED---MNKILK 262
Cdd:cd18018 93 E------RRRILEKLRAGEvKILYVSPERL-----VNESFreLLRQTPpisLLVVDEAHCISEwsHNFRPDylrLCRVLR 161
|
170
....*....|....*....
gi 15229677 263 ILPKTRQTALFSATQTSKV 281
Cdd:cd18018 162 ELLGAPPVLALTATATKRV 180
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
133-407 |
3.47e-07 |
|
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 440816 [Multi-domain] Cd Length: 535 Bit Score: 53.16 E-value: 3.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 133 ARTGSGKTLAFLIPAVELLFKerfspRNGTGVIVICPTRELAIQTKNVA-----EELLKHHSQT-VSMVIGGNNRRSEAQ 206
Cdd:COG1203 154 APTGGGKTEAALLFALRLAAK-----HGGRRIIYALPFTSIINQTYDRLrdlfgEDVLLHHSLAdLDLLEEEEEYESEAR 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 207 RIASGSNL-----VIATPGRLLDHL-QNTKAFIYKHL----KCLVIDEADrileeNFEEDM----NKILKILPKTRQTAL 272
Cdd:COG1203 229 WLKLLKELwdapvVVTTIDQLFESLfSNRKGQERRLHnlanSVIILDEVQ-----AYPPYMlallLRLLEWLKNLGGSVI 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 273 F-SATQTSKVKDLarvsLTSPVHV--DVDDGRRKVTNEGLEQGYCVVPSKQRLILLISFLKKNL--NKKIMVFFSTCKSV 347
Cdd:COG1203 304 LmTATLPPLLREE----LLEAYELipDEPEELPEYFRAFVRKRVELKEGPLSDEELAELILEALhkGKSVLVIVNTVKDA 379
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15229677 348 Q-FHTEI-MKISDVDVSDIHGGMDQNRRT------KTFFDfmKAKKGILLCTDVAARGLDIpSVDWII 407
Cdd:COG1203 380 QeLYEALkEKLPDEEVYLLHSRFCPADRSeiekeiKERLE--RGKPCILVSTQVVEAGVDI-DFDVVI 444
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
133-442 |
8.98e-07 |
|
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DEAD/DEAH box helicase DNA helicase cas3'; Often but not always is fused to HD nuclease domain; signature gene for Type I
Pssm-ID: 187770 [Multi-domain] Cd Length: 353 Bit Score: 51.28 E-value: 8.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 133 ARTGSGKTLAFLIPAVELLFKERFSPrngtgVIVICPTRELAIQTKNVAEELLKH-------HSQTVSMVIGGNNRRSEA 205
Cdd:cd09639 6 APTGYGKTEAALLWALHSLKSQKADR-----VIIALPTRATINAMYRRAKEAFGEtglyhssILSSRIKEMGDSEEFEHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 206 QRIASGSNL-VIATPGRL--LDHLQNTKAFIYKH---------LKCLVIDEADrILEENFEEDMNKILKILPKTRQTA-L 272
Cdd:cd09639 81 FPLYIHSNDtLFLDPITVctIDQVLKSVFGEFGHyeftlasiaNSLLIFDEVH-FYDEYTLALILAVLEVLKDNDVPIlL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 273 FSATQTSKVKDLAR-----VSLTSPVHVDVDDGR-RKVTNEgleqgycVVPSKQRLILLISFLKKNlnKKIMVFFSTC-K 345
Cdd:cd09639 160 MSATLPKFLKEYAEkigyvEENEPLDLKPNERAPfIKIESD-------KVGEISSLERLLEFIKKG--GSVAIIVNTVdR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 346 SVQFHTEIM-KISDVDVSDIHGGMDQNRRTKT----FFDFMKAKKGILLCTDVAARGLDIpSVDWII-QYDPPDKpteYI 419
Cdd:cd09639 231 AQEFYQQLKeKGPEEEIMLIHSRFTEKDRAKKeaelLLEFKKSEKFVIVATQVIEASLDI-SVDVMItELAPIDS---LI 306
|
330 340
....*....|....*....|...
gi 15229677 420 HRVGRTARGEGAKGKALLVLIPE 442
Cdd:cd09639 307 QRLGRLHRYGEKNGEEVYIITDA 329
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
322-442 |
1.15e-06 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 51.41 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 322 LILLISFLKKNLNKKIMVFFSTCKSVQFHTEIMKISDVDV------SDIHG--GMDQNRRTKTFFDFMKAKKGILLCTDV 393
Cdd:PRK13766 353 REIVKEQLGKNPDSRIIVFTQYRDTAEKIVDLLEKEGIKAvrfvgqASKDGdkGMSQKEQIEILDKFRAGEFNVLVSTSV 432
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 15229677 394 AARGLDIPSVDWIIQYDPpdKPTE--YIHRVGRTARGEGAKgkaLLVLIPE 442
Cdd:PRK13766 433 AEEGLDIPSVDLVIFYEP--VPSEirSIQRKGRTGRQEEGR---VVVLIAK 478
|
|
| cas3_core |
TIGR01587 |
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ... |
133-434 |
5.45e-06 |
|
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an alignment of Cas3, a protein found in association with CRISPR repeat elements in a broad range of bacteria and archaea. Cas3 appears to be a helicase, with regions found by pfam00270 (DEAD/DEAH box helicase) and pfam00271 (Helicase conserved C-terminal domain). Some but not all members have an N-terminal HD domain region (pfam01966) that is not included within this model.
Pssm-ID: 273707 [Multi-domain] Cd Length: 359 Bit Score: 48.60 E-value: 5.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 133 ARTGSGKTLAFLIPAVELLFKERFSPrngtgVIVICPTRELAIQTKNVAEELLK------HHSQTVS--MVIGGNNRRSE 204
Cdd:TIGR01587 6 APTGYGKTEAALLWALHSIKSQKADR-----VIIALPTRATINAMYRRAKELFGselvglHHSSSFSriKEMGDSEEFEH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 205 AQRIASGSNL-VIATPGRL--LDHLQNTKAFIYKH---------LKCLVIDEADrILEENFEEDMNKILKILPKTRQTA- 271
Cdd:TIGR01587 81 LFPLYIHSNDkLFLDPITVctIDQVLKSVFGEFGHyeftlasiaNSLLIFDEVH-FYDEYTLALILAVLEVLKDNDVPIl 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 272 LFSATQTSKVKDLARvsltspvHVDVDdgrrkVTNEGLEQGYCVVPSKQRLILL-------ISFLKKNLN-----KKIMV 339
Cdd:TIGR01587 160 LMSATLPKFLKEYAE-------KIGYV-----EFNEPLDLKEERRFENHRFILIesdkvgeISSLERLLEfikkgGSIAI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 340 FFSTC-KSVQFHTEIM-KISDVDVSDIHGGMDQNRRTKTFFDFMKA-----KKGILLCTDVAARGLDIpSVDWII-QYDP 411
Cdd:TIGR01587 228 IVNTVdRAQEFYQQLKeKAPEEEIILYHSRFTEKDRAKKEAELLREmkksnEKFVIVATQVIEASLDI-SADVMItELAP 306
|
330 340
....*....|....*....|...
gi 15229677 412 PDKPTEYIHRVGRTARGEGAKGK 434
Cdd:TIGR01587 307 IDSLIQRLGRLHRYGRKIGENFE 329
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
367-432 |
7.46e-06 |
|
C-terminal helicase domain of the 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. Dicer exists throughout eukaryotes, and a subset has 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 helicase domains 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: 350189 [Multi-domain] Cd Length: 142 Bit Score: 45.66 E-value: 7.46e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15229677 367 GMDQNRRTKTFFDFMKAKKGILLCTDVAARGLDIPSVDWIIQYDPPDKPTEYIHRVGRtARGEGAK 432
Cdd:cd18802 73 LMTQRKQKETLDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARAPNSK 137
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
109-174 |
1.30e-05 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 48.17 E-value: 1.30e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15229677 109 FQYMTQIQAGSIQPLLEGKDVLGAARTGSGKTLA-FLIPAVELLFK-ERFSPRNGTGVIVICPTRELA 174
Cdd:COG1201 22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTLAaFLPALDELARRpRPGELPDGLRVLYISPLKALA 89
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
133-245 |
4.10e-05 |
|
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: 44.59 E-value: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 133 ARTGSGKTLAFLIPAVELLfkERFSPRngtGVIVICPTRELAIQTKNVAEELLK----------HHS-------QTVSMV 195
Cdd:cd17930 8 APTGSGKTEAALLWALKLA--ARGGKR---RIIYALPTRATINQMYERIREILGrlddedkvllLHSkaalellESDEEP 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 15229677 196 IGGNNRRSEAQRIASG---SNLVIATPGRLLDHLQNTKAFIYKHL----KCLVIDEA 245
Cdd:cd17930 83 DDDPVEAVDWALLLKRswlAPIVVTTIDQLLESLLKYKHFERRLHglanSVVVLDEV 139
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
110-276 |
4.96e-05 |
|
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: 44.25 E-value: 4.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 110 QYMTqIQAGsiqpLLEGKDVLGAARTGSGKTLAFLIPAVELLFkerfsprNGTGVIVICPTRELAIQT----KNVAEELL 185
Cdd:cd18028 6 QAEA-VRAG----LLKGENLLISIPTASGKTLIAEMAMVNTLL-------EGGKALYLVPLRALASEKyeefKKLEEIGL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 186 KhhsqtVSMVIGGNNRRSEAqriASGSNLVIATPGRlLDHLQNTKAFIYKHLKCLVIDEADRILEEN----FEEDMNKIL 261
Cdd:cd18028 74 K-----VGISTGDYDEDDEW---LGDYDIIVATYEK-FDSLLRHSPSWLRDVGVVVVDEIHLISDEErgptLESIVARLR 144
|
170
....*....|....*
gi 15229677 262 KILPKTRQTALfSAT 276
Cdd:cd18028 145 RLNPNTQIIGL-SAT 158
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
136-218 |
1.01e-04 |
|
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: 43.17 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 136 GSGKTLAFLIPAVELLfkerfspRNGTGVIVICPTRELAIQTKNVAEELLKHHSqtVSMVIGGNNrrseaQRIASGSNLV 215
Cdd:cd17918 46 GSGKTLVALGAALLAY-------KNGKQVAILVPTEILAHQHYEEARKFLPFIN--VELVTGGTK-----AQILSGISLL 111
|
...
gi 15229677 216 IAT 218
Cdd:cd17918 112 VGT 114
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
135-245 |
1.17e-04 |
|
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350792 [Multi-domain] Cd Length: 200 Bit Score: 43.41 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 135 TGSGKTL--AFLIPavELLFKERFSPRNGTGVIVICPTRELAIQTKNVAEELLKHHSQTVSMVIGGNNRRSEAQRIASGS 212
Cdd:cd18034 25 TGSGKTLiaVMLIK--EMGELNRKEKNPKKRAVFLVPTVPLVAQQAEAIRSHTDLKVGEYSGEMGVDKWTKERWKEELEK 102
|
90 100 110
....*....|....*....|....*....|....
gi 15229677 213 NLVI-ATPGRLLDHLQNTKAFIyKHLKCLVIDEA 245
Cdd:cd18034 103 YDVLvMTAQILLDALRHGFLSL-SDINLLIFDEC 135
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
116-293 |
4.79e-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: 4.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 116 QAGSIQPLLEGKDVLGAARTGSGKTLAFLIPAVellfkerfsPRNGTGViVICPTREL------AIQTKNVAEELLKHHS 189
Cdd:cd18015 23 QLETINATMAGRDVFLVMPTGGGKSLCYQLPAL---------CSDGFTL-VVSPLISLmedqlmALKKLGISATMLNASS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 190 --QTVSMVIGgnnrrsEAQRIASGSNLVIATP------GRLLDHLQntKAFIYKHLKCLVIDEAD--RILEENFEEDMNK 259
Cdd:cd18015 93 skEHVKWVHA------ALTDKNSELKLLYVTPekiaksKRFMSKLE--KAYNAGRLARIAIDEVHccSQWGHDFRPDYKK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15229677 260 --ILKIL-PKTRQTALfSATQTSKV-KDL-------ARVSLTSPV 293
Cdd:cd18015 165 lgILKRQfPNVPILGL-TATATSKVlKDVqkilciqKCLTFTASF 208
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
314-423 |
7.59e-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: 39.77 E-value: 7.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 314 CVVPSKqrLILLISFLKKNL--NKKImVFFSTCKSVQFH-TEIMKISDVDVSDIHGGMDQNRRTKTFFDFMKAKKG--IL 388
Cdd:cd18793 7 EVVSGK--LEALLELLEELRepGEKV-LIFSQFTDTLDIlEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIrvFL 83
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 15229677 389 LCTDVAARGLDIPSVDWIIQYDPPDKP------TEYIHRVG 423
Cdd:cd18793 84 LSTKAGGVGLNLTAANRVILYDPWWNPaveeqaIDRAHRIG 124
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
133-244 |
9.96e-04 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 42.22 E-value: 9.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 133 ARTGSGKTLAFLIPAVELLFKERFS------PRNGTGVIVICPT--------RELAIQTKNVAEELLKHHSQTVSMVIG- 197
Cdd:PRK09751 3 APTGSGKTLAAFLYALDRLFREGGEdtreahKRKTSRILYISPIkalgtdvqRNLQIPLKGIADERRRRGETEVNLRVGi 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 15229677 198 --GNNRRSEAQRIASG-SNLVIATPGRLLDHLQNTKAFIYKHLKCLVIDE 244
Cdd:PRK09751 83 rtGDTPAQERSKLTRNpPDILITTPESLYLMLTSRARETLRGVETVIIDE 132
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
111-244 |
1.43e-03 |
|
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: 40.42 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 111 YMTQIQAGSIQPLLEG-KDVLGAARTGSGKTLAFLIPAVELLFKERFSPRNGTGVIVICPTRELAIQTKNVAEELLKHHS 189
Cdd:cd18023 1 YFNRIQSEVFPDLLYSdKNFVVSAPTGSGKTVLFELAILRLLKERNPLPWGNRKVVYIAPIKALCSEKYDDWKEKFGPLG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 15229677 190 QTVSMVIGGNNrrSEAQRIASGSNLVIATPGR--LLDHLQNTKAFIYKHLKCLVIDE 244
Cdd:cd18023 81 LSCAELTGDTE--MDDTFEIQDADIILTTPEKwdSMTRRWRDNGNLVQLVALVLIDE 135
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
356-407 |
1.71e-03 |
|
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350197 [Multi-domain] Cd Length: 151 Bit Score: 39.25 E-value: 1.71e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 15229677 356 ISDVDVSDIHGGMDQNRRTKTFFDFMKAKKGILLCTDVAARGLDIPSVDWII 407
Cdd:cd18810 49 VPEARIAIAHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTII 100
|
|
| DEXHc_RHA-like |
cd17917 |
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ... |
135-245 |
2.18e-03 |
|
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 438707 [Multi-domain] Cd Length: 159 Bit Score: 38.98 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 135 TGSGKT---LAFLIpavellfkeRFSPRNGTGVIVIC--PTRELAIQ-TKNVAEELLKHHSQTVSMVIGGNNRRSEAQRI 208
Cdd:cd17917 10 TGSGKTtqvPQFLL---------EDGLAKGGKGRIVCtqPRRIAAISvAERVAEERGEKLGEEVGYQIRFESKTSSKTRI 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 15229677 209 asgsnlVIATPGRLLDHLQNTKAFiyKHLKCLVIDEA 245
Cdd:cd17917 81 ------KFCTDGILLRELLSDPLL--SGYSHVILDEA 109
|
|
| mfd |
TIGR00580 |
transcription-repair coupling factor (mfd); All proteins in this family for which functions ... |
160-407 |
2.28e-03 |
|
transcription-repair coupling factor (mfd); All proteins in this family for which functions are known are DNA-dependent ATPases that function in the process of transcription-coupled DNA repair in which the repair of the transcribed strand of actively transcribed genes is repaired at a higher rate than the repair of non-transcribed regions of the genome and than the non-transcribed strand of the same gene. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). This family is closely related to the RecG and UvrB families. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273152 [Multi-domain] Cd Length: 926 Bit Score: 40.80 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 160 NGTGVIVICPTRELAIQTKNVAEELLKHHSQTV---SMVIGGNNRRSEAQRIASGS-NLVIATpGRLLdhlqnTKAFIYK 235
Cdd:TIGR00580 499 DGKQVAVLVPTTLLAQQHFETFKERFANFPVTIellSRFRSAKEQNEILKELASGKiDILIGT-HKLL-----QKDVKFK 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 236 HLKCLVIDEadrilEENF---EEDMNKILKI-----------LPKTRQTALfsatqtSKVKDLArvSLTSPvhvdvDDGR 301
Cdd:TIGR00580 573 DLGLLIIDE-----EQRFgvkQKEKLKELRTsvdvltlsatpIPRTLHMSM------SGIRDLS--IIATP-----PEDR 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 302 RKVtnegleQGYcVVPSKQRLILLIsfLKKNLNKKIMVFFstcksvqFHTEIMKISDVD-----------VSDIHGGMDQ 370
Cdd:TIGR00580 635 LPV------RTF-VMEYDPELVREA--IRRELLRGGQVFY-------VHNRIESIEKLAtqlrelvpearIAIAHGQMTE 698
|
250 260 270
....*....|....*....|....*....|....*..
gi 15229677 371 NRRTKTFFDFMKAKKGILLCTDVAARGLDIPSVDWII 407
Cdd:TIGR00580 699 NELEEVMLEFYKGEFQVLVCTTIIETGIDIPNANTII 735
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
365-438 |
3.00e-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: 38.40 E-value: 3.00e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15229677 365 HGGMDQNRRTKTFFDFMKAKKGILLCTDVAARGLDIPSVDWIIQYDPPDKPTEYIHRVGRTARGEGAKGKALLV 438
Cdd:cd18796 75 HGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGHRPGAASKGRLV 148
|
|
| DEXDc_FANCM |
cd18033 |
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ... |
135-287 |
4.93e-03 |
|
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. In complex with CENPS and CENPX, it binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA), and Holliday junction substrates. Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX. In complex with FAAP24, it efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates. In vitro, on its own, it strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA. FANCM is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350791 [Multi-domain] Cd Length: 182 Bit Score: 38.46 E-value: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 135 TGSGKTLaflIPAVELLFKERFSPrngTGVIV-ICPTRELAIQT----KNVAEELLkhhSQTVSMVigGNNRRSEAQRIA 209
Cdd:cd18033 25 TGLGKTF---IAAVVMLNYYRWFP---KGKIVfMAPTKPLVSQQieacYKITGIPS---SQTAELT--GSVPPTKRAELW 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15229677 210 SGSNLVIATPGRLLDHLQNtKAFIYKHLKCLVIDEADRIL-EENFEEDMNKILKILPKTRQTALfSATQTSKVKDLARV 287
Cdd:cd18033 94 ASKRVFFLTPQTLENDLKE-GDCDPKSIVCLVIDEAHRATgNYAYCQVVRELMRYNSHFRILAL-TATPGSKLEAVQQV 170
|
|
| DEXHc_Snf |
cd17919 |
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ... |
136-248 |
6.74e-03 |
|
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting (SNF) proteins 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: 350677 [Multi-domain] Cd Length: 182 Bit Score: 37.93 E-value: 6.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 136 GSGKTL---AFLipavELLFKERFSPRNgtgVIVICPTRELAiqtkNVAEELLKHHSQTVSMVIGGNNRRSEAQRIASG- 211
Cdd:cd17919 29 GLGKTLqaiAFL----AYLLKEGKERGP---VLVVCPLSVLE----NWEREFEKWTPDLRVVVYHGSQRERAQIRAKEKl 97
|
90 100 110
....*....|....*....|....*....|....*....
gi 15229677 212 --SNLVIATPGRLLDHLQNTKAFiykHLKCLVIDEADRI 248
Cdd:cd17919 98 dkFDVVLTTYETLRRDKASLRKF---RWDLVVVDEAHRL 133
|
|
| VirD4 |
COG3505 |
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, ... |
129-184 |
6.89e-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: 39.20 E-value: 6.89e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 15229677 129 VLGAarTGSGKTLAFLIPAVELLfkerfspRNGTGVIVICPTRELAIQTKNVAEEL 184
Cdd:COG3505 4 VIGP--TGSGKTVGLVIPNLTQL-------ARGESVVVTDPKGDLAELTAGFRRRA 50
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
105-292 |
8.62e-03 |
|
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom syndrome protein homolog or BLM) 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 in RecQ2 cause Bloom syndrome.
Pssm-ID: 350774 [Multi-domain] Cd Length: 208 Bit Score: 37.88 E-value: 8.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 105 KEMGFQYMTQIQAGSIQPLLEGKDVLGAARTGSGKTLAFLIPAVellfkerFSPrngtGV-IVICPTRELAIQTKNVAEE 183
Cdd:cd18016 11 KKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPAC-------VSP----GVtVVISPLRSLIVDQVQKLTS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229677 184 LlkhhsQTVSMVIGGNNRRSEAQRI----ASGSNLV---------IATPGRLLDHLQNTkaFIYKHLKCLVIDEADRILE 250
Cdd:cd18016 80 L-----DIPATYLTGDKTDAEATKIylqlSKKDPIIkllyvtpekISASNRLISTLENL--YERKLLARFVIDEAHCVSQ 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15229677 251 --ENFEED---MNKILKILPKTRQTALfSATQTSKV-KD-LARVSLTSP 292
Cdd:cd18016 153 wgHDFRPDykrLNMLRQKFPSVPMMAL-TATATPRVqKDiLNQLKMLRP 200
|
|
| |
