|
Name |
Accession |
Description |
Interval |
E-value |
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
53-251 |
4.32e-142 |
|
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: 406.36 E-value: 4.32e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 53 TLKAIEKMGFTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLAFLIPAIELLHSLKFKPRNGTGIIVITPTRELALQIFG 132
Cdd:cd17942 1 TLKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKFKPRNGTGVIIISPTRELALQIYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 133 VARELMEFHSQTFGIVIGGANRRQEAEKLMKGVNMLIATPGRLLDHLQNTKGFVFKNLKALIIDEADRILEIGFEDEMRQ 212
Cdd:cd17942 81 VAKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLYKNLQCLIIDEADRILEIGFEEEMRQ 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 6323947 213 IIKILPNEdRQSMLFSATQTTKVEDLARISLRPGPLFIN 251
Cdd:cd17942 161 IIKLLPKR-RQTMLFSATQTRKVEDLARISLKKKPLYVG 198
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
43-419 |
4.34e-130 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 384.11 E-value: 4.34e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 43 KFEELKLSQPTLKAIEKMGFTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLAFLIPaieLLHSLKFKPRNGTGIIVITP 122
Cdd:COG0513 3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLP---LLQRLDPSRPRAPQALILAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 123 TRELALQIFGVARELMEFHSQTFGIVIGGANRRQEAEKLMKGVNMLIATPGRLLDHLQNtKGFVFKNLKALIIDEADRIL 202
Cdd:COG0513 80 TRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIER-GALDLSGVETLVLDEADRML 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 203 EIGFEDEMRQIIKILPnEDRQSMLFSATQTTKVEDLARISLRPgPLFINVVPEtdNSTADGLEQGYVVCDSDKRFLLLFS 282
Cdd:COG0513 159 DMGFIEDIERILKLLP-KERQTLLFSATMPPEIRKLAKRYLKN-PVRIEVAPE--NATAETIEQRYYLVDKRDKLELLRR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 283 FLKRNQKKKIIVFlssCNS---VKYYAELLNYIDLPVLELHGKQKQQKRTNTFFEFCNAERGILICTDVAARGLDIPAVD 359
Cdd:COG0513 235 LLRDEDPERAIVF---CNTkrgADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVS 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6323947 360 WIIQFDPPDDPRDYIHRVGRTARGTKgKGKSLMFLTPNELGFLRYL-KASKVPLNEYEFPE 419
Cdd:COG0513 312 HVINYDLPEDPEDYVHRIGRTGRAGA-EGTAISLVTPDERRLLRAIeKLIGQKIEEEELPG 371
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
53-252 |
4.58e-86 |
|
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: 263.38 E-value: 4.58e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 53 TLKAIEKMGFTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLAFLIPAIELLHSLKFKPRNGTGIIVITPTRELALQIFG 132
Cdd:cd17941 1 TLKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERWTPEDGLGALIISPTRELAMQIFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 133 VARELMEFHSQTFGIVIGGANRRQEAEKLmKGVNMLIATPGRLLDHLQNTKGFVFKNLKALIIDEADRILEIGFEDEMRQ 212
Cdd:cd17941 81 VLRKVGKYHSFSAGLIIGGKDVKEEKERI-NRMNILVCTPGRLLQHMDETPGFDTSNLQMLVLDEADRILDMGFKETLDA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 6323947 213 IIKILPNEdRQSMLFSATQTTKVEDLARISLRpGPLFINV 252
Cdd:cd17941 160 IVENLPKS-RQTLLFSATQTKSVKDLARLSLK-NPEYISV 197
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
53-250 |
8.13e-83 |
|
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: 255.06 E-value: 8.13e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 53 TLKAIEKMGFTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLAFLIPAIELLHSLKFKPRNGTGIIVITPTRELALQIFG 132
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGRGPQALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 133 VARELMEFHSQTFGIVIGGANRRQEAEKLMKGVNMLIATPGRLLDHLQNTKgFVFKNLKALIIDEADRILEIGFEDEMRQ 212
Cdd:cd00268 81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGK-LDLSNVKYLVLDEADRMLDMGFEEDVEK 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 6323947 213 IIKILPNeDRQSMLFSATQTTKVEDLARISLRpGPLFI 250
Cdd:cd00268 160 ILSALPK-DRQTLLFSATLPEEVKELAKKFLK-NPVRI 195
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
44-391 |
2.98e-79 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 254.10 E-value: 2.98e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 44 FEELKLSQPTLKAIEKMGFTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLAFLIPAIEllHSLKFkPRNGTG---IIVI 120
Cdd:PRK11192 3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQ--HLLDF-PRRKSGpprILIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 121 TPTRELALQIFGVARELMEFHSQTFGIVIGGANRRQEAEKLMKGVNMLIATPGRLLDHLQNTKgFVFKNLKALIIDEADR 200
Cdd:PRK11192 80 TPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEEN-FDCRAVETLILDEADR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 201 ILEIGFEdemrQIIKILPNEDR---QSMLFSAT-QTTKVEDLARISLRpGPLFINVVPETdnSTADGLEQGYVVCDSDK- 275
Cdd:PRK11192 159 MLDMGFA----QDIETIAAETRwrkQTLLFSATlEGDAVQDFAERLLN-DPVEVEAEPSR--RERKKIHQWYYRADDLEh 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 276 RFLLLFSFLKRNQKKKIIVFLSSCNSVKYYAELLNYIDLPVLELHGKQKQQKRTNTFFEFCNAERGILICTDVAARGLDI 355
Cdd:PRK11192 232 KTALLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDI 311
|
330 340 350
....*....|....*....|....*....|....*..
gi 6323947 356 PAVDWIIQFDPPDDPRDYIHRVGRTAR-GTKGKGKSL 391
Cdd:PRK11192 312 DDVSHVINFDMPRSADTYLHRIGRTGRaGRKGTAISL 348
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
44-400 |
4.67e-79 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 254.34 E-value: 4.67e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 44 FEELKLSQPTLKAIEKMGFTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLAFlipAIELLHSLKFKpRNGTGIIVITPT 123
Cdd:PRK11776 6 FSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAF---GLGLLQKLDVK-RFRVQALVLCPT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 124 RELALQifgVARELMEFHSQTFGIVI----GGANRRQEAEKLMKGVNMLIATPGRLLDHLQntKG-FVFKNLKALIIDEA 198
Cdd:PRK11776 82 RELADQ---VAKEIRRLARFIPNIKVltlcGGVPMGPQIDSLEHGAHIIVGTPGRILDHLR--KGtLDLDALNTLVLDEA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 199 DRILEIGFEDEMRQIIKILPnEDRQSMLFSATQTTKVEDLARISLRpGPLFINVVPETDNSTadgLEQGYVVCDSDKRFL 278
Cdd:PRK11776 157 DRMLDMGFQDAIDAIIRQAP-ARRQTLLFSATYPEGIAAISQRFQR-DPVEVKVESTHDLPA---IEQRFYEVSPDERLP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 279 LLFSFLKRNQKKKIIVFlssCNS---VKYYAELLNYIDLPVLELHGKQKQQKRTNTFFEFCNAERGILICTDVAARGLDI 355
Cdd:PRK11776 232 ALQRLLLHHQPESCVVF---CNTkkeCQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDI 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 6323947 356 PAVDWIIQFDPPDDPRDYIHRVGRTARGTKgKGKSLMFLTPNELG 400
Cdd:PRK11776 309 KALEAVINYELARDPEVHVHRIGRTGRAGS-KGLALSLVAPEEMQ 352
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
49-251 |
3.36e-77 |
|
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: 240.95 E-value: 3.36e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 49 LSQPTLKAIEKMGFTTMTSVQARTIPPLLA-GRDVLGAAKTGSGKTLAFLIPAIE-LLHSLKFKPRNGTGIIVITPTREL 126
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQsLLNTKPAGRRSGVSALIISPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 127 ALQIFGVARELMEFHSQtFGI--VIGGANRRQEAEKLMK-GVNMLIATPGRLLDHLQNTK-GFVFKNLKALIIDEADRIL 202
Cdd:cd17964 81 ALQIAAEAKKLLQGLRK-LRVqsAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLENPGvAKAFTDLDYLVLDEADRLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6323947 203 EIGFEDEMRQIIKILPN---EDRQSMLFSATQTTKVEDLARISLRPGPLFIN 251
Cdd:cd17964 160 DMGFRPDLEQILRHLPEknaDPRQTLLFSATVPDEVQQIARLTLKKDYKFID 211
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
54-245 |
1.53e-74 |
|
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: 233.69 E-value: 1.53e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 54 LKAIEKMGFTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLAFLIPaieLLHSLKFKPRN--GTGIIVITPTRELALQIF 131
Cdd:cd17947 2 LRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLP---ILERLLYRPKKkaATRVLVLVPTRELAMQCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 132 GVARELMEFHSQTFGIVIGGAN-RRQEAEkLMKGVNMLIATPGRLLDHLQNTKGFVFKNLKALIIDEADRILEIGFEDEM 210
Cdd:cd17947 79 SVLQQLAQFTDITFALAVGGLSlKAQEAA-LRARPDIVIATPGRLIDHLRNSPSFDLDSIEILVLDEADRMLEEGFADEL 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 6323947 211 RQIIKILPnEDRQSMLFSATQTTKVEDLARISL-RP 245
Cdd:cd17947 158 KEILRLCP-RTRQTMLFSATMTDEVKDLAKLSLnKP 192
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
41-438 |
5.47e-74 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 243.53 E-value: 5.47e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 41 VEKFEELKLSQPTLKAIEKMGFTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLAFLIPAI-ELLHSLKFKPRNGTGIIV 119
Cdd:PTZ00110 129 VVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIvHINAQPLLRYGDGPIVLV 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 120 ITPTRELALQIFGVARELMEFHSQTFGIVIGGANRRQEAEKLMKGVNMLIATPGRLLDHLQNTkgfvFKNLKA---LIID 196
Cdd:PTZ00110 209 LAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESN----VTNLRRvtyLVLD 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 197 EADRILEIGFEDEMRQII-KILPneDRQSMLFSATQTTKVEDLARISLRPGPLFINVvPETDNSTADGLEQG-YVVCDSD 274
Cdd:PTZ00110 285 EADRMLDMGFEPQIRKIVsQIRP--DRQTLMWSATWPKEVQSLARDLCKEEPVHVNV-GSLDLTACHNIKQEvFVVEEHE 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 275 KRfLLLFSFLKR--NQKKKIIVFLSSCNSVKYYAELLNYIDLPVLELHGKQKQQKRTNTFFEFCNAERGILICTDVAARG 352
Cdd:PTZ00110 362 KR-GKLKMLLQRimRDGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRG 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 353 LDIPAVDWIIQFDPPDDPRDYIHRVGRTARGtKGKGKSLMFLTPNELGFLRYLkaSKVpLNEYEFPenkianVQSQLEKL 432
Cdd:PTZ00110 441 LDVKDVKYVINFDFPNQIEDYVHRIGRTGRA-GAKGASYTFLTPDKYRLARDL--VKV-LREAKQP------VPPELEKL 510
|
....*.
gi 6323947 433 IKSNYY 438
Cdd:PTZ00110 511 SNERSN 516
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
58-250 |
4.01e-71 |
|
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: 225.54 E-value: 4.01e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 58 EKMGFTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLAFLIPAIELLHSLKFK-PRN-GTGIIVITPTRELALQIFGVAR 135
Cdd:cd17949 7 SKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRvDRSdGTLALVLVPTRELALQIYEVLE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 136 ELME-FHSQTFGIVIGGANRRQEAEKLMKGVNMLIATPGRLLDHLQNTKGFVFKNLKALIIDEADRILEIGFEDEMRQII 214
Cdd:cd17949 87 KLLKpFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQSFDVSNLRWLVLDEADRLLDMGFEKDITKIL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 6323947 215 KILPNED------------RQSMLFSATQTTKVEDLARISLRpGPLFI 250
Cdd:cd17949 167 ELLDDKRskaggekskpsrRQTVLVSATLTDGVKRLAGLSLK-DPVYI 213
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
44-244 |
3.39e-67 |
|
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: 214.87 E-value: 3.39e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 44 FEELKLSQPTLKAIEKMGFTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLAFLIPaieLLHSLKFKPRnGTGIIVITPT 123
Cdd:cd17954 2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALP---ILQALLENPQ-RFFALVLAPT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 124 RELALQIFGVARELMEFHSQTFGIVIGGANRRQEAEKLMKGVNMLIATPGRLLDHLQNTKGFVFKNLKALIIDEADRILE 203
Cdd:cd17954 78 RELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKGFSLKSLKFLVMDEADRLLN 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 6323947 204 IGFEDEMRQIIKILPNEdRQSMLFSATQTTKVEDLARISLR 244
Cdd:cd17954 158 MDFEPEIDKILKVIPRE-RTTYLFSATMTTKVAKLQRASLK 197
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
53-244 |
6.61e-66 |
|
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: 211.67 E-value: 6.61e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 53 TLKAIEKMGFTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLAFLIPAIE-LLHSLKFKPRNGTGIIVITPTRELALQIF 131
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEiLLKRKANLKKGQVGALIISPTRELATQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 132 GVARELMEFHSQTF--GIVIGGANRRQEAEKLM-KGVNMLIATPGRLLDHLQNTKGFV-FKNLKALIIDEADRILEIGFE 207
Cdd:cd17960 81 EVLQSFLEHHLPKLkcQLLIGGTNVEEDVKKFKrNGPNILVGTPGRLEELLSRKADKVkVKSLEVLVLDEADRLLDLGFE 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 6323947 208 DEMRQIIKILPNEdRQSMLFSATQTTKVEDLARISLR 244
Cdd:cd17960 161 ADLNRILSKLPKQ-RRTGLFSATQTDAVEELIKAGLR 196
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
43-386 |
1.23e-64 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 217.09 E-value: 1.23e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 43 KFEELKLSQPTLKAIEKMGFTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLAFLIPAI-ELLHSLKFKPR--NGTGIIV 119
Cdd:PRK01297 88 RFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIInQLLQTPPPKERymGEPRALI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 120 ITPTRELALQIFGVARELMEFHSQTFGIVIGGANRRQEAEKL-MKGVNMLIATPGRLLDHlqNTKGFVFKNL-KALIIDE 197
Cdd:PRK01297 168 IAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLeARFCDILVATPGRLLDF--NQRGEVHLDMvEVMVLDE 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 198 ADRILEIGFEDEMRQIIKILP-NEDRQSMLFSATQTTKVEDLARiSLRPGPLFINVVPEtdNSTADGLEQG-YVVCDSDK 275
Cdd:PRK01297 246 ADRMLDMGFIPQVRQIIRQTPrKEERQTLLFSATFTDDVMNLAK-QWTTDPAIVEIEPE--NVASDTVEQHvYAVAGSDK 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 276 rFLLLFSFLKRNQKKKIIVFLSSCNSVKYYAELLNYIDLPVLELHGKQKQQKRTNTFFEFCNAERGILICTDVAARGLDI 355
Cdd:PRK01297 323 -YKLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHI 401
|
330 340 350
....*....|....*....|....*....|..
gi 6323947 356 PAVDWIIQFDPPDDPRDYIHRVGRTAR-GTKG 386
Cdd:PRK01297 402 DGISHVINFTLPEDPDDYVHRIGRTGRaGASG 433
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
44-391 |
3.17e-63 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 215.97 E-value: 3.17e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 44 FEELKLSQPTLKAIEKMGFTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLAFLIPAIELLHS----LKFKPRNGTGIIv 119
Cdd:PRK04537 11 FSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSrpalADRKPEDPRALI- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 120 ITPTRELALQIFGVARELMEFHSQTFGIVIGGANRRQEAEKLMKGVNMLIATPGRLLDHLQNTKGFVFKNLKALIIDEAD 199
Cdd:PRK04537 90 LAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVVSLHACEICVLDEAD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 200 RILEIGFEDEMRQIIKILPNE-DRQSMLFSATQTTKVEDLARISL-RPGPLfinvVPETDNSTADGLEQGYVVCDSDKRF 277
Cdd:PRK04537 170 RMFDLGFIKDIRFLLRRMPERgTRQTLLFSATLSHRVLELAYEHMnEPEKL----VVETETITAARVRQRIYFPADEEKQ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 278 LLLFSFLKRNQKKKIIVFLSSCNSVKYYAELLNYIDLPVLELHGKQKQQKRTNTFFEFCNAERGILICTDVAARGLDIPA 357
Cdd:PRK04537 246 TLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDG 325
|
330 340 350
....*....|....*....|....*....|....*
gi 6323947 358 VDWIIQFDPPDDPRDYIHRVGRTAR-GTKGKGKSL 391
Cdd:PRK04537 326 VKYVYNYDLPFDAEDYVHRIGRTARlGEEGDAISF 360
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
44-403 |
2.93e-61 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 207.74 E-value: 2.93e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 44 FEELKLSQPTLKAIEKMGFTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLAFLIPAIELL--HSLKFKPRNGTGIIVIT 121
Cdd:PRK10590 3 FDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLitRQPHAKGRRPVRALILT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 122 PTRELALQIFGVARELMEFHSQTFGIVIGGANRRQEAEKLMKGVNMLIATPGRLLDhLQNTKGFVFKNLKALIIDEADRI 201
Cdd:PRK10590 83 PTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLD-LEHQNAVKLDQVEILVLDEADRM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 202 LEIGFEDEMRQIIKILPNEdRQSMLFSATQTTKVEDLARISLRpGPLFINVVPEtdNSTADGLEQGYVVCDSDKRFLLLF 281
Cdd:PRK10590 162 LDMGFIHDIRRVLAKLPAK-RQNLLFSATFSDDIKALAEKLLH-NPLEIEVARR--NTASEQVTQHVHFVDKKRKRELLS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 282 SFLKRNQKKKIIVFLSSCNSVKYYAELLNYIDLPVLELHGKQKQQKRTNTFFEFCNAERGILICTDVAARGLDIPAVDWI 361
Cdd:PRK10590 238 QMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHV 317
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 6323947 362 IQFDPPDDPRDYIHRVGRTARGTkGKGKSLMFLTPNELGFLR 403
Cdd:PRK10590 318 VNYELPNVPEDYVHRIGRTGRAA-ATGEALSLVCVDEHKLLR 358
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
44-474 |
6.03e-61 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 210.86 E-value: 6.03e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 44 FEELKLSQPTLKAIEKMGFTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLAFLIPaieLLHSLKFKPRnGTGIIVITPT 123
Cdd:PRK11634 8 FADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLP---LLHNLDPELK-APQILVLAPT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 124 RELALQifgVARELMEFHSQTFGIVI----GGANRRQEAEKLMKGVNMLIATPGRLLDHLQntKGFV-FKNLKALIIDEA 198
Cdd:PRK11634 84 RELAVQ---VAEAMTDFSKHMRGVNVvalyGGQRYDVQLRALRQGPQIVVGTPGRLLDHLK--RGTLdLSKLSGLVLDEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 199 DRILEIGFEDEMRQIIKILPNEdRQSMLFSATQTtkvEDLARISLRpgplFIN----VVPETDNSTADGLEQGYVVCDSD 274
Cdd:PRK11634 159 DEMLRMGFIEDVETIMAQIPEG-HQTALFSATMP---EAIRRITRR----FMKepqeVRIQSSVTTRPDISQSYWTVWGM 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 275 KRFLLLFSFLKRNQKKKIIVFLSSCNSVKYYAELLNYIDLPVLELHGKQKQQKRTNTFFEFCNAERGILICTDVAARGLD 354
Cdd:PRK11634 231 RKNEALVRFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 355 IPAVDWIIQFDPPDDPRDYIHRVGRTARGTKGkGKSLMFLTPNELGFLRYL-KASKVPLNEYEFPENKI----------A 423
Cdd:PRK11634 311 VERISLVVNYDIPMDSESYVHRIGRTGRAGRA-GRALLFVENRERRLLRNIeRTMKLTIPEVELPNAELlgkrrlekfaA 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 6323947 424 NVQSQLEkliksnyylhQTAKDGYRSYLQayashSLKTVYQIDKLDLAKVA 474
Cdd:PRK11634 390 KVQQQLE----------SSDLDQYRALLA-----KIQPTAEGEELDLETLA 425
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
66-238 |
3.73e-60 |
|
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: 195.15 E-value: 3.73e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 66 TSVQARTIPPLLAGRDVLGAAKTGSGKTLAFLIPAIELLHSLKfkprNGTGIIVITPTRELALQIFGVARELMEFHSQTF 145
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLD----NGPQALVLAPTRELAEQIYEELKKLGKGLGLKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 146 GIVIGGANRRQEAEKLmKGVNMLIATPGRLLDHLQNTKGfvFKNLKALIIDEADRILEIGFEDEMRQIIKILPnEDRQSM 225
Cdd:pfam00270 77 ASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERKL--LKNLKLLVLDEAHRLLDMGFGPDLEEILRRLP-KKRQIL 152
|
170
....*....|...
gi 6323947 226 LFSATQTTKVEDL 238
Cdd:pfam00270 153 LLSATLPRNLEDL 165
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
43-391 |
5.96e-60 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 203.28 E-value: 5.96e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 43 KFEELKLSQPTLKAIEKMGFTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLAFLI---------PAIEllHSLKFKPRn 113
Cdd:PRK04837 9 KFSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTatfhyllshPAPE--DRKVNQPR- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 114 gtgIIVITPTRELALQIFGVARELMEFHSQTFGIVIGGANRRQEAEKLMKGVNMLIATPGRLLDHL-QNTkgFVFKNLKA 192
Cdd:PRK04837 86 ---ALIMAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAkQNH--INLGAIQV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 193 LIIDEADRILEIGFEDEMRQIIKILPN-EDRQSMLFSATQTTKVEDLARISLRpGPLFINVVPETDNSTADGLEQGYVvc 271
Cdd:PRK04837 161 VVLDEADRMFDLGFIKDIRWLFRRMPPaNQRLNMLFSATLSYRVRELAFEHMN-NPEYVEVEPEQKTGHRIKEELFYP-- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 272 DSDKRFLLLFSFLKRNQKKKIIVFLS---SCNSVKYYaelLNYIDLPVLELHGKQKQQKRTNTFFEFCNAERGILICTDV 348
Cdd:PRK04837 238 SNEEKMRLLQTLIEEEWPDRAIIFANtkhRCEEIWGH---LAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDV 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 6323947 349 AARGLDIPAVDWIIQFDPPDDPRDYIHRVGRTAR-GTKGKGKSL 391
Cdd:PRK04837 315 AARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRaGASGHSISL 358
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
21-403 |
3.86e-58 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 197.74 E-value: 3.86e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 21 DEKSTSKQNNAAPEGEQTT--CVEKFEELKLSQPTLKAIEKMGFTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLAFLI 98
Cdd:PTZ00424 5 EQKNQSEQVASTGTIESNYdeIVDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 99 PAIELL-HSLkfkprNGTGIIVITPTRELALQIFGVARELMEFHSQTFGIVIGGANRRQEAEKLMKGVNMLIATPGRLLD 177
Cdd:PTZ00424 85 AALQLIdYDL-----NACQALILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 178 HLqNTKGFVFKNLKALIIDEADRILEIGFEDEMRQIIKILPnEDRQSMLFSATQTTKVEDLARISLRpGPLFINVvpETD 257
Cdd:PTZ00424 160 MI-DKRHLRVDDLKLFILDEADEMLSRGFKGQIYDVFKKLP-PDVQVALFSATMPNEILELTTKFMR-DPKRILV--KKD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 258 NSTADGLEQGYVVCDSDK-RFLLLFSFLKRNQKKKIIVFLSSCNSVKYYAELLNYIDLPVLELHGKQKQQKRTNTFFEFC 336
Cdd:PTZ00424 235 ELTLEGIRQFYVAVEKEEwKFDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFR 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6323947 337 NAERGILICTDVAARGLDIPAVDWIIQFDPPDDPRDYIHRVGRTARGTKgKGKSLMFLTPNELGFLR 403
Cdd:PTZ00424 315 SGSTRVLITTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGR-KGVAINFVTPDDIEQLK 380
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
44-251 |
3.24e-57 |
|
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: 189.05 E-value: 3.24e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 44 FEELKLSQPTLKAIEKMGFTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLAFLIPAIELL--HSlkfkPRNGTGIIVIT 121
Cdd:cd17959 3 FQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLkaHS----PTVGARALILS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 122 PTRELALQIFGVARELMEFHSQTFGIVIGGANRRQEAEKLMKGVNMLIATPGRLLDHLQNTkGFVFKNLKALIIDEADRI 201
Cdd:cd17959 79 PTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEM-NLKLSSVEYVVFDEADRL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6323947 202 LEIGFEDEMRQIIKILPnEDRQSMLFSATQTTKVEDLARISLRpGPLFIN 251
Cdd:cd17959 158 FEMGFAEQLHEILSRLP-ENRQTLLFSATLPKLLVEFAKAGLN-EPVLIR 205
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
44-240 |
1.16e-56 |
|
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: 188.08 E-value: 1.16e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 44 FEELKLSQPTLKAIEKMGFTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLAFLIPAI-ELLHSLKFKPRNGTG-----I 117
Cdd:cd17967 2 FEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIIsKLLEDGPPSVGRGRRkaypsA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 118 IVITPTRELALQIFGVARELMeFHSQTFGIVI-GGANRRQEAEKLMKGVNMLIATPGRLLDHLQntKGFV-FKNLKALII 195
Cdd:cd17967 82 LILAPTRELAIQIYEEARKFS-YRSGVRSVVVyGGADVVHQQLQLLRGCDILVATPGRLVDFIE--RGRIsLSSIKFLVL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 6323947 196 DEADRILEIGFEDEMRQIIK---ILPNEDRQSMLFSATQTTKVEDLAR 240
Cdd:cd17967 159 DEADRMLDMGFEPQIRKIVEhpdMPPKGERQTLMFSATFPREIQRLAA 206
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
44-243 |
1.89e-56 |
|
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: 187.05 E-value: 1.89e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 44 FEELKLSQPTLKAIEKMGFTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLAFLIPaieLLHSLKfkpRNGTGI--IVIT 121
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALP---ILQRLS---EDPYGIfaLVLT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 122 PTRELALQIFGVARELMEFHSQTFGIVIGGANRRQEAEKLMKGVNMLIATPGRLLDHLQNTKG--FVFKNLKALIIDEAD 199
Cdd:cd17955 75 PTRELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSDDttKVLSRVKFLVLDEAD 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 6323947 200 RILEIGFEDEMRQIIKILPNEdRQSMLFSATQTTKVEDLARISL 243
Cdd:cd17955 155 RLLTGSFEDDLATILSALPPK-RQTLLFSATLTDALKALKELFG 197
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
264-394 |
3.34e-55 |
|
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: 181.17 E-value: 3.34e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 264 LEQGYVVCDS-DKRFLLLFSFLKRNQKKKIIVFLSSCNSVKYYAELLNYIDLPVLELHGKQKQQKRTNTFFEFCNAERGI 342
Cdd:cd18787 1 IKQLYVVVEEeEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 6323947 343 LICTDVAARGLDIPAVDWIIQFDPPDDPRDYIHRVGRTARGTKgKGKSLMFL 394
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGR-KGTAITFV 131
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
40-252 |
2.26e-51 |
|
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: 175.54 E-value: 2.26e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 40 CVEKFEELKLSQPTLKAIEKMGFTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLAFLIPAIELLHSLKFKPRNGTGI-- 117
Cdd:cd18052 41 AILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEGLTASSFSEVqe 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 118 ---IVITPTRELALQIFGVARELmefhsqTFGIVI------GGANRRQEAEKLMKGVNMLIATPGRLLDHLqnTKGFV-F 187
Cdd:cd18052 121 pqaLIVAPTRELANQIFLEARKF------SYGTCIrpvvvyGGVSVGHQIRQIEKGCHILVATPGRLLDFI--GRGKIsL 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323947 188 KNLKALIIDEADRILEIGFEDEMRQIIKIL---PNEDRQSMLFSATQTTKVEDLARISLRPGPLFINV 252
Cdd:cd18052 193 SKLKYLILDEADRMLDMGFGPEIRKLVSEPgmpSKEDRQTLMFSATFPEEIQRLAAEFLKEDYLFLTV 260
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
41-244 |
7.41e-49 |
|
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: 167.55 E-value: 7.41e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 41 VEKFEELKLSQPTLKAIEKMGFTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLAFLIPAI-ELLHSLKFKPRNGTGIIV 119
Cdd:cd17953 11 IQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFrHIKDQRPVKPGEGPIGLI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 120 ITPTRELALQIFgvaRELMEFhSQTFGI----VIGGANRRQEAEKLMKGVNMLIATPGRLLDHLQNTKGFVfKNLKA--- 192
Cdd:cd17953 91 MAPTRELALQIY---VECKKF-SKALGLrvvcVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTANNGRV-TNLRRvty 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6323947 193 LIIDEADRILEIGFEDEMRQIIK-ILPneDRQSMLFSATQTTKVEDLARISLR 244
Cdd:cd17953 166 VVLDEADRMFDMGFEPQIMKIVNnIRP--DRQTVLFSATFPRKVEALARKVLH 216
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
54-244 |
4.27e-48 |
|
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: 165.06 E-value: 4.27e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 54 LKAIEKMGFTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLAFLIPAIELLhsLKFK----PRNGTGIIVITPTRELALQ 129
Cdd:cd17961 6 LKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKI--LKAKaesgEEQGTRALILVPTRELAQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 130 IFGVARELMEF---HSQTFGIVIGGANRRQEAeKLMKGVNMLIATPGRLLDHLQNTKGFVFKNLKALIIDEADRILEIGF 206
Cdd:cd17961 84 VSKVLEQLTAYcrkDVRVVNLSASSSDSVQRA-LLAEKPDIVVSTPARLLSHLESGSLLLLSTLKYLVIDEADLVLSYGY 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 6323947 207 EDEMRQIIKILPNeDRQSMLFSATQTTKVEDLARISLR 244
Cdd:cd17961 163 EEDLKSLLSYLPK-NYQTFLMSATLSEDVEALKKLVLH 199
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
54-244 |
1.22e-47 |
|
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: 164.42 E-value: 1.22e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 54 LKAIEKMGFTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLAFLIPAIELLHSL----KFKPRNGTGIIVITPTRELALQ 129
Cdd:cd17945 2 LRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLppldEETKDDGPYALILAPTRELAQQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 130 IFGVARELmefhSQTFGI----VIGGANRRQEAEKLMKGVNMLIATPGRLLDHLQNtKGFVFKNLKALIIDEADRILEIG 205
Cdd:cd17945 82 IEEETQKF----AKPLGIrvvsIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLER-RLLVLNQCTYVVLDEADRMIDMG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6323947 206 FEDEMRQIIKILPNED-------------------RQSMLFSATQTTKVEDLARISLR 244
Cdd:cd17945 157 FEPQVTKILDAMPVSNkkpdteeaeklaasgkhryRQTMMFTATMPPAVEKIAKGYLR 214
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
54-240 |
1.72e-47 |
|
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350724 [Multi-domain] Cd Length: 197 Bit Score: 163.31 E-value: 1.72e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 54 LKAIEKMGFTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLAFLIPAI-ELLHSLKFKPRNGTGIIVITPTRELALQIFG 132
Cdd:cd17966 2 MDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIvHINAQPPLERGDGPIVLVLAPTRELAQQIQQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 133 VARELMEFHSQTFGIVIGGANRRQEAEKLMKGVNMLIATPGRLLDHLQNTKgfvfKNLKA---LIIDEADRILEIGFEDE 209
Cdd:cd17966 82 EANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGK----TNLRRvtyLVLDEADRMLDMGFEPQ 157
|
170 180 190
....*....|....*....|....*....|..
gi 6323947 210 MRQII-KILPneDRQSMLFSATQTTKVEDLAR 240
Cdd:cd17966 158 IRKIVdQIRP--DRQTLMWSATWPKEVRRLAE 187
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
54-240 |
6.83e-47 |
|
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: 161.43 E-value: 6.83e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 54 LKAIEKMGFTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLAFLIPAI-ELLHSLKFKPRNGTGIIVITPTRELALQIFG 132
Cdd:cd17952 2 LNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLvHIMDQRELEKGEGPIAVIVAPTRELAQQIYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 133 VARELmefhSQTFGI----VIGGANRRQEAEKLMKGVNMLIATPGRLLDHLQnTKGFVFKNLKALIIDEADRILEIGFED 208
Cdd:cd17952 82 EAKKF----GKAYNLrvvaVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVK-KKATNLQRVTYLVLDEADRMFDMGFEY 156
|
170 180 190
....*....|....*....|....*....|...
gi 6323947 209 EMRQII-KILPneDRQSMLFSATQTTKVEDLAR 240
Cdd:cd17952 157 QVRSIVgHVRP--DRQTLLFSATFKKKIEQLAR 187
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
44-394 |
2.07e-46 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 169.20 E-value: 2.07e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 44 FEELKLSQPTLKAIEKMGFTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLAFLIPAIE---LLHSLKFKPRNGTGIIVI 120
Cdd:PLN00206 123 FSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISrccTIRSGHPSEQRNPLAMVL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 121 TPTRELALQIFGVARELMEFHSQTFGIVIGGANRRQEAEKLMKGVNMLIATPGRLLDHLqnTKGFV-FKNLKALIIDEAD 199
Cdd:PLN00206 203 TPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLL--SKHDIeLDNVSVLVLDEVD 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 200 RILEIGFEDEMRQIIKILPNEdrQSMLFSATQTTKVEDLARiSLRPGPLFINVVPETDNSTAdgLEQGYVVCDSDKRFLL 279
Cdd:PLN00206 281 CMLERGFRDQVMQIFQALSQP--QVLLFSATVSPEVEKFAS-SLAKDIILISIGNPNRPNKA--VKQLAIWVETKQKKQK 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 280 LFSFLKRNQ--KKKIIVFLSScnsvKYYAELL-NYID----LPVLELHGKQKQQKRTNTFFEFCNAERGILICTDVAARG 352
Cdd:PLN00206 356 LFDILKSKQhfKPPAVVFVSS----RLGADLLaNAITvvtgLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRG 431
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 6323947 353 LDIPAVDWIIQFDPPDDPRDYIHRVGRTARGTKgKGKSLMFL 394
Cdd:PLN00206 432 VDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGE-KGTAIVFV 472
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
57-256 |
2.51e-46 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 160.35 E-value: 2.51e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 57 IEKMGFTTMTSVQARTIPPLLAG-RDVLGAAKTGSGKTLAFLIPAIELLHSLKFKPrngtgIIVITPTRELALQIFGVAR 135
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGKGGR-----VLVLVPTRELAEQWAEELK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 136 ELMEFHSQTFGIVIGGANRRQEAEKLMKGV-NMLIATPGRLLDHLQNtKGFVFKNLKALIIDEADRILEIGFEDEMRQII 214
Cdd:smart00487 76 KLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLEN-DKLSLSNVDLVILDEAHRLLDGGFGDQLEKLL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 6323947 215 KILPNeDRQSMLFSATQTTKVEDLARISLRpGPLFINVVPET 256
Cdd:smart00487 155 KLLPK-NVQLLLLSATPPEEIENLLELFLN-DPVFIDVGFTP 194
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
54-252 |
3.50e-45 |
|
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: 156.98 E-value: 3.50e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 54 LKAIEKMGFTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLAFLIPAIellHSLKfKPRNGTGI--IVITPTRELALQIF 131
Cdd:cd17957 2 LNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPIL---QKLG-KPRKKKGLraLILAPTRELASQIY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 132 GVARELME---FHSqtfgIVIGGANRRQEA--EKLMKGVNMLIATPGRLLDHLQNTKgFVFKNLKALIIDEADRILEIGF 206
Cdd:cd17957 78 RELLKLSKgtgLRI----VLLSKSLEAKAKdgPKSITKYDILVSTPLRLVFLLKQGP-IDLSSVEYLVLDEADKLFEPGF 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6323947 207 EDEMRQIIKILPNEDRQSMLFSATQTTKVEDLARISLRPgPLFINV 252
Cdd:cd17957 153 REQTDEILAACTNPNLQRSLFSATIPSEVEELARSVMKD-PIRIIV 197
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
54-251 |
2.55e-43 |
|
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: 152.49 E-value: 2.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 54 LKAIEKMGFTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLAFLIP----AIELLHSLKFKPRNGTGIIVITPTRELALQ 129
Cdd:cd17951 2 LKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPlimfALEQEKKLPFIKGEGPYGLIVCPSRELARQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 130 IFgvarELMEFHSQTF----------GIVIGGANRRQEAEKLMKGVNMLIATPGRLLDHLqNTKGFVFKNLKALIIDEAD 199
Cdd:cd17951 82 TH----EVIEYYCKALqeggypqlrcLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDML-NKKKINLDICRYLCLDEAD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6323947 200 RILEIGFEDEMRQIIKILPNEdRQSMLFSATQTTKVEDLARISLRPgPLFIN 251
Cdd:cd17951 157 RMIDMGFEEDIRTIFSYFKGQ-RQTLLFSATMPKKIQNFAKSALVK-PVTVN 206
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
54-244 |
1.36e-42 |
|
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: 151.25 E-value: 1.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 54 LKAIEKMGFTTMTSVQARTIPPLLAG---------RDVLGAAKTGSGKTLAFLIPAIELLhSLKFKPRngTGIIVITPTR 124
Cdd:cd17956 2 LKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQAL-SKRVVPR--LRALIVVPTK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 125 ELALQIFGVARELM-EFHSQTfGIVIGGANRRQEAEKLMKG--------VNMLIATPGRLLDHLQNTKGFVFKNLKALII 195
Cdd:cd17956 79 ELVQQVYKVFESLCkGTGLKV-VSLSGQKSFKKEQKLLLVDtsgrylsrVDILVATPGRLVDHLNSTPGFTLKHLRFLVI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323947 196 DEADRILEIGFEDEMRQIIKILPNEDR-------------------QSMLFSATQTTKVEDLARISLR 244
Cdd:cd17956 158 DEADRLLNQSFQDWLETVMKALGRPTApdlgsfgdanllersvrplQKLLFSATLTRDPEKLSSLKLH 225
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
44-251 |
2.80e-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: 149.37 E-value: 2.80e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 44 FEELKLSQPTLKAIEKMGFTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLAFLIPAIELLHSLKfkprNGTGIIVITPT 123
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKK----DVIQALILVPT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 124 RELALQIFGVARELMEFHSQTFGIVIGGANRRQEAEKLMKGVNMLIATPGRLLDhLQNTKGFVFKNLKALIIDEADRILE 203
Cdd:cd17940 77 RELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILD-LAKKGVADLSHCKTLVLDEADKLLS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 6323947 204 IGFEDEMRQIIKILPNEdRQSMLFSATQTTKVEDLARISLRpGPLFIN 251
Cdd:cd17940 156 QDFQPIIEKILNFLPKE-RQILLFSATFPLTVKNFMDRHMH-NPYEIN 201
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
54-232 |
3.98e-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: 150.08 E-value: 3.98e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 54 LKAIEKMGFTTMTSVQARTIPP-LLAGRDVLGAAKTGSGKTLAFLIPAIE-LLHSLKFKPRNGTGI----IVITPTRELA 127
Cdd:cd17946 2 LRALADLGFSEPTPIQALALPAaIRDGKDVIGAAETGSGKTLAFGIPILErLLSQKSSNGVGGKQKplraLILTPTRELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 128 LQIFGVARELMEFHSQTFGIVIGG-ANRRQEaEKLMKGVNMLIATPGRLLDHLQNTKGFV--FKNLKALIIDEADRILEI 204
Cdd:cd17946 82 VQVKDHLKAIAKYTNIKIASIVGGlAVQKQE-RLLKKRPEIVVATPGRLWELIQEGNEHLanLKSLRFLVLDEADRMLEK 160
|
170 180 190
....*....|....*....|....*....|....
gi 6323947 205 GFEDEMRQIIKILP------NEDRQSMLFSATQT 232
Cdd:cd17946 161 GHFAELEKILELLNkdragkKRKRQTFVFSATLT 194
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
54-239 |
4.98e-41 |
|
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: 146.07 E-value: 4.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 54 LKAIEKMGFTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLAFLIPAieLLHsLKFKP-----RNGTGIIVITPTRELAL 128
Cdd:cd17958 2 MKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPG--FIH-LDLQPipreqRNGPGVLVLTPTRELAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 129 QIFGvarELMEFHSQTFGIVI--GGANRRQEAEKLMKGVNMLIATPGRLLDhLQNTKGFVFKNLKALIIDEADRILEIGF 206
Cdd:cd17958 79 QIEA---ECSKYSYKGLKSVCvyGGGNRNEQIEDLSKGVDIIIATPGRLND-LQMNNVINLKSITYLVLDEADRMLDMGF 154
|
170 180 190
....*....|....*....|....*....|....
gi 6323947 207 EDEMRQI-IKILPneDRQSMLFSATQTTKVEDLA 239
Cdd:cd17958 155 EPQIRKIlLDIRP--DRQTIMTSATWPDGVRRLA 186
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
41-240 |
5.11e-41 |
|
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: 147.49 E-value: 5.11e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 41 VEKFEELKLSQPTLKAIEKMGFTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLAFLIPAIELLHSL---KFKPRNGTGI 117
Cdd:cd18051 20 IETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEQgpgESLPSESGYY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 118 ---------IVITPTRELALQIFGVARELmEFHSQTFGIVI-GGANRRQEAEKLMKGVNMLIATPGRLLDHLQNTKgFVF 187
Cdd:cd18051 100 grrkqyplaLVLAPTRELASQIYDEARKF-AYRSRVRPCVVyGGADIGQQMRDLERGCHLLVATPGRLVDMLERGK-IGL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6323947 188 KNLKALIIDEADRILEIGFEDEMRQIIK---ILPNEDRQSMLFSATQTTKVEDLAR 240
Cdd:cd18051 178 DYCKYLVLDEADRMLDMGFEPQIRRIVEqdtMPPTGERQTLMFSATFPKEIQMLAR 233
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
41-244 |
1.16e-38 |
|
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: 140.91 E-value: 1.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 41 VEKFEELKLSQPTLKAIEKMGFTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLAFLIPAIELLHSLKFKPR-NGTGIIV 119
Cdd:cd18049 23 VLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERgDGPICLV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 120 ITPTRELALQIFGVARELMEFHSQTFGIVIGGANRRQEAEKLMKGVNMLIATPGRLLDHLQNTKgfvfKNLKA---LIID 196
Cdd:cd18049 103 LAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGK----TNLRRctyLVLD 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6323947 197 EADRILEIGFEDEMRQII-KILPneDRQSMLFSATQTTKVEDLARISLR 244
Cdd:cd18049 179 EADRMLDMGFEPQIRKIVdQIRP--DRQTLMWSATWPKEVRQLAEDFLK 225
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
46-244 |
1.29e-37 |
|
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: 136.69 E-value: 1.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 46 ELKLSQPTLKAIEKMGFTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLAFLIPAIELLHSLKfkprNGTGIIVITPTRE 125
Cdd:cd17939 1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTV----RETQALVLAPTRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 126 LALQIFGVARELMEFHSQTFGIVIGGANRRQEAEKLMKGVNMLIATPGRLLDHLQNtKGFVFKNLKALIIDEADRILEIG 205
Cdd:cd17939 77 LAQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQR-RSLRTDKIKMFVLDEADEMLSRG 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 6323947 206 FEDEMRQIIKILPNEdRQSMLFSATQTTKVEDLARISLR 244
Cdd:cd17939 156 FKDQIYDIFQFLPPE-TQVVLFSATMPHEVLEVTKKFMR 193
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
44-244 |
6.61e-37 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation factor 4A-I (DDX2A) and eukaryotic initiation factor 4A-II (DDX2B) are involved in cap recognition and are required for mRNA binding to ribosome. They are DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350804 [Multi-domain] Cd Length: 201 Bit Score: 134.88 E-value: 6.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 44 FEELKLSQPTLKAIEKMGFTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLAFLIPAIELL-HSLKfkprnGTGIIVITP 122
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIdTSLK-----ATQALVLAP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 123 TRELALQIFGVARELMEFHSQTFGIVIGGANRRQEAEKLMKGVNMLIATPGRLLDHLqNTKGFVFKNLKALIIDEADRIL 202
Cdd:cd18046 76 TRELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMI-NRRYLRTDYIKMFVLDEADEML 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 6323947 203 EIGFEDEMRQIIKILPnEDRQSMLFSATQTTKVEDLARISLR 244
Cdd:cd18046 155 SRGFKDQIYDIFQKLP-PDTQVVLLSATMPNDVLEVTTKFMR 195
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
41-244 |
7.33e-36 |
|
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: 134.37 E-value: 7.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 41 VEKFEELKLSQPTLKAIEKMGFTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLAFLIPAIELLHSLKFKPR-NGTGIIV 119
Cdd:cd18050 61 VFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERgDGPICLV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 120 ITPTRELALQIFGVARELMEFHSQTFGIVIGGANRRQEAEKLMKGVNMLIATPGRLLDHLQNTKgfvfKNLKA---LIID 196
Cdd:cd18050 141 LAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGK----TNLRRctyLVLD 216
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6323947 197 EADRILEIGFEDEMRQII-KILPneDRQSMLFSATQTTKVEDLARISLR 244
Cdd:cd18050 217 EADRMLDMGFEPQIRKIVdQIRP--DRQTLMWSATWPKEVRQLAEDFLR 263
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
57-239 |
1.07e-35 |
|
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: 131.52 E-value: 1.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 57 IEKMGFTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLAFLIPAIEllhSLKFKPRNGTGIIvITPTRELALQIFGVARE 136
Cdd:cd17962 5 LKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVII---RCLTEHRNPSALI-LTPTRELAVQIEDQAKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 137 LME--FHSQTfGIVIGGANRRQEAEKLMKGVNMLIATPGRLLDHLqNTKGFVFKNLKALIIDEADRILEIGFEDEMRQII 214
Cdd:cd17962 81 LMKglPPMKT-ALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDIL-KQSSVELDNIKIVVVDEADTMLKMGFQQQVLDIL 158
|
170 180
....*....|....*....|....*
gi 6323947 215 KILPNeDRQSMLFSATQTTKVEDLA 239
Cdd:cd17962 159 ENISH-DHQTILVSATIPRGIEQLA 182
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
44-239 |
9.63e-34 |
|
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: 126.67 E-value: 9.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 44 FEELKLSQPTLKAIEKMGFTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLAFLIPAIELLHSlkfkprngtgiIVITPT 123
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIVVA-----------LILEPS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 124 RELALQIFGVARELMEFHSQ---TFGIVIGGANRRQEAEKLMKGVNMLIATPGRLLDHLQNTKgFVFKNLKALIIDEADR 200
Cdd:cd17938 70 RELAEQTYNCIENFKKYLDNpklRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGK-LDLSSVRFFVLDEADR 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 6323947 201 ILEIGFEDEMRQIIKILP----NEDR-QSMLFSAT-QTTKVEDLA 239
Cdd:cd17938 149 LLSQGNLETINRIYNRIPkitsDGKRlQVIVCSATlHSFEVKKLA 193
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
53-230 |
4.35e-33 |
|
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: 124.30 E-value: 4.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 53 TLKAIEKMGFTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLAFLIPAIELLHSLkfkpRNGTGIIVITPTRELALQI-- 130
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLE----RRHPQVLILAPTREIAVQIhd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 131 --FGVARELMEFHSQTFgivIGGANRRQEAEKLmKGVNMLIATPGRLLdHLQNTKGFVFKNLKALIIDEADRILEIGFED 208
Cdd:cd17943 77 vfKKIGKKLEGLKCEVF---IGGTPVKEDKKKL-KGCHIAVGTPGRIK-QLIELGALNVSHVRLFVLDEADKLMEGSFQK 151
|
170 180
....*....|....*....|..
gi 6323947 209 EMRQIIKILPNEdRQSMLFSAT 230
Cdd:cd17943 152 DVNWIFSSLPKN-KQVIAFSAT 172
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
44-238 |
2.99e-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: 122.19 E-value: 2.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 44 FEELKLSQPTLKAIEKMGFTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLAFlipAIELLHSLKFKPRNgTGIIVITPT 123
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATF---SISVLQCLDIQVRE-TQALILSPT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 124 RELALQIFGVARELMEFHSQTFGIVIGGANRRQEAEKLMKGVNMLIATPGRLLDHLQNtKGFVFKNLKALIIDEADRILE 203
Cdd:cd18045 77 RELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRR-RSLRTRHIKMLVLDEADEMLN 155
|
170 180 190
....*....|....*....|....*....|....*
gi 6323947 204 IGFEDEMRQIIKILPNEdRQSMLFSATQTTKVEDL 238
Cdd:cd18045 156 KGFKEQIYDVYRYLPPA-TQVVLVSATLPQDILEM 189
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
53-244 |
2.64e-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: 119.95 E-value: 2.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 53 TLKAIEKMGFTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLAFLIPAIELLHSLKFKPRNGTG--IIVITPTRELALQi 130
Cdd:cd17944 1 TIKLLQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRKRGRApkVLVLAPTRELANQ- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 131 fgVARELMEFHSQ-TFGIVIGGANRRQEAEKLMKGVNMLIATPGRLLDHLQNTKgFVFKNLKALIIDEADRILEIGFEDE 209
Cdd:cd17944 80 --VTKDFKDITRKlSVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGR-LDLTKLKHVVLDEVDQMLDMGFAEQ 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 6323947 210 MRQII----KILPNEDRQSMLFSATQTTKVEDLARISLR 244
Cdd:cd17944 157 VEEILsvsyKKDSEDNPQTLLFSATCPDWVYNVAKKYMK 195
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
54-238 |
4.87e-29 |
|
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: 114.39 E-value: 4.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 54 LKAIEKMGFTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLAFLIPAIELLHSLKFKPRNGTG---IIVITPTRELALQI 130
Cdd:cd17948 2 VEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGPFNaprGLVITPSRELAEQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 131 FGVARELmefhSQTFGIVI----GGANRRQEAEKLMKGVNMLIATPGRLLDHLqnTKGFV-FKNLKALIIDEADRILEIG 205
Cdd:cd17948 82 GSVAQSL----TEGLGLKVkvitGGRTKRQIRNPHFEEVDILVATPGALSKLL--TSRIYsLEQLRHLVLDEADTLLDDS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 6323947 206 FEDEMRQIIKILPNEDRQS------------MLFSATQTTKVEDL 238
Cdd:cd17948 156 FNEKLSHFLRRFPLASRRSentdgldpgtqlVLVSATMPSGVGEV 200
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
49-250 |
8.30e-29 |
|
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: 112.67 E-value: 8.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 49 LSQPTLKAIEKMGFTTMTSVQARTIPPLLAG--RDVLGAAKTGSGKTLAFLIPAIELLHSLKFKPRngtgIIVITPTREL 126
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQ----ALCLAPTREL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 127 ALQIFGVARELMEFHSQTFGIVIGGANRRqeAEKLMKGvNMLIATPGRLLDHLQnTKGFVFKNLKALIIDEADRILEI-G 205
Cdd:cd17963 77 ARQIGEVVEKMGKFTGVKVALAVPGNDVP--RGKKITA-QIVIGTPGTVLDWLK-KRQLDLKKIKILVLDEADVMLDTqG 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 6323947 206 FEDEMRQIIKILPNeDRQSMLFSATQTTKVEDLARiSLRPGPLFI 250
Cdd:cd17963 153 HGDQSIRIKRMLPR-NCQILLFSATFPDSVRKFAE-KIAPNANTI 195
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
275-382 |
1.53e-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: 108.84 E-value: 1.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 275 KRFLLLFSFLKRNQKKKIIVFLSSCNSVKYyAELLNYIDLPVLELHGKQKQQKRTNTFFEFCNAERGILICTDVAARGLD 354
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100
....*....|....*....|....*...
gi 6323947 355 IPAVDWIIQFDPPDDPRDYIHRVGRTAR 382
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIGRAGR 107
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
44-240 |
4.22e-27 |
|
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: 108.20 E-value: 4.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 44 FEELKLSQPTLKAIEKMGFTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLAFLipaIELLHSLKfKPRNGTGIIVITPT 123
Cdd:cd17950 4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFV---LSTLQQLE-PVDGQVSVLVICHT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 124 RELALQIfgvARELMEF----HSQTFGIVIGGANRRQEAEKLMKGV-NMLIATPGRLLDhLQNTKGFVFKNLKALIIDEA 198
Cdd:cd17950 80 RELAFQI---SNEYERFskymPNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILA-LVREKKLKLSHVKHFVLDEC 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6323947 199 DRILEigfEDEMR----QIIKILPnEDRQSMLFSATQTTKVEDLAR 240
Cdd:cd17950 156 DKMLE---QLDMRrdvqEIFRATP-HDKQVMMFSATLSKEIRPVCK 197
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
303-382 |
2.47e-24 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 96.51 E-value: 2.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 303 KYYAELLNYIDLPVLELHGKQKQQKRTNTFFEFCNAERGILICTDVAARGLDIPAVDWIIQFDPPDDPRDYIHRVGRTAR 382
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
|
| DUF4217 |
pfam13959 |
Domain of unknown function (DUF4217); This short domain is found at the C-terminus of many ... |
426-484 |
5.36e-22 |
|
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: 88.99 E-value: 5.36e-22
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 6323947 426 QSQLEKLIKSNYYLHQTAKDGYRSYLQAYASHSLKTVYQIDKLDLAKVAKSYGFPVPPK 484
Cdd:pfam13959 1 QLQLEKLVLKDRELKELAQKAFVSYVRAYSKHLAKSIFNVKKLDLGHLAKSFGLLRAPK 59
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
41-255 |
8.69e-22 |
|
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: 93.93 E-value: 8.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 41 VEKFEELKLSQPTLKAIEKMGFTTMTSVQARTIPPLLAG--RDVLGAAKTGSGKTLAFLIPAIELLHSLKFKPRngtgII 118
Cdd:cd18048 17 VKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQ----CL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 119 VITPTRELALQIFGVARELMEFHSQTFGIVIGGANRRQEAEKLMKgvNMLIATPGRLLDHLQNTKGFVFKNLKALIIDEA 198
Cdd:cd18048 93 CLSPTFELALQTGKVVEEMGKFCVGIQVIYAIRGNRPGKGTDIEA--QIVIGTPGTVLDWCFKLRLIDVTNISVFVLDEA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6323947 199 DRILEI-GFEDEMRQIIKILPNEdRQSMLFSATQTTKVEDLARiSLRPGPLFINVVPE 255
Cdd:cd18048 171 DVMINVqGHSDHSVRVKRSMPKE-CQMLLFSATFEDSVWAFAE-RIVPDPNIIKLKKE 226
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
78-417 |
6.20e-21 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 95.86 E-value: 6.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 78 AGRDVLGAAKTGSGKTLAflipAIELLHSLKFKPRngtgIIVITPTRELALQIfgvARELMEFhsqtFGIVIGGANRRQE 157
Cdd:COG1061 99 GGGRGLVVAPTGTGKTVL----ALALAAELLRGKR----VLVLVPRRELLEQW---AEELRRF----LGDPLAGGGKKDS 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 158 AEklmkgvNMLIATPGRL-----LDHLQNTKGFVfknlkalIIDEADRIleigFEDEMRQIIKILPNEDRqsMLFSATqt 232
Cdd:COG1061 164 DA------PITVATYQSLarrahLDELGDRFGLV-------IIDEAHHA----GAPSYRRILEAFPAAYR--LGLTAT-- 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 233 tkvedLARISLRPGPL--FINVVPETDnsTADGLEQGYVV-----------------CDSDKRFL--LLFSFLKRNQK-- 289
Cdd:COG1061 223 -----PFRSDGREILLflFDGIVYEYS--LKEAIEDGYLAppeyygirvdltderaeYDALSERLreALAADAERKDKil 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 290 ----------KKIIVFLSSCNSVKYYAELLNYIDLPVLELHGKQKQQKRTNTFFEFCNAERGILICTDVAARGLDIPAVD 359
Cdd:COG1061 296 rellrehpddRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLD 375
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 6323947 360 WIIQFDPPDDPRDYIHRVGRTARGTKGKGKSLMF-LTPNELGFLRYLKASKVPLNEYEF 417
Cdd:COG1061 376 VAILLRPTGSPREFIQRLGRGLRPAPGKEDALVYdFVGNDVPVLEELAKDLRDLAGYRV 434
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
79-230 |
7.21e-18 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 80.14 E-value: 7.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 79 GRDVLGAAKTGSGKTLAFLIPAIELLHSlkfkprNGTGIIVITPTRELALQifgVARELMEF--HSQTFGIVIGGANRRQ 156
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLLK------KGKKVLVLVPTKALALQ---TAERLRELfgPGIRVAVLVGGSSAEE 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323947 157 EAEKLMKGVNMLIATPGRLLDHLQNTKGFVFKNLKALIIDEADRILEIGFE-DEMRQIIKILPNEDRQSMLFSAT 230
Cdd:cd00046 72 REKNKLGDADIIIATPDMLLNLLLREDRLFLKDLKLIIVDEAHALLIDSRGaLILDLAVRKAGLKNAQVILLSAT 146
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
42-230 |
1.46e-16 |
|
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: 78.22 E-value: 1.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 42 EKFEELKLSQPTLKAIEKMGFTTMTSVQARTIPPLLAG--RDVLGAAKTGSGKTLAFLIPAIELLH-SLKFkprngTGII 118
Cdd:cd18047 1 KSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEpANKY-----PQCL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 119 VITPTRELALQIFGVARELMEFHSQtfgIVIGGANRRQEAEKLMK-GVNMLIATPGRLLDHLQNTKGFVFKNLKALIIDE 197
Cdd:cd18047 76 CLSPTYELALQTGKVIEQMGKFYPE---LKLAYAVRGNKLERGQKiSEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDE 152
|
170 180 190
....*....|....*....|....*....|....
gi 6323947 198 ADRILEI-GFEDEMRQIIKILPnEDRQSMLFSAT 230
Cdd:cd18047 153 ADVMIATqGHQDQSIRIQRMLP-RNCQMLLFSAT 185
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
56-230 |
3.43e-15 |
|
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: 75.49 E-value: 3.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 56 AIEKMGFTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLAFLIPAIELL----------HSLKFKPRNGTGI---IVITP 122
Cdd:cd17965 38 AIKKLLKTLMRKVTKQTSNEEPKLEVFLLAAETGSGKTLAYLAPLLDYLkrqeqepfeeAEEEYESAKDTGRprsVILVP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 123 TRELALQIFGVARELMEFHSqtFGI-VIG---GANRRQEAEKLMKGVNMLIATPGRLLDhLQNTKGFVFKNLKALIIDEA 198
Cdd:cd17965 118 THELVEQVYSVLKKLSHTVK--LGIkTFSsgfGPSYQRLQLAFKGRIDILVTTPGKLAS-LAKSRPKILSRVTHLVVDEA 194
|
170 180 190
....*....|....*....|....*....|..
gi 6323947 199 DRILEIGFEDEMRQIIKILPNEdRQSMLFSAT 230
Cdd:cd17965 195 DTLFDRSFLQDTTSIIKRAPKL-KHLILCSAT 225
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
279-387 |
2.22e-12 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 69.37 E-value: 2.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 279 LLFSFLKRNQKKKIIVFLSSCNSVKYYAELLNYIDLPVLELHGK----------QKQQKRTNTffEFCNAERGILICTDV 348
Cdd:COG1111 343 ILKEQLGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGQaskegdkgltQKEQIEILE--RFRAGEFNVLVATSV 420
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 6323947 349 AARGLDIPAVDWIIQFDP-PDDPRdYIHRVGRTARGTKGK 387
Cdd:COG1111 421 AEEGLDIPEVDLVIFYEPvPSEIR-SIQRKGRTGRKREGR 459
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
342-393 |
7.70e-12 |
|
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: 60.80 E-value: 7.70e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 6323947 342 ILICTDVAARGLDIPAVDWIIQFDPPDDPRDYIHRVGRTARGTKGKGKSLMF 393
Cdd:cd18785 25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVILF 76
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
291-387 |
2.54e-11 |
|
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: 61.60 E-value: 2.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 291 KIIVFLSSCNSVKYYAELLNYIDLPVL-----------ELHG-KQKQQKRTntFFEFCNAERGILICTDVAARGLDIPAV 358
Cdd:cd18801 32 RVIIFSEFRDSAEEIVNFLSKIRPGIRatrfigqasgkSSKGmSQKEQKEV--IEQFRKGGYNVLVATSIGEEGLDIGEV 109
|
90 100
....*....|....*....|....*....
gi 6323947 359 DWIIQFDPPDDPRDYIHRVGRTARGTKGK 387
Cdd:cd18801 110 DLIICYDASPSPIRMIQRMGRTGRKRQGR 138
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
79-197 |
2.81e-11 |
|
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: 61.83 E-value: 2.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 79 GRDVLGAAKTGSGKTLAFLIPAielLHSLKFKPRNGTGIIVITPTRELALQIFGVARELMEfhSQTFGIVIGG------A 152
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPA---LSSLADEPEKGVQVLYISPLKALINDQERRLEEPLD--EIDLEIPVAVrhgdtsQ 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 6323947 153 NRRQEAEKLMKGVnmLIATPGRLLDHLQNTKGF-VFKNLKALIIDE 197
Cdd:cd17922 76 SEKAKQLKNPPGI--LITTPESLELLLVNKKLReLFAGLRYVVVDE 119
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
284-392 |
1.71e-10 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 63.35 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 284 LKRNQKKKIIVFLSSCNSVKYYAELLNYIDLPVLELHGK----------QKQQKRTNTffEFCNAERGILICTDVAARGL 353
Cdd:PRK13766 360 LGKNPDSRIIVFTQYRDTAEKIVDLLEKEGIKAVRFVGQaskdgdkgmsQKEQIEILD--KFRAGEFNVLVSTSVAEEGL 437
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 6323947 354 DIPAVDWIIQFDP-PDDPRdYIHRVGRTARGTKGKGKSLM 392
Cdd:PRK13766 438 DIPSVDLVIFYEPvPSEIR-SIQRKGRTGRQEEGRVVVLI 476
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
49-198 |
6.06e-10 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 61.78 E-value: 6.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 49 LSQPTLKAIEKMGFTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLAFLIPAIELLHslkfKPRNGTgIIVITPTRELAL 128
Cdd:COG1205 41 LPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALL----EDPGAT-ALYLYPTKALAR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 129 -QifgvARELMEFhSQTFGIVIG-----GANRRQEAEKLMKGVNMLIATP-----GrLLDHLQNTKGFvFKNLKALIIDE 197
Cdd:COG1205 116 dQ----LRRLREL-AEALGLGVRvatydGDTPPEERRWIREHPDIVLTNPdmlhyG-LLPHHTRWARF-FRNLRYVVIDE 188
|
.
gi 6323947 198 A 198
Cdd:COG1205 189 A 189
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
62-127 |
1.18e-09 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 60.89 E-value: 1.18e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323947 62 FTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLA-FLIPAIELL-HSLKFKPRNGTGIIVITPTRELA 127
Cdd:COG1201 22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTLAaFLPALDELArRPRPGELPDGLRVLYISPLKALA 89
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
43-315 |
4.01e-09 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 58.75 E-value: 4.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 43 KFEELKLSqPTLKAIEKMGFTTMTSVQARTIPP-LLAGRDVLGAAKTGSGKTL-AFLipAIelLHSLKfkpRNGTgIIVI 120
Cdd:COG1204 2 KVAELPLE-KVIEFLKERGIEELYPPQAEALEAgLLEGKNLVVSAPTASGKTLiAEL--AI--LKALL---NGGK-ALYI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 121 TPTRELALQIFgvaRELMEFHSQtFGIVIGGA--NRRQEAEKLMKgVNMLIATPGRlLDHLQNTKGFVFKNLKALIIDEA 198
Cdd:COG1204 73 VPLRALASEKY---REFKRDFEE-LGIKVGVStgDYDSDDEWLGR-YDILVATPEK-LDSLLRNGPSWLRDVDLVVVDEA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 199 ------DR--ILEIgfedemrQIIKILPNEDRQSMLF-SATqTTKVEDLAR--------ISLRPGPLFINVVPETDNSTA 261
Cdd:COG1204 147 hliddeSRgpTLEV-------LLARLRRLNPEAQIVAlSAT-IGNAEEIAEwldaelvkSDWRPVPLNEGVLYDGVLRFD 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 6323947 262 DgleqGYVVCDSDKRFLLLFSFLKRNQkkkIIVFLSSCNSV----KYYAELLNYIDLP 315
Cdd:COG1204 219 D----GSRRSKDPTLALALDLLEEGGQ---VLVFVSSRRDAeslaKKLADELKRRLTP 269
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
51-237 |
4.77e-09 |
|
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: 56.39 E-value: 4.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 51 QPTLKaiEKMGFTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLAFLIPAieLLhslkfkpRNGTGiIVITPTreLAL-- 128
Cdd:cd17920 1 EQILK--EVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPA--LL-------LDGVT-LVVSPL--ISLmq 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 129 -QIFGVAR---ELMEFHSQTfgiviGGANRRQEAEKLMKG-VNMLIATPGRL--------LDHLQNTKGFVFknlkaLII 195
Cdd:cd17920 67 dQVDRLQQlgiRAAALNSTL-----SPEEKREVLLRIKNGqYKLLYVTPERLlspdflelLQRLPERKRLAL-----IVV 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 6323947 196 DEADRILEIG--FEDEMRQIIKILPNEDR-QSMLFSATQTTKVED 237
Cdd:cd17920 137 DEAHCVSQWGhdFRPDYLRLGRLRRALPGvPILALTATATPEVRE 181
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
69-198 |
8.98e-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: 54.90 E-value: 8.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 69 QARTIPPLLAGRDVLGAAKTGSGKTLAFLIPAIELLHSlkfkpRNGTGIIVITPTRELALQIFGVARELMEFHSQ--TFG 146
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLR-----DPGSRALYLYPTKALAQDQLRSLRELLEQLGLgiRVA 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 6323947 147 IVIGGANRRQEAEKLMKGVNMLIATPGRL----LDHLQNTKGFvFKNLKALIIDEA 198
Cdd:cd17923 80 TYDGDTPREERRAIIRNPPRILLTNPDMLhyalLPHHDRWARF-LRNLRYVVLDEA 134
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
64-198 |
4.90e-08 |
|
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: 53.03 E-value: 4.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 64 TMTSVQARTIPPL-LAGRDVLGAAKTGSGKTLAFLIPAIELLHSLKFKprngtgIIVITPTRELALQIFGVARELMEFHS 142
Cdd:cd17921 1 LLNPIQREALRALyLSGDSVLVSAPTSSGKTLIAELAILRALATSGGK------AVYIAPTRALVNQKEADLRERFGPLG 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 6323947 143 QTFGIVIGGA--NRRQEAEKlmkgvNMLIATPGRLLDHLQNTKGFVFKNLKALIIDEA 198
Cdd:cd17921 75 KNVGLLTGDPsvNKLLLAEA-----DILVATPEKLDLLLRNGGERLIQDVRLVVVDEA 127
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
69-454 |
6.04e-08 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 55.15 E-value: 6.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 69 QARTIPPLLAGRDVLGAAKTGSGKTLAFLIPAieLLhslkfkpRNGTGiIVITPtreL---------ALQIFGVARELMe 139
Cdd:COG0514 22 QEEIIEAVLAGRDALVVMPTGGGKSLCYQLPA--LL-------LPGLT-LVVSP---LialmkdqvdALRAAGIRAAFL- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 140 fHSQtfgivIGGANRRQEAEKLMKG-VNMLIATPGRL-----LDHLQNTKgfvfknLKALIIDEADRILEIG--FEDEMR 211
Cdd:COG0514 88 -NSS-----LSAEERREVLRALRAGeLKLLYVAPERLlnprfLELLRRLK------ISLFAIDEAHCISQWGhdFRPDYR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 212 QI---IKILPNedRQSMLFSATQTTKV-EDLA-----------RISL-RPGpLFINVVPetdnstadgleqgyvvCDSDK 275
Cdd:COG0514 156 RLgelRERLPN--VPVLALTATATPRVrADIAeqlgledprvfVGSFdRPN-LRLEVVP----------------KPPDD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 276 RFLLLFSFLKRNQKKKIIVFlssCNSVK---YYAELLNYIDLPVLELHGKQKQQKRTNTFFEFCNAERGILICTdVA-AR 351
Cdd:COG0514 217 KLAQLLDFLKEHPGGSGIVY---CLSRKkveELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGM 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 352 GLDIPAVDWIIQFDPPDDPRDYIHRVGRTARGTKgKGKSLMFLTPNELGFLRYLKASKVPlneyefPENKIANVQSQLEK 431
Cdd:COG0514 293 GIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGL-PAEALLLYGPEDVAIQRFFIEQSPP------DEERKRVERAKLDA 365
|
410 420
....*....|....*....|...
gi 6323947 432 LIKsnyYLHqtAKDGYRSYLQAY 454
Cdd:COG0514 366 MLA---YAE--TTGCRRQFLLRY 383
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
49-403 |
1.89e-07 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 53.56 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 49 LSQPTLKaiEKMGFTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLAFLIPAIellhslkfkPRNGTgIIVITPTREL-- 126
Cdd:PRK11057 12 LAKQVLQ--ETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPAL---------VLDGL-TLVVSPLISLmk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 127 ----ALQIFGVARELMEfHSQTfgivigganrRQEAEKLMKG-----VNMLIATPGRL-----LDHLQNTkgfvfkNLKA 192
Cdd:PRK11057 80 dqvdQLLANGVAAACLN-STQT----------REQQLEVMAGcrtgqIKLLYIAPERLmmdnfLEHLAHW------NPAL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 193 LIIDEADRILEIG--FEDEMR---QIIKILPNEDRQSMLFSATQTTKVEDLARISLRPgplfinvvPETDNSTADGLEQG 267
Cdd:PRK11057 143 LAVDEAHCISQWGhdFRPEYAalgQLRQRFPTLPFMALTATADDTTRQDIVRLLGLND--------PLIQISSFDRPNIR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 268 YVVCDSDKRFLLLFSFLKRNQKKKIIVFLSSCNSVKYYAELLNYIDLPVLELHGKQKQQKRTNTFFEFCNAERGILICTD 347
Cdd:PRK11057 215 YTLVEKFKPLDQLMRYVQEQRGKSGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATV 294
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 6323947 348 VAARGLDIPAVDWIIQFDPPDDPRDYIHRVGRTARgtKG-KGKSLMFLTPNELGFLR 403
Cdd:PRK11057 295 AFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGR--DGlPAEAMLFYDPADMAWLR 349
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
88-362 |
2.93e-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: 52.78 E-value: 2.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 88 TGSGKTLAFLIPAIELLhslkfKPRNGTGIIVITPTRELALQIFGVARE-----LMEFHSQTFGIVIGGANRRQEAEK-- 160
Cdd:COG1203 156 TGGGKTEAALLFALRLA-----AKHGGRRIIYALPFTSIINQTYDRLRDlfgedVLLHHSLADLDLLEEEEEYESEARwl 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 161 --LMKGVNM--LIATPGRLLDHLQNTKGFVFKNL-----KALIIDEAD-----------RILEI----G----------- 205
Cdd:COG1203 231 klLKELWDApvVVTTIDQLFESLFSNRKGQERRLhnlanSVIILDEVQayppymlalllRLLEWlknlGgsvilmtatlp 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 206 --FEDEMRQIIKILPNEDRQSMLFSATQTTKvedlaRISLRPGPLfinvvpeTDNSTADGLEQgyvvcdsdkrflllfsf 283
Cdd:COG1203 311 plLREELLEAYELIPDEPEELPEYFRAFVRK-----RVELKEGPL-------SDEELAELILE----------------- 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 284 lKRNQKKKIIVFlssCNSVK----YYAELLNYI-DLPVLELHG------KQKQQKRTNTFFEfcNAERGILICTDVAARG 352
Cdd:COG1203 362 -ALHKGKSVLVI---VNTVKdaqeLYEALKEKLpDEEVYLLHSrfcpadRSEIEKEIKERLE--RGKPCILVSTQVVEAG 435
|
330
....*....|
gi 6323947 353 LDIPAvDWII 362
Cdd:COG1203 436 VDIDF-DVVI 444
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
86-396 |
7.08e-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: 7.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 86 AKTGSGKTLAFLIPAIELLHSLKFkprngTGIIVITPTRELalqIFGVARELMEFHSQTFGIVIGGANRR---------- 155
Cdd:cd09639 6 APTGYGKTEAALLWALHSLKSQKA-----DRVIIALPTRAT---INAMYRRAKEAFGETGLYHSSILSSRikemgdseef 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 156 -QEAEKLMKGVNMLIATPGRL--LDHLQ----NTKGFVFKNLKA-----LIIDEADRIleigfEDEMRQII----KILPN 219
Cdd:cd09639 78 eHLFPLYIHSNDTLFLDPITVctIDQVLksvfGEFGHYEFTLASianslLIFDEVHFY-----DEYTLALIlavlEVLKD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 220 EDRQSMLFSATQTtkvEDLARISLRPGPLFINVVPETDNSTadglEQGYVVCDSDKRFllLFSFLKR-----NQKKKIIV 294
Cdd:cd09639 153 NDVPILLMSATLP---KFLKEYAEKIGYVEENEPLDLKPNE----RAPFIKIESDKVG--EISSLERllefiKKGGSVAI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 295 FlssCNSVK----YYAELL-NYIDLPVLELHG----KQKQQKRTNTFFEFCNAERGILICTDVAARGLDIpAVDWII-QF 364
Cdd:cd09639 224 I---VNTVDraqeFYQQLKeKGPEEEIMLIHSrfteKDRAKKEAELLLEFKKSEKFVIVATQVIEASLDI-SVDVMItEL 299
|
330 340 350
....*....|....*....|....*....|..
gi 6323947 365 DPPDdprDYIHRVGRTARGTKGKGKSLMFLTP 396
Cdd:cd09639 300 APID---SLIQRLGRLHRYGEKNGEEVYIITD 328
|
|
| cas3_core |
TIGR01587 |
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ... |
86-389 |
2.56e-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: 49.37 E-value: 2.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 86 AKTGSGKTLAFLIPAielLHSLKFKPRNGtgIIVITPTRELALQIFGVARELmeFHSQTFGIVIGGANRR---------- 155
Cdd:TIGR01587 6 APTGYGKTEAALLWA---LHSIKSQKADR--VIIALPTRATINAMYRRAKEL--FGSELVGLHHSSSFSRikemgdseef 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 156 -QEAEKLMKGVNMLIATPGRL--LDHLQ----NTKGFVFKNLKA-----LIIDEADRIleigfEDEMRQII----KILPN 219
Cdd:TIGR01587 79 eHLFPLYIHSNDKLFLDPITVctIDQVLksvfGEFGHYEFTLASianslLIFDEVHFY-----DEYTLALIlavlEVLKD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 220 EDRQSMLFSATQTtkvEDLARISLRPGPLFINVVPETDNstADGLE-QGYVVCDSDKRFLllFSFLKR-----NQKKKII 293
Cdd:TIGR01587 154 NDVPILLMSATLP---KFLKEYAEKIGYVEFNEPLDLKE--ERRFEnHRFILIESDKVGE--ISSLERllefiKKGGSIA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 294 VFlssCNSVK----YYAELLNYI-DLPVLELHG----KQKQQKRTNTFFEFCNA-ERGILICTDVAARGLDIpAVDWII- 362
Cdd:TIGR01587 227 II---VNTVDraqeFYQQLKEKApEEEIILYHSrfteKDRAKKEAELLREMKKSnEKFVIVATQVIEASLDI-SADVMIt 302
|
330 340
....*....|....*....|....*..
gi 6323947 363 QFDPPDdprDYIHRVGRTARGTKGKGK 389
Cdd:TIGR01587 303 ELAPID---SLIQRLGRLHRYGRKIGE 326
|
|
| mfd |
TIGR00580 |
transcription-repair coupling factor (mfd); All proteins in this family for which functions ... |
113-365 |
2.96e-06 |
|
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: 50.05 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 113 NGTGIIVITPTRELALQIFGVARELMefhsQTFGIVIGGANR---RQEAEKLMKG-----VNMLIATpGRLLdhlqnTKG 184
Cdd:TIGR00580 499 DGKQVAVLVPTTLLAQQHFETFKERF----ANFPVTIELLSRfrsAKEQNEILKElasgkIDILIGT-HKLL-----QKD 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 185 FVFKNLKALIIDEADRileigFEDEMRQIIKIL-PNEDRQSMlfSAT--------QTTKVEDLARISLRPG---PLFINV 252
Cdd:TIGR00580 569 VKFKDLGLLIIDEEQR-----FGVKQKEKLKELrTSVDVLTL--SATpiprtlhmSMSGIRDLSIIATPPEdrlPVRTFV 641
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 253 VPETDNSTADGLEqgyvvcdsdkrflllfSFLKRNQKkkiiVFL--SSCNSVKYYAELLNYI--DLPVLELHGKQKQQKR 328
Cdd:TIGR00580 642 MEYDPELVREAIR----------------RELLRGGQ----VFYvhNRIESIEKLATQLRELvpEARIAIAHGQMTENEL 701
|
250 260 270
....*....|....*....|....*....|....*..
gi 6323947 329 TNTFFEFCNAERGILICTDVAARGLDIPAVDWIIQFD 365
Cdd:TIGR00580 702 EEVMLEFYKGEFQVLVCTTIIETGIDIPNANTIIIER 738
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
75-200 |
3.65e-06 |
|
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: 47.81 E-value: 3.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 75 PLLAGRDVLGAAKTGSGKTLAFLIPAIEllHSLKFKPRNGTGIIVITPTRELALQIFGVARELMEFH-SQTFGivIGGAN 153
Cdd:cd17927 13 PALKGKNTIICLPTGSGKTFVAVLICEH--HLKKFPAGRKGKVVFLANKVPLVEQQKEVFRKHFERPgYKVTG--LSGDT 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 6323947 154 RRQE-AEKLMKGVNMLIATPGRLLDHLQNTKGFVFKNLKALIIDEADR 200
Cdd:cd17927 89 SENVsVEQIVESSDVIIVTPQILVNDLKSGTIVSLSDFSLLVFDECHN 136
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
80-230 |
1.02e-05 |
|
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350676 [Multi-domain] Cd Length: 180 Bit Score: 46.26 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 80 RDVLGAAKTGSGKTLAFLIPAIELLhslkfkpRNGTGIIVITPTRELALQIFGVARELM-EFHSQtfgIVIGGANrrqea 158
Cdd:cd17918 37 MDRLLSGDVGSGKTLVALGAALLAY-------KNGKQVAILVPTEILAHQHYEEARKFLpFINVE---LVTGGTK----- 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6323947 159 EKLMKGVNMLIATPGRLldHLQNTkgfvFKNLKALIIDEADRileigFEDEMRQIIKILPNEDrqSMLFSAT 230
Cdd:cd17918 102 AQILSGISLLVGTHALL--HLDVK----FKNLDLVIVDEQHR-----FGVAQREALYNLGATH--FLEATAT 160
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
342-382 |
1.04e-05 |
|
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: 45.27 E-value: 1.04e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 6323947 342 ILICTDVAARGLDIPAVDWIIQFDPPDDPRDYIHRVGRtAR 382
Cdd:cd18802 93 LLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-AR 132
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
88-230 |
1.47e-05 |
|
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: 44.99 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 88 TGSGKTLaFLIPAIELLHSLKfkprngtgIIVITPTRELALQIfgvARELMEFHSQTFGIVIGGanrrqEAEKLMKGVNM 167
Cdd:cd17926 27 TGSGKTL-TALALIAYLKELR--------TLIVVPTDALLDQW---KERFEDFLGDSSIGLIGG-----GKKKDFDDANV 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6323947 168 LIATPgRLLDHLQNTKGFVFKNLKALIIDEADRILEIGFEdemrqiiKILPNEDRQSML-FSAT 230
Cdd:cd17926 90 VVATY-QSLSNLAEEEKDLFDQFGLLIVDEAHHLPAKTFS-------EILKELNAKYRLgLTAT 145
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
291-395 |
1.57e-05 |
|
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a 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: 350176 [Multi-domain] Cd Length: 153 Bit Score: 44.93 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 291 KIIVFLSSCNSVKYYAELLNyidLPVLelHGKQKQQKRTNTFFEFCNAERGILICTDVAARGLDIPAVDWIIQFD-PPDD 369
Cdd:cd18789 51 KIIVFTDNVEALYRYAKRLL---KPFI--TGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLPEANVAIQISgHGGS 125
|
90 100
....*....|....*....|....*.
gi 6323947 370 PRDYIHRVGRTARGTKGKGKSLMFLT 395
Cdd:cd18789 126 RRQEAQRLGRILRPKKGGGKNAFFYS 151
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
86-198 |
1.67e-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: 45.36 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 86 AKTGSGKTLAFLIPAieLLHSLKFKPRngtGIIVITPTRELALQIFGVARELM----------EFHS--------QTFGI 147
Cdd:cd17930 8 APTGSGKTEAALLWA--LKLAARGGKR---RIIYALPTRATINQMYERIREILgrlddedkvlLLHSkaalelleSDEEP 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 6323947 148 VIGGANRRQEAEKLMKGVN--MLIATPGRLLDHLQNTKGFVFK--NL--KALIIDEA 198
Cdd:cd17930 83 DDDPVEAVDWALLLKRSWLapIVVTTIDQLLESLLKYKHFERRlhGLanSVVVLDEV 139
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
269-378 |
1.85e-05 |
|
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350180 [Multi-domain] Cd Length: 135 Bit Score: 44.39 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 269 VVCDSDKRFLLLFSFLKRNQKK--KIIVFlssCNSVK---YYAELLNYIDLPVLELHGKQKQQKRTNTFFEF--CNAERG 341
Cdd:cd18793 5 IEEVVSGKLEALLELLEELREPgeKVLIF---SQFTDtldILEEALRERGIKYLRLDGSTSSKERQKLVDRFneDPDIRV 81
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 6323947 342 ILICTDVAARGLDIPAVDWIIQFDPPDDP------RDYIHRVG 378
Cdd:cd18793 82 FLLSTKAGGVGLNLTAANRVILYDPWWNPaveeqaIDRAHRIG 124
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
61-254 |
1.27e-04 |
|
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: 43.01 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 61 GFTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLAFLIPAiellhslKFKPRNGTGI-IVITPTreLAL---QIFGVARE 136
Cdd:cd18018 9 GHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPA-------LLLRRRGPGLtLVVSPL--IALmkdQVDALPRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 137 LMefhsqtfGIVIGGANRRQEAEKLMKGVNM-----LIATPGRLldhlqNTKGFVF-----KNLKALIIDEADRILEIGF 206
Cdd:cd18018 80 IK-------AAALNSSLTREERRRILEKLRAgevkiLYVSPERL-----VNESFREllrqtPPISLLVVDEAHCISEWSH 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 6323947 207 E---DEMR--QIIKILPNEdRQSMLFSATQTTKV-EDLARIsLRPGPLFINVVP 254
Cdd:cd18018 148 NfrpDYLRlcRVLRELLGA-PPVLALTATATKRVvEDIASH-LGIPESGVVRGP 199
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
88-224 |
1.40e-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: 43.02 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 88 TGSGKTL--AFLIPaiELLHSLKFKPRNGTGIIVITPTRELALQIFGVAREL-----MEFHSQTfGIVIGGANRRQEAek 160
Cdd:cd18034 25 TGSGKTLiaVMLIK--EMGELNRKEKNPKKRAVFLVPTVPLVAQQAEAIRSHtdlkvGEYSGEM-GVDKWTKERWKEE-- 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323947 161 lMKGVNMLIATPGRLLDHLQNtkGFV-FKNLKALIIDEADRIleIGfEDEMRQIIKILPNEDRQS 224
Cdd:cd18034 100 -LEKYDVLVMTAQILLDALRH--GFLsLSDINLLIFDECHHA--TG-DHPYARIMKEFYHLEGRT 158
|
|
| VirD4 |
COG3505 |
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, ... |
82-137 |
1.11e-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: 41.51 E-value: 1.11e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 6323947 82 VLGAAKTGSGKTLAFLIPAIELLHslkfkprNGTGIIVITPTRELALQIFGVAREL 137
Cdd:COG3505 2 VLVIGPTGSGKTVGLVIPNLTQLA-------RGESVVVTDPKGDLAELTAGFRRRA 50
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
86-197 |
1.56e-03 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 41.45 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 86 AKTGSGKTLAFLIPAIELL------HSLKFKPRNGTGIIVITPT--------RELALQIFGVARELMEFHSQTFGIVIG- 150
Cdd:PRK09751 3 APTGSGKTLAAFLYALDRLfreggeDTREAHKRKTSRILYISPIkalgtdvqRNLQIPLKGIADERRRRGETEVNLRVGi 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 6323947 151 --GANRRQEAEKLMKG-VNMLIATPGRLLDHLQNTKGFVFKNLKALIIDE 197
Cdd:PRK09751 83 rtGDTPAQERSKLTRNpPDILITTPESLYLMLTSRARETLRGVETVIIDE 132
|
|
| DEXHc_TRCF |
cd17991 |
DEXH/Q-box helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
113-200 |
3.00e-03 |
|
DEXH/Q-box 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 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: 350749 [Multi-domain] Cd Length: 193 Bit Score: 39.09 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 113 NGTGIIVITPTRELALQIFGVARELMEfhsqTFGIVIGGANR---RQEAEKLMKG-----VNMLIATpGRLLdhlqnTKG 184
Cdd:cd17991 63 SGKQVAVLVPTTLLAQQHYETFKERFA----NFPVNVELLSRfttAAEQREILEGlkegkVDIVIGT-HRLL-----SKD 132
|
90
....*....|....*.
gi 6323947 185 FVFKNLKALIIDEADR 200
Cdd:cd17991 133 VEFKNLGLLIIDEEQR 148
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
62-127 |
5.28e-03 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 39.48 E-value: 5.28e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323947 62 FTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLAFLIPAIELLHSL--KFKPRNGTGIIVITPTRELA 127
Cdd:PRK13767 30 FGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTLAAFLAIIDELFRLgrEGELEDKVYCLYVSPLRALN 97
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
76-200 |
5.50e-03 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 39.54 E-value: 5.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 76 LLAGRDVLGAAKTGSGKTLAflipAIELLH-SLkfkpRNGTGIIVITPTRELALQIFgvaRELME-FHSQTFGIVIGGAN 153
Cdd:COG4581 37 LEAGRSVLVAAPTGSGKTLV----AEFAIFlAL----ARGRRSFYTAPIKALSNQKF---FDLVErFGAENVGLLTGDAS 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 6323947 154 RRQEA-------EKLMkgvNMLIATpGRLLDHLqntkGFVfknlkalIIDE----ADR 200
Cdd:COG4581 106 VNPDApivvmttEILR---NMLYRE-GADLEDV----GVV-------VMDEfhylADP 148
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
290-387 |
6.75e-03 |
|
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350186 [Multi-domain] Cd Length: 116 Bit Score: 36.38 E-value: 6.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 290 KKIIVFLSSCNSVKYYAELLNYIDLPVLELHGKQKQQKRTNTF---FEFCNAERGILICTDVAARGLDIPAVDWIIQFDP 366
Cdd:cd18799 7 IKTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGDEAlilLFFGELKPPILVTVDLLTTGVDIPEVDNVVFLRP 86
|
90 100
....*....|....*....|.
gi 6323947 367 PDDPRDYIHRVGRTARGTKGK 387
Cdd:cd18799 87 TESRTLFLQMLGRGLRLHEGK 107
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
88-230 |
6.90e-03 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 37.27 E-value: 6.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 88 TGSGKTL-AFLIpaIELLHSLKFKPRngtgIIVITPTRELALQIFGVARELMEFHSQTFGIVIGGANRRQEAEKlmkgvN 166
Cdd:pfam04851 32 TGSGKTLtAAKL--IARLFKKGPIKK----VLFLVPRKDLLEQALEEFKKFLPNYVEIGEIISGDKKDESVDDN-----K 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6323947 167 MLIATPGRLLDHL-QNTKGFVFKNLKALIIDEADRileiGFEDEMRQIIKILPNedrqSML--FSAT 230
Cdd:pfam04851 101 IVVTTIQSLYKALeLASLELLPDFFDVIIIDEAHR----SGASSYRNILEYFKP----AFLlgLTAT 159
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
258-380 |
7.52e-03 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 39.05 E-value: 7.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 258 NSTADGLEQGYVVCDSDKRFLLLFSFLK--RNQKKKIIVFLSSCNSVKYYAELLNYIDLPVLELHGKQKQQKRTNTFFEF 335
Cdd:COG0553 516 SHPALLLEEGAELSGRSAKLEALLELLEelLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRF 595
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 6323947 336 cNAERG---ILICTDVAARGLDIPAVDWIIQFDPPDDP------RDYIHRVGRT 380
Cdd:COG0553 596 -QEGPEapvFLISLKAGGEGLNLTAADHVIHYDLWWNPaveeqaIDRAHRIGQT 648
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
66-197 |
7.71e-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: 37.72 E-value: 7.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323947 66 TSVQARTIPPLL-AGRDVLGAAKTGSGKTLAFLIPAIELLHSLKFKPRNGTGIIVITPTRELALQIFGVARELMEFHSQT 144
Cdd:cd18023 3 NRIQSEVFPDLLySDKNFVVSAPTGSGKTVLFELAILRLLKERNPLPWGNRKVVYIAPIKALCSEKYDDWKEKFGPLGLS 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 6323947 145 FGIVIGGanrrQEAEKL--MKGVNMLIATPGR--LLDHLQNTKGFVFKNLKALIIDE 197
Cdd:cd18023 83 CAELTGD----TEMDDTfeIQDADIILTTPEKwdSMTRRWRDNGNLVQLVALVLIDE 135
|
|
| |
