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Conserved domains on  [gi|446045882|ref|WP_000123737|]
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MULTISPECIES: ATP-dependent RNA helicase DbpA [Enterobacteriaceae]

Protein Classification

ATP-dependent RNA helicase( domain architecture ID 11485501)

ATP-dependent RNA helicase DbpA is a DEAD-box RNA helicase involved in the assembly of the 50S ribosomal subunit

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
1-457 0e+00

ATP-dependent RNA helicase DbpA; Provisional


:

Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 896.47  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882   1 MTAFSTLNvLPPAQLTNLNELGYLTMTPVQAAALPAILAGKDVRVQAKTGSGKTAAFGLGLLQQIDASLFQTQALVLCPT 80
Cdd:PRK11776   3 MTAFSTLP-LPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCPT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  81 RELADQVAGELRRLARFLPNTKILTLCGGQPFGMQRDSLQHAPHIIVATPGRLLDHLQKGTVSLDALNTLVMDEADRMLD 160
Cdd:PRK11776  82 RELADQVAKEIRRLARFIPNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 161 MGFSDAIDDVIRFAPASRQTLLFSATWPEAIAAISGRVQRDPLAIEIDSTDALPPIEQQFYETSSKGKIPLLQRLLSLHQ 240
Cdd:PRK11776 162 MGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDLPAIEQRFYEVSPDERLPALQRLLLHHQ 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 241 PSSCVVFCNTKKDCQAVCDALNEVGQSALSLHGDLEQRDRDQTLVRFANGSARVLVATDVAARGLDIKSLELVVNFELAW 320
Cdd:PRK11776 242 PESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELAR 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 321 DPEVHVHRIGRTARAGNSGLAISFCAPEEAQRANIISDMLQIKLNWQTPPA--NSSIATLEAEMATLCIDGGKKAKMRPG 398
Cdd:PRK11776 322 DPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLPSlsPLSGVPLLPEMVTLCIDGGKKDKLRPG 401
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446045882 399 DVLGALTGDIGLDGADIGKIAVHPAHVYVAVRQAVAHKAWKQLQGGKIKGKTCRVRLLK 457
Cdd:PRK11776 402 DILGALTGDAGLDGAQIGKINVTDFHAYVAVERAVAKKALKKLQNGKIKGKSFRVRLLK 460
 
Name Accession Description Interval E-value
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
1-457 0e+00

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 896.47  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882   1 MTAFSTLNvLPPAQLTNLNELGYLTMTPVQAAALPAILAGKDVRVQAKTGSGKTAAFGLGLLQQIDASLFQTQALVLCPT 80
Cdd:PRK11776   3 MTAFSTLP-LPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCPT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  81 RELADQVAGELRRLARFLPNTKILTLCGGQPFGMQRDSLQHAPHIIVATPGRLLDHLQKGTVSLDALNTLVMDEADRMLD 160
Cdd:PRK11776  82 RELADQVAKEIRRLARFIPNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 161 MGFSDAIDDVIRFAPASRQTLLFSATWPEAIAAISGRVQRDPLAIEIDSTDALPPIEQQFYETSSKGKIPLLQRLLSLHQ 240
Cdd:PRK11776 162 MGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDLPAIEQRFYEVSPDERLPALQRLLLHHQ 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 241 PSSCVVFCNTKKDCQAVCDALNEVGQSALSLHGDLEQRDRDQTLVRFANGSARVLVATDVAARGLDIKSLELVVNFELAW 320
Cdd:PRK11776 242 PESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELAR 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 321 DPEVHVHRIGRTARAGNSGLAISFCAPEEAQRANIISDMLQIKLNWQTPPA--NSSIATLEAEMATLCIDGGKKAKMRPG 398
Cdd:PRK11776 322 DPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLPSlsPLSGVPLLPEMVTLCIDGGKKDKLRPG 401
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446045882 399 DVLGALTGDIGLDGADIGKIAVHPAHVYVAVRQAVAHKAWKQLQGGKIKGKTCRVRLLK 457
Cdd:PRK11776 402 DILGALTGDAGLDGAQIGKINVTDFHAYVAVERAVAKKALKKLQNGKIKGKSFRVRLLK 460
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
1-381 0e+00

Superfamily II DNA and RNA helicase [Replication, recombination and repair];


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 529.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882   1 MTAFSTLNvLPPAQLTNLNELGYLTMTPVQAAALPAILAGKDVRVQAKTGSGKTAAFGLGLLQQIDASL-FQTQALVLCP 79
Cdd:COG0513    1 MMSFADLG-LSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRpRAPQALILAP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  80 TRELADQVAGELRRLARFLpNTKILTLCGGQPFGMQRDSLQHAPHIIVATPGRLLDHLQKGTVSLDALNTLVMDEADRML 159
Cdd:COG0513   80 TRELALQVAEELRKLAKYL-GLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRML 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 160 DMGFSDAIDDVIRFAPASRQTLLFSATWPEAIAAISGRVQRDPLAIEIDSTDALPP-IEQQFYETSSKGKIPLLQRLLSL 238
Cdd:COG0513  159 DMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAEtIEQRYYLVDKRDKLELLRRLLRD 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 239 HQPSSCVVFCNTKKDCQAVCDALNEVGQSALSLHGDLEQRDRDQTLVRFANGSARVLVATDVAARGLDIKSLELVVNFEL 318
Cdd:COG0513  239 EDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDL 318
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446045882 319 AWDPEVHVHRIGRTARAGNSGLAISFCAPEEAQRANIISDMLQIKLNWQTPPANSSIATLEAE 381
Cdd:COG0513  319 PEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKRLE 381
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
15-206 3.56e-91

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: 274.70  E-value: 3.56e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  15 LTNLNELGYLTMTPVQAAALPAILAGKDVRVQAKTGSGKTAAFGLGLLQQIDASLFQ----TQALVLCPTRELADQVAGE 90
Cdd:cd00268    2 LKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKkgrgPQALVLAPTRELAMQIAEV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  91 LRRLARFlPNTKILTLCGGQPFGMQRDSLQHAPHIIVATPGRLLDHLQKGTVSLDALNTLVMDEADRMLDMGFSDAIDDV 170
Cdd:cd00268   82 ARKLGKG-TGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKI 160
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 446045882 171 IRFAPASRQTLLFSATWPEAIAAISGRVQRDPLAIE 206
Cdd:cd00268  161 LSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
27-194 8.39e-59

DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 190.53  E-value: 8.39e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882   27 TPVQAAALPAILAGKDVRVQAKTGSGKTAAFGLGLLQQIDASLFQTQALVLCPTRELADQVAGELRRLARFLpNTKILTL 106
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGL-GLKVASL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  107 CGGQPFGMQRDSLQHaPHIIVATPGRLLDHLQKgTVSLDALNTLVMDEADRMLDMGFSDAIDDVIRFAPASRQTLLFSAT 186
Cdd:pfam00270  80 LGGDSRKEQLEKLKG-PDILVGTPGRLLDLLQE-RKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSAT 157

                  ....*...
gi 446045882  187 WPEAIAAI 194
Cdd:pfam00270 158 LPRNLEDL 165
DEXDc smart00487
DEAD-like helicases superfamily;
18-218 3.45e-50

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 169.21  E-value: 3.45e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882    18 LNELGYLTMTPVQAAALPAILAG-KDVRVQAKTGSGKTAAFGLGLLQQIDASlFQTQALVLCPTRELADQVAGELRRLAR 96
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRG-KGGRVLVLVPTRELAEQWAEELKKLGP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882    97 FLPNTKILTLCGGQPFGMQRDSLQHAPHIIVATPGRLLDHLQKGTVSLDALNTLVMDEADRMLDMGFSDAIDDVIRFAPA 176
Cdd:smart00487  80 SLGLKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPK 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 446045882   177 SRQTLLFSATWPEAIAAISGRVQRDPLAIEIDSTdALPPIEQ 218
Cdd:smart00487 160 NVQLLLLSATPPEEIENLLELFLNDPVFIDVGFT-PLEPIEQ 200
cas3_core TIGR01587
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ...
42-336 4.00e-10

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: 61.32  E-value: 4.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882   42 DVRVQAKTGSGKTAAFGLGLLQQIDASLFQTQALVLcPTRELADQVAgeLRRLARFLPNTkILTLCGGQP--FGMQRDS- 118
Cdd:TIGR01587   1 LLVIEAPTGYGKTEAALLWALHSIKSQKADRVIIAL-PTRATINAMY--RRAKELFGSEL-VGLHHSSSFsrIKEMGDSe 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  119 --------LQHAPHIIVATPGRL--LDHLQK---GTVSLD-------ALNTLVMDEADRMLD--MGFSDAIDDVIRFAPA 176
Cdd:TIGR01587  77 efehlfplYIHSNDKLFLDPITVctIDQVLKsvfGEFGHYeftlasiANSLLIFDEVHFYDEytLALILAVLEVLKDNDV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  177 SrqTLLFSATWPEaiaaisgRVQRDPLAIEID-STDALPPIEQQFYE--------TSSKGKIPLLQRLL-SLHQPSSCVV 246
Cdd:TIGR01587 157 P--ILLMSATLPK-------FLKEYAEKIGYVeFNEPLDLKEERRFEnhrfilieSDKVGEISSLERLLeFIKKGGSIAI 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  247 FCNTKKDCQAVCDALNEVG--QSALSLHGDLEQRDRD----QTLVRFANGSA-RVLVATDVAARGLDIkSLELVVNfELA 319
Cdd:TIGR01587 228 IVNTVDRAQEFYQQLKEKApeEEIILYHSRFTEKDRAkkeaELLREMKKSNEkFVIVATQVIEASLDI-SADVMIT-ELA 305
                         330
                  ....*....|....*..
gi 446045882  320 wDPEVHVHRIGRTARAG 336
Cdd:TIGR01587 306 -PIDSLIQRLGRLHRYG 321
 
Name Accession Description Interval E-value
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
1-457 0e+00

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 896.47  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882   1 MTAFSTLNvLPPAQLTNLNELGYLTMTPVQAAALPAILAGKDVRVQAKTGSGKTAAFGLGLLQQIDASLFQTQALVLCPT 80
Cdd:PRK11776   3 MTAFSTLP-LPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCPT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  81 RELADQVAGELRRLARFLPNTKILTLCGGQPFGMQRDSLQHAPHIIVATPGRLLDHLQKGTVSLDALNTLVMDEADRMLD 160
Cdd:PRK11776  82 RELADQVAKEIRRLARFIPNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 161 MGFSDAIDDVIRFAPASRQTLLFSATWPEAIAAISGRVQRDPLAIEIDSTDALPPIEQQFYETSSKGKIPLLQRLLSLHQ 240
Cdd:PRK11776 162 MGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDLPAIEQRFYEVSPDERLPALQRLLLHHQ 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 241 PSSCVVFCNTKKDCQAVCDALNEVGQSALSLHGDLEQRDRDQTLVRFANGSARVLVATDVAARGLDIKSLELVVNFELAW 320
Cdd:PRK11776 242 PESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELAR 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 321 DPEVHVHRIGRTARAGNSGLAISFCAPEEAQRANIISDMLQIKLNWQTPPA--NSSIATLEAEMATLCIDGGKKAKMRPG 398
Cdd:PRK11776 322 DPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLPSlsPLSGVPLLPEMVTLCIDGGKKDKLRPG 401
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446045882 399 DVLGALTGDIGLDGADIGKIAVHPAHVYVAVRQAVAHKAWKQLQGGKIKGKTCRVRLLK 457
Cdd:PRK11776 402 DILGALTGDAGLDGAQIGKINVTDFHAYVAVERAVAKKALKKLQNGKIKGKSFRVRLLK 460
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
1-381 0e+00

Superfamily II DNA and RNA helicase [Replication, recombination and repair];


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 529.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882   1 MTAFSTLNvLPPAQLTNLNELGYLTMTPVQAAALPAILAGKDVRVQAKTGSGKTAAFGLGLLQQIDASL-FQTQALVLCP 79
Cdd:COG0513    1 MMSFADLG-LSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRpRAPQALILAP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  80 TRELADQVAGELRRLARFLpNTKILTLCGGQPFGMQRDSLQHAPHIIVATPGRLLDHLQKGTVSLDALNTLVMDEADRML 159
Cdd:COG0513   80 TRELALQVAEELRKLAKYL-GLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRML 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 160 DMGFSDAIDDVIRFAPASRQTLLFSATWPEAIAAISGRVQRDPLAIEIDSTDALPP-IEQQFYETSSKGKIPLLQRLLSL 238
Cdd:COG0513  159 DMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAEtIEQRYYLVDKRDKLELLRRLLRD 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 239 HQPSSCVVFCNTKKDCQAVCDALNEVGQSALSLHGDLEQRDRDQTLVRFANGSARVLVATDVAARGLDIKSLELVVNFEL 318
Cdd:COG0513  239 EDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDL 318
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446045882 319 AWDPEVHVHRIGRTARAGNSGLAISFCAPEEAQRANIISDMLQIKLNWQTPPANSSIATLEAE 381
Cdd:COG0513  319 PEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKRLE 381
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
2-344 2.89e-98

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 307.55  E-value: 2.89e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882   2 TAFSTLNVLPPAqLTNLNELGYLTMTPVQAAALPAILAGKDVRVQAKTGSGKTAAFGLGLLQQIDASLFQTQALVLCPTR 81
Cdd:PRK11634   6 TTFADLGLKAPI-LEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAPTR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  82 ELADQVAGELRRLARFLPNTKILTLCGGQPFGMQRDSLQHAPHIIVATPGRLLDHLQKGTVSLDALNTLVMDEADRMLDM 161
Cdd:PRK11634  85 ELAVQVAEAMTDFSKHMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRM 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 162 GFSDAIDDVIRFAPASRQTLLFSATWPEAIAAISGRVQRDPLAIEIDST-DALPPIEQQFYETSSKGKIPLLQRLLSLHQ 240
Cdd:PRK11634 165 GFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSvTTRPDISQSYWTVWGMRKNEALVRFLEAED 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 241 PSSCVVFCNTKKDCQAVCDALNEVGQSALSLHGDLEQRDRDQTLVRFANGSARVLVATDVAARGLDIKSLELVVNFELAW 320
Cdd:PRK11634 245 FDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPM 324
                        330       340
                 ....*....|....*....|....
gi 446045882 321 DPEVHVHRIGRTARAGNSGLAISF 344
Cdd:PRK11634 325 DSESYVHRIGRTGRAGRAGRALLF 348
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
15-206 3.56e-91

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: 274.70  E-value: 3.56e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  15 LTNLNELGYLTMTPVQAAALPAILAGKDVRVQAKTGSGKTAAFGLGLLQQIDASLFQ----TQALVLCPTRELADQVAGE 90
Cdd:cd00268    2 LKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKkgrgPQALVLAPTRELAMQIAEV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  91 LRRLARFlPNTKILTLCGGQPFGMQRDSLQHAPHIIVATPGRLLDHLQKGTVSLDALNTLVMDEADRMLDMGFSDAIDDV 170
Cdd:cd00268   82 ARKLGKG-TGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKI 160
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 446045882 171 IRFAPASRQTLLFSATWPEAIAAISGRVQRDPLAIE 206
Cdd:cd00268  161 LSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
2-344 7.58e-89

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 277.21  E-value: 7.58e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882   2 TAFSTLNvLPPAQLTNLNELGYLTMTPVQAAALPAILAGKDVRVQAKTGSGKTAAFGLGLLQQ-IDaslF------QTQA 74
Cdd:PRK11192   1 TTFSELE-LDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHlLD---FprrksgPPRI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  75 LVLCPTRELADQVAGELRRLARFLpNTKILTLCGGQPFGMQRDSLQHAPHIIVATPGRLLDHLQKGTVSLDALNTLVMDE 154
Cdd:PRK11192  77 LILTPTRELAMQVADQARELAKHT-HLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDE 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 155 ADRMLDMGFSDAIDDVIRFAPASRQTLLFSATWP-EAIAAISGRVQRDPLAIEIDstdalPP------IEQQFYETSSKG 227
Cdd:PRK11192 156 ADRMLDMGFAQDIETIAAETRWRKQTLLFSATLEgDAVQDFAERLLNDPVEVEAE-----PSrrerkkIHQWYYRADDLE 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 228 -KIPLLQRLLSLHQPSSCVVFCNTKKDCQAVCDALNEVGQSALSLHGDLEQRDRDQTLVRFANGSARVLVATDVAARGLD 306
Cdd:PRK11192 231 hKTALLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGID 310
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 446045882 307 IKSLELVVNFELAWDPEVHVHRIGRTARAGNSGLAISF 344
Cdd:PRK11192 311 IDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISL 348
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
2-371 3.79e-85

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 269.09  E-value: 3.79e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882   2 TAFSTLNvLPPAQLTNLNELGYLTMTPVQAAALPAILAGKDVRVQAKTGSGKTAAFGLGLLQQIDASLFQTQ-------A 74
Cdd:PRK01297  87 TRFHDFN-LAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPKErymgeprA 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  75 LVLCPTRELADQVAGELRRLARFlPNTKILTLCGGQPFGMQRDSLQhAPH--IIVATPGRLLDHLQKGTVSLDALNTLVM 152
Cdd:PRK01297 166 LIIAPTRELVVQIAKDAAALTKY-TGLNVMTFVGGMDFDKQLKQLE-ARFcdILVATPGRLLDFNQRGEVHLDMVEVMVL 243
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 153 DEADRMLDMGFSDAIDDVIRFAP--ASRQTLLFSATWPEAIAAISGRVQRDPLAIEIDSTD-ALPPIEQQFYETSSKGKI 229
Cdd:PRK01297 244 DEADRMLDMGFIPQVRQIIRQTPrkEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENvASDTVEQHVYAVAGSDKY 323
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 230 PLLQRLLSLHQPSSCVVFCNTKKDCQAVCDALNEVGQSALSLHGDLEQRDRDQTLVRFANGSARVLVATDVAARGLDIKS 309
Cdd:PRK01297 324 KLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDG 403
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446045882 310 LELVVNFELAWDPEVHVHRIGRTARAGNSGLAISFCAPEEAQRANIISDMLQIKLNWQTPPA 371
Cdd:PRK01297 404 ISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKISCEMPPA 465
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
3-349 1.06e-77

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 249.34  E-value: 1.06e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882   3 AFSTLNvLPPAQLTNLNELGYLTMTPVQAAALPAILAGKDVRVQAKTGSGKTAAFGLGLLQQIDASLFQTQ------ALV 76
Cdd:PRK10590   2 SFDSLG-LSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKgrrpvrALI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  77 LCPTRELADQVAGELRRLARFLpNTKILTLCGGQPFGMQRDSLQHAPHIIVATPGRLLDHLQKGTVSLDALNTLVMDEAD 156
Cdd:PRK10590  81 LTPTRELAAQIGENVRDYSKYL-NIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEAD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 157 RMLDMGFSDAIDDVIRFAPASRQTLLFSATWPEAIAAISGRVQRDPLAIEIDSTD-ALPPIEQQFYETSSKGKIPLLQRL 235
Cdd:PRK10590 160 RMLDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNtASEQVTQHVHFVDKKRKRELLSQM 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 236 LSLHQPSSCVVFCNTKKDCQAVCDALNEVGQSALSLHGDLEQRDRDQTLVRFANGSARVLVATDVAARGLDIKSLELVVN 315
Cdd:PRK10590 240 IGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVN 319
                        330       340       350
                 ....*....|....*....|....*....|....
gi 446045882 316 FELAWDPEVHVHRIGRTARAGNSGLAISFCAPEE 349
Cdd:PRK10590 320 YELPNVPEDYVHRIGRTGRAAATGEALSLVCVDE 353
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
4-349 3.85e-77

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 246.81  E-value: 3.85e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882   4 FSTLNvLPPAQLTNLNELGYLTMTPVQAAALPAILAGKDVRVQAKTGSGKTAAFGLG----LLQQ---IDASLFQTQALV 76
Cdd:PRK04837  10 FSDFA-LHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTAtfhyLLSHpapEDRKVNQPRALI 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  77 LCPTRELADQVAGELRRLARfLPNTKILTLCGGQPFGMQRDSLQHAPHIIVATPGRLLDHLQKGTVSLDALNTLVMDEAD 156
Cdd:PRK04837  89 MAPTRELAVQIHADAEPLAQ-ATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEAD 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 157 RMLDMGFsdaIDDvIRF------APASRQTLLFSATwpeaiaaISGRVQR-------DPLAIEIDstdalpP-------I 216
Cdd:PRK04837 168 RMFDLGF---IKD-IRWlfrrmpPANQRLNMLFSAT-------LSYRVRElafehmnNPEYVEVE------PeqktghrI 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 217 EQQFYETSSKGKIPLLQRLLSLHQPSSCVVFCNTKKDCQAVCDALNEVGQSALSLHGDLEQRDRDQTLVRFANGSARVLV 296
Cdd:PRK04837 231 KEELFYPSNEEKMRLLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILV 310
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446045882 297 ATDVAARGLDIKSLELVVNFELAWDPEVHVHRIGRTARAGNSGLAISFcAPEE 349
Cdd:PRK04837 311 ATDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL-ACEE 362
PTZ00110 PTZ00110
helicase; Provisional
15-377 2.66e-75

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 245.45  E-value: 2.66e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  15 LTNLNELGYLTMTPVQAAALPAILAGKDVRVQAKTGSGKTAAFGLGLLQQIDAslfqtQA----------LVLCPTRELA 84
Cdd:PTZ00110 142 LKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINA-----QPllrygdgpivLVLAPTRELA 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  85 DQVAGELRRLARflpNTKILTLC--GGQPFGMQRDSLQHAPHIIVATPGRLLDHLQKGTVSLDALNTLVMDEADRMLDMG 162
Cdd:PTZ00110 217 EQIREQCNKFGA---SSKIRNTVayGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMG 293
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 163 FSDAIDDVIRFAPASRQTLLFSATWPEAIAAISGRVQRD-PLAIEIDSTD--ALPPIEQQFY---ETSSKGKIP-LLQRL 235
Cdd:PTZ00110 294 FEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEePVHVNVGSLDltACHNIKQEVFvveEHEKRGKLKmLLQRI 373
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 236 LSlhQPSSCVVFCNTKKDCQAVCDALNEVGQSALSLHGDLEQRDRDQTLVRFANGSARVLVATDVAARGLDIKSLELVVN 315
Cdd:PTZ00110 374 MR--DGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVIN 451
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446045882 316 FELAWDPEVHVHRIGRTARAGNSGLAISFCAPEEAQRANIISDMLQiKLNWQTPPANSSIAT 377
Cdd:PTZ00110 452 FDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVKVLR-EAKQPVPPELEKLSN 512
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
4-344 1.44e-74

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 244.47  E-value: 1.44e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882   4 FSTLNvLPPAQLTNLNELGYLTMTPVQAAALPAILAGKDVRVQAKTGSGKTAAFGLGLLQQI-------DASLFQTQALV 76
Cdd:PRK04537  11 FSSFD-LHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLlsrpalaDRKPEDPRALI 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  77 LCPTRELADQVAGELRRLARFLpNTKILTLCGGQPFGMQRDSLQHAPHIIVATPGRLLDHL-QKGTVSLDALNTLVMDEA 155
Cdd:PRK04537  90 LAPTRELAIQIHKDAVKFGADL-GLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVkQHKVVSLHACEICVLDEA 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 156 DRMLDMGFSDAIDDVIRFAP--ASRQTLLFSATWPEAIAAISGRVQRDP--LAIEIDSTDAlPPIEQQFYETSSKGKIPL 231
Cdd:PRK04537 169 DRMFDLGFIKDIRFLLRRMPerGTRQTLLFSATLSHRVLELAYEHMNEPekLVVETETITA-ARVRQRIYFPADEEKQTL 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 232 LQRLLSLHQPSSCVVFCNTKKDCQAVCDALNEVGQSALSLHGDLEQRDRDQTLVRFANGSARVLVATDVAARGLDIKSLE 311
Cdd:PRK04537 248 LLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVK 327
                        330       340       350
                 ....*....|....*....|....*....|...
gi 446045882 312 LVVNFELAWDPEVHVHRIGRTARAGNSGLAISF 344
Cdd:PRK04537 328 YVYNYDLPFDAEDYVHRIGRTARLGEEGDAISF 360
PTZ00424 PTZ00424
helicase 45; Provisional
22-349 1.21e-68

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 223.94  E-value: 1.21e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  22 GYLTMTPVQAAALPAILAGKDVRVQAKTGSGKTAAFGLGLLQQIDASLFQTQALVLCPTRELADQVAGELRRLARFLpNT 101
Cdd:PTZ00424  47 GFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILAPTRELAQQIQKVVLALGDYL-KV 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 102 KILTLCGGQPFGMQRDSLQHAPHIIVATPGRLLDHLQKGTVSLDALNTLVMDEADRMLDMGFSDAIDDVIRFAPASRQTL 181
Cdd:PTZ00424 126 RCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRGFKGQIYDVFKKLPPDVQVA 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 182 LFSATWPEAIAAISGRVQRDPLAIEIDSTDALPPIEQQFYETSSKG--KIPLLQRLLSLHQPSSCVVFCNTKKDCQAVCD 259
Cdd:PTZ00424 206 LFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEewKFDTLCDLYETLTITQAIIYCNTRRKVDYLTK 285
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 260 ALNEVGQSALSLHGDLEQRDRDQTLVRFANGSARVLVATDVAARGLDIKSLELVVNFELAWDPEVHVHRIGRTARAGNSG 339
Cdd:PTZ00424 286 KMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKG 365
                        330
                 ....*....|
gi 446045882 340 LAISFCAPEE 349
Cdd:PTZ00424 366 VAINFVTPDD 375
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
27-194 8.39e-59

DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 190.53  E-value: 8.39e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882   27 TPVQAAALPAILAGKDVRVQAKTGSGKTAAFGLGLLQQIDASLFQTQALVLCPTRELADQVAGELRRLARFLpNTKILTL 106
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGL-GLKVASL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  107 CGGQPFGMQRDSLQHaPHIIVATPGRLLDHLQKgTVSLDALNTLVMDEADRMLDMGFSDAIDDVIRFAPASRQTLLFSAT 186
Cdd:pfam00270  80 LGGDSRKEQLEKLKG-PDILVGTPGRLLDLLQE-RKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSAT 157

                  ....*...
gi 446045882  187 WPEAIAAI 194
Cdd:pfam00270 158 LPRNLEDL 165
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
4-191 8.81e-58

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: 189.62  E-value: 8.81e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882   4 FSTLNvLPPAQLTNLNELGYLTMTPVQAAALPAILAGKDVRVQAKTGSGKTAAFGLGLLQQI-----DASLF-----QTQ 73
Cdd:cd17967    2 FEEAG-LRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLledgpPSVGRgrrkaYPS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  74 ALVLCPTRELADQVAGELRRLARflpNTKILTLC--GGQPFGMQRDSLQHAPHIIVATPGRLLDHLQKGTVSLDALNTLV 151
Cdd:cd17967   81 ALILAPTRELAIQIYEEARKFSY---RSGVRSVVvyGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLV 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 446045882 152 MDEADRMLDMGFSDAIDDVIRFA----PASRQTLLFSATWPEAI 191
Cdd:cd17967  158 LDEADRMLDMGFEPQIRKIVEHPdmppKGERQTLMFSATFPREI 201
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
10-194 3.05e-57

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: 188.18  E-value: 3.05e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  10 LPPAQLTNLNELGYLTMTPVQAAALPAILA-GKDVRVQAKTGSGKTAAFGLGLLQQIDASLFQTQ-----ALVLCPTREL 83
Cdd:cd17964    1 LDPSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRrsgvsALIISPTREL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  84 ADQVAGELRRLARFLPNTKILTLCGGQPFG-MQRDSLQHAPHIIVATPGRLLDHLQKGTV--SLDALNTLVMDEADRMLD 160
Cdd:cd17964   81 ALQIAAEAKKLLQGLRKLRVQSAVGGTSRRaELNRLRRGRPDILVATPGRLIDHLENPGVakAFTDLDYLVLDEADRLLD 160
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 446045882 161 MGFSDAIDDVIRFAPAS----RQTLLFSATWPEAIAAI 194
Cdd:cd17964  161 MGFRPDLEQILRHLPEKnadpRQTLLFSATVPDEVQQI 198
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
22-205 5.40e-57

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: 187.15  E-value: 5.40e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  22 GYLTMTPVQAAALPAILAGKDVRVQAKTGSGKTAAFGLGLLQQIDASLFQTQALVLCPTRELADQVAGELRRLARFLpNT 101
Cdd:cd17939   16 GFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQQIQKVVKALGDYM-GV 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 102 KILTLCGGQPFGMQRDSLQHAPHIIVATPGRLLDHLQKGTVSLDALNTLVMDEADRMLDMGFSDAIDDVIRFAPASRQTL 181
Cdd:cd17939   95 KVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQIYDIFQFLPPETQVV 174
                        170       180
                 ....*....|....*....|....
gi 446045882 182 LFSATWPEAIAAISGRVQRDPLAI 205
Cdd:cd17939  175 LFSATMPHEVLEVTKKFMRDPVRI 198
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
4-362 8.77e-57

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 195.78  E-value: 8.77e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882   4 FSTLNvLPPAQLTNLNELGYLTMTPVQAAALPAILAGKDVRVQAKTGSGKTAAFGLGLLQQidASLFQTQ---------A 74
Cdd:PLN00206 123 FSSCG-LPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISR--CCTIRSGhpseqrnplA 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  75 LVLCPTRELADQVAGELRRLARFLPnTKILTLCGGQPFGMQRDSLQHAPHIIVATPGRLLDHLQKGTVSLDALNTLVMDE 154
Cdd:PLN00206 200 MVLTPTRELCVQVEDQAKVLGKGLP-FKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDE 278
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 155 ADRMLDMGFSDAIDDVIRfAPASRQTLLFSATWPEAIAAISGRVQRDPLAIEIDSTDALPPIEQQ---FYETSSKgKIPL 231
Cdd:PLN00206 279 VDCMLERGFRDQVMQIFQ-ALSQPQVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQlaiWVETKQK-KQKL 356
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 232 LQRLLS-LHQPSSCVVFCNTKKDCQAVCDALNEV-GQSALSLHGDLEQRDRDQTLVRFANGSARVLVATDVAARGLDIKS 309
Cdd:PLN00206 357 FDILKSkQHFKPPAVVFVSSRLGADLLANAITVVtGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLR 436
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446045882 310 LELVVNFELAWDPEVHVHRIGRTARAGNSGLAISFCAPEEaqrANIISDMLQI 362
Cdd:PLN00206 437 VRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEED---RNLFPELVAL 486
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
18-192 2.24e-56

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: 185.15  E-value: 2.24e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  18 LNELGYLTMTPVQAAALPAILAGKDVRVQAKTGSGKTAAFGLGLLQQI---DASLFQTQALVLCPTRELADQVAGELRRL 94
Cdd:cd17947    5 LSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLlyrPKKKAATRVLVLVPTRELAMQCFSVLQQL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  95 ARFLPNTKILtLCGGQPFGMQRDSLQHAPHIIVATPGRLLDHLQKG-TVSLDALNTLVMDEADRMLDMGFSDAIDDVIRF 173
Cdd:cd17947   85 AQFTDITFAL-AVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSpSFDLDSIEILVLDEADRMLEEGFADELKEILRL 163
                        170
                 ....*....|....*....
gi 446045882 174 APASRQTLLFSATWPEAIA 192
Cdd:cd17947  164 CPRTRQTMLFSATMTDEVK 182
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
216-345 7.50e-56

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: 181.55  E-value: 7.50e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 216 IEQQFYETSSKGKIP-LLQRLLSLHQPSSCVVFCNTKKDCQAVCDALNEVGQSALSLHGDLEQRDRDQTLVRFANGSARV 294
Cdd:cd18787    1 IKQLYVVVEEEEKKLlLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446045882 295 LVATDVAARGLDIKSLELVVNFELAWDPEVHVHRIGRTARAGNSGLAISFC 345
Cdd:cd18787   81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
19-206 1.50e-53

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: 178.28  E-value: 1.50e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  19 NELGYLTMTPVQAAALPAILAGKDVRVQAKTGSGKTAAFGLGLLQQIdasLFQTQ---ALVLCPTRELADQVAGELRRLA 95
Cdd:cd17954   16 EKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQAL---LENPQrffALVLAPTRELAQQISEQFEALG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  96 RfLPNTKILTLCGGQPFGMQRDSLQHAPHIIVATPGRLLDHLQ--KGtVSLDALNTLVMDEADRMLDMGFSDAIDDVIRF 173
Cdd:cd17954   93 S-SIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLEntKG-FSLKSLKFLVMDEADRLLNMDFEPEIDKILKV 170
                        170       180       190
                 ....*....|....*....|....*....|...
gi 446045882 174 APASRQTLLFSATWPEAIAAISGRVQRDPLAIE 206
Cdd:cd17954  171 IPRERTTYLFSATMTTKVAKLQRASLKNPVKIE 203
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
15-191 5.72e-53

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: 178.62  E-value: 5.72e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  15 LTNLNELGYLTMTPVQAAALPAILAGKDVRVQAKTGSGKTAAFGLGLLQQ-----IDASLFQT----QALVLCPTRELAD 85
Cdd:cd18052   55 LKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGmmkegLTASSFSEvqepQALIVAPTRELAN 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  86 QVAGELRRLARflpNTKI--LTLCGGQPFGMQRDSLQHAPHIIVATPGRLLDHLQKGTVSLDALNTLVMDEADRMLDMGF 163
Cdd:cd18052  135 QIFLEARKFSY---GTCIrpVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGF 211
                        170       180       190
                 ....*....|....*....|....*....|..
gi 446045882 164 SDAIDDVIRFA--PA--SRQTLLFSATWPEAI 191
Cdd:cd18052  212 GPEIRKLVSEPgmPSkeDRQTLMFSATFPEEI 243
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
4-206 7.87e-53

DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350713 [Multi-domain]  Cd Length: 204  Bit Score: 176.26  E-value: 7.87e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882   4 FSTLNvLPPAQLTNLNELGYLTMTPVQAAALPAILAGKDVRVQAKTGSGKTAAFGLGLLQQIDASLFQTQALVLCPTREL 83
Cdd:cd17955    1 FEDLG-LSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYGIFALVLTPTREL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  84 ADQVAGELRRLARFLpNTKILTLCGGQPFGMQRDSLQHAPHIIVATPGRLLDHLQ---KGTVSLDALNTLVMDEADRMLD 160
Cdd:cd17955   80 AYQIAEQFRALGAPL-GLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssdDTTKVLSRVKFLVLDEADRLLT 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 446045882 161 MGFSDAIDDVIRFAPASRQTLLFSATWPEAIAAISGRVQRDPLAIE 206
Cdd:cd17955  159 GSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPFFWE 204
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
15-205 4.36e-51

DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or p54) participates in mRNA regulation mediated by miRNA-mediated silencing. It also plays a role in global and transcript-specific messenger RNA (mRNA) storage, translational repression, and decay. It is a member of the DEAD-box helicase family, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350698 [Multi-domain]  Cd Length: 201  Bit Score: 171.71  E-value: 4.36e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  15 LTNLNELGYLTMTPVQAAALPAILAGKDVRVQAKTGSGKTAAFGLGLLQQIDASLFQTQALVLCPTRELADQVAGELRRL 94
Cdd:cd17940   11 LMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELALQTSQVCKEL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  95 ARFLpNTKILTLCGGQPFgmqRDS---LQHAPHIIVATPGRLLDHLQKGTVSLDALNTLVMDEADRMLDMGFSDAIDDVI 171
Cdd:cd17940   91 GKHM-GVKVMVTTGGTSL---RDDimrLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQPIIEKIL 166
                        170       180       190
                 ....*....|....*....|....*....|....
gi 446045882 172 RFAPASRQTLLFSATWPEAIAAISGRVQRDPLAI 205
Cdd:cd17940  167 NFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
DEXDc smart00487
DEAD-like helicases superfamily;
18-218 3.45e-50

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 169.21  E-value: 3.45e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882    18 LNELGYLTMTPVQAAALPAILAG-KDVRVQAKTGSGKTAAFGLGLLQQIDASlFQTQALVLCPTRELADQVAGELRRLAR 96
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRG-KGGRVLVLVPTRELAEQWAEELKKLGP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882    97 FLPNTKILTLCGGQPFGMQRDSLQHAPHIIVATPGRLLDHLQKGTVSLDALNTLVMDEADRMLDMGFSDAIDDVIRFAPA 176
Cdd:smart00487  80 SLGLKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPK 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 446045882   177 SRQTLLFSATWPEAIAAISGRVQRDPLAIEIDSTdALPPIEQ 218
Cdd:smart00487 160 NVQLLLLSATPPEEIENLLELFLNDPVFIDVGFT-PLEPIEQ 200
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
18-194 1.99e-49

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: 167.37  E-value: 1.99e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  18 LNELGYLTMTPVQAAALPAILAGKDVRVQAKTGSGKTAAFGLGLLQQI-----DASLFQTQALVLCPTRELADQVAGELR 92
Cdd:cd17960    5 VAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILlkrkaNLKKGQVGALIISPTRELATQIYEVLQ 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  93 RLARF-LPNTKILTLCGGQPFGMQRDSL-QHAPHIIVATPGRLLDHLQKGT--VSLDALNTLVMDEADRMLDMGFSDAID 168
Cdd:cd17960   85 SFLEHhLPKLKCQLLIGGTNVEEDVKKFkRNGPNILVGTPGRLEELLSRKAdkVKVKSLEVLVLDEADRLLDLGFEADLN 164
                        170       180
                 ....*....|....*....|....*.
gi 446045882 169 DVIRFAPASRQTLLFSATWPEAIAAI 194
Cdd:cd17960  165 RILSKLPKQRRTGLFSATQTDAVEEL 190
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
10-192 1.15e-48

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: 165.56  E-value: 1.15e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  10 LPPAQLTNLNELGYLTMTPVQAAALPAILAGKDVRVQAKTGSGKTAAFGLGLLQQIDASLFQT--QALVLCPTRELADQV 87
Cdd:cd17959    8 LSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTVgaRALILSPTRELALQT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  88 AGELRRLARFLpNTKILTLCGGQPFGMQRDSLQHAPHIIVATPGRLLDHLQKGTVSLDALNTLVMDEADRMLDMGFSDAI 167
Cdd:cd17959   88 LKVTKELGKFT-DLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEMGFAEQL 166
                        170       180
                 ....*....|....*....|....*
gi 446045882 168 DDVIRFAPASRQTLLFSATWPEAIA 192
Cdd:cd17959  167 HEILSRLPENRQTLLFSATLPKLLV 191
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
10-207 8.64e-48

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: 163.28  E-value: 8.64e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  10 LPPAQLTNLNELGYLTMTPVQAAALPAILAGKDVRVQAKTGSGKTAAFGLGLLQQIDASLFQTQALVLCPTRELADQVAG 89
Cdd:cd17950    9 LKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTRELAFQISN 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  90 ELRRLARFLPNTKILTLCGGQPFGMQRDSLQ-HAPHIIVATPGRLLDHLQKGTVSLDALNTLVMDEADRML-DMGFSDAI 167
Cdd:cd17950   89 EYERFSKYMPNVKTAVFFGGVPIKKDIEVLKnKCPHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLeQLDMRRDV 168
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 446045882 168 DDVIRFAPASRQTLLFSATWPEAIAAISGRVQRDPLAIEI 207
Cdd:cd17950  169 QEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
18-205 5.15e-47

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: 160.92  E-value: 5.15e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  18 LNELGYLTMTPVQAAALPAILAGKDVRVQAKTGSGKTAAFGLGLLQQidasLFQTQ--------ALVLCPTRELADQVAG 89
Cdd:cd17941    5 LKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEK----LYRERwtpedglgALIISPTRELAMQIFE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  90 ELRRLARFLPNTKILtLCGGQPFGMQRDSLqHAPHIIVATPGRLLDHLQKgTVSLDA--LNTLVMDEADRMLDMGFSDAI 167
Cdd:cd17941   81 VLRKVGKYHSFSAGL-IIGGKDVKEEKERI-NRMNILVCTPGRLLQHMDE-TPGFDTsnLQMLVLDEADRILDMGFKETL 157
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 446045882 168 DDVIRFAPASRQTLLFSATWPEAIAAISGRVQRDPLAI 205
Cdd:cd17941  158 DAIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYI 195
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
20-205 2.25e-46

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: 159.79  E-value: 2.25e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  20 ELGYLTMTPVQAAALPAILAGKDVRVQAKTGSGKTAAFGLGLLQQIDASLFQT--------QALVLCPTRELADQVAGEL 91
Cdd:cd17945    7 KLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDeetkddgpYALILAPTRELAQQIEEET 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  92 RRLARFLpNTKILTLCGGQPFGMQRDSLQHAPHIIVATPGRLLDHLQKGTVSLDALNTLVMDEADRMLDMGFSDAIDDVI 171
Cdd:cd17945   87 QKFAKPL-GIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQVTKIL 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446045882 172 RFAPAS--------------------RQTLLFSATWPEAIAAISGRVQRDPLAI 205
Cdd:cd17945  166 DAMPVSnkkpdteeaeklaasgkhryRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
15-205 6.12e-45

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: 155.40  E-value: 6.12e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  15 LTNLNELGYLTMTPVQAAALPAILAGKDVRVQAKTGSGKTAAFglgLLQQIDASLFQTQ---ALVLCPTRELADQVAGEL 91
Cdd:cd17962    2 SSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAF---LLPVIIRCLTEHRnpsALILTPTRELAVQIEDQA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  92 RRLARFLPNTKILTLCGGQPFGMQRDSLQHAPHIIVATPGRLLDHLQKGTVSLDALNTLVMDEADRMLDMGFSDAIDDVI 171
Cdd:cd17962   79 KELMKGLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDIL 158
                        170       180       190
                 ....*....|....*....|....*....|....
gi 446045882 172 RFAPASRQTLLFSATWPEAIAAISGRVQRDPLAI 205
Cdd:cd17962  159 ENISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
10-205 6.16e-45

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: 156.38  E-value: 6.16e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  10 LPPAQLTNLNELGYLTMTPVQAAALPAILAGKDVRVQAKTGSGKTAAFGLGLLQQIDASLFQTQ-----ALVLCPTRELA 84
Cdd:cd17953   19 LSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPVKPgegpiGLIMAPTRELA 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  85 DQVAGELRRlarFLPNTKILTLC--GGQPFGMQRDSLQHAPHIIVATPGRLLDHL--QKGTV-SLDALNTLVMDEADRML 159
Cdd:cd17953   99 LQIYVECKK---FSKALGLRVVCvyGGSGISEQIAELKRGAEIVVCTPGRMIDILtaNNGRVtNLRRVTYVVLDEADRMF 175
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 446045882 160 DMGFSDAIDDVIRFAPASRQTLLFSATWPEAIAAISGRVQRDPLAI 205
Cdd:cd17953  176 DMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
18-202 1.51e-44

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: 154.66  E-value: 1.51e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  18 LNELGYLTMTPVQAAALPAILAGKDVRVQAKTGSGKTAAFGLGLLQQI------DASLFQTQALVLCPTRELADQVAGEL 91
Cdd:cd17961    9 IAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKIlkakaeSGEEQGTRALILVPTRELAQQVSKVL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  92 RRLARFL-PNTKILTLCGGQPFGMQRDSLQHAPHIIVATPGRLLDHLQKGTVSL-DALNTLVMDEADRMLDMGFSDAIDD 169
Cdd:cd17961   89 EQLTAYCrKDVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLlSTLKYLVIDEADLVLSYGYEEDLKS 168
                        170       180       190
                 ....*....|....*....|....*....|...
gi 446045882 170 VIRFAPASRQTLLFSATWPEAIAAISGRVQRDP 202
Cdd:cd17961  169 LLSYLPKNYQTFLMSATLSEDVEALKKLVLHNP 201
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
17-205 1.84e-44

DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) plays a role in ribosome biogenesis and TP53/p53 regulation through its interaction with NPM1. DDX31 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350707 [Multi-domain]  Cd Length: 214  Bit Score: 154.67  E-value: 1.84e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  17 NLNE-LGYLTMTPVQAAALPAILAGKDVRVQAKTGSGKTAAFGLGLLQQIDASLFQ------TQALVLCPTRELADQVAG 89
Cdd:cd17949    4 HLKSkMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRvdrsdgTLALVLVPTRELALQIYE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  90 ELRRLARFLPNTKILTLCGGQPFGMQRDSLQHAPHIIVATPGRLLDHLQKgTVSLDALN--TLVMDEADRMLDMGFSDAI 167
Cdd:cd17949   84 VLEKLLKPFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKN-TQSFDVSNlrWLVLDEADRLLDMGFEKDI 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446045882 168 DDVIRF-------------APASRQTLLFSATWPEAIAAISGRVQRDPLAI 205
Cdd:cd17949  163 TKILELlddkrskaggeksKPSRRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
29-205 4.25e-44

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: 153.37  E-value: 4.25e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  29 VQAAALPAILAGKDVRVQAKTGSGKTAAFGLGLLQQIDASLFQTQALVLCPTRELADQVAGELRRLARFLpNTKILTLCG 108
Cdd:cd18046   25 IQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELAQQIQKVVMALGDYM-GIKCHACIG 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 109 GQPFGMQRDSLQHAPHIIVATPGRLLDHLQKGTVSLDALNTLVMDEADRMLDMGFSDAIDDVIRFAPASRQTLLFSATWP 188
Cdd:cd18046  104 GTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFKDQIYDIFQKLPPDTQVVLLSATMP 183
                        170
                 ....*....|....*..
gi 446045882 189 EAIAAISGRVQRDPLAI 205
Cdd:cd18046  184 NDVLEVTTKFMRDPIRI 200
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
23-191 1.06e-43

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: 153.66  E-value: 1.06e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  23 YLTMTPVQAAALPAILAGKDVRVQAKTGSGKTAAFGLGLLQQI------DASLFQTQ----------ALVLCPTRELADQ 86
Cdd:cd18051   41 YTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIyeqgpgESLPSESGyygrrkqyplALVLAPTRELASQ 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  87 VAGELRRLArFLPNTKILTLCGGQPFGMQRDSLQHAPHIIVATPGRLLDHLQKGTVSLDALNTLVMDEADRMLDMGFSDA 166
Cdd:cd18051  121 IYDEARKFA-YRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQ 199
                        170       180
                 ....*....|....*....|....*....
gi 446045882 167 IDDVIRF----APASRQTLLFSATWPEAI 191
Cdd:cd18051  200 IRRIVEQdtmpPTGERQTLMFSATFPKEI 228
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
15-205 1.61e-43

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: 151.75  E-value: 1.61e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  15 LTNLNELGYLTMTPVQAAALPAILAGKDVRVQAKTGSGKTAAFGLGLLQQIDASLFQTQ-----ALVLCPTRELADQVAG 89
Cdd:cd17966    2 MDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERgdgpiVLVLAPTRELAQQIQQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  90 ELRRlarFLPNTKILTLC--GGQPFGMQRDSLQHAPHIIVATPGRLLDHLQKGTVSLDALNTLVMDEADRMLDMGFSDAI 167
Cdd:cd17966   82 EANK---FGGSSRLRNTCvyGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQI 158
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 446045882 168 DDVIRFAPASRQTLLFSATWPEAIAAISGRVQRDPLAI 205
Cdd:cd17966  159 RKIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
15-195 3.58e-43

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: 150.59  E-value: 3.58e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  15 LTNLNELGYLTMTPVQAAALPAILAGKDVRVQAKTGSGKTAAFGLGLLQQIDASLFQ----TQALVLCPTRELADQVAGE 90
Cdd:cd17942    2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKFKprngTGVIIISPTRELALQIYGV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  91 LRRLARFLPNTKILtLCGGQPFGMQRDSLQHAPHIIVATPGRLLDHLQ--KGTVsLDALNTLVMDEADRMLDMGFSDAID 168
Cdd:cd17942   82 AKELLKYHSQTFGI-VIGGANRKAEAEKLGKGVNILVATPGRLLDHLQntKGFL-YKNLQCLIIDEADRILEIGFEEEMR 159
                        170       180       190
                 ....*....|....*....|....*....|
gi 446045882 169 DVIRFAPASRQTLLFSATWP---EAIAAIS 195
Cdd:cd17942  160 QIIKLLPKRRQTMLFSATQTrkvEDLARIS 189
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
15-206 1.44e-42

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: 148.95  E-value: 1.44e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  15 LTNLNELGYLTMTPVQAAALPAILAGKDVRVQAKTGSGKTAAFGLGLLQQIDASLFQTQALVLCPTRELADQVAGELRRL 94
Cdd:cd17943    2 LEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVFKKI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  95 ARFLPNTKILTLCGGQPFGMQRDSLQhAPHIIVATPGRLLDHLQKGTVSLDALNTLVMDEADRMLDMGFSDAIDDVIRFA 174
Cdd:cd17943   82 GKKLEGLKCEVFIGGTPVKEDKKKLK-GCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFSSL 160
                        170       180       190
                 ....*....|....*....|....*....|..
gi 446045882 175 PASRQTLLFSATWPEAIAAISGRVQRDPLAIE 206
Cdd:cd17943  161 PKNKQVIAFSATYPKNLDNLLARYMRKPVLVR 192
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
10-205 1.45e-42

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: 148.88  E-value: 1.45e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  10 LPPAQLTNLNELGYLTMTPVQAAALPAILAG--KDVRVQAKTGSGKTAAFGLGLLQQIDASLFQTQALVLCPTRELADQV 87
Cdd:cd17963    1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  88 AGELRRLARFlPNTKILTLCGGQPFGMQRDSLQhapHIIVATPGRLLDHLQKGTVSLDALNTLVMDEADRMLDM-GFSDA 166
Cdd:cd17963   81 GEVVEKMGKF-TGVKVALAVPGNDVPRGKKITA---QIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTqGHGDQ 156
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 446045882 167 IDDVIRFAPASRQTLLFSATWPEAIAAISGRVQRDPLAI 205
Cdd:cd17963  157 SIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
15-207 2.20e-42

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: 148.51  E-value: 2.20e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  15 LTNLNELGYLTMTPVQAAALPAILAGKDVRVQAKTGSGKTAAFGLGLLQQIDASLFQT--QALVLCPTRELADQVAGELR 92
Cdd:cd17957    2 LNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKKglRALILAPTRELASQIYRELL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  93 RLARFLPN-TKILTLCGGQPFGMQRDSLQHApHIIVATPGRLLDHLQKGTVSLDALNTLVMDEADRMLDMGFSDAIDDVI 171
Cdd:cd17957   82 KLSKGTGLrIVLLSKSLEAKAKDGPKSITKY-DILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDEIL 160
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 446045882 172 RFAPASR-QTLLFSATWPEAIAAISGRVQRDPLAIEI 207
Cdd:cd17957  161 AACTNPNlQRSLFSATIPSEVEELARSVMKDPIRIIV 197
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
15-205 2.86e-42

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: 148.38  E-value: 2.86e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  15 LTNLNELGYLTMTPVQAAALPAILAGKDVRVQAKTGSGKTAAFGLGLLQQIDASLFQTQALVLCPTRELADQVAGELRRL 94
Cdd:cd18045   11 LRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELAVQIQKVLLAL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  95 ARFLpNTKILTLCGGQPFGMQRDSLQHAPHIIVATPGRLLDHLQKGTVSLDALNTLVMDEADRMLDMGFSDAIDDVIRFA 174
Cdd:cd18045   91 GDYM-NVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFKEQIYDVYRYL 169
                        170       180       190
                 ....*....|....*....|....*....|.
gi 446045882 175 PASRQTLLFSATWPEAIAAISGRVQRDPLAI 205
Cdd:cd18045  170 PPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
15-205 4.60e-42

DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts with several spliceosomal proteins and may recognize the bacterial second messengers cyclic di-GMP and cyclic di-AMP, resulting in the induction of genes involved in the innate immune response. Diseases associated with DDX41 include "myeloproliferative/lymphoproliferative neoplasms, familial" and "Ddx41-related susceptibility to familial myeloproliferative/lymphoproliferative neoplasms". DDX41 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350709 [Multi-domain]  Cd Length: 206  Bit Score: 148.26  E-value: 4.60e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  15 LTNLNELGYLTMTPVQAAALPAILAGKDVRVQAKTGSGKTAAFGLGLL-----QQIDASLFQTQ---ALVLCPTRELADQ 86
Cdd:cd17951    2 LKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLImfaleQEKKLPFIKGEgpyGLIVCPSRELARQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  87 VAGELRRLARFL-----PNTKILTLCGGQPFGMQRDSLQHAPHIIVATPGRLLDHLQKGTVSLDALNTLVMDEADRMLDM 161
Cdd:cd17951   82 THEVIEYYCKALqeggyPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMIDM 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 446045882 162 GFSDAIDDVIRFAPASRQTLLFSATWPEAIAAISGRVQRDPLAI 205
Cdd:cd17951  162 GFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
18-186 4.27e-41

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: 146.62  E-value: 4.27e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  18 LNELGYLTMTPVQAAALP-AILAGKDVRVQAKTGSGKTAAFGL----GLLQQIDASLFQT-----QALVLCPTRELADQV 87
Cdd:cd17946    5 LADLGFSEPTPIQALALPaAIRDGKDVIGAAETGSGKTLAFGIpileRLLSQKSSNGVGGkqkplRALILTPTRELAVQV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  88 AGELRRLARFlPNTKILTLCGGQPFGMQRDSLQHAPHIIVATPGRLLDHLQKG---TVSLDALNTLVMDEADRMLDMG-F 163
Cdd:cd17946   85 KDHLKAIAKY-TNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGnehLANLKSLRFLVLDEADRMLEKGhF 163
                        170       180
                 ....*....|....*....|....*....
gi 446045882 164 S------DAIDDVIRFAPASRQTLLFSAT 186
Cdd:cd17946  164 AelekilELLNKDRAGKKRKRQTFVFSAT 192
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
4-186 1.21e-40

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: 144.39  E-value: 1.21e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882   4 FSTLNVLPPAQLTnLNELGYLTMTPVQAAALPAILAGKDVRVQAKTGSGKTAAFGLGLLQQIdaslfqtQALVLCPTREL 83
Cdd:cd17938    1 FEELGVMPELIKA-VEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIV-------VALILEPSREL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  84 ADQVAGELRRLARFLPNTKI--LTLCGGQPFGMQRDSLQHAPHIIVATPGRLLDHLQKGTVSLDALNTLVMDEADRMLDM 161
Cdd:cd17938   73 AEQTYNCIENFKKYLDNPKLrvALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQ 152
                        170       180       190
                 ....*....|....*....|....*....|.
gi 446045882 162 GFSDAIDDVIRFAPASR------QTLLFSAT 186
Cdd:cd17938  153 GNLETINRIYNRIPKITsdgkrlQVIVCSAT 183
RRM_EcDbpA_like cd12501
RNA recognition motif (RRM) found in Escherichia coli RNA helicase dbpA and similar proteins; ...
384-456 1.16e-39

RNA recognition motif (RRM) found in Escherichia coli RNA helicase dbpA and similar proteins; This subgroup corresponds to the C-terminal RRM homology domain of dbpA. E. coli dbpA is a member of the DbpA subfamily of prokaryotic DEAD-box rRNA helicases that have been implicated in ribosome biogenesis. It binds with high affinity and specificity for RNA substrates containing hairpin 92 of 23S rRNA (HP92) with either 3' or 5' extensions. As a non-processive ATP-dependent helicase, DbpA destabilizes and unwinds short <9bp (base pairs) RNA duplexes as well as long duplex RNA stretches. It disrupts RNA helices exclusively in a 3'- 5' direction and requires a single-stranded loading site 3' of the substrate helix. dbpA contains two N-terminal ATPase catalytic domains and a C-terminal RNA binding domain, an atypical RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNPs (ribonucleoprotein domain). The catalytic domains bind to nearby regions of RNA to stimulate ATP hydrolysis and disrupt RNA structures. The C-terminal domain binds specifically to hairpin 92.


Pssm-ID: 409924 [Multi-domain]  Cd Length: 73  Bit Score: 136.99  E-value: 1.16e-39
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446045882 384 TLCIDGGKKAKMRPGDVLGALTGDIGLDGADIGKIAVHPAHVYVAVRQAVAHKAWKQLQGGKIKGKTCRVRLL 456
Cdd:cd12501    1 TIQIDGGKKQKLRPGDILGALTGDNGIDGEDIGKINITDFVSYVAVKRSVAKDALKKLREGKIKGRKFRVRLL 73
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
21-205 3.41e-39

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: 140.24  E-value: 3.41e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  21 LGYLTMTPVQAAALPAILAGKDVRVQAKTGSGKTAAFGLGLLQQI-DASLFQTQ----ALVLCPTRELADQVAGELRRLA 95
Cdd:cd17952    8 QEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHImDQRELEKGegpiAVIVAPTRELAQQIYLEAKKFG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  96 RfLPNTKILTLCGGQPFGMQRDSLQHAPHIIVATPGRLLDHLQKGTVSLDALNTLVMDEADRMLDMGFSDAIDDVIRFAP 175
Cdd:cd17952   88 K-AYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRSIVGHVR 166
                        170       180       190
                 ....*....|....*....|....*....|
gi 446045882 176 ASRQTLLFSATWPEAIAAISGRVQRDPLAI 205
Cdd:cd17952  167 PDRQTLLFSATFKKKIEQLARDILSDPIRV 196
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
15-205 3.14e-38

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: 137.60  E-value: 3.14e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  15 LTNLNELGYLTMTPVQAAALPAILAGKDVRVQAKTGSGKTAAFGLGLLQQIDASLFQTQ------ALVLCPTRELADQVA 88
Cdd:cd17958    2 MKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIPREqrngpgVLVLTPTRELALQIE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  89 GELRRLArfLPNTKILTLCGGQPFGMQRDSLQHAPHIIVATPGRLLDHLQKGTVSLDALNTLVMDEADRMLDMGFSDAID 168
Cdd:cd17958   82 AECSKYS--YKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIR 159
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 446045882 169 DVIRFAPASRQTLLFSATWPEAIAAISGRVQRDPLAI 205
Cdd:cd17958  160 KILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
17-189 1.31e-37

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: 136.13  E-value: 1.31e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  17 NLNELGYLTMTPVQAAALPAILAGKDVRVQAKTGSGKTAAFGLGLLQQIDASLfQT-------QALVLCPTRELADQVAG 89
Cdd:cd17944    4 LLQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQ-QPrkrgrapKVLVLAPTRELANQVTK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  90 ELRRLARFLpntKILTLCGGQPFGMQRDSLQHAPHIIVATPGRLLDHLQKGTVSLDALNTLVMDEADRMLDMGFSDAIDD 169
Cdd:cd17944   83 DFKDITRKL---SVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEE 159
                        170       180
                 ....*....|....*....|....*
gi 446045882 170 VIRFAPASR-----QTLLFSATWPE 189
Cdd:cd17944  160 ILSVSYKKDsednpQTLLFSATCPD 184
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
27-207 1.47e-36

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: 134.37  E-value: 1.47e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  27 TPVQAAALPAILAGKDVRVQAKTGSGKTAAFGLGLLQQIDASLFQTQA-----LVLCPTRELADQV---AGELRRLARFl 98
Cdd:cd18049   48 TAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERGdgpicLVLAPTRELAQQVqqvAAEYGRACRL- 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  99 pntKILTLCGGQPFGMQRDSLQHAPHIIVATPGRLLDHLQKGTVSLDALNTLVMDEADRMLDMGFSDAIDDVIRFAPASR 178
Cdd:cd18049  127 ---KSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDR 203
                        170       180
                 ....*....|....*....|....*....
gi 446045882 179 QTLLFSATWPEAIAAISGRVQRDPLAIEI 207
Cdd:cd18049  204 QTLMWSATWPKEVRQLAEDFLKDYIHINI 232
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
27-207 4.56e-34

DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or DEAD Box Protein P82) has a wide variety of functions including regulating the alternative splicing of exons exhibiting specific features such as the inclusion of AC-rich alternative exons in CD44 transcripts, playing a role in innate immunity, and promoting mRNA degradation mediated by the antiviral zinc-finger protein ZC3HAV1 in an ATPase-dependent manner. DDX17 synergizes with DDX5 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. DDX17 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350808 [Multi-domain]  Cd Length: 271  Bit Score: 128.59  E-value: 4.56e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  27 TPVQAAALPAILAGKDVRVQAKTGSGKTAAFGLGLLQQIDASLFQTQA-----LVLCPTRELADQV---AGELRRLARFl 98
Cdd:cd18050   86 TPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGdgpicLVLAPTRELAQQVqqvADDYGKSSRL- 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  99 pntKILTLCGGQPFGMQRDSLQHAPHIIVATPGRLLDHLQKGTVSLDALNTLVMDEADRMLDMGFSDAIDDVIRFAPASR 178
Cdd:cd18050  165 ---KSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDR 241
                        170       180
                 ....*....|....*....|....*....
gi 446045882 179 QTLLFSATWPEAIAAISGRVQRDPLAIEI 207
Cdd:cd18050  242 QTLMWSATWPKEVRQLAEDFLRDYVQINI 270
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
227-336 1.90e-32

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: 119.24  E-value: 1.90e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  227 GKIPLLQRLLSLHQPSSCVVFCNTKKDCQavCDAL-NEVGQSALSLHGDLEQRDRDQTLVRFANGSARVLVATDVAARGL 305
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLE--AELLlEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 446045882  306 DIKSLELVVNFELAWDPEVHVHRIGRTARAG 336
Cdd:pfam00271  79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
15-220 5.02e-32

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: 122.09  E-value: 5.02e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  15 LTNLNELGYLTMTPVQAAALPAILAGKDVRVQAKTGSGKTAAFGLGLLQQIDASLFQTQ-------ALVLCPTRELADQV 87
Cdd:cd17948    2 VEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEgpfnaprGLVITPSRELAEQI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  88 AGELRRLARFLP-NTKILTlcGGQPFGMQRDSLQHAPHIIVATPGRLLDHLQKGTVSLDALNTLVMDEADRMLDMGFSDA 166
Cdd:cd17948   82 GSVAQSLTEGLGlKVKVIT--GGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEK 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446045882 167 IDDVIRFAP-ASR------------QTLLFSATWPEAIAAISGRVQrDPLAIEIDSTDAL----PPIEQQF 220
Cdd:cd17948  160 LSHFLRRFPlASRrsentdgldpgtQLVLVSATMPSGVGEVLSKVI-DVDSIETVTSDKLhrlmPHVKQKF 229
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
17-186 1.08e-30

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: 118.50  E-value: 1.08e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  17 NLNELGYLTMTPVQAAALPAILAG---------KDVRVQAKTGSGKTAAFGLGLLQQI-DASLFQTQALVLCPTRELADQ 86
Cdd:cd17956    4 NLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQALsKRVVPRLRALIVVPTKELVQQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  87 VAGELRRLARFLpNTKILTLCGGQPFGMQRDSLQHAPH--------IIVATPGRLLDHLQKGT-VSLDALNTLVMDEADR 157
Cdd:cd17956   84 VYKVFESLCKGT-GLKVVSLSGQKSFKKEQKLLLVDTSgrylsrvdILVATPGRLVDHLNSTPgFTLKHLRFLVIDEADR 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 446045882 158 MLDMGFSDAIDDVIR--------------------FAPASRQTLLFSAT 186
Cdd:cd17956  163 LLNQSFQDWLETVMKalgrptapdlgsfgdanlleRSVRPLQKLLFSAT 211
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
15-207 3.35e-25

DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH) is a testis-specific protein essential for completion of spermatogenesis. DDX25 is also a novel negative regulator of IFN pathway and facilitates RNA virus infection. Diseases associated with DDX25 include hydrolethalus syndrome, an autosomal recessive lethal malformation syndrome characterized by multiple developmental defects of fetus.. DDX25 (also called gonadotropin-regulated testicular RNA helicase) is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350806 [Multi-domain]  Cd Length: 229  Bit Score: 103.18  E-value: 3.35e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  15 LTNLNELGYLTMTPVQAAALPAILAG--KDVRVQAKTGSGKTAAFGLGLLQQIDASLFQTQALVLCPTRELADQVAGELR 92
Cdd:cd18048   30 LRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQCLCLSPTFELALQTGKVVE 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  93 RLARFLPNTKIL-TLCGGQPFGMQRDSLQhaphIIVATPGRLLDHLQK-GTVSLDALNTLVMDEADRMLDM-GFSDAIDD 169
Cdd:cd18048  110 EMGKFCVGIQVIyAIRGNRPGKGTDIEAQ----IVIGTPGTVLDWCFKlRLIDVTNISVFVLDEADVMINVqGHSDHSVR 185
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 446045882 170 VIRFAPASRQTLLFSATWPEAIAAISGRVQRDPLAIEI 207
Cdd:cd18048  186 VKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKL 223
HELICc smart00490
helicase superfamily c-terminal domain;
255-336 4.31e-24

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 95.36  E-value: 4.31e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882   255 QAVCDALNEVGQSALSLHGDLEQRDRDQTLVRFANGSARVLVATDVAARGLDIKSLELVVNFELAWDPEVHVHRIGRTAR 334
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   ..
gi 446045882   335 AG 336
Cdd:smart00490  81 AG 82
DbpA pfam03880
DbpA RNA binding domain; This RNA binding domain is found at the C-terminus of a number of ...
384-455 2.69e-23

DbpA RNA binding domain; This RNA binding domain is found at the C-terminus of a number of DEAD helicase proteins. It is sufficient to confer specificity for hairpin 92 of 23S rRNA, which is part of the ribosomal A-site. However, several members of this family lack specificity for 23S rRNA. These can proteins can generally be distinguished by a basic region that extends beyond this domain [Karl Kossen, unpublished data].


Pssm-ID: 461082 [Multi-domain]  Cd Length: 72  Bit Score: 92.82  E-value: 2.69e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446045882  384 TLCIDGGKKAKMRPGDVLGALTGDIGLDGADIGKIAVHPAHVYVAVRQAVAHKAWKQLQGGKIKGKTCRVRL 455
Cdd:pfam03880   1 RLFINVGKKDGVRPGDIVGALANEAGLPGDDIGKIDIFDNFSFVEVPAEKAEKVLKALKGTKIKGRKVRVEP 72
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
28-314 2.89e-23

Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 102.41  E-value: 2.89e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  28 PVQAAALPAILA-----GKDVRVQAKTGSGKTAaFGLGLLQQIdasLFQTQALVLCPTRELADQVAgelRRLARFLPNtk 102
Cdd:COG1061   83 PYQQEALEALLAalergGGRGLVVAPTGTGKTV-LALALAAEL---LRGKRVLVLVPRRELLEQWA---EELRRFLGD-- 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 103 iltlcggQPFGMQRDSLQHapHIIVATPGRLLDHLQKGTVSlDALNTLVMDEADRmldmGFSDAIDDVIRFAPASRqTLL 182
Cdd:COG1061  154 -------PLAGGGKKDSDA--PITVATYQSLARRAHLDELG-DRFGLVIIDEAHH----AGAPSYRRILEAFPAAY-RLG 218
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 183 FSAT----------------------WPEAIAA-----ISGRVQRDPLAIEIDSTDALPPIEQQFYETSSKGKIPLLQRL 235
Cdd:COG1061  219 LTATpfrsdgreillflfdgivyeysLKEAIEDgylapPEYYGIRVDLTDERAEYDALSERLREALAADAERKDKILREL 298
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 236 LSLH-QPSSCVVFCNTKKDCQAVCDALNEVGQSALSLHGDLEQRDRDQTLVRFANGSARVLVATDVAARGLDIKSLELVV 314
Cdd:COG1061  299 LREHpDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI 378
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
10-206 4.60e-22

DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both mRNA (mRNA) export from the nucleus into the cytoplasm and in mRNA translation. DDX19 functions in the nucleus in resolving RNA:DNA hybrids (R-loops). Activation of a DNA damage response pathway dependent upon the ATR kinase, a major regulator of replication fork progression, stimulates translocation of DDX19 from the cytoplasm into the nucleus. Only nuclear Ddx19 is competent to resolve R-loops. DDX19 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350805 [Multi-domain]  Cd Length: 205  Bit Score: 93.63  E-value: 4.60e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  10 LPPAQLTNLNELGYLTMTPVQAAALPAILAG--KDVRVQAKTGSGKTAAFGLGLLQQIDASLFQTQALVLCPTRELADQV 87
Cdd:cd18047    8 LKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYELALQT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  88 AGELRRLARFLPNTKILTLCGGQPfgMQRdSLQHAPHIIVATPGRLLDHLQK-GTVSLDALNTLVMDEADRML-DMGFSD 165
Cdd:cd18047   88 GKVIEQMGKFYPELKLAYAVRGNK--LER-GQKISEQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIaTQGHQD 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 446045882 166 AIDDVIRFAPASRQTLLFSATWPEAIAAISGRVQRDPLAIE 206
Cdd:cd18047  165 QSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 205
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
40-186 4.28e-18

N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 80.91  E-value: 4.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  40 GKDVRVQAKTGSGKTAAFGLGLLQQIDAslFQTQALVLCPTRELADQVAGELRRLARflPNTKILTLCGGQPFGMQRDS- 118
Cdd:cd00046    1 GENVLITAPTGSGKTLAALLAALLLLLK--KGKKVLVLVPTKALALQTAERLRELFG--PGIRVAVLVGGSSAEEREKNk 76
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446045882 119 LQHAPhIIVATPGRLLDHLQ-KGTVSLDALNTLVMDEADRMLDMGFSDAIDD--VIRFAPASRQTLLFSAT 186
Cdd:cd00046   77 LGDAD-IIIATPDMLLNLLLrEDRLFLKDLKLIIVDEAHALLIDSRGALILDlaVRKAGLKNAQVILLSAT 146
RRM_DbpA cd12252
RNA recognition motif (RRM) found in the DbpA subfamily of prokaryotic DEAD-box rRNA helicases; ...
384-454 4.35e-17

RNA recognition motif (RRM) found in the DbpA subfamily of prokaryotic DEAD-box rRNA helicases; This subfamily corresponds to the C-terminal RRM homology domain of dbpA proteins implicated in ribosome biogenesis. They bind with high affinity and specificity to RNA substrates containing hairpin 92 of 23S rRNA (HP92), which is part of the ribosomal A-site. The majority of dbpA proteins contain two N-terminal ATPase catalytic domains and a C-terminal RNA binding domain, an atypical RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNPs (ribonucleoprotein domain). The catalytic domains bind to nearby regions of RNA to stimulate ATP hydrolysis and disrupt RNA structures. The C-terminal domain is responsible for the high-affinity RNA binding. Several members of this family lack specificity for 23S rRNA. These proteins can generally be distinguished by a basic region that extends beyond the C-terminal domain.


Pssm-ID: 409698 [Multi-domain]  Cd Length: 71  Bit Score: 75.28  E-value: 4.35e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446045882 384 TLCIDGGKKAKMRPGDVLGALTGDIGLDGADIGKIAVHPAHVYVAVRQAVAHKAWKQLQGGKIKGKTCRVR 454
Cdd:cd12252    1 RLFINVGRKDGIDPRDLLGAICRAGGISRDDIGAIRIFDNFSFVEVPEAEAERVIEALNGKKIKGKKLRVE 71
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
4-188 2.94e-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: 75.11  E-value: 2.94e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882   4 FSTLNVLPP--------AQLTNLNELGYLTMTPVQAAALPAIL---AGKDVRVQ-------------AKTGSGKTAAFGL 59
Cdd:cd17965    1 FDQLKLLPSvreaiikeILKGSNKTDEEIKPSPIQTLAIKKLLktlMRKVTKQTsneepklevfllaAETGSGKTLAYLA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  60 GLL-----QQIDASLFQTQ------------ALVLCPTRELADQVAGELRRLARFLP-NTKILTLCGGQPFGMQRDSLQH 121
Cdd:cd17965   81 PLLdylkrQEQEPFEEAEEeyesakdtgrprSVILVPTHELVEQVYSVLKKLSHTVKlGIKTFSSGFGPSYQRLQLAFKG 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446045882 122 APHIIVATPGRLLDHLQKGTVSLDALNTLVMDEADRMLDMGFSDAIDDVIRFAPASRQTLLFSATWP 188
Cdd:cd17965  161 RIDILVTTPGKLASLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIP 227
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
231-336 1.62e-14

ERCC4-related helicase [Replication, recombination and repair];


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 75.92  E-value: 1.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 231 LLQRLLSLHQPSSCVVFCNTKKDCQAVCDALNE--------VGQSALSLHGDLEQRDRDQTLVRFANGSARVLVATDVAA 302
Cdd:COG1111  343 ILKEQLGTNPDSRIIVFTQYRDTAEMIVEFLSEpgikagrfVGQASKEGDKGLTQKEQIEILERFRAGEFNVLVATSVAE 422
                         90       100       110
                 ....*....|....*....|....*....|....
gi 446045882 303 RGLDIKSLELVVNFELAWDPEVHVHRIGRTARAG 336
Cdd:COG1111  423 EGLDIPEVDLVIFYEPVPSEIRSIQRKGRTGRKR 456
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
18-298 7.96e-13

Replicative superfamily II helicase [Replication, recombination and repair];


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 70.31  E-value: 7.96e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  18 LNELGYLTMTPVQAAALPA-ILAGKDVRVQAKTGSGKTAAFGLGLLQQIDASLfqtQALVLCPTRELADQVAGELRRLAR 96
Cdd:COG1204   15 LKERGIEELYPPQAEALEAgLLEGKNLVVSAPTASGKTLIAELAILKALLNGG---KALYIVPLRALASEKYREFKRDFE 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  97 FLP-NTKILTlcGGQPFgmqRDSLQHAPHIIVATPGRLLDHLQKGTVSLDALNTLVMDEAdRMLD-----MGFSDAIDDV 170
Cdd:COG1204   92 ELGiKVGVST--GDYDS---DDEWLGRYDILVATPEKLDSLLRNGPSWLRDVDLVVVDEA-HLIDdesrgPTLEVLLARL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 171 IRFAPASrQTLLFSATW--PEAIAAISGrvqrdplAIEIDSTDalPPIEQ----------QFYETSSKGKIPLLQRLL-S 237
Cdd:COG1204  166 RRLNPEA-QIVALSATIgnAEEIAEWLD-------AELVKSDW--RPVPLnegvlydgvlRFDDGSRRSKDPTLALALdL 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 238 LHQPSSCVVFCNTKKDCQAVC----------------DALNEVGQSALSL---------------------HGDLEQRDR 280
Cdd:COG1204  236 LEEGGQVLVFVSSRRDAESLAkkladelkrrltpeerEELEELAEELLEVseethtnekladclekgvafhHAGLPSELR 315
                        330       340
                 ....*....|....*....|
gi 446045882 281 DqtLVR--FANGSARVLVAT 298
Cdd:COG1204  316 R--LVEdaFREGLIKVLVAT 333
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
227-330 6.86e-12

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: 62.49  E-value: 6.86e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 227 GKIPLLQRLLSLHQPSS--CVVFCNTKKDCQAVCDALNEVGQSALSLHGDLEQRDRDQTLVRFANGSA--RVLVATDVAA 302
Cdd:cd18793   11 GKLEALLELLEELREPGekVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDirVFLLSTKAGG 90
                         90       100       110
                 ....*....|....*....|....*....|....
gi 446045882 303 RGLDIKSLELVVNFELAWDPEVH------VHRIG 330
Cdd:cd18793   91 VGLNLTAANRVILYDPWWNPAVEeqaidrAHRIG 124
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
42-336 7.08e-12

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: 66.68  E-value: 7.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  42 DVRVQAKTGSGKTAAFGLGLLQQIDASLFQTQALVLcPTRELADQVAgeLRRLARFLPNTKILTLCGGQPFGMQRDS--- 118
Cdd:cd09639    1 LLVIEAPTGYGKTEAALLWALHSLKSQKADRVIIAL-PTRATINAMY--RRAKEAFGETGLYHSSILSSRIKEMGDSeef 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 119 ------LQHAPHIIVATPGRL--LDHLQK---GTVSLD-------ALNTLVMDEADRMLD--MGFSDAIDDVIRFAPASr 178
Cdd:cd09639   78 ehlfplYIHSNDTLFLDPITVctIDQVLKsvfGEFGHYeftlasiANSLLIFDEVHFYDEytLALILAVLEVLKDNDVP- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 179 qTLLFSATWPEAIAaisgRVQRDPLAIEIDSTDALPPIEQQFY---ETSSKGKIPLLQRLL-SLHQPSSCVVFCNTKKDC 254
Cdd:cd09639  157 -ILLMSATLPKFLK----EYAEKIGYVEENEPLDLKPNERAPFikiESDKVGEISSLERLLeFIKKGGSVAIIVNTVDRA 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 255 QAVCDALNEVGQSA--LSLHGDLEQRDR----DQTLVRFANGSARVLVATDVAARGLDIkSLELVVNfELAwDPEVHVHR 328
Cdd:cd09639  232 QEFYQQLKEKGPEEeiMLIHSRFTEKDRakkeAELLLEFKKSEKFVIVATQVIEASLDI-SVDVMIT-ELA-PIDSLIQR 308

                 ....*...
gi 446045882 329 IGRTARAG 336
Cdd:cd09639  309 LGRLHRYG 316
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
25-155 8.07e-11

DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350679 [Multi-domain]  Cd Length: 181  Bit Score: 60.74  E-value: 8.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  25 TMTPVQAAAL-PAILAGKDVRVQAKTGSGKTAAFGLGLLQQIDASLFQtqALVLCPTRELADQVAGELRRlaRFLPNTKI 103
Cdd:cd17921    1 LLNPIQREALrALYLSGDSVLVSAPTSSGKTLIAELAILRALATSGGK--AVYIAPTRALVNQKEADLRE--RFGPLGKN 76
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446045882 104 LTLCGGQPfgmQRDSLQHA-PHIIVATPGRLLDHLQKG-TVSLDALNTLVMDEA 155
Cdd:cd17921   77 VGLLTGDP---SVNKLLLAeADILVATPEKLDLLLRNGgERLIQDVRLVVVDEA 127
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
30-155 3.87e-10

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: 58.75  E-value: 3.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  30 QAAALPAILAGKDVRVQAKTGSGKTAAFGLGLLQQIdASLFQTQALVLCPTRELA-DQVAgELRRLAR-FLPNTKILTLC 107
Cdd:cd17923    5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEAL-LRDPGSRALYLYPTKALAqDQLR-SLRELLEqLGLGIRVATYD 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446045882 108 GGQPFGMQRDSLQHAPHIIVATPGRL----LDHLQKGTVSLDALNTLVMDEA 155
Cdd:cd17923   83 GDTPREERRAIIRNPPRILLTNPDMLhyalLPHHDRWARFLRNLRYVVLDEA 134
cas3_core TIGR01587
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ...
42-336 4.00e-10

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: 61.32  E-value: 4.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882   42 DVRVQAKTGSGKTAAFGLGLLQQIDASLFQTQALVLcPTRELADQVAgeLRRLARFLPNTkILTLCGGQP--FGMQRDS- 118
Cdd:TIGR01587   1 LLVIEAPTGYGKTEAALLWALHSIKSQKADRVIIAL-PTRATINAMY--RRAKELFGSEL-VGLHHSSSFsrIKEMGDSe 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  119 --------LQHAPHIIVATPGRL--LDHLQK---GTVSLD-------ALNTLVMDEADRMLD--MGFSDAIDDVIRFAPA 176
Cdd:TIGR01587  77 efehlfplYIHSNDKLFLDPITVctIDQVLKsvfGEFGHYeftlasiANSLLIFDEVHFYDEytLALILAVLEVLKDNDV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  177 SrqTLLFSATWPEaiaaisgRVQRDPLAIEID-STDALPPIEQQFYE--------TSSKGKIPLLQRLL-SLHQPSSCVV 246
Cdd:TIGR01587 157 P--ILLMSATLPK-------FLKEYAEKIGYVeFNEPLDLKEERRFEnhrfilieSDKVGEISSLERLLeFIKKGGSIAI 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  247 FCNTKKDCQAVCDALNEVG--QSALSLHGDLEQRDRD----QTLVRFANGSA-RVLVATDVAARGLDIkSLELVVNfELA 319
Cdd:TIGR01587 228 IVNTVDRAQEFYQQLKEKApeEEIILYHSRFTEKDRAkkeaELLREMKKSNEkFVIVATQVIEASLDI-SADVMIT-ELA 305
                         330
                  ....*....|....*..
gi 446045882  320 wDPEVHVHRIGRTARAG 336
Cdd:TIGR01587 306 -PIDSLIQRLGRLHRYG 321
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
30-130 6.51e-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: 61.39  E-value: 6.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  30 QAAALPAILAGKDVRVQAKTGSGKTAAFGL----GLLQQIDASlfqtqALVLCPTRELA-DQVAgELRRLARFL-PNTKI 103
Cdd:COG1205   61 QAEAIEAARAGKNVVIATPTASGKSLAYLLpvleALLEDPGAT-----ALYLYPTKALArDQLR-RLRELAEALgLGVRV 134
                         90       100
                 ....*....|....*....|....*..
gi 446045882 104 LTLCGGQPFGmQRDSLQHAPHIIVATP 130
Cdd:COG1205  135 ATYDGDTPPE-ERRWIREHPDIVLTNP 160
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
228-342 2.11e-09

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: 55.68  E-value: 2.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 228 KIPLLQRL---LSLHQPSS----CVVFCNTKKDCQAV---------------CDALNEVGQSALSLHGDLEQRDRDQTLV 285
Cdd:cd18802    5 VIPKLQKLieiLREYFPKTpdfrGIIFVERRATAVVLsrllkehpstlafirCGFLIGRGNSSQRKRSLMTQRKQKETLD 84
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446045882 286 RFANGSARVLVATDVAARGLDIKSLELVVNFELAWDPEVHVHRIGRtARAGNSGLAI 342
Cdd:cd18802   85 KFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARAPNSKYIL 140
PRK13766 PRK13766
Hef nuclease; Provisional
231-336 3.82e-09

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 59.12  E-value: 3.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 231 LLQRLLSLHQPSSCVVFCNTKKDCQAVCDALNE--------VGQSalSLHGD--LEQRDRDQTLVRFANGSARVLVATDV 300
Cdd:PRK13766 355 IVKEQLGKNPDSRIIVFTQYRDTAEKIVDLLEKegikavrfVGQA--SKDGDkgMSQKEQIEILDKFRAGEFNVLVSTSV 432
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 446045882 301 AARGLDIKSLELVVNFElawdP---EVH-VHRIGRTARAG 336
Cdd:PRK13766 433 AEEGLDIPSVDLVIFYE----PvpsEIRsIQRKGRTGRQE 468
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
220-336 9.60e-09

C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350181 [Multi-domain]  Cd Length: 134  Bit Score: 53.75  E-value: 9.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 220 FYETSSKGKIP----LLQRLLSLHQPSSCVVFCNTKKDCQAVCDALNEVGQSALSLHGDLEQRDRDQTLVRFANGSARVL 295
Cdd:cd18794    5 FYSVRPKDKKDekldLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVI 84
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 446045882 296 VATdVA-ARGLDIKSLELVVNFELAWDPEVHVHRIGRTARAG 336
Cdd:cd18794   85 VAT-VAfGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDG 125
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
49-155 2.14e-08

DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350792 [Multi-domain]  Cd Length: 200  Bit Score: 54.19  E-value: 2.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  49 TGSGKT--AAFGLGLLQQIDASLFQ--TQALVLCPTRELADQVAGELRRLARFlpntKILTLCGGQPFGMQRDSLQHA-- 122
Cdd:cd18034   25 TGSGKTliAVMLIKEMGELNRKEKNpkKRAVFLVPTVPLVAQQAEAIRSHTDL----KVGEYSGEMGVDKWTKERWKEel 100
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446045882 123 --PHIIVATPGRLLDHLQKGTVSLDALNTLVMDEA 155
Cdd:cd18034  101 ekYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
264-334 8.28e-08

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: 51.20  E-value: 8.28e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446045882 264 VGQSALSLHGDLEQRDRDQTLVRFANGSARVLVATDVAARGLDIKSLELVVNFELAWDPEVHVHRIGRTAR 334
Cdd:cd18801   63 IGQASGKSSKGMSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR 133
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
217-332 5.68e-07

Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 52.15  E-value: 5.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 217 EQQFYETSSkGKIPLLQRLLS--LHQPSSCVVFCNTKKDCQAVCDALNEVGQSALSLHGDLEQRDRDQTLVRFANGSA-- 292
Cdd:COG0553  524 EGAELSGRS-AKLEALLELLEelLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEap 602
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 446045882 293 RVLVATDVAARGLDIKSLELVVNFELAWDPEVH------VHRIGRT 332
Cdd:COG0553  603 VFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEeqaidrAHRIGQT 648
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
29-130 1.81e-06

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: 48.51  E-value: 1.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  29 VQAAALPAIL-AGKDVRVQAKTGSGKTAAFGLGLLQ----QIDASLFQTQALVLCPTRELADQVAGELRrlARFLP-NTK 102
Cdd:cd18023    5 IQSEVFPDLLySDKNFVVSAPTGSGKTVLFELAILRllkeRNPLPWGNRKVVYIAPIKALCSEKYDDWK--EKFGPlGLS 82
                         90       100
                 ....*....|....*....|....*...
gi 446045882 103 ILTLCGGQPFGMQRDsLQHApHIIVATP 130
Cdd:cd18023   83 CAELTGDTEMDDTFE-IQDA-DIILTTP 108
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
243-314 2.37e-06

C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350186 [Multi-domain]  Cd Length: 116  Bit Score: 46.40  E-value: 2.37e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446045882 243 SCVVFCNTKKDCQAVCDALNEVGQSALSLHGDLEQRDR-DQTLVRFANG--SARVLVATDVAARGLDIKSLELVV 314
Cdd:cd18799    8 KTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERgDEALILLFFGelKPPILVTVDLLTTGVDIPEVDNVV 82
RRM_BsYxiN_like cd12500
RNA recognition motif (RRM) found in Bacillus subtilis ATP-dependent RNA helicase YxiN and ...
385-454 4.37e-06

RNA recognition motif (RRM) found in Bacillus subtilis ATP-dependent RNA helicase YxiN and similar proteins; This subgroup corresponds to the C-terminal RRM homology domain of YxiN. B. subtilis YxiN is a member of the DbpA subfamily of prokaryotic DEAD-box rRNA helicases that have been implicated in ribosome biogenesis. It binds with high affinity and specificity to RNA substrates containing hairpin 92 of 23S rRNA (HP92) with either 3' or 5' extensions in an ATP-dependent manner. YxiN contains two N-terminal ATPase catalytic domains and a C-terminal RNA binding domain, an atypical RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNPs (ribonucleoprotein domain). The catalytic domains bind to nearby regions of RNA to stimulate ATP hydrolysis and disrupt RNA structures. The C-terminal domain is responsible for the high-affinity RNA binding.


Pssm-ID: 409923 [Multi-domain]  Cd Length: 73  Bit Score: 44.37  E-value: 4.37e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 385 LCIDGGKKAKMRPGDVLGALTGDIGLDGADIGKIAVHPAHVYVAVRQAVAHKAWKQLQGGKIKGKTCRVR 454
Cdd:cd12500    2 LYFNGGKKKKIRAVDIVGAISNIDGVTGDDIGIITVQDNCSYVDILNGKGDHVLKVMKNTTIKGKQVKVN 71
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
27-57 8.84e-06

Lhr-like helicase [Replication, recombination and repair];


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 48.17  E-value: 8.84e-06
                         10        20        30
                 ....*....|....*....|....*....|..
gi 446045882  27 TPVQAAALPAILAGKDVRVQAKTGSGKT-AAF 57
Cdd:COG1201   26 TPPQREAWPAIAAGESTLLIAPTGSGKTlAAF 57
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
1-347 1.47e-05

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 47.40  E-value: 1.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882   1 MTAFSTLNVLPPAQLTNLNELGYLTMTPVQAAALPAILAGKDVRVQAKTGSGKTaafglgLLQQIDASLFQTQALVLCPT 80
Cdd:PRK11057   1 MAQAEVLNLESLAKQVLQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKS------LCYQIPALVLDGLTLVVSPL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  81 REL-ADQVaGELRR---LARFLPNTkiltlcggqpfgMQRDSLQ------HAPHI--IVATPGRL-----LDHLQKGTVS 143
Cdd:PRK11057  75 ISLmKDQV-DQLLAngvAAACLNST------------QTREQQLevmagcRTGQIklLYIAPERLmmdnfLEHLAHWNPA 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 144 LdalntLVMDEADRMLDMGFSdaiddvirFAPASRQTLLFSATWPE----AIAA---------ISGRVQ-RDPLaIEIDS 209
Cdd:PRK11057 142 L-----LAVDEAHCISQWGHD--------FRPEYAALGQLRQRFPTlpfmALTAtaddttrqdIVRLLGlNDPL-IQISS 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 210 TDAlPPIEqqfYETSSKGKiPLLQ--RLLSLHQPSSCVVFCNTKKDCQAVCDALNEVGQSALSLHGDLEQRDRDQTLVRF 287
Cdd:PRK11057 208 FDR-PNIR---YTLVEKFK-PLDQlmRYVQEQRGKSGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAF 282
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 288 ANGSARVLVATDVAARGLDIKSLELVVNFELAWDPEVHVHRIGRTARAGNSGLAISFCAP 347
Cdd:PRK11057 283 QRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYDP 342
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
22-155 2.10e-05

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: 45.22  E-value: 2.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  22 GYLTMTPVQAAALPAILAGKDVRVQAKTGSGKTAAFglgllqQIDASLFQTQALVLCPTREL-ADQVAgELRRLarflpN 100
Cdd:cd17920    9 GYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCY------QLPALLLDGVTLVVSPLISLmQDQVD-RLQQL-----G 76
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446045882 101 TKILTLCGGQPFGMQRDSLQ----HAPHIIVATPGRL-----LDHLQKGTvSLDALNTLVMDEA 155
Cdd:cd17920   77 IRAAALNSTLSPEEKREVLLriknGQYKLLYVTPERLlspdfLELLQRLP-ERKRLALIVVDEA 139
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
294-339 2.20e-05

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: 42.31  E-value: 2.20e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 446045882 294 VLVATDVAARGLDIKSLELVVNFELAWDPEVHVHRIGRTARAGNSG 339
Cdd:cd18785   25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDE 70
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
206-338 3.18e-05

C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350183 [Multi-domain]  Cd Length: 150  Bit Score: 43.79  E-value: 3.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 206 EIDSTDALPPIEQQFYETSSKGKIPLLQRLLSLHQPSSCVVFCNTKKDCQAVCDALNE-------VGQSALSlHGDLEQR 278
Cdd:cd18796    3 KLDIKVILPVAPEIFPWAGESGADAYAEVIFLLERHKSTLVFTNTRSQAERLAQRLRElcpdrvpPDFIALH-HGSLSRE 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446045882 279 DRDQTLVRFANGSARVLVATDVAARGLDIKSLELVVNFELAwdPEVH--VHRIGRTARAGNS 338
Cdd:cd18796   82 LREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSP--KSVArlLQRLGRSGHRPGA 141
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
25-158 3.45e-05

DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350676 [Multi-domain]  Cd Length: 180  Bit Score: 44.33  E-value: 3.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  25 TMTPVQAAALPAILagKDVR--------VQAKTGSGKTAAFGLGLLQQIDASlfqTQALVLCPTRELADQVAGELRrlaR 96
Cdd:cd17918   15 SLTKDQAQAIKDIE--KDLHspepmdrlLSGDVGSGKTLVALGAALLAYKNG---KQVAILVPTEILAHQHYEEAR---K 86
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446045882  97 FLPNTKILTLCGGqpfgmQRDSLQHAPHIIVATPGrLLDHLQKGtvslDALNTLVMDEADRM 158
Cdd:cd17918   87 FLPFINVELVTGG-----TKAQILSGISLLVGTHA-LLHLDVKF----KNLDLVIVDEQHRF 138
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
34-157 7.74e-05

DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350793 [Multi-domain]  Cd Length: 181  Bit Score: 43.27  E-value: 7.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  34 LPAILAGKDVRVQAKTGSGKTAA---FGLGLLQQIDAslfqtQALVLCPTRELADQVAGELRRLarFLPNTKILTLCGG- 109
Cdd:cd18035   10 IAAVALNGNTLIVLPTGLGKTIIailVAADRLTKKGG-----KVLILAPSRPLVEQHAENLKRV--LNIPDKITSLTGEv 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 446045882 110 QPfgMQRDSLQHAPHIIVATPGRLLDHLQKGTVSLDALNTLVMDEADR 157
Cdd:cd18035   83 KP--EERAERWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEAHH 128
ResIII pfam04851
Type III restriction enzyme, res subunit;
24-189 2.01e-04

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 41.89  E-value: 2.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882   24 LTMTPVQAAALPAILAG-----KDVRVQAKTGSGKT--AAFglgLLQQIDASLFQTQALVLCPTRELADQVageLRRLAR 96
Cdd:pfam04851   2 LELRPYQIEAIENLLESikngqKRGLIVMATGSGKTltAAK---LIARLFKKGPIKKVLFLVPRKDLLEQA---LEEFKK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882   97 FLPN----TKILTlcggqpfGMQRDSLQHAPHIIVATPGRL--LDHLQKGTVSLDALNTLVMDEADRmldmGFSDAIDDV 170
Cdd:pfam04851  76 FLPNyveiGEIIS-------GDKKDESVDDNKIVVTTIQSLykALELASLELLPDFFDVIIIDEAHR----SGASSYRNI 144
                         170
                  ....*....|....*....
gi 446045882  171 IRFAPASRQtLLFSATwPE 189
Cdd:pfam04851 145 LEYFKPAFL-LGLTAT-PE 161
RRM_EcCsdA_like cd12499
RNA recognition motif (RRM) found in Escherichia coli cold-shock DEAD box protein A (CsdA) and ...
387-456 3.83e-04

RNA recognition motif (RRM) found in Escherichia coli cold-shock DEAD box protein A (CsdA) and similar proteins; This subgroup corresponds to the C-terminal RRM homology domain of E. coli CsdA, also termed ATP-dependent RNA helicase deaD, or translation factor W2, a member of the DbpA subfamily of prokaryotic DEAD-box rRNA helicases that have been implicated in ribosome biogenesis. CsdA may be involved in translation initiation, gene regulation after cold-shock, mRNA decay and biogenesis of the large or small ribosomal subunit. It contains two N-terminal ATPase catalytic domains and a C-terminal RNA binding domain, an atypical RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNPs (ribonucleoprotein domain). The catalytic domains bind to nearby regions of RNA to stimulate ATP hydrolysis and disrupt RNA structures. The C-terminal domain is responsible for the high-affinity RNA binding.


Pssm-ID: 409922 [Multi-domain]  Cd Length: 73  Bit Score: 38.71  E-value: 3.83e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 387 IDGGKKAKMRPGDVLGALTGDIGLDGADIGKIAVHPAHVYVAVRQAVAHKAWKQLQGGKIKGKTCRVRLL 456
Cdd:cd12499    4 IEVGRKDGVKPGNIVGAIANEAGIDSRFIGRIKIFDDHSTVELPKGMPKDVLQHLKKVRVCGQPLNIKLL 73
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
28-154 7.85e-04

DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350786 [Multi-domain]  Cd Length: 177  Bit Score: 40.40  E-value: 7.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  28 PVQAAALPA-ILAGKDVRVQAKTGSGKTAafgLGLLQQIDASLFQTQALVLCPTRELADQVAGELRRLARFLPNTKILTl 106
Cdd:cd18028    4 PPQAEAVRAgLLKGENLLISIPTASGKTL---IAEMAMVNTLLEGGKALYLVPLRALASEKYEEFKKLEEIGLKVGIST- 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 446045882 107 cggqpfGMQRDSLQHAP--HIIVATPGRLLDHLQKGTVSLDALNTLVMDE 154
Cdd:cd18028   80 ------GDYDEDDEWLGdyDIIVATYEKFDSLLRHSPSWLRDVGVVVVDE 123
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
32-157 9.76e-04

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: 40.49  E-value: 9.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  32 AALPAILaGKDVRVQAKTGSGKTAAFGL---GLLQQIDASlFQTQALVLCPTRELADQVAGELRRLARfLPNTKILTLCG 108
Cdd:cd17927   10 LAQPALK-GKNTIICLPTGSGKTFVAVLiceHHLKKFPAG-RKGKVVFLANKVPLVEQQKEVFRKHFE-RPGYKVTGLSG 86
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 446045882 109 GQPFGMQRDSLQHAPHIIVATPGRLLDHLQKGT-VSLDALNTLVMDEADR 157
Cdd:cd17927   87 DTSENVSVEQIVESSDVIIVTPQILVNDLKSGTiVSLSDFSLLVFDECHN 136
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
40-130 1.06e-03

DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350680 [Multi-domain]  Cd Length: 166  Bit Score: 39.87  E-value: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  40 GKDVRVQAKTGSGKTAAFGLGLLQQI-DASLFQTQALVLCPTRELADQVAGELRRLAR-FLPNTKILTLCGGQPFGMQRD 117
Cdd:cd17922    1 GRNVLIAAPTGSGKTEAAFLPALSSLaDEPEKGVQVLYISPLKALINDQERRLEEPLDeIDLEIPVAVRHGDTSQSEKAK 80
                         90
                 ....*....|...
gi 446045882 118 SLQHAPHIIVATP 130
Cdd:cd17922   81 QLKNPPGILITTP 93
PRK13767 PRK13767
ATP-dependent helicase; Provisional
23-57 1.43e-03

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 41.02  E-value: 1.43e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 446045882  23 YLTMTPVQAAALPAILAGKDVRVQAKTGSGKT-AAF 57
Cdd:PRK13767  30 FGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAF 65
SF2_C_Ski2 cd18795
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ...
229-298 1.79e-03

C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350182 [Multi-domain]  Cd Length: 154  Bit Score: 38.69  E-value: 1.79e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446045882 229 IPLLQRLLSLHQPSSCVVFCNTKKDCQAVCDALNEVGqsalSLHGDLEQRDRdqTLVR--FANGSARVLVAT 298
Cdd:cd18795   31 IIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLAGIA----FHHAGLTREDR--ELVEelFREGLIKVLVAT 96
PRK07246 PRK07246
bifunctional ATP-dependent DNA helicase/DNA polymerase III subunit epsilon; Validated
45-95 2.04e-03

bifunctional ATP-dependent DNA helicase/DNA polymerase III subunit epsilon; Validated


Pssm-ID: 180905 [Multi-domain]  Cd Length: 820  Bit Score: 40.83  E-value: 2.04e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446045882  45 VQAKTGSGKTAAFGLGLLQQIDaslfQTQALVLCPTRELADQV-AGELRRLA 95
Cdd:PRK07246 269 IEAQTGIGKTYGYLLPLLAQSD----QRQIIVSVPTKILQDQImAEEVKAIQ 316
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
28-186 2.15e-03

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: 38.44  E-value: 2.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  28 PVQAAALPAILAGKDVR---VQAKTGSGKTAafglgLLQQIDASLFQTQALVLCPTRELADQVAgelRRLARFLPNTKIL 104
Cdd:cd17926    3 PYQEEALEAWLAHKNNRrgiLVLPTGSGKTL-----TALALIAYLKELRTLIVVPTDALLDQWK---ERFEDFLGDSSIG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882 105 TLCGGqpfgmQRDSLQHAPhIIVATPGRLLDHLQKGTVSLDALNTLVMDEADRMLDMGFSDAIDdviRFAPASRqtLLFS 184
Cdd:cd17926   75 LIGGG-----KKKDFDDAN-VVVATYQSLSNLAEEEKDLFDQFGLLIVDEAHHLPAKTFSEILK---ELNAKYR--LGLT 143

                 ..
gi 446045882 185 AT 186
Cdd:cd17926  144 AT 145
DEXHc_RecQ4-like cd18018
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ...
21-186 6.05e-03

DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations cause Rothmund-Thomson/RAPADILINO/Baller-Gerold syndrome.


Pssm-ID: 350776 [Multi-domain]  Cd Length: 201  Bit Score: 38.01  E-value: 6.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  21 LGYLTMTPVQAAALPAILAGKDVRVQAKTGSGKTAAFglgllqQIDASLFQTQ----ALVLCPTREL-ADQVAGelrrLA 95
Cdd:cd18018    8 FGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCY------QLPALLLRRRgpglTLVVSPLIALmKDQVDA----LP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446045882  96 RFLpntKILTLCGGQPFGMQRDSLQHAP----HIIVATPGRLLDH------LQKGTVSLdalntLVMDEADRMLDMGFS- 164
Cdd:cd18018   78 RAI---KAAALNSSLTREERRRILEKLRagevKILYVSPERLVNEsfrellRQTPPISL-----LVVDEAHCISEWSHNf 149
                        170       180
                 ....*....|....*....|....*.
gi 446045882 165 --D--AIDDVIRFAPASRQTLLFSAT 186
Cdd:cd18018  150 rpDylRLCRVLRELLGAPPVLALTAT 175
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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