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Conserved domains on  [gi|1717936739|ref|WP_144453130|]
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MULTISPECIES: ATP-dependent RNA helicase DbpA [Bacillus]

Protein Classification

DEADc and RRM_BsYxiN_like domain-containing protein( domain architecture ID 11423694)

DEADc and RRM_BsYxiN_like domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
1-393 0e+00

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


:

Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 561.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739   1 MSHFKNYQISHDILRALEGLGYTEPTKVQQSVIPAVLERKDLVVKSQTGSGKTASFGIPLCELADWD-ENKPQALILTPT 79
Cdd:COG0513     1 MMSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSrPRAPQALILAPT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  80 RELAVQVKEDITNIGRFKRIKATAVFGKSSFDKQKAELKQKSHIVVGTPGRVLDHIEKGTLPLDRLSYLVIDEADEMLNM 159
Cdd:COG0513    81 RELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 160 GFIEQVEAIIKHLPTERTTMLFSATLPQDIEKLSRQYMQNPEHIEVKAAGLTTRNIEHAVIQVREENKFSLLKDVLMTEN 239
Cdd:COG0513   161 GFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLRDED 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 240 PDSCIIFCRTKEHVNQLTDELDDLGYPCDKIHGGMIQEDRFDVMNEFKRGEYRYLVATDVAARGIDIENISLVINYDLPL 319
Cdd:COG0513   241 PERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPE 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1717936739 320 EKESYVHRTGRTGRAGNKGKAISFVAAFEKRFLADIEEYIGFEIQKIEAPSQEEVARKKPE-FLAKLNDRPESKK 393
Cdd:COG0513   321 DPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKRLErLKPKIKEKLKGKK 395
RRM_BsYxiN_like cd12500
RNA recognition motif (RRM) found in Bacillus subtilis ATP-dependent RNA helicase YxiN and ...
405-477 4.55e-35

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: 125.27  E-value: 4.55e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1717936739 405 KLYFNGGKKKKIRAVDFVGTIAKIDGVSADDIGIITIMDNASYVEILNGKGPHVLKVMKNTTVKGKQLKVNKA 477
Cdd:cd12500     1 KLYFNGGKKKKIRAVDIVGAISNIDGVTGDDIGIITVQDNCSYVDILNGKGDHVLKVMKNTTIKGKQVKVNKA 73
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
1-393 0e+00

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 561.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739   1 MSHFKNYQISHDILRALEGLGYTEPTKVQQSVIPAVLERKDLVVKSQTGSGKTASFGIPLCELADWD-ENKPQALILTPT 79
Cdd:COG0513     1 MMSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSrPRAPQALILAPT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  80 RELAVQVKEDITNIGRFKRIKATAVFGKSSFDKQKAELKQKSHIVVGTPGRVLDHIEKGTLPLDRLSYLVIDEADEMLNM 159
Cdd:COG0513    81 RELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 160 GFIEQVEAIIKHLPTERTTMLFSATLPQDIEKLSRQYMQNPEHIEVKAAGLTTRNIEHAVIQVREENKFSLLKDVLMTEN 239
Cdd:COG0513   161 GFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLRDED 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 240 PDSCIIFCRTKEHVNQLTDELDDLGYPCDKIHGGMIQEDRFDVMNEFKRGEYRYLVATDVAARGIDIENISLVINYDLPL 319
Cdd:COG0513   241 PERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPE 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1717936739 320 EKESYVHRTGRTGRAGNKGKAISFVAAFEKRFLADIEEYIGFEIQKIEAPSQEEVARKKPE-FLAKLNDRPESKK 393
Cdd:COG0513   321 DPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKRLErLKPKIKEKLKGKK 395
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
14-474 6.94e-144

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 419.98  E-value: 6.94e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  14 LRALEGLGYTEPTKVQQSVIPAVLERKDLVVKSQTGSGKTASFGIPLCELADWDENKPQALILTPTRELAVQVKEDITNI 93
Cdd:PRK11776   16 LANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCPTRELADQVAKEIRRL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  94 GRFKR-IKATAVFGKSSFDKQKAELKQKSHIVVGTPGRVLDHIEKGTLPLDRLSYLVIDEADEMLNMGFIEQVEAIIKHL 172
Cdd:PRK11776   96 ARFIPnIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLDMGFQDAIDAIIRQA 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 173 PTERTTMLFSATLPQDIEKLSRQYMQNPEHIEVKAAGLTTRnIEHAVIQVREENKFSLLKDVLMTENPDSCIIFCRTKEH 252
Cdd:PRK11776  176 PARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDLPA-IEQRFYEVSPDERLPALQRLLLHHQPESCVVFCNTKKE 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 253 VNQLTDELDDLGYPCDKIHGGMIQEDRFDVMNEFKRGEYRYLVATDVAARGIDIENISLVINYDLPLEKESYVHRTGRTG 332
Cdd:PRK11776  255 CQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELARDPEVHVHRIGRTG 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 333 RAGNKGKAISFVAAFEKRFLADIEEYIGFEIQKIEAPSqeevarkkpefLAKLNDRPeskkdkseeLNKDIMKLYFNGGK 412
Cdd:PRK11776  335 RAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLPS-----------LSPLSGVP---------LLPEMVTLCIDGGK 394
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1717936739 413 KKKIRAVDFVGTIAKIDGVSADDIGIITIMDNASYVEILNGKGPHVLKVMKNTTVKGKQLKV 474
Cdd:PRK11776  395 KDKLRPGDILGALTGDAGLDGAQIGKINVTDFHAYVAVERAVAKKALKKLQNGKIKGKSFRV 456
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
13-204 5.55e-99

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: 295.51  E-value: 5.55e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  13 ILRALEGLGYTEPTKVQQSVIPAVLERKDLVVKSQTGSGKTASFGIPLCELADWDE----NKPQALILTPTRELAVQVKE 88
Cdd:cd00268     1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPkkkgRGPQALVLAPTRELAMQIAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  89 DITNIGRFKRIKATAVFGKSSFDKQKAELKQKSHIVVGTPGRVLDHIEKGTLPLDRLSYLVIDEADEMLNMGFIEQVEAI 168
Cdd:cd00268    81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKI 160
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1717936739 169 IKHLPTERTTMLFSATLPQDIEKLSRQYMQNPEHIE 204
Cdd:cd00268   161 LSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
26-192 3.89e-62

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


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 199.78  E-value: 3.89e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  26 TKVQQSVIPAVLERKDLVVKSQTGSGKTASFGIPLCELADWDENKPQALILTPTRELAVQVKEDITNIGRFKRIKATAVF 105
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 106 GKSSFDKQKAELKqKSHIVVGTPGRVLDHIEKgTLPLDRLSYLVIDEADEMLNMGFIEQVEAIIKHLPTERTTMLFSATL 185
Cdd:pfam00270  81 GGDSRKEQLEKLK-GPDILVGTPGRLLDLLQE-RKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSATL 158

                  ....*..
gi 1717936739 186 PQDIEKL 192
Cdd:pfam00270 159 PRNLEDL 165
DEXDc smart00487
DEAD-like helicases superfamily;
17-216 6.27e-53

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 176.91  E-value: 6.27e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739   17 LEGLGYTEPTKVQQSVIPAVLER-KDLVVKSQTGSGKTASFGIPLCELADwDENKPQALILTPTRELAVQVKEDITNIGR 95
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALK-RGKGGRVLVLVPTRELAEQWAEELKKLGP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739   96 FKRIKATAVFGKSSFDKQKAEL-KQKSHIVVGTPGRVLDHIEKGTLPLDRLSYLVIDEADEMLNMGFIEQVEAIIKHLPT 174
Cdd:smart00487  80 SLGLKVVGLYGGDSKREQLRKLeSGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPK 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1717936739  175 ERTTMLFSATLPQDIEKLSRQYMQNPEHIEVKAAGLTTRNIE 216
Cdd:smart00487 160 NVQLLLLSATPPEEIENLLELFLNDPVFIDVGFTPLEPIEQF 201
RRM_BsYxiN_like cd12500
RNA recognition motif (RRM) found in Bacillus subtilis ATP-dependent RNA helicase YxiN and ...
405-477 4.55e-35

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: 125.27  E-value: 4.55e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1717936739 405 KLYFNGGKKKKIRAVDFVGTIAKIDGVSADDIGIITIMDNASYVEILNGKGPHVLKVMKNTTVKGKQLKVNKA 477
Cdd:cd12500     1 KLYFNGGKKKKIRAVDIVGAISNIDGVTGDDIGIITVQDNCSYVDILNGKGDHVLKVMKNTTIKGKQVKVNKA 73
DbpA pfam03880
DbpA RNA binding domain; This RNA binding domain is found at the C-terminus of a number of ...
405-476 5.17e-21

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: 86.66  E-value: 5.17e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1717936739 405 KLYFNGGKKKKIRAVDFVGTIAKIDGVSADDIGIITIMDNASYVEILNGKGPHVLKVMKNTTVKGKQLKVNK 476
Cdd:pfam03880   1 RLFINVGKKDGVRPGDIVGALANEAGLPGDDIGKIDIFDNFSFVEVPAEKAEKVLKALKGTKIKGRKVRVEP 72
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
1-393 0e+00

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 561.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739   1 MSHFKNYQISHDILRALEGLGYTEPTKVQQSVIPAVLERKDLVVKSQTGSGKTASFGIPLCELADWD-ENKPQALILTPT 79
Cdd:COG0513     1 MMSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSrPRAPQALILAPT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  80 RELAVQVKEDITNIGRFKRIKATAVFGKSSFDKQKAELKQKSHIVVGTPGRVLDHIEKGTLPLDRLSYLVIDEADEMLNM 159
Cdd:COG0513    81 RELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 160 GFIEQVEAIIKHLPTERTTMLFSATLPQDIEKLSRQYMQNPEHIEVKAAGLTTRNIEHAVIQVREENKFSLLKDVLMTEN 239
Cdd:COG0513   161 GFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLRDED 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 240 PDSCIIFCRTKEHVNQLTDELDDLGYPCDKIHGGMIQEDRFDVMNEFKRGEYRYLVATDVAARGIDIENISLVINYDLPL 319
Cdd:COG0513   241 PERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPE 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1717936739 320 EKESYVHRTGRTGRAGNKGKAISFVAAFEKRFLADIEEYIGFEIQKIEAPSQEEVARKKPE-FLAKLNDRPESKK 393
Cdd:COG0513   321 DPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKRLErLKPKIKEKLKGKK 395
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
14-474 6.94e-144

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 419.98  E-value: 6.94e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  14 LRALEGLGYTEPTKVQQSVIPAVLERKDLVVKSQTGSGKTASFGIPLCELADWDENKPQALILTPTRELAVQVKEDITNI 93
Cdd:PRK11776   16 LANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCPTRELADQVAKEIRRL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  94 GRFKR-IKATAVFGKSSFDKQKAELKQKSHIVVGTPGRVLDHIEKGTLPLDRLSYLVIDEADEMLNMGFIEQVEAIIKHL 172
Cdd:PRK11776   96 ARFIPnIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLDMGFQDAIDAIIRQA 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 173 PTERTTMLFSATLPQDIEKLSRQYMQNPEHIEVKAAGLTTRnIEHAVIQVREENKFSLLKDVLMTENPDSCIIFCRTKEH 252
Cdd:PRK11776  176 PARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDLPA-IEQRFYEVSPDERLPALQRLLLHHQPESCVVFCNTKKE 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 253 VNQLTDELDDLGYPCDKIHGGMIQEDRFDVMNEFKRGEYRYLVATDVAARGIDIENISLVINYDLPLEKESYVHRTGRTG 332
Cdd:PRK11776  255 CQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELARDPEVHVHRIGRTG 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 333 RAGNKGKAISFVAAFEKRFLADIEEYIGFEIQKIEAPSqeevarkkpefLAKLNDRPeskkdkseeLNKDIMKLYFNGGK 412
Cdd:PRK11776  335 RAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLPS-----------LSPLSGVP---------LLPEMVTLCIDGGK 394
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1717936739 413 KKKIRAVDFVGTIAKIDGVSADDIGIITIMDNASYVEILNGKGPHVLKVMKNTTVKGKQLKV 474
Cdd:PRK11776  395 KDKLRPGDILGALTGDAGLDGAQIGKINVTDFHAYVAVERAVAKKALKKLQNGKIKGKSFRV 456
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
4-391 5.44e-113

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 346.45  E-value: 5.44e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739   4 FKNYQISHDILRALEGLGYTEPTKVQQSVIPAVLERKDLVVKSQTGSGKTASFGIPLCELADWDENKPQALILTPTRELA 83
Cdd:PRK11634    8 FADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAPTRELA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  84 VQVKEDITNIGRFKR-IKATAVFGKSSFDKQKAELKQKSHIVVGTPGRVLDHIEKGTLPLDRLSYLVIDEADEMLNMGFI 162
Cdd:PRK11634   88 VQVAEAMTDFSKHMRgVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGFI 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 163 EQVEAIIKHLPTERTTMLFSATLPQDIEKLSRQYMQNPEHIEVKAAgLTTR-NIEHAVIQVREENKFSLLKDVLMTENPD 241
Cdd:PRK11634  168 EDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSS-VTTRpDISQSYWTVWGMRKNEALVRFLEAEDFD 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 242 SCIIFCRTKEHVNQLTDELDDLGYPCDKIHGGMIQEDRFDVMNEFKRGEYRYLVATDVAARGIDIENISLVINYDLPLEK 321
Cdd:PRK11634  247 AAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDS 326
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1717936739 322 ESYVHRTGRTGRAGNKGKAISFVAAFEKRFLADIEEYIGFEIQKIEAPSQEEVA-RKKPEFLAKLNDRPES 391
Cdd:PRK11634  327 ESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEVELPNAELLGkRRLEKFAAKVQQQLES 397
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
4-415 6.57e-102

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 311.88  E-value: 6.57e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739   4 FKNYQISHDILRALEGLGYTEPTKVQQSVIPAVLERKDLVVKSQTGSGKTASFGIPLCE-LADWDENKPQA---LILTPT 79
Cdd:PRK11192    3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQhLLDFPRRKSGPpriLILTPT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  80 RELAVQVKEDITNIGRFKRIKATAVFGKSSFDKQKAELKQKSHIVVGTPGRVLDHIEKGTLPLDRLSYLVIDEADEMLNM 159
Cdd:PRK11192   83 RELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRMLDM 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 160 GFIEQVEAIIKHLPTERTTMLFSATLPQD-IEKLSRQYMQNPEHIEVKAAgltTRniEHAVIQV------REENKFSLLK 232
Cdd:PRK11192  163 GFAQDIETIAAETRWRKQTLLFSATLEGDaVQDFAERLLNDPVEVEAEPS---RR--ERKKIHQwyyradDLEHKTALLC 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 233 DVLMTENPDSCIIFCRTKEHVNQLTDELDDLGYPCDKIHGGMIQEDRFDVMNEFKRGEYRYLVATDVAARGIDIENISLV 312
Cdd:PRK11192  238 HLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHV 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 313 INYDLPLEKESYVHRTGRTGRAGNKGKAISFVAAFEKRFLADIEEYIGFEIQ---------KIEAPSQEEVARKKPEFLA 383
Cdd:PRK11192  318 INFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERYIEEPLKarvidelrpKTKAPSEKKTGKPSKKVLA 397
                         410       420       430
                  ....*....|....*....|....*....|..
gi 1717936739 384 KLNDRPESKKDKSEElnKDIMKLYFNGGKKKK 415
Cdd:PRK11192  398 KRAEKKEKEKEKPKV--KKRHRDTKNIGKRRK 427
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
1-372 1.93e-100

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 308.66  E-value: 1.93e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739   1 MShFKNYQISHDILRALEGLGYTEPTKVQQSVIPAVLERKDLVVKSQTGSGKTASFGIPLCELADWDENKPQ------AL 74
Cdd:PRK10590    1 MS-FDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKgrrpvrAL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  75 ILTPTRELAVQVKEDITNIGRFKRIKATAVFGKSSFDKQKAELKQKSHIVVGTPGRVLDHIEKGTLPLDRLSYLVIDEAD 154
Cdd:PRK10590   80 ILTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEAD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 155 EMLNMGFIEQVEAIIKHLPTERTTMLFSATLPQDIEKLSRQYMQNPEHIEVKAAGLTTRNIEHAVIQVREENKFSLLKDV 234
Cdd:PRK10590  160 RMLDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKRELLSQM 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 235 LMTENPDSCIIFCRTKEHVNQLTDELDDLGYPCDKIHGGMIQEDRFDVMNEFKRGEYRYLVATDVAARGIDIENISLVIN 314
Cdd:PRK10590  240 IGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVN 319
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1717936739 315 YDLPLEKESYVHRTGRTGRAGNKGKAISFVAAFEKRFLADIEEYIGFEIQKIEAPSQE 372
Cdd:PRK10590  320 YELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEIPRIAIPGYE 377
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
13-204 5.55e-99

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: 295.51  E-value: 5.55e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  13 ILRALEGLGYTEPTKVQQSVIPAVLERKDLVVKSQTGSGKTASFGIPLCELADWDE----NKPQALILTPTRELAVQVKE 88
Cdd:cd00268     1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPkkkgRGPQALVLAPTRELAMQIAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  89 DITNIGRFKRIKATAVFGKSSFDKQKAELKQKSHIVVGTPGRVLDHIEKGTLPLDRLSYLVIDEADEMLNMGFIEQVEAI 168
Cdd:cd00268    81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKI 160
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1717936739 169 IKHLPTERTTMLFSATLPQDIEKLSRQYMQNPEHIE 204
Cdd:cd00268   161 LSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
PTZ00424 PTZ00424
helicase 45; Provisional
4-368 2.03e-97

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 299.05  E-value: 2.03e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739   4 FKNYQISHDILRALEGLGYTEPTKVQQSVIPAVLERKDLVVKSQTGSGKTASFGIPLCELADWDENKPQALILTPTRELA 83
Cdd:PTZ00424   30 FDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILAPTRELA 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  84 VQVKEDITNIGRFKRIKATAVFGKSSFDKQKAELKQKSHIVVGTPGRVLDHIEKGTLPLDRLSYLVIDEADEMLNMGFIE 163
Cdd:PTZ00424  110 QQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRGFKG 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 164 QVEAIIKHLPTERTTMLFSATLPQDIEKLSRQYMQNPEHIEVKAAGLTTRNIEHAVIQV-REENKFSLLKDVLMTENPDS 242
Cdd:PTZ00424  190 QIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVeKEEWKFDTLCDLYETLTITQ 269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 243 CIIFCRTKEHVNQLTDELDDLGYPCDKIHGGMIQEDRFDVMNEFKRGEYRYLVATDVAARGIDIENISLVINYDLPLEKE 322
Cdd:PTZ00424  270 AIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPE 349
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1717936739 323 SYVHRTGRTGRAGNKGKAISFVAAFEKRFLADIEEYIGFEIQKIEA 368
Cdd:PTZ00424  350 NYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIEEMPM 395
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
2-371 5.69e-90

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 282.57  E-value: 5.69e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739   2 SHFKNYQISHDILRALEGLGYTEPTKVQQSVIPAVLERKDLVVKSQTGSGKTASFGIPLceLADWDENKPQ--------- 72
Cdd:PRK01297   87 TRFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISI--INQLLQTPPPkerymgepr 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  73 ALILTPTRELAVQVKEDITNIGRFKRIKATAVFGKSSFDKQKAELKQK-SHIVVGTPGRVLDHIEKGTLPLDRLSYLVID 151
Cdd:PRK01297  165 ALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEARfCDILVATPGRLLDFNQRGEVHLDMVEVMVLD 244
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 152 EADEMLNMGFIEQVEAIIKHLP--TERTTMLFSATLPQDIEKLSRQYMQNPEHIEVKAAGLTTRNIEHAVIQVREENKFS 229
Cdd:PRK01297  245 EADRMLDMGFIPQVRQIIRQTPrkEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAGSDKYK 324
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 230 LLKDVLMTENPDSCIIFCRTKEHVNQLTDELDDLGYPCDKIHGGMIQEDRFDVMNEFKRGEYRYLVATDVAARGIDIENI 309
Cdd:PRK01297  325 LLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGI 404
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1717936739 310 SLVINYDLPLEKESYVHRTGRTGRAGNKGKAISFVAAFEKRFLADIEEYIGFEIQKIEAPSQ 371
Cdd:PRK01297  405 SHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKISCEMPPAE 466
PTZ00110 PTZ00110
helicase; Provisional
2-355 3.32e-87

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 277.42  E-value: 3.32e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739   2 SHFKNYqishdILRALEGLGYTEPTKVQQSVIPAVLERKDLVVKSQTGSGKTASFGIP---------LCELADwdenKPQ 72
Cdd:PTZ00110  135 TSFPDY-----ILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPaivhinaqpLLRYGD----GPI 205
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  73 ALILTPTRELAVQVKEDITNIGRFKRIKATAVFGKSSFDKQKAELKQKSHIVVGTPGRVLDHIEKGTLPLDRLSYLVIDE 152
Cdd:PTZ00110  206 VLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDE 285
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 153 ADEMLNMGFIEQVEAIIKHLPTERTTMLFSATLPQDIEKLSRQYM-QNPEHIEVKAAGLTT-RNIEHAVIQVREENKFSL 230
Cdd:PTZ00110  286 ADRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCkEEPVHVNVGSLDLTAcHNIKQEVFVVEEHEKRGK 365
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 231 LKDVL---MTENpDSCIIFCRTKEHVNQLTDELDDLGYPCDKIHGGMIQEDRFDVMNEFKRGEYRYLVATDVAARGIDIE 307
Cdd:PTZ00110  366 LKMLLqriMRDG-DKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVK 444
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1717936739 308 NISLVINYDLPLEKESYVHRTGRTGRAGNKGKAISFVAAFEKRFLADI 355
Cdd:PTZ00110  445 DVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDL 492
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
3-363 1.17e-82

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 261.83  E-value: 1.17e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739   3 HFKNYQISHDILRALEGLGYTEPTKVQQSVIPAVLERKDLVVKSQTGSGKTASFGIPLC-------ELADWDENKPQALI 75
Cdd:PRK04837    9 KFSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFhyllshpAPEDRKVNQPRALI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  76 LTPTRELAVQVKEDITNIGRFKRIKATAVFGKSSFDKQKAELKQKSHIVVGTPGRVLDHIEKGTLPLDRLSYLVIDEADE 155
Cdd:PRK04837   89 MAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADR 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 156 MLNMGFIEQVEAIIKHLP--TERTTMLFSATLPQDIEKLSRQYMQNPEHIEVKAAGLTTRNIEHAVIQVREENKFSLLKD 233
Cdd:PRK04837  169 MFDLGFIKDIRWLFRRMPpaNQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEELFYPSNEEKMRLLQT 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 234 VLMTENPDSCIIFCRTKEHVNQLTDELDDLGYPCDKIHGGMIQEDRFDVMNEFKRGEYRYLVATDVAARGIDIENISLVI 313
Cdd:PRK04837  249 LIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHVF 328
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1717936739 314 NYDLPLEKESYVHRTGRTGRAGNKGKAISFvAAFEKRF-LADIEEYIGFEI 363
Cdd:PRK04837  329 NYDLPDDCEDYVHRIGRTGRAGASGHSISL-ACEEYALnLPAIETYIGHSI 378
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
4-398 4.37e-79

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 256.80  E-value: 4.37e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739   4 FKNYQISHDILRALEGLGYTEPTKVQQSVIPAVLERKDLVVKSQTGSGKTASFGIPLCE-------LADWDENKPQALIL 76
Cdd:PRK04537   11 FSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNrllsrpaLADRKPEDPRALIL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  77 TPTRELAVQVKEDITNIGRFKRIKATAVFGKSSFDKQKAELKQKSHIVVGTPGRVLDHIEK-GTLPLDRLSYLVIDEADE 155
Cdd:PRK04537   91 APTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQhKVVSLHACEICVLDEADR 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 156 MLNMGFIEQVEAIIKHLP--TERTTMLFSATLPQDIEKLSRQYMQNPEHIEVKAAGLTTRNIEHAVIQVREENKFSLLKD 233
Cdd:PRK04537  171 MFDLGFIKDIRFLLRRMPerGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRIYFPADEEKQTLLLG 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 234 VLMTENPDSCIIFCRTKEHVNQLTDELDDLGYPCDKIHGGMIQEDRFDVMNEFKRGEYRYLVATDVAARGIDIENISLVI 313
Cdd:PRK04537  251 LLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKYVY 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 314 NYDLPLEKESYVHRTGRTGRAGNKGKAISFVAAFEKRFLADIEEYIGfeiQKIeaPSQEEVArkkpEFLAKLNdRPESKK 393
Cdd:PRK04537  331 NYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYIE---QKI--PVEPVTA----ELLTPLP-RPPRVP 400

                  ....*
gi 1717936739 394 DKSEE 398
Cdd:PRK04537  401 VEGEE 405
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
13-357 3.58e-64

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 216.19  E-value: 3.58e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  13 ILRALEGLGYTEPTKVQQSVIPAVLERKDLVVKSQTGSGKTASFGIPL---CEL----ADWDENKPQALILTPTRELAVQ 85
Cdd:PLN00206  132 LLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIisrCCTirsgHPSEQRNPLAMVLTPTRELCVQ 211
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  86 VKEDITNIGRFKRIKATAVFGKSSFDKQKAELKQKSHIVVGTPGRVLDHIEKGTLPLDRLSYLVIDEADEMLNMGFIEQV 165
Cdd:PLN00206  212 VEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERGFRDQV 291
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 166 EAIIKHLPTERtTMLFSATLPQDIEKLSRQYMQNPEHIEVKAAGLTTRNIEHAVIQVREENKFSLLKDVLMTEN---PDS 242
Cdd:PLN00206  292 MQIFQALSQPQ-VLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKKQKLFDILKSKQhfkPPA 370
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 243 cIIFCRTKEHVNQLTDELDDL-GYPCDKIHGGMIQEDRFDVMNEFKRGEYRYLVATDVAARGIDIENISLVINYDLPLEK 321
Cdd:PLN00206  371 -VVFVSSRLGADLLANAITVVtGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTI 449
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1717936739 322 ESYVHRTGRTGRAGNKGKAISFVAAFEKRFLADIEE 357
Cdd:PLN00206  450 KEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVA 485
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
4-204 3.80e-64

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: 206.40  E-value: 3.80e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739   4 FKNYQISHDILRALEGLGYTEPTKVQQSVIPAVLERKDLVVKSQTGSGKTASFGIPLCEladWDENKPQ---ALILTPTR 80
Cdd:cd17954     2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQ---ALLENPQrffALVLAPTR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  81 ELAVQVKEDITNIGRFKRIKATAVFGKSSFDKQKAELKQKSHIVVGTPGRVLDHIE--KGtLPLDRLSYLVIDEADEMLN 158
Cdd:cd17954    79 ELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLEntKG-FSLKSLKFLVMDEADRLLN 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1717936739 159 MGFIEQVEAIIKHLPTERTTMLFSATLPQDIEKLSRQYMQNPEHIE 204
Cdd:cd17954   158 MDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKIE 203
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
26-192 3.89e-62

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


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 199.78  E-value: 3.89e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  26 TKVQQSVIPAVLERKDLVVKSQTGSGKTASFGIPLCELADWDENKPQALILTPTRELAVQVKEDITNIGRFKRIKATAVF 105
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 106 GKSSFDKQKAELKqKSHIVVGTPGRVLDHIEKgTLPLDRLSYLVIDEADEMLNMGFIEQVEAIIKHLPTERTTMLFSATL 185
Cdd:pfam00270  81 GGDSRKEQLEKLK-GPDILVGTPGRLLDLLQE-RKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSATL 158

                  ....*..
gi 1717936739 186 PQDIEKL 192
Cdd:pfam00270 159 PRNLEDL 165
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
13-203 1.97e-61

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: 199.02  E-value: 1.97e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  13 ILRALEGLGYTEPTKVQQSVIPAVLERKDLVVKSQTGSGKTASFGIPLCELADW-DENKP--QALILTPTRELAVQVKED 89
Cdd:cd17947     1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYrPKKKAatRVLVLVPTRELAMQCFSV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  90 ITNIGRFKRIKATAVFGKSSFDKQKAELKQKSHIVVGTPGRVLDHIEKG-TLPLDRLSYLVIDEADEMLNMGFIEQVEAI 168
Cdd:cd17947    81 LQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSpSFDLDSIEILVLDEADRMLEEGFADELKEI 160
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1717936739 169 IKHLPTERTTMLFSATLPQDIEKLSRQYMQNPEHI 203
Cdd:cd17947   161 LRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRV 195
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
215-344 8.84e-61

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: 195.03  E-value: 8.84e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 215 IEHAVIQVREENKFSLLKDVLMTEN-PDSCIIFCRTKEHVNQLTDELDDLGYPCDKIHGGMIQEDRFDVMNEFKRGEYRY 293
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLLLLLLEKLkPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1717936739 294 LVATDVAARGIDIENISLVINYDLPLEKESYVHRTGRTGRAGNKGKAISFV 344
Cdd:cd18787    81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
7-203 3.88e-60

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: 195.62  E-value: 3.88e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739   7 YQISHDILRALEGLGYTEPTKVQQSVIPAVLERKDLVVKSQTGSGKTASFGIPLCELADWDENKPQALILTPTRELAVQV 86
Cdd:cd17939     2 MGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQQI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  87 KEDITNIGRFKRIKATAVFGKSSFDKQKAELKQKSHIVVGTPGRVLDHIEKGTLPLDRLSYLVIDEADEMLNMGFIEQVE 166
Cdd:cd17939    82 QKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQIY 161
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1717936739 167 AIIKHLPTERTTMLFSATLPQDIEKLSRQYMQNPEHI 203
Cdd:cd17939   162 DIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
13-203 1.43e-59

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: 194.85  E-value: 1.43e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  13 ILRALEGLGYTEPTKVQQSVIPAVLERKDLVVKSQTGSGKTASFGIPL----CELADWDENK----PQALILTPTRELAV 84
Cdd:cd17945     1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLlvyiSRLPPLDEETkddgPYALILAPTRELAQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  85 QVKEDITNIGRFKRIKATAVFGKSSFDKQKAELKQKSHIVVGTPGRVLDHIEKGTLPLDRLSYLVIDEADEMLNMGFIEQ 164
Cdd:cd17945    81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1717936739 165 VEAIIKHLPTE--------------------RTTMLFSATLPQDIEKLSRQYMQNPEHI 203
Cdd:cd17945   161 VTKILDAMPVSnkkpdteeaeklaasgkhryRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
21-199 1.36e-57

DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes Drosophila melanogaster Vasa, which is essential for development. DEAD box protein 3 (DDX3) has been reported to display a high level of RNA-independent ATPase activity stimulated by both RNA and DNA. DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DDX3 and DDX4 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350725 [Multi-domain]  Cd Length: 221  Bit Score: 190.01  E-value: 1.36e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  21 GYTEPTKVQQSVIPAVLERKDLVVKSQTGSGKTASFGIPL--------CELADWDENK--PQALILTPTRELAVQVKEDI 90
Cdd:cd17967    19 GYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIisklledgPPSVGRGRRKayPSALILAPTRELAIQIYEEA 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  91 TNIGRFKRIKATAVFGKSSFDKQKAELKQKSHIVVGTPGRVLDHIEKGTLPLDRLSYLVIDEADEMLNMGFIEQVEAIIK 170
Cdd:cd17967    99 RKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDEADRMLDMGFEPQIRKIVE 178
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1717936739 171 H----LPTERTTMLFSATLPQDIEKLSRQYMQN 199
Cdd:cd17967   179 HpdmpPKGERQTLMFSATFPREIQRLAADFLKN 211
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
4-203 3.26e-55

DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner with nuclear receptors, and represses their transcriptional activity. DDX54 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350717 [Multi-domain]  Cd Length: 205  Bit Score: 183.27  E-value: 3.26e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739   4 FKNYQISHDILRALEGLGYTEPTKVQQSVIPAVLERKDLVVKSQTGSGKTASFGIPLCELADWDENK--PQALILTPTRE 81
Cdd:cd17959     3 FQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTvgARALILSPTRE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  82 LAVQVKEDITNIGRFKRIKATAVFGKSSFDKQKAELKQKSHIVVGTPGRVLDHIEKGTLPLDRLSYLVIDEADEMLNMGF 161
Cdd:cd17959    83 LALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEMGF 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1717936739 162 IEQVEAIIKHLPTERTTMLFSATLPQDIEKLSRQYMQNPEHI 203
Cdd:cd17959   163 AEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
4-200 4.36e-55

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: 182.81  E-value: 4.36e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739   4 FKNYQISHDILRALEGLGYTEPTKVQQSVIPAVLERKDLVVKSQTGSGKTASFGIPLCELADWDENKPQALILTPTRELA 83
Cdd:cd17955     1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYGIFALVLTPTRELA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  84 VQVKEDITNIGRFKRIKATAVFGKSSFDKQKAELKQKSHIVVGTPGRVLDHIE---KGTLPLDRLSYLVIDEADEMLNMG 160
Cdd:cd17955    81 YQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssdDTTKVLSRVKFLVLDEADRLLTGS 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1717936739 161 FIEQVEAIIKHLPTERTTMLFSATLPQDIEKLSRQYMQNP 200
Cdd:cd17955   161 FEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKP 200
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
4-203 1.56e-54

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: 181.34  E-value: 1.56e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739   4 FKNYQISHDILRALEGLGYTEPTKVQQSVIPAVLERKDLVVKSQTGSGKTASFGIPLCELADWDENKPQALILTPTRELA 83
Cdd:cd17940     1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  84 VQVKEDITNIGRFKRIKATAVFGKSSFDKQKAELKQKSHIVVGTPGRVLDHIEKGTLPLDRLSYLVIDEADEMLNMGFIE 163
Cdd:cd17940    81 LQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQP 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1717936739 164 QVEAIIKHLPTERTTMLFSATLPQDIEKLSRQYMQNPEHI 203
Cdd:cd17940   161 IIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
13-185 1.04e-53

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: 180.13  E-value: 1.04e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  13 ILRALEGLGYTEPTKVQQSVIP-AVLERKDLVVKSQTGSGKTASFGIP-LCELADWDE--------NKPQALILTPTREL 82
Cdd:cd17946     1 ILRALADLGFSEPTPIQALALPaAIRDGKDVIGAAETGSGKTLAFGIPiLERLLSQKSsngvggkqKPLRALILTPTREL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  83 AVQVKEDITNIGRFKRIKATAVFGKSSFDKQKAELKQKSHIVVGTPGRVLDHIEKGTLPLDRL---SYLVIDEADEMLNM 159
Cdd:cd17946    81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEHLANLkslRFLVLDEADRMLEK 160
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1717936739 160 GFIEQVEAIIKHLPTERT-------TMLFSATL 185
Cdd:cd17946   161 GHFAELEKILELLNKDRAgkkrkrqTFVFSATL 193
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
13-203 3.78e-53

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: 177.56  E-value: 3.78e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  13 ILRALEGLGYTEPTKVQQSVIPAVLERKDLVVKSQTGSGKTASFGIP---------LCELADwdenKPQALILTPTRELA 83
Cdd:cd17966     1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPaivhinaqpPLERGD----GPIVLVLAPTRELA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  84 VQVKEDITNIGRFKRIKATAVFGKSSFDKQKAELKQKSHIVVGTPGRVLDHIEKGTLPLDRLSYLVIDEADEMLNMGFIE 163
Cdd:cd17966    77 QQIQQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEP 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1717936739 164 QVEAIIKHLPTERTTMLFSATLPQDIEKLSRQYMQNPEHI 203
Cdd:cd17966   157 QIRKIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
13-200 4.60e-53

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: 177.39  E-value: 4.60e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  13 ILRALEGLGYTEPTKVQQSVIPAVLERKDLVVKSQTGSGKTASFGIPLCEL------ADWDENKPQALILTPTRELAVQV 86
Cdd:cd17961     5 LLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKilkakaESGEEQGTRALILVPTRELAQQV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  87 KEDITNIGRF--KRIKATAVFGKSSFDKQKAELKQKSHIVVGTPGRVLDHIEKGTL-PLDRLSYLVIDEADEMLNMGFIE 163
Cdd:cd17961    85 SKVLEQLTAYcrKDVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLlLLSTLKYLVIDEADLVLSYGYEE 164
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1717936739 164 QVEAIIKHLPTERTTMLFSATLPQDIEKLSRQYMQNP 200
Cdd:cd17961   165 DLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNP 201
DEXDc smart00487
DEAD-like helicases superfamily;
17-216 6.27e-53

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 176.91  E-value: 6.27e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739   17 LEGLGYTEPTKVQQSVIPAVLER-KDLVVKSQTGSGKTASFGIPLCELADwDENKPQALILTPTRELAVQVKEDITNIGR 95
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALK-RGKGGRVLVLVPTRELAEQWAEELKKLGP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739   96 FKRIKATAVFGKSSFDKQKAEL-KQKSHIVVGTPGRVLDHIEKGTLPLDRLSYLVIDEADEMLNMGFIEQVEAIIKHLPT 174
Cdd:smart00487  80 SLGLKVVGLYGGDSKREQLRKLeSGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPK 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1717936739  175 ERTTMLFSATLPQDIEKLSRQYMQNPEHIEVKAAGLTTRNIE 216
Cdd:smart00487 160 NVQLLLLSATPPEEIENLLELFLNDPVFIDVGFTPLEPIEQF 201
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
13-200 9.24e-53

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: 176.61  E-value: 9.24e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  13 ILRALEGLGYTEPTKVQQSVIPAVLERKDLVVKSQTGSGKTASFGIPLCEL-----ADWDENKPQALILTPTRELAVQVK 87
Cdd:cd17960     1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEIllkrkANLKKGQVGALIISPTRELATQIY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  88 EDITNIGRFKRIKATAVF---GKSSFDKQKAELKQKSHIVVGTPGRVLDHIEKGTLPLD--RLSYLVIDEADEMLNMGFI 162
Cdd:cd17960    81 EVLQSFLEHHLPKLKCQLligGTNVEEDVKKFKRNGPNILVGTPGRLEELLSRKADKVKvkSLEVLVLDEADRLLDLGFE 160
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1717936739 163 EQVEAIIKHLPTERTTMLFSATLPQDIEKLSRQYMQNP 200
Cdd:cd17960   161 ADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNP 198
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
4-203 1.00e-51

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: 173.79  E-value: 1.00e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739   4 FKNYQISHDILRALEGLGYTEPTKVQQSVIPAVLERKDLVVKSQTGSGKTASFGIPLCELADWDENKPQALILTPTRELA 83
Cdd:cd18046     1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  84 VQVKEDITNIGRFKRIKATAVFGKSSFDKQKAELKQKSHIVVGTPGRVLDHIEKGTLPLDRLSYLVIDEADEMLNMGFIE 163
Cdd:cd18046    81 QQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFKD 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1717936739 164 QVEAIIKHLPTERTTMLFSATLPQDIEKLSRQYMQNPEHI 203
Cdd:cd18046   161 QIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
13-202 2.13e-51

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: 173.15  E-value: 2.13e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  13 ILRALEGLGYTEPTKVQQSVIPAVLE-RKDLVVKSQTGSGKTASFGIPLCE-----LADWDENKPQALILTPTRELAVQV 86
Cdd:cd17964     5 LLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQsllntKPAGRRSGVSALIISPTRELALQI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  87 KEDITN-IGRFKRIKATAVFGKSSFDKQKAEL-KQKSHIVVGTPGRVLDHIEKGTLP--LDRLSYLVIDEADEMLNMGFI 162
Cdd:cd17964    85 AAEAKKlLQGLRKLRVQSAVGGTSRRAELNRLrRGRPDILVATPGRLIDHLENPGVAkaFTDLDYLVLDEADRLLDMGFR 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1717936739 163 EQVEAIIKHLP----TERTTMLFSATLPQDIEKLSRQYMqNPEH 202
Cdd:cd17964   165 PDLEQILRHLPeknaDPRQTLLFSATVPDEVQQIARLTL-KKDY 207
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
4-203 1.30e-50

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: 171.11  E-value: 1.30e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739   4 FKNYQISHDILRALEGLGYTEPTKVQQSVIPAVLERKDLVVKSQTGSGKTASFGIPLCELADWDENKPQALILTPTRELA 83
Cdd:cd18045     1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  84 VQVKEDITNIGRFKRIKATAVFGKSSFDKQKAELKQKSHIVVGTPGRVLDHIEKGTLPLDRLSYLVIDEADEMLNMGFIE 163
Cdd:cd18045    81 VQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFKE 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1717936739 164 QVEAIIKHLPTERTTMLFSATLPQDIEKLSRQYMQNPEHI 203
Cdd:cd18045   161 QIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
4-203 1.19e-49

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: 170.53  E-value: 1.19e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739   4 FKNYQISHDILRALEGLGYTEPTKVQQSVIPAVLERKDLVVKSQTGSGKTASFGIPL--------CELADWDENK-PQAL 74
Cdd:cd18052    45 FEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVltgmmkegLTASSFSEVQePQAL 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  75 ILTPTRELAVQVKEDITNIGRFKRIKATAVFGKSSFDKQKAELKQKSHIVVGTPGRVLDHIEKGTLPLDRLSYLVIDEAD 154
Cdd:cd18052   125 IVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEAD 204
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1717936739 155 EMLNMGFIEQVEAIIKHL----PTERTTMLFSATLPQDIEKLSRQYMqNPEHI 203
Cdd:cd18052   205 RMLDMGFGPEIRKLVSEPgmpsKEDRQTLMFSATFPEEIQRLAAEFL-KEDYL 256
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
13-205 2.00e-49

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: 167.85  E-value: 2.00e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  13 ILRALEGLGYTEPTKVQQSVIPAVLERKDLVVKSQTGSGKTASFGIPLCEL---ADW-DENKPQALILTPTRELAVQVKE 88
Cdd:cd17941     1 TLKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKlyrERWtPEDGLGALIISPTRELAMQIFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  89 DITNIGRFKRIKATAVFGKSSFDKQKAELKQKShIVVGTPGRVLDHIEKG-TLPLDRLSYLVIDEADEMLNMGFIEQVEA 167
Cdd:cd17941    81 VLRKVGKYHSFSAGLIIGGKDVKEEKERINRMN-ILVCTPGRLLQHMDETpGFDTSNLQMLVLDEADRILDMGFKETLDA 159
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1717936739 168 IIKHLPTERTTMLFSATLPQDIEKLSRQYMQNPEHIEV 205
Cdd:cd17941   160 IVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
13-204 4.47e-49

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: 166.67  E-value: 4.47e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  13 ILRALEGLGYTEPTKVQQSVIPAVLERKDLVVKSQTGSGKTASFGIPLCELADWDENKPQALILTPTRELAVQVKEDITN 92
Cdd:cd17943     1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVFKK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  93 IG-RFKRIKATAVFGKSSFDKQKAELKqKSHIVVGTPGRVLDHIEKGTLPLDRLSYLVIDEADEMLNMGFIEQVEAIIKH 171
Cdd:cd17943    81 IGkKLEGLKCEVFIGGTPVKEDKKKLK-GCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFSS 159
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1717936739 172 LPTERTTMLFSATLPQDIEKLSRQYMQNPEHIE 204
Cdd:cd17943   160 LPKNKQVIAFSATYPKNLDNLLARYMRKPVLVR 192
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
13-203 2.37e-48

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: 164.90  E-value: 2.37e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  13 ILRALEGLGYTEPTKVQQSVIPAVLERKDLVVKSQTGSGKTASFGIP-LCELADWDENKPQ----ALILTPTRELAVQVK 87
Cdd:cd17952     1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPmLVHIMDQRELEKGegpiAVIVAPTRELAQQIY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  88 EDITNIGRFKRIKATAVFGKSSFDKQKAELKQKSHIVVGTPGRVLDHIEKGTLPLDRLSYLVIDEADEMLNMGFIEQVEA 167
Cdd:cd17952    81 LEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRS 160
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1717936739 168 IIKHLPTERTTMLFSATLPQDIEKLSRQYMQNPEHI 203
Cdd:cd17952   161 IVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
9-203 1.21e-47

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: 163.70  E-value: 1.21e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739   9 ISHDILRALEGLGYTEPTKVQQSVIPAVLERKDLVVKSQTGSGKTASFGIPLC-----ELADWDENKPQALILTPTRELA 83
Cdd:cd17953    19 LSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFrhikdQRPVKPGEGPIGLIMAPTRELA 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  84 VQVKEDITNIGRFKRIKATAVFGKSSFDKQKAELKQKSHIVVGTPGRVLDHIEKGT---LPLDRLSYLVIDEADEMLNMG 160
Cdd:cd17953    99 LQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTANNgrvTNLRRVTYVVLDEADRMFDMG 178
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1717936739 161 FIEQVEAIIKHLPTERTTMLFSATLPQDIEKLSRQYMQNPEHI 203
Cdd:cd17953   179 FEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
18-203 2.77e-47

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: 162.76  E-value: 2.77e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  18 EGLGYTEPTKVQQSVIPAVLERKDLVVKSQTGSGKTASFGIPLCEL-----ADWDENK-PQALILTPTRELAVQVKEDIT 91
Cdd:cd17949     7 SKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRllslePRVDRSDgTLALVLVPTRELALQIYEVLE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  92 NIGR-FKRIKATAVFGKSSFDKQKAELKQKSHIVVGTPGRVLDHIEKGT-LPLDRLSYLVIDEADEMLNMGFIEQVEAII 169
Cdd:cd17949    87 KLLKpFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQsFDVSNLRWLVLDEADRLLDMGFEKDITKIL 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1717936739 170 KHL-------------PTERTTMLFSATLPQDIEKLSRQYMQNPEHI 203
Cdd:cd17949   167 ELLddkrskaggekskPSRRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
9-200 5.18e-47

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: 161.20  E-value: 5.18e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739   9 ISHDILRALEGLGYTEPTKVQQSVIPAVLE--RKDLVVKSQTGSGKTASFGIPLCELADWDENKPQALILTPTRELAVQV 86
Cdd:cd17963     1 LKPELLKGLYAMGFNKPSKIQETALPLILSdpPENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  87 KEDITNIGRFKRIKATAVFgKSSFDKQKAELKQksHIVVGTPGRVLDHIEKGTLPLDRLSYLVIDEADEMLNM-GFIEQV 165
Cdd:cd17963    81 GEVVEKMGKFTGVKVALAV-PGNDVPRGKKITA--QIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTqGHGDQS 157
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1717936739 166 EAIIKHLPTERTTMLFSATLPQDIEKLSRQYMQNP 200
Cdd:cd17963   158 IRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNA 192
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
17-203 1.09e-46

DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer development by promoting DNA replication. DDX59 knockdown mice showed reduced cell proliferation, anchorage-independent cell growth, and reduction of tumor formation. Recent work shows that EGFR and Ras regulate DDX59 during lung cancer development. Diseases associated with DDX59 (also called zinc finger HIT domain-containing protein 5) include orofaciodigital syndrome V and orofaciodigital syndrome. DDX59 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350720 [Multi-domain]  Cd Length: 193  Bit Score: 160.41  E-value: 1.09e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  17 LEGLGYTEPTKVQQSVIPAVLERKDLVVKSQTGSGKTASFGIPLCELADWDENKPQALILTPTRELAVQVKEDITNIGR- 95
Cdd:cd17962     5 LKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQAKELMKg 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  96 FKRIKATAVFGKSSFDKQKAELKQKSHIVVGTPGRVLDHIEKGTLPLDRLSYLVIDEADEMLNMGFIEQVEAIIKHLPTE 175
Cdd:cd17962    85 LPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILENISHD 164
                         170       180
                  ....*....|....*....|....*...
gi 1717936739 176 RTTMLFSATLPQDIEKLSRQYMQNPEHI 203
Cdd:cd17962   165 HQTILVSATIPRGIEQLAGQLLQNPVRI 192
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
22-199 1.33e-46

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: 162.13  E-value: 1.33e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  22 YTEPTKVQQSVIPAVLERKDLVVKSQTGSGKTASFGIPLC---------ELADWDENK-------PQALILTPTRELAVQ 85
Cdd:cd18051    41 YTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILsqiyeqgpgESLPSESGYygrrkqyPLALVLAPTRELASQ 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  86 VKEDITNIGRFKRIKATAVFGKSSFDKQKAELKQKSHIVVGTPGRVLDHIEKGTLPLDRLSYLVIDEADEMLNMGFIEQV 165
Cdd:cd18051   121 IYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQI 200
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1717936739 166 EAIIKHL---PT-ERTTMLFSATLPQDIEKLSRQYMQN 199
Cdd:cd18051   201 RRIVEQDtmpPTgERQTLMFSATFPKEIQMLARDFLDN 238
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
13-200 1.04e-45

DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ubiquitously expressed in testis, endometrium, and other tissues in humans. DDX52 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350715 [Multi-domain]  Cd Length: 198  Bit Score: 157.75  E-value: 1.04e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  13 ILRALEGLGYTEPTKVQQSVIPAVLERKDLVVKSQTGSGKTASFGIPLCE--LADWDENKPQALILTPTRELAVQVKEDI 90
Cdd:cd17957     1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQklGKPRKKKGLRALILAPTRELASQIYREL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  91 TNIGRFKRIKaTAVFGKSSFDKQK--AELKQKSHIVVGTPGRVLDHIEKGTLPLDRLSYLVIDEADEMLNMGFIEQVEAI 168
Cdd:cd17957    81 LKLSKGTGLR-IVLLSKSLEAKAKdgPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDEI 159
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1717936739 169 IKHLP-TERTTMLFSATLPQDIEKLSRQYMQNP 200
Cdd:cd17957   160 LAACTnPNLQRSLFSATIPSEVEELARSVMKDP 192
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
2-205 6.45e-45

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: 156.35  E-value: 6.45e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739   2 SHFKNYQISHDILRALEGLGYTEPTKVQQSVIPAVLERKDLVVKSQTGSGKTASFGIPLCELADWDENKPQALILTPTRE 81
Cdd:cd17950     2 SGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTRE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  82 LAVQVKEDITNIGRF-KRIKATAVFGKSSFDKQKAELKQKS-HIVVGTPGRVLDHIEKGTLPLDRLSYLVIDEADEM--- 156
Cdd:cd17950    82 LAFQISNEYERFSKYmPNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMleq 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1717936739 157 LNMGfiEQVEAIIKHLPTERTTMLFSATLPQDIEKLSRQYMQNPEHIEV 205
Cdd:cd17950   162 LDMR--RDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
22-207 5.46e-41

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: 146.69  E-value: 5.46e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  22 YTEPTKVQQSVIPAVLERKDLVVKSQTGSGKTASF---GI------PLCELADwdenKPQALILTPTRELAVQVKEDITN 92
Cdd:cd18049    44 FTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYllpAIvhinhqPFLERGD----GPICLVLAPTRELAQQVQQVAAE 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  93 IGRFKRIKATAVFGKSSFDKQKAELKQKSHIVVGTPGRVLDHIEKGTLPLDRLSYLVIDEADEMLNMGFIEQVEAIIKHL 172
Cdd:cd18049   120 YGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQI 199
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1717936739 173 PTERTTMLFSATLPQDIEKLSRQYMQNPEHIEVKA 207
Cdd:cd18049   200 RPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIGA 234
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
14-204 5.55e-41

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: 145.38  E-value: 5.55e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  14 LRALEGLGYTEPTKVQQSVIPAVLERKDLVVKSQTGSGKTASFGIPLCELADWDENK------PQALILTPTRELAVQVK 87
Cdd:cd17944     2 IKLLQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPrkrgraPKVLVLAPTRELANQVT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  88 EDITNIGRfkRIKATAVFGKSSFDKQKAELKQKSHIVVGTPGRVLDHIEKGTLPLDRLSYLVIDEADEMLNMGFIEQVEA 167
Cdd:cd17944    82 KDFKDITR--KLSVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEE 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1717936739 168 II----KHLPTER-TTMLFSATLPQDIEKLSRQYMQNP-EHIE 204
Cdd:cd17944   160 ILsvsyKKDSEDNpQTLLFSATCPDWVYNVAKKYMKSQyEQVD 202
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
13-203 6.99e-41

DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis antigen 13 or helical antigen) displays tumor-specific expression. Diseases associated with DDX43 include rheumatoid lung disease. DDX53 is also called cancer/testis antigen 26 or DEAD-Box Protein CAGE. Both DDX46 and DDX53 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350716 [Multi-domain]  Cd Length: 197  Bit Score: 144.91  E-value: 6.99e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  13 ILRALEGLGYTEPTKVQQSVIPAVLERKDLVVKSQTGSGKTASFGIP-----LCELADWDE-NKPQALILTPTRELAVQV 86
Cdd:cd17958     1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPgfihlDLQPIPREQrNGPGVLVLTPTRELALQI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  87 KEDITNIgRFKRIKATAVFGKSSFDKQKAELKQKSHIVVGTPGRVLDHIEKGTLPLDRLSYLVIDEADEMLNMGFIEQVE 166
Cdd:cd17958    81 EAECSKY-SYKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIR 159
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1717936739 167 AIIKHLPTERTTMLFSATLPQDIEKLSRQYMQNPEHI 203
Cdd:cd17958   160 KILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
13-194 4.53e-39

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: 140.19  E-value: 4.53e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  13 ILRALEGLGYTEPTKVQQSVIPAVLERKDLVVKSQTGSGKTASFGIPLCELADWDENKPQ----ALILTPTRELAVQVKE 88
Cdd:cd17942     1 TLKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKFKPRngtgVIIISPTRELALQIYG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  89 DITNIGRFKRIKATAVFGKSSfDKQKAE-LKQKSHIVVGTPGRVLDHIE-KGTLPLDRLSYLVIDEADEMLNMGFIEQVE 166
Cdd:cd17942    81 VAKELLKYHSQTFGIVIGGAN-RKAEAEkLGKGVNILVATPGRLLDHLQnTKGFLYKNLQCLIIDEADRILEIGFEEEMR 159
                         170       180
                  ....*....|....*....|....*...
gi 1717936739 167 AIIKHLPTERTTMLFSATLPQDIEKLSR 194
Cdd:cd17942   160 QIIKLLPKRRQTMLFSATQTRKVEDLAR 187
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
12-200 4.98e-39

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: 140.53  E-value: 4.98e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  12 DILRALEGLGYTEPTKVQQSVIPAVLERKDLVVKSQTGSGKTASFGIPLCELAdwdenkpQALILTPTRELAVQVKEDIT 91
Cdd:cd17938     9 ELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIV-------VALILEPSRELAEQTYNCIE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  92 NIGRF---KRIKATAVFGKSSFDKQKAELKQKSHIVVGTPGRVLDHIEKGTLPLDRLSYLVIDEADEMLNMGFIEQVEAI 168
Cdd:cd17938    82 NFKKYldnPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQGNLETINRI 161
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1717936739 169 IKHLP--TER----TTMLFSATLPQ-DIEKLSRQYMQNP 200
Cdd:cd17938   162 YNRIPkiTSDgkrlQVIVCSATLHSfEVKKLADKIMHFP 200
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
4-205 2.82e-38

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: 140.53  E-value: 2.82e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739   4 FKNYQISHDILRALEGLGYTEPTKVQQSVIPAVLERKDLVVKSQTGSGKTASFGIP---------LCELADwdenKPQAL 74
Cdd:cd18050    64 FHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPaivhinhqpYLERGD----GPICL 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  75 ILTPTRELAVQVKEDITNIGRFKRIKATAVFGKSSFDKQKAELKQKSHIVVGTPGRVLDHIEKGTLPLDRLSYLVIDEAD 154
Cdd:cd18050   140 VLAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEAD 219
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1717936739 155 EMLNMGFIEQVEAIIKHLPTERTTMLFSATLPQDIEKLSRQYMQNPEHIEV 205
Cdd:cd18050   220 RMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQINI 270
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
13-200 2.11e-37

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: 135.93  E-value: 2.11e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  13 ILRALEGLGYTEPTKVQQSVIPAVLERKDLVVKSQTGSGKTASFGIPLCELADWDENK--------PQALILTPTRELAV 84
Cdd:cd17951     1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQEKKlpfikgegPYGLIVCPSRELAR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  85 QVKEDITNI------GRFKRIKATAVFGKSSFDKQKAELKQKSHIVVGTPGRVLDHIEKGTLPLDRLSYLVIDEADEMLN 158
Cdd:cd17951    81 QTHEVIEYYckalqeGGYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1717936739 159 MGFIEQVEAIIKHLPTERTTMLFSATLPQDIEKLSRQYMQNP 200
Cdd:cd17951   161 MGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKP 202
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
13-203 2.51e-37

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: 136.61  E-value: 2.51e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  13 ILRALEGLGYTEPTKVQQSVIPAVLE---------RKDLVVKSQTGSGKTASFGIPLCE-LADWDENKPQALILTPTREL 82
Cdd:cd17956     1 LLKNLQNNGITSAFPVQAAVIPWLLPsskstppyrPGDLCVSAPTGSGKTLAYVLPIVQaLSKRVVPRLRALIVVPTKEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  83 AVQVKEDITNIGRFKRIKATAVFGKSSFDKQKAELKQKSH--------IVVGTPGRVLDHIeKGTLP--LDRLSYLVIDE 152
Cdd:cd17956    81 VQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDTSgrylsrvdILVATPGRLVDHL-NSTPGftLKHLRFLVIDE 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1717936739 153 ADEMLNMGF---IEQVEAIIKHLPTERTT-----------------MLFSATLPQDIEKLSRQYMQNPEHI 203
Cdd:cd17956   160 ADRLLNQSFqdwLETVMKALGRPTAPDLGsfgdanllersvrplqkLLFSATLTRDPEKLSSLKLHRPRLF 230
RRM_BsYxiN_like cd12500
RNA recognition motif (RRM) found in Bacillus subtilis ATP-dependent RNA helicase YxiN and ...
405-477 4.55e-35

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: 125.27  E-value: 4.55e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1717936739 405 KLYFNGGKKKKIRAVDFVGTIAKIDGVSADDIGIITIMDNASYVEILNGKGPHVLKVMKNTTVKGKQLKVNKA 477
Cdd:cd12500     1 KLYFNGGKKKKIRAVDIVGAISNIDGVTGDDIGIITVQDNCSYVDILNGKGDHVLKVMKNTTIKGKQVKVNKA 73
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
226-335 3.13e-34

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: 124.25  E-value: 3.13e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 226 NKFSLLKDVLMTENPDSCIIFCRTKEHVNqlTDEL-DDLGYPCDKIHGGMIQEDRFDVMNEFKRGEYRYLVATDVAARGI 304
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLE--AELLlEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1717936739 305 DIENISLVINYDLPLEKESYVHRTGRTGRAG 335
Cdd:pfam00271  79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
255-335 1.18e-28

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 108.07  E-value: 1.18e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  255 QLTDELDDLGYPCDKIHGGMIQEDRFDVMNEFKRGEYRYLVATDVAARGIDIENISLVINYDLPLEKESYVHRTGRTGRA 334
Cdd:smart00490   2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRA 81

                   .
gi 1717936739  335 G 335
Cdd:smart00490  82 G 82
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
4-211 4.03e-28

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: 111.65  E-value: 4.03e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739   4 FKNYQISHDILRALEGLGYTEPTKVQQSVIPAVLER--KDLVVKSQTGSGKTASFGIPLCELADWDENKPQALILTPTRE 81
Cdd:cd18048    20 FEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQCLCLSPTFE 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  82 LAVQVKEDITNIGRF-KRIKAT-AVFGKSSFDKQKAElkqkSHIVVGTPGRVLDHIEKGTL-PLDRLSYLVIDEADEMLN 158
Cdd:cd18048   100 LALQTGKVVEEMGKFcVGIQVIyAIRGNRPGKGTDIE----AQIVIGTPGTVLDWCFKLRLiDVTNISVFVLDEADVMIN 175
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1717936739 159 M-GFIEQVEAIIKHLPTERTTMLFSATLPQDIEKLSRQYMQNPEHIEVKAAGLT 211
Cdd:cd18048   176 VqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
13-194 3.59e-25

DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350706 [Multi-domain]  Cd Length: 231  Bit Score: 103.22  E-value: 3.59e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  13 ILRALEGLGYTEPTKVQQSVIPAVLERKDLVVKSQTGSGKTASFGIPLCE-LADWDE------NKPQALILTPTRELAVQ 85
Cdd:cd17948     1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQrLLRYKLlaegpfNAPRGLVITPSRELAEQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  86 VKEDITNIGRFKRIKATAVFGKSSFDKQKAELKQKSHIVVGTPGRVLDHIEKGTLPLDRLSYLVIDEADEMLNMGFIEQV 165
Cdd:cd17948    81 IGSVAQSLTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKL 160
                         170       180
                  ....*....|....*....|....*....
gi 1717936739 166 EAIIKHLPterttmlFSATLPQDIEKLSR 194
Cdd:cd17948   161 SHFLRRFP-------LASRRSENTDGLDP 182
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
4-204 1.31e-22

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


Pssm-ID: 350805 [Multi-domain]  Cd Length: 205  Bit Score: 95.56  E-value: 1.31e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739   4 FKNYQISHDILRALEGLGYTEPTKVQQSVIPAVLER--KDLVVKSQTGSGKTASFGIPLCELADWDENKPQALILTPTRE 81
Cdd:cd18047     3 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  82 LAVQVKEDITNIGRF--KRIKATAVFGKssfdKQKAELKQKSHIVVGTPGRVLDH-IEKGTLPLDRLSYLVIDEADEML- 157
Cdd:cd18047    83 LALQTGKVIEQMGKFypELKLAYAVRGN----KLERGQKISEQIVIGTPGTVLDWcSKLKFIDPKKIKVFVLDEADVMIa 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1717936739 158 NMGFIEQVEAIIKHLPTERTTMLFSATLPQDIEKLSRQYMQNPEHIE 204
Cdd:cd18047   159 TQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 205
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
11-378 3.87e-21

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 95.98  E-value: 3.87e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  11 HDILRALegLGYTEPTKVQQSVIPAVLERKDLVVKSQTGSGKTASFGIPlceladwdenkpqALILT-PTreLAV----- 84
Cdd:COG0514     6 LEVLKRV--FGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLP-------------ALLLPgLT--LVVsplia 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  85 ----QVkEDITNIGrfkrIKATAVfgKSSFDKQKAElkqkshivvgtpgRVLDHIEKGTL------P--------LDRL- 145
Cdd:COG0514    69 lmkdQV-DALRAAG----IRAAFL--NSSLSAEERR-------------EVLRALRAGELkllyvaPerllnprfLELLr 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 146 ----SYLVIDEA--------D---EMLNMGfieqveAIIKHLPtERTTMLFSATLP----QDI-EKLSrqyMQNPEHIev 205
Cdd:COG0514   129 rlkiSLFAIDEAhcisqwghDfrpDYRRLG------ELRERLP-NVPVLALTATATprvrADIaEQLG---LEDPRVF-- 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 206 kAAGLTTRNIEHAVIQVREENKFSLLKDVLMTENPDSCIIFCRTKEHVNQLTDELDDLGYPCDKIHGGMIQEDRFDVMNE 285
Cdd:COG0514   197 -VGSFDRPNLRLEVVPKPPDDKLAQLLDFLKEHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDR 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 286 FKRGEYRYLVATdVA-ARGIDIENISLVINYDLPLEKESYVHRTGRTGRAGNKGKAISFVAA--FEK-RFLADieeyigf 361
Cdd:COG0514   276 FLRDEVDVIVAT-IAfGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPedVAIqRFFIE------- 347
                         410
                  ....*....|....*..
gi 1717936739 362 eiQKIEAPSQEEVARKK 378
Cdd:COG0514   348 --QSPPDEERKRVERAK 362
DbpA pfam03880
DbpA RNA binding domain; This RNA binding domain is found at the C-terminus of a number of ...
405-476 5.17e-21

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: 86.66  E-value: 5.17e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1717936739 405 KLYFNGGKKKKIRAVDFVGTIAKIDGVSADDIGIITIMDNASYVEILNGKGPHVLKVMKNTTVKGKQLKVNK 476
Cdd:pfam03880   1 RLFINVGKKDGVRPGDIVGALANEAGLPGDDIGKIDIFDNFSFVEVPAEKAEKVLKALKGTKIKGRKVRVEP 72
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
38-313 7.71e-21

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 95.48  E-value: 7.71e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  38 ERKDLVVKSQTGSGKTASFgiplCELADWDENKPQALILTPTRELAVQVKEditnigRFKRIKATAVFGKSSFDKQKael 117
Cdd:COG1061    99 GGGRGLVVAPTGTGKTVLA----LALAAELLRGKRVLVLVPRRELLEQWAE------ELRRFLGDPLAGGGKKDSDA--- 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 118 kqksHIVVGTPGRVLDHIEKGTLPlDRLSYLVIDEADEMLNMGFieqvEAIIKHLPTERTtMLFSAT------LPQDIEK 191
Cdd:COG1061   166 ----PITVATYQSLARRAHLDELG-DRFGLVIIDEAHHAGAPSY----RRILEAFPAAYR-LGLTATpfrsdgREILLFL 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 192 -------------LSRQYMQNPEHIEVKAaGLTTRNIEHAVIQVR--------EENKFSLLKDVLMTE-NPDSCIIFCRT 249
Cdd:COG1061   236 fdgivyeyslkeaIEDGYLAPPEYYGIRV-DLTDERAEYDALSERlrealaadAERKDKILRELLREHpDDRKTLVFCSS 314
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1717936739 250 KEHVNQLTDELDDLGYPCDKIHGGMIQEDRFDVMNEFKRGEYRYLVATDVAARGIDIENISLVI 313
Cdd:COG1061   315 VDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI 378
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
20-196 1.13e-17

DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 (MRH4) plays an essential role during the late stages of mitochondrial ribosome or mitoribosome assembly by promoting remodeling of the 21S rRNA-protein interactions. MRH4 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350723 [Multi-domain]  Cd Length: 251  Bit Score: 82.42  E-value: 1.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  20 LGYTEPTKVQQSVIPAVLE----------------RKDLVVKSQTGSGKTASFGIPLC-----ELADWDEN--------- 69
Cdd:cd17965    26 DEEIKPSPIQTLAIKKLLKtlmrkvtkqtsneepkLEVFLLAAETGSGKTLAYLAPLLdylkrQEQEPFEEaeeeyesak 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  70 ---KPQALILTPTRELAVQVKEDITNIGRFKRIKATAV---FGKSSFDKQKAeLKQKSHIVVGTPGRVLDHIEKGTLPLD 143
Cdd:cd17965   106 dtgRPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFssgFGPSYQRLQLA-FKGRIDILVTTPGKLASLAKSRPKILS 184
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1717936739 144 RLSYLVIDEADEMLNMGFIEQVEAIIKHLPTERTTMLFSATLPQDIEK-LSRQY 196
Cdd:cd17965   185 RVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKEFDKtLRKLF 238
RRM_DbpA cd12252
RNA recognition motif (RRM) found in the DbpA subfamily of prokaryotic DEAD-box rRNA helicases; ...
405-475 7.74e-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: 74.89  E-value: 7.74e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1717936739 405 KLYFNGGKKKKIRAVDFVGTIAKIDGVSADDIGIITIMDNASYVEILNGKGPHVLKVMKNTTVKGKQLKVN 475
Cdd:cd12252     1 RLFINVGRKDGIDPRDLLGAICRAGGISRDDIGAIRIFDNFSFVEVPEAEAERVIEALNGKKIKGKKLRVE 71
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
214-343 2.62e-16

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: 75.32  E-value: 2.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 214 NIEHAVIQVR-EENKFSLLKDVLMTENPDSCIIFCRTKEHVNQLTDELDDLGYPCDKIHGGMIQEDRFDVMNEFKRGEYR 292
Cdd:cd18794     3 NLFYSVRPKDkKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQ 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1717936739 293 YLVATDVAARGIDIENISLVINYDLPLEKESYVHRTGRTGRAGNKGKAISF 343
Cdd:cd18794    83 VIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILF 133
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
214-443 4.04e-16

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 80.93  E-value: 4.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 214 NIEHA-VIQVREenkfsLLKDVLMTENPDSCIIFCRTKEHVNQLTDELDDLGYPCDKIHG--------GMIQEDRFDVMN 284
Cdd:COG1111   331 DIEHPkLSKLRE-----ILKEQLGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGqaskegdkGLTQKEQIEILE 405
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 285 EFKRGEYRYLVATDVAARGIDIENISLVINYDL-PLEKESyVHRTGRTGRaGNKGKAISFVA------AF-------EKR 350
Cdd:COG1111   406 RFRAGEFNVLVATSVAEEGLDIPEVDLVIFYEPvPSEIRS-IQRKGRTGR-KREGRVVVLIAkgtrdeAYywssrrkEKK 483
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 351 FLADIEEYIGFEIQKIEAPSQEEVARKKPEFLAKLNDRPESKKDKSEELNKDIMklyfNGGKKKKIRAVDFVGTIAKIDG 430
Cdd:COG1111   484 MKSILKKLKKLLDKQEKEKLKESAQATLDEFESIKELAEDEINEKDLDEIESSE----NGAHVDWREPVLLQVIVSTLAE 559
                         250
                  ....*....|...
gi 1717936739 431 VSADDIGIITIMD 443
Cdd:COG1111   560 SLELRELGEKVDD 572
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
40-184 6.18e-15

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: 71.67  E-value: 6.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  40 KDLVVKSQTGSGKTASFGIPLCELADwdENKPQALILTPTRELAVQVKEDITniGRFKRIKATAVFGKSSFDKQKAELK- 118
Cdd:cd00046     2 ENVLITAPTGSGKTLAALLAALLLLL--KKGKKVLVLVPTKALALQTAERLR--ELFGPGIRVAVLVGGSSAEEREKNKl 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1717936739 119 QKSHIVVGTPGRVLDHIEKGTLP-LDRLSYLVIDEADEML-NMGFIEQV-EAIIKHLPTERTTMLFSAT 184
Cdd:cd00046    78 GDADIIIATPDMLLNLLLREDRLfLKDLKLIIVDEAHALLiDSRGALILdLAVRKAGLKNAQVILLSAT 146
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
12-409 1.51e-14

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 75.70  E-value: 1.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  12 DILRALEGLGYTEPTKVQQSVIPA-VLERKDLVVKSQTGSGKTAsfgipLCELADWD--ENKPQALILTPTRELAVQVKE 88
Cdd:COG1204    10 KVIEFLKERGIEELYPPQAEALEAgLLEGKNLVVSAPTASGKTL-----IAELAILKalLNGGKALYIVPLRALASEKYR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  89 DITNIGRFKRIKATAVFGksSFDKQKAELKQKShIVVGTPGRVLDHIEKGTLPLDRLSYLVIDEA----DEmlNMGFI-E 163
Cdd:COG1204    85 EFKRDFEELGIKVGVSTG--DYDSDDEWLGRYD-ILVATPEKLDSLLRNGPSWLRDVDLVVVDEAhlidDE--SRGPTlE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 164 QVEAIIKHLPTERTTMLFSATLPqdieklsrqymqNPEHIE-------VKAAGLTTRNIE----HAVIQVREENKFS--- 229
Cdd:COG1204   160 VLLARLRRLNPEAQIVALSATIG------------NAEEIAewldaelVKSDWRPVPLNEgvlyDGVLRFDDGSRRSkdp 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 230 ---LLKDVLmtENPDSCIIFCRTKEHVNQL----------------TDELDDLGYPCDKI-------------------- 270
Cdd:COG1204   228 tlaLALDLL--EEGGQVLVFVSSRRDAESLakkladelkrrltpeeREELEELAEELLEVseethtnekladclekgvaf 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 271 -HGGMIQEDRFDVMNEFKRGEYRYLVATD-------VAARGIDIENISLVINYDLP-LEkesyVHR-TGRTGRAG--NKG 338
Cdd:COG1204   306 hHAGLPSELRRLVEDAFREGLIKVLVATPtlaagvnLPARRVIIRDTKRGGMVPIPvLE----FKQmAGRAGRPGydPYG 381
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1717936739 339 KAIsFVAAFEKRFLADIEEYIGFEIQKIEAPSQEEVArkkpeFLAKLNDRPESKKDKSEElnkDIMKLYFN 409
Cdd:COG1204   382 EAI-LVAKSSDEADELFERYILGEPEPIRSKLANESA-----LRTHLLALIASGFANSRE---ELLDFLEN 443
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
10-343 1.75e-13

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 72.82  E-value: 1.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  10 SHDILRalEGLGYTEPTKVQQSVIPAVLERKDLVVKSQTGSGKTASFGIPlceladwdenkpqALI---LTPTRELAVQV 86
Cdd:PRK11057   13 AKQVLQ--ETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIP-------------ALVldgLTLVVSPLISL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  87 KEDITNIGRFKRIKATAVFGKSSFDKQKA--------ELKqkshIVVGTPGRVL--DHIEkgTLPLDRLSYLVIDEAD-- 154
Cdd:PRK11057   78 MKDQVDQLLANGVAAACLNSTQTREQQLEvmagcrtgQIK----LLYIAPERLMmdNFLE--HLAHWNPALLAVDEAHci 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 155 ---------EMLNMGFIEQVeaiIKHLPTERTTMLFSATLPQDIekLSRQYMQNPeHIEVKAagLTTRNIEHAVIQvree 225
Cdd:PRK11057  152 sqwghdfrpEYAALGQLRQR---FPTLPFMALTATADDTTRQDI--VRLLGLNDP-LIQISS--FDRPNIRYTLVE---- 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 226 nKFSLLKDVLM---TENPDSCIIFCRTKEHVNQLTDELDDLGYPCDKIHGGMIQEDRFDVMNEFKRGEYRYLVATDVAAR 302
Cdd:PRK11057  220 -KFKPLDQLMRyvqEQRGKSGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGM 298
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1717936739 303 GIDIENISLVINYDLPLEKESYVHRTGRTGRAGNKGKAISF 343
Cdd:PRK11057  299 GINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLF 339
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
13-345 1.96e-12

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: 69.48  E-value: 1.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  13 ILRALEGLGYTEPTKVQQSVIPAVLERKDLVVKSQTGSGKTASFGIP-LCELAdwDENKPQALILTPTRELAV-QVK--- 87
Cdd:COG1205    45 LRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPvLEALL--EDPGATALYLYPTKALARdQLRrlr 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  88 EDITNIGRfkRIKATAVFGKSSFDkQKAELKQKSHIVVGTPgrvlDHIEKGTLP--------LDRLSYLVIDEADE---- 155
Cdd:COG1205   123 ELAEALGL--GVRVATYDGDTPPE-ERRWIREHPDIVLTNP----DMLHYGLLPhhtrwarfFRNLRYVVIDEAHTyrgv 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 156 ----MLNMgfIEQVEAIIKHLPTERTTMLFSATLpqdieklsrqymQNP-EHievkAAGLTTRNIEH------------- 217
Cdd:COG1205   196 fgshVANV--LRRLRRICRHYGSDPQFILASATI------------GNPaEH----AERLTGRPVTVvdedgsprgertf 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 218 ------AVIQVREENKFSLLKDVLM--TENPDSCIIFCRTKEHVNQLT----DELDDLGYPcDKI---HGGMIQEDRFDV 282
Cdd:COG1205   258 vlwnppLVDDGIRRSALAEAARLLAdlVREGLRTLVFTRSRRGAELLAryarRALREPDLA-DRVaayRAGYLPEERREI 336
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1717936739 283 MNEFKRGEYRYLVATDVAARGIDIENISLVINYDLPLEKESYVHRTGRTGRAGNKGKAIsFVA 345
Cdd:COG1205   337 ERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVV-LVA 398
PRK13766 PRK13766
Hef nuclease; Provisional
227-416 6.96e-12

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 67.98  E-value: 6.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 227 KFSLLKDVL---MTENPDSCII-FCRTKEHVNQLTDELDDLGYPCDKIHG--------GMIQEDRFDVMNEFKRGEYRYL 294
Cdd:PRK13766  348 KLEKLREIVkeqLGKNPDSRIIvFTQYRDTAEKIVDLLEKEGIKAVRFVGqaskdgdkGMSQKEQIEILDKFRAGEFNVL 427
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 295 VATDVAARGIDIENISLVINYD-LPLEKESyVHRTGRTGRaGNKGKAISFVA------AF-------EKRF---LADIEE 357
Cdd:PRK13766  428 VSTSVAEEGLDIPSVDLVIFYEpVPSEIRS-IQRKGRTGR-QEEGRVVVLIAkgtrdeAYywssrrkEKKMkeeLKNLKG 505
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1717936739 358 YIGfEIQKIEAPSQEEVARKKPEFLAKLNDRPESKKDKSEELNKDIMKLYFNGGKKKKI 416
Cdd:PRK13766  506 ILN-KKLQELDEEQKGEEEEKDEQLSLDDFVKSKGKEEEEEEEKEEKDKETEEDEPEGP 563
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
227-318 2.84e-11

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: 60.95  E-value: 2.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 227 KFSLLKDVLMT--ENPDSCIIFCRTKEHVNQLTDELDDLGYPCDKIHGGMIQEDRFDVMNEFKR--GEYRYLVATDVAAR 302
Cdd:cd18793    12 KLEALLELLEElrEPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEdpDIRVFLLSTKAGGV 91
                          90
                  ....*....|....*.
gi 1717936739 303 GIDIENISLVINYDLP 318
Cdd:cd18793    92 GLNLTAANRVILYDPW 107
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
227-337 3.80e-11

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: 60.68  E-value: 3.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 227 KFSLLKDVLMTENPDS----CIIFCRTKEHVNQLTDELDDLGYPCDKIHGG---------------MIQEDRFDVMNEFK 287
Cdd:cd18802     8 KLQKLIEILREYFPKTpdfrGIIFVERRATAVVLSRLLKEHPSTLAFIRCGfligrgnssqrkrslMTQRKQKETLDKFR 87
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1717936739 288 RGEYRYLVATDVAARGIDIENISLVINYDLPLEKESYVHRTGRTGRAGNK 337
Cdd:cd18802    88 DGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGRARAPNSK 137
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
240-344 6.02e-10

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: 55.40  E-value: 6.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 240 PDSCIIFCRTKEHVNQLTDELddlgypcdKIhggmiqedrfdvmnefkrgeyryLVATDVAARGIDIENISLVINYDLPL 319
Cdd:cd18785     3 VVKIIVFTNSIEHAEEIASSL--------EI-----------------------LVATNVLGEGIDVPSLDTVIFFDPPS 51
                          90       100
                  ....*....|....*....|....*.
gi 1717936739 320 EKESYVHRTGRTGRAGNK-GKAISFV 344
Cdd:cd18785    52 SAASYIQRVGRAGRGGKDeGEVILFV 77
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
242-336 2.73e-09

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: 55.73  E-value: 2.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 242 SCIIFCRTKEHVNQLTDELDDLG---YPCDKI---HGGMIQEDRFDVMNEFKRGEYRYLVATDVAARGIDIENISLVINY 315
Cdd:cd18796    40 STLVFTNTRSQAERLAQRLRELCpdrVPPDFIalhHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQI 119
                          90       100
                  ....*....|....*....|.
gi 1717936739 316 DLPLEKESYVHRTGRTGRAGN 336
Cdd:cd18796   120 GSPKSVARLLQRLGRSGHRPG 140
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
227-318 7.56e-09

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 57.93  E-value: 7.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 227 KFSLLKDVL--MTENPDSCIIFCRTKEHVNQLTDELDDLGYPCDKIHGGMIQEDRFDVMNEFKRGEY--RYLVATDVAAR 302
Cdd:COG0553   534 KLEALLELLeeLLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEapVFLISLKAGGE 613
                          90
                  ....*....|....*.
gi 1717936739 303 GIDIENISLVINYDLP 318
Cdd:COG0553   614 GLNLTAADHVIHYDLW 629
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
273-341 1.04e-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: 53.90  E-value: 1.04e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1717936739 273 GMIQEDRFDVMNEFKRGEYRYLVATDVAARGIDIENISLVINYDLPLEKESYVHRTGRTGRaGNKGKAI 341
Cdd:cd18801    73 GMSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR-KRQGRVV 140
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
29-187 1.07e-08

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


Pssm-ID: 350679 [Multi-domain]  Cd Length: 181  Bit Score: 54.58  E-value: 1.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  29 QQSVIPAVLERKD-LVVKSQTGSGKT--ASFGIplceLADWDENKPQALILTPTRELAVQVKEDITNIGRFKRIKATAVF 105
Cdd:cd17921     6 QREALRALYLSGDsVLVSAPTSSGKTliAELAI----LRALATSGGKAVYIAPTRALVNQKEADLRERFGPLGKNVGLLT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 106 GKSSFDKQKAelkQKSHIVVGTPgrvldhiEK--------GTLPLDRLSYLVIDEAdEMLNMGfiEQ---VEAIIKHLPT 174
Cdd:cd17921    82 GDPSVNKLLL---AEADILVATP-------EKldlllrngGERLIQDVRLVVVDEA-HLIGDG--ERgvvLELLLSRLLR 148
                         170
                  ....*....|....*.
gi 1717936739 175 ERTTMLF---SATLPQ 187
Cdd:cd17921   149 INKNARFvglSATLPN 164
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
29-153 1.10e-08

DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350681 [Multi-domain]  Cd Length: 182  Bit Score: 54.51  E-value: 1.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  29 QQSVIPAVLERKDLVVKSQTGSGKTASFGIPLCELADWDENkPQALILTPTRELAVQVKEDITNIGR--FKRIKATAVFG 106
Cdd:cd17923     5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDPG-SRALYLYPTKALAQDQLRSLRELLEqlGLGIRVATYDG 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1717936739 107 KSSFDKQKAELKQKSHIVVGTPgrvlDHIEKGTLP--------LDRLSYLVIDEA 153
Cdd:cd17923    84 DTPREERRAIIRNPPRILLTNP----DMLHYALLPhhdrwarfLRNLRYVVLDEA 134
RRM_EcDbpA_like cd12501
RNA recognition motif (RRM) found in Escherichia coli RNA helicase dbpA and similar proteins; ...
409-476 1.90e-08

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: 51.09  E-value: 1.90e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1717936739 409 NGGKKKKIRAVDFVGTIAKIDGVSADDIGIITIMDNASYVEILNGKGPHVLKVMKNTTVKGKQLKVNK 476
Cdd:cd12501     5 DGGKKQKLRPGDILGALTGDNGIDGEDIGKINITDFVSYVAVKRSVAKDALKKLREGKIKGRKFRVRL 72
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
27-153 7.04e-08

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: 52.52  E-value: 7.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  27 KVQQSVIPAVLERKDLVVKSQTGSGKTAsfgIPLCELADWDENKP-QALILTPTRELAVQVKEditnigRFKRI-----K 100
Cdd:cd18035     4 RLYQVLIAAVALNGNTLIVLPTGLGKTI---IAILVAADRLTKKGgKVLILAPSRPLVEQHAE------NLKRVlnipdK 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1717936739 101 ATAVFGKSSFDKqKAELKQKSHIVVGTPGRVLDHIEKGTLPLDRLSYLVIDEA 153
Cdd:cd18035    75 ITSLTGEVKPEE-RAERWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEA 126
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
243-341 7.39e-08

C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350184 [Multi-domain]  Cd Length: 146  Bit Score: 51.49  E-value: 7.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 243 CIIFCRTKEHVNQLT----DELDDLGYPCDKI---HGGMIQEDRFDVMNEFKRGEYRYLVATDVAARGIDIENISLVINY 315
Cdd:cd18797    38 TIVFCRSRKLAELLLrylkARLVEEGPLASKVasyRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLA 117
                          90       100
                  ....*....|....*....|....*.
gi 1717936739 316 DLPLEKESYVHRTGRTGRAGNKGKAI 341
Cdd:cd18797   118 GYPGSLASLWQQAGRAGRRGKDSLVI 143
Cas3 COG1203
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ...
26-306 1.66e-07

CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system


Pssm-ID: 440816 [Multi-domain]  Cd Length: 535  Bit Score: 53.55  E-value: 1.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  26 TKVQQSVIPAVLERKDLVV-KSQTGSGKT-ASFGIPLcELAdwDENKPQALILT-PTRELAVQVKEDITNIGRFKRIKA- 101
Cdd:COG1203   133 NEALELALEAAEEEPGLFIlTAPTGGGKTeAALLFAL-RLA--AKHGGRRIIYAlPFTSIINQTYDRLRDLFGEDVLLHh 209
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 102 -TAVF----GKSSFDKQKAELKQKSH-----IVVGTPGRVLDHIEKG----TLPLDRLSY--LVIDEAD----EMLNMgF 161
Cdd:COG1203   210 sLADLdlleEEEEYESEARWLKLLKElwdapVVVTTIDQLFESLFSNrkgqERRLHNLANsvIILDEVQayppYMLAL-L 288
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 162 IEQVEAiIKHLPTerTTMLFSATLPQ-DIEKLSRQYM---QNPEHIEVKAAGLTTRNIEHAVIQVREENKFSLLKDVLMT 237
Cdd:COG1203   289 LRLLEW-LKNLGG--SVILMTATLPPlLREELLEAYElipDEPEELPEYFRAFVRKRVELKEGPLSDEELAELILEALHK 365
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1717936739 238 ENpdSCIIFCRTKEHVNQLTDELDDLG--YPCDKIHGGMIQEDRFD----VMNEFKRGEYRYLVATDVAARGIDI 306
Cdd:COG1203   366 GK--SVLVIVNTVKDAQELYEALKEKLpdEEVYLLHSRFCPADRSEiekeIKERLERGKPCILVSTQVVEAGVDI 438
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
41-337 3.73e-07

CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DEAD/DEAH box helicase DNA helicase cas3'; Often but not always is fused to HD nuclease domain; signature gene for Type I


Pssm-ID: 187770 [Multi-domain]  Cd Length: 353  Bit Score: 52.05  E-value: 3.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  41 DLVVKSQTGSGKT-ASFGIPLCELADWDENKpqALILTPTRELAvqvkEDITNigrfkriKATAVFGKSSFDKQKAELKQ 119
Cdd:cd09639     1 LLVIEAPTGYGKTeAALLWALHSLKSQKADR--VIIALPTRATI----NAMYR-------RAKEAFGETGLYHSSILSSR 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 120 KSH-------------------------IVVGTP-------GRVLDHIEKGTLPLDRlSYLVIDEAD--EMLNMGFIEqv 165
Cdd:cd09639    68 IKEmgdseefehlfplyihsndtlfldpITVCTIdqvlksvFGEFGHYEFTLASIAN-SLLIFDEVHfyDEYTLALIL-- 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 166 eAIIKHLPTERTT-MLFSATLPQDIEKLSRQYMQNPEHIevkaaGLTTRNIEHAVIQVREEN---KFSLLKDVLMTEN-P 240
Cdd:cd09639   145 -AVLEVLKDNDVPiLLMSATLPKFLKEYAEKIGYVEENE-----PLDLKPNERAPFIKIESDkvgEISSLERLLEFIKkG 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 241 DSCIIFCRTKEHVNQLTDELDDLGYPCDK--IHGGMIQEDRFD----VMNEFKRGEYRYLVATDVAARGIDIeNISLVIN 314
Cdd:cd09639   219 GSVAIIVNTVDRAQEFYQQLKEKGPEEEImlIHSRFTEKDRAKkeaeLLLEFKKSEKFVIVATQVIEASLDI-SVDVMIT 297
                         330       340
                  ....*....|....*....|...
gi 1717936739 315 YDLPLekESYVHRTGRTGRAGNK 337
Cdd:cd09639   298 ELAPI--DSLIQRLGRLHRYGEK 318
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
242-313 1.70e-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: 46.78  E-value: 1.70e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1717936739 242 SCIIFCRTKEHVNQLTDELDDLGYPCDKIHGGMIQEDRFDVM---NEFKRGEYRYLVATDVAARGIDIENISLVI 313
Cdd:cd18799     8 KTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGDEAlilLFFGELKPPILVTVDLLTTGVDIPEVDNVV 82
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
48-153 6.38e-06

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


Pssm-ID: 350792 [Multi-domain]  Cd Length: 200  Bit Score: 46.88  E-value: 6.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  48 TGSGKT--ASFGIPlcELADWD----ENKPQALILTPTRELAVQVKEDITNIGRFKRIKATAVFGKSSFDKQ--KAELKQ 119
Cdd:cd18034    25 TGSGKTliAVMLIK--EMGELNrkekNPKKRAVFLVPTVPLVAQQAEAIRSHTDLKVGEYSGEMGVDKWTKErwKEELEK 102
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1717936739 120 KsHIVVGTPGRVLDHIEKGTLPLDRLSYLVIDEA 153
Cdd:cd18034   103 Y-DVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
220-344 6.98e-06

C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350176 [Multi-domain]  Cd Length: 153  Bit Score: 46.09  E-value: 6.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 220 IQVREENKFSLLKDVL-MTENPDSCIIFCRTKEHVNQLTDeldDLGYPCdkIHGGMIQEDRFDVMNEFKRGEYRYLVATD 298
Cdd:cd18789    28 LAAMNPNKLRALEELLkRHEQGDKIIVFTDNVEALYRYAK---RLLKPF--ITGETPQSEREEILQNFREGEYNTLVVSK 102
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1717936739 299 VAARGIDI--ENISLVINYDLPLEKEsYVHRTGRTGRAGNKGKAISFV 344
Cdd:cd18789   103 VGDEGIDLpeANVAIQISGHGGSRRQ-EAQRLGRILRPKKGGGKNAFF 149
PLN03137 PLN03137
ATP-dependent DNA helicase; Q4-like; Provisional
233-337 1.04e-05

ATP-dependent DNA helicase; Q4-like; Provisional


Pssm-ID: 215597 [Multi-domain]  Cd Length: 1195  Bit Score: 48.35  E-value: 1.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  233 DVLMTENP-DSC-IIFCRTKEHVNQLTDELDDLGYPCDKIHGGMIQEDRFDVMNEFKRGEYRYLVATDVAARGIDIENIS 310
Cdd:PLN03137   671 DKFIKENHfDECgIIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVR 750
                           90       100
                   ....*....|....*....|....*..
gi 1717936739  311 LVINYDLPLEKESYVHRTGRTGRAGNK 337
Cdd:PLN03137   751 FVIHHSLPKSIEGYHQECGRAGRDGQR 777
RRM_EcCsdA_like cd12499
RNA recognition motif (RRM) found in Escherichia coli cold-shock DEAD box protein A (CsdA) and ...
411-477 1.57e-05

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: 42.95  E-value: 1.57e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1717936739 411 GKKKKIRAVDFVGTIAKIDGVSADDIGIITIMDNASYVEILNGKGPHVLKVMKNTTVKGKQLKVNKA 477
Cdd:cd12499     7 GRKDGVKPGNIVGAIANEAGIDSRFIGRIKIFDDHSTVELPKGMPKDVLQHLKKVRVCGQPLNIKLL 73
ResIII pfam04851
Type III restriction enzyme, res subunit;
24-184 4.03e-05

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 43.81  E-value: 4.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  24 EPTKVQQSVIPAVLE-----RKDLVVKSQTGSGKTA-SFGIPLcELADWDENKPqALILTPTRELAVQVKEDITnigrfK 97
Cdd:pfam04851   3 ELRPYQIEAIENLLEsikngQKRGLIVMATGSGKTLtAAKLIA-RLFKKGPIKK-VLFLVPRKDLLEQALEEFK-----K 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  98 RIKATAVFGKSSFDKQKAELKQKSHIVVGTPGRVLDHIEKGTLPL--DRLSYLVIDEADEmlnmGFIEQVEAIIKHLPte 175
Cdd:pfam04851  76 FLPNYVEIGEIISGDKKDESVDDNKIVVTTIQSLYKALELASLELlpDFFDVIIIDEAHR----SGASSYRNILEYFK-- 149
                         170
                  ....*....|
gi 1717936739 176 RTTML-FSAT 184
Cdd:pfam04851 150 PAFLLgLTAT 159
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
270-335 6.30e-05

C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350198 [Multi-domain]  Cd Length: 159  Bit Score: 43.10  E-value: 6.30e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1717936739 270 IHGGMIQEDRFDVMNEFKRGEYRYLVATDVAARGIDIENISLVINYDLPLEKESYVHR-TGRTGRAG 335
Cdd:cd18811    67 LHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIEDAERFGLSQLHQlRGRVGRGD 133
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
26-128 7.71e-05

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: 43.88  E-value: 7.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  26 TKVQQSVIPAVLE-RKDLVVKSQTGSGKTASFgiplcELA---------DWDENKPQALILTPTRELAVQVKEDITniGR 95
Cdd:cd18023     3 NRIQSEVFPDLLYsDKNFVVSAPTGSGKTVLF-----ELAilrllkernPLPWGNRKVVYIAPIKALCSEKYDDWK--EK 75
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1717936739  96 FKR--IKATAVFGKSSFDKQKaELkQKSHIVVGTP 128
Cdd:cd18023    76 FGPlgLSCAELTGDTEMDDTF-EI-QDADIILTTP 108
DEXHc_cas3 cd17930
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ...
42-198 9.63e-05

DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase responsible for degradation of dsDNA. The two enzymatic units of Cas3, a histidine-aspartate (HD) nuclease and a Superfamily 2 (SF2) helicase, may be expressed from separate genes as Cas3' (SF2 helicase) and Cas3'' (HD nuclease) or may be fused as a single HD-SF2 polypeptide. The nucleolytic activity of most Cas3 enzymes is transition metal ion-dependent. Cas3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350688 [Multi-domain]  Cd Length: 186  Bit Score: 43.05  E-value: 9.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  42 LVVKSQTGSGKT-ASFgipLCELADWDENKPQALILT-PTRELAVQVKEDITNI-GRFKR----------------IKAT 102
Cdd:cd17930     4 VILEAPTGSGKTeAAL---LWALKLAARGGKRRIIYAlPTRATINQMYERIREIlGRLDDedkvlllhskaalellESDE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 103 AVFGKSSFDKQKAELKQK---SHIVVGTPGRVLDHIEKGTLPLDRL-----SYLVIDEA----DEMLNMgFIEQVEAIIK 170
Cdd:cd17930    81 EPDDDPVEAVDWALLLKRswlAPIVVTTIDQLLESLLKYKHFERRLhglanSVVVLDEVqaydPEYMAL-LLKALLELLG 159
                         170       180
                  ....*....|....*....|....*...
gi 1717936739 171 HLPTerTTMLFSATLPQDIEKLSRQYMQ 198
Cdd:cd17930   160 ELGG--PVVLMTATLPALLRDELLEALL 185
PRK09751 PRK09751
putative ATP-dependent helicase Lhr; Provisional
271-332 1.04e-04

putative ATP-dependent helicase Lhr; Provisional


Pssm-ID: 137505 [Multi-domain]  Cd Length: 1490  Bit Score: 44.92  E-value: 1.04e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1717936739  271 HGGMIQEDRFDVMNEFKRGEYRYLVATDVAARGIDIENISLVINYDLPLEKESYVHRTGRTG 332
Cdd:PRK09751   308 HGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAG 369
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
24-168 1.29e-04

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


Pssm-ID: 350676 [Multi-domain]  Cd Length: 180  Bit Score: 42.79  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  24 EPTKVQQSVIPAVL------ERKDLVVKSQTGSGKTASFGIPlceLADWDENKPQALILTPTRELAVQVKEDITNigRFK 97
Cdd:cd17918    15 SLTKDQAQAIKDIEkdlhspEPMDRLLSGDVGSGKTLVALGA---ALLAYKNGKQVAILVPTEILAHQHYEEARK--FLP 89
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1717936739  98 RIKATAVfgkSSFDKQKAElkQKSHIVVGTpgRVLDHIEKGTLPLDrlsyLVIdeADEMLNMGfIEQVEAI 168
Cdd:cd17918    90 FINVELV---TGGTKAQIL--SGISLLVGT--HALLHLDVKFKNLD----LVI--VDEQHRFG-VAQREAL 146
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
22-90 1.63e-04

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 44.32  E-value: 1.63e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1717936739  22 YTEPTKVQQSVIPAVLERKDLVVKSQTGSGKT-ASFGIPLCELA-----DWDENKPQALILTPTRELAVqvkeDI 90
Cdd:COG1201    22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAFLPALDELArrprpGELPDGLRVLYISPLKALAN----DI 92
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
24-153 3.42e-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: 41.65  E-value: 3.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  24 EPTKVQQSVIPAVLERKDLVVKSQTGSGKTaSFGIPLCE-LADWDENKPQA--LILTPTRELAVQVKEDITNIGRFKRIK 100
Cdd:cd17927     2 KPRNYQLELAQPALKGKNTIICLPTGSGKT-FVAVLICEhHLKKFPAGRKGkvVFLANKVPLVEQQKEVFRKHFERPGYK 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1717936739 101 ATAVFGKSSFDKQKAELKQKSHIVVGTPGRVLDHIEKGTLP-LDRLSYLVIDEA 153
Cdd:cd17927    81 VTGLSGDTSENVSVEQIVESSDVIIVTPQILVNDLKSGTIVsLSDFSLLVFDEC 134
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
270-316 4.66e-04

C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. 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: 350179 [Multi-domain]  Cd Length: 160  Bit Score: 40.71  E-value: 4.66e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1717936739 270 IHGGMIQEDRFDVMNEFKRGEYRYLVATDVAARGIDIENISLVINYD 316
Cdd:cd18792    66 LHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIED 112
SF2_C_TRCF cd18810
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ...
270-340 6.48e-04

C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350197 [Multi-domain]  Cd Length: 151  Bit Score: 40.02  E-value: 6.48e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1717936739 270 IHGGMIQEDRFDVMNEFKRGEYRYLVATDVAARGIDIENISLVINYDLPLEKESYVHR-TGRTGRAGNKGKA 340
Cdd:cd18810    57 AHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIIERADKFGLAQLYQlRGRVGRSKERAYA 128
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
43-185 8.45e-04

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: 39.60  E-value: 8.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  43 VVKSQTGSGKTA-SFGIPlCELAdwdenKPQALILTPTRELAVQVKEDITNIGRFKRIKataVFGKSSFDKQKAELkqks 121
Cdd:cd17926    22 ILVLPTGSGKTLtALALI-AYLK-----ELRTLIVVPTDALLDQWKERFEDFLGDSSIG---LIGGGKKKDFDDAN---- 88
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1717936739 122 hIVVGTPGRVLDHIEKGTLPLDRLSYLVIDEADEMLNMGFieqvEAIIKHLPTERtTMLFSATL 185
Cdd:cd17926    89 -VVVATYQSLSNLAEEEKDLFDQFGLLIVDEAHHLPAKTF----SEILKELNAKY-RLGLTATP 146
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
40-157 1.72e-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: 39.10  E-value: 1.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  40 KDLVVKSQTGSGKT-ASFGIPLCELADWDENKPQALILTPTRELAVqvkeDItnigrFKRIKATA--------VFGK--- 107
Cdd:cd17922     2 RNVLIAAPTGSGKTeAAFLPALSSLADEPEKGVQVLYISPLKALIN----DQ-----ERRLEEPLdeidleipVAVRhgd 72
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1717936739 108 -SSFDKQKAeLKQKSHIVVGTP--------GRVLDHIEKGtlpldrLSYLVIDEADEML 157
Cdd:cd17922    73 tSQSEKAKQ-LKNPPGILITTPeslelllvNKKLRELFAG------LRYVVVDEIHALL 124
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
28-186 3.47e-03

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: 38.47  E-value: 3.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  28 VQQSVIPAVLER-KDLVVKSQTGSGKTAsfgipLCELA---DWDENKpQALILTPTRELAVQVKEDitnigrFKRIKATA 103
Cdd:cd18028     5 PQAEAVRAGLLKgENLLISIPTASGKTL-----IAEMAmvnTLLEGG-KALYLVPLRALASEKYEE------FKKLEEIG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 104 V-FGKSSFD-KQKAELKQKSHIVVGTPGRVLDHIEKGTLPLDRLSYLVIDE---ADEMLNMGFIEQVEAIIKHLPTERTT 178
Cdd:cd18028    73 LkVGISTGDyDEDDEWLGDYDIIVATYEKFDSLLRHSPSWLRDVGVVVVDEihlISDEERGPTLESIVARLRRLNPNTQI 152

                  ....*...
gi 1717936739 179 MLFSATLP 186
Cdd:cd18028   153 IGLSATIG 160
PRK13767 PRK13767
ATP-dependent helicase; Provisional
22-313 3.53e-03

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 39.87  E-value: 3.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  22 YTEPTKVQQSVIPAVLERKDLVVKSQTGSGKT-ASF-GI--PLCELADWD--ENKPQALILTPTRELAVQVK-------E 88
Cdd:PRK13767   30 FGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAFlAIidELFRLGREGelEDKVYCLYVSPLRALNNDIHrnleeplT 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  89 DITNIGRFKRIK------ATAVFGKSSFDKQKAeLKQKSHIVVGTPgrvldhiEkgTLPL--------DRLS---YLVID 151
Cdd:PRK13767  110 EIREIAKERGEElpeirvAIRTGDTSSYEKQKM-LKKPPHILITTP-------E--SLAIllnspkfrEKLRtvkWVIVD 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 152 EADEMLN-------MGFIEQVEAIIKHLPTeRTTMlfSATlpqdIEKLS--------RQYMQNPEHIE------VKAAGL 210
Cdd:PRK13767  180 EIHSLAEnkrgvhlSLSLERLEELAGGEFV-RIGL--SAT----IEPLEevakflvgYEDDGEPRDCEivdarfVKPFDI 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739 211 T----TRNIEHAVIQVREENKFSLLKDVLMTENpdSCIIFCRTK---EHV-NQLTDELDDlGYPCDKI---HGGMIQEDR 279
Cdd:PRK13767  253 KvispVDDLIHTPAEEISEALYETLHELIKEHR--TTLIFTNTRsgaERVlYNLRKRFPE-EYDEDNIgahHSSLSREVR 329
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1717936739 280 FDVMNEFKRGEYRYLVATDVAARGIDIENISLVI 313
Cdd:PRK13767  330 LEVEEKLKRGELKVVVSSTSLELGIDIGYIDLVV 363
PRK10917 PRK10917
ATP-dependent DNA helicase RecG; Provisional
270-313 7.22e-03

ATP-dependent DNA helicase RecG; Provisional


Pssm-ID: 236794 [Multi-domain]  Cd Length: 681  Bit Score: 38.98  E-value: 7.22e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1717936739 270 IHGGMIQEDRFDVMNEFKRGEYRYLVATDVAARGIDIENISL-VI 313
Cdd:PRK10917  511 LHGRMKPAEKDAVMAAFKAGEIDILVATTVIEVGVDVPNATVmVI 555
DEXDc_FANCM cd18033
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ...
71-153 9.41e-03

DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. In complex with CENPS and CENPX, it binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA), and Holliday junction substrates. Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX. In complex with FAAP24, it efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates. In vitro, on its own, it strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA. FANCM is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350791 [Multi-domain]  Cd Length: 182  Bit Score: 37.30  E-value: 9.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717936739  71 PQALI--LTPTRELAVQVKEDITNIGRFKRiKATAVFGKSSFDKQKAELKQKSHIVVGTPGRVLDHIEKGTLPLDRLSYL 148
Cdd:cd18033    45 PKGKIvfMAPTKPLVSQQIEACYKITGIPS-SQTAELTGSVPPTKRAELWASKRVFFLTPQTLENDLKEGDCDPKSIVCL 123

                  ....*
gi 1717936739 149 VIDEA 153
Cdd:cd18033   124 VIDEA 128
RecG COG1200
RecG-like helicase [Replication, recombination and repair];
264-313 9.53e-03

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


Pssm-ID: 440813 [Multi-domain]  Cd Length: 684  Bit Score: 38.49  E-value: 9.53e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1717936739 264 GYPCDKIHGGMIQEDRFDVMNEFKRGEYRYLVATDVAARGIDIENISL-VI 313
Cdd:COG1200   503 GLRVGLLHGRMKPAEKDAVMAAFKAGEIDVLVATTVIEVGVDVPNATVmVI 553
 
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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