NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1198450891|gb|OUN38494|]
View 

DEAD/DEAH box helicase [Massilimicrobiota sp. An80]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 11424260)

DEAD/DEAH box containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA; contains an RNA recognition motif (RRM)

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
5-386 0e+00

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


:

Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 575.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891   5 TFYDLGLSKLVLQGIEMMGYVIPSPIQEKAIPVLLEGKDIIGQAQTGTGKTLAFGSVLLSCINKKDDG-VKALVLSPTRE 83
Cdd:COG0513     3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRaPQALILAPTRE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  84 LALQIDEELRRIGKYTSLSIVSVFGGSEIEKQIRSLKKGADIVVGTPGRVLDLMRRKALKLDCVEWLVLDEADEMLNMGF 163
Cdd:COG0513    83 LALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMGF 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 164 IDDIETILQTVPEDRHTVLFSATMPSDIKKIASFYMHeDYQHIQIKAKTMTASTVSQYYFETKVNRRFEVLCRILDSREM 243
Cdd:COG0513   163 IEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLK-NPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLRDEDP 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 244 DNAIIFCKTKRSVDEVVAAMQQKHYNVEAMHGDLSQNQRMNTLRRFKTGQIQYLVATDVAARGIDVDNISHVINYELPQD 323
Cdd:COG0513   242 ERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPED 321
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1198450891 324 EELYIHRIGRTGRANKKGEAYSIVTSRERNFLKAIEKHTHSHIEKLDIPAIEDIFDQKVKELL 386
Cdd:COG0513   322 PEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKRLERLK 384
DbpA pfam03880
DbpA RNA binding domain; This RNA binding domain is found at the C-terminus of a number of ...
445-516 5.53e-19

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: 80.88  E-value: 5.53e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1198450891 445 RIFMTVGSMDKVNVKDIIDFFVRYADIPKREIGDITIKRKFTFVNLSPGAAQKVLDYCYNQKIKGRRVRIEL 516
Cdd:pfam03880   1 RLFINVGKKDGVRPGDIVGALANEAGLPGDDIGKIDIFDNFSFVEVPAEKAEKVLKALKGTKIKGRKVRVEP 72
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
5-386 0e+00

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 575.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891   5 TFYDLGLSKLVLQGIEMMGYVIPSPIQEKAIPVLLEGKDIIGQAQTGTGKTLAFGSVLLSCINKKDDG-VKALVLSPTRE 83
Cdd:COG0513     3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRaPQALILAPTRE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  84 LALQIDEELRRIGKYTSLSIVSVFGGSEIEKQIRSLKKGADIVVGTPGRVLDLMRRKALKLDCVEWLVLDEADEMLNMGF 163
Cdd:COG0513    83 LALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMGF 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 164 IDDIETILQTVPEDRHTVLFSATMPSDIKKIASFYMHeDYQHIQIKAKTMTASTVSQYYFETKVNRRFEVLCRILDSREM 243
Cdd:COG0513   163 IEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLK-NPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLRDEDP 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 244 DNAIIFCKTKRSVDEVVAAMQQKHYNVEAMHGDLSQNQRMNTLRRFKTGQIQYLVATDVAARGIDVDNISHVINYELPQD 323
Cdd:COG0513   242 ERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPED 321
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1198450891 324 EELYIHRIGRTGRANKKGEAYSIVTSRERNFLKAIEKHTHSHIEKLDIPAIEDIFDQKVKELL 386
Cdd:COG0513   322 PEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKRLERLK 384
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
1-516 1.20e-130

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 387.62  E-value: 1.20e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891   1 MQQVTFYDLGLSKLVLQGIEMMGYVIPSPIQEKAIPVLLEGKDIIGQAQTGTGKTLAFGSVLLSCINKKDDGVKALVLSP 80
Cdd:PRK11776    1 MSMTAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  81 TRELALQIDEELRRIGKYT-SLSIVSVFGGSEIEKQIRSLKKGADIVVGTPGRVLDLMRRKALKLDCVEWLVLDEADEML 159
Cdd:PRK11776   81 TRELADQVAKEIRRLARFIpNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRML 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 160 NMGFIDDIETILQTVPEDRHTVLFSATMPSDIKKIASFYMHeDYQHIQIKAkTMTASTVSQYYFETKVNRRFEVLCRILD 239
Cdd:PRK11776  161 DMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQR-DPVEVKVES-THDLPAIEQRFYEVSPDERLPALQRLLL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 240 SREMDNAIIFCKTKRSVDEVVAAMQQKHYNVEAMHGDLSQNQRMNTLRRFKTGQIQYLVATDVAARGIDVDNISHVINYE 319
Cdd:PRK11776  239 HHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYE 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 320 LPQDEELYIHRIGRTGRANKKGEAYSIVTSRERNFLKAIEKHTHSHIEKLDIPAiedifdqkvkellfdvqeimlkgnmk 399
Cdd:PRK11776  319 LARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLPS-------------------------- 372
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 400 pfqkivkdipqhMKNDVIAALLAmcysqrvgydyqslnEMnkeeqrifMTV----GSMDKVNVKDIIDFFVRYADIPKRE 475
Cdd:PRK11776  373 ------------LSPLSGVPLLP---------------EM--------VTLcidgGKKDKLRPGDILGALTGDAGLDGAQ 417
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 1198450891 476 IGDITIKRKFTFVNLSPGAAQKVLDYCYNQKIKGRRVRIEL 516
Cdd:PRK11776  418 IGKINVTDFHAYVAVERAVAKKALKKLQNGKIKGKSFRVRL 458
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
15-207 4.42e-96

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: 289.34  E-value: 4.42e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  15 VLQGIEMMGYVIPSPIQEKAIPVLLEGKDIIGQAQTGTGKTLAFGSVLLSCIN----KKDDGVKALVLSPTRELALQIDE 90
Cdd:cd00268     1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLpepkKKGRGPQALVLAPTRELAMQIAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  91 ELRRIGKYTSLSIVSVFGGSEIEKQIRSLKKGADIVVGTPGRVLDLMRRKALKLDCVEWLVLDEADEMLNMGFIDDIETI 170
Cdd:cd00268    81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKI 160
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1198450891 171 LQTVPEDRHTVLFSATMPSDIKKIASFYMHeDYQHIQ 207
Cdd:cd00268   161 LSALPKDRQTLLFSATLPEEVKELAKKFLK-NPVRIE 196
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
28-194 6.02e-64

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: 205.55  E-value: 6.02e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  28 SPIQEKAIPVLLEGKDIIGQAQTGTGKTLAFGSVLLSCINKKDDGVKALVLSPTRELALQIDEELRRIGKYTSLSIVSVF 107
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 108 GGSEIEKQIRSLkKGADIVVGTPGRVLDLMRRKAlKLDCVEWLVLDEADEMLNMGFIDDIETILQTVPEDRHTVLFSATM 187
Cdd:pfam00270  81 GGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSATL 158

                  ....*..
gi 1198450891 188 PSDIKKI 194
Cdd:pfam00270 159 PRNLEDL 165
DEXDc smart00487
DEAD-like helicases superfamily;
19-221 1.35e-52

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 177.30  E-value: 1.35e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891   19 IEMMGYVIPSPIQEKAIPVLLEG-KDIIGQAQTGTGKTLAFGSVLLSCInKKDDGVKALVLSPTRELALQIDEELRRIGK 97
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEAL-KRGKGGRVLVLVPTRELAEQWAEELKKLGP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891   98 YTSLSIVSVFGGSEIEKQIRSLKKG-ADIVVGTPGRVLDLMRRKALKLDCVEWLVLDEADEMLNMGFIDDIETILQTVPE 176
Cdd:smart00487  80 SLGLKVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPK 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1198450891  177 DRHTVLFSATMPSDIKKIASFYMHEDyqhIQIKAKTMTASTVSQY 221
Cdd:smart00487 160 NVQLLLLSATPPEEIENLLELFLNDP---VFIDVGFTPLEPIEQF 201
DbpA pfam03880
DbpA RNA binding domain; This RNA binding domain is found at the C-terminus of a number of ...
445-516 5.53e-19

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: 80.88  E-value: 5.53e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1198450891 445 RIFMTVGSMDKVNVKDIIDFFVRYADIPKREIGDITIKRKFTFVNLSPGAAQKVLDYCYNQKIKGRRVRIEL 516
Cdd:pfam03880   1 RLFINVGKKDGVRPGDIVGALANEAGLPGDDIGKIDIFDNFSFVEVPAEKAEKVLKALKGTKIKGRKVRVEP 72
RRM_DbpA cd12252
RNA recognition motif (RRM) found in the DbpA subfamily of prokaryotic DEAD-box rRNA helicases; ...
445-515 8.64e-16

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: 71.81  E-value: 8.64e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1198450891 445 RIFMTVGSMDKVNVKDIIDFFVRYADIPKREIGDITIKRKFTFVNLSPGAAQKVLDYCYNQKIKGRRVRIE 515
Cdd:cd12252     1 RLFINVGRKDGIDPRDLLGAICRAGGISRDDIGAIRIFDNFSFVEVPEAEAERVIEALNGKKIKGKKLRVE 71
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
5-386 0e+00

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 575.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891   5 TFYDLGLSKLVLQGIEMMGYVIPSPIQEKAIPVLLEGKDIIGQAQTGTGKTLAFGSVLLSCINKKDDG-VKALVLSPTRE 83
Cdd:COG0513     3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRaPQALILAPTRE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  84 LALQIDEELRRIGKYTSLSIVSVFGGSEIEKQIRSLKKGADIVVGTPGRVLDLMRRKALKLDCVEWLVLDEADEMLNMGF 163
Cdd:COG0513    83 LALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMGF 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 164 IDDIETILQTVPEDRHTVLFSATMPSDIKKIASFYMHeDYQHIQIKAKTMTASTVSQYYFETKVNRRFEVLCRILDSREM 243
Cdd:COG0513   163 IEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLK-NPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLRDEDP 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 244 DNAIIFCKTKRSVDEVVAAMQQKHYNVEAMHGDLSQNQRMNTLRRFKTGQIQYLVATDVAARGIDVDNISHVINYELPQD 323
Cdd:COG0513   242 ERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPED 321
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1198450891 324 EELYIHRIGRTGRANKKGEAYSIVTSRERNFLKAIEKHTHSHIEKLDIPAIEDIFDQKVKELL 386
Cdd:COG0513   322 PEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKRLERLK 384
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
1-516 1.20e-130

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 387.62  E-value: 1.20e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891   1 MQQVTFYDLGLSKLVLQGIEMMGYVIPSPIQEKAIPVLLEGKDIIGQAQTGTGKTLAFGSVLLSCINKKDDGVKALVLSP 80
Cdd:PRK11776    1 MSMTAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  81 TRELALQIDEELRRIGKYT-SLSIVSVFGGSEIEKQIRSLKKGADIVVGTPGRVLDLMRRKALKLDCVEWLVLDEADEML 159
Cdd:PRK11776   81 TRELADQVAKEIRRLARFIpNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRML 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 160 NMGFIDDIETILQTVPEDRHTVLFSATMPSDIKKIASFYMHeDYQHIQIKAkTMTASTVSQYYFETKVNRRFEVLCRILD 239
Cdd:PRK11776  161 DMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQR-DPVEVKVES-THDLPAIEQRFYEVSPDERLPALQRLLL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 240 SREMDNAIIFCKTKRSVDEVVAAMQQKHYNVEAMHGDLSQNQRMNTLRRFKTGQIQYLVATDVAARGIDVDNISHVINYE 319
Cdd:PRK11776  239 HHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYE 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 320 LPQDEELYIHRIGRTGRANKKGEAYSIVTSRERNFLKAIEKHTHSHIEKLDIPAiedifdqkvkellfdvqeimlkgnmk 399
Cdd:PRK11776  319 LARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLPS-------------------------- 372
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 400 pfqkivkdipqhMKNDVIAALLAmcysqrvgydyqslnEMnkeeqrifMTV----GSMDKVNVKDIIDFFVRYADIPKRE 475
Cdd:PRK11776  373 ------------LSPLSGVPLLP---------------EM--------VTLcidgGKKDKLRPGDILGALTGDAGLDGAQ 417
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 1198450891 476 IGDITIKRKFTFVNLSPGAAQKVLDYCYNQKIKGRRVRIEL 516
Cdd:PRK11776  418 IGKINVTDFHAYVAVERAVAKKALKKLQNGKIKGKSFRVRL 458
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
3-428 1.71e-124

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 377.65  E-value: 1.71e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891   3 QVTFYDLGLSKLVLQGIEMMGYVIPSPIQEKAIPVLLEGKDIIGQAQTGTGKTLAFGSVLLSCINKKDDGVKALVLSPTR 82
Cdd:PRK11634    5 ETTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAPTR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  83 ELALQIDEELRRIGKYT-SLSIVSVFGGSEIEKQIRSLKKGADIVVGTPGRVLDLMRRKALKLDCVEWLVLDEADEMLNM 161
Cdd:PRK11634   85 ELAVQVAEAMTDFSKHMrGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRM 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 162 GFIDDIETILQTVPEDRHTVLFSATMPSDIKKIASFYMhEDYQHIQIKAKTMTASTVSQYYFETKVNRRFEVLCRILDSR 241
Cdd:PRK11634  165 GFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFM-KEPQEVRIQSSVTTRPDISQSYWTVWGMRKNEALVRFLEAE 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 242 EMDNAIIFCKTKRSVDEVVAAMQQKHYNVEAMHGDLSQNQRMNTLRRFKTGQIQYLVATDVAARGIDVDNISHVINYELP 321
Cdd:PRK11634  244 DFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIP 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 322 QDEELYIHRIGRTGRANKKGEAYSIVTSRERNFLKAIEKHTHSHIEKLDIPAIEDIFDQKVKELLFDVQEIMLKGNMKPF 401
Cdd:PRK11634  324 MDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEVELPNAELLGKRRLEKFAAKVQQQLESSDLDQY 403
                         410       420       430
                  ....*....|....*....|....*....|...
gi 1198450891 402 QKIVKDI-PQHMKND-----VIAALLAMCYSQR 428
Cdd:PRK11634  404 RALLAKIqPTAEGEEldletLAAALLKMAQGER 436
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
4-375 4.38e-106

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 324.84  E-value: 4.38e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891   4 VTFYDLGLSKLVLQGIEMMGYVIPSPIQEKAIPVLLEGKDIIGQAQTGTGKTLAFGSVLLSCINKKDDG------VKALV 77
Cdd:PRK10590    1 MSFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHakgrrpVRALI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  78 LSPTRELALQIDEELRRIGKYTSLSIVSVFGGSEIEKQIRSLKKGADIVVGTPGRVLDLMRRKALKLDCVEWLVLDEADE 157
Cdd:PRK10590   81 LTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 158 MLNMGFIDDIETILQTVPEDRHTVLFSATMPSDIKKIASFYMHEDYQhIQIKAKTMTASTVSQYYFETKVNRRFEVLCRI 237
Cdd:PRK10590  161 MLDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLE-IEVARRNTASEQVTQHVHFVDKKRKRELLSQM 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 238 LDSREMDNAIIFCKTKRSVDEVVAAMQQKHYNVEAMHGDLSQNQRMNTLRRFKTGQIQYLVATDVAARGIDVDNISHVIN 317
Cdd:PRK10590  240 IGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVN 319
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1198450891 318 YELPQDEELYIHRIGRTGRANKKGEAYSIVTSRERNFLKAIEKHTHSHIEKLDIPAIE 375
Cdd:PRK10590  320 YELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEIPRIAIPGYE 377
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
15-207 4.42e-96

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: 289.34  E-value: 4.42e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  15 VLQGIEMMGYVIPSPIQEKAIPVLLEGKDIIGQAQTGTGKTLAFGSVLLSCIN----KKDDGVKALVLSPTRELALQIDE 90
Cdd:cd00268     1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLpepkKKGRGPQALVLAPTRELAMQIAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  91 ELRRIGKYTSLSIVSVFGGSEIEKQIRSLKKGADIVVGTPGRVLDLMRRKALKLDCVEWLVLDEADEMLNMGFIDDIETI 170
Cdd:cd00268    81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKI 160
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1198450891 171 LQTVPEDRHTVLFSATMPSDIKKIASFYMHeDYQHIQ 207
Cdd:cd00268   161 LSALPKDRQTLLFSATLPEEVKELAKKFLK-NPVRIE 196
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
5-362 1.20e-95

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 296.85  E-value: 1.20e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891   5 TFYDLGLSKLVLQGIEMMGYVIPSPIQEKAIPVLLEGKDIIGQAQTGTGKTLAFgsvLLSCIN-------KKDDGVKALV 77
Cdd:PRK11192    2 TFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAF---LLPALQhlldfprRKSGPPRILI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  78 LSPTRELALQIDEELRRIGKYTSLSIVSVFGGSEIEKQIRSLKKGADIVVGTPGRVLDLMrrKALKLDC--VEWLVLDEA 155
Cdd:PRK11192   79 LTPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYI--KEENFDCraVETLILDEA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 156 DEMLNMGFIDDIETILQTVPEDRHTVLFSATMPSD-IKKIASFYMhEDYQHIQIKAKTMTASTVSQ-YYFETKVNRRFEV 233
Cdd:PRK11192  157 DRMLDMGFAQDIETIAAETRWRKQTLLFSATLEGDaVQDFAERLL-NDPVEVEAEPSRRERKKIHQwYYRADDLEHKTAL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 234 LCRILDSREMDNAIIFCKTKRSVDEVVAAMQQKHYNVEAMHGDLSQNQRMNTLRRFKTGQIQYLVATDVAARGIDVDNIS 313
Cdd:PRK11192  236 LCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVS 315
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1198450891 314 HVINYELPQDEELYIHRIGRTGRANKKGEAYSIVTSRERNFLKAIEKHT 362
Cdd:PRK11192  316 HVINFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERYI 364
PTZ00424 PTZ00424
helicase 45; Provisional
5-369 1.65e-95

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 295.58  E-value: 1.65e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891   5 TFYDLGLSKLVLQGIEMMGYVIPSPIQEKAIPVLLEGKDIIGQAQTGTGKTLAFGSVLLSCINKKDDGVKALVLSPTREL 84
Cdd:PTZ00424   29 SFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILAPTREL 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  85 ALQIDEELRRIGKYTSLSIVSVFGGSEIEKQIRSLKKGADIVVGTPGRVLDLMRRKALKLDCVEWLVLDEADEMLNMGFI 164
Cdd:PTZ00424  109 AQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRGFK 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 165 DDIETILQTVPEDRHTVLFSATMPSDIKKIASFYMhEDYQHIQIKAKTMTASTVSQYYFET-KVNRRFEVLCRILDSREM 243
Cdd:PTZ00424  189 GQIYDVFKKLPPDVQVALFSATMPNEILELTTKFM-RDPKRILVKKDELTLEGIRQFYVAVeKEEWKFDTLCDLYETLTI 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 244 DNAIIFCKTKRSVDEVVAAMQQKHYNVEAMHGDLSQNQRMNTLRRFKTGQIQYLVATDVAARGIDVDNISHVINYELPQD 323
Cdd:PTZ00424  268 TQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPAS 347
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1198450891 324 EELYIHRIGRTGRANKKGEAYSIVTSRERNFLKAIEKHTHSHIEKL 369
Cdd:PTZ00424  348 PENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIEEM 393
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
6-366 5.43e-93

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 289.95  E-value: 5.43e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891   6 FYDLGLSKLVLQGIEMMGYVIPSPIQEKAIPVLLEGKDIIGQAQTGTGKTLAFgsvLLSCIN----------KKDDGVKA 75
Cdd:PRK04837   10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAF---LTATFHyllshpapedRKVNQPRA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  76 LVLSPTRELALQIDEELRRIGKYTSLSIVSVFGGSEIEKQIRSLKKGADIVVGTPGRVLDLMRRKALKLDCVEWLVLDEA 155
Cdd:PRK04837   87 LIMAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEA 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 156 DEMLNMGFIDDIETILQTVPE--DRHTVLFSATMPSDIKKIASFYMHeDYQHIQIKAKTMTASTVSQYYFETKVNRRFEV 233
Cdd:PRK04837  167 DRMFDLGFIKDIRWLFRRMPPanQRLNMLFSATLSYRVRELAFEHMN-NPEYVEVEPEQKTGHRIKEELFYPSNEEKMRL 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 234 LCRILDSREMDNAIIFCKTKRSVDEVVAAMQQKHYNVEAMHGDLSQNQRMNTLRRFKTGQIQYLVATDVAARGIDVDNIS 313
Cdd:PRK04837  246 LQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVT 325
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1198450891 314 HVINYELPQDEELYIHRIGRTGRANKKGEAYSIVTSRERNFLKAIEKHTHSHI 366
Cdd:PRK04837  326 HVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEEYALNLPAIETYIGHSI 378
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
6-360 3.28e-89

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 281.80  E-value: 3.28e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891   6 FYDLGLSKLVLQGIEMMGYVIPSPIQEKAIPVLLEGKDIIGQAQTGTGKTLAFgsvLLSCINKKDDG----------VKA 75
Cdd:PRK01297   89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAF---LISIINQLLQTpppkerymgePRA 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  76 LVLSPTRELALQIDEELRRIGKYTSLSIVSVFGGSEIEKQIRSLK-KGADIVVGTPGRVLDLMRRKALKLDCVEWLVLDE 154
Cdd:PRK01297  166 LIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEaRFCDILVATPGRLLDFNQRGEVHLDMVEVMVLDE 245
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 155 ADEMLNMGFIDDIETILQTVP--EDRHTVLFSATMPSDIKKIASFYMhEDYQHIQIKAKTMTASTVSQYYFETKVNRRFE 232
Cdd:PRK01297  246 ADRMLDMGFIPQVRQIIRQTPrkEERQTLLFSATFTDDVMNLAKQWT-TDPAIVEIEPENVASDTVEQHVYAVAGSDKYK 324
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 233 VLCRILDSREMDNAIIFCKTKRSVDEVVAAMQQKHYNVEAMHGDLSQNQRMNTLRRFKTGQIQYLVATDVAARGIDVDNI 312
Cdd:PRK01297  325 LLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGI 404
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1198450891 313 SHVINYELPQDEELYIHRIGRTGRANKKGEAYSIVTSRERNFLKAIEK 360
Cdd:PRK01297  405 SHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEE 452
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
1-386 6.06e-89

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 284.15  E-value: 6.06e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891   1 MQQVTFYDLGLSKLVLQGIEMMGYVIPSPIQEKAIPVLLEGKDIIGQAQTGTGKTLAFGSV----LLS---CINKKDDGV 73
Cdd:PRK04537    6 LTDLTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAvmnrLLSrpaLADRKPEDP 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  74 KALVLSPTRELALQIDEELRRIGKYTSLSIVSVFGGSEIEKQIRSLKKGADIVVGTPGRVLDLMRR-KALKLDCVEWLVL 152
Cdd:PRK04537   86 RALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQhKVVSLHACEICVL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 153 DEADEMLNMGFIDDIETILQTVPE--DRHTVLFSATMPSDIKKIASFYMHEDyQHIQIKAKTMTASTVSQYYFETKVNRR 230
Cdd:PRK04537  166 DEADRMFDLGFIKDIRFLLRRMPErgTRQTLLFSATLSHRVLELAYEHMNEP-EKLVVETETITAARVRQRIYFPADEEK 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 231 FEVLCRILDSREMDNAIIFCKTKRSVDEVVAAMQQKHYNVEAMHGDLSQNQRMNTLRRFKTGQIQYLVATDVAARGIDVD 310
Cdd:PRK04537  245 QTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHID 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 311 NISHVINYELPQDEELYIHRIGRTGRANKKGEAYSIvtsrernflkAIEKHTHShiekldIPAIEDIFDQKV------KE 384
Cdd:PRK04537  325 GVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISF----------ACERYAMS------LPDIEAYIEQKIpvepvtAE 388

                  ..
gi 1198450891 385 LL 386
Cdd:PRK04537  389 LL 390
PTZ00110 PTZ00110
helicase; Provisional
4-349 5.98e-84

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 270.11  E-value: 5.98e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891   4 VTFYDLGLSKLVLQGIEMMGYVIPSPIQEKAIPVLLEGKDIIGQAQTGTGKTLAFGSVLLSCIN-----KKDDGVKALVL 78
Cdd:PTZ00110  130 VSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINaqpllRYGDGPIVLVL 209
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  79 SPTRELALQIDEELRRIGKYTSLSIVSVFGGSEIEKQIRSLKKGADIVVGTPGRVLDLMRRKALKLDCVEWLVLDEADEM 158
Cdd:PTZ00110  210 APTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRM 289
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 159 LNMGFIDDIETILQTVPEDRHTVLFSATMPSDIKKIASFYMHEDYQHIQIKAKTMTAS-TVSQYYF-----ETKVNRRfE 232
Cdd:PTZ00110  290 LDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEEPVHVNVGSLDLTAChNIKQEVFvveehEKRGKLK-M 368
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 233 VLCRILdsREMDNAIIFCKTKRSVDEVVAAMQQKHYNVEAMHGDLSQNQRMNTLRRFKTGQIQYLVATDVAARGIDVDNI 312
Cdd:PTZ00110  369 LLQRIM--RDGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDV 446
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1198450891 313 SHVINYELPQDEELYIHRIGRTGRANKKGEAYSIVTS 349
Cdd:PTZ00110  447 KYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTP 483
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
5-203 5.04e-68

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: 218.13  E-value: 5.04e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891   5 TFYDLGLSKLVLQGIEMMGYVIPSPIQEKAIPVLLEGKDIIGQAQTGTGKTLAFgsvLLSCINK--KDDGV--------- 73
Cdd:cd17967     1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAF---LLPIISKllEDGPPsvgrgrrka 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  74 --KALVLSPTRELALQIDEELRRIGKYTSLSIVSVFGGSEIEKQIRSLKKGADIVVGTPGRVLDLMRRKALKLDCVEWLV 151
Cdd:cd17967    78 ypSALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLV 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1198450891 152 LDEADEMLNMGFIDDIETILQ----TVPEDRHTVLFSATMPSDIKKIASFYMHeDY 203
Cdd:cd17967   158 LDEADRMLDMGFEPQIRKIVEhpdmPPKGERQTLMFSATFPREIQRLAADFLK-NY 212
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
5-189 3.97e-65

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: 209.85  E-value: 3.97e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891   5 TFYDLGLSKLVLQGIEMMGYVIPSPIQEKAIPVLLEGKDIIGQAQTGTGKTLAFgsvLLSCINK-----KDDGVKALVLS 79
Cdd:cd17959     2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAF---LIPMIEKlkahsPTVGARALILS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  80 PTRELALQIDEELRRIGKYTSLSIVSVFGGSEIEKQIRSLKKGADIVVGTPGRVLDLMRRKALKLDCVEWLVLDEADEML 159
Cdd:cd17959    79 PTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLF 158
                         170       180       190
                  ....*....|....*....|....*....|
gi 1198450891 160 NMGFIDDIETILQTVPEDRHTVLFSATMPS 189
Cdd:cd17959   159 EMGFAEQLHEILSRLPENRQTLLFSATLPK 188
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
28-194 6.02e-64

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: 205.55  E-value: 6.02e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  28 SPIQEKAIPVLLEGKDIIGQAQTGTGKTLAFGSVLLSCINKKDDGVKALVLSPTRELALQIDEELRRIGKYTSLSIVSVF 107
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 108 GGSEIEKQIRSLkKGADIVVGTPGRVLDLMRRKAlKLDCVEWLVLDEADEMLNMGFIDDIETILQTVPEDRHTVLFSATM 187
Cdd:pfam00270  81 GGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSATL 158

                  ....*..
gi 1198450891 188 PSDIKKI 194
Cdd:pfam00270 159 PRNLEDL 165
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
15-199 7.33e-62

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: 202.16  E-value: 7.33e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  15 VLQGIEMMGYVIPSPIQEKAIPVLLEGKDIIGQAQTGTGKTLAFGSVLLSCIN--------KKDDGVKALVLSPTRELAL 86
Cdd:cd17945     1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISrlppldeeTKDDGPYALILAPTRELAQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  87 QIDEELRRIGKYTSLSIVSVFGGSEIEKQIRSLKKGADIVVGTPGRVLDLMRRKALKLDCVEWLVLDEADEMLNMGFIDD 166
Cdd:cd17945    81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1198450891 167 IETILQTVPED--------------------RHTVLFSATMPSDIKKIASFYM 199
Cdd:cd17945   161 VTKILDAMPVSnkkpdteeaeklaasgkhryRQTMMFTATMPPAVEKIAKGYL 213
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
6-204 1.40e-61

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: 200.60  E-value: 1.40e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891   6 FYDLGLSKLVLQGIEMMGYVIPSPIQEKAIPVLLEGKDIIGQAQTGTGKTLAFGSVLLSCINKKDDGVKALVLSPTRELA 85
Cdd:cd17940     1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  86 LQIDEELRRIGKYTSLSIVSVFGGSEIEKQIRSLKKGADIVVGTPGRVLDLMRRKALKLDCVEWLVLDEADEMLNMGFID 165
Cdd:cd17940    81 LQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQP 160
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1198450891 166 DIETILQTVPEDRHTVLFSATMPSDIKKIASFYMHEDYQ 204
Cdd:cd17940   161 IIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYE 199
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
5-194 3.59e-61

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: 199.47  E-value: 3.59e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891   5 TFYDLGLSKLVLQGIEMMGYVIPSPIQEKAIPVLLEGKDIIGQAQTGTGKTLAFGSVLLSCINKKDDGVKALVLSPTREL 84
Cdd:cd17954     1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQRFFALVLAPTREL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  85 ALQIDEELRRIGKYTSLSIVSVFGGSEIEKQIRSLKKGADIVVGTPGRVLD-LMRRKALKLDCVEWLVLDEADEMLNMGF 163
Cdd:cd17954    81 AQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDhLENTKGFSLKSLKFLVMDEADRLLNMDF 160
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1198450891 164 IDDIETILQTVPEDRHTVLFSATMPSDIKKI 194
Cdd:cd17954   161 EPEIDKILKVIPRERTTYLFSATMTTKVAKL 191
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
11-207 1.76e-60

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: 198.19  E-value: 1.76e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  11 LSKLVLQGIEMMGYVIPSPIQEKAIPVLLE-GKDIIGQAQTGTGKTLAFgsvLLSCINK--------KDDGVKALVLSPT 81
Cdd:cd17964     1 LDPSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAF---LLPAIQSllntkpagRRSGVSALIISPT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  82 RELALQIDEELRRIGKY-TSLSIVSVFGGSEIEKQIRSLKK-GADIVVGTPGRVLDLMR--RKALKLDCVEWLVLDEADE 157
Cdd:cd17964    78 RELALQIAAEAKKLLQGlRKLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLEnpGVAKAFTDLDYLVLDEADR 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1198450891 158 MLNMGFIDDIETILQTVP----EDRHTVLFSATMPSDIKKIASFYMHEDYQHIQ 207
Cdd:cd17964   158 LLDMGFRPDLEQILRHLPeknaDPRQTLLFSATVPDEVQQIARLTLKKDYKFID 211
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
5-195 2.65e-60

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: 197.98  E-value: 2.65e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891   5 TFYDLGLSKLVLQGIEMMGYVIPSPIQEKAIPVLLEGKDIIGQAQTGTGKTLAFGSVLLSCIN-----KKDDGVKALVLS 79
Cdd:cd17953    13 KWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKdqrpvKPGEGPIGLIMA 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  80 PTRELALQIDEELRRIGKYTSLSIVSVFGGSEIEKQIRSLKKGADIVVGTPGRVLDLM---RRKALKLDCVEWLVLDEAD 156
Cdd:cd17953    93 PTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtanNGRVTNLRRVTYVVLDEAD 172
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1198450891 157 EMLNMGFIDDIETILQTVPEDRHTVLFSATMPSDIKKIA 195
Cdd:cd17953   173 RMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALA 211
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
8-199 4.65e-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: 196.78  E-value: 4.65e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891   8 DLGLSKLVLQGIEMMGYVIPSPIQEKAIPVLLEGKDIIGQAQTGTGKTLAFGSVLLSCINKKDDGVKALVLSPTRELALQ 87
Cdd:cd17939     1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  88 IDEELRRIGKYTSLSIVSVFGGSEIEKQIRSLKKGADIVVGTPGRVLDLMRRKALKLDCVEWLVLDEADEMLNMGFIDDI 167
Cdd:cd17939    81 IQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQI 160
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1198450891 168 ETILQTVPEDRHTVLFSATMPSDIKKIASFYM 199
Cdd:cd17939   161 YDIFQFLPPETQVVLFSATMPHEVLEVTKKFM 192
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
15-200 6.04e-60

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: 196.32  E-value: 6.04e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  15 VLQGIEMMGYVIPSPIQEKAIPVLLEGKDIIGQAQTGTGKTLAFGSVLLSCI---NKKDDGVKALVLSPTRELALQIDEE 91
Cdd:cd17947     1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLlyrPKKKAATRVLVLVPTRELAMQCFSV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  92 LRRIGKYTSLSIVSVFGGSEIEKQIRSLKKGADIVVGTPGRVLDLMRR-KALKLDCVEWLVLDEADEMLNMGFIDDIETI 170
Cdd:cd17947    81 LQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNsPSFDLDSIEILVLDEADRMLEEGFADELKEI 160
                         170       180       190
                  ....*....|....*....|....*....|
gi 1198450891 171 LQTVPEDRHTVLFSATMPSDIKKIASFYMH 200
Cdd:cd17947   161 LRLCPRTRQTMLFSATMTDEVKDLAKLSLN 190
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
6-201 9.80e-57

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: 188.20  E-value: 9.80e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891   6 FYDLGLSKLVLQGIEMMGYVIPSPIQEKAIPVLLEGKDIIGQAQTGTGKTLAFGSVLLSCINKKDDGVKALVLSPTRELA 85
Cdd:cd17955     1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYGIFALVLTPTRELA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  86 LQIDEELRRIGKYTSLSIVSVFGGSEIEKQIRSLKKGADIVVGTPGRVLDLMR-----RKALKLdcVEWLVLDEADEMLN 160
Cdd:cd17955    81 YQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssddtTKVLSR--VKFLVLDEADRLLT 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1198450891 161 MGFIDDIETILQTVPEDRHTVLFSATMPSDIKKIASFYMHE 201
Cdd:cd17955   159 GSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNK 199
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
4-356 4.15e-56

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 195.78  E-value: 4.15e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891   4 VTFYDLGLSKLVLQGIEMMGYVIPSPIQEKAIPVLLEGKDIIGQAQTGTGKTLAF-GSVLLSCINKKDDGVK------AL 76
Cdd:PLN00206  121 LSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFlVPIISRCCTIRSGHPSeqrnplAM 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  77 VLSPTRELALQIDEELRRIGKYTSLSIVSVFGGSEIEKQIRSLKKGADIVVGTPGRVLDLMRRKALKLDCVEWLVLDEAD 156
Cdd:PLN00206  201 VLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVD 280
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 157 EMLNMGFIDDIETILQTVPEDRhTVLFSATMPSDIKKIASfYMHEDYQHIQIKAKTMTASTVSQY--YFETKvnRRFEVL 234
Cdd:PLN00206  281 CMLERGFRDQVMQIFQALSQPQ-VLLFSATVSPEVEKFAS-SLAKDIILISIGNPNRPNKAVKQLaiWVETK--QKKQKL 356
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 235 CRILDSRE--MDNAIIFCKTKRSVDEVVAAMQQ-KHYNVEAMHGDLSQNQRMNTLRRFKTGQIQYLVATDVAARGIDVDN 311
Cdd:PLN00206  357 FDILKSKQhfKPPAVVFVSSRLGADLLANAITVvTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLR 436
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1198450891 312 ISHVINYELPQDEELYIHRIGRTGRANKKGEAYSIVTSRERNFLK 356
Cdd:PLN00206  437 VRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFP 481
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
5-203 4.53e-56

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: 188.25  E-value: 4.53e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891   5 TFYDLGLSKLVLQGIEMMGYVIPSPIQEKAIPVLLEGKDIIGQAQTGTGKTLAFgsvLLSCINKK-DDGVK--------- 74
Cdd:cd18052    44 TFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAF---LLPVLTGMmKEGLTassfsevqe 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  75 --ALVLSPTRELALQIDEELRRIGKYTSLSIVSVFGGSEIEKQIRSLKKGADIVVGTPGRVLDLMRRKALKLDCVEWLVL 152
Cdd:cd18052   121 pqALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLIL 200
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1198450891 153 DEADEMLNMGFIDDIETILQT--VP--EDRHTVLFSATMPSDIKKIASFYMHEDY 203
Cdd:cd18052   201 DEADRMLDMGFGPEIRKLVSEpgMPskEDRQTLMFSATFPEEIQRLAAEFLKEDY 255
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
218-347 6.89e-56

C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 183.09  E-value: 6.89e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 218 VSQYYFETKVNRRFEVL-CRILDSREMDNAIIFCKTKRSVDEVVAAMQQKHYNVEAMHGDLSQNQRMNTLRRFKTGQIQY 296
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLlLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1198450891 297 LVATDVAARGIDVDNISHVINYELPQDEELYIHRIGRTGRANKKGEAYSIV 347
Cdd:cd18787    81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
15-195 4.27e-55

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: 183.55  E-value: 4.27e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  15 VLQGIEMMGYVIPSPIQEKAIPVLLEGKDIIGQAQTGTGKTLAFGSVLLSCI-----NKKDDGVKALVLSPTRELALQID 89
Cdd:cd17960     1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILlkrkaNLKKGQVGALIISPTRELATQIY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  90 EELRRIGKYTSLSIVSVF--GGSEIEKQIRSLK-KGADIVVGTPGRVLDLMRRKALKLD--CVEWLVLDEADEMLNMGFI 164
Cdd:cd17960    81 EVLQSFLEHHLPKLKCQLliGGTNVEEDVKKFKrNGPNILVGTPGRLEELLSRKADKVKvkSLEVLVLDEADRLLDLGFE 160
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1198450891 165 DDIETILQTVPEDRHTVLFSATMPSDIKKIA 195
Cdd:cd17960   161 ADLNRILSKLPKQRRTGLFSATQTDAVEELI 191
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
6-201 1.44e-54

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: 182.26  E-value: 1.44e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891   6 FYDLGLSKLVLQGIEMMGYVIPSPIQEKAIPVLLEGKDIIGQAQTGTGKTLAFGSVLLSCINKKDDGVKALVLSPTRELA 85
Cdd:cd18046     1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  86 LQIDEELRRIGKYTSLSIVSVFGGSEIEKQIRSLKKGADIVVGTPGRVLDLMRRKALKLDCVEWLVLDEADEMLNMGFID 165
Cdd:cd18046    81 QQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFKD 160
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1198450891 166 DIETILQTVPEDRHTVLFSATMPSDIKKIASFYMHE 201
Cdd:cd18046   161 QIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRD 196
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
15-207 2.05e-54

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: 181.80  E-value: 2.05e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  15 VLQGIEMMGYVIPSPIQEKAIPVLLEGKDIIGQAQTGTGKTLAFGSVLLSCIN-----KKDDGVKALVLSPTRELALQID 89
Cdd:cd17966     1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINaqpplERGDGPIVLVLAPTRELAQQIQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  90 EELRRIGKYTSLSIVSVFGGSEIEKQIRSLKKGADIVVGTPGRVLDLMRRKALKLDCVEWLVLDEADEMLNMGFIDDIET 169
Cdd:cd17966    81 QEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRK 160
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1198450891 170 ILQTVPEDRHTVLFSATMPSDIKKIASFYMhEDYQHIQ 207
Cdd:cd17966   161 IVDQIRPDRQTLMWSATWPKEVRRLAEDFL-KDYIQVN 197
DEXDc smart00487
DEAD-like helicases superfamily;
19-221 1.35e-52

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 177.30  E-value: 1.35e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891   19 IEMMGYVIPSPIQEKAIPVLLEG-KDIIGQAQTGTGKTLAFGSVLLSCInKKDDGVKALVLSPTRELALQIDEELRRIGK 97
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEAL-KRGKGGRVLVLVPTRELAEQWAEELKKLGP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891   98 YTSLSIVSVFGGSEIEKQIRSLKKG-ADIVVGTPGRVLDLMRRKALKLDCVEWLVLDEADEMLNMGFIDDIETILQTVPE 176
Cdd:smart00487  80 SLGLKVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPK 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1198450891  177 DRHTVLFSATMPSDIKKIASFYMHEDyqhIQIKAKTMTASTVSQY 221
Cdd:smart00487 160 NVQLLLLSATPPEEIENLLELFLNDP---VFIDVGFTPLEPIEQF 201
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
15-187 2.85e-52

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: 177.43  E-value: 2.85e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  15 VLQGIEMMGYVIPSPIQEKAIPV-LLEGKDIIGQAQTGTGKTLAFG-SVLLSCINKKDD--------GVKALVLSPTREL 84
Cdd:cd17946     1 ILRALADLGFSEPTPIQALALPAaIRDGKDVIGAAETGSGKTLAFGiPILERLLSQKSSngvggkqkPLRALILTPTREL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  85 ALQIDEELRRIGKYTSLSIVSVFGGSEIEKQIRSLKKGADIVVGTPGRVLDLMRRK---ALKLDCVEWLVLDEADEMLNM 161
Cdd:cd17946    81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGnehLANLKSLRFLVLDEADRMLEK 160
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1198450891 162 GFIDDIETILQTVPED-------RHTVLFSATM 187
Cdd:cd17946   161 GHFAELEKILELLNKDragkkrkRQTFVFSATL 193
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
16-201 3.81e-52

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: 175.94  E-value: 3.81e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  16 LQGIEMMGYVIPSPIQEKAIPVLLEGKDIIGQAQTGTGKTLAFGSVLLSCINKK----DDGVKALVLSPTRELALQIDEE 91
Cdd:cd17941     2 LKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRErwtpEDGLGALIISPTRELAMQIFEV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  92 LRRIGKYTSLSIVSVFGGSEIEKQiRSLKKGADIVVGTPGRVLDLMRRKALkLDC--VEWLVLDEADEMLNMGFIDDIET 169
Cdd:cd17941    82 LRKVGKYHSFSAGLIIGGKDVKEE-KERINRMNILVCTPGRLLQHMDETPG-FDTsnLQMLVLDEADRILDMGFKETLDA 159
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1198450891 170 ILQTVPEDRHTVLFSATMPSDIKKIASFYMHE 201
Cdd:cd17941   160 IVENLPKSRQTLLFSATQTKSVKDLARLSLKN 191
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
5-201 4.45e-52

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: 177.54  E-value: 4.45e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891   5 TFYDLGLSKLVLQGIEMMGYVIPSPIQEKAIPVLLEGKDIIGQAQTGTGKTLAFGSVLLSCINKKDDGVK---------- 74
Cdd:cd18051    22 TFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEQGPGESlpsesgyygr 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  75 ------ALVLSPTRELALQIDEELRrigKYTSLSIVS---VFGGSEIEKQIRSLKKGADIVVGTPGRVLDLMRRKALKLD 145
Cdd:cd18051   102 rkqyplALVLAPTRELASQIYDEAR---KFAYRSRVRpcvVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLD 178
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 146 CVEWLVLDEADEMLNMGFIDDIETILQ--TVPE--DRHTVLFSATMPSDIKKIASFYMHE 201
Cdd:cd18051   179 YCKYLVLDEADRMLDMGFEPQIRRIVEqdTMPPtgERQTLMFSATFPKEIQMLARDFLDN 238
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
11-195 6.42e-52

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: 175.07  E-value: 6.42e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  11 LSKLVLQGIEMMGYVIPSPIQEKAIPVLLEG--KDIIGQAQTGTGKTLAFGSVLLSCINKKDDGVKALVLSPTRELALQI 88
Cdd:cd17963     1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  89 DEELRRIGKYTSLSIVSVFGGSEIEkqiRSLKKGADIVVGTPGRVLDLMRRKALKLDCVEWLVLDEADEMLNM-GFIDDI 167
Cdd:cd17963    81 GEVVEKMGKFTGVKVALAVPGNDVP---RGKKITAQIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTqGHGDQS 157
                         170       180
                  ....*....|....*....|....*...
gi 1198450891 168 ETILQTVPEDRHTVLFSATMPSDIKKIA 195
Cdd:cd17963   158 IRIKRMLPRNCQILLFSATFPDSVRKFA 185
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
15-201 6.48e-52

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: 175.35  E-value: 6.48e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  15 VLQGIEMMGYVIPSPIQEKAIPVLLEGKDIIGQAQTGTGKTLAF------GSVLLSCINKKDDGVKALVLSPTRELALQI 88
Cdd:cd17958     1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYllpgfiHLDLQPIPREQRNGPGVLVLTPTRELALQI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  89 DEELRRIgKYTSLSIVSVFGGSEIEKQIRSLKKGADIVVGTPGRVLDLMRRKALKLDCVEWLVLDEADEMLNMGFIDDIE 168
Cdd:cd17958    81 EAECSKY-SYKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIR 159
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1198450891 169 TILQTVPEDRHTVLFSATMPSDIKKIASFYMHE 201
Cdd:cd17958   160 KILLDIRPDRQTIMTSATWPDGVRRLAQSYLKD 192
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
15-196 7.29e-52

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: 174.91  E-value: 7.29e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  15 VLQGIEMMGYVIPSPIQEKAIPVLLEGKDIIGQAQTGTGKTLAFGSVLLSCIN-----KKDDGVKALVLSPTRELALQID 89
Cdd:cd17952     1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMdqrelEKGEGPIAVIVAPTRELAQQIY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  90 EELRRIGKYTSLSIVSVFGGSEIEKQIRSLKKGADIVVGTPGRVLDLMRRKALKLDCVEWLVLDEADEMLNMGFIDDIET 169
Cdd:cd17952    81 LEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRS 160
                         170       180
                  ....*....|....*....|....*..
gi 1198450891 170 ILQTVPEDRHTVLFSATMPSDIKKIAS 196
Cdd:cd17952   161 IVGHVRPDRQTLLFSATFKKKIEQLAR 187
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
15-201 1.91e-50

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: 171.23  E-value: 1.91e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  15 VLQGIEMMGYVIPSPIQEKAIPVLLEGKDIIGQAQTGTGKTLAFgsvLLSCINK-----KDDGVKALVLSPTRELALQID 89
Cdd:cd17957     1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAF---LIPILQKlgkprKKKGLRALILAPTRELASQIY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  90 EELRRIGKYTSLSIVSVFGGSE-IEKQIRSLKKGADIVVGTPGRVLDLMRRKALKLDCVEWLVLDEADEMLNMGFIDDIE 168
Cdd:cd17957    78 RELLKLSKGTGLRIVLLSKSLEaKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTD 157
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1198450891 169 TILQ--TVPEDRhTVLFSATMPSDIKKIASFYMHE 201
Cdd:cd17957   158 EILAacTNPNLQ-RSLFSATIPSEVEELARSVMKD 191
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
6-201 6.97e-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: 169.96  E-value: 6.97e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891   6 FYDLGLSKLVLQGIEMMGYVIPSPIQEKAIPVLLEGKDIIGQAQTGTGKTLAFGSVLLSCINKKDDGVKALVLSPTRELA 85
Cdd:cd18045     1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  86 LQIDEELRRIGKYTSLSIVSVFGGSEIEKQIRSLKKGADIVVGTPGRVLDLMRRKALKLDCVEWLVLDEADEMLNMGFID 165
Cdd:cd18045    81 VQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFKE 160
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1198450891 166 DIETILQTVPEDRHTVLFSATMPSDIKKIASFYMHE 201
Cdd:cd18045   161 QIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTD 196
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
15-200 4.19e-48

DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of infectious West Nile virus particles. New research suggests that DDX56 relocalizes to the site of virus assembly during WNV infection and that its interaction with WNV capsid in the cytoplasm may occur transiently during virion morphogenesis. DDX56 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350719 [Multi-domain]  Cd Length: 206  Bit Score: 165.45  E-value: 4.19e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  15 VLQGIEMMGYVIPSPIQEKAIPVLLEGKDIIGQAQTGTGKTLAFGSVLLSCI------NKKDDGVKALVLSPTRELALQI 88
Cdd:cd17961     5 LLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKIlkakaeSGEEQGTRALILVPTRELAQQV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  89 DEELRRIGKYTS--LSIVSVFGGSEIEKQIRSLKKGADIVVGTPGRVLDLMRRKALKL-DCVEWLVLDEADEMLNMGFID 165
Cdd:cd17961    85 SKVLEQLTAYCRkdVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLlSTLKYLVIDEADLVLSYGYEE 164
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1198450891 166 DIETILQTVPEDRHTVLFSATMPSDIKKIASFYMH 200
Cdd:cd17961   165 DLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLH 199
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
6-199 8.93e-47

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: 162.13  E-value: 8.93e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891   6 FYDLGLSKLVLQGIEMMGYVIPSPIQEKAIPVLLEGKDIIGQAQTGTGKTLAFGSVLLSCINKKDDGVKALVLSPTRELA 85
Cdd:cd17950     4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTRELA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  86 LQIDEELRRIGKY-TSLSIVSVFGGSEIEKQIRSLK-KGADIVVGTPGRVLDLMRRKALKLDCVEWLVLDEADEM---LN 160
Cdd:cd17950    84 FQISNEYERFSKYmPNVKTAVFFGGVPIKKDIEVLKnKCPHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMleqLD 163
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1198450891 161 MGfiDDIETILQTVPEDRHTVLFSATMPSDIKKIASFYM 199
Cdd:cd17950   164 MR--RDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFM 200
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
14-197 2.12e-46

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: 161.21  E-value: 2.12e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  14 LVLQGIEMMGYVIPSPIQEKAIPVLLEGKDIIGQAQTGTGKTLAFG----SVLLSCINK--KDDGVKALVLSPTRELALQ 87
Cdd:cd17949     1 LVSHLKSKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLlpiiQRLLSLEPRvdRSDGTLALVLVPTRELALQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  88 IDEELRRIGKYTSLsIV--SVFGGSEIEKQIRSLKKGADIVVGTPGRVLD-LMRRKALKLDCVEWLVLDEADEMLNMGFI 164
Cdd:cd17949    81 IYEVLEKLLKPFHW-IVpgYLIGGEKRKSEKARLRKGVNILIATPGRLLDhLKNTQSFDVSNLRWLVLDEADRLLDMGFE 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1198450891 165 DDIETILQTV-------------PEDRHTVLFSATMPSDIKKIASF 197
Cdd:cd17949   160 KDITKILELLddkrskaggekskPSRRQTVLVSATLTDGVKRLAGL 205
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
15-207 8.17e-46

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: 158.97  E-value: 8.17e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  15 VLQGIEMMGYVIPSPIQEKAIPVLLEGKDIIGQAQTGTGKTLAFGSVLLSCINKKDDGVKALVLSPTRELALQIDEELRR 94
Cdd:cd17943     1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVFKK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  95 IGKYTSLSIVSVF-GGSEIEKQIRSLkKGADIVVGTPGRVLDLMRRKALKLDCVEWLVLDEADEMLNMGFIDDIETILQT 173
Cdd:cd17943    81 IGKKLEGLKCEVFiGGTPVKEDKKKL-KGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFSS 159
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1198450891 174 VPEDRHTVLFSATMPSDIKKIASFYMhEDYQHIQ 207
Cdd:cd17943   160 LPKNKQVIAFSATYPKNLDNLLARYM-RKPVLVR 192
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
4-210 2.53e-45

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: 159.02  E-value: 2.53e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891   4 VTFYDLGLSKLVLQGIEMMGYVIPSPIQEKAIPVLLEGKDIIGQAQTGTGKTLAFGSVLLSCIN-----KKDDGVKALVL 78
Cdd:cd18049    24 LNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINhqpflERGDGPICLVL 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  79 SPTRELALQIDEELRRIGKYTSLSIVSVFGGSEIEKQIRSLKKGADIVVGTPGRVLDLMRRKALKLDCVEWLVLDEADEM 158
Cdd:cd18049   104 APTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRM 183
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1198450891 159 LNMGFIDDIETILQTVPEDRHTVLFSATMPSDIKKIASFYMhEDYQHIQIKA 210
Cdd:cd18049   184 LDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFL-KDYIHINIGA 234
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
15-197 2.71e-45

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: 157.89  E-value: 2.71e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  15 VLQGIEMMGYVIPSPIQEKAIPVLLEGKDIIGQAQTGTGKTLAFG-SVLLSCINK-------KDDGVKALVLSPTRELAL 86
Cdd:cd17951     1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTlPLIMFALEQekklpfiKGEGPYGLIVCPSRELAR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  87 QIDEELRRI------GKYTSLSIVSVFGGSEIEKQIRSLKKGADIVVGTPGRVLDLMRRKALKLDCVEWLVLDEADEMLN 160
Cdd:cd17951    81 QTHEVIEYYckalqeGGYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1198450891 161 MGFIDDIETILQTVPEDRHTVLFSATMPsdiKKIASF 197
Cdd:cd17951   161 MGFEEDIRTIFSYFKGQRQTLLFSATMP---KKIQNF 194
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
15-201 4.50e-45

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


Pssm-ID: 350720 [Multi-domain]  Cd Length: 193  Bit Score: 156.94  E-value: 4.50e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  15 VLQGIEMMGYVIPSPIQEKAIPVLLEGKDIIGQAQTGTGKTLAF-GSVLLSCINKKDDGVkALVLSPTRELALQIDEELR 93
Cdd:cd17962     1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFlLPVIIRCLTEHRNPS-ALILTPTRELAVQIEDQAK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  94 RIGK-YTSLSIVSVFGGSEIEKQIRSLKKGADIVVGTPGRVLDLMRRKALKLDCVEWLVLDEADEMLNMGFIDDIETILQ 172
Cdd:cd17962    80 ELMKgLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILE 159
                         170       180
                  ....*....|....*....|....*....
gi 1198450891 173 TVPEDRHTVLFSATMPSDIKKIASFYMHE 201
Cdd:cd17962   160 NISHDHQTILVSATIPRGIEQLAGQLLQN 188
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
6-200 1.28e-42

DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. It possesses 5' single-stranded RNA overhang nuclease activity as well as ATPase activity on various RNA, but not DNA polynucleotides. DDX1 may play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. It may also be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. DDX1 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350696 [Multi-domain]  Cd Length: 204  Bit Score: 150.55  E-value: 1.28e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891   6 FYDLGLSKLVLQGIEMMGYVIPSPIQEKAIPVLLEGKDIIGQAQTGTGKTLAFGSVLLSCinkkddgVKALVLSPTRELA 85
Cdd:cd17938     1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQI-------VVALILEPSRELA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  86 LQIDEELRRIGKY-TSLSIVS--VFGGSEIEKQIRSLKKGADIVVGTPGRVLDLMRRKALKLDCVEWLVLDEADEMLNMG 162
Cdd:cd17938    74 EQTYNCIENFKKYlDNPKLRValLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQG 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1198450891 163 FIDDIETILQTVP-----EDR-HTVLFSATMPS-DIKKIASFYMH 200
Cdd:cd17938   154 NLETINRIYNRIPkitsdGKRlQVIVCSATLHSfEVKKLADKIMH 198
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
16-195 1.32e-41

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: 147.89  E-value: 1.32e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  16 LQGIEMMGYVIPSPIQEKAIPVLLEGKDIIGQAQTGTGKTLAFGSVLLSCINK----KDDGVKALVLSPTRELALQIDEE 91
Cdd:cd17942     2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKlkfkPRNGTGVIIISPTRELALQIYGV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  92 LRRIGKYTSLSIVSVFGGSEIEKQIRSLKKGADIVVGTPGRVLDLMRRKA----LKLDCvewLVLDEADEMLNMGFIDDI 167
Cdd:cd17942    82 AKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKgflyKNLQC---LIIDEADRILEIGFEEEM 158
                         170       180
                  ....*....|....*....|....*...
gi 1198450891 168 ETILQTVPEDRHTVLFSATMPSDIKKIA 195
Cdd:cd17942   159 RQIIKLLPKRRQTMLFSATQTRKVEDLA 186
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
27-208 5.75e-41

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: 148.62  E-value: 5.75e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  27 PSPIQEKAIPVLLEGKDIIGQAQTGTGKTLAFGSVLLSCIN-----KKDDGVKALVLSPTRELALQIDEELRRIGKYTSL 101
Cdd:cd18050    85 PTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINhqpylERGDGPICLVLAPTRELAQQVQQVADDYGKSSRL 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 102 SIVSVFGGSEIEKQIRSLKKGADIVVGTPGRVLDLMRRKALKLDCVEWLVLDEADEMLNMGFIDDIETILQTVPEDRHTV 181
Cdd:cd18050   165 KSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTL 244
                         170       180
                  ....*....|....*....|....*..
gi 1198450891 182 LFSATMPSDIKKIASFYMhEDYQHIQI 208
Cdd:cd18050   245 MWSATWPKEVRQLAEDFL-RDYVQINI 270
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
29-206 6.77e-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: 146.15  E-value: 6.77e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  29 PIQEKAIPVLLEGKDIIGQAQTGTGKTLAFGSVLLSCIN------KKDDGVKALVLSPTRELALQIDEELRRIGKytSLS 102
Cdd:cd17944    15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQedqqprKRGRAPKVLVLAPTRELANQVTKDFKDITR--KLS 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 103 IVSVFGGSEIEKQIRSLKKGADIVVGTPGRVLDLMRRKALKLDCVEWLVLDEADEMLNMGFIDDIETILQTV----PEDR 178
Cdd:cd17944    93 VACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILSVSykkdSEDN 172
                         170       180
                  ....*....|....*....|....*....
gi 1198450891 179 -HTVLFSATMPSDIKKIASFYMHEDYQHI 206
Cdd:cd17944   173 pQTLLFSATCPDWVYNVAKKYMKSQYEQV 201
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
230-338 9.32e-35

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: 126.17  E-value: 9.32e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 230 RFEVLCRILDSREMDNAIIFCKTKRSVDEVVAaMQQKHYNVEAMHGDLSQNQRMNTLRRFKTGQIQYLVATDVAARGIDV 309
Cdd:pfam00271   2 KLEALLELLKKERGGKVLIFSQTKKTLEAELL-LEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDL 80
                          90       100
                  ....*....|....*....|....*....
gi 1198450891 310 DNISHVINYELPQDEELYIHRIGRTGRAN 338
Cdd:pfam00271  81 PDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
15-196 5.73e-30

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: 117.08  E-value: 5.73e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  15 VLQGIEMMGYVIPSPIQEKAIPVLLEGKDIIGQAQTGTGKTLAFgsvLLSCINK----------KDDGVKALVLSPTREL 84
Cdd:cd17948     1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTY---LLPIIQRllrykllaegPFNAPRGLVITPSREL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  85 ALQIDEELRRIGKYTSLSiVSVFGGSEIEKQIRSLKKG-ADIVVGTPGRVLDLMRRKALKLDCVEWLVLDEADEMLNMGF 163
Cdd:cd17948    78 AEQIGSVAQSLTEGLGLK-VKVITGGRTKRQIRNPHFEeVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSF 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1198450891 164 IDDIETILQTVP-----------EDRHT--VLFSATMPSDIKKIAS 196
Cdd:cd17948   157 NEKLSHFLRRFPlasrrsentdgLDPGTqlVLVSATMPSGVGEVLS 202
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
5-186 5.83e-30

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: 117.04  E-value: 5.83e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891   5 TFYDLGLSKLVLQGIEMMGYVIPSPIQEKAIPVLLEG--KDIIGQAQTGTGKTLAFGSVLLSCINKKDDGVKALVLSPTR 82
Cdd:cd18048    19 SFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQCLCLSPTF 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  83 ELALQIDEELRRIGKYTS--LSIVSVFG-----GSEIEKQirslkkgadIVVGTPGRVLD-LMRRKALKLDCVEWLVLDE 154
Cdd:cd18048    99 ELALQTGKVVEEMGKFCVgiQVIYAIRGnrpgkGTDIEAQ---------IVIGTPGTVLDwCFKLRLIDVTNISVFVLDE 169
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1198450891 155 ADEMLNM-GFIDDIETILQTVPEDRHTVLFSAT 186
Cdd:cd18048   170 ADVMINVqGHSDHSVRVKRSMPKECQMLLFSAT 202
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
25-200 6.52e-29

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: 114.27  E-value: 6.52e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  25 VIPSPIQEKAIPVLLEGKDIIGQAQTGTGKTLAFGSVLLSCINKK-DDGVKALVLSPTRELALQIDEELRRIGKYTSLSI 103
Cdd:cd17956    20 VIPWLLPSSKSTPPYRPGDLCVSAPTGSGKTLAYVLPIVQALSKRvVPRLRALIVVPTKELVQQVYKVFESLCKGTGLKV 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 104 VSVFGGSEIEKQIRSLKKG--------ADIVVGTPGRVLD-LMRRKALKLDCVEWLVLDEADEMLNMGFIDDIETILQTV 174
Cdd:cd17956   100 VSLSGQKSFKKEQKLLLVDtsgrylsrVDILVATPGRLVDhLNSTPGFTLKHLRFLVIDEADRLLNQSFQDWLETVMKAL 179
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1198450891 175 PEDR--------------------HTVLFSATMPSDIKKIASFYMH 200
Cdd:cd17956   180 GRPTapdlgsfgdanllersvrplQKLLFSATLTRDPEKLSSLKLH 225
HELICc smart00490
helicase superfamily c-terminal domain;
257-338 2.00e-27

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 104.99  E-value: 2.00e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  257 DEVVAAMQQKHYNVEAMHGDLSQNQRMNTLRRFKTGQIQYLVATDVAARGIDVDNISHVINYELPQDEELYIHRIGRTGR 336
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   ..
gi 1198450891  337 AN 338
Cdd:smart00490  81 AG 82
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
5-195 2.81e-26

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: 105.96  E-value: 2.81e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891   5 TFYDLGLSKLVLQGIEMMGYVIPSPIQEKAIPVLLEG--KDIIGQAQTGTGKTLAFGSVLLSCINKKDDGVKALVLSPTR 82
Cdd:cd18047     2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  83 ELALQIDEELRRIGK-YTSLSIVSVFGGSEIEKQIRSLKKgadIVVGTPGRVLD-LMRRKALKLDCVEWLVLDEADEML- 159
Cdd:cd18047    82 ELALQTGKVIEQMGKfYPELKLAYAVRGNKLERGQKISEQ---IVIGTPGTVLDwCSKLKFIDPKKIKVFVLDEADVMIa 158
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1198450891 160 NMGFIDDIETILQTVPEDRHTVLFSATMPSDIKKIA 195
Cdd:cd18047   159 TQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFA 194
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
22-207 3.15e-23

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: 98.60  E-value: 3.15e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  22 MGYVIPSPIQEKAIPVLL---------EGKDIIGQ-------AQTGTGKTLAFGSVLLSCINK----------------K 69
Cdd:cd17965    26 DEEIKPSPIQTLAIKKLLktlmrkvtkQTSNEEPKlevfllaAETGSGKTLAYLAPLLDYLKRqeqepfeeaeeeyesaK 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  70 DDG-VKALVLSPTRELALQIDEELRRIGKYTSLSIVSV---FGGSEIEKQiRSLKKGADIVVGTPGRVLDLMRRKALKLD 145
Cdd:cd17965   106 DTGrPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFssgFGPSYQRLQ-LAFKGRIDILVTTPGKLASLAKSRPKILS 184
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1198450891 146 CVEWLVLDEADEMLNMGFIDDIETILQTVPEDRHTVLFSATMPSDIKKiasfYMHEDYQHIQ 207
Cdd:cd17965   185 RVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKEFDK----TLRKLFPDVV 242
DbpA pfam03880
DbpA RNA binding domain; This RNA binding domain is found at the C-terminus of a number of ...
445-516 5.53e-19

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: 80.88  E-value: 5.53e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1198450891 445 RIFMTVGSMDKVNVKDIIDFFVRYADIPKREIGDITIKRKFTFVNLSPGAAQKVLDYCYNQKIKGRRVRIEL 516
Cdd:pfam03880   1 RLFINVGKKDGVRPGDIVGALANEAGLPGDDIGKIDIFDNFSFVEVPAEKAEKVLKALKGTKIKGRKVRVEP 72
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
50-487 9.07e-18

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 86.23  E-value: 9.07e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  50 TGTGKTLafgsVLLSCINKKDDGVKALVLSPTRELALQIDEELRRIgkytsLSIVSVFGGSEiekqirslKKGADIVVGT 129
Cdd:COG1061   109 TGTGKTV----LALALAAELLRGKRVLVLVPRRELLEQWAEELRRF-----LGDPLAGGGKK--------DSDAPITVAT 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 130 pgrVLDLMRRKALKLDCVEW--LVLDEADEMLNMGFiddiETILQTVPeDRHTVLFSATmP--SD--------------- 190
Cdd:COG1061   172 ---YQSLARRAHLDELGDRFglVIIDEAHHAGAPSY----RRILEAFP-AAYRLGLTAT-PfrSDgreillflfdgivye 242
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 191 -----------IKKIASFYMHEDYQHIQIKAKTMTASTVSQYYFETKVNRRfeVLCRILDS-REMDNAIIFCKTKRSVDE 258
Cdd:COG1061   243 yslkeaiedgyLAPPEYYGIRVDLTDERAEYDALSERLREALAADAERKDK--ILRELLREhPDDRKTLVFCSSVDHAEA 320
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 259 VVAAMQQKHYNVEAMHGDLSQNQRMNTLRRFKTGQIQYLVATDVAARGIDVDNISHVINYELPQDEELYIHRIGRTGRAN 338
Cdd:COG1061   321 LAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGRGLRPA 400
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 339 KKGEA---YSIVTSRE---RNFLKAIEKHTHSHIEKLDIPA-IEDIFDQKVKELLFDVQEIMLKGNMKPFQKIVKDIPQH 411
Cdd:COG1061   401 PGKEDalvYDFVGNDVpvlEELAKDLRDLAGYRVEFLDEEEsEELALLIAVKPALEVKGELEEELLEELELLEDALLLVL 480
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1198450891 412 MKNDVIAALLAMCYSQRVGYDYQSLNEMNKEEQRIFMTVGSMDKVNVKDIIDFFVRYADIPKREIGDITIKRKFTF 487
Cdd:COG1061   481 AELLLLELLALALELLELAKAEGKAEEEEEEKELLLLLALAKLLKLLLLLLLLLLLELLELLAALLRLEELAALLL 556
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
41-186 4.45e-16

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: 75.13  E-value: 4.45e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  41 GKDIIGQAQTGTGKTLAFGSVLLSCINKKddGVKALVLSPTRELALQIDEELRRIGKYtSLSIVSVFGGSEIEKQIRSLK 120
Cdd:cd00046     1 GENVLITAPTGSGKTLAALLAALLLLLKK--GKKVLVLVPTKALALQTAERLRELFGP-GIRVAVLVGGSSAEEREKNKL 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1198450891 121 KGADIVVGTPGRVLDLMRR-KALKLDCVEWLVLDEADEML-NMGFID-DIETILQTVPEDRHTVLFSAT 186
Cdd:cd00046    78 GDADIIIATPDMLLNLLLReDRLFLKDLKLIIVDEAHALLiDSRGALiLDLAVRKAGLKNAQVILLSAT 146
RRM_DbpA cd12252
RNA recognition motif (RRM) found in the DbpA subfamily of prokaryotic DEAD-box rRNA helicases; ...
445-515 8.64e-16

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: 71.81  E-value: 8.64e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1198450891 445 RIFMTVGSMDKVNVKDIIDFFVRYADIPKREIGDITIKRKFTFVNLSPGAAQKVLDYCYNQKIKGRRVRIE 515
Cdd:cd12252     1 RLFINVGRKDGIDPRDLLGAICRAGGISRDDIGAIRIFDNFSFVEVPEAEAERVIEALNGKKIKGKKLRVE 71
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
230-343 3.54e-14

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 74.79  E-value: 3.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 230 RFEVLCRILDSREMDNAIIFCKTKRSVDEVVAAMQQKHYNVEAMHGDLSQNQRMNTLRRFKTGQIQYLVATdVA-ARGID 308
Cdd:COG0514   217 KLAQLLDFLKEHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGID 295
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1198450891 309 VDNISHVINYELPQDEELYIHRIGRTGRANKKGEA 343
Cdd:COG0514   296 KPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEA 330
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
236-336 3.98e-14

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: 69.16  E-value: 3.98e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 236 RILDSREMDNAIIFCKTKRSVDEVVAAMQQKHYNVEAMHGDLSQNQRMNTLRRFKTGQIQYLVATDVAARGIDVDNISHV 315
Cdd:cd18794    23 RIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFV 102
                          90       100
                  ....*....|....*....|.
gi 1198450891 316 INYELPQDEELYIHRIGRTGR 336
Cdd:cd18794   103 IHYSLPKSMESYYQESGRAGR 123
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
226-340 4.77e-13

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 71.68  E-value: 4.77e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 226 KVNRRFEVLCRILDSREMDNAIIFCKTKRSVDEVVAAMQQKHYNVE------AMHGD--LSQNQRMNTLRRFKTGQIQYL 297
Cdd:COG1111   336 KLSKLREILKEQLGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGrfvgqaSKEGDkgLTQKEQIEILERFRAGEFNVL 415
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1198450891 298 VATDVAARGIDVDNISHVINYELPQDEELYIHRIGRTGRANKK 340
Cdd:COG1111   416 VATSVAEEGLDIPEVDLVIFYEPVPSEIRSIQRKGRTGRKREG 458
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
29-360 4.88e-13

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 71.46  E-value: 4.88e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  29 PIQEKAIP-VLLEGKDIIGQAQTGTGKTLAFGSVLLSCINKkddGVKALVLSPTRELALQIDEELRRigKYTSLSI-VSV 106
Cdd:COG1204    25 PPQAEALEaGLLEGKNLVVSAPTASGKTLIAELAILKALLN---GGKALYIVPLRALASEKYREFKR--DFEELGIkVGV 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 107 FGGsEIEKQIRSLKKgADIVVGTPGRVLDLMRRKAL---KLDCVewlVLDEADemlnmgFIDD----------IETILQT 173
Cdd:COG1204   100 STG-DYDSDDEWLGR-YDILVATPEKLDSLLRNGPSwlrDVDLV---VVDEAH------LIDDesrgptlevlLARLRRL 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 174 VPEDRhTVLFSATMPSdIKKIA-------------------------SFYMHEDYQHIQIKAKTMTASTVSQ-----YYF 223
Cdd:COG1204   169 NPEAQ-IVALSATIGN-AEEIAewldaelvksdwrpvplnegvlydgVLRFDDGSRRSKDPTLALALDLLEEggqvlVFV 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 224 ETKVN-----RRF-EVLCRILDS------REMDNAIIFCKTKRSVDEVVAAMQQK----HynveamHGDLSQNQRMNTLR 287
Cdd:COG1204   247 SSRRDaeslaKKLaDELKRRLTPeereelEELAEELLEVSEETHTNEKLADCLEKgvafH------HAGLPSELRRLVED 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 288 RFKTGQIQYLVATD-------VAARGIDVDNISHVINYELPQDEelYIHRIGRTGRANK--KGEAYsIVTSRERNFLKAI 358
Cdd:COG1204   321 AFREGLIKVLVATPtlaagvnLPARRVIIRDTKRGGMVPIPVLE--FKQMAGRAGRPGYdpYGEAI-LVAKSSDEADELF 397

                  ..
gi 1198450891 359 EK 360
Cdd:COG1204   398 ER 399
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
227-348 8.96e-12

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: 62.61  E-value: 8.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 227 VNRRFEVLCRILDSREMDN----AIIFCKTKRSVDEVVAAMQQ-----KHYNVEAMHG----------DLSQNQRMNTLR 287
Cdd:cd18802     5 VIPKLQKLIEILREYFPKTpdfrGIIFVERRATAVVLSRLLKEhpstlAFIRCGFLIGrgnssqrkrsLMTQRKQKETLD 84
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1198450891 288 RFKTGQIQYLVATDVAARGIDVDNISHVINYELPQDEELYIHrigRTGRANKKGEAYSIVT 348
Cdd:cd18802    85 KFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQ---SRGRARAPNSKYILMV 142
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
29-155 5.95e-09

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: 55.73  E-value: 5.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  29 PIQEKAI-PVLLEGKDIIGQAQTGTGKTLAFGSVLLSCINKKddGVKALVLSPTRELALQIDEELRRIGKYTSLSIVSVF 107
Cdd:cd17921     4 PIQREALrALYLSGDSVLVSAPTSSGKTLIAELAILRALATS--GGKAVYIAPTRALVNQKEADLRERFGPLGKNVGLLT 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1198450891 108 GGSEIEKQirsLKKGADIVVGTPGRvLDLMRRKA--LKLDCVEWLVLDEA 155
Cdd:cd17921    82 GDPSVNKL---LLAEADILVATPEK-LDLLLRNGgeRLIQDVRLVVVDEA 127
PRK13766 PRK13766
Hef nuclease; Provisional
226-384 7.12e-09

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 58.35  E-value: 7.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 226 KVNRRFEVLCRILDSREMDNAIIFCKTKRSVDEVVAAMQQKHYNVEAMHGD--------LSQNQRMNTLRRFKTGQIQYL 297
Cdd:PRK13766  348 KLEKLREIVKEQLGKNPDSRIIVFTQYRDTAEKIVDLLEKEGIKAVRFVGQaskdgdkgMSQKEQIEILDKFRAGEFNVL 427
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 298 VATDVAARGIDVDNISHVINYELPQDEELYIHRIGRTGRANK--------KG---EAYSIVT-SRERNFLKAIEKhTHSH 365
Cdd:PRK13766  428 VSTSVAEEGLDIPSVDLVIFYEPVPSEIRSIQRKGRTGRQEEgrvvvliaKGtrdEAYYWSSrRKEKKMKEELKN-LKGI 506
                         170
                  ....*....|....*....
gi 1198450891 366 IEKLDIPAIEDIFDQKVKE 384
Cdd:PRK13766  507 LNKKLQELDEEQKGEEEEK 525
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
234-343 1.07e-08

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 57.80  E-value: 1.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 234 LCRILDSREMDNAIIFCKTKRSVDEVVAAMQQKHYNVEAMHGDLSQNQRMNTLRRFKTGQIQYLVATDVAARGIDVDNIS 313
Cdd:PRK11057  227 LMRYVQEQRGKSGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVR 306
                          90       100       110
                  ....*....|....*....|....*....|
gi 1198450891 314 HVINYELPQDEELYIHRIGRTGRANKKGEA 343
Cdd:PRK11057  307 FVVHFDIPRNIESYYQETGRAGRDGLPAEA 336
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
226-339 1.41e-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: 53.51  E-value: 1.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 226 KVNRRFEVLCRILDSREMDN---AIIFCKTKRSVDEVVAAMQQKHYNVEAM----HGD------LSQNQRMNTLRRFKTG 292
Cdd:cd18801    10 KLEKLEEIVKEHFKKKQEGSdtrVIIFSEFRDSAEEIVNFLSKIRPGIRATrfigQASgksskgMSQKEQKEVIEQFRKG 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1198450891 293 QIQYLVATDVAARGIDVDNISHVINYELPQDEELYIHRIGRTGRANK 339
Cdd:cd18801    90 GYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGRKRQ 136
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
224-332 3.19e-08

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: 52.48  E-value: 3.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 224 ETKVNRRFEVLCRILDS--REMDNAIIFCKTKRSVDEVVAAMQQKHYNVEAMHGDLSQNQRMNTLRRFKTGQ--IQYLVA 299
Cdd:cd18793     6 EEVVSGKLEALLELLEElrEPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPdiRVFLLS 85
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1198450891 300 TDVAARGIDVDNISHVINYEL---PQDEELYI---HRIG 332
Cdd:cd18793    86 TKAGGVGLNLTAANRVILYDPwwnPAVEEQAIdraHRIG 124
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
31-155 6.21e-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: 52.59  E-value: 6.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  31 QEKAIPVLLEGKDIIGQAQTGTGKTLAFgsvLLSCINK--KDDGVKALVLSPTRELALQIDEELRRIGKYTSLSI-VSVF 107
Cdd:cd17923     5 QAEAIEAARAGRSVVVTTGTASGKSLCY---QLPILEAllRDPGSRALYLYPTKALAQDQLRSLRELLEQLGLGIrVATY 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1198450891 108 GG-SEIEKQIRSLKKGADIVVGTPgRVLD--LMRRKALK---LDCVEWLVLDEA 155
Cdd:cd17923    82 DGdTPREERRAIIRNPPRILLTNP-DMLHyaLLPHHDRWarfLRNLRYVVLDEA 134
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
293-341 1.51e-07

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: 48.85  E-value: 1.51e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1198450891 293 QIQYLVATDVAARGIDVDNISHVINYELPQDEELYIHRIGRTGRANKKG 341
Cdd:cd18785    22 SLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDE 70
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
41-159 1.95e-07

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: 50.66  E-value: 1.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  41 GKDIIGQAQTGTGKTLA-FGSVLLSCINKKDDGVKALVLSPTRELALQIDEELRRIGKYTSLSI-VSVFGG--SEIEKQi 116
Cdd:cd17922     1 GRNVLIAAPTGSGKTEAaFLPALSSLADEPEKGVQVLYISPLKALINDQERRLEEPLDEIDLEIpVAVRHGdtSQSEKA- 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1198450891 117 RSLKKGADIVVGTPGRVLDLMRRKAL--KLDCVEWLVLDEADEML 159
Cdd:cd17922    80 KQLKNPPGILITTPESLELLLVNKKLreLFAGLRYVVVDEIHALL 124
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
31-130 2.81e-07

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: 53.30  E-value: 2.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  31 QEKAIPVLLEGKDIIGQAQTGTGKTLAFGSVLLSCInKKDDGVKALVLSPTRELAL-QIdEELRRIGKYTSLSI-VSVFG 108
Cdd:COG1205    61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEAL-LEDPGATALYLYPTKALARdQL-RRLRELAEALGLGVrVATYD 138
                          90       100
                  ....*....|....*....|....*
gi 1198450891 109 G---SEIEKQIRslkKGADIVVGTP 130
Cdd:COG1205   139 GdtpPEERRWIR---EHPDIVLTNP 160
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
229-347 5.46e-07

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: 49.17  E-value: 5.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 229 RRFEVLCRILDSREM-DNAIIFCKTKRSVDEVvaamqQKHYNVEAMHGDLSQNQRMNTLRRFKTGQIQYLVATDVAARGI 307
Cdd:cd18789    34 NKLRALEELLKRHEQgDKIIVFTDNVEALYRY-----AKRLLKPFITGETPQSEREEILQNFREGEYNTLVVSKVGDEGI 108
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1198450891 308 DVD--NISHVINYELPQDEElYIHRIGRTGRANKKGEA----YSIV 347
Cdd:cd18789   109 DLPeaNVAIQISGHGGSRRQ-EAQRLGRILRPKKGGGKnaffYSLV 153
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
226-334 9.91e-07

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 51.38  E-value: 9.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 226 KVNRRFEVLCRILDSREmdNAIIFCKTKRSVDEVVAAMQQKHYNVEAMHGDLSQNQRMNTLRRFKTGQ--IQYLVATDVA 303
Cdd:COG0553   534 KLEALLELLEELLAEGE--KVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeaPVFLISLKAG 611
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1198450891 304 ARGIDVDNISHVINYEL---PQDEE---LYIHRIGRT 334
Cdd:COG0553   612 GEGLNLTAADHVIHYDLwwnPAVEEqaiDRAHRIGQT 648
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
31-209 1.27e-06

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: 48.66  E-value: 1.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  31 QEKAIPVLLEGKDIIgQAQTGTGKTLAFGSVLLSCINKKDDgvKALVLSPTRELALQIDEELRRIGKyTSLSIVSVFGGS 110
Cdd:cd18035     7 QVLIAAVALNGNTLI-VLPTGLGKTIIAILVAADRLTKKGG--KVLILAPSRPLVEQHAENLKRVLN-IPDKITSLTGEV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 111 EIEKQIRSLKKGAdIVVGTPGRVLDLMRRKALKLDCVEWLVLDEADEMLNMGFIDDIETILQTVPEDRHTVLFSATMPSD 190
Cdd:cd18035    83 KPEERAERWDASK-IIVATPQVIENDLLAGRITLDDVSLLIFDEAHHAVGNYAYVYIAHRYKREANNPLILGLTASPGSD 161
                         170
                  ....*....|....*....
gi 1198450891 191 IKKIASFYMHEDYQHIQIK 209
Cdd:cd18035   162 KEKIMEICENLGIEHIEIK 180
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
50-155 2.13e-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: 48.42  E-value: 2.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  50 TGTGKTLAfgSVLL------SCINKKDDGVKALVLSPTRELALQIDEELRRigkYTSLSIVSVFGGSEIEKQIRSLKKGA 123
Cdd:cd18034    25 TGSGKTLI--AVMLikemgeLNRKEKNPKKRAVFLVPTVPLVAQQAEAIRS---HTDLKVGEYSGEMGVDKWTKERWKEE 99
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1198450891 124 ----DIVVGTPGRVLDLMRRKALKLDCVEWLVLDEA 155
Cdd:cd18034   100 lekyDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
29-154 4.03e-06

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: 47.33  E-value: 4.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  29 PIQEKAI-PVLLEGKDIIGQAQTGTGKTLAfgsVLLSCINKKDDGVKALVLSPTRELAlqiDEELRRIGKYTSLSI-VSV 106
Cdd:cd18028     4 PPQAEAVrAGLLKGENLLISIPTASGKTLI---AEMAMVNTLLEGGKALYLVPLRALA---SEKYEEFKKLEEIGLkVGI 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1198450891 107 FGGSEiEKQIRSLKKgADIVVGTPGRVLDLMRRKALKLDCVEWLVLDE 154
Cdd:cd18028    78 STGDY-DEDDEWLGD-YDIIVATYEKFDSLLRHSPSWLRDVGVVVVDE 123
Cas3 COG1203
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ...
48-310 2.80e-05

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: 46.61  E-value: 2.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  48 AQTGTGKTLAFGSVLLsCINKKDDGVKALVLSPTRELALQIDEELRRI-----GKYTSLSIVSVFGGSEIE----KQIRS 118
Cdd:COG1203   154 APTGGGKTEAALLFAL-RLAAKHGGRRIIYALPFTSIINQTYDRLRDLfgedvLLHHSLADLDLLEEEEEYeseaRWLKL 232
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 119 LKKG--ADIVVGTPGRVLDLM----RRKALKL----DCVewLVLDEAD----EMLNMgfiddIETILQTVPE-DRHTVLF 183
Cdd:COG1203   233 LKELwdAPVVVTTIDQLFESLfsnrKGQERRLhnlaNSV--IILDEVQayppYMLAL-----LLRLLEWLKNlGGSVILM 305
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 184 SATMPSDIKKiasfymhedyQHIQIKAKTMTASTVSQYYFETKVNRRFEVLCRILDSREM-----------DNAIIFCKT 252
Cdd:COG1203   306 TATLPPLLRE----------ELLEAYELIPDEPEELPEYFRAFVRKRVELKEGPLSDEELaelilealhkgKSVLVIVNT 375
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1198450891 253 KRSVDEVVAAMQQKHYNVEAM--HGDLSQNQRMNTLR----RFKTGQIQYLVATDVAARGIDVD 310
Cdd:COG1203   376 VKDAQELYEALKEKLPDEEVYllHSRFCPADRSEIEKeikeRLERGKPCILVSTQVVEAGVDID 439
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
240-312 3.38e-05

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: 43.32  E-value: 3.38e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1198450891 240 SREMDNAIIFCKTKRSVDEVVAAMQQKHYNVEAMHGDLSQNQR-MNTLRRFKTGQI--QYLVATDVAARGIDVDNI 312
Cdd:cd18799     3 KYVEIKTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERgDEALILLFFGELkpPILVTVDLLTTGVDIPEV 78
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
268-360 4.68e-05

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: 43.79  E-value: 4.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 268 YNVEAMHGDLSQNQRMNTLRRFKTGQIQYLVATDVAARGIDVDN-----ISHVINYELPQdeeLYIHRiGRTGRANKKGE 342
Cdd:cd18792    61 ARVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNantmiIEDADRFGLSQ---LHQLR-GRVGRGKHQSY 136
                          90       100
                  ....*....|....*....|....*.
gi 1198450891 343 AYSIV--------TSRERnfLKAIEK 360
Cdd:cd18792   137 CYLLYpdpkklteTAKKR--LRAIAE 160
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
268-339 5.92e-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: 43.49  E-value: 5.92e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1198450891 268 YNVEAMHGDLSQNQRMNTLRRFKTGQIQYLVATDVAARGIDVDN-----ISHVINYELPQdeelyIHRI-GRTGRANK 339
Cdd:cd18811    62 LNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNatvmvIEDAERFGLSQ-----LHQLrGRVGRGDH 134
PRK13767 PRK13767
ATP-dependent helicase; Provisional
28-158 6.83e-05

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 45.65  E-value: 6.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  28 SPIQEKAIPVLLEGKDIIGQAQTGTGKTL-AFGSVL-----LSCINKKDDGVKALVLSPTRELALQID-------EELRR 94
Cdd:PRK13767   34 TPPQRYAIPLIHEGKNVLISSPTGSGKTLaAFLAIIdelfrLGREGELEDKVYCLYVSPLRALNNDIHrnleeplTEIRE 113
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1198450891  95 IGKYTSLSI----VSVFGG--SEIEKQiRSLKKGADIVVGTP---GRVLDLMR-RKalKLDCVEWLVLDEADEM 158
Cdd:PRK13767  114 IAKERGEELpeirVAIRTGdtSSYEKQ-KMLKKPPHILITTPeslAILLNSPKfRE--KLRTVKWVIVDEIHSL 184
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
50-155 7.96e-05

DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 42.68  E-value: 7.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  50 TGTGKTLAfgSVLLSCINKKDdgvKALVLSPTRELALQIdeeLRRIGKYTSLSIVSVFGGSEIEKqirslKKGADIVVGT 129
Cdd:cd17926    27 TGSGKTLT--ALALIAYLKEL---RTLIVVPTDALLDQW---KERFEDFLGDSSIGLIGGGKKKD-----FDDANVVVAT 93
                          90       100
                  ....*....|....*....|....*..
gi 1198450891 130 P-GRVLDLMRRKALKLDCvEWLVLDEA 155
Cdd:cd17926    94 YqSLSNLAEEEKDLFDQF-GLLIVDEA 119
RRM_EcCsdA_like cd12499
RNA recognition motif (RRM) found in Escherichia coli cold-shock DEAD box protein A (CsdA) and ...
450-517 1.15e-04

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


Pssm-ID: 409922 [Multi-domain]  Cd Length: 73  Bit Score: 40.63  E-value: 1.15e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1198450891 450 VGSMDKVNVKDIIDFFVRYADIPKREIGDITIKRKFTFVNLSPGAAQKVLDYCYNQKIKGRRVRIELA 517
Cdd:cd12499     6 VGRKDGVKPGNIVGAIANEAGIDSRFIGRIKIFDDHSTVELPKGMPKDVLQHLKKVRVCGQPLNIKLL 73
DEXHc_RecQ4-like cd18018
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ...
28-155 1.18e-04

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


Pssm-ID: 350776 [Multi-domain]  Cd Length: 201  Bit Score: 43.40  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  28 SPIQEKAIPVLLEGKDIIGQAQTGTGKTLAF--GSVLLScinKKDDGVkALVLSPTreLALQIDEE--LRRIGKYTSLSi 103
Cdd:cd18018    14 RPGQEEAIARLLSGRSTLVVLPTGAGKSLCYqlPALLLR---RRGPGL-TLVVSPL--IALMKDQVdaLPRAIKAAALN- 86
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1198450891 104 vSVFGGSEIEKQIRSLKKG-ADIVVGTPGRVLDLMRRKALKL-DCVEWLVLDEA 155
Cdd:cd18018    87 -SSLTREERRRILEKLRAGeVKILYVSPERLVNESFRELLRQtPPISLLVVDEA 139
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
232-336 1.72e-04

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: 41.87  E-value: 1.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 232 EVLCRILDSRemdNAIIFCKTKRSVDEVVAAMQQKHY------NVEAMHGDLSQNQRMNTLRRFKTGQIQYLVATDVAAR 305
Cdd:cd18796    30 EVIFLLERHK---STLVFTNTRSQAERLAQRLRELCPdrvppdFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLEL 106
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1198450891 306 GIDVDNISHVINYELPQDEELYIHRIGRTGR 336
Cdd:cd18796   107 GIDIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
SF2_C_TRCF cd18810
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ...
274-360 3.04e-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: 41.18  E-value: 3.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 274 HGDLSQNQRMNTLRRFKTGQIQYLVATDVAARGIDVDNISHVI-----NYELPQdeeLYIHRiGRTGRANKKGEAYSIV- 347
Cdd:cd18810    58 HGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIieradKFGLAQ---LYQLR-GRVGRSKERAYAYFLYp 133
                          90
                  ....*....|....*...
gi 1198450891 348 -----TSRERNFLKAIEK 360
Cdd:cd18810   134 dqkklTEDALKRLEAIQE 151
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
27-154 7.33e-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: 40.48  E-value: 7.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  27 PSPIQEKAIpvllegKDIIG------------QAQTGTGKTLAFgsvLLSCINKKDDGVKALVLSPTRELALQIDEELRR 94
Cdd:cd17918    16 LTKDQAQAI------KDIEKdlhspepmdrllSGDVGSGKTLVA---LGAALLAYKNGKQVAILVPTEILAHQHYEEARK 86
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  95 igKYTSLSIVSVFGGSEiekqiRSLKKGADIVVGTPGrvldLMRRKALKLDcVEWLVLDE 154
Cdd:cd17918    87 --FLPFINVELVTGGTK-----AQILSGISLLVGTHA----LLHLDVKFKN-LDLVIVDE 134
RRM_BsYxiN_like cd12500
RNA recognition motif (RRM) found in Bacillus subtilis ATP-dependent RNA helicase YxiN and ...
445-517 1.09e-03

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: 37.82  E-value: 1.09e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1198450891 445 RIFMTVGSMDKVNVKDIIDFFVRYADIPKREIGDITIKRKFTFVNLSPGAAQKVLDYCYNQKIKGRRVRIELA 517
Cdd:cd12500     1 KLYFNGGKKKKIRAVDIVGAISNIDGVTGDDIGIITVQDNCSYVDILNGKGDHVLKVMKNTTIKGKQVKVNKA 73
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
20-155 1.12e-03

DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.


Pssm-ID: 350678 [Multi-domain]  Cd Length: 200  Bit Score: 40.21  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  20 EMMGYVIPSPIQEKAIPVLLEGKDIIGQAQTGTGKTLAF---GSVLlscinkkdDGVkALVLSPTreLALQID--EELRR 94
Cdd:cd17920     6 EVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYqlpALLL--------DGV-TLVVSPL--ISLMQDqvDRLQQ 74
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  95 IG-KYTSLSivSVFGGSEIEKQIRSLKKG-ADIVVGTP-----GRVLDLMRRK--ALKLDCVewlVLDEA 155
Cdd:cd17920    75 LGiRAAALN--STLSPEEKREVLLRIKNGqYKLLYVTPerllsPDFLELLQRLpeRKRLALI---VVDEA 139
DinG COG1199
Rad3-related DNA helicase DinG [Replication, recombination and repair];
19-103 1.35e-03

Rad3-related DNA helicase DinG [Replication, recombination and repair];


Pssm-ID: 440812 [Multi-domain]  Cd Length: 629  Bit Score: 41.45  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  19 IEMMGYVipspiqEKAIpvlLEGKDIIGQAQTGTGKTLA--FGSVLLSCINKKddgvKALVLSPTRelALQ---IDEELR 93
Cdd:COG1199    20 REMAEAV------ARAL---AEGRHLLIEAGTGTGKTLAylVPALLAARETGK----KVVISTATK--ALQeqlVEKDLP 84
                          90
                  ....*....|
gi 1198450891  94 RIGKYTSLSI 103
Cdd:COG1199    85 LLRKALGLPL 94
PLN03137 PLN03137
ATP-dependent DNA helicase; Q4-like; Provisional
247-336 1.44e-03

ATP-dependent DNA helicase; Q4-like; Provisional


Pssm-ID: 215597 [Multi-domain]  Cd Length: 1195  Bit Score: 41.42  E-value: 1.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  247 IIFCKTKRSVDEVVAAMQQKHYNVEAMHGDLSQNQRMNTLRRFKTGQIQYLVATDVAARGIDVDNISHVINYELPQDEEL 326
Cdd:PLN03137   684 IIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEG 763
                           90
                   ....*....|
gi 1198450891  327 YIHRIGRTGR 336
Cdd:PLN03137   764 YHQECGRAGR 773
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
247-347 1.95e-03

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: 38.78  E-value: 1.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 247 IIFCKTKRSVdEVVAAM--------QQKHYNVEAMHGDLSQNQRMNTLRRFKTGQIQYLVATDVAARGIDVDNISHVINY 318
Cdd:cd18797    39 IVFCRSRKLA-ELLLRYlkarlveeGPLASKVASYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLA 117
                          90       100
                  ....*....|....*....|....*....
gi 1198450891 319 ELPQDEELYIHRIGRTGRANKkgEAYSIV 347
Cdd:cd18797   118 GYPGSLASLWQQAGRAGRRGK--DSLVIL 144
RecG COG1200
RecG-like helicase [Replication, recombination and repair];
254-311 2.45e-03

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


Pssm-ID: 440813 [Multi-domain]  Cd Length: 684  Bit Score: 40.42  E-value: 2.45e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891 254 RSVDEVVAAMQQ--KHYNVEAMHGDLSQNQRMNTLRRFKTGQIQYLVATDVAARGIDVDN 311
Cdd:COG1200   488 QAAEETYEELREafPGLRVGLLHGRMKPAEKDAVMAAFKAGEIDVLVATTVIEVGVDVPN 547
PRK09751 PRK09751
putative ATP-dependent helicase Lhr; Provisional
274-335 3.06e-03

putative ATP-dependent helicase Lhr; Provisional


Pssm-ID: 137505 [Multi-domain]  Cd Length: 1490  Bit Score: 40.29  E-value: 3.06e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1198450891  274 HGDLSQNQRMNTLRRFKTGQIQYLVATDVAARGIDVDNISHVINYELPQDEELYIHRIGRTG 335
Cdd:PRK09751   308 HGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAG 369
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
30-140 7.92e-03

DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350781 [Multi-domain]  Cd Length: 206  Bit Score: 37.72  E-value: 7.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198450891  30 IQEKAIPVLLEG-KDIIGQAQTGTGKT----LAFGSVLLSCINKKDDGVKALVLSPTRELALQI----DEELRRIGkyts 100
Cdd:cd18023     5 IQSEVFPDLLYSdKNFVVSAPTGSGKTvlfeLAILRLLKERNPLPWGNRKVVYIAPIKALCSEKyddwKEKFGPLG---- 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1198450891 101 LSIVSVFGGSEIE--KQIRSlkkgADIVVGTPGRvLDLMRRK 140
Cdd:cd18023    81 LSCAELTGDTEMDdtFEIQD----ADIILTTPEK-WDSMTRR 117
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH