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Conserved domains on  [gi|116497013|gb|AAI26288|]
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DEAD (Asp-Glu-Ala-Asp) box polypeptide 27 [Homo sapiens]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 11423521)

DEAD/DEAH box-containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA

EC:  3.6.4.-
Gene Ontology:  GO:0016887|GO:0003676|GO:0005524
PubMed:  20206133
SCOP:  4000282|3002019

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
219-608 3.26e-155

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


:

Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 458.84  E-value: 3.26e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 219 SFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQAPvtRVLVLVPT 298
Cdd:COG0513    3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRAP--QALILAPT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 299 RELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEADRMLD 378
Cdd:COG0513   81 RELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIER-GALDLSGVETLVLDEADRMLD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 379 EYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRIFVNSNTDVAPFLRQEFIRIRPNregDREAIVAALL 458
Cdd:COG0513  160 MGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKR---DKLELLRRLL 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 459 TRTFTDHVMLFTQTKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKTVINF 538
Cdd:COG0513  237 RDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINY 316
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 539 TMPNTIKHYVHRVGRTARAGRAGRSVSLVGEDERKMLKEIVKAAKAPVKARILPQDVILKFRDKIEKMEK 608
Cdd:COG0513  317 DLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKRLERLKPK 386
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
219-608 3.26e-155

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 458.84  E-value: 3.26e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 219 SFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQAPvtRVLVLVPT 298
Cdd:COG0513    3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRAP--QALILAPT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 299 RELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEADRMLD 378
Cdd:COG0513   81 RELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIER-GALDLSGVETLVLDEADRMLD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 379 EYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRIFVNSNTDVAPFLRQEFIRIRPNregDREAIVAALL 458
Cdd:COG0513  160 MGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKR---DKLELLRRLL 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 459 TRTFTDHVMLFTQTKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKTVINF 538
Cdd:COG0513  237 RDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINY 316
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 539 TMPNTIKHYVHRVGRTARAGRAGRSVSLVGEDERKMLKEIVKAAKAPVKARILPQDVILKFRDKIEKMEK 608
Cdd:COG0513  317 DLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKRLERLKPK 386
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
229-424 1.22e-134

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: 397.01  E-value: 1.22e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 229 LLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQAPVTRVLVLVPTRELGIQVHSV 308
Cdd:cd17947    1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRPKKKAATRVLVLVPTRELAMQCFSV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 309 TRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNCPSFHLSSIEVLILDEADRMLDEYFEEQMKEI 388
Cdd:cd17947   81 LQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPSFDLDSIEILVLDEADRMLEEGFADELKEI 160
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 116497013 389 IRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRIF 424
Cdd:cd17947  161 LRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRVF 196
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
220-590 6.19e-95

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 303.02  E-value: 6.19e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 220 FQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQAP-VTRVLVLVPT 298
Cdd:PRK11192   3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFPRRKSgPPRILILTPT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 299 RELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEADRMLD 378
Cdd:PRK11192  83 RELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKE-ENFDCRAVETLILDEADRMLD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 379 EYFEEQMKEIIRMCSHHRQTMLFSATMTDE-VKDLASVSLKNPVRIfvnsntDVAPFLR-----QEFIRIRPNREgDREA 452
Cdd:PRK11192 162 MGFAQDIETIAAETRWRKQTLLFSATLEGDaVQDFAERLLNDPVEV------EAEPSRRerkkiHQWYYRADDLE-HKTA 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 453 IVAALLTRTFTDHVMLFTQTKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGV 532
Cdd:PRK11192 235 LLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDV 314
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 116497013 533 KTVINFTMPNTIKHYVHRVGRTARAGRAGRSVSLVGEDERKMLKEIVKAAKAPVKARI 590
Cdd:PRK11192 315 SHVINFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERYIEEPLKARV 372
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
242-412 8.10e-57

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: 191.69  E-value: 8.10e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013  242 TPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPrqaPVTRVLVLVPTRELGIQVHSVTRQLAQFCNITTC 321
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLD---NGPQALVLAPTRELAEQIYEELKKLGKGLGLKVA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013  322 LAVGGLDVKSQEAALRAaPDILIATPGRLIDHLHNcpSFHLSSIEVLILDEADRMLDEYFEEQMKEIIRMCSHHRQTMLF 401
Cdd:pfam00270  78 SLLGGDSRKEQLEKLKG-PDILVGTPGRLLDLLQE--RKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLL 154
                         170
                  ....*....|.
gi 116497013  402 SATMTDEVKDL 412
Cdd:pfam00270 155 SATLPRNLEDL 165
DEXDc smart00487
DEAD-like helicases superfamily;
233-423 5.48e-48

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 168.82  E-value: 5.48e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013   233 ITAMGFKQPTPIQKACIPVGLLG-KDICACAATGTGKTAAFALPVLERLIYKPRqapvTRVLVLVPTRELGIQVHSVTRQ 311
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGKG----GRVLVLVPTRELAEQWAEELKK 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013   312 LAQFCNITTCLAVGGLDVKSQEAAL-RAAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEADRMLDEYFEEQMKEIIR 390
Cdd:smart00487  77 LGPSLGLKVVGLYGGDSKREQLRKLeSGKTDILVTTPGRLLDLLEN-DKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLK 155
                          170       180       190
                   ....*....|....*....|....*....|...
gi 116497013   391 MCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 423
Cdd:smart00487 156 LLPKNVQLLLLSATPPEEIENLLELFLNDPVFI 188
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
219-608 3.26e-155

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 458.84  E-value: 3.26e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 219 SFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQAPvtRVLVLVPT 298
Cdd:COG0513    3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRAP--QALILAPT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 299 RELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEADRMLD 378
Cdd:COG0513   81 RELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIER-GALDLSGVETLVLDEADRMLD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 379 EYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRIFVNSNTDVAPFLRQEFIRIRPNregDREAIVAALL 458
Cdd:COG0513  160 MGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKR---DKLELLRRLL 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 459 TRTFTDHVMLFTQTKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKTVINF 538
Cdd:COG0513  237 RDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINY 316
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 539 TMPNTIKHYVHRVGRTARAGRAGRSVSLVGEDERKMLKEIVKAAKAPVKARILPQDVILKFRDKIEKMEK 608
Cdd:COG0513  317 DLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKRLERLKPK 386
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
229-424 1.22e-134

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: 397.01  E-value: 1.22e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 229 LLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQAPVTRVLVLVPTRELGIQVHSV 308
Cdd:cd17947    1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRPKKKAATRVLVLVPTRELAMQCFSV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 309 TRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNCPSFHLSSIEVLILDEADRMLDEYFEEQMKEI 388
Cdd:cd17947   81 LQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPSFDLDSIEILVLDEADRMLEEGFADELKEI 160
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 116497013 389 IRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRIF 424
Cdd:cd17947  161 LRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRVF 196
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
220-590 6.19e-95

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 303.02  E-value: 6.19e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 220 FQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQAP-VTRVLVLVPT 298
Cdd:PRK11192   3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFPRRKSgPPRILILTPT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 299 RELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEADRMLD 378
Cdd:PRK11192  83 RELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKE-ENFDCRAVETLILDEADRMLD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 379 EYFEEQMKEIIRMCSHHRQTMLFSATMTDE-VKDLASVSLKNPVRIfvnsntDVAPFLR-----QEFIRIRPNREgDREA 452
Cdd:PRK11192 162 MGFAQDIETIAAETRWRKQTLLFSATLEGDaVQDFAERLLNDPVEV------EAEPSRRerkkiHQWYYRADDLE-HKTA 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 453 IVAALLTRTFTDHVMLFTQTKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGV 532
Cdd:PRK11192 235 LLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDV 314
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 116497013 533 KTVINFTMPNTIKHYVHRVGRTARAGRAGRSVSLVGEDERKMLKEIVKAAKAPVKARI 590
Cdd:PRK11192 315 SHVINFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERYIEEPLKARV 372
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
229-423 8.40e-92

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: 285.88  E-value: 8.40e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 229 LLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQAPV-TRVLVLVPTRELGIQVHS 307
Cdd:cd00268    1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGRgPQALVLAPTRELAMQIAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 308 VTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNCpSFHLSSIEVLILDEADRMLDEYFEEQMKE 387
Cdd:cd00268   81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERG-KLDLSNVKYLVLDEADRMLDMGFEEDVEK 159
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 116497013 388 IIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 423
Cdd:cd00268  160 ILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRI 195
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
219-593 3.39e-89

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 289.01  E-value: 3.39e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 219 SFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLiyKPRQaPVTRVLVLVPT 298
Cdd:PRK11776   5 AFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKL--DVKR-FRVQALVLCPT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 299 RELGIQVHSVTRQLAQFC-NI---TTClavGGLDVKSQEAALRAAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEAD 374
Cdd:PRK11776  82 RELADQVAKEIRRLARFIpNIkvlTLC---GGVPMGPQIDSLEHGAHIIVGTPGRILDHLRK-GTLDLDALNTLVLDEAD 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 375 RMLDEYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRIFVNSnTDVAPFLRQEFIRIRPNregDREAIV 454
Cdd:PRK11776 158 RMLDMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVES-THDLPAIEQRFYEVSPD---ERLPAL 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 455 AALLTRTFTDHVMLFTQTKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKT 534
Cdd:PRK11776 234 QRLLLHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEA 313
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 116497013 535 VINFTMPNTIKHYVHRVGRTARAGRAGRSVSLVGEDERKMLKEIVKAAKAPVKARILPQ 593
Cdd:PRK11776 314 VINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLPS 372
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
218-586 6.53e-87

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 282.85  E-value: 6.53e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 218 LSFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQA----PVtRVL 293
Cdd:PRK10590   1 MSFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAkgrrPV-RAL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 294 VLVPTRELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEA 373
Cdd:PRK10590  80 ILTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQ-NAVKLDQVEILVLDEA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 374 DRMLDEYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRIFVNSNTDVAPFLRQEFIRIRPNREGDreaI 453
Cdd:PRK10590 159 DRMLDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKRE---L 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 454 VAALLTRTFTDHVMLFTQTKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVK 533
Cdd:PRK10590 236 LSQMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELP 315
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 116497013 534 TVINFTMPNTIKHYVHRVGRTARAGRAGRSVSLVGEDERKMLKEIVKAAKAPV 586
Cdd:PRK10590 316 HVVNYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEI 368
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
220-596 5.31e-80

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 264.85  E-value: 5.31e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 220 FQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKP----RQAPVTRVLVL 295
Cdd:PRK01297  89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPppkeRYMGEPRALII 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 296 VPTRELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAA-PDILIATPGRLIDHLHNcPSFHLSSIEVLILDEAD 374
Cdd:PRK01297 169 APTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEARfCDILVATPGRLLDFNQR-GEVHLDMVEVMVLDEAD 247
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 375 RMLDEYFEEQMKEIIRMCSH--HRQTMLFSATMTDEVKDLASVSLKNPVRIFVNSNTDVAPFLRQefiRIRPNREGDREA 452
Cdd:PRK01297 248 RMLDMGFIPQVRQIIRQTPRkeERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQ---HVYAVAGSDKYK 324
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 453 IVAALLTRTFTDHVMLFTQTKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGV 532
Cdd:PRK01297 325 LLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGI 404
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116497013 533 KTVINFTMPNTIKHYVHRVGRTARAGRAGRSVSLVGEDERKMLKEIVKAAKAPVKARILPQDVI 596
Cdd:PRK01297 405 SHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKISCEMPPAELL 468
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
220-570 4.24e-76

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 252.97  E-value: 4.24e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 220 FQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKP----RQAPVTRVLVL 295
Cdd:PRK04837  10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPapedRKVNQPRALIM 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 296 VPTRELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHL-HNCpsFHLSSIEVLILDEAD 374
Cdd:PRK04837  90 APTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAkQNH--INLGAIQVVVLDEAD 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 375 RMLDEYFEEQMKEIIRMC--SHHRQTMLFSATMTDEVKDLASVSLKNPVRIfvnsntDVAPfLRQEFIRIR-----PNRE 447
Cdd:PRK04837 168 RMFDLGFIKDIRWLFRRMppANQRLNMLFSATLSYRVRELAFEHMNNPEYV------EVEP-EQKTGHRIKeelfyPSNE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 448 gDREAIVAALLTRTFTDHVMLFTQTKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGL 527
Cdd:PRK04837 241 -EKMRLLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGL 319
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 116497013 528 DIEGVKTVINFTMPNTIKHYVHRVGRTARAGRAGRSVSLVGED 570
Cdd:PRK04837 320 HIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEE 362
PTZ00110 PTZ00110
helicase; Provisional
219-586 7.35e-76

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 255.85  E-value: 7.35e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 219 SFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALP----VLERLIYKPRQAPVtrVLV 294
Cdd:PTZ00110 131 SFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPaivhINAQPLLRYGDGPI--VLV 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 295 LVPTRELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLH-NCPSfhLSSIEVLILDEA 373
Cdd:PTZ00110 209 LAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLEsNVTN--LRRVTYLVLDEA 286
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 374 DRMLDEYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKN-PVRIFVNSNTDVAPF-LRQEFIRIRpnrEGDRE 451
Cdd:PTZ00110 287 DRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEePVHVNVGSLDLTACHnIKQEVFVVE---EHEKR 363
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 452 AIVAALLTRTFTD--HVMLFTQTKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDI 529
Cdd:PTZ00110 364 GKLKMLLQRIMRDgdKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDV 443
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 530 EGVKTVINFTMPNTIKHYVHRVGRTARAGRAGRSVSLVGEDERKMLKEIVK---AAKAPV 586
Cdd:PTZ00110 444 KDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVKvlrEAKQPV 503
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
219-659 9.14e-76

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 258.24  E-value: 9.14e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 219 SFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLiyKPR-QAPvtRVLVLVP 297
Cdd:PRK11634   7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNL--DPElKAP--QILVLAP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 298 TRELGIQVHSVTRQLAQFCNITTCLAV-GGLDVKSQEAALRAAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEADRM 376
Cdd:PRK11634  83 TRELAVQVAEAMTDFSKHMRGVNVVALyGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKR-GTLDLSKLSGLVLDEADEM 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 377 LDEYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRIFVNSNTDVAPFLRQEFIRIRPNREgdREAIVAA 456
Cdd:PRK11634 162 LRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRK--NEALVRF 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 457 LLTRTFtDHVMLFTQTKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKTVI 536
Cdd:PRK11634 240 LEAEDF-DAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVV 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 537 NFTMPNTIKHYVHRVGRTARAGRAGRSVSLVGEDERKMLKEIVKAAKAPV------KARILPQDVILKFRDKI----EKM 606
Cdd:PRK11634 319 NYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIpevelpNAELLGKRRLEKFAAKVqqqlESS 398
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116497013 607 EKDVYAVLqLEAEEKEMQQSEAQINT-AKRLLE--KGKEAVVQEPE-----RSWFQTKEER 659
Cdd:PRK11634 399 DLDQYRAL-LAKIQPTAEGEELDLETlAAALLKmaQGERPLILPPDapmrpKREFRDRDDR 458
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
217-591 1.29e-74

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 253.33  E-value: 1.29e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 217 NLSFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKP----RQAPVTRV 292
Cdd:PRK04537   8 DLTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPaladRKPEDPRA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 293 LVLVPTRELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNCPSFHLSSIEVLILDE 372
Cdd:PRK04537  88 LILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVVSLHACEICVLDE 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 373 ADRMLDEYFEEQMKEIIRMCSHH--RQTMLFSATMTDEVKDLASVSLKNPVRIFVNSNTDVAPFLRQefiRIRPNREGDR 450
Cdd:PRK04537 168 ADRMFDLGFIKDIRFLLRRMPERgtRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQ---RIYFPADEEK 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 451 EAIVAALLTRTFTDHVMLFTQTKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIE 530
Cdd:PRK04537 245 QTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHID 324
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116497013 531 GVKTVINFTMPNTIKHYVHRVGRTARAGRAGRSVSLVGEDERKMLKEI-----VKAAKAPVKARIL 591
Cdd:PRK04537 325 GVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIeayieQKIPVEPVTAELL 390
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
219-423 2.15e-69

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: 227.20  E-value: 2.15e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 219 SFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQapvTRVLVLVPT 298
Cdd:cd17954    1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQR---FFALVLAPT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 299 RELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNCPSFHLSSIEVLILDEADRMLD 378
Cdd:cd17954   78 RELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKGFSLKSLKFLVMDEADRLLN 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 116497013 379 EYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 423
Cdd:cd17954  158 MDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKI 202
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
220-421 2.51e-68

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: 224.41  E-value: 2.51e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 220 FQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLiykpRQAPV-TRVLVLVPT 298
Cdd:cd17955    1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRL----SEDPYgIFALVLTPT 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 299 RELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNCPS--FHLSSIEVLILDEADRM 376
Cdd:cd17955   77 RELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSDDttKVLSRVKFLVLDEADRL 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 116497013 377 LDEYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPV 421
Cdd:cd17955  157 LTGSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPF 201
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
219-423 2.80e-67

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: 221.41  E-value: 2.80e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 219 SFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLiyKPRQAPV-TRVLVLVP 297
Cdd:cd17959    2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKL--KAHSPTVgARALILSP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 298 TRELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNCpSFHLSSIEVLILDEADRML 377
Cdd:cd17959   80 TRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEM-NLKLSSVEYVVFDEADRLF 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 116497013 378 DEYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 423
Cdd:cd17959  159 EMGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
219-425 1.17e-62

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: 209.65  E-value: 1.17e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 219 SFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQAPVTR------- 291
Cdd:cd17967    1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVGRGrrkayps 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 292 VLVLVPTRELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLhNCPSFHLSSIEVLILD 371
Cdd:cd17967   81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFI-ERGRISLSSIKFLVLD 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 116497013 372 EADRMLDEYFEEQMKEIIRMCS----HHRQTMLFSATMTDEVKDLASVSLKNpvRIFV 425
Cdd:cd17967  160 EADRMLDMGFEPQIRKIVEHPDmppkGERQTLMFSATFPREIQRLAADFLKN--YIFL 215
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
230-426 3.79e-62

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: 207.53  E-value: 3.79e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 230 LKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLiYKPRQAPVTRV--LVLVPTRELGIQVHS 307
Cdd:cd17941    2 LKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKL-YRERWTPEDGLgaLIISPTRELAMQIFE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 308 VTRQLAQFCNITTCLAVGGLDVKsQEAALRAAPDILIATPGRLIDHLHNCPSFHLSSIEVLILDEADRMLDEYFEEQMKE 387
Cdd:cd17941   81 VLRKVGKYHSFSAGLIIGGKDVK-EEKERINRMNILVCTPGRLLQHMDETPGFDTSNLQMLVLDEADRILDMGFKETLDA 159
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 116497013 388 IIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRIFVN 426
Cdd:cd17941  160 IVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISVH 198
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
218-584 1.61e-60

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 213.50  E-value: 1.61e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 218 LSFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQAPVTR----VL 293
Cdd:PLN00206 121 LSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCTIRSGHPSEQrnplAM 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 294 VLVPTRELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHL--HNcpsFHLSSIEVLILD 371
Cdd:PLN00206 201 VLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLskHD---IELDNVSVLVLD 277
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 372 EADRMLDEYFEEQMKEIIRMCShHRQTMLFSATMTDEVKDLASVSLKNPVRIFVNSNTDVAPFLRQEFIRIRPNREgdRE 451
Cdd:PLN00206 278 EVDCMLERGFRDQVMQIFQALS-QPQVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQK--KQ 354
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 452 AIVAALLTRT-FTDHVMLFTQTKKQAHrmhiLLG-----LMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAAR 525
Cdd:PLN00206 355 KLFDILKSKQhFKPPAVVFVSSRLGAD----LLAnaitvVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGR 430
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 116497013 526 GLDIEGVKTVINFTMPNTIKHYVHRVGRTARAGRAGRSVSLVGEDERKMLKEIVKAAKA 584
Cdd:PLN00206 431 GVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALLKS 489
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
225-423 2.70e-60

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: 202.82  E-value: 2.70e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 225 LSRPLlkaITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIykPRQAPVTR-----VLVLVPTR 299
Cdd:cd17949    1 LVSHL---KSKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLL--SLEPRVDRsdgtlALVLVPTR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 300 ELGIQVHSVTRQLAQFC-NITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNCPSFHLSSIEVLILDEADRMLD 378
Cdd:cd17949   76 ELALQIYEVLEKLLKPFhWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQSFDVSNLRWLVLDEADRLLD 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 116497013 379 EYFEEQMKEIIRM-------------CSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 423
Cdd:cd17949  156 MGFEKDITKILELlddkrskaggeksKPSRRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
PTZ00424 PTZ00424
helicase 45; Provisional
212-578 4.45e-59

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 206.22  E-value: 4.45e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 212 SQYDENL-SFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQapvT 290
Cdd:PTZ00424  21 SNYDEIVdSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNA---C 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 291 RVLVLVPTRELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLhNCPSFHLSSIEVLIL 370
Cdd:PTZ00424  98 QALILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMI-DKRHLRVDDLKLFIL 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 371 DEADRMLDEYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRIFVNSNTDVAPFLRQEFIRIRpNREGDR 450
Cdd:PTZ00424 177 DEADEMLSRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVE-KEEWKF 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 451 EAIVAALLTRTFTdHVMLFTQTKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIE 530
Cdd:PTZ00424 256 DTLCDLYETLTIT-QAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQ 334
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 116497013 531 GVKTVINFTMPNTIKHYVHRVGRTARAGRAGRSVSLVGEDERKMLKEI 578
Cdd:PTZ00424 335 QVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEI 382
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
225-421 2.37e-58

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: 197.42  E-value: 2.37e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 225 LSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLErLIYKPRQA----PVTRVLVLVPTRE 300
Cdd:cd17961    1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQ-KILKAKAEsgeeQGTRALILVPTRE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 301 LGIQVHSVTRQLAQFC-NITTCLAVGG-LDVKSQEAALRAAPDILIATPGRLIDHLHNCPSFHLSSIEVLILDEADRMLD 378
Cdd:cd17961   80 LAQQVSKVLEQLTAYCrKDVRVVNLSAsSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLLSTLKYLVIDEADLVLS 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 116497013 379 EYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPV 421
Cdd:cd17961  160 YGYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPA 202
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
229-425 5.33e-58

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: 196.27  E-value: 5.33e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 229 LLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIyKPRQAPVTRVLVLVPTRELGIQVHSV 308
Cdd:cd17957    1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLG-KPRKKKGLRALILAPTRELASQIYRE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 309 TRQLAQFCNITTCLavggLDvKSQEAALRAAP------DILIATPGRLIDHLHNCPSfHLSSIEVLILDEADRMLDEYFE 382
Cdd:cd17957   80 LLKLSKGTGLRIVL----LS-KSLEAKAKDGPksitkyDILVSTPLRLVFLLKQGPI-DLSSVEYLVLDEADKLFEPGFR 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 116497013 383 EQMKEIIRMCSHHR-QTMLFSATMTDEVKDLASVSLKNPVRIFV 425
Cdd:cd17957  154 EQTDEILAACTNPNlQRSLFSATIPSEVEELARSVMKDPIRIIV 197
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
229-423 7.56e-58

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: 195.87  E-value: 7.56e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 229 LLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQAPVTRV--LVLVPTRELGIQVH 306
Cdd:cd17960    1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANLKKGQVgaLIISPTRELATQIY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 307 SVTRQLAQFC--NITTCLAVGGLDVKSQEAALRA-APDILIATPGRLIDHL-HNCPSFHLSSIEVLILDEADRMLDEYFE 382
Cdd:cd17960   81 EVLQSFLEHHlpKLKCQLLIGGTNVEEDVKKFKRnGPNILVGTPGRLEELLsRKADKVKVKSLEVLVLDEADRLLDLGFE 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 116497013 383 EQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 423
Cdd:cd17960  161 ADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRV 201
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
230-426 4.60e-57

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: 193.73  E-value: 4.60e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 230 LKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLErLIYKPRQAPV--TRVLVLVPTRELGIQVHS 307
Cdd:cd17942    2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIE-LLYKLKFKPRngTGVIIISPTRELALQIYG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 308 VTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNCPSFHLSSIEVLILDEADRMLDEYFEEQMKE 387
Cdd:cd17942   81 VAKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLYKNLQCLIIDEADRILEIGFEEEMRQ 160
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 116497013 388 IIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPvRIFVN 426
Cdd:cd17942  161 IIKLLPKRRQTMLFSATQTRKVEDLARISLKKK-PLYVG 198
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
242-412 8.10e-57

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: 191.69  E-value: 8.10e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013  242 TPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPrqaPVTRVLVLVPTRELGIQVHSVTRQLAQFCNITTC 321
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLD---NGPQALVLAPTRELAEQIYEELKKLGKGLGLKVA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013  322 LAVGGLDVKSQEAALRAaPDILIATPGRLIDHLHNcpSFHLSSIEVLILDEADRMLDEYFEEQMKEIIRMCSHHRQTMLF 401
Cdd:pfam00270  78 SLLGGDSRKEQLEKLKG-PDILVGTPGRLLDLLQE--RKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLL 154
                         170
                  ....*....|.
gi 116497013  402 SATMTDEVKDL 412
Cdd:pfam00270 155 SATLPRNLEDL 165
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
225-418 9.78e-56

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: 190.49  E-value: 9.78e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 225 LSRPLLKAITAMGFKQPTPIQKACIPVGL-LGKDICACAATGTGKTAAFALPVLERLIYKPRQAPVTRV--LVLVPTREL 301
Cdd:cd17964    1 LDPSLLKALTRMGFETMTPVQQKTLKPILsTGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSGVsaLIISPTREL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 302 GIQVHSVTRQLAQFC-NITTCLAVGGLDVKSQEAAL-RAAPDILIATPGRLIDHLHNCPSF-HLSSIEVLILDEADRMLD 378
Cdd:cd17964   81 ALQIAAEAKKLLQGLrKLRVQSAVGGTSRRAELNRLrRGRPDILVATPGRLIDHLENPGVAkAFTDLDYLVLDEADRLLD 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 116497013 379 EYFEEQMKEIIR----MCSHHRQTMLFSATMTDEVKDLASVSLK 418
Cdd:cd17964  161 MGFRPDLEQILRhlpeKNADPRQTLLFSATVPDEVQQIARLTLK 204
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
229-423 9.26e-55

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: 188.30  E-value: 9.26e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 229 LLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQAPVTR-----VLVLVPTRELGI 303
Cdd:cd17945    1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDEETKddgpyALILAPTRELAQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 304 QVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNcpsfH---LSSIEVLILDEADRMLDEY 380
Cdd:cd17945   81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLER----RllvLNQCTYVVLDEADRMIDMG 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116497013 381 FEEQMKEII--------------------RMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 423
Cdd:cd17945  157 FEPQVTKILdampvsnkkpdteeaeklaaSGKHRYRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
222-424 1.98e-51

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: 178.29  E-value: 1.98e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 222 DMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLiykPRQAPVTRVLVLVPTREL 301
Cdd:cd17939    1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRI---DTTVRETQALVLAPTREL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 302 GIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEADRMLDEYF 381
Cdd:cd17939   78 AQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQR-RSLRTDKIKMFVLDEADEMLSRGF 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 116497013 382 EEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRIF 424
Cdd:cd17939  157 KDQIYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRIL 199
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
218-418 5.78e-51

DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DEAD-box helicases are a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350810 [Multi-domain]  Cd Length: 264  Bit Score: 179.39  E-value: 5.78e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 218 LSFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLI--------YKPRQAPv 289
Cdd:cd18052   43 LTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMkegltassFSEVQEP- 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 290 tRVLVLVPTRELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLhNCPSFHLSSIEVLI 369
Cdd:cd18052  122 -QALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFI-GRGKISLSKLKYLI 199
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 116497013 370 LDEADRMLDEYFEEQMKEIIRMCS----HHRQTMLFSATMTDEVKDLASVSLK 418
Cdd:cd18052  200 LDEADRMLDMGFGPEIRKLVSEPGmpskEDRQTLMFSATFPEEIQRLAAEFLK 252
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
229-425 7.74e-51

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: 177.82  E-value: 7.74e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 229 LLKAITAMGFKQPTPIQKACIP---------VGLLGKDICACAATGTGKTAAFALPVLERLiyKPRQAPVTRVLVLVPTR 299
Cdd:cd17956    1 LLKNLQNNGITSAFPVQAAVIPwllpsskstPPYRPGDLCVSAPTGSGKTLAYVLPIVQAL--SKRVVPRLRALIVVPTK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 300 ELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAA--------PDILIATPGRLIDHLHNCPSFHLSSIEVLILD 371
Cdd:cd17956   79 ELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDtsgrylsrVDILVATPGRLVDHLNSTPGFTLKHLRFLVID 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116497013 372 EADRMLDEYFEE------------------QMKEIIRMCSHHR--QTMLFSATMTDEVKDLASVSLKNPvRIFV 425
Cdd:cd17956  159 EADRLLNQSFQDwletvmkalgrptapdlgSFGDANLLERSVRplQKLLFSATLTRDPEKLSSLKLHRP-RLFT 231
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
435-567 1.03e-49

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: 170.77  E-value: 1.03e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 435 LRQEFIRIRPnrEGDREAIVAALLTRTFTDHVMLFTQTKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQI 514
Cdd:cd18787    1 IKQLYVVVEE--EEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKV 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 116497013 515 DILVATDVAARGLDIEGVKTVINFTMPNTIKHYVHRVGRTARAGRAGRSVSLV 567
Cdd:cd18787   79 RVLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
229-423 3.80e-49

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: 171.78  E-value: 3.80e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 229 LLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQAPV--TRVLVLVPTRELGIQVH 306
Cdd:cd17966    1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERGdgPIVLVLAPTRELAQQIQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 307 SVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDhLHNCPSFHLSSIEVLILDEADRMLDEYFEEQMK 386
Cdd:cd17966   81 QEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLID-FLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIR 159
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 116497013 387 EIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 423
Cdd:cd17966  160 KIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
220-423 5.92e-49

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


Pssm-ID: 350698 [Multi-domain]  Cd Length: 201  Bit Score: 171.33  E-value: 5.92e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 220 FQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKprqAPVTRVLVLVPTR 299
Cdd:cd17940    1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPK---KDVIQALILVPTR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 300 ELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDhLHNCPSFHLSSIEVLILDEADRMLDE 379
Cdd:cd17940   78 ELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILD-LAKKGVADLSHCKTLVLDEADKLLSQ 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 116497013 380 YFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 423
Cdd:cd17940  157 DFQPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
229-423 9.79e-49

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: 170.67  E-value: 9.79e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 229 LLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLI----YKPRQAPVtrVLVLVPTRELGIQ 304
Cdd:cd17952    1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMdqreLEKGEGPI--AVIVAPTRELAQQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 305 VHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEADRMLDEYFEEQ 384
Cdd:cd17952   79 IYLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKK-KATNLQRVTYLVLDEADRMFDMGFEYQ 157
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 116497013 385 MKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 423
Cdd:cd17952  158 VRSIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
DEXDc smart00487
DEAD-like helicases superfamily;
233-423 5.48e-48

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 168.82  E-value: 5.48e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013   233 ITAMGFKQPTPIQKACIPVGLLG-KDICACAATGTGKTAAFALPVLERLIYKPRqapvTRVLVLVPTRELGIQVHSVTRQ 311
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGKG----GRVLVLVPTRELAEQWAEELKK 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013   312 LAQFCNITTCLAVGGLDVKSQEAAL-RAAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEADRMLDEYFEEQMKEIIR 390
Cdd:smart00487  77 LGPSLGLKVVGLYGGDSKREQLRKLeSGKTDILVTTPGRLLDLLEN-DKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLK 155
                          170       180       190
                   ....*....|....*....|....*....|...
gi 116497013   391 MCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 423
Cdd:smart00487 156 LLPKNVQLLLLSATPPEEIENLLELFLNDPVFI 188
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
229-406 3.03e-46

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: 165.10  E-value: 3.03e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 229 LLKAITAMGFKQPTPIQKACIPVGLL-GKDICACAATGTGKTAAFALPVLERLIYKPRQAPVT------RVLVLVPTREL 301
Cdd:cd17946    1 ILRALADLGFSEPTPIQALALPAAIRdGKDVIGAAETGSGKTLAFGIPILERLLSQKSSNGVGgkqkplRALILTPTREL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 302 GIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNCPSF--HLSSIEVLILDEADRMLDE 379
Cdd:cd17946   81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEHlaNLKSLRFLVLDEADRMLEK 160
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 116497013 380 -YFEEqMKEIIRM-------CSHHRQTMLFSATMT 406
Cdd:cd17946  161 gHFAE-LEKILELlnkdragKKRKRQTFVFSATLT 194
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
220-423 6.65e-45

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: 159.92  E-value: 6.65e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 220 FQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYkprQAPVTRVLVLVPTR 299
Cdd:cd18046    1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDT---SLKATQALVLAPTR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 300 ELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLhNCPSFHLSSIEVLILDEADRMLDE 379
Cdd:cd18046   78 ELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMI-NRRYLRTDYIKMFVLDEADEMLSR 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 116497013 380 YFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 423
Cdd:cd18046  157 GFKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
229-423 1.45e-44

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: 159.43  E-value: 1.45e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 229 LLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVL-------ERLIYKPRQAPVTrvLVLVPTREL 301
Cdd:cd17951    1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLImfaleqeKKLPFIKGEGPYG--LIVCPSREL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 302 GIQVHSVTRQLAQFCN------ITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLhNCPSFHLSSIEVLILDEADR 375
Cdd:cd17951   79 ARQTHEVIEYYCKALQeggypqLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDML-NKKKINLDICRYLCLDEADR 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 116497013 376 MLDEYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 423
Cdd:cd17951  158 MIDMGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
229-423 2.75e-43

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


Pssm-ID: 350720 [Multi-domain]  Cd Length: 193  Bit Score: 155.40  E-value: 2.75e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 229 LLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRqAPVTrvLVLVPTRELGIQVHSV 308
Cdd:cd17962    1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHR-NPSA--LILTPTRELAVQIEDQ 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 309 TRQLAQ-FCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLhNCPSFHLSSIEVLILDEADRMLDEYFEEQMKE 387
Cdd:cd17962   78 AKELMKgLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDIL-KQSSVELDNIKIVVVDEADTMLKMGFQQQVLD 156
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 116497013 388 IIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 423
Cdd:cd17962  157 ILENISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
225-423 3.23e-43

DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) is a component of the 17S U2 snRNP complex. It plays an important role in pre-mRNA splicing and has a role in antiviral innate immunity. DDX46 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350711 [Multi-domain]  Cd Length: 222  Bit Score: 156.00  E-value: 3.23e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 225 LSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALP----VLERLIYKPRQAPVTrvLVLVPTRE 300
Cdd:cd17953   19 LSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPmfrhIKDQRPVKPGEGPIG--LIMAPTRE 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 301 LGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHL--HNCPSFHLSSIEVLILDEADRMLD 378
Cdd:cd17953   97 LALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtaNNGRVTNLRRVTYVVLDEADRMFD 176
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 116497013 379 EYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 423
Cdd:cd17953  177 MGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
229-404 5.36e-43

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: 154.34  E-value: 5.36e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 229 LLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQapvTRVLVLVPTRELGIQVHSV 308
Cdd:cd17943    1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRH---PQVLILAPTREIAVQIHDV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 309 TRQLAQFC-NITTCLAVGGLDVKSQEAALRaAPDILIATPGRlIDHLHNCPSFHLSSIEVLILDEADRMLDEYFEEQMKE 387
Cdd:cd17943   78 FKKIGKKLeGLKCEVFIGGTPVKEDKKKLK-GCHIAVGTPGR-IKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNW 155
                        170
                 ....*....|....*..
gi 116497013 388 IIRMCSHHRQTMLFSAT 404
Cdd:cd17943  156 IFSSLPKNKQVIAFSAT 172
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
229-424 1.37e-42

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: 153.39  E-value: 1.37e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 229 LLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKP---RQAPVTRVLVLVPTRELGIQV 305
Cdd:cd17958    1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPiprEQRNGPGVLVLTPTRELALQI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 306 HSVTRQLAqFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDhLHNCPSFHLSSIEVLILDEADRMLDEYFEEQM 385
Cdd:cd17958   81 EAECSKYS-YKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLND-LQMNNVINLKSITYLVLDEADRMLDMGFEPQI 158
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 116497013 386 KEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRIF 424
Cdd:cd17958  159 RKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIVY 197
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
225-423 2.98e-42

DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called DEAD box RNA helicase DEAD5) and DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH)) are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350721 [Multi-domain]  Cd Length: 196  Bit Score: 152.34  E-value: 2.98e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 225 LSRPLLKAITAMGFKQPTPIQKACIPVgLLG---KDICACAATGTGKTAAFALPVLERLiyKPRQaPVTRVLVLVPTREL 301
Cdd:cd17963    1 LKPELLKGLYAMGFNKPSKIQETALPL-ILSdppENLIAQSQSGTGKTAAFVLAMLSRV--DPTL-KSPQALCLAPTREL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 302 GIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEaalRAAPDILIATPGRLIDHL-HNCpsFHLSSIEVLILDEADRMLD-E 379
Cdd:cd17963   77 ARQIGEVVEKMGKFTGVKVALAVPGNDVPRGK---KITAQIVIGTPGTVLDWLkKRQ--LDLKKIKILVLDEADVMLDtQ 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 116497013 380 YFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 423
Cdd:cd17963  152 GHGDQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
219-419 5.01e-42

DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD box, X isoform, or DDX14) has been reported to display a high level of RNA-independent ATPase activity stimulated by both RNA and DNA. This protein has multiple conserved domains and is thought to play roles in both the nucleus and cytoplasm. Nuclear roles include transcriptional regulation, mRNP assembly, pre-mRNA splicing, and mRNA export. In the cytoplasm, this protein is thought to be involved in translation, cellular signaling, and viral replication. Misregulation of this gene has been implicated in tumorigenesis. Diseases associated with DDX3 include mental retardation, X-linked 102 and agenesis of the corpus callosum, with facial anomalies and robin sequence. DDX3 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350809 [Multi-domain]  Cd Length: 249  Bit Score: 153.66  E-value: 5.01e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 219 SFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLI----YKPRQAPVTR--- 291
Cdd:cd18051   22 TFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYeqgpGESLPSESGYygr 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 292 ------VLVLVPTRELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNcPSFHLSSI 365
Cdd:cd18051  102 rkqyplALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLER-GKIGLDYC 180
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 116497013 366 EVLILDEADRMLDEYFEEQMKEIIRMC----SHHRQTMLFSATMTDEVKDLASVSLKN 419
Cdd:cd18051  181 KYLVLDEADRMLDMGFEPQIRRIVEQDtmppTGERQTLMFSATFPKEIQMLARDFLDN 238
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
219-425 2.55e-40

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: 147.49  E-value: 2.55e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 219 SFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQapvTRVLVLVPT 298
Cdd:cd17950    3 GFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQ---VSVLVICHT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 299 RELGIQVHSVTRQLAQFC-NITTCLAVGGLDVKSQEAALR-AAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEADRM 376
Cdd:cd17950   80 RELAFQISNEYERFSKYMpNVKTAVFFGGVPIKKDIEVLKnKCPHIVVGTPGRILALVRE-KKLKLSHVKHFVLDECDKM 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 116497013 377 LDEY-FEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRIFV 425
Cdd:cd17950  159 LEQLdMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
218-427 3.18e-39

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: 145.15  E-value: 3.18e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 218 LSFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKP----RQAPVtrVL 293
Cdd:cd18049   24 LNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPflerGDGPI--CL 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 294 VLVPTRELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHnCPSFHLSSIEVLILDEA 373
Cdd:cd18049  102 VLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLE-AGKTNLRRCTYLVLDEA 180
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 116497013 374 DRMLDEYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRIFVNS 427
Cdd:cd18049  181 DRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIGA 234
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
220-421 8.36e-37

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: 137.07  E-value: 8.36e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 220 FQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLErliykprqapVTRVLVLVPTR 299
Cdd:cd17938    1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQ----------IVVALILEPSR 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 300 ELGIQVHSVTRQLAQFCN---ITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEADRM 376
Cdd:cd17938   71 ELAEQTYNCIENFKKYLDnpkLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKT-GKLDLSSVRFFVLDEADRL 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 116497013 377 LDEYFEEQMKEIIRMCSHHR------QTMLFSATM-TDEVKDLASVSLKNPV 421
Cdd:cd17938  150 LSQGNLETINRIYNRIPKITsdgkrlQVIVCSATLhSFEVKKLADKIMHFPT 201
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
220-423 3.40e-35

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: 132.59  E-value: 3.40e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 220 FQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQapvTRVLVLVPTR 299
Cdd:cd18045    1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRE---TQALILSPTR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 300 ELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEADRMLDE 379
Cdd:cd18045   78 ELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRR-RSLRTRHIKMLVLDEADEMLNK 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 116497013 380 YFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 423
Cdd:cd18045  157 GFKEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
219-423 3.72e-33

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


Pssm-ID: 350808 [Multi-domain]  Cd Length: 271  Bit Score: 128.98  E-value: 3.72e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 219 SFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPR----QAPVtrVLV 294
Cdd:cd18050   63 AFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYlergDGPI--CLV 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 295 LVPTRELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNCPSfHLSSIEVLILDEAD 374
Cdd:cd18050  141 LAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKT-NLRRCTYLVLDEAD 219
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 116497013 375 RMLDEYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 423
Cdd:cd18050  220 RMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQI 268
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
229-414 1.66e-31

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


Pssm-ID: 350706 [Multi-domain]  Cd Length: 231  Bit Score: 122.86  E-value: 1.66e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 229 LLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKP----RQAPVTRVLVLVPTRELGIQ 304
Cdd:cd17948    1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKllaeGPFNAPRGLVITPSRELAEQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 305 VHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGrLIDHLHNCPSFHLSSIEVLILDEADRMLDEYFEEQ 384
Cdd:cd17948   81 IGSVAQSLTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPG-ALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEK 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 116497013 385 MKEIIRMCSHHR-------------QTMLFSATMTDEVKDLAS 414
Cdd:cd17948  160 LSHFLRRFPLASrrsentdgldpgtQLVLVSATMPSGVGEVLS 202
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
449-558 1.87e-30

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: 115.77  E-value: 1.87e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013  449 DREAIVAALLTRTFTDHVMLFTQTKKQAHrMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLD 528
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
                          90       100       110
                  ....*....|....*....|....*....|
gi 116497013  529 IEGVKTVINFTMPNTIKHYVHRVGRTARAG 558
Cdd:pfam00271  80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
230-418 5.47e-30

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: 117.64  E-value: 5.47e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 230 LKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERL---IYKPRQAPVTRVLVLVPTRELGIQV- 305
Cdd:cd17944    2 IKLLQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLqedQQPRKRGRAPKVLVLAPTRELANQVt 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 306 ---HSVTRQLAQFCnittclAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEADRMLDEYFE 382
Cdd:cd17944   82 kdfKDITRKLSVAC------FYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQN-GRLDLTKLKHVVLDEVDQMLDMGFA 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 116497013 383 EQMKEIIRMC-----SHHRQTMLFSATMTDEVKDLASVSLK 418
Cdd:cd17944  155 EQVEEILSVSykkdsEDNPQTLLFSATCPDWVYNVAKKYMK 195
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
219-420 5.87e-26

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: 107.03  E-value: 5.87e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 219 SFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLG--KDICACAATGTGKTAAFALPVLERLIYKpRQAPvtRVLVLV 296
Cdd:cd18048   19 SFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDAL-KLYP--QCLCLS 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 297 PTRELGIQVHSVTRQLAQFCN-ITTCLAVGGldvKSQEAALRAAPDILIATPGRLIDHLHNCPSFHLSSIEVLILDEADR 375
Cdd:cd18048   96 PTFELALQTGKVVEEMGKFCVgIQVIYAIRG---NRPGKGTDIEAQIVIGTPGTVLDWCFKLRLIDVTNISVFVLDEADV 172
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 116497013 376 MLD-EYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNP 420
Cdd:cd18048  173 MINvQGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDP 218
HELICc smart00490
helicase superfamily c-terminal domain;
478-558 1.18e-24

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 98.05  E-value: 1.18e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013   478 RMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKTVINFTMPNTIKHYVHRVGRTARA 557
Cdd:smart00490   2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRA 81

                   .
gi 116497013   558 G 558
Cdd:smart00490  82 G 82
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
219-420 2.72e-21

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: 92.86  E-value: 2.72e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 219 SFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLG--KDICACAATGTGKTAAFALPVLERLiykPRQAPVTRVLVLV 296
Cdd:cd18047    2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV---EPANKYPQCLCLS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 297 PTRELGIQVHSVTRQLAQFC-NITTCLAVGGldvKSQEAALRAAPDILIATPGRLIDHLHNCPSFHLSSIEVLILDEADR 375
Cdd:cd18047   79 PTYELALQTGKVIEQMGKFYpELKLAYAVRG---NKLERGQKISEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADV 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 116497013 376 ML-DEYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNP 420
Cdd:cd18047  156 MIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
255-713 1.80e-20

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 96.25  E-value: 1.80e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 255 GKDICACAATGTGKTAAFALpVLERLIYKPRqapvtrVLVLVPTRELGIQVHsvtrqlAQFCNITTCLAVGGLDVKSQEa 334
Cdd:COG1061  100 GGRGLVVAPTGTGKTVLALA-LAAELLRGKR------VLVLVPRRELLEQWA------EELRRFLGDPLAGGGKKDSDA- 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 335 alraapDILIATPGRLIDHLHNcpSFHLSSIEVLILDEADRMLDEYFEEqmkeIIRMCSHHRqTMLFSAT--MTDEvKDL 412
Cdd:COG1061  166 ------PITVATYQSLARRAHL--DELGDRFGLVIIDEAHHAGAPSYRR----ILEAFPAAY-RLGLTATpfRSDG-REI 231
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 413 ASVSLKN-----------------PVRIFV------NSNTDVAPFLRQEFIRIRPNREGDREAIVAALLTRTFTDHVMLF 469
Cdd:COG1061  232 LLFLFDGivyeyslkeaiedgylaPPEYYGirvdltDERAEYDALSERLREALAADAERKDKILRELLREHPDDRKTLVF 311
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 470 TQTKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKTVINFTMPNTIKHYVH 549
Cdd:COG1061  312 CSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQ 391
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 550 RVGRTARAGRAGRSVS---LVGEDeRKMLKEIVKAAKAPVKARILPQDVILKFRDKIEKMEKDVYAVLQLEAEEKEMQQS 626
Cdd:COG1061  392 RLGRGLRPAPGKEDALvydFVGND-VPVLEELAKDLRDLAGYRVEFLDEEESEELALLIAVKPALEVKGELEEELLEELE 470
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 627 EAQINTAKRLLEkGKEAVVQEPERSWFQTKEERKKEKIAKALQEFDLALRGKKKRKKFMKDAKKKGEMTAEERSQFEILK 706
Cdd:COG1061  471 LLEDALLLVLAE-LLLLELLALALELLELAKAEGKAEEEEEEKELLLLLALAKLLKLLLLLLLLLLLELLELLAALLRLE 549

                 ....*..
gi 116497013 707 AQMFAER 713
Cdd:COG1061  550 ELAALLL 556
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
255-404 1.54e-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: 77.06  E-value: 1.54e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 255 GKDICACAATGTGKTAAFALPVLERLIYKPRQapvtrVLVLVPTRELGIQVHSVTRQLAQFcNITTCLAVGGLDVKSQEA 334
Cdd:cd00046    1 GENVLITAPTGSGKTLAALLAALLLLLKKGKK-----VLVLVPTKALALQTAERLRELFGP-GIRVAVLVGGSSAEEREK 74
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116497013 335 ALRAAPDILIATPGRLIDHLHNCPSFHLSSIEVLILDEADRMLDEYFEEQMkEIIRMCSHHR---QTMLFSAT 404
Cdd:cd00046   75 NKLGDADIIIATPDMLLNLLLREDRLFLKDLKLIIVDEAHALLIDSRGALI-LDLAVRKAGLknaQVILLSAT 146
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
224-567 5.59e-16

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: 82.19  E-value: 5.59e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 224 NLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRqapvTRVLVLVPTRELGI 303
Cdd:COG1205   40 WLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDPG----ATALYLYPTKALAR 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 304 -QVHSVtRQLAQFCNITTCLAV--GglDVKSQE-AALRAAPDILIATPgrliD--HLHNCPSFH-----LSSIEVLILDE 372
Cdd:COG1205  116 dQLRRL-RELAEALGLGVRVATydG--DTPPEErRWIREHPDIVLTNP----DmlHYGLLPHHTrwarfFRNLRYVVIDE 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 373 A---------------DRMLdeyfeeqmkeiiRMCSHHRQTMLF---SATMtDEVKDLASVSLKNPVRIfVNSNTdvAPF 434
Cdd:COG1205  189 AhtyrgvfgshvanvlRRLR------------RICRHYGSDPQFilaSATI-GNPAEHAERLTGRPVTV-VDEDG--SPR 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 435 LRQEFIRIRP---NREGDREAIV-AALLTRTFTDH---VMLFTQTKKQAHRMHILL------GLMGLQVGELHGNLSQTQ 501
Cdd:COG1205  253 GERTFVLWNPplvDDGIRRSALAeAARLLADLVREglrTLVFTRSRRGAELLARYArralrePDLADRVAAYRAGYLPEE 332
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116497013 502 RLEALRRFKDEQIDILVATDVAARGLDIEGVKTVINFTMPNTIKHYVHRVGrtaRAGRAGRSvSLV 567
Cdd:COG1205  333 RREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAG---RAGRRGQD-SLV 394
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
240-408 2.14e-15

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


Pssm-ID: 350723 [Multi-domain]  Cd Length: 251  Bit Score: 76.65  E-value: 2.14e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 240 QPTPIQKACIPVgLLGK----------------DICACAA-TGTGKTAAFALPVLERL-------------IYKPRQAPV 289
Cdd:cd17965   30 KPSPIQTLAIKK-LLKTlmrkvtkqtsneepklEVFLLAAeTGSGKTLAYLAPLLDYLkrqeqepfeeaeeEYESAKDTG 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 290 T-RVLVLVPTRELGIQVHSVTRQLAQFC--NITTCLAVGGLDVKSQEAALRAAPDILIATPGrLIDHLHNCPSFHLSSIE 366
Cdd:cd17965  109 RpRSVILVPTHELVEQVYSVLKKLSHTVklGIKTFSSGFGPSYQRLQLAFKGRIDILVTTPG-KLASLAKSRPKILSRVT 187
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 116497013 367 VLILDEADRMLDEYFEEQMKEIIRMCSHHRQTMLFSATMTDE 408
Cdd:cd17965  188 HLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKE 229
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
497-578 7.73e-13

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 72.07  E-value: 7.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 497 LSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKTVINF-TMPNTIKhYVHRVGRTARaGRAGRSVSLVGED----- 570
Cdd:COG1111  395 LTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYePVPSEIR-SIQRKGRTGR-KREGRVVVLIAKGtrdea 472
                         90
                 ....*....|....*.
gi 116497013 571 --------ERKMLKEI 578
Cdd:COG1111  473 yywssrrkEKKMKSIL 488
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
255-373 1.12e-10

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


Pssm-ID: 350681 [Multi-domain]  Cd Length: 182  Bit Score: 61.45  E-value: 1.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 255 GKDICACAATGTGKTAAFALPVLERLIYKPRqapvTRVLVLVPTRELGI-QVHSVTRQLAQFCNITTCLAVGG-LDVKSQ 332
Cdd:cd17923   15 GRSVVVTTGTASGKSLCYQLPILEALLRDPG----SRALYLYPTKALAQdQLRSLRELLEQLGLGIRVATYDGdTPREER 90
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 116497013 333 EAALRAAPDILIATPGRL---IDHLHNCPSFHLSSIEVLILDEA 373
Cdd:cd17923   91 RAIIRNPPRILLTNPDMLhyaLLPHHDRWARFLRNLRYVVLDEA 134
PRK13766 PRK13766
Hef nuclease; Provisional
497-645 1.59e-10

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 64.89  E-value: 1.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 497 LSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKTVINFT-MPNTIKhYVHRVGRTARaGRAGRSVSLVGED----- 570
Cdd:PRK13766 407 MSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVIFYEpVPSEIR-SIQRKGRTGR-QEEGRVVVLIAKGtrdea 484
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 571 --------ERKMlKEIVKAAKAPVKARILPQDVILKFRDKIEKMEKDVYAVLQL-EAEEKEMQQSEAQINTAKRLLEKGK 641
Cdd:PRK13766 485 yywssrrkEKKM-KEELKNLKGILNKKLQELDEEQKGEEEEKDEQLSLDDFVKSkGKEEEEEEEKEEKDKETEEDEPEGP 563

                 ....
gi 116497013 642 EAVV 645
Cdd:PRK13766 564 KIIV 567
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
253-380 2.04e-09

DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350685 [Multi-domain]  Cd Length: 201  Bit Score: 58.21  E-value: 2.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 253 LLGKDICACAATGTGKTAAfALPVLERLIYKPRQAPVTRVLVLVPTrelgiqVHSVTRQLAQFCNITTCLA--VGGL--D 328
Cdd:cd17927   15 LKGKNTIICLPTGSGKTFV-AVLICEHHLKKFPAGRKGKVVFLANK------VPLVEQQKEVFRKHFERPGykVTGLsgD 87
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 116497013 329 VKSQEAALRAAP--DILIATPGRLIDHLHNCPSFHLSSIEVLILDEADRMLDEY 380
Cdd:cd17927   88 TSENVSVEQIVEssDVIIVTPQILVNDLKSGTIVSLSDFSLLVFDECHNTTKNH 141
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
395-561 2.44e-09

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 60.54  E-value: 2.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 395 HRQTMLFSATMTDEVKD--LASVSLKNPvRIFVnsntdvAPFLRQE-FIRIRPNREGDREAIVAALLTRTFTDHVMLFTQ 471
Cdd:COG0514  166 NVPVLALTATATPRVRAdiAEQLGLEDP-RVFV------GSFDRPNlRLEVVPKPPDDKLAQLLDFLKEHPGGSGIVYCL 238
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 472 TKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATdVA-ARGLDIEGVKTVINFTMPNTIKHYVHR 550
Cdd:COG0514  239 SRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGIDKPDVRFVIHYDLPKSIEAYYQE 317
                        170
                 ....*....|.
gi 116497013 551 VGrtaRAGRAG 561
Cdd:COG0514  318 IG---RAGRDG 325
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
512-558 1.06e-08

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: 52.71  E-value: 1.06e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 116497013 512 EQIDILVATDVAARGLDIEGVKTVINFTMPNTIKHYVHRVGRTARAG 558
Cdd:cd18785   21 SSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGG 67
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
238-564 1.27e-08

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 58.58  E-value: 1.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 238 FKQPTPIQKACIPVGLLGKDICACAATGTGKT-AAFaLPVLERLIYKPRQAPV---TRVLVLVPTRELGIQVHsvtRQLA 313
Cdd:COG1201   22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAF-LPALDELARRPRPGELpdgLRVLYISPLKALANDIE---RNLR 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 314 QFCNITTCLAVGGL----------DVKSQE--AALRAAPDILIATPgrliDHLH---NCPSF--HLSSIEVLILDE---- 372
Cdd:COG1201   98 APLEEIGEAAGLPLpeirvgvrtgDTPASErqRQRRRPPHILITTP----ESLAlllTSPDAreLLRGVRTVIVDEihal 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 373 ------ADRMLD-EYFEeqmkeiiRMCSHHRQTMLFSATMT--DEVKD-LASVSLKNPVRIfVNSNTDVAPFLR-----Q 437
Cdd:COG1201  174 agskrgVHLALSlERLR-------ALAPRPLQRIGLSATVGplEEVARfLVGYEDPRPVTI-VDAGAGKKPDLEvlvpvE 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 438 EFIRIRPNREGDREAIVAALLT-----RTftdhVMLFTQTKKQA----HRMHILLGLMGLQVGELHGNLSQTQRLEALRR 508
Cdd:COG1201  246 DLIERFPWAGHLWPHLYPRVLDlieahRT----TLVFTNTRSQAerlfQRLNELNPEDALPIAAHHGSLSREQRLEVEEA 321
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 509 FKDEQIDILVAT---DVaarGLDIEGVKTVINFTMPntikhyvHRVGRTA-RAGRAGRSV 564
Cdd:COG1201  322 LKAGELRAVVATsslEL---GIDIGDVDLVIQVGSP-------KSVARLLqRIGRAGHRV 371
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
497-557 1.48e-08

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: 54.13  E-value: 1.48e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116497013 497 LSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKTVINFTMPNTIKHYVHRVGRtARA 557
Cdd:cd18802   74 MTQRKQKETLDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARA 133
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
497-566 7.65e-08

C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350188 [Multi-domain]  Cd Length: 143  Bit Score: 51.97  E-value: 7.65e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116497013 497 LSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKTVINF-TMPNTIKhYVHRVGRTARaGRAGRSVSL 566
Cdd:cd18801   74 MSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYdASPSPIR-MIQRMGRTGR-KRQGRVVVL 142
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
469-562 7.77e-08

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: 51.83  E-value: 7.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 469 FTQTKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKTVINFTMPNTIKHYV 548
Cdd:cd18794   36 YCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYY 115
                         90
                 ....*....|....
gi 116497013 549 HRVGrtaRAGRAGR 562
Cdd:cd18794  116 QESG---RAGRDGL 126
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
261-404 2.82e-07

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: 50.38  E-value: 2.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 261 CAATGTGKTA-AFALPVLerliykprqAPVTRVLVLVPTRELgiqVHSVTRQLAQFCNITTCLAVGGLDVKSQEAAlraa 339
Cdd:cd17926   24 VLPTGSGKTLtALALIAY---------LKELRTLIVVPTDAL---LDQWKERFEDFLGDSSIGLIGGGKKKDFDDA---- 87
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116497013 340 pDILIATPGRLIDHLHNcPSFHLSSIEVLILDEADRmldeYFEEQMKEIIRMCSHHRQtMLFSAT 404
Cdd:cd17926   88 -NVVVATYQSLSNLAEE-EKDLFDQFGLLIVDEAHH----LPAKTFSEILKELNAKYR-LGLTAT 145
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
229-373 3.86e-07

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 53.36  E-value: 3.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 229 LLKAITAMGFKQPTPIQKACIPVGLL-GKDICACAATGTGKTAafalpVLERLIYK--PRQApvtRVLVLVPTRELGIQV 305
Cdd:COG1204   11 VIEFLKERGIEELYPPQAEALEAGLLeGKNLVVSAPTASGKTL-----IAELAILKalLNGG---KALYIVPLRALASEK 82
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116497013 306 HS-VTRQLAQFcNITTCLAVGGLDVKSQEAAlraAPDILIATPGRLIDHLHNCPSFhLSSIEVLILDEA 373
Cdd:COG1204   83 YReFKRDFEEL-GIKVGVSTGDYDSDDEWLG---RYDILVATPEKLDSLLRNGPSW-LRDVDLVVVDEA 146
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
468-566 7.38e-07

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: 49.57  E-value: 7.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 468 LFTQTKKQAHRMHILLG------LMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKTVINFTMP 541
Cdd:cd18796   43 VFTNTRSQAERLAQRLRelcpdrVPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSP 122
                         90       100
                 ....*....|....*....|....*
gi 116497013 542 NTIKHYVHRVGrtaRAGRAGRSVSL 566
Cdd:cd18796  123 KSVARLLQRLG---RSGHRPGAASK 144
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
466-541 1.03e-06

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: 48.63  E-value: 1.03e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116497013 466 VMLFTQTKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQ--IDILVATDVAARGLDIEGVKTVINFTMP 541
Cdd:cd18793   30 VLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPdiRVFLLSTKAGGVGLNLTAANRVILYDPW 107
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
256-373 1.49e-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: 49.57  E-value: 1.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 256 KDICACAATGTGKTaAFALPVLERLIYKPRQ--APVTRVLVLVPTRELGIQVHSVTRQLaqfcnitTCLAVG---GLDVK 330
Cdd:cd18034   17 RNTIVVLPTGSGKT-LIAVMLIKEMGELNRKekNPKKRAVFLVPTVPLVAQQAEAIRSH-------TDLKVGeysGEMGV 88
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 116497013 331 SQEAALR-----AAPDILIATPGRLIDHLHNCpSFHLSSIEVLILDEA 373
Cdd:cd18034   89 DKWTKERwkeelEKYDVLVMTAQILLDALRHG-FLSLSDINLLIFDEC 135
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
242-414 7.25e-06

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: 47.26  E-value: 7.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 242 TPIQKACIPVGLL-GKDICACAATGTGKTAAFALPVLERLIYKPRqapvtRVLVLVPTRELGIQVHSVTRQLAQFCNITT 320
Cdd:cd17921    3 NPIQREALRALYLsGDSVLVSAPTSSGKTLIAELAILRALATSGG-----KAVYIAPTRALVNQKEADLRERFGPLGKNV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 321 CLAVGGLDVKSQEAAlraAPDILIATPGRLIDHLHNCPSFHLSSIEVLILDEADRMLDE----YFEEQMKEIIRMCSHHR 396
Cdd:cd17921   78 GLLTGDPSVNKLLLA---EADILVATPEKLDLLLRNGGERLIQDVRLVVVDEAHLIGDGergvVLELLLSRLLRINKNAR 154
                        170
                 ....*....|....*...
gi 116497013 397 qtMLFSATMTDEVKDLAS 414
Cdd:cd17921  155 --FVGLSATLPNAEDLAE 170
UTP25 pfam06862
Utp25, U3 small nucleolar RNA-associated SSU processome protein 25; UTP25 is a family of ...
341-442 8.31e-06

Utp25, U3 small nucleolar RNA-associated SSU processome protein 25; UTP25 is a family of eukaryotic proteins. The family displays limited sequence similarity to DEAD-box RNA helicases, having alternative residues at the Walker A and DEAD-box sites, but conservation of structural and other key residues. The domain is required and sufficient for the interaction of Utp25 with Utp3. UTP25 interacts with nucleolar protein Nop19 in S. cerevisiae, and Nop19p is essential for the incorporation of Utp25p into pre-ribosomes.


Pssm-ID: 369113  Cd Length: 471  Bit Score: 49.18  E-value: 8.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013  341 DILIATP-G-RLI----DHLHNCPSFhLSSIEVLILDEADRMLD---EYFEEQMKEI--------------IRM------ 391
Cdd:pfam06862 161 DIIIASPlGlRMIigneDKKKRDFDF-LSSIEVLIVDQADSIEMqnwEHVLTVFKHLnlipkeshgcdfsrVRMwyldgq 239
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 116497013  392 CSHHRQTMLFSATMTDEVKDLASVSLKN---PVRIFVNSNT----DVAPFLRQEFIRI 442
Cdd:pfam06862 240 AKYYRQTIVFSSYITPEINSLFNSKCHNiagKVRVKPIYKGgsigQVGLKVRQVFQRF 297
PRK09751 PRK09751
putative ATP-dependent helicase Lhr; Provisional
262-553 8.34e-06

putative ATP-dependent helicase Lhr; Provisional


Pssm-ID: 137505 [Multi-domain]  Cd Length: 1490  Bit Score: 49.54  E-value: 8.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013  262 AATGTGKTAAFALPVLERLIYK-------PRQAPVTRVLVLVPTRELG--------IQVHSVT----RQLAQFCNITTCL 322
Cdd:PRK09751    3 APTGSGKTLAAFLYALDRLFREggedtreAHKRKTSRILYISPIKALGtdvqrnlqIPLKGIAderrRRGETEVNLRVGI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013  323 AVGglDVKSQEAA--LRAAPDILIATPGRLIDHLHNCPSFHLSSIEVLILDE----ADRMLDEYFEEQMKEIIRMCSHHR 396
Cdd:PRK09751   83 RTG--DTPAQERSklTRNPPDILITTPESLYLMLTSRARETLRGVETVIIDEvhavAGSKRGAHLALSLERLDALLHTSA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013  397 QTMLFSATMTdEVKDLAS-------VSLKNP-------VRIF--VNSNTDVAPFLRQEFIRIRPNREGD-----REAIVA 455
Cdd:PRK09751  161 QRIGLSATVR-SASDVAAflggdrpVTVVNPpamrhpqIRIVvpVANMDDVSSVASGTGEDSHAGREGSiwpyiETGILD 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013  456 ALLTRTFTdhvMLFTQTKKQAHRMHILL---------------------------------GLMGLQVGELHGNLSQTQR 502
Cdd:PRK09751  240 EVLRHRST---IVFTNSRGLAEKLTARLnelyaarlqrspsiavdaahfestsgatsnrvqSSDVFIARSHHGSVSKEQR 316
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 116497013  503 LEALRRFKDEQIDILVATDVAARGLDIEGVKTVINFTMPNTIKHYVHRVGR 553
Cdd:PRK09751  317 AITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGR 367
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
235-427 2.22e-05

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


Pssm-ID: 350678 [Multi-domain]  Cd Length: 200  Bit Score: 45.99  E-value: 2.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 235 AMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERliykprqAPVTrvLVLVPTRELGI-QVHSVTRQLA 313
Cdd:cd17920    7 VFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLL-------DGVT--LVVSPLISLMQdQVDRLQQLGI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 314 QFCNITtclavGGLDVKSQEAALRAAP----DILIATPGRL-----IDHLHNCPSFHLssIEVLILDEA--------Drm 376
Cdd:cd17920   78 RAAALN-----STLSPEEKREVLLRIKngqyKLLYVTPERLlspdfLELLQRLPERKR--LALIVVDEAhcvsqwghD-- 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 116497013 377 ldeyFEEQMKEI--IRMCSHHRQTMLFSATMTDEVKDLASVSLK-NPVRIFVNS 427
Cdd:cd17920  149 ----FRPDYLRLgrLRRALPGVPILALTATATPEVREDILKRLGlRNPVIFRAS 198
DDXDc_reverse_gyrase cd17924
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ...
234-377 2.37e-05

DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase 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: 350682 [Multi-domain]  Cd Length: 189  Bit Score: 45.78  E-value: 2.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 234 TAMGFKqPTPIQKACIPVGLLGKDICACAATGTGKT---AAFALpvlerLIYKPRQapvtRVLVLVPTRELGIQVHSVTR 310
Cdd:cd17924   12 KKTGFP-PWGAQRTWAKRLLRGKSFAIIAPTGVGKTtfgLATSL-----YLASKGK----RSYLIFPTKSLVKQAYERLS 81
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116497013 311 QLAQFCNITTCLAV--GGLDVKSQEAALRAAP----DILIATPGRLIDHLHNCPSFHLSSIevlILDEADRML 377
Cdd:cd17924   82 KYAEKAGVEVKILVyhSRLKKKEKEELLEKIEkgdfDILVTTNQFLSKNFDLLSNKKFDFV---FVDDVDAVL 151
Cas3 COG1203
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ...
262-529 1.41e-04

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: 45.07  E-value: 1.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 262 AATGTGKT---AAFAL-----PVLERLIYkprqapvtrvlVLvPTRelgiqvhSVTRQLAQ-FCNIT-------TCLAV- 324
Cdd:COG1203  154 APTGGGKTeaaLLFALrlaakHGGRRIIY-----------AL-PFT-------SIINQTYDrLRDLFgedvllhHSLADl 214
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 325 ------GGLDVKSQEAALRA----APdILIATpgrlIDHL---------HNCPSFH--LSSieVLILDEADrMLDEYFEE 383
Cdd:COG1203  215 dlleeeEEYESEARWLKLLKelwdAP-VVVTT----IDQLfeslfsnrkGQERRLHnlANS--VIILDEVQ-AYPPYMLA 286
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 384 QMKEIIRMCSHHRQTMLF-SATMTDEVKDLasvsLKNPVRIfVNSNTDVAPFLRQEFIRIRPN-REG--DREAIVAALLT 459
Cdd:COG1203  287 LLLRLLEWLKNLGGSVILmTATLPPLLREE----LLEAYEL-IPDEPEELPEYFRAFVRKRVElKEGplSDEELAELILE 361
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116497013 460 RTFTDH-VMLFTQTKKQAHRMHILL--GLMGLQVGELHGNLSQTQRLE----ALRRFKDEQIDILVATDVAARGLDI 529
Cdd:COG1203  362 ALHKGKsVLVIVNTVKDAQELYEALkeKLPDEEVYLLHSRFCPADRSEiekeIKERLERGKPCILVSTQVVEAGVDI 438
DEXHc_RLR cd18036
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ...
253-372 1.49e-04

DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members 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: 350794 [Multi-domain]  Cd Length: 204  Bit Score: 43.62  E-value: 1.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 253 LLGKDICACAATGTGKTAAFALPVLERLIYKPRQAPVTRVLVLVPtrelgiQVHSVTRQLAQFCNIttCLAV-------G 325
Cdd:cd18036   15 LRGKNTIICAPTGSGKTRVAVYICRHHLEKRRSAGEKGRVVVLVN------KVPLVEQQLEKFFKY--FRKGykvtglsG 86
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 116497013 326 GLDVKSQEAALRAAPDILIATPGRLIDHLHN---CPSFHLSSIEVLILDE 372
Cdd:cd18036   87 DSSHKVSFGQIVKASDVIICTPQILINNLLSgreEERVYLSDFSLLIFDE 136
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
255-347 4.07e-04

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: 41.80  E-value: 4.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 255 GKDICACAATGTGKTAAFALPVLERLiYKPRQAPVtRVLVLVPTRELGIQVHsvtRQLAQFCN-ITTCLAVG---GlDVK 330
Cdd:cd17922    1 GRNVLIAAPTGSGKTEAAFLPALSSL-ADEPEKGV-QVLYISPLKALINDQE---RRLEEPLDeIDLEIPVAvrhG-DTS 74
                         90
                 ....*....|....*....
gi 116497013 331 SQE--AALRAAPDILIATP 347
Cdd:cd17922   75 QSEkaKQLKNPPGILITTP 93
RecG COG1200
RecG-like helicase [Replication, recombination and repair];
487-532 8.17e-04

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


Pssm-ID: 440813 [Multi-domain]  Cd Length: 684  Bit Score: 42.73  E-value: 8.17e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 116497013 487 GLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVaargldIE-GV 532
Cdd:COG1200  503 GLRVGLLHGRMKPAEKDAVMAAFKAGEIDVLVATTV------IEvGV 543
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
451-559 1.09e-03

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: 40.31  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 451 EAIVAALLTRTF-TDHVMLFTQTKKQAHRMHILLGLMGLqvgelHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDI 529
Cdd:cd18789   36 LRALEELLKRHEqGDKIIVFTDNVEALYRYAKRLLKPFI-----TGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDL 110
                         90       100       110
                 ....*....|....*....|....*....|..
gi 116497013 530 --EGVKTVINFTMPNTiKHYVHRVGRTARAGR 559
Cdd:cd18789  111 peANVAIQISGHGGSR-RQEAQRLGRILRPKK 141
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
487-561 1.89e-03

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 41.62  E-value: 1.89e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116497013 487 GLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKTVINFTMPNTIKHYVHrvgRTARAGRAG 561
Cdd:PRK11057 260 GISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQ---ETGRAGRDG 331
ResIII pfam04851
Type III restriction enzyme, res subunit;
256-404 2.57e-03

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 39.19  E-value: 2.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013  256 KDICACAATGTGKTA-AFALPvlERLIykpRQAPVTRVLVLVPTRELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEA 334
Cdd:pfam04851  24 KRGLIVMATGSGKTLtAAKLI--ARLF---KKGPIKKVLFLVPRKDLLEQALEEFKKFLPNYVEIGEIISGDKKDESVDD 98
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116497013  335 AlraapDILIATPGRLIDHLHNCP-SFHLSSIEVLILDEADRmldeYFEEQMKEIIRMCSHhrQTML-FSAT 404
Cdd:pfam04851  99 N-----KIVVTTIQSLYKALELASlELLPDFFDVIIIDEAHR----SGASSYRNILEYFKP--AFLLgLTAT 159
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
488-529 3.30e-03

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: 38.86  E-value: 3.30e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 116497013 488 LQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDI 529
Cdd:cd18811   62 LNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDV 103
AAA_22 pfam13401
AAA domain;
258-383 4.44e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 38.09  E-value: 4.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013  258 ICACAATGTGKTAafalpVLERLIYKPRQAPVTRVLVLVPtrelgiqvHSVTRQ--LAQFCNITTCLAVGGLDVKsqeaA 335
Cdd:pfam13401   8 LVLTGESGTGKTT-----LLRRLLEQLPEVRDSVVFVDLP--------SGTSPKdlLRALLRALGLPLSGRLSKE----E 70
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 116497013  336 LRAapdiliatpgRLIDHLHncpsfHLSSIEVLILDEADRMLDEYFEE 383
Cdd:pfam13401  71 LLA----------ALQQLLL-----ALAVAVVLIIDEAQHLSLEALEE 103
PRK10917 PRK10917
ATP-dependent DNA helicase RecG; Provisional
487-532 4.62e-03

ATP-dependent DNA helicase RecG; Provisional


Pssm-ID: 236794 [Multi-domain]  Cd Length: 681  Bit Score: 40.52  E-value: 4.62e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 116497013 487 GLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVaargldIE-GV 532
Cdd:PRK10917 505 ELRVGLLHGRMKPAEKDAVMAAFKAGEIDILVATTV------IEvGV 545
DEXHc_RE_I_III_res cd18032
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ...
262-382 4.99e-03

DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs are members 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: 350790 [Multi-domain]  Cd Length: 163  Bit Score: 38.70  E-value: 4.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 262 AATGTGKT--AAFalpvlerLIYK-PRQAPVTRVLVLVPTRELGIQVHSvtrqlaQFCNITTCLAVGGLDVKSQEAALRa 338
Cdd:cd18032   27 MATGTGKTytAAF-------LIKRlLEANRKKRILFLAHREELLEQAER------SFKEVLPDGSFGNLKGGKKKPDDA- 92
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 116497013 339 apDILIATPGRL--IDHLHNCPSFHLSSIevlILDEADR-------MLDEYFE 382
Cdd:cd18032   93 --RVVFATVQTLnkRKRLEKFPPDYFDLI---IIDEAHHaiassyrKILEYFE 140
PLN03137 PLN03137
ATP-dependent DNA helicase; Q4-like; Provisional
494-567 6.73e-03

ATP-dependent DNA helicase; Q4-like; Provisional


Pssm-ID: 215597 [Multi-domain]  Cd Length: 1195  Bit Score: 40.26  E-value: 6.73e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116497013  494 HGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKTVINFTMPNTIKHYVHRVGrtaRAGRAGRSVSLV 567
Cdd:PLN03137  711 HGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQECG---RAGRDGQRSSCV 781
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
262-380 8.76e-03

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: 38.26  E-value: 8.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116497013 262 AATGTGKTAAFALPVLERLIYKPrqapvTRVLVLVPTRELGIQvHSvtRQLAQFCNIT-TCLAVGGLDVKSQEAALRAAP 340
Cdd:cd18035   23 LPTGLGKTIIAILVAADRLTKKG-----GKVLILAPSRPLVEQ-HA--ENLKRVLNIPdKITSLTGEVKPEERAERWDAS 94
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 116497013 341 DILIATPGRLIDHLHNcPSFHLSSIEVLILDEADRMLDEY 380
Cdd:cd18035   95 KIIVATPQVIENDLLA-GRITLDDVSLLIFDEAHHAVGNY 133
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
466-541 9.52e-03

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 39.44  E-value: 9.52e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116497013 466 VMLFTQTKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQ--IDILVATDVAARGLDIEGVKTVINFTMP 541
Cdd:COG0553  552 VLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeaPVFLISLKAGGEGLNLTAADHVIHYDLW 629
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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