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Conserved domains on  [gi|19112388|ref|NP_595596|]
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ATP-dependent RNA helicase Mss116 [Schizosaccharomyces pombe]

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
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
45-250 1.33e-97

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: 294.49  E-value: 1.33e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  45 LSSTFKNSLSRAGFEKMTPVQQRVLNEVFPNEENAVVQAKTGTGKTLAFLLVAFKDVLKGKPRLNSSKIHSVILSPTREL 124
Cdd:cd17964   1 LDPSLLKALTRMGFETMTPVQQKTLKPILSTGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSGVSALIISPTREL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 125 ALQIFEEARKLTYG-TGIRVSYAIGGNSKMREENAIRRGNANLLIATPGRLEDHLQNPRILESLS-TDSFILDEADRLMD 202
Cdd:cd17964  81 ALQIAAEAKKLLQGlRKLRVQSAVGGTSRRAELNRLRRGRPDILVATPGRLIDHLENPGVAKAFTdLDYLVLDEADRLLD 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 19112388 203 MGFAESILNIHEAVTT---TKTRKLCFSATMPPKVSNVFRGILGTDFKLIN 250
Cdd:cd17964 161 MGFRPDLEQILRHLPEknaDPRQTLLFSATVPDEVQQIARLTLKKDYKFID 211
SrmB super family cl33924
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
45-468 3.32e-92

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


The actual alignment was detected with superfamily member COG0513:

Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 288.20  E-value: 3.32e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  45 LSSTFKNSLSRAGFEKMTPVQQrvlnEVFP---NEENAVVQAKTGTGKTLAFLLVAFKDVLKGKPRlnssKIHSVILSPT 121
Cdd:COG0513   9 LSPPLLKALAELGYTTPTPIQA----QAIPlilAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPR----APQALILAPT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 122 RELALQIFEEARKLTYGTGIRVSYAIGGNSKMREENAIRRGnANLLIATPGRLEDHLQNPRI-LESLSTdsFILDEADRL 200
Cdd:COG0513  81 RELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRG-VDIVVATPGRLLDLIERGALdLSGVET--LVLDEADRM 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 201 MDMGFAESILNIHEAvtTTKTRK-LCFSATMPPKVSNVFRGILgTDFKLINCLDPNepPTHERVPQFVIETK-------L 272
Cdd:COG0513 158 LDMGFIEDIERILKL--LPKERQtLLFSATMPPEIRKLAKRYL-KNPVRIEVAPEN--ATAETIEQRYYLVDkrdklelL 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 273 DKVFSSslsllqqltssNPSSRIIVFLPTISMVDFVGGVLENHlKIPCFILHSGLTTAQRRSITESFRKCQSGILFATDV 352
Cdd:COG0513 233 RRLLRD-----------EDPERAIVFCNTKRGADRLAEKLQKR-GISAAALHGDLSQGQRERALDAFRNGKIRVLVATDV 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 353 VARGMDFPNITQVVQITGPSNTDDYIHRIGRTGRAGKTGEAYLILLEQEKPFLNSIKHL---PLKRATIEPLSDqaLSTL 429
Cdd:COG0513 301 AARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLigqKIEEEELPGFEP--VEEK 378
                       410       420       430
                ....*....|....*....|....*....|....*....
gi 19112388 430 RSDIEKSSKFSRTNALKTLYGSKPHVFSGSSQRRATGKN 468
Cdd:COG0513 379 RLERLKPKIKEKLKGKKAGRGGRPGPKGERKARRGKRRR 417
 
Name Accession Description Interval E-value
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
45-250 1.33e-97

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: 294.49  E-value: 1.33e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  45 LSSTFKNSLSRAGFEKMTPVQQRVLNEVFPNEENAVVQAKTGTGKTLAFLLVAFKDVLKGKPRLNSSKIHSVILSPTREL 124
Cdd:cd17964   1 LDPSLLKALTRMGFETMTPVQQKTLKPILSTGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSGVSALIISPTREL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 125 ALQIFEEARKLTYG-TGIRVSYAIGGNSKMREENAIRRGNANLLIATPGRLEDHLQNPRILESLS-TDSFILDEADRLMD 202
Cdd:cd17964  81 ALQIAAEAKKLLQGlRKLRVQSAVGGTSRRAELNRLRRGRPDILVATPGRLIDHLENPGVAKAFTdLDYLVLDEADRLLD 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 19112388 203 MGFAESILNIHEAVTT---TKTRKLCFSATMPPKVSNVFRGILGTDFKLIN 250
Cdd:cd17964 161 MGFRPDLEQILRHLPEknaDPRQTLLFSATVPDEVQQIARLTLKKDYKFID 211
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
45-468 3.32e-92

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 288.20  E-value: 3.32e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  45 LSSTFKNSLSRAGFEKMTPVQQrvlnEVFP---NEENAVVQAKTGTGKTLAFLLVAFKDVLKGKPRlnssKIHSVILSPT 121
Cdd:COG0513   9 LSPPLLKALAELGYTTPTPIQA----QAIPlilAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPR----APQALILAPT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 122 RELALQIFEEARKLTYGTGIRVSYAIGGNSKMREENAIRRGnANLLIATPGRLEDHLQNPRI-LESLSTdsFILDEADRL 200
Cdd:COG0513  81 RELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRG-VDIVVATPGRLLDLIERGALdLSGVET--LVLDEADRM 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 201 MDMGFAESILNIHEAvtTTKTRK-LCFSATMPPKVSNVFRGILgTDFKLINCLDPNepPTHERVPQFVIETK-------L 272
Cdd:COG0513 158 LDMGFIEDIERILKL--LPKERQtLLFSATMPPEIRKLAKRYL-KNPVRIEVAPEN--ATAETIEQRYYLVDkrdklelL 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 273 DKVFSSslsllqqltssNPSSRIIVFLPTISMVDFVGGVLENHlKIPCFILHSGLTTAQRRSITESFRKCQSGILFATDV 352
Cdd:COG0513 233 RRLLRD-----------EDPERAIVFCNTKRGADRLAEKLQKR-GISAAALHGDLSQGQRERALDAFRNGKIRVLVATDV 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 353 VARGMDFPNITQVVQITGPSNTDDYIHRIGRTGRAGKTGEAYLILLEQEKPFLNSIKHL---PLKRATIEPLSDqaLSTL 429
Cdd:COG0513 301 AARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLigqKIEEEELPGFEP--VEEK 378
                       410       420       430
                ....*....|....*....|....*....|....*....
gi 19112388 430 RSDIEKSSKFSRTNALKTLYGSKPHVFSGSSQRRATGKN 468
Cdd:COG0513 379 RLERLKPKIKEKLKGKKAGRGGRPGPKGERKARRGKRRR 417
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
37-421 3.30e-50

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 178.21  E-value: 3.30e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388   37 TLFSEVaSLSSTFKNSLSRAGFEKMTPVQQrvlnEVFP---NEENAVVQAKTGTGKTLAFLLVAFKDVL------KGKPR 107
Cdd:PRK11192   1 TTFSEL-ELDESLLEALQDKGYTRPTAIQA----EAIPpalDGRDVLGSAPTGTGKTAAFLLPALQHLLdfprrkSGPPR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  108 LnsskihsVILSPTRELALQIFEEARKLTYGTGIRVSYAIGGNSKMREENAIRrGNANLLIATPGRLEDHLQ----NPRI 183
Cdd:PRK11192  76 I-------LILTPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFS-ENQDIVVATPGRLLQYIKeenfDCRA 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  184 LESLstdsfILDEADRLMDMGFAESILNIheaVTTTKTRK--LCFSATMppkvsnvfRGILGTDF--KLINclDP----N 255
Cdd:PRK11192 148 VETL-----ILDEADRMLDMGFAQDIETI---AAETRWRKqtLLFSATL--------EGDAVQDFaeRLLN--DPveveA 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  256 EPPTHER--VPQFV-----IETKLDKVfssslsllqQLTSSNPS-SRIIVFLPTISMVDFVGGVLENHlKIPCFILHSGL 327
Cdd:PRK11192 210 EPSRRERkkIHQWYyraddLEHKTALL---------CHLLKQPEvTRSIVFVRTRERVHELAGWLRKA-GINCCYLEGEM 279
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  328 TTAQRRSITESFRKCQSGILFATDVVARGMDFPNITQVVQITGPSNTDDYIHRIGRTGRAGKTGEAYLILLEQEKPFLNS 407
Cdd:PRK11192 280 VQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGK 359
                        410
                 ....*....|....*..
gi 19112388  408 IKHL---PLKRATIEPL 421
Cdd:PRK11192 360 IERYieePLKARVIDEL 376
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
62-237 9.16e-49

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: 165.88  E-value: 9.16e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388    62 TPVQQRVLNEVFPNEeNAVVQAKTGTGKTLAFLLVAFKDVlkgkpRLNSSKIHSVILSPTRELALQIFEEARKLTYGTGI 141
Cdd:pfam00270   1 TPIQAEAIPAILEGR-DVLVQAPTGSGKTLAFLLPALEAL-----DKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388   142 RVSYAIGGNSKMREENAIRrgNANLLIATPGRLEDHLQNPRILESLSTdsFILDEADRLMDMGFAESILNIHEAVtTTKT 221
Cdd:pfam00270  75 KVASLLGGDSRKEQLEKLK--GPDILVGTPGRLLDLLQERKLLKNLKL--LVLDEAHRLLDMGFGPDLEEILRRL-PKKR 149
                         170
                  ....*....|....*.
gi 19112388   222 RKLCFSATMPPKVSNV 237
Cdd:pfam00270 150 QILLLSATLPRNLEDL 165
DEXDc smart00487
DEAD-like helicases superfamily;
53-266 1.07e-42

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 151.11  E-value: 1.07e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388     53 LSRAGFEKMTPVQQRVLNEVFPNEENAVVQAKTGTGKTLAFLLVAFKDVLKGKprlnssKIHSVILSPTRELALQIFEEA 132
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGK------GGRVLVLVPTRELAEQWAEEL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388    133 RKLTYGTGIRVSYAIGGNSKMREENAIRRGNANLLIATPGRLEDHLQNPRILESlSTDSFILDEADRLMDMGFAESILNI 212
Cdd:smart00487  75 KKLGPSLGLKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLENDKLSLS-NVDLVILDEAHRLLDGGFGDQLEKL 153
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 19112388    213 HEAVTTTKtRKLCFSATMPPKVSNVFRGILGTDFKLIncldpNEPPTHERVPQF 266
Cdd:smart00487 154 LKLLPKNV-QLLLLSATPPEEIENLLELFLNDPVFID-----VGFTPLEPIEQF 201
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
263-397 2.08e-41

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: 144.96  E-value: 2.08e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 263 VPQFVIETKLDKVFSSSLSLLQQLtssNPSSRIIVFLPTISMVDFVGGVLENhLKIPCFILHSGLTTAQRRSITESFRKC 342
Cdd:cd18787   1 IKQLYVVVEEEEKKLLLLLLLLEK---LKPGKAIIFVNTKKRVDRLAELLEE-LGIKVAALHGDLSQEERERALKKFRSG 76
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 19112388 343 QSGILFATDVVARGMDFPNITQVVQITGPSNTDDYIHRIGRTGRAGKTGEAYLIL 397
Cdd:cd18787  77 KVRVLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
290-388 2.98e-26

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: 103.06  E-value: 2.98e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388   290 NPSSRIIVFLPTISMVDFvgGVLENHLKIPCFILHSGLTTAQRRSITESFRKCQSGILFATDVVARGMDFPNITQVVQIT 369
Cdd:pfam00271  13 ERGGKVLIFSQTKKTLEA--ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDLVINYD 90
                          90
                  ....*....|....*....
gi 19112388   370 GPSNTDDYIHRIGRTGRAG 388
Cdd:pfam00271  91 LPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
314-388 1.05e-21

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 89.19  E-value: 1.05e-21
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19112388    314 NHLKIPCFILHSGLTTAQRRSITESFRKCQSGILFATDVVARGMDFPNITQVVQITGPSNTDDYIHRIGRTGRAG 388
Cdd:smart00490   8 KELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
63-434 2.76e-17

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 85.08  E-value: 2.76e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  63 PVQQRVLNEVF----PNEENAVVQAKTGTGKTLAFLLVAFKdvLKGKPRLnsskihsVILSPTRELALQIFEEARKLTYG 138
Cdd:COG1061  83 PYQQEALEALLaaleRGGGRGLVVAPTGTGKTVLALALAAE--LLRGKRV-------LVLVPRRELLEQWAEELRRFLGD 153
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 139 TGIrvsyaiGGNSKMREenairrgnANLLIATPGRLEDHLQnpriLESLStDSF---ILDEADRLMDMGFAESILNIHea 215
Cdd:COG1061 154 PLA------GGGKKDSD--------APITVATYQSLARRAH----LDELG-DRFglvIIDEAHHAGAPSYRRILEAFP-- 212
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 216 vtttKTRKLCFSATmP------PKVSNVFRGIL-GTDFK-LIN--------CLDPNEPPTHERVPQFVIETKLDKVFSSS 279
Cdd:COG1061 213 ----AAYRLGLTAT-PfrsdgrEILLFLFDGIVyEYSLKeAIEdgylappeYYGIRVDLTDERAEYDALSERLREALAAD 287
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 280 LSLLQQ-----LTSSNPSSRIIVFLPTISMVDFVGGVLENHlKIPCFILHSGLTTAQRRSITESFRKCQSGILFATDVVA 354
Cdd:COG1061 288 AERKDKilrelLREHPDDRKTLVFCSSVDHAEALAELLNEA-GIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLN 366
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 355 RGMDFPNITQVVQITGPSNTDDYIHRIGRTGRAGKTGE-AYLILL-----EQEKPFLNSIKHLPLKRATIEPLSDQALST 428
Cdd:COG1061 367 EGVDVPRLDVAILLRPTGSPREFIQRLGRGLRPAPGKEdALVYDFvgndvPVLEELAKDLRDLAGYRVEFLDEEESEELA 446

                ....*.
gi 19112388 429 LRSDIE 434
Cdd:COG1061 447 LLIAVK 452
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
324-395 2.71e-05

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 47.02  E-value: 2.71e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19112388  324 HSGLTTAQRRSITESFRKCQSGILFATdvVARGMDF--PNITQVVQITGPSNTDDYIHRIGRTGRAGKTGEAYL 395
Cdd:PRK11057 267 HAGLDNDVRADVQEAFQRDDLQIVVAT--VAFGMGInkPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAML 338
 
Name Accession Description Interval E-value
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
45-250 1.33e-97

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: 294.49  E-value: 1.33e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  45 LSSTFKNSLSRAGFEKMTPVQQRVLNEVFPNEENAVVQAKTGTGKTLAFLLVAFKDVLKGKPRLNSSKIHSVILSPTREL 124
Cdd:cd17964   1 LDPSLLKALTRMGFETMTPVQQKTLKPILSTGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSGVSALIISPTREL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 125 ALQIFEEARKLTYG-TGIRVSYAIGGNSKMREENAIRRGNANLLIATPGRLEDHLQNPRILESLS-TDSFILDEADRLMD 202
Cdd:cd17964  81 ALQIAAEAKKLLQGlRKLRVQSAVGGTSRRAELNRLRRGRPDILVATPGRLIDHLENPGVAKAFTdLDYLVLDEADRLLD 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 19112388 203 MGFAESILNIHEAVTT---TKTRKLCFSATMPPKVSNVFRGILGTDFKLIN 250
Cdd:cd17964 161 MGFRPDLEQILRHLPEknaDPRQTLLFSATVPDEVQQIARLTLKKDYKFID 211
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
45-468 3.32e-92

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 288.20  E-value: 3.32e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  45 LSSTFKNSLSRAGFEKMTPVQQrvlnEVFP---NEENAVVQAKTGTGKTLAFLLVAFKDVLKGKPRlnssKIHSVILSPT 121
Cdd:COG0513   9 LSPPLLKALAELGYTTPTPIQA----QAIPlilAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPR----APQALILAPT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 122 RELALQIFEEARKLTYGTGIRVSYAIGGNSKMREENAIRRGnANLLIATPGRLEDHLQNPRI-LESLSTdsFILDEADRL 200
Cdd:COG0513  81 RELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRG-VDIVVATPGRLLDLIERGALdLSGVET--LVLDEADRM 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 201 MDMGFAESILNIHEAvtTTKTRK-LCFSATMPPKVSNVFRGILgTDFKLINCLDPNepPTHERVPQFVIETK-------L 272
Cdd:COG0513 158 LDMGFIEDIERILKL--LPKERQtLLFSATMPPEIRKLAKRYL-KNPVRIEVAPEN--ATAETIEQRYYLVDkrdklelL 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 273 DKVFSSslsllqqltssNPSSRIIVFLPTISMVDFVGGVLENHlKIPCFILHSGLTTAQRRSITESFRKCQSGILFATDV 352
Cdd:COG0513 233 RRLLRD-----------EDPERAIVFCNTKRGADRLAEKLQKR-GISAAALHGDLSQGQRERALDAFRNGKIRVLVATDV 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 353 VARGMDFPNITQVVQITGPSNTDDYIHRIGRTGRAGKTGEAYLILLEQEKPFLNSIKHL---PLKRATIEPLSDqaLSTL 429
Cdd:COG0513 301 AARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLigqKIEEEELPGFEP--VEEK 378
                       410       420       430
                ....*....|....*....|....*....|....*....
gi 19112388 430 RSDIEKSSKFSRTNALKTLYGSKPHVFSGSSQRRATGKN 468
Cdd:COG0513 379 RLERLKPKIKEKLKGKKAGRGGRPGPKGERKARRGKRRR 417
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
51-242 5.34e-58

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: 191.50  E-value: 5.34e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  51 NSLSRAGFEKMTPVQQRVLNEVFpNEENAVVQAKTGTGKTLAFLLVAFkDVLKGKPRLNSSKIHSVILSPTRELALQIFE 130
Cdd:cd00268   3 KALKKLGFEKPTPIQAQAIPLIL-SGRDVIGQAQTGSGKTLAFLLPIL-EKLLPEPKKKGRGPQALVLAPTRELAMQIAE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 131 EARKLTYGTGIRVSYAIGGNSKMREENAIRRGnANLLIATPGRLEDHLQNPRI-LESLSTdsFILDEADRLMDMGFAESI 209
Cdd:cd00268  81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKG-PDIVVGTPGRLLDLIERGKLdLSNVKY--LVLDEADRMLDMGFEEDV 157
                       170       180       190
                ....*....|....*....|....*....|...
gi 19112388 210 LNIHEAvTTTKTRKLCFSATMPPKVSNVFRGIL 242
Cdd:cd00268 158 EKILSA-LPKDRQTLLFSATLPEEVKELAKKFL 189
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
37-421 3.30e-50

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 178.21  E-value: 3.30e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388   37 TLFSEVaSLSSTFKNSLSRAGFEKMTPVQQrvlnEVFP---NEENAVVQAKTGTGKTLAFLLVAFKDVL------KGKPR 107
Cdd:PRK11192   1 TTFSEL-ELDESLLEALQDKGYTRPTAIQA----EAIPpalDGRDVLGSAPTGTGKTAAFLLPALQHLLdfprrkSGPPR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  108 LnsskihsVILSPTRELALQIFEEARKLTYGTGIRVSYAIGGNSKMREENAIRrGNANLLIATPGRLEDHLQ----NPRI 183
Cdd:PRK11192  76 I-------LILTPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFS-ENQDIVVATPGRLLQYIKeenfDCRA 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  184 LESLstdsfILDEADRLMDMGFAESILNIheaVTTTKTRK--LCFSATMppkvsnvfRGILGTDF--KLINclDP----N 255
Cdd:PRK11192 148 VETL-----ILDEADRMLDMGFAQDIETI---AAETRWRKqtLLFSATL--------EGDAVQDFaeRLLN--DPveveA 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  256 EPPTHER--VPQFV-----IETKLDKVfssslsllqQLTSSNPS-SRIIVFLPTISMVDFVGGVLENHlKIPCFILHSGL 327
Cdd:PRK11192 210 EPSRRERkkIHQWYyraddLEHKTALL---------CHLLKQPEvTRSIVFVRTRERVHELAGWLRKA-GINCCYLEGEM 279
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  328 TTAQRRSITESFRKCQSGILFATDVVARGMDFPNITQVVQITGPSNTDDYIHRIGRTGRAGKTGEAYLILLEQEKPFLNS 407
Cdd:PRK11192 280 VQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGK 359
                        410
                 ....*....|....*..
gi 19112388  408 IKHL---PLKRATIEPL 421
Cdd:PRK11192 360 IERYieePLKARVIDEL 376
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
50-239 4.88e-49

DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350718 [Multi-domain]  Cd Length: 202  Bit Score: 168.14  E-value: 4.88e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  50 KNSLSRAGFEKMTPVQQRVlNEVFPNEENAVVQAKTGTGKTLAFLLVAFKDVLKGKPRLNSSKIHSVILSPTRELALQIF 129
Cdd:cd17960   2 LDVVAELGFTSMTPVQAAT-IPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANLKKGQVGALIISPTRELATQIY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 130 EEARKLT--YGTGIRVSYAIGGNSKMREENAIRRGNANLLIATPGRLEDHLQNPRILESLST-DSFILDEADRLMDMGFA 206
Cdd:cd17960  81 EVLQSFLehHLPKLKCQLLIGGTNVEEDVKKFKRNGPNILVGTPGRLEELLSRKADKVKVKSlEVLVLDEADRLLDLGFE 160
                       170       180       190
                ....*....|....*....|....*....|....*
gi 19112388 207 ESILNIHEAVttTKTRK--LcFSATMPPKVSNVFR 239
Cdd:cd17960 161 ADLNRILSKL--PKQRRtgL-FSATQTDAVEELIK 192
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
62-237 9.16e-49

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: 165.88  E-value: 9.16e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388    62 TPVQQRVLNEVFPNEeNAVVQAKTGTGKTLAFLLVAFKDVlkgkpRLNSSKIHSVILSPTRELALQIFEEARKLTYGTGI 141
Cdd:pfam00270   1 TPIQAEAIPAILEGR-DVLVQAPTGSGKTLAFLLPALEAL-----DKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388   142 RVSYAIGGNSKMREENAIRrgNANLLIATPGRLEDHLQNPRILESLSTdsFILDEADRLMDMGFAESILNIHEAVtTTKT 221
Cdd:pfam00270  75 KVASLLGGDSRKEQLEKLK--GPDILVGTPGRLLDLLQERKLLKNLKL--LVLDEAHRLLDMGFGPDLEEILRRL-PKKR 149
                         170
                  ....*....|....*.
gi 19112388   222 RKLCFSATMPPKVSNV 237
Cdd:pfam00270 150 QILLLSATLPRNLEDL 165
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
53-429 1.41e-45

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 168.59  E-value: 1.41e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388   53 LSRAGFEKMTPVQQRVLNEVFPNEENAVvQAKTGTGKTLAFLlVAFKDVLKGKPRLNSSKIH---SVILSPTRELALQIF 129
Cdd:PRK04537  24 LESAGFTRCTPIQALTLPVALPGGDVAG-QAQTGTGKTLAFL-VAVMNRLLSRPALADRKPEdprALILAPTRELAIQIH 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  130 EEARKLTYGTGIRVSYAIGGNSKMREENAIRRGnANLLIATPGRLEDHLQNPRILESLSTDSFILDEADRLMDMGFAESI 209
Cdd:PRK04537 102 KDAVKFGADLGLRFALVYGGVDYDKQRELLQQG-VDVIIATPGRLIDYVKQHKVVSLHACEICVLDEADRMFDLGFIKDI 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  210 LNIHEAVTTTKTRK-LCFSATMPPKVSNVFRGILGTDFKLINcldPNEPPTHERVPQFVI----ETKLDKVFSSSLSllq 284
Cdd:PRK04537 181 RFLLRRMPERGTRQtLLFSATLSHRVLELAYEHMNEPEKLVV---ETETITAARVRQRIYfpadEEKQTLLLGLLSR--- 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  285 qltssNPSSRIIVFLPTISMVDFVGGVLENHlKIPCFILHSGLTTAQRRSITESFRKCQSGILFATDVVARGMDFPNITQ 364
Cdd:PRK04537 255 -----SEGARTMVFVNTKAFVERVARTLERH-GYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKY 328
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19112388  365 VVQITGPSNTDDYIHRIGRTGRAGKTGEAYLILLEQEKPFLNSIKHLPLKRATIEPLSDQALSTL 429
Cdd:PRK04537 329 VYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYIEQKIPVEPVTAELLTPL 393
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
45-429 7.60e-45

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 164.70  E-value: 7.60e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388   45 LSSTFKNSLSRAGFEKMTPVQQRVLNEVFPNEEnAVVQAKTGTGKTLAFLLVAFKDVLK---------GKPRlnsskihS 115
Cdd:PRK01297  94 LAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHD-AIGRAQTGTGKTAAFLISIINQLLQtpppkerymGEPR-------A 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  116 VILSPTRELALQIFEEARKLTYGTGIRVSYAIGGNSKMREENAIRRGNANLLIATPGRLEDHLQNPRILESLsTDSFILD 195
Cdd:PRK01297 166 LIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEARFCDILVATPGRLLDFNQRGEVHLDM-VEVMVLD 244
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  196 EADRLMDMGFAESILNIHEAVTTTKTRK-LCFSATMPPKVSNVFRGILgTDFKLINcLDPnEPPTHERVPQFV-IETKLD 273
Cdd:PRK01297 245 EADRMLDMGFIPQVRQIIRQTPRKEERQtLLFSATFTDDVMNLAKQWT-TDPAIVE-IEP-ENVASDTVEQHVyAVAGSD 321
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  274 KVfssslSLLQQLTSSNPSSRIIVFLPTISMVDfvggVLENHLK---IPCFILHSGLTTAQRRSITESFRKCQSGILFAT 350
Cdd:PRK01297 322 KY-----KLLYNLVTQNPWERVMVFANRKDEVR----RIEERLVkdgINAAQLSGDVPQHKRIKTLEGFREGKIRVLVAT 392
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19112388  351 DVVARGMDFPNITQVVQITGPSNTDDYIHRIGRTGRAGKTGEAYLILLEQEKPFLNSIKHLPLKRATIEPLSDQALSTL 429
Cdd:PRK01297 393 DVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKISCEMPPAELLKPV 471
PTZ00110 PTZ00110
helicase; Provisional
52-397 8.29e-45

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 166.10  E-value: 8.29e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388   52 SLSRAGFEKMTPVQQrvlnEVFP---NEENAVVQAKTGTGKTLAFLLVAFKDVLkGKPRLNSSKIHSV-ILSPTRELALQ 127
Cdd:PTZ00110 144 SLKNAGFTEPTPIQV----QGWPialSGRDMIGIAETGSGKTLAFLLPAIVHIN-AQPLLRYGDGPIVlVLAPTRELAEQ 218
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  128 IFEEARKLTYGTGIRVSYAIGGNSKMREENAIRRGnANLLIATPGRLEDhlqnprILESLSTD-----SFILDEADRLMD 202
Cdd:PTZ00110 219 IREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRG-VEILIACPGRLID------FLESNVTNlrrvtYLVLDEADRMLD 291
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  203 MGFAESILNIHEAVTTTKtRKLCFSATMPPKVSNVFRGILGTDFKLIN--CLDPNeppTHERVPQ--FVIETKLDKVfss 278
Cdd:PTZ00110 292 MGFEPQIRKIVSQIRPDR-QTLMWSATWPKEVQSLARDLCKEEPVHVNvgSLDLT---ACHNIKQevFVVEEHEKRG--- 364
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  279 sLSLLQQLTSSNPSSRIIVFLPTISMVDFvggvLENHLKI---PCFILHSGLTTAQRRSITESFRKCQSGILFATDVVAR 355
Cdd:PTZ00110 365 -KLKMLLQRIMRDGDKILIFVETKKGADF----LTKELRLdgwPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASR 439
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 19112388  356 GMDFPNITQVVQITGPSNTDDYIHRIGRTGRAGKTGEAYLIL 397
Cdd:PTZ00110 440 GLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFL 481
DEXDc smart00487
DEAD-like helicases superfamily;
53-266 1.07e-42

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 151.11  E-value: 1.07e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388     53 LSRAGFEKMTPVQQRVLNEVFPNEENAVVQAKTGTGKTLAFLLVAFKDVLKGKprlnssKIHSVILSPTRELALQIFEEA 132
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGK------GGRVLVLVPTRELAEQWAEEL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388    133 RKLTYGTGIRVSYAIGGNSKMREENAIRRGNANLLIATPGRLEDHLQNPRILESlSTDSFILDEADRLMDMGFAESILNI 212
Cdd:smart00487  75 KKLGPSLGLKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLENDKLSLS-NVDLVILDEAHRLLDGGFGDQLEKL 153
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 19112388    213 HEAVTTTKtRKLCFSATMPPKVSNVFRGILGTDFKLIncldpNEPPTHERVPQF 266
Cdd:smart00487 154 LKLLPKNV-QLLLLSATPPEEIENLLELFLNDPVFID-----VGFTPLEPIEQF 201
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
54-237 1.31e-42

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: 151.20  E-value: 1.31e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  54 SRAGFEKMTPVQQRVLNEVFpNEENAVVQAKTGTGKTLAFLLVAFKDVLKGKPRLN-SSKIHSVILSPTRELALQIFEEA 132
Cdd:cd17949   7 SKMGIEKPTAIQKLAIPVLL-QGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRVDrSDGTLALVLVPTRELALQIYEVL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 133 RKLT-YGTGIRVSYAIGGNSKMREENAIRRGnANLLIATPGRLEDHLQNPRILESLSTDSFILDEADRLMDMGFAESILN 211
Cdd:cd17949  86 EKLLkPFHWIVPGYLIGGEKRKSEKARLRKG-VNILIATPGRLLDHLKNTQSFDVSNLRWLVLDEADRLLDMGFEKDITK 164
                       170       180
                ....*....|....*....|....*.
gi 19112388 212 IHEAVtTTKTRKLCFSATMPPKVSNV 237
Cdd:cd17949 165 ILELL-DDKRSKAGGEKSKPSRRQTV 189
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
39-234 1.16e-41

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: 148.79  E-value: 1.16e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  39 FSEvASLSSTFKNSLSRAGFEKMTPVQQRVLnevfPneenAVVQ-------AKTGTGKTLAFLLVAFKDVLKGKPRLNSS 111
Cdd:cd17967   2 FEE-AGLRELLLENIKRAGYTKPTPVQKYAI----P----IILAgrdlmacAQTGSGKTAAFLLPIISKLLEDGPPSVGR 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 112 KIHS-----VILSPTRELALQIFEEARKLTYGTGIRVSYAIGGNSKMREENAIRRGnANLLIATPGRLEDHLQNPRIleS 186
Cdd:cd17967  73 GRRKaypsaLILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRG-CDILVATPGRLVDFIERGRI--S 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 19112388 187 LSTDSF-ILDEADRLMDMGFAESILNIHEAVTTTKTRK---LCFSATMPPKV 234
Cdd:cd17967 150 LSSIKFlVLDEADRMLDMGFEPQIRKIVEHPDMPPKGErqtLMFSATFPREI 201
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
263-397 2.08e-41

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: 144.96  E-value: 2.08e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 263 VPQFVIETKLDKVFSSSLSLLQQLtssNPSSRIIVFLPTISMVDFVGGVLENhLKIPCFILHSGLTTAQRRSITESFRKC 342
Cdd:cd18787   1 IKQLYVVVEEEEKKLLLLLLLLEK---LKPGKAIIFVNTKKRVDRLAELLEE-LGIKVAALHGDLSQEERERALKKFRSG 76
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 19112388 343 QSGILFATDVVARGMDFPNITQVVQITGPSNTDDYIHRIGRTGRAGKTGEAYLIL 397
Cdd:cd18787  77 KVRVLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
36-246 4.47e-41

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: 148.96  E-value: 4.47e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  36 PTLFSEvASLSSTFKNSLSRAGFEKMTPVQQRVLNEVFPNEEnAVVQAKTGTGKTLAFLLVAFKDVLKGKPRLNSSKI-- 113
Cdd:cd18052  42 ILTFEE-ANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRD-LMACAQTGSGKTAAFLLPVLTGMMKEGLTASSFSEvq 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 114 --HSVILSPTRELALQIFEEARKLTYGTGIRVSYAIGGNSKMREENAIRRGnANLLIATPGRLEDHLQNPRIleSLSTDS 191
Cdd:cd18052 120 epQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKG-CHILVATPGRLLDFIGRGKI--SLSKLK 196
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 19112388 192 F-ILDEADRLMDMGFA---ESILNIHEAVTTTKTRKLCFSATMPPKVSNVFRGILGTDF 246
Cdd:cd18052 197 YlILDEADRMLDMGFGpeiRKLVSEPGMPSKEDRQTLMFSATFPEEIQRLAAEFLKEDY 255
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
35-422 1.37e-39

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 149.57  E-value: 1.37e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388   35 QPTLFSEVAsLSSTFKNSLSRAGFEKMTPVQQRVLNEVFpNEENAVVQAKTGTGKTLAF---LLvafkdvlkgkPRLNSS 111
Cdd:PRK11776   2 SMTAFSTLP-LPPALLANLNELGYTEMTPIQAQSLPAIL-AGKDVIAQAKTGSGKTAAFglgLL----------QKLDVK 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  112 --KIHSVILSPTRELALQIFEEARKLTYGT-GIRVSYAIGGNSkMREE-NAIRRGnANLLIATPGRLEDHLQNPRI-LES 186
Cdd:PRK11776  70 rfRVQALVLCPTRELADQVAKEIRRLARFIpNIKVLTLCGGVP-MGPQiDSLEHG-AHIIVGTPGRILDHLRKGTLdLDA 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  187 LSTdsFILDEADRLMDMGFAESILNIHEAvtTTKTRK-LCFSATMPPKVSNVFRGILgTDFKLINCLDPNEPPTHErvpQ 265
Cdd:PRK11776 148 LNT--LVLDEADRMLDMGFQDAIDAIIRQ--APARRQtLLFSATYPEGIAAISQRFQ-RDPVEVKVESTHDLPAIE---Q 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  266 FVIET----KLDKVfssslslLQQLTSSNPSSrIIVFLPTISMVDFVGGVLeNHLKIPCFILHSGLTTAQRRSITESFRK 341
Cdd:PRK11776 220 RFYEVspdeRLPAL-------QRLLLHHQPES-CVVFCNTKKECQEVADAL-NAQGFSALALHGDLEQRDRDQVLVRFAN 290
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  342 CQSGILFATDVVARGMDFPNITQVVQITGPSNTDDYIHRIGRTGRAGKTGEAYLILLEQEKPFLNSIKHL---PLKRATI 418
Cdd:PRK11776 291 RSCSVLVATDVAARGLDIKALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYlgrKLNWEPL 370

                 ....
gi 19112388  419 EPLS 422
Cdd:PRK11776 371 PSLS 374
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
51-234 3.22e-39

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: 141.57  E-value: 3.22e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  51 NSLSRAGFEKMTPVQQRVLnevfP---NEENAVVQAKTGTGKTLAFLLVAFKDVLKgkpRLNSSKIHSVILSPTRELALQ 127
Cdd:cd17957   3 NNLEESGYREPTPIQMQAI----PillHGRDLLACAPTGSGKTLAFLIPILQKLGK---PRKKKGLRALILAPTRELASQ 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 128 IFEEARKLTYGTGIRVSYAIGGNSKMREENAIRRGNANLLIATPGRLEDHLQNprILESLST-DSFILDEADRLMDMGFA 206
Cdd:cd17957  76 IYRELLKLSKGTGLRIVLLSKSLEAKAKDGPKSITKYDILVSTPLRLVFLLKQ--GPIDLSSvEYLVLDEADKLFEPGFR 153
                       170       180
                ....*....|....*....|....*...
gi 19112388 207 ESILNIHEAVTTTKTRKLCFSATMPPKV 234
Cdd:cd17957 154 EQTDEILAACTNPNLQRSLFSATIPSEV 181
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
39-444 2.12e-38

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 145.50  E-value: 2.12e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388   39 FSEVAsLSSTFKNSLSRAGFEKMTPVQQRVLNEVFPNEENAVvQAKTGTGKTLAFLLVAFKDVLKgKPRLNSSKIH---S 115
Cdd:PRK04837  10 FSDFA-LHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAG-QAQTGTGKTMAFLTATFHYLLS-HPAPEDRKVNqprA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  116 VILSPTRELALQIFEEARKLTYGTGIRVSYAIGGNSKMREENAIRRGnANLLIATPGRLEDHLQNpRILESLSTDSFILD 195
Cdd:PRK04837  87 LIMAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESG-VDILIGTTGRLIDYAKQ-NHINLGAIQVVVLD 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  196 EADRLMDMGFAESILNIHEAVTTTKTR-KLCFSATMPPKVSNVfrgilgtDFKLINclDPN----EP------------- 257
Cdd:PRK04837 165 EADRMFDLGFIKDIRWLFRRMPPANQRlNMLFSATLSYRVREL-------AFEHMN--NPEyvevEPeqktghrikeelf 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  258 -PTHE---RVPQFVIETKLdkvfssslsllqqltssnpSSRIIVFLPTISMVDFVGGVLE--NHlkipcfilHSGLTT-- 329
Cdd:PRK04837 236 yPSNEekmRLLQTLIEEEW-------------------PDRAIIFANTKHRCEEIWGHLAadGH--------RVGLLTgd 288
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  330 -AQ--RRSITESFRKCQSGILFATDVVARGMDFPNITQVVQITGPSNTDDYIHRIGRTGRAGKTGEAylILLEQEKPFLN 406
Cdd:PRK04837 289 vAQkkRLRILEEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHS--ISLACEEYALN 366
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 19112388  407 sikhLPLKRATIE---PLSDQALSTLRSDIEKSSKFSRTNA 444
Cdd:PRK04837 367 ----LPAIETYIGhsiPVSKYDSDALLTDLPKPLRLTRPRT 403
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
51-242 2.91e-37

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: 137.07  E-value: 2.91e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  51 NSLSRAGFEKMTPVQQRVLnevfPNEENA---VVQAKTGTGKTLAFLLVAFKDVLKgKPRLNSSKIHS----VILSPTRE 123
Cdd:cd17945   3 RVIRKLGYKEPTPIQRQAI----PIGLQNrdiIGIAETGSGKTAAFLIPLLVYISR-LPPLDEETKDDgpyaLILAPTRE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 124 LALQIFEEARKLTYGTGIRVSYAIGGNSKMREENAIRRGnANLLIATPGRLEDHLQNpRILESLSTDSFILDEADRLMDM 203
Cdd:cd17945  78 LAQQIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNG-CEILIATPGRLLDCLER-RLLVLNQCTYVVLDEADRMIDM 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 19112388 204 GFAESILNIHEAVTTTKTRK-------------------LCFSATMPPKVSNVFRGIL 242
Cdd:cd17945 156 GFEPQVTKILDAMPVSNKKPdteeaeklaasgkhryrqtMMFTATMPPAVEKIAKGYL 213
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
53-402 8.16e-37

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 143.00  E-value: 8.16e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388   53 LSRAGFEKMTPVQQRVLNEVFPNEeNAVVQAKTGTGKTLAFLL--VAFKDVLKGKPRLNSSKIHSVILSPTRELALQIFE 130
Cdd:PLN00206 136 LETAGYEFPTPIQMQAIPAALSGR-SLLVSADTGSGKTASFLVpiISRCCTIRSGHPSEQRNPLAMVLTPTRELCVQVED 214
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  131 EARKLTYGTGIRVSYAIGGNSKMREENAIRRGnANLLIATPGRLEDHLQNPRI-LESLSTdsFILDEADRLMDMGFAESI 209
Cdd:PLN00206 215 QAKVLGKGLPFKTALVVGGDAMPQQLYRIQQG-VELIVGTPGRLIDLLSKHDIeLDNVSV--LVLDEVDCMLERGFRDQV 291
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  210 LNIHEAVTTTKTrkLCFSATMPPKVSNvFRGILGTDFKLINCLDPNEPptHERVPQFVI----ETKLDKVFSSSLSLLQQ 285
Cdd:PLN00206 292 MQIFQALSQPQV--LLFSATVSPEVEK-FASSLAKDIILISIGNPNRP--NKAVKQLAIwvetKQKKQKLFDILKSKQHF 366
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  286 LtssnPSSriIVFLPTISMVDFVGGVLENHLKIPCFILHSGLTTAQRRSITESFRKCQSGILFATDVVARGMDFPNITQV 365
Cdd:PLN00206 367 K----PPA--VVFVSSRLGADLLANAITVVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQV 440
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 19112388  366 VQITGPSNTDDYIHRIGRTGRAGKTGEAYLILLEQEK 402
Cdd:PLN00206 441 IIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDR 477
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
53-234 6.13e-36

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: 132.76  E-value: 6.13e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  53 LSRAGFEKMTPVQQRVLNEVFpNEENAVVQAKTGTGKTLAFLLVAFKDVLKGKPRLNSSKIhsVILSPTRELALQIFEEA 132
Cdd:cd17947   5 LSSLGFTKPTPIQAAAIPLAL-LGKDICASAVTGSGKTAAFLLPILERLLYRPKKKAATRV--LVLVPTRELAMQCFSVL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 133 RKLTYGTGIRVSYAIGGNSKMREENAIRRGnANLLIATPGRLEDHLQNPRILESLSTDSFILDEADRLMDMGFAESILNI 212
Cdd:cd17947  82 QQLAQFTDITFALAVGGLSLKAQEAALRAR-PDIVIATPGRLIDHLRNSPSFDLDSIEILVLDEADRMLEEGFADELKEI 160
                       170       180
                ....*....|....*....|...
gi 19112388 213 HEAVttTKTRK-LCFSATMPPKV 234
Cdd:cd17947 161 LRLC--PRTRQtMLFSATMTDEV 181
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
45-242 1.00e-35

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: 132.89  E-value: 1.00e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  45 LSSTFKNSLSRAGFEKMTPVQQRVLNEVFpNEENAVVQAKTGTGKTLAFLLVAFKDVLKGKPRLNSSKIHSVILSPTREL 124
Cdd:cd17953  19 LSEKVLDLIKKLGYEKPTPIQAQALPAIM-SGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPVKPGEGPIGLIMAPTREL 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 125 ALQIFEEARKLTYGTGIRVSYAIGGNSKMREENAIRRGnANLLIATPGRLEDHL--QNPRILESLSTDSFILDEADRLMD 202
Cdd:cd17953  98 ALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRG-AEIVVCTPGRMIDILtaNNGRVTNLRRVTYVVLDEADRMFD 176
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 19112388 203 MGFAESILNIHEAVTTTKTRKLcFSATMPPKVSNVFRGIL 242
Cdd:cd17953 177 MGFEPQIMKIVNNIRPDRQTVL-FSATFPRKVEALARKVL 215
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
37-409 1.89e-34

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 137.67  E-value: 1.89e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388   37 TLFSEVAsLSSTFKNSLSRAGFEKMTPVQQRVLNEVFpNEENAVVQAKTGTGKTLAFLLVAFKDVlkgKPRLNSSKIhsV 116
Cdd:PRK11634   6 TTFADLG-LKAPILEALNDLGYEKPSPIQAECIPHLL-NGRDVLGMAQTGSGKTAAFSLPLLHNL---DPELKAPQI--L 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  117 ILSPTRELALQIFEEARKLT-YGTGIRVSYAIGGNSKMREENAIRRGnANLLIATPGRLEDHLQNPRI-LESLStdSFIL 194
Cdd:PRK11634  79 VLAPTRELAVQVAEAMTDFSkHMRGVNVVALYGGQRYDVQLRALRQG-PQIVVGTPGRLLDHLKRGTLdLSKLS--GLVL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  195 DEADRLMDMGFAESILNIHEAVTTTKTRKLcFSATMPPKVSNVFRGILgtdfklincldpNEPptHERVPQFVIETKLD- 273
Cdd:PRK11634 156 DEADEMLRMGFIEDVETIMAQIPEGHQTAL-FSATMPEAIRRITRRFM------------KEP--QEVRIQSSVTTRPDi 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  274 -----KVFSSSLSLLQQLTSSNPS-SRIIVFLPTISMVDFVGGVLENHlKIPCFILHSGLTTAQRRSITESFRKCQSGIL 347
Cdd:PRK11634 221 sqsywTVWGMRKNEALVRFLEAEDfDAAIIFVRTKNATLEVAEALERN-GYNSAALNGDMNQALREQTLERLKDGRLDIL 299
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19112388  348 FATDVVARGMDFPNITQVVQITGPSNTDDYIHRIGRTGRAGKTGEAYLILLEQEKPFLNSIK 409
Cdd:PRK11634 300 IATDVAARGLDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIE 361
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
45-250 5.25e-34

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: 127.81  E-value: 5.25e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  45 LSSTFKNSLSRAGFEKMTPVQQRVLNEVFPNEEnAVVQAKTGTGKTLAFLLVAFKdvlKGKPRLNSSKIHSVILSPTREL 124
Cdd:cd17959   8 LSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRD-VVAMARTGSGKTAAFLIPMIE---KLKAHSPTVGARALILSPTREL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 125 ALQIFEEARKLTYGTGIRVSYAIGGNSkMREENAIRRGNANLLIATPGRLEDHLQNPRiLESLSTDSFILDEADRLMDMG 204
Cdd:cd17959  84 ALQTLKVTKELGKFTDLRTALLVGGDS-LEEQFEALASNPDIIIATPGRLLHLLVEMN-LKLSSVEYVVFDEADRLFEMG 161
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 19112388 205 FAESILNIHEAVTTTKTRkLCFSATMPPKVSNVFRGILgTDFKLIN 250
Cdd:cd17959 162 FAEQLHEILSRLPENRQT-LLFSATLPKLLVEFAKAGL-NEPVLIR 205
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
39-246 6.10e-34

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: 129.00  E-value: 6.10e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  39 FSEVaSLSSTFKNSLSRAGFEKMTPVQQRVLnEVFPNEENAVVQAKTGTGKTLAFLLVAFKDVLKGKP---------RLN 109
Cdd:cd18051  23 FSDL-DLGEIIRNNIELARYTKPTPVQKHAI-PIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEQGPgeslpsesgYYG 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 110 SSKIH--SVILSPTRELALQIFEEARKLTYGTGIRVSYAIGG---NSKMREenaIRRGnANLLIATPGRLEDHLQNPRIl 184
Cdd:cd18051 101 RRKQYplALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGadiGQQMRD---LERG-CHLLVATPGRLVDMLERGKI- 175
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19112388 185 eSLSTDSF-ILDEADRLMDMGFAESILNIHEAVTTTKT---RKLCFSATMPPKVSnvfrgILGTDF 246
Cdd:cd18051 176 -GLDYCKYlVLDEADRMLDMGFEPQIRRIVEQDTMPPTgerQTLMFSATFPKEIQ-----MLARDF 235
PTZ00424 PTZ00424
helicase 45; Provisional
57-409 9.10e-34

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 132.26  E-value: 9.10e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388   57 GFEKMTPVQQRVLNEVFPNEENaVVQAKTGTGKTLAFLLVAFKDVlkgKPRLNSSKIhsVILSPTRELALQIFEEARKLT 136
Cdd:PTZ00424  47 GFEKPSAIQQRGIKPILDGYDT-IGQAQSGTGKTATFVIAALQLI---DYDLNACQA--LILAPTRELAQQIQKVVLALG 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  137 YGTGIRVSYAIGGNSkMREENAIRRGNANLLIATPGRLEDHLqNPRILESLSTDSFILDEADRLMDMGFAESILNIHEAV 216
Cdd:PTZ00424 121 DYLKVRCHACVGGTV-VRDDINKLKAGVHMVVGTPGRVYDMI-DKRHLRVDDLKLFILDEADEMLSRGFKGQIYDVFKKL 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  217 TTTKTRKLcFSATMPPKVSNvfrgiLGTDF----KLIncLDPNEPPTHERVPQFVI-----ETKLDKVFSSSLSLLQqlt 287
Cdd:PTZ00424 199 PPDVQVAL-FSATMPNEILE-----LTTKFmrdpKRI--LVKKDELTLEGIRQFYVavekeEWKFDTLCDLYETLTI--- 267
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  288 ssnpsSRIIVFLPTISMVDFVGGVLENHLkIPCFILHSGLTTAQRRSITESFRKCQSGILFATDVVARGMDFPNITQVVQ 367
Cdd:PTZ00424 268 -----TQAIIYCNTRRKVDYLTKKMHERD-FTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVIN 341
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 19112388  368 ITGPSNTDDYIHRIGRTGRAGKTGEAYLILLEQEKPFLNSIK 409
Cdd:PTZ00424 342 YDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIE 383
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
50-242 9.01e-33

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: 123.94  E-value: 9.01e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  50 KNSLSRAGFEKMTPVQQRVLNEVFpNEENAVVQAKTGTGKTLAFLLVAFKdvlkgkpRLNSSK------IHSVILSPTRE 123
Cdd:cd17941   2 LKGLKEAGFIKMTEIQRDSIPHAL-QGRDILGAAKTGSGKTLAFLVPLLE-------KLYRERwtpedgLGALIISPTRE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 124 LALQIFEEARKLTYGTGIRVSYAIGGNSKmrEENAIRRGNANLLIATPGRLEDHL-QNPrileSLSTDS---FILDEADR 199
Cdd:cd17941  74 LAMQIFEVLRKVGKYHSFSAGLIIGGKDV--KEEKERINRMNILVCTPGRLLQHMdETP----GFDTSNlqmLVLDEADR 147
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 19112388 200 LMDMGFAESILNIHEAVTTTKtRKLCFSATMPPKVSNVFRGIL 242
Cdd:cd17941 148 ILDMGFKETLDAIVENLPKSR-QTLLFSATQTKSVKDLARLSL 189
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
52-239 1.56e-31

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: 120.54  E-value: 1.56e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  52 SLSRAGFEKMTPVQQRVLNEVFPNEEnAVVQAKTGTGKTLAFLLVAFKDV--LKGKPRlNSSKIhsVILSPTRELALQIF 129
Cdd:cd17942   4 AIEEMGFTKMTEIQAKSIPPLLEGRD-VLGAAKTGSGKTLAFLIPAIELLykLKFKPR-NGTGV--IIISPTRELALQIY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 130 EEARKL------TYGTgirvsyAIGGNSKMREENAIRRGnANLLIATPGRLEDHLQNPRILESLSTDSFILDEADRLMDM 203
Cdd:cd17942  80 GVAKELlkyhsqTFGI------VIGGANRKAEAEKLGKG-VNILVATPGRLLDHLQNTKGFLYKNLQCLIIDEADRILEI 152
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 19112388 204 GFAESILNIHEAVTTTKTRKLcFSATMPPKVSNVFR 239
Cdd:cd17942 153 GFEEEMRQIIKLLPKRRQTML-FSATQTRKVEDLAR 187
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
51-242 1.57e-31

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: 120.60  E-value: 1.57e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  51 NSLSRAGFEKMTPVQQRVLNEVFPNEeNAVVQAKTGTGKTLAFLLVAFKDVLKGKPRLNSSKIHSVILSPTRELALQIFE 130
Cdd:cd17952   3 NAIRKQEYEQPTPIQAQALPVALSGR-DMIGIAKTGSGKTAAFIWPMLVHIMDQRELEKGEGPIAVIVAPTRELAQQIYL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 131 EARKLTYGTGIRVSYAIGGNSKMREENAIRRGnANLLIATPGRLEDHLQNpRILESLSTDSFILDEADRLMDMGFAESIL 210
Cdd:cd17952  82 EAKKFGKAYNLRVVAVYGGGSKWEQAKALQEG-AEIVVATPGRLIDMVKK-KATNLQRVTYLVLDEADRMFDMGFEYQVR 159
                       170       180       190
                ....*....|....*....|....*....|..
gi 19112388 211 NIHEAVTTTKtRKLCFSATMPPKVSNVFRGIL 242
Cdd:cd17952 160 SIVGHVRPDR-QTLLFSATFKKKIEQLARDIL 190
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
54-242 4.15e-31

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: 119.73  E-value: 4.15e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  54 SRAGFEKMTPVQQrvlnEVFP---NEENAVVQAKTGTGKTLAFLLVAFKDVLKGKPRLnsskiHSVILSPTRELALQIFE 130
Cdd:cd17954  16 EKLGWKKPTKIQE----EAIPvalQGRDIIGLAETGSGKTAAFALPILQALLENPQRF-----FALVLAPTRELAQQISE 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 131 EARKLTYGTGIRVSYAIGGNSKMREENAIRRgNANLLIATPGRLEDHLQNPRILESLSTDSFILDEADRLMDMGFAESIL 210
Cdd:cd17954  87 QFEALGSSIGLKSAVLVGGMDMMAQAIALAK-KPHVIVATPGRLVDHLENTKGFSLKSLKFLVMDEADRLLNMDFEPEID 165
                       170       180       190
                ....*....|....*....|....*....|..
gi 19112388 211 NIHEAVTTTKTRKLcFSATMPPKVSNVFRGIL 242
Cdd:cd17954 166 KILKVIPRERTTYL-FSATMTTKVAKLQRASL 196
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
45-415 4.71e-31

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 125.69  E-value: 4.71e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388   45 LSSTFKNSLSRAGFEKMTPVQQRVLNEVFPNEEnAVVQAKTGTGKTLAFLLVAFKDVLKGKPRLNSSK-IHSVILSPTRE 123
Cdd:PRK10590   8 LSPDILRAVAEQGYREPTPIQQQAIPAVLEGRD-LMASAQTGTGKTAGFTLPLLQHLITRQPHAKGRRpVRALILTPTRE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  124 LALQIFEEARKLTYGTGIRVSYAIGG---NSKMREenaiRRGNANLLIATPGRLEDhLQNPRILESLSTDSFILDEADRL 200
Cdd:PRK10590  87 LAAQIGENVRDYSKYLNIRSLVVFGGvsiNPQMMK----LRGGVDVLVATPGRLLD-LEHQNAVKLDQVEILVLDEADRM 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  201 MDMGFAESILNIHeAVTTTKTRKLCFSATMPPKVSNVFRGILgTDFKLINCLDPNEPPthERVPQFVieTKLDKvfSSSL 280
Cdd:PRK10590 162 LDMGFIHDIRRVL-AKLPAKRQNLLFSATFSDDIKALAEKLL-HNPLEIEVARRNTAS--EQVTQHV--HFVDK--KRKR 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  281 SLLQQLTSSNPSSRIIVFLPTISMVDFVGGVLeNHLKIPCFILHSGLTTAQRRSITESFRKCQSGILFATDVVARGMDFP 360
Cdd:PRK10590 234 ELLSQMIGKGNWQQVLVFTRTKHGANHLAEQL-NKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIE 312
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 19112388  361 NITQVVQITGPSNTDDYIHRIGRTGRAGKTGEAYLILLEQEKPFLNSIKHLpLKR 415
Cdd:PRK10590 313 ELPHVVNYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKL-LKK 366
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
51-231 2.17e-29

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: 114.28  E-value: 2.17e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  51 NSLSRAGFEKMTPVQQRVLNEVFPNEEnAVVQAKTGTGKTLAFLLVAFKDVlkgkpRLNSSKIHSVILSPTRELALQIFE 130
Cdd:cd17943   3 EGLKAAGFQRPSPIQLAAIPLGLAGHD-LIVQAKSGTGKTLVFVVIALESL-----DLERRHPQVLILAPTREIAVQIHD 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 131 EARKL-TYGTGIRVSYAIGGNSKmrEENAIRRGNANLLIATPGRLEdHLQNPRILESLSTDSFILDEADRLMDMGFAESI 209
Cdd:cd17943  77 VFKKIgKKLEGLKCEVFIGGTPV--KEDKKKLKGCHIAVGTPGRIK-QLIELGALNVSHVRLFVLDEADKLMEGSFQKDV 153
                       170       180
                ....*....|....*....|..
gi 19112388 210 LNIHEAVTTTKtRKLCFSATMP 231
Cdd:cd17943 154 NWIFSSLPKNK-QVIAFSATYP 174
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
52-234 4.88e-29

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: 113.86  E-value: 4.88e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  52 SLSRAGFEKMTPVQQRVLNEVFpNEENAVVQAKTGTGKTLAFLLVAFkDVLKGKPrlnsSKIHSVILSPTRELALQIFEE 131
Cdd:cd17955  13 QCASLGIKEPTPIQKLCIPEIL-AGRDVIGGAKTGSGKTAAFALPIL-QRLSEDP----YGIFALVLTPTRELAYQIAEQ 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 132 ARKLTYGTGIRVSYAIGGNSKMREENAIRRgNANLLIATPGRLEDHLQN-PRILESLS-TDSFILDEADRLMDMGFAESI 209
Cdd:cd17955  87 FRALGAPLGLRCCVIVGGMDMVKQALELSK-RPHIVVATPGRLADHLRSsDDTTKVLSrVKFLVLDEADRLLTGSFEDDL 165
                       170       180
                ....*....|....*....|....*
gi 19112388 210 LNIHEAVTTTKtRKLCFSATMPPKV 234
Cdd:cd17955 166 ATILSALPPKR-QTLLFSATLTDAL 189
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
51-234 1.04e-28

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: 112.85  E-value: 1.04e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  51 NSLSRAGFEKMTPVQQrvlnEVFP---NEENAVVQAKTGTGKTLAFLLVAFKDVLKGKPRLNSSKIHSVILSPTRELALQ 127
Cdd:cd17966   3 DELKRQGFTEPTAIQA----QGWPmalSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERGDGPIVLVLAPTRELAQQ 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 128 IFEEARKLTYGTGIRVSYAIGGNSKMREENAIRRGnANLLIATPGRLEDHLQNPRIleSLSTDSF-ILDEADRLMDMGFA 206
Cdd:cd17966  79 IQQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRG-VEICIATPGRLIDFLDQGKT--NLRRVTYlVLDEADRMLDMGFE 155
                       170       180
                ....*....|....*....|....*...
gi 19112388 207 ESILNIHEAVTTTKtRKLCFSATMPPKV 234
Cdd:cd17966 156 PQIRKIVDQIRPDR-QTLMWSATWPKEV 182
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
51-230 3.34e-28

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: 112.33  E-value: 3.34e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  51 NSLSRAGFEKMTPVQQRVLNEVFPNEENAVVQAKTGTGKTLAF---LLVAFKDVLKGKPRLNSSK-IHSVILSPTRELAL 126
Cdd:cd17946   3 RALADLGFSEPTPIQALALPAAIRDGKDVIGAAETGSGKTLAFgipILERLLSQKSSNGVGGKQKpLRALILTPTRELAV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 127 QIFEEARKLTYGTGIRVSYAIGGNSKMREENAIRRGnANLLIATPGRLEDHLQN-PRILESLSTDSF-ILDEADRLMDMG 204
Cdd:cd17946  83 QVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKR-PEIVVATPGRLWELIQEgNEHLANLKSLRFlVLDEADRMLEKG 161
                       170       180       190
                ....*....|....*....|....*....|..
gi 19112388 205 -FAE-----SILNIHEAVTTTKTRKLCFSATM 230
Cdd:cd17946 162 hFAElekilELLNKDRAGKKRKRQTFVFSATL 193
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
52-237 4.45e-28

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: 111.02  E-value: 4.45e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  52 SLSRAGFEKMTPVQQRVLNEVFPNEENAVVqAKTGTGKTLAFLLVAF-KDVLKGKPRLNSSKIHSVILSPTRELALQIFE 130
Cdd:cd17958   4 EIKKQGFEKPSPIQSQAWPIILQGIDLIGV-AQTGTGKTLAYLLPGFiHLDLQPIPREQRNGPGVLVLTPTRELALQIEA 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 131 EARKLTYgTGIRVSYAIGGNSKMREENAIRRGnANLLIATPGRLEDhLQNPRILESLSTDSFILDEADRLMDMGFAESIL 210
Cdd:cd17958  83 ECSKYSY-KGLKSVCVYGGGNRNEQIEDLSKG-VDIIIATPGRLND-LQMNNVINLKSITYLVLDEADRMLDMGFEPQIR 159
                       170       180
                ....*....|....*....|....*..
gi 19112388 211 NIHEAVTTTKTRKLCfSATMPPKVSNV 237
Cdd:cd17958 160 KILLDIRPDRQTIMT-SATWPDGVRRL 185
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
57-242 9.45e-28

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: 110.11  E-value: 9.45e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  57 GFEKMTPVQQRVLNEvFPNEENAVVQAKTGTGKTLAFLLVAFKDVlkgKPRLNSSKIhsVILSPTRELALQIFEEARKLT 136
Cdd:cd17939  16 GFEKPSAIQQRAIVP-IIKGRDVIAQAQSGTGKTATFSIGALQRI---DTTVRETQA--LVLAPTRELAQQIQKVVKALG 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 137 YGTGIRVSYAIGGNSkMREENAIRRGNANLLIATPGRLEDHLQNprilESLSTDS---FILDEADRLMDMGFAESILNIH 213
Cdd:cd17939  90 DYMGVKVHACIGGTS-VREDRRKLQYGPHIVVGTPGRVFDMLQR----RSLRTDKikmFVLDEADEMLSRGFKDQIYDIF 164
                       170       180
                ....*....|....*....|....*....
gi 19112388 214 EAVtTTKTRKLCFSATMPPKVSNVFRGIL 242
Cdd:cd17939 165 QFL-PPETQVVLFSATMPHEVLEVTKKFM 192
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
290-388 2.98e-26

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: 103.06  E-value: 2.98e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388   290 NPSSRIIVFLPTISMVDFvgGVLENHLKIPCFILHSGLTTAQRRSITESFRKCQSGILFATDVVARGMDFPNITQVVQIT 369
Cdd:pfam00271  13 ERGGKVLIFSQTKKTLEA--ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDLVINYD 90
                          90
                  ....*....|....*....
gi 19112388   370 GPSNTDDYIHRIGRTGRAG 388
Cdd:pfam00271  91 LPWNPASYIQRIGRAGRAG 109
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
48-250 9.96e-26

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: 104.54  E-value: 9.96e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  48 TFKNSLSRaGFEKMTPVQQRVLNEVFPNEEnAVVQAKTGTGKTLAFLLVAFKDVLKG-KPRLNSSKIHSVILSPTRELAL 126
Cdd:cd17944   1 TIKLLQAR-GVTYLFPIQVKTFHPVYSGKD-LIAQARTGTGKTFSFAIPLIEKLQEDqQPRKRGRAPKVLVLAPTRELAN 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 127 QIFEEARKLTygTGIRVSYAIGGNSKMREENAIRRGnANLLIATPGRLEDHLQNPRiLESLSTDSFILDEADRLMDMGFA 206
Cdd:cd17944  79 QVTKDFKDIT--RKLSVACFYGGTPYQQQIFAIRNG-IDILVGTPGRIKDHLQNGR-LDLTKLKHVVLDEVDQMLDMGFA 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 19112388 207 ESILNI----HEAVTTTKTRKLCFSATMPPKVSNVFRGILGTDFKLIN 250
Cdd:cd17944 155 EQVEEIlsvsYKKDSEDNPQTLLFSATCPDWVYNVAKKYMKSQYEQVD 202
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
49-230 3.98e-24

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: 100.78  E-value: 3.98e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  49 FKNSLSRAGFEKMTPVQQRVLNEVFPNEENA--------VVQAKTGTGKTLAFLLVAFKDVLKGKprlnSSKIHSVILSP 120
Cdd:cd17956   1 LLKNLQNNGITSAFPVQAAVIPWLLPSSKSTppyrpgdlCVSAPTGSGKTLAYVLPIVQALSKRV----VPRLRALIVVP 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 121 TRELALQIFEEARKLTYGTGIRVSYAIGGNSKMREENAIRRGNANL-------LIATPGRLEDHLQNPR--ILESLstdS 191
Cdd:cd17956  77 TKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDTSGRylsrvdiLVATPGRLVDHLNSTPgfTLKHL---R 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 19112388 192 F-ILDEADRLMDMGFAE------SILNIHEAVTTTKT-------------RKLCFSATM 230
Cdd:cd17956 154 FlVIDEADRLLNQSFQDwletvmKALGRPTAPDLGSFgdanllersvrplQKLLFSATL 212
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
51-242 9.34e-24

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: 98.95  E-value: 9.34e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  51 NSLSRAGFEKMTPVQQRVLNEVFPNEENAVVqAKTGTGKTLAFLLVAFKDVL---KGKPRLNSSKIHSVILSPTRELALQ 127
Cdd:cd17951   3 KGLKKKGIKKPTPIQMQGLPTILSGRDMIGI-AFTGSGKTLVFTLPLIMFALeqeKKLPFIKGEGPYGLIVCPSRELARQ 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 128 IFEE----ARKLTYG--TGIRVSYAIGGNSKMREENAIRRGnANLLIATPGRLEDHLQNPRIleSLSTDSFI-LDEADRL 200
Cdd:cd17951  82 THEVieyyCKALQEGgyPQLRCLLCIGGMSVKEQLEVIRKG-VHIVVATPGRLMDMLNKKKI--NLDICRYLcLDEADRM 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 19112388 201 MDMGFAESILNIHEAVTTTKtRKLCFSATMPPKVSNVFRGIL 242
Cdd:cd17951 159 IDMGFEEDIRTIFSYFKGQR-QTLLFSATMPKKIQNFAKSAL 199
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
57-230 1.39e-23

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: 98.42  E-value: 1.39e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  57 GFEKMTPVQQRVLnevfP---NEENAVVQAKTGTGKTLAFLLVAFKDVLKGKPRLNSSK-IHSVILSPTRELALQIFEEA 132
Cdd:cd17961  13 GWEKPTLIQSKAI----PlalEGKDILARARTGSGKTAAYALPIIQKILKAKAESGEEQgTRALILVPTRELAQQVSKVL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 133 RKLTYGTGIRVSYA-IGGNSKMREENAIRRGNANLLIATPGRLEDHLQ--NPRILESLSTdsFILDEADRLMDMGFAESI 209
Cdd:cd17961  89 EQLTAYCRKDVRVVnLSASSSDSVQRALLAEKPDIVVSTPARLLSHLEsgSLLLLSTLKY--LVIDEADLVLSYGYEEDL 166
                       170       180
                ....*....|....*....|.
gi 19112388 210 LNIHEAVTTTKtRKLCFSATM 230
Cdd:cd17961 167 KSLLSYLPKNY-QTFLMSATL 186
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
57-237 1.39e-23

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: 98.29  E-value: 1.39e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  57 GFEKMTPVQQRVLNEVFPNEEnAVVQAKTGTGKTLAFLLVAFKDVlkgkpRLNSSKIHSVILSPTRELALQIFEEARKLT 136
Cdd:cd18046  18 GFEKPSAIQQRAIMPCIKGYD-VIAQAQSGTGKTATFSISILQQI-----DTSLKATQALVLAPTRELAQQIQKVVMALG 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 137 YGTGIRVSYAIGGNSkMREENAIRRGNANLLIATPGRLEDHLqNPRILESLSTDSFILDEADRLMDMGFAESILNIHEAV 216
Cdd:cd18046  92 DYMGIKCHACIGGTS-VRDDAQKLQAGPHIVVGTPGRVFDMI-NRRYLRTDYIKMFVLDEADEMLSRGFKDQIYDIFQKL 169
                       170       180
                ....*....|....*....|.
gi 19112388 217 TTTkTRKLCFSATMPPKVSNV 237
Cdd:cd18046 170 PPD-TQVVLLSATMPNDVLEV 189
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
57-234 2.57e-23

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: 97.65  E-value: 2.57e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  57 GFEKMTPVQQRVLNEVFPNE-ENAVVQAKTGTGKTLAFllvafkdVLKGKPRLNSSKIH--SVILSPTRELALQIFEEAR 133
Cdd:cd17963  13 GFNKPSKIQETALPLILSDPpENLIAQSQSGTGKTAAF-------VLAMLSRVDPTLKSpqALCLAPTRELARQIGEVVE 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 134 KLTYGTGIRVSYAIGGNSKMREENAirrgNANLLIATPGRLEDHLQNPRI-LESLSTdsFILDEADRLMDM-GFAESILN 211
Cdd:cd17963  86 KMGKFTGVKVALAVPGNDVPRGKKI----TAQIVIGTPGTVLDWLKKRQLdLKKIKI--LVLDEADVMLDTqGHGDQSIR 159
                       170       180
                ....*....|....*....|...
gi 19112388 212 IHEAVTTTkTRKLCFSATMPPKV 234
Cdd:cd17963 160 IKRMLPRN-CQILLFSATFPDSV 181
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
56-236 9.35e-23

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: 96.21  E-value: 9.35e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  56 AGFEKMTPVQQRVLNEVFPNEeNAVVQAKTGTGKTLAFLLvafkdvlkgkPRLN-----SSKIHSVILSPTRELALQIFE 130
Cdd:cd17940  17 KGFEKPSPIQEESIPIALSGR-DILARAKNGTGKTGAYLI----------PILEkidpkKDVIQALILVPTRELALQTSQ 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 131 EARKLTYGTGIRVSYAIGGNS----KMREENAIrrgnaNLLIATPGRLEDHLQnpRILESLSTDS-FILDEADRLMDMGF 205
Cdd:cd17940  86 VCKELGKHMGVKVMVTTGGTSlrddIMRLYQTV-----HVLVGTPGRILDLAK--KGVADLSHCKtLVLDEADKLLSQDF 158
                       170       180       190
                ....*....|....*....|....*....|..
gi 19112388 206 AESILNIHEavTTTKTRKLC-FSATMPPKVSN 236
Cdd:cd17940 159 QPIIEKILN--FLPKERQILlFSATFPLTVKN 188
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
53-237 4.10e-22

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: 95.13  E-value: 4.10e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  53 LSRAGFEKMTPVQQRVLNEVFpNEENAVVQAKTGTGKTLAFLLVAFKDVL--KGKPRLNSSKIHSVILSPTRELALQIFE 130
Cdd:cd17948   5 LQRQGITKPTTVQKQGIPSIL-RGRNTLCAAETGSGKTLTYLLPIIQRLLryKLLAEGPFNAPRGLVITPSRELAEQIGS 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 131 EARKLTYGTGIRVSYAIGGNSKMREENaIRRGNANLLIATPGRLEDhLQNPRI--LESLStdSFILDEADRLMDMGFAES 208
Cdd:cd17948  84 VAQSLTEGLGLKVKVITGGRTKRQIRN-PHFEEVDILVATPGALSK-LLTSRIysLEQLR--HLVLDEADTLLDDSFNEK 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 19112388 209 ILNI------------HEAVTTTKTRKLCFSATMPPKVSNV 237
Cdd:cd17948 160 LSHFlrrfplasrrseNTDGLDPGTQLVLVSATMPSGVGEV 200
HELICc smart00490
helicase superfamily c-terminal domain;
314-388 1.05e-21

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 89.19  E-value: 1.05e-21
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19112388    314 NHLKIPCFILHSGLTTAQRRSITESFRKCQSGILFATDVVARGMDFPNITQVVQITGPSNTDDYIHRIGRTGRAG 388
Cdd:smart00490   8 KELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
52-237 5.85e-20

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: 87.99  E-value: 5.85e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  52 SLSRAGFEKMTPVQQRVLnEVFPNEENAVVQAKTGTGKTLAFLLVAFKDVLkGKPRLNSSkihsVILSPTRELALQIFEE 131
Cdd:cd17962   4 NLKKAGYEVPTPIQMQMI-PVGLLGRDILASADTGSGKTAAFLLPVIIRCL-TEHRNPSA----LILTPTRELAVQIEDQ 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 132 ARKLTYGT-GIRVSYAIGGNSKMREENAIRRGnANLLIATPGRLEDHLQNPRI-LESLSTdsFILDEADRLMDMGFAESI 209
Cdd:cd17962  78 AKELMKGLpPMKTALLVGGLPLPPQLYRLQQG-VKVIIATPGRLLDILKQSSVeLDNIKI--VVVDEADTMLKMGFQQQV 154
                       170       180
                ....*....|....*....|....*...
gi 19112388 210 LNIHEAVtTTKTRKLCFSATMPPKVSNV 237
Cdd:cd17962 155 LDILENI-SHDHQTILVSATIPRGIEQL 181
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
81-230 2.79e-19

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: 86.22  E-value: 2.79e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  81 VQAKTGTGKTLAFLLVAFKDVLkgkprlnsskihSVILSPTRELALQIFEEARKLTY---GTGIRVSYAIGGnSKMREEN 157
Cdd:cd17938  41 MAAETGSGKTGAFCLPVLQIVV------------ALILEPSRELAEQTYNCIENFKKyldNPKLRVALLIGG-VKAREQL 107
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19112388 158 AIRRGNANLLIATPGRLEDHLQNPRILESlSTDSFILDEADRLMDMGFAESILNIHEAV--TTTKTRKL---CFSATM 230
Cdd:cd17938 108 KRLESGVDIVVGTPGRLEDLIKTGKLDLS-SVRFFVLDEADRLLSQGNLETINRIYNRIpkITSDGKRLqviVCSATL 184
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
46-239 4.66e-19

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: 85.47  E-value: 4.66e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  46 SSTFKN-----SLSRA----GFEKMTPVQQrvlnEVFPNE---ENAVVQAKTGTGKTLAFLLVAFKDVlkgKPrlNSSKI 113
Cdd:cd17950   1 SSGFRDfllkpELLRAivdcGFEHPSEVQH----ECIPQAilgMDVLCQAKSGMGKTAVFVLSTLQQL---EP--VDGQV 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 114 HSVILSPTRELALQIFEEARKLT-YGTGIRVSYAIGGNSKMREENAIRRGNANLLIATPGRLEDHLQNprilESLSTDS- 191
Cdd:cd17950  72 SVLVICHTRELAFQISNEYERFSkYMPNVKTAVFFGGVPIKKDIEVLKNKCPHIVVGTPGRILALVRE----KKLKLSHv 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 19112388 192 --FILDEADRLMdmgfaESI---LNIHEAVTTTKTRK--LCFSATMPPKVSNVFR 239
Cdd:cd17950 148 khFVLDECDKML-----EQLdmrRDVQEIFRATPHDKqvMMFSATLSKEIRPVCK 197
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
57-234 2.11e-18

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: 83.67  E-value: 2.11e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  57 GFEKMTPVQQRVLNEVFPNEEnAVVQAKTGTGKTLAFLLVAFKDVlkgkpRLNSSKIHSVILSPTRELALQIFEEARKLT 136
Cdd:cd18045  18 GFEKPSAIQQRAIKPIIKGRD-VIAQSQSGTGKTATFSISVLQCL-----DIQVRETQALILSPTRELAVQIQKVLLALG 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 137 YGTGIRVSYAIGGNSKMREENAIRRGnANLLIATPGRLEDHLQNpRILESLSTDSFILDEADRLMDMGFAESILNIHEAV 216
Cdd:cd18045  92 DYMNVQCHACIGGTSVGDDIRKLDYG-QHIVSGTPGRVFDMIRR-RSLRTRHIKMLVLDEADEMLNKGFKEQIYDVYRYL 169
                       170
                ....*....|....*...
gi 19112388 217 tTTKTRKLCFSATMPPKV 234
Cdd:cd18045 170 -PPATQVVLVSATLPQDI 186
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
76-229 3.11e-18

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


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 81.30  E-value: 3.11e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  76 EENAVVQAKTGTGKTLAFLLVAFKDVLKGKPRlnsskihSVILSPTRELALQIFEEARKLtYGTGIRVSYaIGGNSKMRE 155
Cdd:cd00046   1 GENVLITAPTGSGKTLAALLAALLLLLKKGKK-------VLVLVPTKALALQTAERLREL-FGPGIRVAV-LVGGSSAEE 71
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19112388 156 ENAIRRGNANLLIATPGRLEDHLQNPRILESLSTDSFILDEADRLMDMGFAESILNI-HEAVTTTKTRKLCFSAT 229
Cdd:cd00046  72 REKNKLGDADIIIATPDMLLNLLLREDRLFLKDLKLIIVDEAHALLIDSRGALILDLaVRKAGLKNAQVILLSAT 146
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
35-250 1.84e-17

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: 81.59  E-value: 1.84e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  35 QPTLFSEVASLSSTFKNSLSRAGFEKMTPVQQRVLnEVFPNEENAVVQAKTGTGKTLAFLLVAFKDVlKGKPRLNSSKIH 114
Cdd:cd18049  21 KPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGW-PVALSGLDMVGVAQTGSGKTLSYLLPAIVHI-NHQPFLERGDGP 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 115 -SVILSPTRELALQIFEEARKLTYGTGIRVSYAIGGNSKMREENAIRRGnANLLIATPGRLEDHLQNPRILESLSTdSFI 193
Cdd:cd18049  99 iCLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERG-VEICIATPGRLIDFLEAGKTNLRRCT-YLV 176
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 19112388 194 LDEADRLMDMGFAESILNIHEAVTTTKtRKLCFSATMPPKVSNVFRGILgTDFKLIN 250
Cdd:cd18049 177 LDEADRMLDMGFEPQIRKIVDQIRPDR-QTLMWSATWPKEVRQLAEDFL-KDYIHIN 231
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
63-434 2.76e-17

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 85.08  E-value: 2.76e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  63 PVQQRVLNEVF----PNEENAVVQAKTGTGKTLAFLLVAFKdvLKGKPRLnsskihsVILSPTRELALQIFEEARKLTYG 138
Cdd:COG1061  83 PYQQEALEALLaaleRGGGRGLVVAPTGTGKTVLALALAAE--LLRGKRV-------LVLVPRRELLEQWAEELRRFLGD 153
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 139 TGIrvsyaiGGNSKMREenairrgnANLLIATPGRLEDHLQnpriLESLStDSF---ILDEADRLMDMGFAESILNIHea 215
Cdd:COG1061 154 PLA------GGGKKDSD--------APITVATYQSLARRAH----LDELG-DRFglvIIDEAHHAGAPSYRRILEAFP-- 212
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 216 vtttKTRKLCFSATmP------PKVSNVFRGIL-GTDFK-LIN--------CLDPNEPPTHERVPQFVIETKLDKVFSSS 279
Cdd:COG1061 213 ----AAYRLGLTAT-PfrsdgrEILLFLFDGIVyEYSLKeAIEdgylappeYYGIRVDLTDERAEYDALSERLREALAAD 287
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 280 LSLLQQ-----LTSSNPSSRIIVFLPTISMVDFVGGVLENHlKIPCFILHSGLTTAQRRSITESFRKCQSGILFATDVVA 354
Cdd:COG1061 288 AERKDKilrelLREHPDDRKTLVFCSSVDHAEALAELLNEA-GIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLN 366
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 355 RGMDFPNITQVVQITGPSNTDDYIHRIGRTGRAGKTGE-AYLILL-----EQEKPFLNSIKHLPLKRATIEPLSDQALST 428
Cdd:COG1061 367 EGVDVPRLDVAILLRPTGSPREFIQRLGRGLRPAPGKEdALVYDFvgndvPVLEELAKDLRDLAGYRVEFLDEEESEELA 446

                ....*.
gi 19112388 429 LRSDIE 434
Cdd:COG1061 447 LLIAVK 452
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
58-250 1.65e-16

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: 79.67  E-value: 1.65e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  58 FEKMTPVQQrvlnEVFP---NEENAVVQAKTGTGKTLAFLLVAFKDVlKGKPRLNSSKIH-SVILSPTRELALQIFEEAR 133
Cdd:cd18050  82 FKEPTPIQC----QGFPlalSGRDMVGIAQTGSGKTLAYLLPAIVHI-NHQPYLERGDGPiCLVLAPTRELAQQVQQVAD 156
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 134 KLTYGTGIRVSYAIGGNSKMREENAIRRGnANLLIATPGRLEDHLQNPRILESLSTdSFILDEADRLMDMGFAESILNIH 213
Cdd:cd18050 157 DYGKSSRLKSTCIYGGAPKGPQIRDLERG-VEICIATPGRLIDFLEAGKTNLRRCT-YLVLDEADRMLDMGFEPQIRKIV 234
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 19112388 214 EAVTTTKtRKLCFSATMPPKVSNVFRGILgTDFKLIN 250
Cdd:cd18050 235 DQIRPDR-QTLMWSATWPKEVRQLAEDFL-RDYVQIN 269
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
49-234 3.10e-16

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: 78.14  E-value: 3.10e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  49 FKNSLSRA----GFEKMTPVQQRVLNEVFPNE-ENAVVQAKTGTGKTLAFLLVAFKdvlkgkpRLNSSKIHS--VILSPT 121
Cdd:cd18048  25 LKEELLRGiyamGFNRPSKIQENALPMMLADPpQNLIAQSQSGTGKTAAFVLAMLS-------RVDALKLYPqcLCLSPT 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 122 RELALQ---IFEEARKltYGTGIRVSYAIGGNSKMREEnairRGNANLLIATPGRLEDHLQNPRILESLSTDSFILDEAD 198
Cdd:cd18048  98 FELALQtgkVVEEMGK--FCVGIQVIYAIRGNRPGKGT----DIEAQIVIGTPGTVLDWCFKLRLIDVTNISVFVLDEAD 171
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 19112388 199 RLMDM-GFAESILNIHEAVTTTkTRKLCFSATMPPKV 234
Cdd:cd18048 172 VMINVqGHSDHSVRVKRSMPKE-CQMLLFSATFEDSV 207
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
74-231 2.34e-14

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: 72.79  E-value: 2.34e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  74 PNEENAVVQAKTGTGKTLAFLLVAFkDVLK-------------GKPRLNSSKIHSVILSPTRELALQIFEEARKLTYGTG 140
Cdd:cd17965  59 PKLEVFLLAAETGSGKTLAYLAPLL-DYLKrqeqepfeeaeeeYESAKDTGRPRSVILVPTHELVEQVYSVLKKLSHTVK 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 141 IRVSYAIGGNSKMREENAIR-RGNANLLIATPGRLEDHLQ-NPRILESLStdSFILDEADRLMDMGFAESILNIHEAVTT 218
Cdd:cd17965 138 LGIKTFSSGFGPSYQRLQLAfKGRIDILVTTPGKLASLAKsRPKILSRVT--HLVVDEADTLFDRSFLQDTTSIIKRAPK 215
                       170
                ....*....|...
gi 19112388 219 TKTRKLCfSATMP 231
Cdd:cd17965 216 LKHLILC-SATIP 227
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
61-202 8.31e-14

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: 69.60  E-value: 8.31e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  61 MTPVQQRVLNEVFPNEENAVVQAKTGTGKTLAFLLVAFKDVLKGKPRlnsskihSVILSPTRELALQIFEEARKLTYGTG 140
Cdd:cd17921   2 LNPIQREALRALYLSGDSVLVSAPTSSGKTLIAELAILRALATSGGK-------AVYIAPTRALVNQKEADLRERFGPLG 74
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19112388 141 IRVSYAIGGnskmREENAIRRGNANLLIATPGRLEDHLQNPRILESLSTDSFILDEADRLMD 202
Cdd:cd17921  75 KNVGLLTGD----PSVNKLLLAEADILVATPEKLDLLLRNGGERLIQDVRLVVVDEAHLIGD 132
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
41-197 4.70e-13

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 71.46  E-value: 4.70e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  41 EVASLSS-TFKNSLSRAGFEKMTPVQQRVLNEVFPNEENAVVQAKTGTGKTLAFLLVAFKDVLKGKPrlnsskihSVILS 119
Cdd:COG1204   2 KVAELPLeKVIEFLKERGIEELYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLNGGK--------ALYIV 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 120 PTRELALQIFEEARKLTYGTGIRVSYAIGGnskmREENAIRRGNANLLIATPGRLeDHL--QNPRILESLSTdsFILDEA 197
Cdd:COG1204  74 PLRALASEKYREFKRDFEELGIKVGVSTGD----YDSDDEWLGRYDILVATPEKL-DSLlrNGPSWLRDVDL--VVVDEA 146
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
57-234 1.50e-09

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: 57.81  E-value: 1.50e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  57 GFEKMTPVQQRVLNEVFPNE-ENAVVQAKTGTGKTLAFLLVAFKDVlkgKPRLNSSKihSVILSPTRELALQ---IFEEA 132
Cdd:cd18047  20 GFNRPSKIQENALPLMLAEPpQNLIAQSQSGTGKTAAFVLAMLSQV---EPANKYPQ--CLCLSPTYELALQtgkVIEQM 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 133 RKltYGTGIRVSYAIGGNskmREENAIRRGNaNLLIATPGRLEDHLQNPRILESLSTDSFILDEADRLM-DMGFAESILN 211
Cdd:cd18047  95 GK--FYPELKLAYAVRGN---KLERGQKISE-QIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIaTQGHQDQSIR 168
                       170       180
                ....*....|....*....|...
gi 19112388 212 IHEAVtTTKTRKLCFSATMPPKV 234
Cdd:cd18047 169 IQRML-PRNCQMLLFSATFEDSV 190
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
77-197 7.48e-09

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


Pssm-ID: 350681 [Multi-domain]  Cd Length: 182  Bit Score: 55.28  E-value: 7.48e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  77 ENAVVQAKTGTGKTLAFLLVAFKDVLkgkpRLNSSKihSVILSPTRELALQIFEEARKLT--YGTGIRVSyAIGGNSKMR 154
Cdd:cd17923  16 RSVVVTTGTASGKSLCYQLPILEALL----RDPGSR--ALYLYPTKALAQDQLRSLRELLeqLGLGIRVA-TYDGDTPRE 88
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 19112388 155 EENAIRRGNANLLIATPGRLE-----DHLQNPRILESLstDSFILDEA 197
Cdd:cd17923  89 ERRAIIRNPPRILLTNPDMLHyallpHHDRWARFLRNL--RYVVLDEA 134
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
45-397 2.21e-08

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: 56.77  E-value: 2.21e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  45 LSSTFKNSLSRAGFEKMTPVQQRVLNEVFpNEENAVVQAKTGTGKTLAFLLVAFKDVLKGkprlnsSKIHSVILSPTREL 124
Cdd:COG1205  41 LPPELRAALKKRGIERLYSHQAEAIEAAR-AGKNVVIATPTASGKSLAYLLPVLEALLED------PGATALYLYPTKAL 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 125 ALQIFEEARKLTYGTGIRVSYAI-GGNSKMREENAIRRgNANLLIATP-----GRLEDHLQNPRILESLSTdsFILDEA- 197
Cdd:COG1205 114 ARDQLRRLRELAEALGLGVRVATyDGDTPPEERRWIRE-HPDIVLTNPdmlhyGLLPHHTRWARFFRNLRY--VVIDEAh 190
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 198 --------------DRLmdmgfaesilniheavtttktRKLC--------F---SATMP-PKVSnvFRGILGTDFKLInc 251
Cdd:COG1205 191 tyrgvfgshvanvlRRL---------------------RRICrhygsdpqFilaSATIGnPAEH--AERLTGRPVTVV-- 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 252 lDPNEPPTHERvpQFVIetkldkVFSSSLSLLQQLTSSNPSSRI-----------IVFLPTISMVDFVGGVLENHLKIPC 320
Cdd:COG1205 246 -DEDGSPRGER--TFVL------WNPPLVDDGIRRSALAEAARLladlvreglrtLVFTRSRRGAELLARYARRALREPD 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 321 F---IL--HSGLTTAQRRSITESFRkcqSGILFAtdVVAR-----GMDFPNItQVVQITG-PSNTDDYIHRIGRTGRAGK 389
Cdd:COG1205 317 LadrVAayRAGYLPEERREIERGLR---SGELLG--VVSTnalelGIDIGGL-DAVVLAGyPGTRASFWQQAGRAGRRGQ 390

                ....*...
gi 19112388 390 TGEAYLIL 397
Cdd:COG1205 391 DSLVVLVA 398
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
80-389 2.47e-08

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


Pssm-ID: 187770 [Multi-domain]  Cd Length: 353  Bit Score: 55.90  E-value: 2.47e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  80 VVQAKTGTGKTLAFLLVAFKDVLKGKprlnSSKIhsVILSPTRELALQIFEEARKLTYGTGIRVSYAIGGNSKMRE-ENA 158
Cdd:cd09639   3 VIEAPTGYGKTEAALLWALHSLKSQK----ADRV--IIALPTRATINAMYRRAKEAFGETGLYHSSILSSRIKEMGdSEE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 159 IRRGNANL------LIATPGRLE--DHLQNPR---------ILESLSTDSFILDEADRLMD--MGFAESILnihEAVTTT 219
Cdd:cd09639  77 FEHLFPLYihsndtLFLDPITVCtiDQVLKSVfgefghyefTLASIANSLLIFDEVHFYDEytLALILAVL---EVLKDN 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 220 KTRKLCFSATMPPKVSNVFRGILgtdfkliNCLDPNEPPTHERVPQFVIETKLDKVFSSSLSLLQQLTSSNPSSRIIVFL 299
Cdd:cd09639 154 DVPILLMSATLPKFLKEYAEKIG-------YVEENEPLDLKPNERAPFIKIESDKVGEISSLERLLEFIKKGGSVAIIVN 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 300 PTISMVDFVGGVLENHLKIPCFILHSGLTTAQRRS----ITESFRKCQSGILFATDVVARGMDfpnITQVVQITGPSNTD 375
Cdd:cd09639 227 TVDRAQEFYQQLKEKGPEEEIMLIHSRFTEKDRAKkeaeLLLEFKKSEKFVIVATQVIEASLD---ISVDVMITELAPID 303
                       330
                ....*....|....
gi 19112388 376 DYIHRIGRTGRAGK 389
Cdd:cd09639 304 SLIQRLGRLHRYGE 317
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
75-199 6.76e-08

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: 52.82  E-value: 6.76e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  75 NEENAVVQAKTGTGKTLAFLLVAfKDVLKGKPRLNSSKIhsVILSPTRELALQIFEEARKLTYGTGIRVSyAIGGNSKMR 154
Cdd:cd17927  16 KGKNTIICLPTGSGKTFVAVLIC-EHHLKKFPAGRKGKV--VFLANKVPLVEQQKEVFRKHFERPGYKVT-GLSGDTSEN 91
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 19112388 155 EENAIRRGNANLLIATPGRLEDHLQNPRILeSLSTDSF-ILDEADR 199
Cdd:cd17927  92 VSVEQIVESSDVIIVTPQILVNDLKSGTIV-SLSDFSLlVFDECHN 136
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
346-398 2.53e-07

C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 48.08  E-value: 2.53e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 19112388 346 ILFATDVVARGMDFPNITQVVQITGPSNTDDYIHRIGRTGRAGKTgEAYLILL 398
Cdd:cd18785  25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKD-EGEVILF 76
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
64-171 3.54e-07

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


Pssm-ID: 350781 [Multi-domain]  Cd Length: 206  Bit Score: 50.82  E-value: 3.54e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  64 VQQRVLNEVFPNEENAVVQAKTGTGKTLAFLLvAFKDVLKGKPRLNSSKIHSVILSPTRELALQIFEEARKLTYGTGIRV 143
Cdd:cd18023   5 IQSEVFPDLLYSDKNFVVSAPTGSGKTVLFEL-AILRLLKERNPLPWGNRKVVYIAPIKALCSEKYDDWKEKFGPLGLSC 83
                        90       100
                ....*....|....*....|....*...
gi 19112388 144 SyAIGGNSKMREENAIRrgNANLLIATP 171
Cdd:cd18023  84 A-ELTGDTEMDDTFEIQ--DADIILTTP 108
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
63-196 5.46e-07

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


Pssm-ID: 350786 [Multi-domain]  Cd Length: 177  Bit Score: 49.64  E-value: 5.46e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  63 PVQQRVLNEVFPNEENAVVQAKTGTGKTLAFLLVAFKDVLKGKprlnsskiHSVILSPTRELALQIFEEARKLtYGTGIR 142
Cdd:cd18028   4 PPQAEAVRAGLLKGENLLISIPTASGKTLIAEMAMVNTLLEGG--------KALYLVPLRALASEKYEEFKKL-EEIGLK 74
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 19112388 143 VSYAIGgnskMREENAIRRGNANLLIATPGRLEDHLQN-PRILESLSTdsFILDE 196
Cdd:cd18028  75 VGISTG----DYDEDDEWLGDYDIIVATYEKFDSLLRHsPSWLRDVGV--VVVDE 123
ResIII pfam04851
Type III restriction enzyme, res subunit;
60-229 1.40e-06

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 48.44  E-value: 1.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388    60 KMTPVQQ----RVLNEVFPNEENAVVQAKTGTGKTlaflLVAFKDVLKGKPRLNSSKIhsVILSPTRELALQIFEEARKL 135
Cdd:pfam04851   3 ELRPYQIeaieNLLESIKNGQKRGLIVMATGSGKT----LTAAKLIARLFKKGPIKKV--LFLVPRKDLLEQALEEFKKF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388   136 TYGtgirvSYAIGGNSKMREENAIrRGNANLLIATPgrleDHLQNPRILESLSTDS-----FILDEADRLmdmgFAESIL 210
Cdd:pfam04851  77 LPN-----YVEIGEIISGDKKDES-VDDNKIVVTTI----QSLYKALELASLELLPdffdvIIIDEAHRS----GASSYR 142
                         170
                  ....*....|....*....
gi 19112388   211 NIHEAVttTKTRKLCFSAT 229
Cdd:pfam04851 143 NILEYF--KPAFLLGLTAT 159
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
290-398 2.90e-06

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: 46.82  E-value: 2.90e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 290 NPSSRIIVFLPTISMVDFVGGVLENHLkIPCFILHSGLTTAQRRSITESFRKCQSGILFATdvVARGM--DFPNITQVVQ 367
Cdd:cd18794  28 HLGGSGIIYCLSRKECEQVAARLQSKG-ISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVAT--VAFGMgiDKPDVRFVIH 104
                        90       100       110
                ....*....|....*....|....*....|.
gi 19112388 368 ITGPSNTDDYIHRIGRTGRAGKTgeAYLILL 398
Cdd:cd18794 105 YSLPKSMESYYQESGRAGRDGLP--SECILF 133
SF2_C_Ski2 cd18795
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ...
322-396 7.23e-06

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


Pssm-ID: 350182 [Multi-domain]  Cd Length: 154  Bit Score: 46.01  E-value: 7.23e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 322 ILHSGLTTAQRRSITESFRKCQSGILFATDVVARGMDFPNITqVVqITGPS----------NTDDYIHRIGRTGRAG--K 389
Cdd:cd18795  68 FHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPART-VI-IKGTQrydgkgyrelSPLEYLQMIGRAGRPGfdT 145

                ....*..
gi 19112388 390 TGEAYLI 396
Cdd:cd18795 146 RGEAIIM 152
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
60-149 1.79e-05

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


Pssm-ID: 350676 [Multi-domain]  Cd Length: 180  Bit Score: 45.48  E-value: 1.79e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  60 KMTPVQQRVLNEV---FPNEE--NAVVQAKTGTGKTLAFLLVAFKDVLKGKprlnsskiHSVILSPTRELALQIFEEARK 134
Cdd:cd17918  15 SLTKDQAQAIKDIekdLHSPEpmDRLLSGDVGSGKTLVALGAALLAYKNGK--------QVAILVPTEILAHQHYEEARK 86
                        90
                ....*....|....*
gi 19112388 135 ltYGTGIRVSYAIGG 149
Cdd:cd17918  87 --FLPFINVELVTGG 99
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
63-229 2.69e-05

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


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 44.22  E-value: 2.69e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  63 PVQQRVLNEVFPNEEN--AVVQAKTGTGKTLaFLLVAFKDVLKGKprlnsskihSVILSPTRELALQIFEEARKLtygTG 140
Cdd:cd17926   3 PYQEEALEAWLAHKNNrrGILVLPTGSGKTL-TALALIAYLKELR---------TLIVVPTDALLDQWKERFEDF---LG 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 141 IRVSYAIGGNSKMREEnairrgNANLLIATPGRLEDHLQNPRILeSLSTDSFILDEADRLMDMGFaESILNIHEAvtttk 220
Cdd:cd17926  70 DSSIGLIGGGKKKDFD------DANVVVATYQSLSNLAEEEKDL-FDQFGLLIVDEAHHLPAKTF-SEILKELNA----- 136

                ....*....
gi 19112388 221 TRKLCFSAT 229
Cdd:cd17926 137 KYRLGLTAT 145
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
324-395 2.71e-05

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 47.02  E-value: 2.71e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19112388  324 HSGLTTAQRRSITESFRKCQSGILFATdvVARGMDF--PNITQVVQITGPSNTDDYIHRIGRTGRAGKTGEAYL 395
Cdd:PRK11057 267 HAGLDNDVRADVQEAFQRDDLQIVVAT--VAFGMGInkPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAML 338
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
54-197 2.81e-05

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


Pssm-ID: 350678 [Multi-domain]  Cd Length: 200  Bit Score: 45.22  E-value: 2.81e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  54 SRAGFEKMTPVQQRVLNEVFpNEENAVVQAKTGTGKTLAFLLVAfkdVLKGKPrlnsskihSVILSPTreLALqIFEEAR 133
Cdd:cd17920   6 EVFGYDEFRPGQLEAINAVL-AGRDVLVVMPTGGGKSLCYQLPA---LLLDGV--------TLVVSPL--ISL-MQDQVD 70
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19112388 134 KLTyGTGIRVSYAIGGNS---KMREENAIRRGNANLLIATPGRledhLQNPRILESLST-------DSFILDEA 197
Cdd:cd17920  71 RLQ-QLGIRAAALNSTLSpeeKREVLLRIKNGQYKLLYVTPER----LLSPDFLELLQRlperkrlALIVVDEA 139
DEXHc_RecG cd17992
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in ...
32-170 3.48e-05

DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. It is a member of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350750 [Multi-domain]  Cd Length: 225  Bit Score: 45.22  E-value: 3.48e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  32 KSQQPTLFSEVASLSSTFKNSLsraGFEkMTPVQQRVLNEVF-----PNEENAVVQAKTGTGKTLAFLLVAFKDVLKGKp 106
Cdd:cd17992  21 EELKGIILEISGELLKKFLEAL---PFE-LTGAQKRVIDEILrdlasEKPMNRLLQGDVGSGKTVVAALAMLAAVENGY- 95
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19112388 107 rlnsskiHSVILSPTRELALQIFEEARKLTYGTGIRVSYAIGGNS-KMREE--NAIRRGNANLLIAT 170
Cdd:cd17992  96 -------QVALMAPTEILAEQHYDSLKKLLEPLGIRVALLTGSTKaKEKREilEKIASGEIDIVIGT 155
Cas3 COG1203
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ...
63-424 3.48e-05

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


Pssm-ID: 440816 [Multi-domain]  Cd Length: 535  Bit Score: 46.61  E-value: 3.48e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  63 PVQQRVLNEVFPNEENA----VVQAKTGTGKTLAFLLVAFKDVLKGKPRlnssKIhSVILsPTRELALQIFEEARKLTYG 138
Cdd:COG1203 130 PLQNEALELALEAAEEEpglfILTAPTGGGKTEAALLFALRLAAKHGGR----RI-IYAL-PFTSIINQTYDRLRDLFGE 203
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 139 T-----GIRVSYAIGGNSKMREENAIRRGNANLL-----IATPgrleDHL----------QNPRILeSLSTDSFILDEAD 198
Cdd:COG1203 204 DvllhhSLADLDLLEEEEEYESEARWLKLLKELWdapvvVTTI----DQLfeslfsnrkgQERRLH-NLANSVIILDEVQ 278
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 199 rLMDMGFAESILNIHEAVTTTKTRKLCFSATMPPKvsnvFRGILGTDFKLIncldPNEPPTHERVPQF-------VIETK 271
Cdd:COG1203 279 -AYPPYMLALLLRLLEWLKNLGGSVILMTATLPPL----LREELLEAYELI----PDEPEELPEYFRAfvrkrveLKEGP 349
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 272 LDkvfsSSLSLLQQLTSSNPSSRIIVFLPTI-SMVDFVGGVLENHLKIPCFILHSGLTTAQRR----SITESFRKCQSGI 346
Cdd:COG1203 350 LS----DEELAELILEALHKGKSVLVIVNTVkDAQELYEALKEKLPDEEVYLLHSRFCPADRSeiekEIKERLERGKPCI 425
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 347 LFATDVVARG--MDFPnitqVVqITGPSNTDDYIHRIGRT---GRAGKTGEAYLILLEQEKPflNSIKHLPLKRATIEPL 421
Cdd:COG1203 426 LVSTQVVEAGvdIDFD----VV-IRDLAPLDSLIQRAGRCnrhGRKEEEGNVYVFDPEDEGG--GYVYDKPLLERTRELL 498

                ...
gi 19112388 422 SDQ 424
Cdd:COG1203 499 REH 501
DEXHc_Brr2_2 cd18021
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ...
58-171 4.46e-05

C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 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: 350779 [Multi-domain]  Cd Length: 191  Bit Score: 44.56  E-value: 4.46e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  58 FEKMTPVQQRVLNEVFPNEENAVVQAKTGTGKT----LAfLLVAFKDVLKGKprlnsskihSVILSPTRELALQIFEE-A 132
Cdd:cd18021   1 FKFFNPIQTQVFNSLYNTDDNVFVGAPTGSGKTvcaeLA-LLRHWRQNPKGR---------AVYIAPMQELVDARYKDwR 70
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 19112388 133 RKLTYGTGIRVSYAIGgnskmrEENAIRR--GNANLLIATP 171
Cdd:cd18021  71 AKFGPLLGKKVVKLTG------ETSTDLKllAKSDVILATP 105
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
324-395 4.54e-05

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 45.90  E-value: 4.54e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19112388 324 HSGLTTAQRRSITESFRKCQSGILFATdvVARGM--DFPNITQVVQITGPSNTDDYIHRIGRTGRAGKTGEAYL 395
Cdd:COG0514 261 HAGLDAEEREANQDRFLRDEVDVIVAT--IAFGMgiDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALL 332
PRK10917 PRK10917
ATP-dependent DNA helicase RecG; Provisional
31-170 5.03e-05

ATP-dependent DNA helicase RecG; Provisional


Pssm-ID: 236794 [Multi-domain]  Cd Length: 681  Bit Score: 45.91  E-value: 5.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388   31 MKSQQPTLFSEVASLSSTFKNSLSragFEkMTPVQQRVLNEVF-----PNEENAVVQAKTGTGKTLAFLLVAFKDVLKGK 105
Cdd:PRK10917 236 RRSKKAGPLPYDGELLKKFLASLP---FE-LTGAQKRVVAEILadlasPKPMNRLLQGDVGSGKTVVAALAALAAIEAGY 311
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19112388  106 PrlnsskihSVILSPTRELALQIFEEARKLTYGTGIRVSYAIGGNS-KMREE--NAIRRGNANLLIAT 170
Cdd:PRK10917 312 Q--------AALMAPTEILAEQHYENLKKLLEPLGIRVALLTGSLKgKERREilEAIASGEADIVIGT 371
SF2_C_priA cd18804
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication ...
331-410 1.09e-04

C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication factor Y or primosomal protein N', is a 3'-->5' DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA 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: 350191 [Multi-domain]  Cd Length: 238  Bit Score: 43.77  E-value: 1.09e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 331 QRRSITESFRKCQSGILFATDVVARGMDFPNITQVVQITGPS--NTDDY---------IHRI-GRTGRAGKTGEAYLILL 398
Cdd:cd18804 132 ALEKLLDQFERGEIDILIGTQMIAKGLDFPNVTLVGILNADSglNSPDFraserafqlLTQVsGRAGRGDKPGKVIIQTY 211
                        90
                ....*....|..
gi 19112388 399 EQEKPFLNSIKH 410
Cdd:cd18804 212 NPEHPLIQAAKE 223
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
77-196 1.23e-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: 42.57  E-value: 1.23e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  77 ENAVVQAKTGTGKTLAFLLVAFKDVLKGKPrlnsSKIHSVILSPTRELALQIFEEARKLT--YGTGIRVSYAIGGNSKmR 154
Cdd:cd17922   2 RNVLIAAPTGSGKTEAAFLPALSSLADEPE----KGVQVLYISPLKALINDQERRLEEPLdeIDLEIPVAVRHGDTSQ-S 76
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 19112388 155 EENAIRRGNANLLIATPGRLEDHLQNPRILESLSTDSF-ILDE 196
Cdd:cd17922  77 EKAKQLKNPPGILITTPESLELLLVNKKLRELFAGLRYvVVDE 119
PRK08074 PRK08074
bifunctional ATP-dependent DNA helicase/DNA polymerase III subunit epsilon; Validated
40-131 2.79e-04

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


Pssm-ID: 236148 [Multi-domain]  Cd Length: 928  Bit Score: 43.79  E-value: 2.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388   40 SEVASLSSTFKNSLSRA--GFEKMTPvQQRVLNEV---FPNEENAVVQAKTGTGKTLAFLL-VAFKDVLKGKPrlnsski 113
Cdd:PRK08074 236 SDFDAFLEKTEEKLSLAmpKYEKREG-QQEMMKEVytaLRDSEHALIEAGTGTGKSLAYLLpAAYFAKKKEEP------- 307
                         90
                 ....*....|....*....
gi 19112388  114 hsVILSP-TRELALQIFEE 131
Cdd:PRK08074 308 --VVISTyTIQLQQQLLEK 324
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
290-389 3.33e-04

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 43.57  E-value: 3.33e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 290 NPSSRIIVFLP---TISM-VDFVGgvlENHLKIPCFILHS------GLTTAQRRSITESFRKCQSGILFATDVVARGMDF 359
Cdd:COG1111 351 NPDSRIIVFTQyrdTAEMiVEFLS---EPGIKAGRFVGQAskegdkGLTQKEQIEILERFRAGEFNVLVATSVAEEGLDI 427
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 19112388 360 PNITQVV-------QITgpsntddYIHRIGRTGRAGK 389
Cdd:COG1111 428 PEVDLVIfyepvpsEIR-------SIQRKGRTGRKRE 457
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
291-399 3.53e-04

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: 41.08  E-value: 3.53e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 291 PSSRIIVF------LPTISMVdfvggvlenhLKIPcFILHsGLTTAQRRSITESFRKCQSGILFATDVVARGMDFPNITQ 364
Cdd:cd18789  48 QGDKIIVFtdnveaLYRYAKR----------LLKP-FITG-ETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLPEANV 115
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 19112388 365 VVQITG-PSNTDDYIHRIGRTGRAGKTGEAYLILLE 399
Cdd:cd18789 116 AIQISGhGGSRRQEAQRLGRILRPKKGGGKNAFFYS 151
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
64-199 3.95e-04

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: 41.35  E-value: 3.95e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  64 VQQRVLNEVFPN---EENAVVQAKTGTGKTLAFLLVAfkdvlkgKPRLNSSKIHSVILSPTRELALQIFEEARKLTygTG 140
Cdd:cd18035   1 EERRLYQVLIAAvalNGNTLIVLPTGLGKTIIAILVA-------ADRLTKKGGKVLILAPSRPLVEQHAENLKRVL--NI 71
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 141 IRVSYAIGGNSKmREENAIRRGNANLLIATPGRLEDHLQNPRI-LESLSTdsFILDEADR 199
Cdd:cd18035  72 PDKITSLTGEVK-PEERAERWDASKIIVATPQVIENDLLAGRItLDDVSL--LIFDEAHH 128
PRK01172 PRK01172
ATP-dependent DNA helicase;
65-388 5.06e-04

ATP-dependent DNA helicase;


Pssm-ID: 100801 [Multi-domain]  Cd Length: 674  Bit Score: 42.95  E-value: 5.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388   65 QQRVLNEVFPNEENAVVQAKTGTGKTLAFLLVAFKDVLKGKprlnsskiHSVILSPTRELALQIFEEARKLTyGTGIRVS 144
Cdd:PRK01172  26 HQRMAIEQLRKGENVIVSVPTAAGKTLIAYSAIYETFLAGL--------KSIYIVPLRSLAMEKYEELSRLR-SLGMRVK 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  145 YAIGGNSKmrEENAIRRGNAnlLIATPGRLEDHL-QNPRILESLStdSFILDEADRLMDMGFA---ESILNIHEAVtTTK 220
Cdd:PRK01172  97 ISIGDYDD--PPDFIKRYDV--VILTSEKADSLIhHDPYIINDVG--LIVADEIHIIGDEDRGptlETVLSSARYV-NPD 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  221 TRKLCFSATM----------------------PPKVSNVFRGILGTDFKLINCLDPNeppthervpQFVIETKLDK---- 274
Cdd:PRK01172 170 ARILALSATVsnanelaqwlnasliksnfrpvPLKLGILYRKRLILDGYERSQVDIN---------SLIKETVNDGgqvl 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  275 VFSSSLSLLQQLtssnpSSRIIVFLPTISmvDFVGGVLENHLK-------IPCFIL--HSGLTTAQRRSITESFRKCQSG 345
Cdd:PRK01172 241 VFVSSRKNAEDY-----AEMLIQHFPEFN--DFKVSSENNNVYddslnemLPHGVAfhHAGLSNEQRRFIEEMFRNRYIK 313
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 19112388  346 ILFATDVVARGMDFPNITQVVQ-ITGPSNtdDYI---------HRIGRTGRAG 388
Cdd:PRK01172 314 VIVATPTLAAGVNLPARLVIVRdITRYGN--GGIrylsnmeikQMIGRAGRPG 364
DDXDc_reverse_gyrase cd17924
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ...
83-201 6.74e-04

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: 40.77  E-value: 6.74e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  83 AKTGTGKTLAFLLVAFKDVLKGKprlnsskiHSVILSPTRELALQIFEEARKLTYGTG--IRVSYAIGGNSKMREENA-- 158
Cdd:cd17924  39 APTGVGKTTFGLATSLYLASKGK--------RSYLIFPTKSLVKQAYERLSKYAEKAGveVKILVYHSRLKKKEKEELle 110
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 19112388 159 -IRRGNANLLIATPGRLEDhlqNPRILESLSTDSFILDEADRLM 201
Cdd:cd17924 111 kIEKGDFDILVTTNQFLSK---NFDLLSNKKFDFVFVDDVDAVL 151
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
322-403 7.19e-04

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: 40.41  E-value: 7.19e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388 322 ILHSGLTTAQRRSITESFRKCQSGILFATDVVARGMDFPNITQVVQitgpSNTDDY----IHRI-GRTGRAGKtgEAYLI 396
Cdd:cd18811  66 LLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVI----EDAERFglsqLHQLrGRVGRGDH--QSYCL 139

                ....*..
gi 19112388 397 LLEQEKP 403
Cdd:cd18811 140 LVYKDPL 146
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
324-389 1.60e-03

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: 39.17  E-value: 1.60e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19112388 324 HSGLTTAQRRSITESFRKcqsGILFAtdVVAR-----GMDFPNITQVVQITGPSNTDDYIHRIGRTGRAGK 389
Cdd:cd18796  75 HGSLSRELREEVEAALKR---GDLKV--VVATsslelGIDIGDVDLVIQIGSPKSVARLLQRLGRSGHRPG 140
PRK13767 PRK13767
ATP-dependent helicase; Provisional
58-196 2.93e-03

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 40.64  E-value: 2.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388   58 FEKMTPVQQRVLNEVFPNEeNAVVQAKTGTGKTL-AFLLVAFKDVLKGKPRLNSSKIHSVILSPTRELA----------L 126
Cdd:PRK13767  30 FGTFTPPQRYAIPLIHEGK-NVLISSPTGSGKTLaAFLAIIDELFRLGREGELEDKVYCLYVSPLRALNndihrnleepL 108
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19112388  127 Q-IFEEARKLTYG-TGIRVSYAIGGNSKmREENAIRRGNANLLIATPGRLEDHLQNPRILESLSTDSF-ILDE 196
Cdd:PRK13767 109 TeIREIAKERGEElPEIRVAIRTGDTSS-YEKQKMLKKPPHILITTPESLAILLNSPKFREKLRTVKWvIVDE 180
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
65-197 3.68e-03

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: 38.79  E-value: 3.68e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  65 QQRVLNEVFpnEENAVVQAKTGTGKTL-AFLLVafKDVLKGKPRLNSSKIHSVILSPTRELALQIFEEARKLTYGTGIRV 143
Cdd:cd18034   7 QLELFEAAL--KRNTIVVLPTGSGKTLiAVMLI--KEMGELNRKEKNPKKRAVFLVPTVPLVAQQAEAIRSHTDLKVGEY 82
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 19112388 144 SYAIG--GNSKMREENAIRrgNANLLIATPGRLEDHLQNPRI-LESLSTdsFILDEA 197
Cdd:cd18034  83 SGEMGvdKWTKERWKEELE--KYDVLVMTAQILLDALRHGFLsLSDINL--LIFDEC 135
DEXHc_Brr2_1 cd18019
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ...
57-171 5.12e-03

N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 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: 350777 [Multi-domain]  Cd Length: 214  Bit Score: 38.51  E-value: 5.12e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112388  57 GFEKMTPVQQRVLNEVFPNEENAVVQAKTGTGKTLAFLLVAFKDVLK-----GKPRLNSSKIhsVILSPTREL-ALQIFE 130
Cdd:cd18019  14 GFKSLNRIQSKLFPAAFETDENLLLCAPTGAGKTNVALLTILREIGKhrnpdGTINLDAFKI--VYIAPMKALvQEMVGN 91
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 19112388 131 EARKLTYgTGIRVSYAIGGNSKMREENAirrgNANLLIATP 171
Cdd:cd18019  92 FSKRLAP-YGITVAELTGDQQLTKEQIS----ETQIIVTTP 127
 
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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