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Conserved domains on  [gi|21410145|gb|AAH30895|]
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Ddx21 protein, partial [Mus musculus]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 11423699)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
98-484 5.55e-146

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


:

Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 431.49  E-value: 5.55e-146
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145  98 FSNFPISEETVKLLKARGVNFLFPIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKLqgglqERKRGRAPQVLVLA 177
Cdd:COG0513   4 FADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRL-----DPSRPRAPQALILA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 178 PTRELANQVSKDFSDITK--KLSVACFYGGTPYGGQIERMRSGIDILVGTPGRIKDHLQNGKLDLTKLKHVVLDEVDQML 255
Cdd:COG0513  79 PTRELALQVAEELRKLAKylGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRML 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 256 DMGFADQVEEILcvaykKDSEDNPQTLLFSATCPHWVFNVAKKYMKStYEQVDlIGKKTQKAAiTVEHLAIKCHWTERAA 335
Cdd:COG0513 159 DMGFIEDIERIL-----KLLPKERQTLLFSATMPPEIRKLAKRYLKN-PVRIE-VAPENATAE-TIEQRYYLVDKRDKLE 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 336 VIGDVIRVYSGhqGRTIIFCETKKDAQELSQNTCIKQ-DAQSLHGDIPQKQREITLKGFRNGNFGVLVATNVAARGLDIP 414
Cdd:COG0513 231 LLRRLLRDEDP--ERAIVFCNTKRGADRLAEKLQKRGiSAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDID 308
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 415 EVDLVVQSCPPKDVESYIHRSGRTGRAGRTGVCICFYQNKEEYQLAQVEQKAGIKFKRIGVPSATEIIKA 484
Cdd:COG0513 309 DVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEK 378
GUCT_RHII_Gualpha_beta cd12936
RNA-binding GUCT domain found in vertebrate RNA helicase II/Gualpha (RH-II/Gualpha), RNA ...
527-619 1.11e-51

RNA-binding GUCT domain found in vertebrate RNA helicase II/Gualpha (RH-II/Gualpha), RNA helicase II/Gubeta (RH-II/Gubeta) and similar proteins; This subfamily corresponds to the Gu C-terminal (GUCT) domain of RH-II/Gualpha and RH-II/Gubeta, two paralogues found in vertebrates. RH-II/Gualpha, also termed nucleolar RNA helicase 2, or DEAD box protein 21, or nucleolar RNA helicase Gu, is a bifunctional enzyme that displays independent RNA-unwinding and RNA-folding activities. It unwinds double-stranded RNA in the 5' to 3' direction in the presence of Mg2+ through the domains in its N-terminal region. In contrast, it folds single-stranded RNA in an ATP-dependent manner and its C-terminal region is responsible for the Mg2+ independent RNA-foldase activity. RH-II/Gualpha consists of a DEAD box helicase domain (DEAD), a helicase conserved C-terminal domain (helicase_C), and a GUCT followed by three FRGQR repeats and one PRGQR sequence. The DEAD and helicase_C domains may play critical roles in the RNA-helicase activity of RH-II/Gualpha. The function of GUCT domain remains unclear. The C-terminal region responsible for the RNA-foldase activity does not overlap with the GUCT domain. RH-II/Gubeta, also termed ATP-dependent RNA helicase DDX50, or DEAD box protein 50, or nucleolar protein Gu2, shows significant sequence homology with RH-II/Gualpha. It contains a DEAD domain, a helicase_C domain, and a GUCT domain followed by an arginine-serine-rich sequence but not (F/P)RGQR repeats in RH-II/Gualpha. Both RH-II/Gualpha and RH-II/Gubeta localize to nucleoli, suggesting roles in ribosomal RNA production, but RH-II/Gubeta also localizes to nuclear speckles containing the splicing factor SC35, suggesting its possible involvement in pre-mRNA splicing. In contrast to RH-II/Gualpha, RH-II/Gubeta has RNA-unwinding activity, but no RNA-folding activity.


:

Pssm-ID: 240593  Cd Length: 93  Bit Score: 173.79  E-value: 1.11e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 527 HISGATSVDQRSLINSQAGFVTMILRCSIEMPNISYAWKELKEQLGESIDAKVKGMVFLKGKLGVCFDVRTEAVTEIQEK 606
Cdd:cd12936   1 HISGATSKEQRSLLNSDKGFVTMALRCSEEIPNRSYAWKELKEKLGVDADAHISRMCLLKGRMGVCFDVPTAEVESIQAE 80
                        90
                ....*....|...
gi 21410145 607 WHDSRRWQLTVAT 619
Cdd:cd12936  81 WHDSRRWQLSVAT 93
AdoMet_MTases super family cl17173
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
632-678 4.39e-03

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


The actual alignment was detected with superfamily member PTZ00146:

Pssm-ID: 473071  Cd Length: 293  Bit Score: 39.72  E-value: 4.39e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 21410145  632 RGRMGQRDGSRGAFRGQRGGSRNFRGQGQRGGSRNFRGQRPGGGNRG 678
Cdd:PTZ00146   4 GGFGGGRGGGRGGGGGGGRGGGGRGGGRGGGRGRGRGGGGGGRGGGG 50
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
98-484 5.55e-146

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 431.49  E-value: 5.55e-146
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145  98 FSNFPISEETVKLLKARGVNFLFPIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKLqgglqERKRGRAPQVLVLA 177
Cdd:COG0513   4 FADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRL-----DPSRPRAPQALILA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 178 PTRELANQVSKDFSDITK--KLSVACFYGGTPYGGQIERMRSGIDILVGTPGRIKDHLQNGKLDLTKLKHVVLDEVDQML 255
Cdd:COG0513  79 PTRELALQVAEELRKLAKylGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRML 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 256 DMGFADQVEEILcvaykKDSEDNPQTLLFSATCPHWVFNVAKKYMKStYEQVDlIGKKTQKAAiTVEHLAIKCHWTERAA 335
Cdd:COG0513 159 DMGFIEDIERIL-----KLLPKERQTLLFSATMPPEIRKLAKRYLKN-PVRIE-VAPENATAE-TIEQRYYLVDKRDKLE 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 336 VIGDVIRVYSGhqGRTIIFCETKKDAQELSQNTCIKQ-DAQSLHGDIPQKQREITLKGFRNGNFGVLVATNVAARGLDIP 414
Cdd:COG0513 231 LLRRLLRDEDP--ERAIVFCNTKRGADRLAEKLQKRGiSAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDID 308
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 415 EVDLVVQSCPPKDVESYIHRSGRTGRAGRTGVCICFYQNKEEYQLAQVEQKAGIKFKRIGVPSATEIIKA 484
Cdd:COG0513 309 DVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEK 378
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
107-308 3.28e-144

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: 418.48  E-value: 3.28e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 107 TVKLLKARGVNFLFPIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKLQGGLQERKRGRAPQVLVLAPTRELANQV 186
Cdd:cd17944   1 TIKLLQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRKRGRAPKVLVLAPTRELANQV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 187 SKDFSDITKKLSVACFYGGTPYGGQIERMRSGIDILVGTPGRIKDHLQNGKLDLTKLKHVVLDEVDQMLDMGFADQVEEI 266
Cdd:cd17944  81 TKDFKDITRKLSVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEI 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 21410145 267 LCVAYKKDSEDNPQTLLFSATCPHWVFNVAKKYMKSTYEQVD 308
Cdd:cd17944 161 LSVSYKKDSEDNPQTLLFSATCPDWVYNVAKKYMKSQYEQVD 202
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
97-479 7.15e-96

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 303.65  E-value: 7.15e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145   97 AFSNFPISEETVKLLKARGVNFLFPIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKLQgglqerKRGRAPQVLVL 176
Cdd:PRK11776   5 AFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLD------VKRFRVQALVL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145  177 APTRELANQVSKD------FSDITKKLSVaCfyGGTPYGGQIERMRSGIDILVGTPGRIKDHLQNGKLDLTKLKHVVLDE 250
Cdd:PRK11776  79 CPTRELADQVAKEirrlarFIPNIKVLTL-C--GGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDE 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145  251 VDQMLDMGFADQVEEILCVAYKKDsednpQTLLFSATCPHWVFNVAKKYMKSTYE-QVDligkkTQKAAITVEHLAIKCH 329
Cdd:PRK11776 156 ADRMLDMGFQDAIDAIIRQAPARR-----QTLLFSATYPEGIAAISQRFQRDPVEvKVE-----STHDLPAIEQRFYEVS 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145  330 WTERAAVigdVIRVYSGHQ-GRTIIFCETKKDAQELSQN-TCIKQDAQSLHGDIPQKQREITLKGFRNGNFGVLVATNVA 407
Cdd:PRK11776 226 PDERLPA---LQRLLLHHQpESCVVFCNTKKECQEVADAlNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVA 302
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21410145  408 ARGLDIPEVDLVVQSCPPKDVESYIHRSGRTGRAGRTGVCICFYQNKEEYQLAQVEQKAGIKFKRIGVPSAT 479
Cdd:PRK11776 303 ARGLDIKALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLPSLS 374
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
121-295 2.38e-53

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: 180.90  E-value: 2.38e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145   121 PIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKLqgglqeRKRGRAPQVLVLAPTRELANQVSKDFSDITK--KLS 198
Cdd:pfam00270   2 PIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEAL------DKLDNGPQALVLAPTRELAEQIYEELKKLGKglGLK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145   199 VACFYGGTPYGGQIERMRsGIDILVGTPGRIKDHLQNGKLdLTKLKHVVLDEVDQMLDMGFADQVEEILcvaykKDSEDN 278
Cdd:pfam00270  76 VASLLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQERKL-LKNLKLLVLDEAHRLLDMGFGPDLEEIL-----RRLPKK 148
                         170
                  ....*....|....*..
gi 21410145   279 PQTLLFSATCPHWVFNV 295
Cdd:pfam00270 149 RQILLLSATLPRNLEDL 165
GUCT_RHII_Gualpha_beta cd12936
RNA-binding GUCT domain found in vertebrate RNA helicase II/Gualpha (RH-II/Gualpha), RNA ...
527-619 1.11e-51

RNA-binding GUCT domain found in vertebrate RNA helicase II/Gualpha (RH-II/Gualpha), RNA helicase II/Gubeta (RH-II/Gubeta) and similar proteins; This subfamily corresponds to the Gu C-terminal (GUCT) domain of RH-II/Gualpha and RH-II/Gubeta, two paralogues found in vertebrates. RH-II/Gualpha, also termed nucleolar RNA helicase 2, or DEAD box protein 21, or nucleolar RNA helicase Gu, is a bifunctional enzyme that displays independent RNA-unwinding and RNA-folding activities. It unwinds double-stranded RNA in the 5' to 3' direction in the presence of Mg2+ through the domains in its N-terminal region. In contrast, it folds single-stranded RNA in an ATP-dependent manner and its C-terminal region is responsible for the Mg2+ independent RNA-foldase activity. RH-II/Gualpha consists of a DEAD box helicase domain (DEAD), a helicase conserved C-terminal domain (helicase_C), and a GUCT followed by three FRGQR repeats and one PRGQR sequence. The DEAD and helicase_C domains may play critical roles in the RNA-helicase activity of RH-II/Gualpha. The function of GUCT domain remains unclear. The C-terminal region responsible for the RNA-foldase activity does not overlap with the GUCT domain. RH-II/Gubeta, also termed ATP-dependent RNA helicase DDX50, or DEAD box protein 50, or nucleolar protein Gu2, shows significant sequence homology with RH-II/Gualpha. It contains a DEAD domain, a helicase_C domain, and a GUCT domain followed by an arginine-serine-rich sequence but not (F/P)RGQR repeats in RH-II/Gualpha. Both RH-II/Gualpha and RH-II/Gubeta localize to nucleoli, suggesting roles in ribosomal RNA production, but RH-II/Gubeta also localizes to nuclear speckles containing the splicing factor SC35, suggesting its possible involvement in pre-mRNA splicing. In contrast to RH-II/Gualpha, RH-II/Gubeta has RNA-unwinding activity, but no RNA-folding activity.


Pssm-ID: 240593  Cd Length: 93  Bit Score: 173.79  E-value: 1.11e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 527 HISGATSVDQRSLINSQAGFVTMILRCSIEMPNISYAWKELKEQLGESIDAKVKGMVFLKGKLGVCFDVRTEAVTEIQEK 606
Cdd:cd12936   1 HISGATSKEQRSLLNSDKGFVTMALRCSEEIPNRSYAWKELKEKLGVDADAHISRMCLLKGRMGVCFDVPTAEVESIQAE 80
                        90
                ....*....|...
gi 21410145 607 WHDSRRWQLTVAT 619
Cdd:cd12936  81 WHDSRRWQLSVAT 93
DEXDc smart00487
DEAD-like helicases superfamily;
111-301 1.10e-48

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 169.59  E-value: 1.10e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145    111 LKARGVNFLFPIQAKTFHHVYSG-KDLIAQARTGTGKTFSFAIPLIEKLqgglqerKRGRAPQVLVLAPTRELANQVSKD 189
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEAL-------KRGKGGRVLVLVPTRELAEQWAEE 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145    190 FSDITKK--LSVACFYGGTPYGGQIERMRSG-IDILVGTPGRIKDHLQNGKLDLTKLKHVVLDEVDQMLDMGFADQVEEI 266
Cdd:smart00487  74 LKKLGPSlgLKVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKL 153
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 21410145    267 LCVAYKkdsedNPQTLLFSATCPHWVFNVAKKYMK 301
Cdd:smart00487 154 LKLLPK-----NVQLLLLSATPPEEIENLLELFLN 183
GUCT pfam08152
GUCT (NUC152) domain; This is the C terminal domain found in the RNA helicase II / Gu protein ...
530-625 5.39e-41

GUCT (NUC152) domain; This is the C terminal domain found in the RNA helicase II / Gu protein family.


Pssm-ID: 462378  Cd Length: 96  Bit Score: 144.60  E-value: 5.39e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145   530 GATSVDQRSLINSQAGFVTMILRCSIEMPNISYAWKELKEQLGESIDAKVKGMVFLKGKLGVCFDVRTEAVTEIQEKWHD 609
Cdd:pfam08152   1 GYTEIKQRSLLSSEEGFVTLLLTSSREIRTPGYAWSILRRNLSEEIADKVKGMRLTKDKMGAVFDVPSELVEEFLAGWED 80
                          90
                  ....*....|....*.
gi 21410145   610 SRRWQLTVATEQPELE 625
Cdd:pfam08152  81 SRGVTLEVATELPELQ 96
cas3_core TIGR01587
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ...
135-443 7.86e-09

CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an alignment of Cas3, a protein found in association with CRISPR repeat elements in a broad range of bacteria and archaea. Cas3 appears to be a helicase, with regions found by pfam00270 (DEAD/DEAH box helicase) and pfam00271 (Helicase conserved C-terminal domain). Some but not all members have an N-terminal HD domain region (pfam01966) that is not included within this model.


Pssm-ID: 273707 [Multi-domain]  Cd Length: 359  Bit Score: 57.85  E-value: 7.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145   135 DLIAQARTGTGKT---FSFAIPLIeklqgglqerKRGRAPQVLVLAPTRELAN----QVSKDFSDITKKL-SVACFYGGT 206
Cdd:TIGR01587   1 LLVIEAPTGYGKTeaaLLWALHSI----------KSQKADRVIIALPTRATINamyrRAKELFGSELVGLhHSSSFSRIK 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145   207 PYG--GQIERMRS--GIDILVGTPGRIK----DHLQN------GKLDLTKL----KHVVLDEVDqmldmGFADQVEEILC 268
Cdd:TIGR01587  71 EMGdsEEFEHLFPlyIHSNDKLFLDPITvctiDQVLKsvfgefGHYEFTLAsianSLLIFDEVH-----FYDEYTLALIL 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145   269 VAYKKDSEDNPQTLLFSATCPhwvfNVAKKYMKSTYEQVDLIGKKTQKAAITVEHLAIKC--HWTERAAVIGDVIRVYSG 346
Cdd:TIGR01587 146 AVLEVLKDNDVPILLMSATLP----KFLKEYAEKIGYVEFNEPLDLKEERRFENHRFILIesDKVGEISSLERLLEFIKK 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145   347 hQGRTIIFCETKKDAQELSQNtcIKQDAQS-----LHGDIPQKQRE----ITLKGFRNGN-FGVLVATNVAARGLDIpEV 416
Cdd:TIGR01587 222 -GGSIAIIVNTVDRAQEFYQQ--LKEKAPEeeiilYHSRFTEKDRAkkeaELLREMKKSNeKFVIVATQVIEASLDI-SA 297
                         330       340
                  ....*....|....*....|....*...
gi 21410145   417 D-LVVQSCPPkdvESYIHRSGRTGRAGR 443
Cdd:TIGR01587 298 DvMITELAPI---DSLIQRLGRLHRYGR 322
PTZ00146 PTZ00146
fibrillarin; Provisional
632-678 4.39e-03

fibrillarin; Provisional


Pssm-ID: 240291  Cd Length: 293  Bit Score: 39.72  E-value: 4.39e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 21410145  632 RGRMGQRDGSRGAFRGQRGGSRNFRGQGQRGGSRNFRGQRPGGGNRG 678
Cdd:PTZ00146   4 GGFGGGRGGGRGGGGGGGRGGGGRGGGRGGGRGRGRGGGGGGRGGGG 50
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
98-484 5.55e-146

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 431.49  E-value: 5.55e-146
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145  98 FSNFPISEETVKLLKARGVNFLFPIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKLqgglqERKRGRAPQVLVLA 177
Cdd:COG0513   4 FADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRL-----DPSRPRAPQALILA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 178 PTRELANQVSKDFSDITK--KLSVACFYGGTPYGGQIERMRSGIDILVGTPGRIKDHLQNGKLDLTKLKHVVLDEVDQML 255
Cdd:COG0513  79 PTRELALQVAEELRKLAKylGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRML 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 256 DMGFADQVEEILcvaykKDSEDNPQTLLFSATCPHWVFNVAKKYMKStYEQVDlIGKKTQKAAiTVEHLAIKCHWTERAA 335
Cdd:COG0513 159 DMGFIEDIERIL-----KLLPKERQTLLFSATMPPEIRKLAKRYLKN-PVRIE-VAPENATAE-TIEQRYYLVDKRDKLE 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 336 VIGDVIRVYSGhqGRTIIFCETKKDAQELSQNTCIKQ-DAQSLHGDIPQKQREITLKGFRNGNFGVLVATNVAARGLDIP 414
Cdd:COG0513 231 LLRRLLRDEDP--ERAIVFCNTKRGADRLAEKLQKRGiSAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDID 308
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 415 EVDLVVQSCPPKDVESYIHRSGRTGRAGRTGVCICFYQNKEEYQLAQVEQKAGIKFKRIGVPSATEIIKA 484
Cdd:COG0513 309 DVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEK 378
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
107-308 3.28e-144

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: 418.48  E-value: 3.28e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 107 TVKLLKARGVNFLFPIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKLQGGLQERKRGRAPQVLVLAPTRELANQV 186
Cdd:cd17944   1 TIKLLQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRKRGRAPKVLVLAPTRELANQV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 187 SKDFSDITKKLSVACFYGGTPYGGQIERMRSGIDILVGTPGRIKDHLQNGKLDLTKLKHVVLDEVDQMLDMGFADQVEEI 266
Cdd:cd17944  81 TKDFKDITRKLSVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEI 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 21410145 267 LCVAYKKDSEDNPQTLLFSATCPHWVFNVAKKYMKSTYEQVD 308
Cdd:cd17944 161 LSVSYKKDSEDNPQTLLFSATCPDWVYNVAKKYMKSQYEQVD 202
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
97-479 7.15e-96

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 303.65  E-value: 7.15e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145   97 AFSNFPISEETVKLLKARGVNFLFPIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKLQgglqerKRGRAPQVLVL 176
Cdd:PRK11776   5 AFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLD------VKRFRVQALVL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145  177 APTRELANQVSKD------FSDITKKLSVaCfyGGTPYGGQIERMRSGIDILVGTPGRIKDHLQNGKLDLTKLKHVVLDE 250
Cdd:PRK11776  79 CPTRELADQVAKEirrlarFIPNIKVLTL-C--GGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDE 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145  251 VDQMLDMGFADQVEEILCVAYKKDsednpQTLLFSATCPHWVFNVAKKYMKSTYE-QVDligkkTQKAAITVEHLAIKCH 329
Cdd:PRK11776 156 ADRMLDMGFQDAIDAIIRQAPARR-----QTLLFSATYPEGIAAISQRFQRDPVEvKVE-----STHDLPAIEQRFYEVS 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145  330 WTERAAVigdVIRVYSGHQ-GRTIIFCETKKDAQELSQN-TCIKQDAQSLHGDIPQKQREITLKGFRNGNFGVLVATNVA 407
Cdd:PRK11776 226 PDERLPA---LQRLLLHHQpESCVVFCNTKKECQEVADAlNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVA 302
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21410145  408 ARGLDIPEVDLVVQSCPPKDVESYIHRSGRTGRAGRTGVCICFYQNKEEYQLAQVEQKAGIKFKRIGVPSAT 479
Cdd:PRK11776 303 ARGLDIKALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLPSLS 374
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
107-301 8.17e-87

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: 270.47  E-value: 8.17e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 107 TVKLLKARGVNFLFPIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKLQGglQERKRGRAPQVLVLAPTRELANQV 186
Cdd:cd00268   1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLP--EPKKKGRGPQALVLAPTRELAMQI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 187 SKDFSDITK--KLSVACFYGGTPYGGQIERMRSGIDILVGTPGRIKDHLQNGKLDLTKLKHVVLDEVDQMLDMGFADQVE 264
Cdd:cd00268  79 AEVARKLGKgtGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVE 158
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 21410145 265 EILcvaykKDSEDNPQTLLFSATCPHWVFNVAKKYMK 301
Cdd:cd00268 159 KIL-----SALPKDRQTLLFSATLPEEVKELAKKFLK 190
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
95-478 6.08e-75

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 253.23  E-value: 6.08e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145   95 EGAFSNFPISEETVKLLKARGVNFLFPIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKLQGGLqerkrgRAPQVL 174
Cdd:PRK11634   5 ETTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPEL------KAPQIL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145  175 VLAPTRELANQVSK---DFSDITKKLSVACFYGGTPYGGQIERMRSGIDILVGTPGRIKDHLQNGKLDLTKLKHVVLDEV 251
Cdd:PRK11634  79 VLAPTRELAVQVAEamtDFSKHMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145  252 DQMLDMGFADQVEEILCvaykkDSEDNPQTLLFSATCPHWVFNVAKKYMKSTYEqVDLIGKKTQKAAITvehlaiKCHWT 331
Cdd:PRK11634 159 DEMLRMGFIEDVETIMA-----QIPEGHQTALFSATMPEAIRRITRRFMKEPQE-VRIQSSVTTRPDIS------QSYWT 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145  332 ERAAVIGD-VIRVYSGHQ-GRTIIFCETKKD----AQELSQNtciKQDAQSLHGDIPQKQREITLKGFRNGNFGVLVATN 405
Cdd:PRK11634 227 VWGMRKNEaLVRFLEAEDfDAAIIFVRTKNAtlevAEALERN---GYNSAALNGDMNQALREQTLERLKDGRLDILIATD 303
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21410145  406 VAARGLDIPEVDLVVQSCPPKDVESYIHRSGRTGRAGRTGVCICFYQNKEEYQLAQVEQKAGIKFKRIGVPSA 478
Cdd:PRK11634 304 VAARGLDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEVELPNA 376
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
29-471 1.53e-71

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 240.20  E-value: 1.53e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145   29 PSEEEVDIPKPKKMKKGKEASGDAGEKSPRLKDGLSQPSEPKSNSSDAPGEESSSETEKEIPVEQKEGaFSNFPISEETV 108
Cdd:PRK01297  21 PPSPAAAPAPPPPAKTAAPATKAAAPAAAAPRAEKPKKDKPRRERKPKPASLWKLEDFVVEPQEGKTR-FHDFNLAPELM 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145  109 KLLKARGVNFLFPIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKLQGG--LQERKRGRaPQVLVLAPTRELANQV 186
Cdd:PRK01297 100 HAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTppPKERYMGE-PRALIIAPTRELVVQI 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145  187 SKDFSDITK--KLSVACFYGGTPYGGQIERMRSG-IDILVGTPGRIKDHLQNGKLDLTKLKHVVLDEVDQMLDMGFADQV 263
Cdd:PRK01297 179 AKDAAALTKytGLNVMTFVGGMDFDKQLKQLEARfCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEADRMLDMGFIPQV 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145  264 EEILCVAYKKDSEdnpQTLLFSATCPHWVFNVAKKYmksTYEQVDLIGKKTQKAAITVEHLAIKCHWTERAAVIGDVIRv 343
Cdd:PRK01297 259 RQIIRQTPRKEER---QTLLFSATFTDDVMNLAKQW---TTDPAIVEIEPENVASDTVEQHVYAVAGSDKYKLLYNLVT- 331
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145  344 ySGHQGRTIIFCETKKDAQELSQNtcIKQD---AQSLHGDIPQKQREITLKGFRNGNFGVLVATNVAARGLDIPEVDLVV 420
Cdd:PRK01297 332 -QNPWERVMVFANRKDEVRRIEER--LVKDginAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVI 408
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 21410145  421 QSCPPKDVESYIHRSGRTGRAGRTGVCICFYQNKEEYQLAQVEQKAGIKFK 471
Cdd:PRK01297 409 NFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKIS 459
PTZ00110 PTZ00110
helicase; Provisional
90-461 5.78e-64

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 221.57  E-value: 5.78e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145   90 PVEQKEgaFSNFPisEETVKLLKARGVNFLFPIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKLQGglQERKR-G 168
Cdd:PTZ00110 128 PVVSFE--YTSFP--DYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINA--QPLLRyG 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145  169 RAPQVLVLAPTRELANQVSKD---FSDITKkLSVACFYGGTPYGGQIERMRSGIDILVGTPGRIKDHLQNGKLDLTKLKH 245
Cdd:PTZ00110 202 DGPIVLVLAPTRELAEQIREQcnkFGASSK-IRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTY 280
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145  246 VVLDEVDQMLDMGFADQVEEILcvaykkdSEDNP--QTLLFSATCPHWVFNVAKKYMKSTYEQVDlIGKKTQKAAITVEH 323
Cdd:PTZ00110 281 LVLDEADRMLDMGFEPQIRKIV-------SQIRPdrQTLMWSATWPKEVQSLARDLCKEEPVHVN-VGSLDLTACHNIKQ 352
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145  324 LAIKCHWTERAAVIGDVIRVYSGHQGRTIIFCETKKDAQELSQNtcIKQD---AQSLHGDIPQKQREITLKGFRNGNFGV 400
Cdd:PTZ00110 353 EVFVVEEHEKRGKLKMLLQRIMRDGDKILIFVETKKGADFLTKE--LRLDgwpALCIHGDKKQEERTWVLNEFKTGKSPI 430
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21410145  401 LVATNVAARGLDIPEVDLVVQSCPPKDVESYIHRSGRTGRAGRTGVCICFYqNKEEYQLAQ 461
Cdd:PTZ00110 431 MIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFL-TPDKYRLAR 490
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
92-498 3.17e-63

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 216.38  E-value: 3.17e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145   92 EQKegaFSNFPISEETVKLLKARGVNFLFPIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKL-QGGLQERKRGRA 170
Cdd:PRK04837   7 EQK---FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLlSHPAPEDRKVNQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145  171 PQVLVLAPTRELANQVSKDFSDITK--KLSVACFYGGTPYGGQIERMRSGIDILVGTPGRIKDHLQNGKLDLTKLKHVVL 248
Cdd:PRK04837  84 PRALIMAPTRELAVQIHADAEPLAQatGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145  249 DEVDQMLDMGFadqVEEILCVAYKKDSEDNPQTLLFSATCPHWVFNVAKKYMKS-TYEQVDligkKTQKAA--ITVE--- 322
Cdd:PRK04837 164 DEADRMFDLGF---IKDIRWLFRRMPPANQRLNMLFSATLSYRVRELAFEHMNNpEYVEVE----PEQKTGhrIKEElfy 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145  323 ----------HLAIKCHWTERAavigdvirvysghqgrtIIFCETKKDAQELSQNtcIKQDAQS---LHGDIPQKQREIT 389
Cdd:PRK04837 237 psneekmrllQTLIEEEWPDRA-----------------IIFANTKHRCEEIWGH--LAADGHRvglLTGDVAQKKRLRI 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145  390 LKGFRNGNFGVLVATNVAARGLDIPEVDLVVQSCPPKDVESYIHRSGRTGRAGRTGVCICFyqNKEEY--QLAQVEQkag 467
Cdd:PRK04837 298 LEEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL--ACEEYalNLPAIET--- 372
                        410       420       430
                 ....*....|....*....|....*....|.
gi 21410145  468 ikfkRIGVPsateiIKASSKDAIRLLDSVPP 498
Cdd:PRK04837 373 ----YIGHS-----IPVSKYDSDALLTDLPK 394
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
98-448 1.12e-62

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 215.19  E-value: 1.12e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145   98 FSNFPISEETVKLLKARGVNFLFPIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKLQGglQERKRGRAPQVLVLA 177
Cdd:PRK11192   3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLD--FPRRKSGPPRILILT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145  178 PTRELANQVSKDFSDITK--KLSVACFYGGTPYGGQIERMRSGIDILVGTPGRIKDHLQNGKLDLTKLKHVVLDEVDQML 255
Cdd:PRK11192  81 PTRELAMQVADQARELAKhtHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRML 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145  256 DMGFADQVEEILCVA-YKKdsednpQTLLFSATCP-HWVFNVAKKYMKSTyEQVDLIGKKTQKAAI--------TVEH-L 324
Cdd:PRK11192 161 DMGFAQDIETIAAETrWRK------QTLLFSATLEgDAVQDFAERLLNDP-VEVEAEPSRRERKKIhqwyyradDLEHkT 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145  325 AIKCHWTERAAVigdvirvysghqGRTIIFCETKKDAQELSqNTCIKQDAQS--LHGDIPQKQREITLKGFRNGNFGVLV 402
Cdd:PRK11192 234 ALLCHLLKQPEV------------TRSIVFVRTRERVHELA-GWLRKAGINCcyLEGEMVQAKRNEAIKRLTDGRVNVLV 300
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 21410145  403 ATNVAARGLDIPEVDLVVQSCPPKDVESYIHRSGRTGRAGRTGVCI 448
Cdd:PRK11192 301 ATDVAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAI 346
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
103-308 2.06e-58

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: 196.26  E-value: 2.06e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 103 ISEETVKLLKARGVNFLFPIQAKTFHHVYS-GKDLIAQARTGTGKTFSFAIPLIEKLqggLQERKRGRAPQV--LVLAPT 179
Cdd:cd17964   1 LDPSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSL---LNTKPAGRRSGVsaLIISPT 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 180 RELANQVSKDFSDIT---KKLSVACFYGGTPYGGQIERM-RSGIDILVGTPGRIKDHLQN--GKLDLTKLKHVVLDEVDQ 253
Cdd:cd17964  78 RELALQIAAEAKKLLqglRKLRVQSAVGGTSRRAELNRLrRGRPDILVATPGRLIDHLENpgVAKAFTDLDYLVLDEADR 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21410145 254 MLDMGFADQVEEILcVAYKKDSEDNPQTLLFSATCPHWVFNVAKKYMKSTYEQVD 308
Cdd:cd17964 158 LLDMGFRPDLEQIL-RHLPEKNADPRQTLLFSATVPDEVQQIARLTLKKDYKFID 211
PTZ00424 PTZ00424
helicase 45; Provisional
122-464 2.43e-56

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 196.97  E-value: 2.43e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145  122 IQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKLQGGLqerkrgRAPQVLVLAPTRELANQVSKDFSDITKKLSVAC 201
Cdd:PTZ00424  54 IQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDL------NACQALILAPTRELAQQIQKVVLALGDYLKVRC 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145  202 F--YGGTPYGGQIERMRSGIDILVGTPGRIKDHLQNGKLDLTKLKHVVLDEVDQMLDMGFADQVEEIlcvaYKKDSEDnP 279
Cdd:PTZ00424 128 HacVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRGFKGQIYDV----FKKLPPD-V 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145  280 QTLLFSATCPHWVFNVAKKYMKS------TYEQVDLIGKKTQKAAITVEH--LAIKCHWTERAAVIgdvirvysghqgRT 351
Cdd:PTZ00424 203 QVALFSATMPNEILELTTKFMRDpkrilvKKDELTLEGIRQFYVAVEKEEwkFDTLCDLYETLTIT------------QA 270
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145  352 IIFCETKKDAQELSQNTCIKQ-DAQSLHGDIPQKQREITLKGFRNGNFGVLVATNVAARGLDIPEVDLVVQSCPPKDVES 430
Cdd:PTZ00424 271 IIYCNTRRKVDYLTKKMHERDfTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPEN 350
                        330       340       350
                 ....*....|....*....|....*....|....
gi 21410145  431 YIHRSGRTGRAGRTGVCICFYQNKEEYQLAQVEQ 464
Cdd:PTZ00424 351 YIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIER 384
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
98-465 2.29e-55

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 198.64  E-value: 2.29e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145   98 FSNFPISEETVKLLKARGVNFLFPIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKL--QGGLQERKRgRAPQVLV 175
Cdd:PRK04537  11 FSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLlsRPALADRKP-EDPRALI 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145  176 LAPTRELANQVSKDFSDITKKLSV--ACFYGGTPYGGQIERMRSGIDILVGTPGRIKDHLQNGKL-DLTKLKHVVLDEVD 252
Cdd:PRK04537  90 LAPTRELAIQIHKDAVKFGADLGLrfALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVvSLHACEICVLDEAD 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145  253 QMLDMGFadqVEEILCVAYKKDSEDNPQTLLFSATCPHWVFNVAKKYMKSTYEQVdligkkTQKAAITVEHLAIKCHWTE 332
Cdd:PRK04537 170 RMFDLGF---IKDIRFLLRRMPERGTRQTLLFSATLSHRVLELAYEHMNEPEKLV------VETETITAARVRQRIYFPA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145  333 RAAVIGDVIRVYSGHQG-RTIIFCETK----KDAQELSQNtciKQDAQSLHGDIPQKQREITLKGFRNGNFGVLVATNVA 407
Cdd:PRK04537 241 DEEKQTLLLGLLSRSEGaRTMVFVNTKafveRVARTLERH---GYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVA 317
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21410145  408 ARGLDIPEVDLVVQSCPPKDVESYIHRSGRTGRAGRTGVCICFYQNKEEYQL----AQVEQK 465
Cdd:PRK04537 318 ARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLpdieAYIEQK 379
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
121-295 2.38e-53

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: 180.90  E-value: 2.38e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145   121 PIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKLqgglqeRKRGRAPQVLVLAPTRELANQVSKDFSDITK--KLS 198
Cdd:pfam00270   2 PIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEAL------DKLDNGPQALVLAPTRELAEQIYEELKKLGKglGLK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145   199 VACFYGGTPYGGQIERMRsGIDILVGTPGRIKDHLQNGKLdLTKLKHVVLDEVDQMLDMGFADQVEEILcvaykKDSEDN 278
Cdd:pfam00270  76 VASLLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQERKL-LKNLKLLVLDEAHRLLDMGFGPDLEEIL-----RRLPKK 148
                         170
                  ....*....|....*..
gi 21410145   279 PQTLLFSATCPHWVFNV 295
Cdd:pfam00270 149 RQILLLSATLPRNLEDL 165
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
97-448 3.22e-53

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 190.02  E-value: 3.22e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145   97 AFSNFPISEETVKLLKARGVNFLFPIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKLQGGLQERKRGRAPQVLVL 176
Cdd:PRK10590   2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGRRPVRALIL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145  177 APTRELANQVSKDFSDITKKLSVACF--YGGTPYGGQIERMRSGIDILVGTPGRIKDHLQNGKLDLTKLKHVVLDEVDQM 254
Cdd:PRK10590  82 TPTRELAAQIGENVRDYSKYLNIRSLvvFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRM 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145  255 LDMGFADQVEEILCVAYKKDsednpQTLLFSATCPHWVFNVAKKYMKSTyEQVDLIGKKTQKAAITVE-HLAIKCHWTER 333
Cdd:PRK10590 162 LDMGFIHDIRRVLAKLPAKR-----QNLLFSATFSDDIKALAEKLLHNP-LEIEVARRNTASEQVTQHvHFVDKKRKREL 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145  334 -AAVIGDvirvysGHQGRTIIFCETKKDAQELSQNtcIKQD---AQSLHGDIPQKQREITLKGFRNGNFGVLVATNVAAR 409
Cdd:PRK10590 236 lSQMIGK------GNWQQVLVFTRTKHGANHLAEQ--LNKDgirSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAAR 307
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 21410145  410 GLDIPEVDLVVQSCPPKDVESYIHRSGRTGRAGRTG-----VCI 448
Cdd:PRK10590 308 GLDIEELPHVVNYELPNVPEDYVHRIGRTGRAAATGealslVCV 351
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
121-301 8.12e-53

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: 181.53  E-value: 8.12e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 121 PIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKL--QGGLQERKRGRA--PQVLVLAPTRELANQ---VSKDFSDI 193
Cdd:cd17967  25 PVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLleDGPPSVGRGRRKayPSALILAPTRELAIQiyeEARKFSYR 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 194 TKKLSVACfYGGTPYGGQIERMRSGIDILVGTPGRIKDHLQNGKLDLTKLKHVVLDEVDQMLDMGFADQVEEILcvaykk 273
Cdd:cd17967 105 SGVRSVVV-YGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDEADRMLDMGFEPQIRKIV------ 177
                       170       180       190
                ....*....|....*....|....*....|...
gi 21410145 274 DSEDNP-----QTLLFSATCPHWVFNVAKKYMK 301
Cdd:cd17967 178 EHPDMPpkgerQTLMFSATFPREIQRLAADFLK 210
GUCT_RHII_Gualpha_beta cd12936
RNA-binding GUCT domain found in vertebrate RNA helicase II/Gualpha (RH-II/Gualpha), RNA ...
527-619 1.11e-51

RNA-binding GUCT domain found in vertebrate RNA helicase II/Gualpha (RH-II/Gualpha), RNA helicase II/Gubeta (RH-II/Gubeta) and similar proteins; This subfamily corresponds to the Gu C-terminal (GUCT) domain of RH-II/Gualpha and RH-II/Gubeta, two paralogues found in vertebrates. RH-II/Gualpha, also termed nucleolar RNA helicase 2, or DEAD box protein 21, or nucleolar RNA helicase Gu, is a bifunctional enzyme that displays independent RNA-unwinding and RNA-folding activities. It unwinds double-stranded RNA in the 5' to 3' direction in the presence of Mg2+ through the domains in its N-terminal region. In contrast, it folds single-stranded RNA in an ATP-dependent manner and its C-terminal region is responsible for the Mg2+ independent RNA-foldase activity. RH-II/Gualpha consists of a DEAD box helicase domain (DEAD), a helicase conserved C-terminal domain (helicase_C), and a GUCT followed by three FRGQR repeats and one PRGQR sequence. The DEAD and helicase_C domains may play critical roles in the RNA-helicase activity of RH-II/Gualpha. The function of GUCT domain remains unclear. The C-terminal region responsible for the RNA-foldase activity does not overlap with the GUCT domain. RH-II/Gubeta, also termed ATP-dependent RNA helicase DDX50, or DEAD box protein 50, or nucleolar protein Gu2, shows significant sequence homology with RH-II/Gualpha. It contains a DEAD domain, a helicase_C domain, and a GUCT domain followed by an arginine-serine-rich sequence but not (F/P)RGQR repeats in RH-II/Gualpha. Both RH-II/Gualpha and RH-II/Gubeta localize to nucleoli, suggesting roles in ribosomal RNA production, but RH-II/Gubeta also localizes to nuclear speckles containing the splicing factor SC35, suggesting its possible involvement in pre-mRNA splicing. In contrast to RH-II/Gualpha, RH-II/Gubeta has RNA-unwinding activity, but no RNA-folding activity.


Pssm-ID: 240593  Cd Length: 93  Bit Score: 173.79  E-value: 1.11e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 527 HISGATSVDQRSLINSQAGFVTMILRCSIEMPNISYAWKELKEQLGESIDAKVKGMVFLKGKLGVCFDVRTEAVTEIQEK 606
Cdd:cd12936   1 HISGATSKEQRSLLNSDKGFVTMALRCSEEIPNRSYAWKELKEKLGVDADAHISRMCLLKGRMGVCFDVPTAEVESIQAE 80
                        90
                ....*....|...
gi 21410145 607 WHDSRRWQLTVAT 619
Cdd:cd12936  81 WHDSRRWQLSVAT 93
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
98-472 5.62e-49

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 179.60  E-value: 5.62e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145   98 FSNFPISEETVKLLKARGVNFLFPIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKL----QGGLQERkrgRAPQV 173
Cdd:PLN00206 123 FSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCctirSGHPSEQ---RNPLA 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145  174 LVLAPTRELANQVSKDFSDITKKL--SVACFYGGTPYGGQIERMRSGIDILVGTPGRIKDHLQNGKLDLTKLKHVVLDEV 251
Cdd:PLN00206 200 MVLTPTRELCVQVEDQAKVLGKGLpfKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEV 279
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145  252 DQMLDMGFADQVEEILcvaykkDSEDNPQTLLFSATCPHWVFNVAKKYMKSTYeqVDLIGkKTQKAAITVEHLAIkchWT 331
Cdd:PLN00206 280 DCMLERGFRDQVMQIF------QALSQPQVLLFSATVSPEVEKFASSLAKDII--LISIG-NPNRPNKAVKQLAI---WV 347
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145  332 E---RAAVIGDVIRVYSGHQGRTIIFCETKKDAQELSQ--NTCIKQDAQSLHGDIPQKQREITLKGFRNGNFGVLVATNV 406
Cdd:PLN00206 348 EtkqKKQKLFDILKSKQHFKPPAVVFVSSRLGADLLANaiTVVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGV 427
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21410145  407 AARGLDIPEVDLVVQSCPPKDVESYIHRSGRTGRAGRTGVCICFYQNKEEY---QLAQVEQKAGIKFKR 472
Cdd:PLN00206 428 LGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNlfpELVALLKSSGAAIPR 496
DEXDc smart00487
DEAD-like helicases superfamily;
111-301 1.10e-48

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 169.59  E-value: 1.10e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145    111 LKARGVNFLFPIQAKTFHHVYSG-KDLIAQARTGTGKTFSFAIPLIEKLqgglqerKRGRAPQVLVLAPTRELANQVSKD 189
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEAL-------KRGKGGRVLVLVPTRELAEQWAEE 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145    190 FSDITKK--LSVACFYGGTPYGGQIERMRSG-IDILVGTPGRIKDHLQNGKLDLTKLKHVVLDEVDQMLDMGFADQVEEI 266
Cdd:smart00487  74 LKKLGPSlgLKVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKL 153
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 21410145    267 LCVAYKkdsedNPQTLLFSATCPHWVFNVAKKYMK 301
Cdd:smart00487 154 LKLLPK-----NVQLLLLSATPPEEIENLLELFLN 183
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
321-451 1.38e-48

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: 166.53  E-value: 1.38e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 321 VEHLAIKCHWTERAAVIGdVIRVYSGHQGRTIIFCETKKDAQELSQN-TCIKQDAQSLHGDIPQKQREITLKGFRNGNFG 399
Cdd:cd18787   1 IKQLYVVVEEEEKKLLLL-LLLLEKLKPGKAIIFVNTKKRVDRLAELlEELGIKVAALHGDLSQEERERALKKFRSGKVR 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 21410145 400 VLVATNVAARGLDIPEVDLVVQSCPPKDVESYIHRSGRTGRAGRTGVCICFY 451
Cdd:cd18787  80 VLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
96-289 7.51e-47

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: 164.79  E-value: 7.51e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145  96 GAFSNFPISEETVKLLKARGVNFLFPIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKLQGglqerkrgRAPQV-- 173
Cdd:cd17959   1 GGFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKA--------HSPTVga 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 174 --LVLAPTRELANQVSKDFSDITKK--LSVACFYGGTPYGGQIERMRSGIDILVGTPGRIKDHLQNGKLDLTKLKHVVLD 249
Cdd:cd17959  73 raLILSPTRELALQTLKVTKELGKFtdLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFD 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 21410145 250 EVDQMLDMGFADQVEEILcvaykKDSEDNPQTLLFSATCP 289
Cdd:cd17959 153 EADRLFEMGFAEQLHEIL-----SRLPENRQTLLFSATLP 187
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
108-307 3.77e-46

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: 162.54  E-value: 3.77e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 108 VKLLKARGVNFLFPIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKLQGglQER-KRGRAPQVLVLAPTRELANQV 186
Cdd:cd17966   2 MDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINA--QPPlERGDGPIVLVLAPTRELAQQI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 187 SKDFSDITK--KLSVACFYGGTPYGGQIERMRSGIDILVGTPGRIKDHLQNGKLDLTKLKHVVLDEVDQMLDMGFADQVE 264
Cdd:cd17966  80 QQEANKFGGssRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIR 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 21410145 265 EILcvaykkdSEDNP--QTLLFSATCPHWVFNVAKKYMKStYEQV 307
Cdd:cd17966 160 KIV-------DQIRPdrQTLMWSATWPKEVRRLAEDFLKD-YIQV 196
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
121-304 2.70e-45

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: 162.44  E-value: 2.70e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 121 PIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKL-QGGLQ--ERKRGRAPQVLVLAPTRELANQVSKD---FSDIT 194
Cdd:cd18052  68 PVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMmKEGLTasSFSEVQEPQALIVAPTRELANQIFLEarkFSYGT 147
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 195 KKLSVACfYGGTPYGGQIERMRSGIDILVGTPGRIKDHLQNGKLDLTKLKHVVLDEVDQMLDMGFADQVEEILcVAYKKD 274
Cdd:cd18052 148 CIRPVVV-YGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLV-SEPGMP 225
                       170       180       190
                ....*....|....*....|....*....|
gi 21410145 275 SEDNPQTLLFSATCPHWVFNVAKKYMKSTY 304
Cdd:cd18052 226 SKEDRQTLMFSATFPEEIQRLAAEFLKEDY 255
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
98-305 4.00e-45

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: 159.77  E-value: 4.00e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145  98 FSNFPISEETVKLLKARGVNFLFPIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKLQGGLqerkrgRAPQVLVLA 177
Cdd:cd17940   1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKK------DVIQALILV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 178 PTRELANQVSKDFSDITK--KLSVACFYGGTPYGGQIERMRSGIDILVGTPGRIKDHLQNGKLDLTKLKHVVLDEVDQML 255
Cdd:cd17940  75 PTRELALQTSQVCKELGKhmGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLL 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 21410145 256 DMGFADQVEEILCVAYKkdsedNPQTLLFSATCPHWVFNVAKKYMKSTYE 305
Cdd:cd17940 155 SQDFQPIIEKILNFLPK-----ERQILLFSATFPLTVKNFMDRHMHNPYE 199
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
121-287 1.46e-43

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: 155.49  E-value: 1.46e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 121 PIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKLqggLQERKRGRAPQVLVLAPTRELANQVSK------DFSDIT 194
Cdd:cd17947  15 PIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERL---LYRPKKKAATRVLVLVPTRELAMQCFSvlqqlaQFTDIT 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 195 KKLSVacfyGGTPYGGQIERMRSGIDILVGTPGRIKDHLQNGK-LDLTKLKHVVLDEVDQMLDMGFADQVEEILcvaykK 273
Cdd:cd17947  92 FALAV----GGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPsFDLDSIEILVLDEADRMLEEGFADELKEIL-----R 162
                       170
                ....*....|....
gi 21410145 274 DSEDNPQTLLFSAT 287
Cdd:cd17947 163 LCPRTRQTMLFSAT 176
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
121-302 1.54e-43

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: 155.94  E-value: 1.54e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 121 PIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKLQG--GLQERKRGRAPQVLVLAPTRELANQVSKDFSDITKKL- 197
Cdd:cd17945  15 PIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRlpPLDEETKDDGPYALILAPTRELAQQIEEETQKFAKPLg 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 198 -SVACFYGGTPYGGQIERMRSGIDILVGTPGRIKDHLQNGKLDLTKLKHVVLDEVDQMLDMGFADQVEEILC---VAYKK 273
Cdd:cd17945  95 iRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQVTKILDampVSNKK 174
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 21410145 274 DSEDNP------------QTLLFSATCPHWVFNVAKKYMKS 302
Cdd:cd17945 175 PDTEEAeklaasgkhryrQTMMFTATMPPAVEKIAKGYLRR 215
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
103-305 9.82e-43

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


Pssm-ID: 350711 [Multi-domain]  Cd Length: 222  Bit Score: 154.07  E-value: 9.82e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 103 ISEETVKLLKARGVNFLFPIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKLqggLQER--KRGRAPQVLVLAPTR 180
Cdd:cd17953  19 LSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHI---KDQRpvKPGEGPIGLIMAPTR 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 181 ELANQVSKDFSDITKKLS--VACFYGGTPYGGQIERMRSGIDILVGTPGRIKDHL--QNGKL-DLTKLKHVVLDEVDQML 255
Cdd:cd17953  96 ELALQIYVECKKFSKALGlrVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtaNNGRVtNLRRVTYVVLDEADRMF 175
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 21410145 256 DMGFADQVEEILcvaykKDSEDNPQTLLFSATCPHWVFNVAKKYMKSTYE 305
Cdd:cd17953 176 DMGFEPQIMKIV-----NNIRPDRQTVLFSATFPRKVEALARKVLHKPIE 220
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
121-301 3.90e-42

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


Pssm-ID: 350716 [Multi-domain]  Cd Length: 197  Bit Score: 151.46  E-value: 3.90e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 121 PIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIP-LIEKLQGGLQERKRGRaPQVLVLAPTRELANQVSKDFSDIT-KKLS 198
Cdd:cd17958  15 PIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPgFIHLDLQPIPREQRNG-PGVLVLTPTRELALQIEAECSKYSyKGLK 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 199 VACFYGGTPYGGQIERMRSGIDILVGTPGRIKDHLQNGKLDLTKLKHVVLDEVDQMLDMGFADQVEEILcvaykKDSEDN 278
Cdd:cd17958  94 SVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIRKIL-----LDIRPD 168
                       170       180
                ....*....|....*....|...
gi 21410145 279 PQTLLFSATCPHWVFNVAKKYMK 301
Cdd:cd17958 169 RQTIMTSATWPDGVRRLAQSYLK 191
GUCT pfam08152
GUCT (NUC152) domain; This is the C terminal domain found in the RNA helicase II / Gu protein ...
530-625 5.39e-41

GUCT (NUC152) domain; This is the C terminal domain found in the RNA helicase II / Gu protein family.


Pssm-ID: 462378  Cd Length: 96  Bit Score: 144.60  E-value: 5.39e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145   530 GATSVDQRSLINSQAGFVTMILRCSIEMPNISYAWKELKEQLGESIDAKVKGMVFLKGKLGVCFDVRTEAVTEIQEKWHD 609
Cdd:pfam08152   1 GYTEIKQRSLLSSEEGFVTLLLTSSREIRTPGYAWSILRRNLSEEIADKVKGMRLTKDKMGAVFDVPSELVEEFLAGWED 80
                          90
                  ....*....|....*.
gi 21410145   610 SRRWQLTVATEQPELE 625
Cdd:pfam08152  81 SRGVTLEVATELPELQ 96
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
122-300 1.09e-40

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: 147.47  E-value: 1.09e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 122 IQAKTFHHVYSGKDLIAQARTGTGKTFSFAIplieklqGGLQE-RKRGRAPQVLVLAPTRELANQVSKDFSDITKKLSV- 199
Cdd:cd17939  23 IQQRAIVPIIKGRDVIAQAQSGTGKTATFSI-------GALQRiDTTVRETQALVLAPTRELAQQIQKVVKALGDYMGVk 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 200 -ACFYGGTPYGGQIERMRSGIDILVGTPGRIKDHLQNGKLDLTKLKHVVLDEVDQMLDMGFADQVEEILcvaykKDSEDN 278
Cdd:cd17939  96 vHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQIYDIF-----QFLPPE 170
                       170       180
                ....*....|....*....|..
gi 21410145 279 PQTLLFSATCPHWVFNVAKKYM 300
Cdd:cd17939 171 TQVVLFSATMPHEVLEVTKKFM 192
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
121-309 9.08e-40

DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, G17P1, or HUMP68) is involved in pathways that include the alteration of RNA structures, plays a role as a coregulator of transcription, a regulator of splicing, and in the processing of small noncoding RNAs. It synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. Dysregulation of this gene may play a role in cancer development. DDX5 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350807 [Multi-domain]  Cd Length: 234  Bit Score: 146.31  E-value: 9.08e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 121 PIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKL--QGGLQerkRGRAPQVLVLAPTRELANQVSKDFSDITK--K 196
Cdd:cd18049  49 AIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHInhQPFLE---RGDGPICLVLAPTRELAQQVQQVAAEYGRacR 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 197 LSVACFYGGTPYGGQIERMRSGIDILVGTPGRIKDHLQNGKLDLTKLKHVVLDEVDQMLDMGFADQVEEILcvaykKDSE 276
Cdd:cd18049 126 LKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIV-----DQIR 200
                       170       180       190
                ....*....|....*....|....*....|...
gi 21410145 277 DNPQTLLFSATCPHWVFNVAKKYMKStYEQVDL 309
Cdd:cd18049 201 PDRQTLMWSATWPKEVRQLAEDFLKD-YIHINI 232
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
107-287 4.42e-39

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: 142.81  E-value: 4.42e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 107 TVKLLKARGVNFLFPIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKLqggLQER-KRGRAPQVLVLAPTRELANQ 185
Cdd:cd17941   1 TLKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKL---YRERwTPEDGLGALIISPTRELAMQ 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 186 VSKDFSDITKK--LSVACFYGGTPYggQIERMR-SGIDILVGTPGRIKDHL-QNGKLDLTKLKHVVLDEVDQMLDMGFAD 261
Cdd:cd17941  78 IFEVLRKVGKYhsFSAGLIIGGKDV--KEEKERiNRMNILVCTPGRLLQHMdETPGFDTSNLQMLVLDEADRILDMGFKE 155
                       170       180
                ....*....|....*....|....*....
gi 21410145 262 QVEEILcvaykkdsEDNP---QTLLFSAT 287
Cdd:cd17941 156 TLDAIV--------ENLPksrQTLLFSAT 176
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
122-287 4.63e-39

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: 143.50  E-value: 4.63e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 122 IQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKLQGGLQERKRGRAPQVLVLAPTRELANQVSKDFSDITKK---LS 198
Cdd:cd17949  17 IQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRVDRSDGTLALVLVPTRELALQIYEVLEKLLKPfhwIV 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 199 VACFYGGTPYGGQIERMRSGIDILVGTPGRIKDHLQNGK-LDLTKLKHVVLDEVDQMLDMGFADQVEEIL------CVAY 271
Cdd:cd17949  97 PGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQsFDVSNLRWLVLDEADRLLDMGFEKDITKILellddkRSKA 176
                       170
                ....*....|....*...
gi 21410145 272 KKDSEDNP--QTLLFSAT 287
Cdd:cd17949 177 GGEKSKPSrrQTVLVSAT 194
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
121-301 9.68e-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: 141.96  E-value: 9.68e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 121 PIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKLQgglqERKRGRAPQVLVLAPTRELANQVSKDFSDITKK--LS 198
Cdd:cd17957  15 PIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLG----KPRKKKGLRALILAPTRELASQIYRELLKLSKGtgLR 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 199 VACFYGGT-PYGGQIERMRSGIDILVGTPGRIKDHLQNGKLDLTKLKHVVLDEVDQMLDMGFADQVEEIL--Cvaykkds 275
Cdd:cd17957  91 IVLLSKSLeAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDEILaaC------- 163
                       170       180
                ....*....|....*....|....*...
gi 21410145 276 eDNP--QTLLFSATCPHWVFNVAKKYMK 301
Cdd:cd17957 164 -TNPnlQRSLFSATIPSEVEELARSVMK 190
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
122-301 1.03e-38

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: 142.20  E-value: 1.03e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 122 IQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKLQGGLqerkrgRAPQVLVLAPTRELANQVSKDFSDITKKLSVAC 201
Cdd:cd18046  25 IQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSL------KATQALVLAPTRELAQQIQKVVMALGDYMGIKC 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 202 F--YGGTPYGGQIERMRSGIDILVGTPGRIKDHLQNGKLDLTKLKHVVLDEVDQMLDMGFADQVEEIlcvaYKKDSEDNp 279
Cdd:cd18046  99 HacIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFKDQIYDI----FQKLPPDT- 173
                       170       180
                ....*....|....*....|..
gi 21410145 280 QTLLFSATCPHWVFNVAKKYMK 301
Cdd:cd18046 174 QVVLLSATMPNDVLEVTTKFMR 195
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
107-287 3.82e-38

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: 140.40  E-value: 3.82e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 107 TVKLLKARGVNFLFPIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKLQGGLQERKRGrAPQVLVLAPTRELANQV 186
Cdd:cd17960   1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANLKKG-QVGALIISPTRELATQI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 187 SKDFSDITK----KLSVACFYGGT-PYGGQIERMRSGIDILVGTPGRIKDHLQN--GKLDLTKLKHVVLDEVDQMLDMGF 259
Cdd:cd17960  80 YEVLQSFLEhhlpKLKCQLLIGGTnVEEDVKKFKRNGPNILVGTPGRLEELLSRkaDKVKVKSLEVLVLDEADRLLDLGF 159
                       170       180
                ....*....|....*....|....*...
gi 21410145 260 ADQVEEILCVAYKkdsedNPQTLLFSAT 287
Cdd:cd17960 160 EADLNRILSKLPK-----QRRTGLFSAT 182
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
121-309 7.88e-38

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


Pssm-ID: 350808 [Multi-domain]  Cd Length: 271  Bit Score: 142.07  E-value: 7.88e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 121 PIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKL--QGGLQerkRGRAPQVLVLAPTRELANQVSKDFSDITK--K 196
Cdd:cd18050  87 PIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHInhQPYLE---RGDGPICLVLAPTRELAQQVQQVADDYGKssR 163
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 197 LSVACFYGGTPYGGQIERMRSGIDILVGTPGRIKDHLQNGKLDLTKLKHVVLDEVDQMLDMGFADQVEEILcvaykKDSE 276
Cdd:cd18050 164 LKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIV-----DQIR 238
                       170       180       190
                ....*....|....*....|....*....|...
gi 21410145 277 DNPQTLLFSATCPHWVFNVAKKYMKStYEQVDL 309
Cdd:cd18050 239 PDRQTLMWSATWPKEVRQLAEDFLRD-YVQINI 270
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
121-287 2.48e-37

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: 138.22  E-value: 2.48e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 121 PIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKLqggLQERKRGRApqvLVLAPTRELANQVSKDFSDITKKLSV- 199
Cdd:cd17954  25 KIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQAL---LENPQRFFA---LVLAPTRELAQQISEQFEALGSSIGLk 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 200 -ACFYGGtpyggqIERMRSGID------ILVGTPGRIKDHLQNGK-LDLTKLKHVVLDEVDQMLDMGFADQVEEILcvay 271
Cdd:cd17954  99 sAVLVGG------MDMMAQAIAlakkphVIVATPGRLVDHLENTKgFSLKSLKFLVMDEADRLLNMDFEPEIDKIL---- 168
                       170
                ....*....|....*.
gi 21410145 272 kKDSEDNPQTLLFSAT 287
Cdd:cd17954 169 -KVIPRERTTYLFSAT 183
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
121-287 1.09e-36

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: 136.56  E-value: 1.09e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 121 PIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKLQGGLQERKRGRAPQVLVLAPTRELANQVSKDFSDIT----KK 196
Cdd:cd17961  19 LIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAESGEEQGTRALILVPTRELAQQVSKVLEQLTaycrKD 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 197 LSVACFYGGTPYGGQIERMRSGIDILVGTPGRIKDHLQNGKL-DLTKLKHVVLDEVDQMLDMGFADQVEEILCVAYKkds 275
Cdd:cd17961  99 VRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLlLLSTLKYLVIDEADLVLSYGYEEDLKSLLSYLPK--- 175
                       170
                ....*....|..
gi 21410145 276 edNPQTLLFSAT 287
Cdd:cd17961 176 --NYQTFLMSAT 185
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
111-301 1.40e-36

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: 135.75  E-value: 1.40e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 111 LKARGVNFLFPIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKLQGglqerkRGRAPQVLVLAPTRELANQVSKDF 190
Cdd:cd17962   5 LKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLT------EHRNPSALILTPTRELAVQIEDQA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 191 SDITKKL---SVACFYGGTPYGGQIERMRSGIDILVGTPGRIKDHLQNGKLDLTKLKHVVLDEVDQMLDMGFADQVEEIL 267
Cdd:cd17962  79 KELMKGLppmKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDIL 158
                       170       180       190
                ....*....|....*....|....*....|....
gi 21410145 268 cvaykKDSEDNPQTLLFSATCPHWVFNVAKKYMK 301
Cdd:cd17962 159 -----ENISHDHQTILVSATIPRGIEQLAGQLLQ 187
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
108-297 6.52e-36

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: 134.39  E-value: 6.52e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 108 VKLLKARGVNFLFPIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIekLQGGLQERK----RGRAPQVLVLAPTRELA 183
Cdd:cd17951   2 LKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLI--MFALEQEKKlpfiKGEGPYGLIVCPSRELA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 184 NQVSKDFSDITKKLS--------VACFYGGTPYGGQIERMRSGIDILVGTPGRIKDHLQNGKLDLTKLKHVVLDEVDQML 255
Cdd:cd17951  80 RQTHEVIEYYCKALQeggypqlrCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMI 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 21410145 256 DMGFADQVEEILcvAYKKDSEdnpQTLLFSATCPHWVFNVAK 297
Cdd:cd17951 160 DMGFEEDIRTIF--SYFKGQR---QTLLFSATMPKKIQNFAK 196
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
110-301 8.08e-36

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: 133.85  E-value: 8.08e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 110 LLKA-RGVNFLFP--IQAKTFHHVYSG--KDLIAQARTGTGKTFSFAIPLIEKLQGGLqerkrgRAPQVLVLAPTRELAN 184
Cdd:cd17963   5 LLKGlYAMGFNKPskIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPTL------KSPQALCLAPTRELAR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 185 QVSKDFSDITKKLSVACFYGgTPygGQIERMRSGID--ILVGTPGRIKDHLQNGKLDLTKLKHVVLDEVDQMLDM-GFAD 261
Cdd:cd17963  79 QIGEVVEKMGKFTGVKVALA-VP--GNDVPRGKKITaqIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTqGHGD 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 21410145 262 QVEEIlcvayKKDSEDNPQTLLFSATCPHWVFNVAKKYMK 301
Cdd:cd17963 156 QSIRI-----KRMLPRNCQILLFSATFPDSVRKFAEKIAP 190
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
98-287 9.70e-36

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: 133.89  E-value: 9.70e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145  98 FSNFPISEETVKLLKARGVNFLFPIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKLqgglqeRKRGRAPQVLVLA 177
Cdd:cd17955   1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRL------SEDPYGIFALVLT 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 178 PTRELANQVSKDFSDITKKLSVAC--FYGGTPYGGQIERMRSGIDILVGTPGRIKDHLQNG---KLDLTKLKHVVLDEVD 252
Cdd:cd17955  75 PTRELAYQIAEQFRALGAPLGLRCcvIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSddtTKVLSRVKFLVLDEAD 154
                       170       180       190
                ....*....|....*....|....*....|....*
gi 21410145 253 QMLDMGFADQVEEILCVAYKKdsednPQTLLFSAT 287
Cdd:cd17955 155 RLLTGSFEDDLATILSALPPK-----RQTLLFSAT 184
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
107-287 1.27e-35

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: 133.25  E-value: 1.27e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 107 TVKLLKARGVNFLFPIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKLQGGLQERKRGRApqVLVLAPTRELANQV 186
Cdd:cd17942   1 TLKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKFKPRNGTG--VIIISPTRELALQI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 187 skdfSDITKKL------SVACFYGGTPYGGQIERMRSGIDILVGTPGRIKDHLQNGKLDLTK-LKHVVLDEVDQMLDMGF 259
Cdd:cd17942  79 ----YGVAKELlkyhsqTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLYKnLQCLIIDEADRILEIGF 154
                       170       180
                ....*....|....*....|....*...
gi 21410145 260 ADQVEEILCVAYKKDsednpQTLLFSAT 287
Cdd:cd17942 155 EEEMRQIIKLLPKRR-----QTMLFSAT 177
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
107-302 2.79e-35

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: 132.00  E-value: 2.79e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 107 TVKLLKARGVNFLFPIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKLqgglqeRKRGRAPQVLVLAPTRELANQV 186
Cdd:cd17943   1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESL------DLERRHPQVLILAPTREIAVQI 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 187 SKDFSDITKK---LSVACFYGGTPYGGQIERMRsGIDILVGTPGRIKDHLQNGKLDLTKLKHVVLDEVDQMLDMGFADQV 263
Cdd:cd17943  75 HDVFKKIGKKlegLKCEVFIGGTPVKEDKKKLK-GCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDV 153
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 21410145 264 EEILCVAYKkdsedNPQTLLFSATCPHWVFNVAKKYMKS 302
Cdd:cd17943 154 NWIFSSLPK-----NKQVIAFSATYPKNLDNLLARYMRK 187
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
98-305 4.90e-35

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: 132.08  E-value: 4.90e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145  98 FSNFPISEEtvkLLKA-RGVNFLFP--IQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKLQGGLQErkrgraPQVL 174
Cdd:cd17950   4 FRDFLLKPE---LLRAiVDCGFEHPseVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQ------VSVL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 175 VLAPTRELANQVSKDFSDITKKL---SVACFYGGTPYGGQIERMRSGI-DILVGTPGRIKDHLQNGKLDLTKLKHVVLDE 250
Cdd:cd17950  75 VICHTRELAFQISNEYERFSKYMpnvKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDE 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 21410145 251 VDQML-DMGFADQVEEIlcvaYKKDSEDNpQTLLFSATCPHWVFNVAKKYMKSTYE 305
Cdd:cd17950 155 CDKMLeQLDMRRDVQEI----FRATPHDK-QVMMFSATLSKEIRPVCKKFMQDPLE 205
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
121-289 5.26e-35

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: 133.24  E-value: 5.26e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 121 PIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKL----------QGGLQERKRGRAPQVLVLAPTRELANQV---S 187
Cdd:cd18051  46 PVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIyeqgpgeslpSESGYYGRRKQYPLALVLAPTRELASQIydeA 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 188 KDFSdITKKLSVACFYGGTPYGGQIERMRSGIDILVGTPGRIKDHLQNGKLDLTKLKHVVLDEVDQMLDMGFADQVEEIL 267
Cdd:cd18051 126 RKFA-YRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIV 204
                       170       180
                ....*....|....*....|....*
gi 21410145 268 cvayKKDSEDNP---QTLLFSATCP 289
Cdd:cd18051 205 ----EQDTMPPTgerQTLMFSATFP 225
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
121-287 5.54e-35

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: 131.38  E-value: 5.54e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 121 PIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKLQGGlQERKRGRAPQVLVLAPTRELANQVSKDFSDITK--KLS 198
Cdd:cd17952  15 PIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQ-RELEKGEGPIAVIVAPTRELAQQIYLEAKKFGKayNLR 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 199 VACFYGGTPYGGQIERMRSGIDILVGTPGRIKDHLQNGKLDLTKLKHVVLDEVDQMLDMGFADQVEEILcvaykkdSEDN 278
Cdd:cd17952  94 VVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRSIV-------GHVR 166
                       170
                ....*....|.
gi 21410145 279 P--QTLLFSAT 287
Cdd:cd17952 167 PdrQTLLFSAT 177
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
332-442 1.89e-32

Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 121.16  E-value: 1.89e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145   332 ERAAVIGDVIRVYSGHqgRTIIFCETKK--DAQELSQNTCIKqdAQSLHGDIPQKQREITLKGFRNGNFGVLVATNVAAR 409
Cdd:pfam00271   1 EKLEALLELLKKERGG--KVLIFSQTKKtlEAELLLEKEGIK--VARLHGDLSQEEREEILEDFRKGKIDVLVATDVAER 76
                          90       100       110
                  ....*....|....*....|....*....|...
gi 21410145   410 GLDIPEVDLVVQSCPPKDVESYIHRSGRTGRAG 442
Cdd:pfam00271  77 GLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
121-287 2.45e-32

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: 125.04  E-value: 2.45e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 121 PIQAKTFHH-VYSGKDLIAQARTGTGKTFSFAIPLIEKLQGGLQERKRG---RAPQVLVLAPTRELANQVSKDFSDITK- 195
Cdd:cd17946  15 PIQALALPAaIRDGKDVIGAAETGSGKTLAFGIPILERLLSQKSSNGVGgkqKPLRALILTPTRELAVQVKDHLKAIAKy 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 196 -KLSVACFYGGTPYGGQIERMRSGIDILVGTPGRIKDHLQNGKLDLTKLKHV---VLDEVDQMLDMGFADQVEEILCVAY 271
Cdd:cd17946  95 tNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEHLANLKSLrflVLDEADRMLEKGHFAELEKILELLN 174
                       170
                ....*....|....*...
gi 21410145 272 KKDSEDNP--QTLLFSAT 287
Cdd:cd17946 175 KDRAGKKRkrQTFVFSAT 192
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
121-287 3.68e-32

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: 123.59  E-value: 3.68e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 121 PIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKLQGglqerkrgrapqvLVLAPTRELANQVSKDFSDITK----- 195
Cdd:cd17938  24 DIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIVVA-------------LILEPSRELAEQTYNCIENFKKyldnp 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 196 KLSVACFYGGTPYGGQIERMRSGIDILVGTPGRIKDHLQNGKLDLTKLKHVVLDEVDQMLDMGFADQVEEIlcvaYKK-- 273
Cdd:cd17938  91 KLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQGNLETINRI----YNRip 166
                       170
                ....*....|....*..
gi 21410145 274 ---DSEDNPQTLLFSAT 287
Cdd:cd17938 167 kitSDGKRLQVIVCSAT 183
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
98-300 2.58e-31

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: 121.04  E-value: 2.58e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145  98 FSNFPISEETVKLLKARGVNFLFPIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKLQGGLQErkrgraPQVLVLA 177
Cdd:cd18045   1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRE------TQALILS 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 178 PTRELANQVSKDFSDITKKLSVACF--YGGTPYGGQIERMRSGIDILVGTPGRIKDHLQNGKLDLTKLKHVVLDEVDQML 255
Cdd:cd18045  75 PTRELAVQIQKVLLALGDYMNVQCHacIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEML 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 21410145 256 DMGFADQVEEILcvaykKDSEDNPQTLLFSATCPHWVFNVAKKYM 300
Cdd:cd18045 155 NKGFKEQIYDVY-----RYLPPATQVVLVSATLPQDILEMTNKFM 194
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
108-287 1.22e-29

DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by regulating multiple signalling pathways. Mammalian DEAD box protein Ddx51 acts in 3' end maturation of 28S rRNA by promoting the release of U8 snoRNA.It is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350714 [Multi-domain]  Cd Length: 231  Bit Score: 117.35  E-value: 1.22e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 108 VKLLKARGVNFLFPIQAKTFHHV---------YSGKDLIAQARTGTGKTFSFAIPLIEKLQGglQERKRGRApqvLVLAP 178
Cdd:cd17956   2 LKNLQNNGITSAFPVQAAVIPWLlpsskstppYRPGDLCVSAPTGSGKTLAYVLPIVQALSK--RVVPRLRA---LIVVP 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 179 TRELANQVSKDFSDITK--KLSVAC------FYGGTPYGGQIERMR--SGIDILVGTPGRIKDHLQNGK-LDLTKLKHVV 247
Cdd:cd17956  77 TKELVQQVYKVFESLCKgtGLKVVSlsgqksFKKEQKLLLVDTSGRylSRVDILVATPGRLVDHLNSTPgFTLKHLRFLV 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21410145 248 LDEVDQMLDMGFAD---QVEEILC------------VAYKKDSEDNPQTLLFSAT 287
Cdd:cd17956 157 IDEADRLLNQSFQDwleTVMKALGrptapdlgsfgdANLLERSVRPLQKLLFSAT 211
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
108-289 1.16e-26

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: 108.61  E-value: 1.16e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 108 VKLLKARGVNFLFPIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKLQGGLQERKRG-RAPQVLVLAPTRELANQV 186
Cdd:cd17948   2 VEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGPfNAPRGLVITPSRELAEQI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 187 SKDFSDITKKLS--VACFYGGTPYGGQIERMRSGIDILVGTPGRIKDHLQNGKLDLTKLKHVVLDEVDQMLDMGFADQVE 264
Cdd:cd17948  82 GSVAQSLTEGLGlkVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKLS 161
                       170       180       190
                ....*....|....*....|....*....|...
gi 21410145 265 EILC---VAYKKDSEDNP-----QTLLFSATCP 289
Cdd:cd17948 162 HFLRrfpLASRRSENTDGldpgtQLVLVSATMP 194
HELICc smart00490
helicase superfamily c-terminal domain;
376-442 7.03e-26

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 101.52  E-value: 7.03e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21410145    376 SLHGDIPQKQREITLKGFRNGNFGVLVATNVAARGLDIPEVDLVVQSCPPKDVESYIHRSGRTGRAG 442
Cdd:smart00490  16 RLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
133-287 1.59e-20

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: 88.23  E-value: 1.59e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 133 GKDLIAQARTGTGKTFSFAIPLIEKLqgglqerkRGRAPQVLVLAPTRELANQVSKDFSDI-TKKLSVACFYGGTPYGGQ 211
Cdd:cd00046   1 GENVLITAPTGSGKTLAALLAALLLL--------LKKGKKVLVLVPTKALALQTAERLRELfGPGIRVAVLVGGSSAEER 72
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21410145 212 IERMRSGIDILVGTPGRI-KDHLQNGKLDLTKLKHVVLDEVDqmlDMGFADQVEEILCVAYKKDSEDNPQTLLFSAT 287
Cdd:cd00046  73 EKNKLGDADIIIATPDMLlNLLLREDRLFLKDLKLIIVDEAH---ALLIDSRGALILDLAVRKAGLKNAQVILLSAT 146
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
94-448 1.13e-19

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: 93.75  E-value: 1.13e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145  94 KEGAFSNFP--ISEETVKLLKARGVNFLFPIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKLQgglqerkRGRAP 171
Cdd:COG1205  30 REARYAPWPdwLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALL-------EDPGA 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 172 QVLVLAPTRELAN-QVSKdFSDITKKL----SVACFYGGTPyggQIER--MRSGIDILVGTP-----GRIKDHLQNGKLd 239
Cdd:COG1205 103 TALYLYPTKALARdQLRR-LRELAEALglgvRVATYDGDTP---PEERrwIREHPDIVLTNPdmlhyGLLPHHTRWARF- 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 240 LTKLKHVVLDE------VdqmldmgFADQVEEIL------CVAYKKDsednPQTLLFSATcphwVFNVAKKYMKSTYEQV 307
Cdd:COG1205 178 FRNLRYVVIDEahtyrgV-------FGSHVANVLrrlrriCRHYGSD----PQFILASAT----IGNPAEHAERLTGRPV 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 308 DLI-------GKKTQkaaITVEHLAIkcHWTERAAVIGDVIR-----VYSGHQgrTIIFCETKK-------DAQELSQNT 368
Cdd:COG1205 243 TVVdedgsprGERTF---VLWNPPLV--DDGIRRSALAEAARlladlVREGLR--TLVFTRSRRgaellarYARRALREP 315
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 369 CIKQDAQSLHGDIPQKQREITLKGFRNGNFGVLVATNVAARGLDIPEVDLVVQSCPPKDVESYIHRSGRTGRAGRTGVCI 448
Cdd:COG1205 316 DLADRVAAYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVV 395
GUCT_RH7_like cd12937
RNA-binding GUCT domain found in plant DEAD-box ATP-dependent RNA helicase 7 (RH7) and similar ...
537-622 3.34e-19

RNA-binding GUCT domain found in plant DEAD-box ATP-dependent RNA helicase 7 (RH7) and similar proteins; This subfamily corresponds to the Gu C-terminal (GUCT) domain of RH7 and similar proteins. RH7, also termed plant RNA helicase 75 (PRH75), is a new nucleus-localized member of the DEAD-box protein family from higher plants. It displays a weak ATPase activity which is barely stimulated by RNA ligands. RH7 contains an N-terminal KDES domain rich in lysine, glutamic acid, aspartic acid, and serine residues, seven highly conserved helicase motifs in the central region, a GUCT domain, and a C-terminal GYR domain harboring a large number of glycine residues interrupted by either arginines or tyrosines. RH7 is RNA specific and harbors two possible RNA-binding motifs, the helicase motif VI (HRIGRTGR) and the C-terminal glycine-rich GYR domain.


Pssm-ID: 240594  Cd Length: 86  Bit Score: 82.61  E-value: 3.34e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 537 RSLINSQAGFVTMILRCSIEMPNISYAWKELKEQLGESIDAKVKGMVFLKGKLGVCFDVRTEAVTEIQEKWHDSRRWQLT 616
Cdd:cd12937   1 RSLLTSHEGYTTLLLKSNTPIRSPGYVWNALRRYLPEDIVESIKGMTLTADGKGAVFDVPSELIEEFLSAWVDKRGVTLE 80

                ....*.
gi 21410145 617 VATEQP 622
Cdd:cd12937  81 VATELP 86
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
133-421 7.96e-18

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 87.39  E-value: 7.96e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 133 GKDLIAQARTGTGKTFsFAIPLIEKLQGGlqerkrgraPQVLVLAPTRELANQVSKDFSDITKKLSVacfyggtpYGGQI 212
Cdd:COG1061 100 GGRGLVVAPTGTGKTV-LALALAAELLRG---------KRVLVLVPRRELLEQWAEELRRFLGDPLA--------GGGKK 161
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 213 ERMRsgiDILVGTPGRIKDHLQNGKLDlTKLKHVVLDEVDQmldmGFADQVEEILcvaykkDSEDNPQTLLFSAT----- 287
Cdd:COG1061 162 DSDA---PITVATYQSLARRAHLDELG-DRFGLVIIDEAHH----AGAPSYRRIL------EAFPAAYRLGLTATpfrsd 227
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 288 ----CPHWVFNVAKKYmksTYEQ----------------VDLIGKKTQKAAITvEHLAIK-CHWTERAAVIGDVIRVYSG 346
Cdd:COG1061 228 greiLLFLFDGIVYEY---SLKEaiedgylappeyygirVDLTDERAEYDALS-ERLREAlAADAERKDKILRELLREHP 303
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21410145 347 HQGRTIIFCETKKDAQELSQ--NTcIKQDAQSLHGDIPQKQREITLKGFRNGNFGVLVATNVAARGLDIPEVDLVVQ 421
Cdd:COG1061 304 DDRKTLVFCSSVDHAEALAEllNE-AGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAIL 379
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
136-304 2.38e-17

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


Pssm-ID: 350723 [Multi-domain]  Cd Length: 251  Bit Score: 82.04  E-value: 2.38e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 136 LIAqARTGTGKTFSFAIPLIEKLQGGLQE-----------RKRGRAPQVLVLAPTRELANQVS---KDFSDITkKLSVAC 201
Cdd:cd17965  65 LLA-AETGSGKTLAYLAPLLDYLKRQEQEpfeeaeeeyesAKDTGRPRSVILVPTHELVEQVYsvlKKLSHTV-KLGIKT 142
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 202 FYG--GTPYGGQIERMRSGIDILVGTPGRIkdhLQNGKLD---LTKLKHVVLDEVDQMLDMGFADQVEEILcvaykKDSE 276
Cdd:cd17965 143 FSSgfGPSYQRLQLAFKGRIDILVTTPGKL---ASLAKSRpkiLSRVTHLVVDEADTLFDRSFLQDTTSII-----KRAP 214
                       170       180
                ....*....|....*....|....*...
gi 21410145 277 DNPQTLLFSATCPhwvfNVAKKYMKSTY 304
Cdd:cd17965 215 KLKHLILCSATIP----KEFDKTLRKLF 238
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
97-298 5.92e-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: 77.75  E-value: 5.92e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145  97 AFSNFPISEETVKLLKARGVNFLFPIQAKTFHHVYSG--KDLIAQARTGTGKTFSFAIPLIEKLQGglqerkRGRAPQVL 174
Cdd:cd18048  19 SFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDA------LKLYPQCL 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 175 VLAPTRELANQVSKDFSDITK-----KLSVACFYGGTPYGGQIERmrsgiDILVGTPGRIKDHLQNGKL-DLTKLKHVVL 248
Cdd:cd18048  93 CLSPTFELALQTGKVVEEMGKfcvgiQVIYAIRGNRPGKGTDIEA-----QIVIGTPGTVLDWCFKLRLiDVTNISVFVL 167
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 21410145 249 DEVDQMLDM-GFADQveeilCVAYKKDSEDNPQTLLFSATCPHWVFNVAKK 298
Cdd:cd18048 168 DEADVMINVqGHSDH-----SVRVKRSMPKECQMLLFSATFEDSVWAFAER 213
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
105-445 1.40e-15

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 79.94  E-value: 1.40e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 105 EETVKLLKARGVNFLFPIQAKTFH-HVYSGKDLIAQARTGTGKTFSFAIPLIEKLQGGlqerkrGRApqvLVLAPTRELA 183
Cdd:COG1204   9 EKVIEFLKERGIEELYPPQAEALEaGLLEGKNLVVSAPTASGKTLIAELAILKALLNG------GKA---LYIVPLRALA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 184 NQVSKDFSDI--TKKLSVACFYGgtPYGGQIERMRSGiDILVGTPGRIkDHL-QNGKLDLTKLKHVVLDEVdQMLDmgfa 260
Cdd:COG1204  80 SEKYREFKRDfeELGIKVGVSTG--DYDSDDEWLGRY-DILVATPEKL-DSLlRNGPSWLRDVDLVVVDEA-HLID---- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 261 DQ-----VEEILcvAYKKDSEDNPQTLLFSATCP------HWvFNVAKkyMKSTYEQVDLigkktqkaaitveHLAIKCH 329
Cdd:COG1204 151 DEsrgptLEVLL--ARLRRLNPEAQIVALSATIGnaeeiaEW-LDAEL--VKSDWRPVPL-------------NEGVLYD 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 330 W--------TERAAVIGDVIRVYSGHQGRTIIFCETKKD----AQELSQNTC----------IKQDAQSL---------- 377
Cdd:COG1204 213 GvlrfddgsRRSKDPTLALALDLLEEGGQVLVFVSSRRDaeslAKKLADELKrrltpeereeLEELAEELlevseethtn 292
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 378 --------------HGDIPQKQREITLKGFRNGNFGVLVATNVAARGLDIPeVDLVVqscppkdVESYiHRSGRT----- 438
Cdd:COG1204 293 ekladclekgvafhHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLP-ARRVI-------IRDT-KRGGMVpipvl 363
                       410
                ....*....|...
gi 21410145 439 ------GRAGRTG 445
Cdd:COG1204 364 efkqmaGRAGRPG 376
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
341-451 2.90e-15

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: 73.01  E-value: 2.90e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 341 IRVYSGHqGRTIIFCETKKDAQELS---QNTCIKqdAQSLHGDIPQKQREITLKGFRNGNFGVLVATNVAARGLDIPEVD 417
Cdd:cd18794  24 IKVEHLG-GSGIIYCLSRKECEQVAarlQSKGIS--AAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVR 100
                        90       100       110
                ....*....|....*....|....*....|....
gi 21410145 418 LVVQSCPPKDVESYIHRSGRTGRAGRTGVCICFY 451
Cdd:cd18794 101 FVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
PRK13766 PRK13766
Hef nuclease; Provisional
383-539 1.97e-14

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 76.84  E-value: 1.97e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145  383 QKQREITLKGFRNGNFGVLVATNVAARGLDIPEVDLVVQSCP-PKDVESyIHRSGRTGR--AGRTGVCIC-------FY- 451
Cdd:PRK13766 409 QKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVIFYEPvPSEIRS-IQRKGRTGRqeEGRVVVLIAkgtrdeaYYw 487
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145  452 --QNKEEYQLAQVEQKAGIKFKRIGVPSATEIIKASSKDAIRLLDSVPPTAISHFKQSAEKLIEEKGAVEALAAALAHIs 529
Cdd:PRK13766 488 ssRRKEKKMKEELKNLKGILNKKLQELDEEQKGEEEEKDEQLSLDDFVKSKGKEEEEEEEKEEKDKETEEDEPEGPKII- 566
                        170
                 ....*....|
gi 21410145  530 gatsVDQRSL 539
Cdd:PRK13766 567 ----VDSREL 572
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
383-442 1.44e-13

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 74.00  E-value: 1.44e-13
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21410145 383 QKQREITLKGFRNGNFGVLVATNVAARGLDIPEVDLVVQSCPpkdVES---YIHRSGRTGRAG 442
Cdd:COG1111 397 QKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYEP---VPSeirSIQRKGRTGRKR 456
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
118-287 2.71e-13

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: 68.83  E-value: 2.71e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 118 FLFPIQAKTFHHVY-SGKDLIAQARTGTGKTF--SFAIpliekLQGGLQERKRgrapqVLVLAPTRELANQVSKDFSDIT 194
Cdd:cd17921   1 LLNPIQREALRALYlSGDSVLVSAPTSSGKTLiaELAI-----LRALATSGGK-----AVYIAPTRALVNQKEADLRERF 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 195 KKL--SVACFYGGTPYGGQIERMRsgiDILVGTPGRIKDHLQNGKLDLTK-LKHVVLDEVdQMLDMG-FADQVEEILcvA 270
Cdd:cd17921  71 GPLgkNVGLLTGDPSVNKLLLAEA---DILVATPEKLDLLLRNGGERLIQdVRLVVVDEA-HLIGDGeRGVVLELLL--S 144
                       170
                ....*....|....*..
gi 21410145 271 YKKDSEDNPQTLLFSAT 287
Cdd:cd17921 145 RLLRINKNARFVGLSAT 161
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
350-440 3.39e-12

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


Pssm-ID: 350188 [Multi-domain]  Cd Length: 143  Bit Score: 64.30  E-value: 3.39e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 350 RTIIFCETKKDAQE----LSQN-------TCIKQ-DAQSLHGdIPQKQREITLKGFRNGNFGVLVATNVAARGLDIPEVD 417
Cdd:cd18801  32 RVIIFSEFRDSAEEivnfLSKIrpgiratRFIGQaSGKSSKG-MSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVD 110
                        90       100
                ....*....|....*....|...
gi 21410145 418 LVVQSCPPKDVESYIHRSGRTGR 440
Cdd:cd18801 111 LIICYDASPSPIRMIQRMGRTGR 133
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
350-441 8.27e-12

C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350189 [Multi-domain]  Cd Length: 142  Bit Score: 63.38  E-value: 8.27e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 350 RTIIFCETKKDAQELSQntCIKQDAQSLHG------------------DIPQKQREITLKGFRNGNFGVLVATNVAARGL 411
Cdd:cd18802  27 RGIIFVERRATAVVLSR--LLKEHPSTLAFircgfligrgnssqrkrsLMTQRKQKETLDKFRDGELNLLIATSVLEEGI 104
                        90       100       110
                ....*....|....*....|....*....|
gi 21410145 412 DIPEVDLVVQSCPPKDVESYIHRSGRtGRA 441
Cdd:cd18802 105 DVPACNLVIRFDLPKTLRSYIQSRGR-ARA 133
GUCT cd12929
RNA-binding GUCT domain found in the RNA helicase II/Gu protein family; This family includes ...
545-618 2.44e-10

RNA-binding GUCT domain found in the RNA helicase II/Gu protein family; This family includes vertebrate RNA helicase II/Gualpha (RH-II/Gualpha) and RNA helicase II/Gubeta (RH-II/Gubeta), both of which consist of a DEAD box helicase domain (DEAD), a helicase conserved C-terminal domain, and a Gu C-terminal (GUCT) domain. They localize to nucleoli, suggesting roles in ribosomal RNA production, but RH-II/Gubeta also localizes to nuclear speckles containing the splicing factor SC35, suggesting its possible involvement in pre-mRNA splicing. In contrast to RH-II/Gualpha, RH-II/Gubeta has RNA-unwinding activity, but no RNA-folding activity. The family also contains plant DEAD-box ATP-dependent RNA helicase 7 (RH7 or PRH75), Thermus thermophilus heat resistant RNA-dependent ATPase (Hera) and similar proteins. RH7 is a new nucleus-localized member of the DEAD-box protein family from higher plants. It displays a weak ATPase activity which is barely stimulated by RNA ligands. RH7 contains an N-terminal KDES domain rich in lysine, glutamic acid, aspartic acid, and serine residues, seven highly conserved helicase motifs in the central region, a GUCT domain, and a C-terminal GYR domain harboring a large number of glycine residues interrupted by either arginines or tyrosines. Thermus thermophilus Hera is a DEAD box helicase that binds fragments of 23S rRNA and RNase P RNA via its C-terminal domain. It contains a helicase core that harbors two RecA-like domains termed RecA_N and RecA_C, a dimerization domain (DD), and a C-terminal RNA-binding domain (RBD) that reveals a compact, RRM-like fold and shows sequence similarity with the typical GUCT domain found in the RNA helicase II/Gu protein family.


Pssm-ID: 240592  Cd Length: 72  Bit Score: 56.95  E-value: 2.44e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21410145 545 GFVTMILRCSIEMPNISYAWKELKEQLGESIdAKVKGMVFLKGKLGVCFDVRTEAVTEIQEKWHDSrRWQLTVA 618
Cdd:cd12929   1 GWVTYKLEGPRLIQSLSRLVALLKRQLLSNV-SEVGKVAELEGNGGFYFDVRPEARERLQAEPEVA-GLRLEVA 72
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
134-298 3.75e-10

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: 60.12  E-value: 3.75e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 134 KDLIAQARTGTGKTFSFAIPLIEKLQGGLqerkrgRAPQVLVLAPTRELANQVSKDFSDITKklsvacFYGGT--PYGGQ 211
Cdd:cd18047  41 QNLIAQSQSGTGKTAAFVLAMLSQVEPAN------KYPQCLCLSPTYELALQTGKVIEQMGK------FYPELklAYAVR 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 212 IERMRSGI----DILVGTPGRIKDHLQNGKL-DLTKLKHVVLDEVDQMLdmgfADQVEEILCVAYKKDSEDNPQTLLFSA 286
Cdd:cd18047 109 GNKLERGQkiseQIVIGTPGTVLDWCSKLKFiDPKKIKVFVLDEADVMI----ATQGHQDQSIRIQRMLPRNCQMLLFSA 184
                       170
                ....*....|..
gi 21410145 287 TCPHWVFNVAKK 298
Cdd:cd18047 185 TFEDSVWKFAQK 196
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
349-443 5.50e-10

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: 58.41  E-value: 5.50e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 349 GRTIIFCETKKDAQELSQntciKQDAQSLHGDIPQKQREITLKGFRNGNFGVLVATNVAARGLDIPEVDLVVQ-SCPPKD 427
Cdd:cd18789  50 DKIIVFTDNVEALYRYAK----RLLKPFITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLPEANVAIQiSGHGGS 125
                        90
                ....*....|....*.
gi 21410145 428 VESYIHRSGRTGRAGR 443
Cdd:cd18789 126 RRQEAQRLGRILRPKK 141
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
347-451 5.51e-10

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 56.17  E-value: 5.51e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 347 HQGRTIIFCETKKDAQELSQNtcikqdaqslhgdipqkqreitlkgfrngnFGVLVATNVAARGLDIPEVDLVVQSCPPK 426
Cdd:cd18785   2 MVVKIIVFTNSIEHAEEIASS------------------------------LEILVATNVLGEGIDVPSLDTVIFFDPPS 51
                        90       100
                ....*....|....*....|....*.
gi 21410145 427 DVESYIHRSGRTGRAG-RTGVCICFY 451
Cdd:cd18785  52 SAASYIQRVGRAGRGGkDEGEVILFV 77
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
123-250 9.46e-10

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


Pssm-ID: 350681 [Multi-domain]  Cd Length: 182  Bit Score: 58.37  E-value: 9.46e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 123 QAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEklqgGLQERKRGRApqvLVLAPTRELAN-QVSK--DF-SDITKKLS 198
Cdd:cd17923   5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILE----ALLRDPGSRA---LYLYPTKALAQdQLRSlrELlEQLGLGIR 77
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 21410145 199 VACFYGGTPYGGQIERMRSGIDILVGTP-----GRIKDHLQNGKLdLTKLKHVVLDE 250
Cdd:cd17923  78 VATYDGDTPREERRAIIRNPPRILLTNPdmlhyALLPHHDRWARF-LRNLRYVVLDE 133
COG1202 COG1202
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
92-414 5.08e-09

Superfamily II helicase, archaea-specific [Replication, recombination and repair];


Pssm-ID: 440815 [Multi-domain]  Cd Length: 790  Bit Score: 59.52  E-value: 5.08e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145  92 EQKEGAFSNFPISEETVKLLKARGVNFLfPIQAKTFHH-VYSGKDLIAQARTGTGKTfsfaipLIEKLqGGLQERKRGRA 170
Cdd:COG1202 184 EVDTVPVDDLDLPPELKDLLEGRGEELL-PVQSLAVENgLLEGKDQLVVSATATGKT------LIGEL-AGIKNALEGKG 255
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 171 pQVLVLAPTRELANQVSKDFSD-ITKKLSVACFYGGTPYGGQIERMRSGIDILVGTPGRIkDH-LQNGKlDLTKLKHVVL 248
Cdd:COG1202 256 -KMLFLVPLVALANQKYEDFKDrYGDGLDVSIRVGASRIRDDGTRFDPNADIIVGTYEGI-DHaLRTGR-DLGDIGTVVI 332
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 249 DEVdQMLDM--------GFadqveeilcVAYKKDSEDNPQTLLFSATC--PHWvfnVAKK-------YMK---------- 301
Cdd:COG1202 333 DEV-HMLEDperghrldGL---------IARLKYYCPGAQWIYLSATVgnPEE---LAKKlgaklveYEErpvplerhlt 399
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 302 --STYEQVDLIGKKTQKAAITvehlaikchwteraavigdvirVYS-GHQGRTIIFCETKKDAQELSQNTCIKQDAqsLH 378
Cdd:COG1202 400 faDGREKIRIINKLVKREFDT----------------------KSSkGYRGQTIIFTNSRRRCHEIARALGYKAAP--YH 455
                       330       340       350
                ....*....|....*....|....*....|....*.
gi 21410145 379 GDIPQKQREITLKGFRNGNFGVLVATNVAARGLDIP 414
Cdd:COG1202 456 AGLDYGERKKVERRFADQELAAVVTTAALAAGVDFP 491
cas3_core TIGR01587
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ...
135-443 7.86e-09

CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an alignment of Cas3, a protein found in association with CRISPR repeat elements in a broad range of bacteria and archaea. Cas3 appears to be a helicase, with regions found by pfam00270 (DEAD/DEAH box helicase) and pfam00271 (Helicase conserved C-terminal domain). Some but not all members have an N-terminal HD domain region (pfam01966) that is not included within this model.


Pssm-ID: 273707 [Multi-domain]  Cd Length: 359  Bit Score: 57.85  E-value: 7.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145   135 DLIAQARTGTGKT---FSFAIPLIeklqgglqerKRGRAPQVLVLAPTRELAN----QVSKDFSDITKKL-SVACFYGGT 206
Cdd:TIGR01587   1 LLVIEAPTGYGKTeaaLLWALHSI----------KSQKADRVIIALPTRATINamyrRAKELFGSELVGLhHSSSFSRIK 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145   207 PYG--GQIERMRS--GIDILVGTPGRIK----DHLQN------GKLDLTKL----KHVVLDEVDqmldmGFADQVEEILC 268
Cdd:TIGR01587  71 EMGdsEEFEHLFPlyIHSNDKLFLDPITvctiDQVLKsvfgefGHYEFTLAsianSLLIFDEVH-----FYDEYTLALIL 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145   269 VAYKKDSEDNPQTLLFSATCPhwvfNVAKKYMKSTYEQVDLIGKKTQKAAITVEHLAIKC--HWTERAAVIGDVIRVYSG 346
Cdd:TIGR01587 146 AVLEVLKDNDVPILLMSATLP----KFLKEYAEKIGYVEFNEPLDLKEERRFENHRFILIesDKVGEISSLERLLEFIKK 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145   347 hQGRTIIFCETKKDAQELSQNtcIKQDAQS-----LHGDIPQKQRE----ITLKGFRNGN-FGVLVATNVAARGLDIpEV 416
Cdd:TIGR01587 222 -GGSIAIIVNTVDRAQEFYQQ--LKEKAPEeeiilYHSRFTEKDRAkkeaELLREMKKSNeKFVIVATQVIEASLDI-SA 297
                         330       340
                  ....*....|....*....|....*...
gi 21410145   417 D-LVVQSCPPkdvESYIHRSGRTGRAGR 443
Cdd:TIGR01587 298 DvMITELAPI---DSLIQRLGRLHRYGR 322
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
135-443 7.98e-09

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: 57.82  E-value: 7.98e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 135 DLIAQARTGTGKT---FSFAIPLIeklqgglqerKRGRAPQVLVLAPTRELAN----QVSKDFSDITKKLSVACFYGGTP 207
Cdd:cd09639   1 LLVIEAPTGYGKTeaaLLWALHSL----------KSQKADRVIIALPTRATINamyrRAKEAFGETGLYHSSILSSRIKE 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 208 YG--GQIERMRS--GIDILVGTPGRIK----DHLQN------GKLDLTKL----KHVVLDEVDqmldmGFADQVEEILCV 269
Cdd:cd09639  71 MGdsEEFEHLFPlyIHSNDTLFLDPITvctiDQVLKsvfgefGHYEFTLAsianSLLIFDEVH-----FYDEYTLALILA 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 270 AYKKDSEDNPQTLLFSATCPhwvfnvakKYMKSTYEQVDLIGKKTQKAAITVE-HLAIKC--HWTERAAVIGDVIRVYSG 346
Cdd:cd09639 146 VLEVLKDNDVPILLMSATLP--------KFLKEYAEKIGYVEENEPLDLKPNErAPFIKIesDKVGEISSLERLLEFIKK 217
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 347 hQGRTIIFCETKKDAQELSQNtcIKQDAQS-----LHGDIPQKQR----EITLKGFRNGNFGVLVATNVAARGLDIpEVD 417
Cdd:cd09639 218 -GGSVAIIVNTVDRAQEFYQQ--LKEKGPEeeimlIHSRFTEKDRakkeAELLLEFKKSEKFVIVATQVIEASLDI-SVD 293
                       330       340
                ....*....|....*....|....*..
gi 21410145 418 -LVVQSCPPkdvESYIHRSGRTGRAGR 443
Cdd:cd09639 294 vMITELAPI---DSLIQRLGRLHRYGE 317
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
343-420 9.27e-09

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


Pssm-ID: 350186 [Multi-domain]  Cd Length: 116  Bit Score: 53.72  E-value: 9.27e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 343 VYSGHQGRTIIFCETKKDAQELSQ--NTCIKqDAQSLHGDIPQKQRE---ITLKGFRNGNFGVLVATNVAARGLDIPEVD 417
Cdd:cd18799   1 PYKYVEIKTLIFCVSIEHAEFMAEafNEAGI-DAVALNSDYSDRERGdeaLILLFFGELKPPILVTVDLLTTGVDIPEVD 79

                ...
gi 21410145 418 LVV 420
Cdd:cd18799  80 NVV 82
Cas3 COG1203
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ...
119-443 1.47e-08

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: 57.78  E-value: 1.47e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 119 LFPIQAKTFHHVYSGKDL-----IAQARTGTGKTFS---FAiplieklqggLQERKRGRAPQVLVLAPTRELANQVSKDF 190
Cdd:COG1203 128 INPLQNEALELALEAAEEepglfILTAPTGGGKTEAallFA----------LRLAAKHGGRRIIYALPFTSIINQTYDRL 197
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 191 SDITK--------KLSVACFYGGTPYGGQIERMRSGI-----DILVGTPgrikDHL-----QNGKLDLTKL-----KHVV 247
Cdd:COG1203 198 RDLFGedvllhhsLADLDLLEEEEEYESEARWLKLLKelwdaPVVVTTI----DQLfeslfSNRKGQERRLhnlanSVII 273
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 248 LDEVdQMLDMGFADQVEEILCVAYKKDSednpQTLLFSATCPHWVfnvaKKYMKSTYEqvdLIGKKTQKAAITVEHLAIK 327
Cdd:COG1203 274 LDEV-QAYPPYMLALLLRLLEWLKNLGG----SVILMTATLPPLL----REELLEAYE---LIPDEPEELPEYFRAFVRK 341
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 328 CHW-----TERAAVIGDVIRVYSGHqGRTIIFCETKKDAQELSQNtcIKQDAQS-----LHGDIPQKQR-----EItLKG 392
Cdd:COG1203 342 RVElkegpLSDEELAELILEALHKG-KSVLVIVNTVKDAQELYEA--LKEKLPDeevylLHSRFCPADRseiekEI-KER 417
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21410145 393 FRNGNFGVLVATNVAARGLDI--PEV-------DLVVQS---CppkdvesyiHRSGRTGRAGR 443
Cdd:COG1203 418 LERGKPCILVSTQVVEAGVDIdfDVVirdlaplDSLIQRagrC---------NRHGRKEEEGN 471
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
326-451 1.85e-08

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 57.46  E-value: 1.85e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 326 IKCHWTERAAVIGDVIRVYSGHQGrtIIFCETKKDAQELSQNTCIKQ-DAQSLHGDIPQKQREITLKGFRNGNFGVLVAT 404
Cdd:COG0514 210 VPKPPDDKLAQLLDFLKEHPGGSG--IVYCLSRKKVEELAEWLREAGiRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT 287
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 21410145 405 NvaARGL--DIPEVDLVVQSCPPKDVESYIHRSGRTGRAGRTGVCICFY 451
Cdd:COG0514 288 I--AFGMgiDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLY 334
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
378-440 2.27e-07

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


Pssm-ID: 350183 [Multi-domain]  Cd Length: 150  Bit Score: 50.73  E-value: 2.27e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21410145 378 HGDIPQKQREITLKGFRNGNFGVLVATNVAARGLDIPEVDLVVQSCPPKDVESYIHRSGRTGR 440
Cdd:cd18796  75 HGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
ResIII pfam04851
Type III restriction enzyme, res subunit;
134-290 4.14e-07

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 50.36  E-value: 4.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145   134 KDLIAQARTGTGKTF-SFAIplIEKLqgglqeRKRGRAPQVLVLAPTRELANQVSKDFsditKKLSVACFYGGTPYGGQ- 211
Cdd:pfam04851  24 KRGLIVMATGSGKTLtAAKL--IARL------FKKGPIKKVLFLVPRKDLLEQALEEF----KKFLPNYVEIGEIISGDk 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145   212 IERMRSGIDILVGTPGRIKDHLQNGKLDLTKLKHVVL--DEVDQmldmGFADQVEEILcvaykkDSEDNPQTLLFSATCP 289
Cdd:pfam04851  92 KDESVDDNKIVVTTIQSLYKALELASLELLPDFFDVIiiDEAHR----SGASSYRNIL------EYFKPAFLLGLTATPE 161

                  .
gi 21410145   290 H 290
Cdd:pfam04851 162 R 162
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
134-251 4.19e-07

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: 51.11  E-value: 4.19e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 134 KDLIAQARTGTGKTFsFAIPLI-EKLQGGLQERKRGRapQVLVLAPTRELANQVSKDFSDITKkLSVACFYGGTPYGGQI 212
Cdd:cd18034  17 RNTIVVLPTGSGKTL-IAVMLIkEMGELNRKEKNPKK--RAVFLVPTVPLVAQQAEAIRSHTD-LKVGEYSGEMGVDKWT 92
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 21410145 213 ERMR----SGIDILVGTPGRIKDHLQNGKLDLTKLKHVVLDEV 251
Cdd:cd18034  93 KERWkeelEKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
uvrb TIGR00631
excinuclease ABC, B subunit; All proteins in this family for wich functions are known are DNA ...
341-453 5.21e-07

excinuclease ABC, B subunit; All proteins in this family for wich functions are known are DNA helicases that function in the nucleotide excision repair and are endonucleases that make the 3' incision next to DNA damage. They are part of a pathway requiring UvrA, UvrB, UvrC, and UvrD homologs. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273185 [Multi-domain]  Cd Length: 655  Bit Score: 53.07  E-value: 5.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145   341 IRVYSGHQGRTIIFCETKKDAQELSQ---NTCIKqdAQSLHGDIPQKQREITLKGFRNGNFGVLVATNVAARGLDIPEVD 417
Cdd:TIGR00631 435 IRQRVARNERVLVTTLTKKMAEDLTDylkELGIK--VRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVS 512
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 21410145   418 LVvqSCPPKDVESYIhRSGRT-----GRAGRT--GVCICFYQN 453
Cdd:TIGR00631 513 LV--AILDADKEGFL-RSERSliqtiGRAARNvnGKVIMYADK 552
SF2_C_UvrB cd18790
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ...
350-443 6.44e-07

C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II), and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA. Its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB 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: 350177 [Multi-domain]  Cd Length: 171  Bit Score: 49.94  E-value: 6.44e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 350 RTIIFCETKKDAQELS---QNTCIKqdAQSLHGDIPQKQREITLKGFRNGNFGVLVATNVAARGLDIPEVDLVvqSCPPK 426
Cdd:cd18790  29 RVLVTTLTKRMAEDLTeylQELGVK--VRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLV--AILDA 104
                        90       100
                ....*....|....*....|..
gi 21410145 427 DVESYIhRSGRT-----GRAGR 443
Cdd:cd18790 105 DKEGFL-RSETSliqtiGRAAR 125
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
350-443 1.09e-06

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


Pssm-ID: 350184 [Multi-domain]  Cd Length: 146  Bit Score: 48.79  E-value: 1.09e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 350 RTIIFCETKKDAQELSQNT-CIKQDAQSLHGDI--------PQKQREITlKGFRNGNFGVLVATNVAARGLDIPEVDLVV 420
Cdd:cd18797  37 KTIVFCRSRKLAELLLRYLkARLVEEGPLASKVasyragylAEDRREIE-AELFNGELLGVVATNALELGIDIGGLDAVV 115
                        90       100
                ....*....|....*....|...
gi 21410145 421 QSCPPKDVESYIHRSGRTGRAGR 443
Cdd:cd18797 116 LAGYPGSLASLWQQAGRAGRRGK 138
PRK09751 PRK09751
putative ATP-dependent helicase Lhr; Provisional
374-439 1.66e-06

putative ATP-dependent helicase Lhr; Provisional


Pssm-ID: 137505 [Multi-domain]  Cd Length: 1490  Bit Score: 51.85  E-value: 1.66e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21410145   374 AQSLHGDIPQKQREITLKGFRNGNFGVLVATNVAARGLDIPEVDLVVQSCPPKDVESYIHRSGRTG 439
Cdd:PRK09751  304 ARSHHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAG 369
PRK00254 PRK00254
ski2-like helicase; Provisional
102-251 3.14e-06

ski2-like helicase; Provisional


Pssm-ID: 234702 [Multi-domain]  Cd Length: 720  Bit Score: 50.59  E-value: 3.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145  102 PISEETVKLLKARGVNFLFPIQAKTFHH-VYSGKDLIAQARTGTGKTFSFAIPLIEKL--QGGlqerkrgrapQVLVLAP 178
Cdd:PRK00254   7 RVDERIKRVLKERGIEELYPPQAEALKSgVLEGKNLVLAIPTASGKTLVAEIVMVNKLlrEGG----------KAVYLVP 76
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21410145  179 TRELANQVSKDFSDITK-KLSVACFYGGtpYGGQIERMrSGIDILVGTPGRIKDHLQNGKLDLTKLKHVVLDEV 251
Cdd:PRK00254  77 LKALAEEKYREFKDWEKlGLRVAMTTGD--YDSTDEWL-GKYDIIIATAEKFDSLLRHGSSWIKDVKLVVADEI 147
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
340-451 2.10e-05

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 47.79  E-value: 2.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145  340 VIRVYSGHQGRT-IIFCETKKDAQELSQNTCIKQ-DAQSLHGDIPQKQREITLKGFRNGNFGVLVATNVAARGLDIPEVD 417
Cdd:PRK11057 227 LMRYVQEQRGKSgIIYCNSRAKVEDTAARLQSRGiSAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVR 306
                         90       100       110
                 ....*....|....*....|....*....|....
gi 21410145  418 LVVQSCPPKDVESYIHRSGRTGRAGRTGVCICFY 451
Cdd:PRK11057 307 FVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFY 340
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
377-455 2.52e-05

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


Pssm-ID: 350179 [Multi-domain]  Cd Length: 160  Bit Score: 44.95  E-value: 2.52e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 377 LHGDIPQKQREITLKGFRNGNFGVLVATNVAARGLDIPEVDLVVQSCPPKDVESYIHR-SGRTGRAGRTGVCICFYQNKE 455
Cdd:cd18792  66 LHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIEDADRFGLSQLHQlRGRVGRGKHQSYCYLLYPDPK 145
PLN03137 PLN03137
ATP-dependent DNA helicase; Q4-like; Provisional
352-451 3.37e-05

ATP-dependent DNA helicase; Q4-like; Provisional


Pssm-ID: 215597 [Multi-domain]  Cd Length: 1195  Bit Score: 47.20  E-value: 3.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145   352 IIFCETKKDAQELSQ--NTCiKQDAQSLHGDIPQKQREITLKGFRNGNFGVLVATNVAARGLDIPEVDLVVQSCPPKDVE 429
Cdd:PLN03137  684 IIYCLSRMDCEKVAErlQEF-GHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIE 762
                          90       100
                  ....*....|....*....|..
gi 21410145   430 SYIHRSGRTGRAGRTGVCICFY 451
Cdd:PLN03137  763 GYHQECGRAGRDGQRSSCVLYY 784
HsdR COG4096
Type I site-specific restriction endonuclease, part of a restriction-modification system ...
136-192 4.76e-05

Type I site-specific restriction endonuclease, part of a restriction-modification system [Defense mechanisms];


Pssm-ID: 443272 [Multi-domain]  Cd Length: 806  Bit Score: 46.76  E-value: 4.76e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 21410145 136 LIAQArTGTGKTFSfAIPLIEKLQgglqerKRGRAPQVLVLAPTRELANQVSKDFSD 192
Cdd:COG4096 182 LLVMA-TGTGKTRT-AIALIYRLL------KAGRAKRILFLADRNALVDQAKNAFKP 230
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
119-289 1.12e-04

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


Pssm-ID: 350786 [Multi-domain]  Cd Length: 177  Bit Score: 43.48  E-value: 1.12e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 119 LFPIQAKTFHHVY-SGKDLIAQARTGTGKTFSFAIPLIEKLQGGlqerkrGRApqvLVLAPTRELANQVSKDFSDITKK- 196
Cdd:cd18028   2 LYPPQAEAVRAGLlKGENLLISIPTASGKTLIAEMAMVNTLLEG------GKA---LYLVPLRALASEKYEEFKKLEEIg 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 197 LSVACFYGGtpYGGQIERMrSGIDILVGTPGRIKDHLQNGKLDLTKLKHVVLDEVDQMLDMGFADQVEEIlcVAYKKDSE 276
Cdd:cd18028  73 LKVGISTGD--YDEDDEWL-GDYDIIVATYEKFDSLLRHSPSWLRDVGVVVVDEIHLISDEERGPTLESI--VARLRRLN 147
                       170
                ....*....|...
gi 21410145 277 DNPQTLLFSATCP 289
Cdd:cd18028 148 PNTQIIGLSATIG 160
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
142-287 1.17e-04

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


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 42.68  E-value: 1.17e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 142 TGTGKTFsFAIPLIEKLqgglqerkrgRAPQVLVLAPTRELANQVSKDFSDITKKLSVACFYGGtpyggqIERMRSGIDI 221
Cdd:cd17926  27 TGSGKTL-TALALIAYL----------KELRTLIVVPTDALLDQWKERFEDFLGDSSIGLIGGG------KKKDFDDANV 89
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21410145 222 LVGTPGRIKDHLQNGKLDLTKLKHVVLDEVDQmldmGFADQVEEILcvaykKDSEDNPQtLLFSAT 287
Cdd:cd17926  90 VVATYQSLSNLAEEEKDLFDQFGLLIVDEAHH----LPAKTFSEIL-----KELNAKYR-LGLTAT 145
UvrB COG0556
Excinuclease UvrABC helicase subunit UvrB [Replication, recombination and repair];
357-419 1.49e-04

Excinuclease UvrABC helicase subunit UvrB [Replication, recombination and repair];


Pssm-ID: 440322 [Multi-domain]  Cd Length: 657  Bit Score: 45.00  E-value: 1.49e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21410145 357 TKKDAQELS---QNTCIKqdAQSLHGDIPQKQR-EItLKGFRNGNFGVLVATNVAARGLDIPEVDLV 419
Cdd:COG0556 452 TKRMAEDLTdylKELGIK--VRYLHSDIDTLERvEI-IRDLRLGEFDVLVGINLLREGLDLPEVSLV 515
SF2_C_TRCF cd18810
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ...
377-455 1.51e-04

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


Pssm-ID: 350197 [Multi-domain]  Cd Length: 151  Bit Score: 42.72  E-value: 1.51e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 377 LHGDIPQKQREITLKGFRNGNFGVLVATNVAARGLDIPEVDLVVQSCPPKDVESYIHR-SGRTGRAGRTGVCICFYQNKE 455
Cdd:cd18810  57 AHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIIERADKFGLAQLYQlRGRVGRSKERAYAYFLYPDQK 136
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
135-250 1.58e-04

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


Pssm-ID: 350676 [Multi-domain]  Cd Length: 180  Bit Score: 43.17  E-value: 1.58e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 135 DLIAQARTGTGKTFSFAIPLIEKLqgglqerKRGRapQVLVLAPTRELANQVSKDFSDITKKLSVACFYGGTPyggqiER 214
Cdd:cd17918  38 DRLLSGDVGSGKTLVALGAALLAY-------KNGK--QVAILVPTEILAHQHYEEARKFLPFINVELVTGGTK-----AQ 103
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 21410145 215 MRSGIDILVGTPGRIKDHLQNGKLDLtklkhVVLDE 250
Cdd:cd17918 104 ILSGISLLVGTHALLHLDVKFKNLDL-----VIVDE 134
PRK05298 PRK05298
excinuclease ABC subunit UvrB;
357-419 2.20e-04

excinuclease ABC subunit UvrB;


Pssm-ID: 235395 [Multi-domain]  Cd Length: 652  Bit Score: 44.65  E-value: 2.20e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21410145  357 TKKDAQELS---QNTCIKqdAQSLHGDIPQKQR-EItLKGFRNGNFGVLVATNVAARGLDIPEVDLV 419
Cdd:PRK05298 455 TKRMAEDLTdylKELGIK--VRYLHSDIDTLERvEI-IRDLRLGEFDVLVGINLLREGLDIPEVSLV 518
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
133-250 2.41e-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: 42.50  E-value: 2.41e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 133 GKDLIAqARTGTGKTFsFAIPLIEklqgGLQERKRGRapqVLVLAPTRELANQVSKDFSDI-TKKLSVACFYGGTPYGGQ 211
Cdd:cd18035  17 GNTLIV-LPTGLGKTI-IAILVAA----DRLTKKGGK---VLILAPSRPLVEQHAENLKRVlNIPDKITSLTGEVKPEER 87
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 21410145 212 IERMRSGiDILVGTPGRIKDHLQNGKLDLTKLKHVVLDE 250
Cdd:cd18035  88 AERWDAS-KIIVATPQVIENDLLAGRITLDDVSLLIFDE 125
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
377-454 2.52e-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: 41.95  E-value: 2.52e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21410145 377 LHGDIPQKQREITLKGFRNGNFGVLVATNVAARGLDIPEVDLVVQSCPPKDVESYIHR-SGRTGRAGRTGVCICFYQNK 454
Cdd:cd18811  67 LHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIEDAERFGLSQLHQlRGRVGRGDHQSYCLLVYKDP 145
SF2_C_Ski2 cd18795
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ...
340-445 4.84e-04

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: 41.00  E-value: 4.84e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 340 VIRVYSGHQgrTIIFCETKKDAQELsqntcikqdAQSL------HGDIPQKQREITLKGFRNGNFGVLVATNVAARGLDI 413
Cdd:cd18795  37 IETVSEGKP--VLVFCSSRKECEKT---------AKDLagiafhHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNL 105
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 21410145 414 PeVDLVVqscppkdVESYIHRSGRT-------------GRAGRTG 445
Cdd:cd18795 106 P-ARTVI-------IKGTQRYDGKGyrelspleylqmiGRAGRPG 142
DDXDc_reverse_gyrase cd17924
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ...
359-405 7.80e-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: 41.16  E-value: 7.80e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 21410145 359 KDAQELSQNTCIKQDAQSLHGDIPQKQREITLKGFRNGNFGVLVATN 405
Cdd:cd17924  78 ERLSKYAEKAGVEVKILVYHSRLKKKEKEELLEKIEKGDFDILVTTN 124
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
133-250 8.19e-04

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


Pssm-ID: 350685 [Multi-domain]  Cd Length: 201  Bit Score: 41.26  E-value: 8.19e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 133 GKDLIAQARTGTGKTFsFAIPLIEKLqggLQERKRGRAPQVLVLAPTRELANQVSKDFSDIT--KKLSVACFYGGTPYGG 210
Cdd:cd17927  17 GKNTIICLPTGSGKTF-VAVLICEHH---LKKFPAGRKGKVVFLANKVPLVEQQKEVFRKHFerPGYKVTGLSGDTSENV 92
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 21410145 211 QIERMRSGIDILVGTPGRIKDHLQNGKL-DLTKLKHVVLDE 250
Cdd:cd17927  93 SVEQIVESSDVIIVTPQILVNDLKSGTIvSLSDFSLLVFDE 133
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
133-256 1.28e-03

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


Pssm-ID: 350680 [Multi-domain]  Cd Length: 166  Bit Score: 40.26  E-value: 1.28e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 133 GKDLIAQARTGTGKTFSFAIPLIEKLqgglqeRKRGRAP-QVLVLAPTRELANQVSKDF----SDITKKLSVACFYGGTP 207
Cdd:cd17922   1 GRNVLIAAPTGSGKTEAAFLPALSSL------ADEPEKGvQVLYISPLKALINDQERRLeeplDEIDLEIPVAVRHGDTS 74
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 21410145 208 yggQIER---MRSGIDILVGTPGRIKDHLQNGKLD--LTKLKHVVLDEVDQMLD 256
Cdd:cd17922  75 ---QSEKakqLKNPPGILITTPESLELLLVNKKLRelFAGLRYVVVDEIHALLG 125
SF2_C_reverse_gyrase cd18798
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ...
390-455 1.50e-03

C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase 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: 350185 [Multi-domain]  Cd Length: 174  Bit Score: 39.98  E-value: 1.50e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21410145 390 LKGFRNGNFGVLVAT----NVAARGLDIPE-VDLVVQSCPPkdVESYIHRSGRTGR--AGR--TGVCICFYQNKE 455
Cdd:cd18798  65 LEKFEEGEIDVLIGVasyyGVLVRGIDLPErIKYAIFYGVP--VTTYIQASGRTSRlyAGGltKGLSVVLVDDPE 137
CMS1 pfam14617
U3-containing 90S pre-ribosomal complex subunit; This is a family of fungal and plant ...
216-249 1.55e-03

U3-containing 90S pre-ribosomal complex subunit; This is a family of fungal and plant CMS1-like proteins. The family has similarity to the DEAD-box helicases.


Pssm-ID: 373164  Cd Length: 250  Bit Score: 41.00  E-value: 1.55e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 21410145   216 RSGIDILVGTPGRIKDHLQNGKLDLTKLKHVVLD 249
Cdd:pfam14617 173 ASRIGIGVGTPGRIADLLENESLSVDNLKYIILD 206
GUCT_Hera cd12938
RNA-binding GUCT-like domain found in Thermus thermophilus heat resistant RNA-dependent ATPase ...
536-606 1.68e-03

RNA-binding GUCT-like domain found in Thermus thermophilus heat resistant RNA-dependent ATPase (Hera) and similar proteins; This subfamily corresponds to the Gu C-terminal (GUCT)-like domain of Hera and similar proteins. Thermus thermophilus Hera is a DEAD box helicase that binds fragments of 23S rRNA and RNase P RNA via its C-terminal domain. It contains a helicase core that harbors two RecA-like domains termed RecA_N and RecA_C, a dimerization domain (DD), and a C-terminal RNA-binding domain (RBD) that reveals a compact, RRM-like fold and shows sequence similarity with GUCT domain found in vertebrate RNA helicase II/Gualpha (RH-II/Gualpha), RNA helicase II/Gubeta (RH-II/Gubeta) and plant DEAD-box ATP-dependent RNA helicase 7 (RH7 or PRH75).


Pssm-ID: 240595  Cd Length: 74  Bit Score: 37.66  E-value: 1.68e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21410145 536 QRSLINSQAGFVTMILRCSIEMPNIS--YAWKELKEQLGESIdAKVKgmvFLKGKLGVCFDVRTEAVTEIQEK 606
Cdd:cd12938   1 PRSLLTGEEGWTTLQLTGSRLLPPGSvrRAVGLLSRAAADGV-GKIR---ILADAGGAVFDLPEEIAKELLAK 69
DEAD-like_helicase_C cd09300
C-terminal helicase domain of the DEAD-like helicases; This hierarchy of DEAD-like helicases ...
400-445 1.83e-03

C-terminal helicase domain of the DEAD-like helicases; This hierarchy of DEAD-like helicases is composed of two superfamilies, SF1 and SF2, that share almost identical folds and extensive structural similarity in their catalytic core. Helicases are involved in ATP-dependent RNA or DNA unwinding. Two distinct types of helicases exist, those forming toroidal, predominantly hexameric structures, and those that do not. SF1 and SF2 helicases do not form toroidal structures, while SF3-6 helicases do. Their conserved 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: 350171 [Multi-domain]  Cd Length: 59  Bit Score: 37.14  E-value: 1.83e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 21410145 400 VLVATNVAARGLDIPEVDLVVQSCPPKDVESYIHRSGRTGRAGRTG 445
Cdd:cd09300   8 VLIAVN*ALTGFDAPELNTIIVDKNLRSYRGLNQAFGRANRIYTFG 53
SF2_C_RHA cd18791
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ...
377-451 1.94e-03

C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family members 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: 350178 [Multi-domain]  Cd Length: 171  Bit Score: 39.82  E-value: 1.94e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 377 LHGDIP-QKQREI---TLKGFRNgnfgVLVATNVAARGLDIPEVDLVVQSCPPKdVESYIHRSG---------------- 436
Cdd:cd18791  80 LHSSLPpEEQQRVfepPPPGVRK----VVLATNIAETSITIPGVVYVIDSGLVK-EKVYDPRTGlsslvtvwiskasaeq 154
                        90
                ....*....|....*..
gi 21410145 437 RTGRAGRT--GVCICFY 451
Cdd:cd18791 155 RAGRAGRTrpGKCYRLY 171
DinG COG1199
Rad3-related DNA helicase DinG [Replication, recombination and repair];
124-197 1.95e-03

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


Pssm-ID: 440812 [Multi-domain]  Cd Length: 629  Bit Score: 41.45  E-value: 1.95e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21410145 124 AKTFHhvySGKDLIAQARTGTGKTFSFAIPLIeklqggLQERKRGRapQVLVLAPTRELANQ-VSKDFSDITKKL 197
Cdd:COG1199  27 ARALA---EGRHLLIEAGTGTGKTLAYLVPAL------LAARETGK--KVVISTATKALQEQlVEKDLPLLRKAL 90
DEXHc_RE_I_III_res cd18032
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ...
136-198 2.28e-03

DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350790 [Multi-domain]  Cd Length: 163  Bit Score: 39.47  E-value: 2.28e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21410145 136 LIAQArTGTGKTFSfAIPLIEKLQgglqerKRGRAPQVLVLAPTRELANQVSKDFSDITKKLS 198
Cdd:cd18032  24 LLVMA-TGTGKTYT-AAFLIKRLL------EANRKKRILFLAHREELLEQAERSFKEVLPDGS 78
PTZ00146 PTZ00146
fibrillarin; Provisional
632-678 4.39e-03

fibrillarin; Provisional


Pssm-ID: 240291  Cd Length: 293  Bit Score: 39.72  E-value: 4.39e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 21410145  632 RGRMGQRDGSRGAFRGQRGGSRNFRGQGQRGGSRNFRGQRPGGGNRG 678
Cdd:PTZ00146   4 GGFGGGRGGGRGGGGGGGRGGGGRGGGRGGGRGRGRGGGGGGRGGGG 50
DEXDc_ComFA cd17925
DEXD-box helicase domain of ComFA; ATP-dependent helicase ComFA (also called ComF operon ...
130-287 4.63e-03

DEXD-box helicase domain of ComFA; ATP-dependent helicase ComFA (also called ComF operon protein 1) is part of the complex mediating the binding and uptake of single-stranded DNA. ComFA is required for DNA uptake but not for binding. It 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: 350683 [Multi-domain]  Cd Length: 143  Bit Score: 38.05  E-value: 4.63e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 130 VYSGKDLIAQARTGTGKTfSFAIPLIEKLqggLQERKRgrapqVLVLAP----TRELANQVSKDFSDITkklsVACFYGG 205
Cdd:cd17925  13 IDAKEDLLVWAVTGAGKT-EMLFPAIAQA---LRQGGR-----VAIASPridvCLELAPRLKAAFPGAA----IVLLHGG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21410145 206 TPYGGQIErmrsgiDILVGTPG---RIKDHlqngkLDLtklkhVVLDEVDqmldmGFADQVEEILCVAYKKDSEDNPQTL 282
Cdd:cd17925  80 SEDQYQRS------PLVIATTHqllRFYRA-----FDL-----LIIDEVD-----AFPYAGDPMLYYAVEKARKEEGSLI 138

                ....*
gi 21410145 283 LFSAT 287
Cdd:cd17925 139 YLTAT 143
PTZ00146 PTZ00146
fibrillarin; Provisional
630-678 9.12e-03

fibrillarin; Provisional


Pssm-ID: 240291  Cd Length: 293  Bit Score: 38.56  E-value: 9.12e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 21410145  630 GYRGRMGQRDGSRGAFRGQRGGSRNFRGQGQRGGSRNFRGQRPGGGNRG 678
Cdd:PTZ00146   8 GGRGGGRGGGGGGGRGGGGRGGGRGGGRGRGRGGGGGGRGGGGGGGPGK 56
PTZ00146 PTZ00146
fibrillarin; Provisional
633-680 9.53e-03

fibrillarin; Provisional


Pssm-ID: 240291  Cd Length: 293  Bit Score: 38.56  E-value: 9.53e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 21410145  633 GRMGQRDGSRGAFRGQRGGSRnfRGQGQRGGSRNFRGQRPGGGNRGQK 680
Cdd:PTZ00146   1 GMGGGFGGGRGGGRGGGGGGG--RGGGGRGGGRGGGRGRGRGGGGGGR 46
 
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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