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Conserved domains on  [gi|1001624560|ref|NP_001307455|]
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ATP-dependent RNA helicase DDX19A isoform 4 [Homo sapiens]

Protein Classification

DEAD/DEAH box helicase domain-containing protein( domain architecture ID 1000559)

DEAD/DEAH box helicase domain-containing protein may function as an RNA helicase

EC:  3.6.4.-
Gene Ontology:  GO:0005524|GO:0004386|GO:0003676
PubMed:  20206133

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SrmB super family cl33924
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
1-325 1.06e-95

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


The actual alignment was detected with superfamily member COG0513:

Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 289.74  E-value: 1.06e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560   1 MLSRVEPS-DRYPQCLCLSPTYELALQTGKVIEQMGKFYPeLKLAYAVRG-------NKLERGQkiseQIVIGTPGTVLD 72
Cdd:COG0513    60 LLQRLDPSrPRAPQALILAPTRELALQVAEELRKLAKYLG-LRVATVYGGvsigrqiRALKRGV----DIVVATPGRLLD 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560  73 WCSKlKFIDPKKIKVFVLDEADVMIAtQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIKLKREEET 152
Cdd:COG0513   135 LIER-GALDLSGVETLVLDEADRMLD-MGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENAT 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560 153 LDTIKQYYVLCSSRDeKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGK 232
Cdd:COG0513   213 AETIEQRYYLVDKRD-KLELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGK 291
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560 233 EKVLVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAVNMVdSKHSMNILNRIQEHFNKKI 312
Cdd:COG0513   292 IRVLVATDVAARGIDIDDVSHVINYDLPEDP------EDYVHRIGRTGRAGAEGTAISLV-TPDERRLLRAIEKLIGQKI 364
                         330
                  ....*....|...
gi 1001624560 313 ERLDTDDLDEIEK 325
Cdd:COG0513   365 EEEELPGFEPVEE 377
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
1-325 1.06e-95

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 289.74  E-value: 1.06e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560   1 MLSRVEPS-DRYPQCLCLSPTYELALQTGKVIEQMGKFYPeLKLAYAVRG-------NKLERGQkiseQIVIGTPGTVLD 72
Cdd:COG0513    60 LLQRLDPSrPRAPQALILAPTRELALQVAEELRKLAKYLG-LRVATVYGGvsigrqiRALKRGV----DIVVATPGRLLD 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560  73 WCSKlKFIDPKKIKVFVLDEADVMIAtQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIKLKREEET 152
Cdd:COG0513   135 LIER-GALDLSGVETLVLDEADRMLD-MGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENAT 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560 153 LDTIKQYYVLCSSRDeKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGK 232
Cdd:COG0513   213 AETIEQRYYLVDKRD-KLELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGK 291
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560 233 EKVLVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAVNMVdSKHSMNILNRIQEHFNKKI 312
Cdd:COG0513   292 IRVLVATDVAARGIDIDDVSHVINYDLPEDP------EDYVHRIGRTGRAGAEGTAISLV-TPDERRLLRAIEKLIGQKI 364
                         330
                  ....*....|...
gi 1001624560 313 ERLDTDDLDEIEK 325
Cdd:COG0513   365 EEEELPGFEPVEE 377
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
1-145 1.18e-90

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: 269.28  E-value: 1.18e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560   1 MLSRVEPSDRYPQCLCLSPTYELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKISEQIVIGTPGTVLDWCSKLKFI 80
Cdd:cd18047    61 MLSQVEPANKYPQCLCLSPTYELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKISEQIVIGTPGTVLDWCSKLKFI 140
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1001624560  81 DPKKIKVFVLDEADVMIATQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 145
Cdd:cd18047   141 DPKKIKVFVLDEADVMIATQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 205
PTZ00424 PTZ00424
helicase 45; Provisional
2-318 2.10e-76

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 239.73  E-value: 2.10e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560   2 LSRVEPSDRYPQCLCLSPTYELALQTGKVIEQMGKfYPELKLAYAVRG-------NKLERGQkiseQIVIGTPGTVLDWC 74
Cdd:PTZ00424   87 LQLIDYDLNACQALILAPTRELAQQIQKVVLALGD-YLKVRCHACVGGtvvrddiNKLKAGV----HMVVGTPGRVYDMI 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560  75 SKlKFIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIKLKREEETLD 154
Cdd:PTZ00424  162 DK-RHLRVDDLKLFILDEADEML-SRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLE 239
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560 155 TIKQYYVLCSSRDEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEK 234
Cdd:PTZ00424  240 GIRQFYVAVEKEEWKFDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTR 319
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560 235 VLVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAVNMVDSKhSMNILNRIQEHFNKKIER 314
Cdd:PTZ00424  320 VLITTDLLARGIDVQQVSLVINYDLPASP------ENYIHRIGRSGRFGRKGVAINFVTPD-DIEQLKEIERHYNTQIEE 392

                  ....
gi 1001624560 315 LDTD 318
Cdd:PTZ00424  393 MPME 396
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
168-283 8.72e-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: 115.00  E-value: 8.72e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560 168 EKFQALCNLYGAITIAQAMIFCHTRKTA--SWLaaeLSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARG 245
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLeaELL---LEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERG 77
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1001624560 246 IDVEQVSVVINFDLPvdkdGNPdnETYLHRIGRTGRFG 283
Cdd:pfam00271  78 LDLPDVDLVINYDLP----WNP--ASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
197-283 8.00e-27

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 100.75  E-value: 8.00e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560  197 WLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRI 276
Cdd:smart00490   2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSP------ASYIQRI 75

                   ....*..
gi 1001624560  277 GRTGRFG 283
Cdd:smart00490  76 GRAGRAG 82
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
1-325 1.06e-95

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 289.74  E-value: 1.06e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560   1 MLSRVEPS-DRYPQCLCLSPTYELALQTGKVIEQMGKFYPeLKLAYAVRG-------NKLERGQkiseQIVIGTPGTVLD 72
Cdd:COG0513    60 LLQRLDPSrPRAPQALILAPTRELALQVAEELRKLAKYLG-LRVATVYGGvsigrqiRALKRGV----DIVVATPGRLLD 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560  73 WCSKlKFIDPKKIKVFVLDEADVMIAtQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIKLKREEET 152
Cdd:COG0513   135 LIER-GALDLSGVETLVLDEADRMLD-MGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENAT 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560 153 LDTIKQYYVLCSSRDeKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGK 232
Cdd:COG0513   213 AETIEQRYYLVDKRD-KLELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGK 291
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560 233 EKVLVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAVNMVdSKHSMNILNRIQEHFNKKI 312
Cdd:COG0513   292 IRVLVATDVAARGIDIDDVSHVINYDLPEDP------EDYVHRIGRTGRAGAEGTAISLV-TPDERRLLRAIEKLIGQKI 364
                         330
                  ....*....|...
gi 1001624560 313 ERLDTDDLDEIEK 325
Cdd:COG0513   365 EEEELPGFEPVEE 377
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
1-145 1.18e-90

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: 269.28  E-value: 1.18e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560   1 MLSRVEPSDRYPQCLCLSPTYELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKISEQIVIGTPGTVLDWCSKLKFI 80
Cdd:cd18047    61 MLSQVEPANKYPQCLCLSPTYELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKISEQIVIGTPGTVLDWCSKLKFI 140
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1001624560  81 DPKKIKVFVLDEADVMIATQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 145
Cdd:cd18047   141 DPKKIKVFVLDEADVMIATQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 205
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
1-152 2.45e-88

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: 264.19  E-value: 2.45e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560   1 MLSRVEPSDRYPQCLCLSPTYELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKISEQIVIGTPGTVLDWCSKLKFI 80
Cdd:cd18048    78 MLSRVDALKLYPQCLCLSPTFELALQTGKVVEEMGKFCVGIQVIYAIRGNRPGKGTDIEAQIVIGTPGTVLDWCFKLRLI 157
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1001624560  81 DPKKIKVFVLDEADVMIATQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIKLKREEET 152
Cdd:cd18048   158 DVTNISVFVLDEADVMINVQGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
1-145 9.78e-84

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: 251.34  E-value: 9.78e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560   1 MLSRVEPSDRYPQCLCLSPTYELALQTGKVIEQMGKFyPELKLAYAVRGNKLERGQKISEQIVIGTPGTVLDWCSKlKFI 80
Cdd:cd17963    54 MLSRVDPTLKSPQALCLAPTRELARQIGEVVEKMGKF-TGVKVALAVPGNDVPRGKKITAQIVIGTPGTVLDWLKK-RQL 131
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1001624560  81 DPKKIKVFVLDEADVMIATQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 145
Cdd:cd17963   132 DLKKIKILVLDEADVMLDTQGHGDQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTIK 196
PTZ00424 PTZ00424
helicase 45; Provisional
2-318 2.10e-76

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 239.73  E-value: 2.10e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560   2 LSRVEPSDRYPQCLCLSPTYELALQTGKVIEQMGKfYPELKLAYAVRG-------NKLERGQkiseQIVIGTPGTVLDWC 74
Cdd:PTZ00424   87 LQLIDYDLNACQALILAPTRELAQQIQKVVLALGD-YLKVRCHACVGGtvvrddiNKLKAGV----HMVVGTPGRVYDMI 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560  75 SKlKFIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIKLKREEETLD 154
Cdd:PTZ00424  162 DK-RHLRVDDLKLFILDEADEML-SRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLE 239
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560 155 TIKQYYVLCSSRDEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEK 234
Cdd:PTZ00424  240 GIRQFYVAVEKEEWKFDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTR 319
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560 235 VLVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAVNMVDSKhSMNILNRIQEHFNKKIER 314
Cdd:PTZ00424  320 VLITTDLLARGIDVQQVSLVINYDLPASP------ENYIHRIGRSGRFGRKGVAINFVTPD-DIEQLKEIERHYNTQIEE 392

                  ....
gi 1001624560 315 LDTD 318
Cdd:PTZ00424  393 MPME 396
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
1-321 2.06e-55

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 186.93  E-value: 2.06e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560   1 MLSRVEPSDRYPQCLCLSPTYELALQTGKVIEQMGKFYPELKLAYAVRG-------NKLERGQkiseQIVIGTPGTVLDW 73
Cdd:PRK11776   62 LLQKLDVKRFRVQALVLCPTRELADQVAKEIRRLARFIPNIKVLTLCGGvpmgpqiDSLEHGA----HIIVGTPGRILDH 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560  74 CSKlKFIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIKLKrEEETL 153
Cdd:PRK11776  138 LRK-GTLDLDALNTLVLDEADRML-DMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVE-STHDL 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560 154 DTIKQYYVLCSsRDEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMmvEQ--RAAVIERFREG 231
Cdd:PRK11776  215 PAIEQRFYEVS-PDERLPALQRLLLHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDL--EQrdRDQVLVRFANR 291
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560 232 KEKVLVTTNVCARGIDVEQVSVVINFDLPvdkdgnPDNETYLHRIGRTGRFGKRGLAVNMVdSKHSMNILNRIQEHFNKK 311
Cdd:PRK11776  292 SCSVLVATDVAARGLDIKALEAVINYELA------RDPEVHVHRIGRTGRAGSKGLALSLV-APEEMQRANAIEDYLGRK 364
                         330
                  ....*....|
gi 1001624560 312 IERLDTDDLD 321
Cdd:PRK11776  365 LNWEPLPSLS 374
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
12-320 8.48e-55

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 184.38  E-value: 8.48e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560  12 PQCLCLSPTYELALQtgkVIEQMGKFYPELKL---------AYAVRGNKLERGQkiseQIVIGTPGTVLDWCSKLKFiDP 82
Cdd:PRK11192   74 PRILILTPTRELAMQ---VADQARELAKHTHLdiatitggvAYMNHAEVFSENQ----DIVVATPGRLLQYIKEENF-DC 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560  83 KKIKVFVLDEADVMIATQGHQD-QSIRIQrmlPRNC-QMLLFSATFE-DSVWKFAQKVVPDPNVIKL---KREEETldtI 156
Cdd:PRK11192  146 RAVETLILDEADRMLDMGFAQDiETIAAE---TRWRkQTLLFSATLEgDAVQDFAERLLNDPVEVEAepsRRERKK---I 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560 157 KQYYVLCSSRDEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVL 236
Cdd:PRK11192  220 HQWYYRADDLEHKTALLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVL 299
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560 237 VTTNVCARGIDVEQVSVVINFDLPVDKDgnpdneTYLHRIGRTGRFGKRGLAVNMVDSkHSMNILNRIQEHFNKKIERLD 316
Cdd:PRK11192  300 VATDVAARGIDIDDVSHVINFDMPRSAD------TYLHRIGRTGRAGRKGTAISLVEA-HDHLLLGKIERYIEEPLKARV 372

                  ....
gi 1001624560 317 TDDL 320
Cdd:PRK11192  373 IDEL 376
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
156-292 4.28e-52

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: 168.07  E-value: 4.28e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560 156 IKQYYVLCSSRDEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKV 235
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1001624560 236 LVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAVNMV 292
Cdd:cd18787    81 LVATDVAARGLDIPGVDHVINYDLPRDA------EDYVHRIGRTGRAGRKGTAITFV 131
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
7-313 2.57e-48

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 168.55  E-value: 2.57e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560   7 PSDRY---PQCLCLSPTYELALQTGKVIEQMGKfYPELKLAYAVRGNKLERGQKISEQ----IVIGTPGTVLDWCSKlKF 79
Cdd:PRK01297  155 PKERYmgePRALIIAPTRELVVQIAKDAAALTK-YTGLNVMTFVGGMDFDKQLKQLEArfcdILVATPGRLLDFNQR-GE 232
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560  80 IDPKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNC--QMLLFSATFEDSVWKFAQKVVPDPNVIKLKREEETLDTIK 157
Cdd:PRK01297  233 VHLDMVEVMVLDEADRML-DMGFIPQVRQIIRQTPRKEerQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVE 311
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560 158 QYYVLCSSRDeKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLV 237
Cdd:PRK01297  312 QHVYAVAGSD-KYKLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLV 390
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1001624560 238 TTNVCARGIDVEQVSVVINFDLPVDkdgnPDNetYLHRIGRTGRFGKRGLAVNMVDSKHSMNiLNRIQEHFNKKIE 313
Cdd:PRK01297  391 ATDVAGRGIHIDGISHVINFTLPED----PDD--YVHRIGRTGRAGASGVSISFAGEDDAFQ-LPEIEELLGRKIS 459
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
1-295 5.40e-45

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 162.32  E-value: 5.40e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560   1 MLSRVEPSDRYPQCLCLSPTYELALQTGKVIEQMGKFYPELKLAYAVRGNKLE---RGQKISEQIVIGTPGTVLDWCsKL 77
Cdd:PRK11634   64 LLHNLDPELKAPQILVLAPTRELAVQVAEAMTDFSKHMRGVNVVALYGGQRYDvqlRALRQGPQIVVGTPGRLLDHL-KR 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560  78 KFIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIKLKREEETLDTIK 157
Cdd:PRK11634  143 GTLDLSKLSGLVLDEADEML-RMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDIS 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560 158 Q-YYVLCSSRdeKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVL 236
Cdd:PRK11634  222 QsYWTVWGMR--KNEALVRFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDIL 299
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1001624560 237 VTTNVCARGIDVEQVSVVINFDLPVdkdgnpDNETYLHRIGRTGRFGKRGLAVNMVDSK 295
Cdd:PRK11634  300 IATDVAARGLDVERISLVVNYDIPM------DSESYVHRIGRTGRAGRAGRALLFVENR 352
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
1-312 1.74e-43

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 157.42  E-value: 1.74e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560   1 MLSRVEPSDRYPQ---CLCLSPTYELALQTGKvieQMGKFYPELKLAYAV--RGNKLERGQKISEQ---IVIGTPGTVLD 72
Cdd:PRK04537   71 LLSRPALADRKPEdprALILAPTRELAIQIHK---DAVKFGADLGLRFALvyGGVDYDKQRELLQQgvdVIIATPGRLID 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560  73 WCSKLKFIDPKKIKVFVLDEADVMIATQGHQDqsIR-IQRMLPRNC--QMLLFSATFEDSVWKFAQKVVPDPNviKLKRE 149
Cdd:PRK04537  148 YVKQHKVVSLHACEICVLDEADRMFDLGFIKD--IRfLLRRMPERGtrQTLLFSATLSHRVLELAYEHMNEPE--KLVVE 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560 150 EETLDTIK-QYYVLCSSRDEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERF 228
Cdd:PRK04537  224 TETITAARvRQRIYFPADEEKQTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRF 303
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560 229 REGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAVNMVDSKHSMNiLNRIQEHF 308
Cdd:PRK04537  304 QKGQLEILVATDVAARGLHIDGVKYVYNYDLPFDA------EDYVHRIGRTARLGEEGDAISFACERYAMS-LPDIEAYI 376

                  ....
gi 1001624560 309 NKKI 312
Cdd:PRK04537  377 EQKI 380
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
1-312 1.07e-41

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 149.74  E-value: 1.07e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560   1 MLSRVEPSDRY---PQCLCLSPTYELALQTGKVIEQMGKfYPELKLAYAVRGNKLERGQKISEQ---IVIGTPGTVLDWc 74
Cdd:PRK04837   70 LLSHPAPEDRKvnqPRALIMAPTRELAVQIHADAEPLAQ-ATGLKLGLAYGGDGYDKQLKVLESgvdILIGTTGRLIDY- 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560  75 SKLKFIDPKKIKVFVLDEADVMIATQGHQDqsIR--IQRMLPRNCQM-LLFSATFEDSVWKFAQKVVPDPNVIKLKREEE 151
Cdd:PRK04837  148 AKQNHINLGAIQVVVLDEADRMFDLGFIKD--IRwlFRRMPPANQRLnMLFSATLSYRVRELAFEHMNNPEYVEVEPEQK 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560 152 TLDTIKQ--YYvlcSSRDEKFQALCNLYGAITIAQAMIFCHTR----KTASWLAAElskeGHQVALLSGEMMVEQRAAVI 225
Cdd:PRK04837  226 TGHRIKEelFY---PSNEEKMRLLQTLIEEEWPDRAIIFANTKhrceEIWGHLAAD----GHRVGLLTGDVAQKKRLRIL 298
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560 226 ERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPvdkdgnPDNETYLHRIGRTGRFGKRGLAVNMVDSKHSMNiLNRIQ 305
Cdd:PRK04837  299 EEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLP------DDCEDYVHRIGRTGRAGASGHSISLACEEYALN-LPAIE 371

                  ....*..
gi 1001624560 306 EHFNKKI 312
Cdd:PRK04837  372 TYIGHSI 378
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
7-292 1.00e-35

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 134.17  E-value: 1.00e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560   7 PSDRYP-QCLCLSPTYELALQTGKVIEQMGKFYPELKLAyaVRGnklerGQKISEQ---------IVIGTPGTVLDwCSK 76
Cdd:PRK10590   70 AKGRRPvRALILTPTRELAAQIGENVRDYSKYLNIRSLV--VFG-----GVSINPQmmklrggvdVLVATPGRLLD-LEH 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560  77 LKFIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIKLKREEETLDTI 156
Cdd:PRK10590  142 QNAVKLDQVEILVLDEADRML-DMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQV 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560 157 KQYyVLCSSRDEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVL 236
Cdd:PRK10590  221 TQH-VHFVDKKRKRELLSQMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVL 299
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1001624560 237 VTTNVCARGIDVEQVSVVINFDLP-VDKDgnpdnetYLHRIGRTGRFGKRGLAVNMV 292
Cdd:PRK10590  300 VATDIAARGLDIEELPHVVNYELPnVPED-------YVHRIGRTGRAAATGEALSLV 349
PTZ00110 PTZ00110
helicase; Provisional
4-288 1.02e-32

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 127.20  E-value: 1.02e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560   4 RVEPSDRY---PQCLCLSPTYELALQtgkVIEQMGKFYPELKLAYAVR-GNKLERGQKIS----EQIVIGTPGTVLDW-- 73
Cdd:PTZ00110  193 NAQPLLRYgdgPIVLVLAPTRELAEQ---IREQCNKFGASSKIRNTVAyGGVPKRGQIYAlrrgVEILIACPGRLIDFle 269
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560  74 --CSKLKfidpkKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP----NV--IK 145
Cdd:PTZ00110  270 snVTNLR-----RVTYLVLDEADRML-DMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEEpvhvNVgsLD 343
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560 146 LKreeeTLDTIKQYYVLCSSRdEKFQALCNLYGAITI--AQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAA 223
Cdd:PTZ00110  344 LT----ACHNIKQEVFVVEEH-EKRGKLKMLLQRIMRdgDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTW 418
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1001624560 224 VIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPvdkdgnPDNETYLHRIGRTGRFGKRGLA 288
Cdd:PTZ00110  419 VLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFP------NQIEDYVHRIGRTGRAGAKGAS 477
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
1-145 3.79e-32

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: 118.70  E-value: 3.79e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560   1 MLSRVEPSDRYPQCLCLSPTYELALQTGKVIEQMGKfYPELKlAYAVRGnklerGQKISEQ---------IVIGTPGTVL 71
Cdd:cd00268    52 LLPEPKKKGRGPQALVLAPTRELAMQIAEVARKLGK-GTGLK-VAAIYG-----GAPIKKQiealkkgpdIVVGTPGRLL 124
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1001624560  72 DWCSKlKFIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 145
Cdd:cd00268   125 DLIER-GKLDLSNVKYLVLDEADRML-DMGFEEDVEKILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
168-283 8.72e-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: 115.00  E-value: 8.72e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560 168 EKFQALCNLYGAITIAQAMIFCHTRKTA--SWLaaeLSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARG 245
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLeaELL---LEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERG 77
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1001624560 246 IDVEQVSVVINFDLPvdkdGNPdnETYLHRIGRTGRFG 283
Cdd:pfam00271  78 LDLPDVDLVINYDLP----WNP--ASYIQRIGRAGRAG 109
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
7-293 6.12e-31

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 121.82  E-value: 6.12e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560   7 PSDRYPQCLCLSPTYELALQTGKVIEQMGKFYPeLKLAYAVRGN----KLERGQKISEQIViGTPGTVLDWCSKLKfIDP 82
Cdd:PLN00206  192 SEQRNPLAMVLTPTRELCVQVEDQAKVLGKGLP-FKTALVVGGDampqQLYRIQQGVELIV-GTPGRLIDLLSKHD-IEL 268
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560  83 KKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNcQMLLFSATFEDSVWKFAQKVVPDPNVIKLKREEETLDTIKQYYVL 162
Cdd:PLN00206  269 DNVSVLVLDEVDCML-ERGFRDQVMQIFQALSQP-QVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIW 346
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560 163 CSSRDEKFQalcnLYGAITIAQ-----AMIFCHTRKTASWLAAELSK-EGHQVALLSGEMMVEQRAAVIERFREGKEKVL 236
Cdd:PLN00206  347 VETKQKKQK----LFDILKSKQhfkppAVVFVSSRLGADLLANAITVvTGLKALSIHGEKSMKERREVMKSFLVGEVPVI 422
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1001624560 237 VTTNVCARGIDVEQVSVVINFDLPvdkdgNPDNEtYLHRIGRTGRFGKRGLAVNMVD 293
Cdd:PLN00206  423 VATGVLGRGVDLLRVRQVIIFDMP-----NTIKE-YIHQIGRASRMGEKGTAIVFVN 473
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
2-144 1.02e-27

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: 107.02  E-value: 1.02e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560   2 LSRVEPSDRYPQCLCLSPTYELALQTGKVIEQMGkFYPELKLAYAVRGNKLE---RGQKISEQIVIGTPGTVLDWCSKlK 78
Cdd:cd17939    56 LQRIDTTVRETQALVLAPTRELAQQIQKVVKALG-DYMGVKVHACIGGTSVRedrRKLQYGPHIVVGTPGRVFDMLQR-R 133
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1001624560  79 FIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVI 144
Cdd:cd17939   134 SLRTDKIKMFVLDEADEML-SRGFKDQIYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
HELICc smart00490
helicase superfamily c-terminal domain;
197-283 8.00e-27

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 100.75  E-value: 8.00e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560  197 WLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRI 276
Cdd:smart00490   2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSP------ASYIQRI 75

                   ....*..
gi 1001624560  277 GRTGRFG 283
Cdd:smart00490  76 GRAGRAG 82
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
1-130 2.37e-25

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: 99.62  E-value: 2.37e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560   1 MLSRVEPSDRYPQCLCLSPTYELALQTGKVIEQMGKFYpELKLAYAVRGN--KLERGQKISEQIVIGTPGTVLDWCSKLK 78
Cdd:pfam00270  35 ALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGL-GLKVASLLGGDsrKEQLEKLKGPDILVGTPGRLLDLLQERK 113
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1001624560  79 FIdpKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSV 130
Cdd:pfam00270 114 LL--KNLKLLVLDEAHRLL-DMGFGPDLEEILRRLPKKRQILLLSATLPRNL 162
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
2-141 1.04e-24

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: 99.06  E-value: 1.04e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560   2 LSRVEPSDRYPQCLCLSPTYELALQTGKVIEQMGkFYPELKLAYAVRG-------NKLERGQkiseQIVIGTPGTVLDWC 74
Cdd:cd18046    58 LQQIDTSLKATQALVLAPTRELAQQIQKVVMALG-DYMGIKCHACIGGtsvrddaQKLQAGP----HIVVGTPGRVFDMI 132
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1001624560  75 SKlKFIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 141
Cdd:cd18046   133 NR-RYLRTDYIKMFVLDEADEML-SRGFKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDP 197
DEXDc smart00487
DEAD-like helicases superfamily;
8-159 5.65e-23

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 94.48  E-value: 5.65e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560    8 SDRYPQCLCLSPTYELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKISE---QIVIGTPGTVLDWCSKlKFIDPKK 84
Cdd:smart00487  51 RGKGGRVLVLVPTRELAEQWAEELKKLGPSLGLKVVGLYGGDSKREQLRKLESgktDILVTTPGRLLDLLEN-DKLSLSN 129
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1001624560   85 IKVFVLDEADVMIAtQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIklKREEETLDTIKQY 159
Cdd:smart00487 130 VDLVILDEAHRLLD-GGFGDQLEKLLKLLPKNVQLLLLSATPPEEIENLLELFLNDPVFI--DVGFTPLEPIEQF 201
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
1-144 5.90e-23

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


Pssm-ID: 350698 [Multi-domain]  Cd Length: 201  Bit Score: 94.29  E-value: 5.90e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560   1 MLSRVEPSDRYPQCLCLSPTYELALQTGKVIEQMGKfYPELKLAYAVRGNKL-ERGQKISE--QIVIGTPGTVLDWCSKl 77
Cdd:cd17940    57 ILEKIDPKKDVIQALILVPTRELALQTSQVCKELGK-HMGVKVMVTTGGTSLrDDIMRLYQtvHVLVGTPGRILDLAKK- 134
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1001624560  78 KFIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVI 144
Cdd:cd17940   135 GVADLSHCKTLVLDEADKLL-SQDFQPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
1-144 4.10e-21

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: 89.45  E-value: 4.10e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560   1 MLSRVEPSDRYPQCLCLSPTYELALQTGKVIEQMGKFYpELKLAYAVRGN-------KLERGQkiseQIVIGTPGTVLDW 73
Cdd:cd18045    57 VLQCLDIQVRETQALILSPTRELAVQIQKVLLALGDYM-NVQCHACIGGTsvgddirKLDYGQ----HIVSGTPGRVFDM 131
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1001624560  74 CSKlKFIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVI 144
Cdd:cd18045   132 IRR-RSLRTRHIKMLVLDEADEML-NKGFKEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
15-145 1.05e-19

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: 85.43  E-value: 1.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560  15 LCLSPTYELALQTGKVIEQMGKFyPELKLAYAVRGNKLERG-QKISEQ--IVIGTPGTVLDWCSKLKFiDPKKIKVFVLD 91
Cdd:cd17959    75 LILSPTRELALQTLKVTKELGKF-TDLRTALLVGGDSLEEQfEALASNpdIIIATPGRLLHLLVEMNL-KLSSVEYVVFD 152
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1001624560  92 EADVMIAtQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 145
Cdd:cd17959   153 EADRLFE-MGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLIR 205
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
8-146 1.34e-19

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: 85.33  E-value: 1.34e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560   8 SDRYPQCLCLSPTYELALQTGKVIEQMGKFY-PELKLAyAVRGNKLERGQK--ISEQ--IVIGTPGTVLDWCSKLKFIDP 82
Cdd:cd17961    65 EEQGTRALILVPTRELAQQVSKVLEQLTAYCrKDVRVV-NLSASSSDSVQRalLAEKpdIVVSTPARLLSHLESGSLLLL 143
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1001624560  83 KKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIKL 146
Cdd:cd17961   144 STLKYLVIDEADLVL-SYGYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPAILKL 206
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
1-145 1.98e-19

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: 84.62  E-value: 1.98e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560   1 MLSRVEPSDRYPQCLCLSPTYELALQTGKVIEQMGKFYPELKLAYAVRGNKLERG-QKISE-QIVIGTPGTVLDWCsKLK 78
Cdd:cd17943    48 ALESLDLERRHPQVLILAPTREIAVQIHDVFKKIGKKLEGLKCEVFIGGTPVKEDkKKLKGcHIAVGTPGRIKQLI-ELG 126
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1001624560  79 FIDPKKIKVFVLDEAD-VMIATqgHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 145
Cdd:cd17943   127 ALNVSHVRLFVLDEADkLMEGS--FQKDVNWIFSSLPKNKQVIAFSATYPKNLDNLLARYMRKPVLVR 192
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
1-141 7.52e-19

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: 82.98  E-value: 7.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560   1 MLSRVEPSDRYPQCLCLSPTYELALQTGKVIEQMGKFYPELKLAYAVRGN----KLERGQKiSEQIVIGTPGTVLDWCSK 76
Cdd:cd17962    48 VIIRCLTEHRNPSALILTPTRELAVQIEDQAKELMKGLPPMKTALLVGGLplppQLYRLQQ-GVKVIIATPGRLLDILKQ 126
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1001624560  77 lKFIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 141
Cdd:cd17962   127 -SSVELDNIKIVVVDEADTML-KMGFQQQVLDILENISHDHQTILVSATIPRGIEQLAGQLLQNP 189
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
13-141 6.20e-18

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: 80.83  E-value: 6.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560  13 QCLCLSPTYELALQTGKVIEQMGKFY--PELKLAYAVRGNKLERGQKISEQ---IVIGTPGTVLDWCSKLKfIDPKKIKV 87
Cdd:cd17938    62 VALILEPSRELAEQTYNCIENFKKYLdnPKLRVALLIGGVKAREQLKRLESgvdIVVGTPGRLEDLIKTGK-LDLSSVRF 140
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1001624560  88 FVLDEADVMIaTQGHQDQSIRIQRMLP------RNCQMLLFSATFE-DSVWKFAQKVVPDP 141
Cdd:cd17938   141 FVLDEADRLL-SQGNLETINRIYNRIPkitsdgKRLQVIVCSATLHsFEVKKLADKIMHFP 200
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
10-134 2.44e-17

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: 78.84  E-value: 2.44e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560  10 RYPQCLCLSPTYELALQTGKVIEQMGKFYPeLKLAYAVRGNKL---ERGQKISEQIVIGTPGTVLDWCSKLKFIDPKKIK 86
Cdd:cd17947    60 AATRVLVLVPTRELAMQCFSVLQQLAQFTD-ITFALAVGGLSLkaqEAALRARPDIVIATPGRLIDHLRNSPSFDLDSIE 138
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1001624560  87 VFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFA 134
Cdd:cd17947   139 ILVLDEADRML-EEGFADELKEILRLCPRTRQTMLFSATMTDEVKDLA 185
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
1-144 3.88e-17

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: 78.78  E-value: 3.88e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560   1 MLSRVEPSDRYP-QCLCLSPTYELALQTGKVIEQMGKFYPELKLAYAVRGNK----LERGQKISEQIVIGTPG---TVLD 72
Cdd:cd17964    57 LLNTKPAGRRSGvSALIISPTRELALQIAAEAKKLLQGLRKLRVQSAVGGTSrraeLNRLRRGRPDILVATPGrliDHLE 136
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1001624560  73 WCSKLKFIdpKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNC----QMLLFSATFEDSVWKFAQKVV-PDPNVI 144
Cdd:cd17964   137 NPGVAKAF--TDLDYLVLDEADRLL-DMGFRPDLEQILRHLPEKNadprQTLLFSATVPDEVQQIARLTLkKDYKFI 210
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
2-141 4.42e-17

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: 78.54  E-value: 4.42e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560   2 LSRVEPSDRYPQCLCLSPTYELALQTGKVIEQMGKFYPELKLAY-----AVRGNKlERGQKISEQIVIGTPGTVLDwCSK 76
Cdd:cd17950    61 LQQLEPVDGQVSVLVICHTRELAFQISNEYERFSKYMPNVKTAVffggvPIKKDI-EVLKNKCPHIVVGTPGRILA-LVR 138
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1001624560  77 LKFIDPKKIKVFVLDEADVMIATQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 141
Cdd:cd17950   139 EKKLKLSHVKHFVLDECDKMLEQLDMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDP 203
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
14-144 1.77e-14

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: 70.78  E-value: 1.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560  14 CLCLSPTYELALQTGKVIEQMGKfYPELKLAYAVRGNKLERGQ-KISE-QIVIGTPGTVLDWCSKLKFIDPKKIKVFVLD 91
Cdd:cd17941    65 ALIISPTRELAMQIFEVLRKVGK-YHSFSAGLIIGGKDVKEEKeRINRmNILVCTPGRLLQHMDETPGFDTSNLQMLVLD 143
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1001624560  92 EADvMIATQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVI 144
Cdd:cd17941   144 EAD-RILDMGFKETLDAIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYI 195
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
14-141 6.02e-14

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: 69.56  E-value: 6.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560  14 CLCLSPTYELALQtgkVIEQM---GKFyPELKLAYAVRG-NKLERGQKISEQ--IVIGTPGTVLDW---CSKLKFiDPKK 84
Cdd:cd17955    70 ALVLTPTRELAYQ---IAEQFralGAP-LGLRCCVIVGGmDMVKQALELSKRphIVVATPGRLADHlrsSDDTTK-VLSR 144
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1001624560  85 IKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 141
Cdd:cd17955   145 VKFLVLDEADRLL-TGSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKP 200
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
14-141 1.09e-13

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: 68.88  E-value: 1.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560  14 CLCLSPTYELALQTGKVIEQMGKFyPELKLAYAVRG-----NKLERGQKisEQIVIGTPGTVLDWCSKLKFIDPKKIKVF 88
Cdd:cd17954    71 ALVLAPTRELAQQISEQFEALGSS-IGLKSAVLVGGmdmmaQAIALAKK--PHVIVATPGRLVDHLENTKGFSLKSLKFL 147
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1001624560  89 VLDEADVMIatqgHQDQSIRIQRML---PRNCQMLLFSATFEDSVWKFAQKVVPDP 141
Cdd:cd17954   148 VMDEADRLL----NMDFEPEIDKILkviPRERTTYLFSATMTTKVAKLQRASLKNP 199
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
1-130 4.43e-13

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: 66.83  E-value: 4.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560   1 MLSRVEPSDRYPQ--CLCLSPTYELALQTGKVIEQMGKFY-PELKLAYAVRGNKLERGQKI----SEQIVIGTPGTVLD- 72
Cdd:cd17960    51 ILLKRKANLKKGQvgALIISPTRELATQIYEVLQSFLEHHlPKLKCQLLIGGTNVEEDVKKfkrnGPNILVGTPGRLEEl 130
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1001624560  73 WCSKLKFIDPKKIKVFVLDEADVMIATqGHQDQSIRIQRMLPRNCQMLLFSATFEDSV 130
Cdd:cd17960   131 LSRKADKVKVKSLEVLVLDEADRLLDL-GFEADLNRILSKLPKQRRTGLFSATQTDAV 187
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
11-135 5.16e-13

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: 67.13  E-value: 5.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560  11 YPQCLCLSPTYELALQTgkvieqmgkfYPE-LKLAY-------AVRGNKLERGQKISEQ----IVIGTPGTVLDWCSKLK 78
Cdd:cd17967    78 YPSALILAPTRELAIQI----------YEEaRKFSYrsgvrsvVVYGGADVVHQQLQLLrgcdILVATPGRLVDFIERGR 147
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1001624560  79 fIDPKKIKVFVLDEADVMIaTQGHQDQsirIQRML-------PRNCQMLLFSATFEDSVWKFAQ 135
Cdd:cd17967   148 -ISLSSIKFLVLDEADRML-DMGFEPQ---IRKIVehpdmppKGERQTLMFSATFPREIQRLAA 206
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
8-126 1.81e-12

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: 65.72  E-value: 1.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560   8 SDRYPQCLCLSPTYELALQTGKVIEQMGKfYPELKLAYAVRGNKLERGQKISEQ---IVIGTPGTVLDW----CSKLKFI 80
Cdd:cd17946    65 KQKPLRALILTPTRELAVQVKDHLKAIAK-YTNIKIASIVGGLAVQKQERLLKKrpeIVVATPGRLWELiqegNEHLANL 143
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1001624560  81 dpKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNC-------QMLLFSATF 126
Cdd:cd17946   144 --KSLRFLVLDEADRML-EKGHFAELEKILELLNKDRagkkrkrQTFVFSATL 193
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
132-284 2.14e-12

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 67.83  E-value: 2.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560 132 KFAQKVVPDPNVIKLKREEETLDtikqyyvlcssrDE--KFQALCNL----YGAITIAQAMIFCHTRKTASWLAAELSKE 205
Cdd:COG1111   309 KASKRLVSDPRFRKAMRLAEEAD------------IEhpKLSKLREIlkeqLGTNPDSRIIVFTQYRDTAEMIVEFLSEP 376
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560 206 GHQVALLSGE--------MMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDlPVdkdgnPDNETYLHRIG 277
Cdd:COG1111   377 GIKAGRFVGQaskegdkgLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYE-PV-----PSEIRSIQRKG 450

                  ....*..
gi 1001624560 278 RTGRFGK 284
Cdd:COG1111   451 RTGRKRE 457
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
187-283 4.34e-12

C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 62.49  E-value: 4.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560 187 IFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEK--VLVTTNVCARGIDVEQVSVVINFDLPvdkd 264
Cdd:cd18793    32 IFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIrvFLLSTKAGGVGLNLTAANRVILYDPW---- 107
                          90
                  ....*....|....*....
gi 1001624560 265 GNPDNEtyLHRIGRTGRFG 283
Cdd:cd18793   108 WNPAVE--EQAIDRAHRIG 124
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
12-136 5.94e-12

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: 64.99  E-value: 5.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560  12 PQCLCLSPTYELALQTGKvieQMGKF-----------YPELKLAYAVRgnKLERGQkiseQIVIGTPGTVLDWCSKLKfI 80
Cdd:cd18052   121 PQALIVAPTRELANQIFL---EARKFsygtcirpvvvYGGVSVGHQIR--QIEKGC----HILVATPGRLLDFIGRGK-I 190
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1001624560  81 DPKKIKVFVLDEADVMIATQGHQDqsirIQRML-----PR--NCQMLLFSATFEDSVWKFAQK 136
Cdd:cd18052   191 SLSKLKYLILDEADRMLDMGFGPE----IRKLVsepgmPSkeDRQTLMFSATFPEEIQRLAAE 249
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
187-283 2.99e-11

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 64.09  E-value: 2.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560 187 IFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEK--VLVTTNVCARGIDVEQVSVVINFDLPVdkd 264
Cdd:COG0553   554 VFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEApvFLISLKAGGEGLNLTAADHVIHYDLWW--- 630
                          90
                  ....*....|....*....
gi 1001624560 265 gNPDNEtyLHRIGRTGRFG 283
Cdd:COG0553   631 -NPAVE--EQAIDRAHRIG 646
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
184-326 3.64e-11

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 63.89  E-value: 3.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560 184 QAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDlPVdk 263
Cdd:COG1061   307 KTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLR-PT-- 383
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1001624560 264 dGNPDneTYLHRIGR---TGRFGKRGLAVNMVDSKHSM--NILNRIQEHFNKKIERLDTDDLDEIEKI 326
Cdd:COG1061   384 -GSPR--EFIQRLGRglrPAPGKEDALVYDFVGNDVPVleELAKDLRDLAGYRVEFLDEEESEELALL 448
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
5-141 7.88e-11

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: 60.85  E-value: 7.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560   5 VEPSDRyPQCLCLSPTYELALQtgkVIEQMGKFYPELKL-AYAVRGnklerGQKISEQI---------VIGTPGTVLDW- 73
Cdd:cd17953    80 VKPGEG-PIGLIMAPTRELALQ---IYVECKKFSKALGLrVVCVYG-----GSGISEQIaelkrgaeiVVCTPGRMIDIl 150
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1001624560  74 -CSKLKFIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 141
Cdd:cd17953   151 tANNGRVTNLRRVTYVVLDEADRMF-DMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKP 218
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
12-144 1.43e-10

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: 59.74  E-value: 1.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560  12 PQCLCLSPTYELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKISE--QIVIGTPGTVLDWCsKLKFIDPKKIKVFV 89
Cdd:cd17952    64 PIAVIVAPTRELAQQIYLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEgaEIVVATPGRLIDMV-KKKATNLQRVTYLV 142
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1001624560  90 LDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVI 144
Cdd:cd17952   143 LDEADRMF-DMGFEYQVRSIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
14-125 2.22e-10

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: 59.30  E-value: 2.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560  14 CLCLSPTYELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKISE--QIVIGTPGTVLDWCSKLKFIDPKKIKVFVLD 91
Cdd:cd17942    65 VIIISPTRELALQIYGVAKELLKYHSQTFGIVIGGANRKAEAEKLGKgvNILVATPGRLLDHLQNTKGFLYKNLQCLIID 144
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1001624560  92 EADvMIATQGHQDQSIRIQRMLPRNCQMLLFSAT 125
Cdd:cd17942   145 EAD-RILEIGFEEEMRQIIKLLPKRRQTMLFSAT 177
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
12-144 3.24e-10

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: 58.89  E-value: 3.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560  12 PQCLCLSPTYELALQTGKVIEQMGKF-----YPELKLAYAVRGNKLERGQKISEQ---IVIGTPGTVLDWCSKlKFIDPK 83
Cdd:cd17951    67 PYGLIVCPSRELARQTHEVIEYYCKAlqeggYPQLRCLLCIGGMSVKEQLEVIRKgvhIVVATPGRLMDMLNK-KKINLD 145
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1001624560  84 KIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVI 144
Cdd:cd17951   146 ICRYLCLDEADRMI-DMGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
166-260 3.54e-10

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: 57.22  E-value: 3.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560 166 RDEKFQALCNL----YGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMV-------------EQRA--AVIE 226
Cdd:cd18802     5 VIPKLQKLIEIlreyFPKTPDFRGIIFVERRATAVVLSRLLKEHPSTLAFIRCGFLIgrgnssqrkrslmTQRKqkETLD 84
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1001624560 227 RFREGKEKVLVTTNVCARGIDVEQVSVVINFDLP 260
Cdd:cd18802    85 KFRDGELNLLIATSVLEEGIDVPACNLVIRFDLP 118
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
12-136 8.55e-10

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: 57.72  E-value: 8.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560  12 PQCLCLSPTYELALQTGKVIEQMGKFYPeLKLAYAVRGNKLE-RGQKISE--QIVIGTPGTVLDwCSKLKFIDPKKIKVF 88
Cdd:cd17945    67 PYALILAPTRELAQQIEEETQKFAKPLG-IRVVSIVGGHSIEeQAFSLRNgcEILIATPGRLLD-CLERRLLVLNQCTYV 144
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1001624560  89 VLDEADVMIaTQGHQDQSIRIQRMLP--------------------RNCQMLLFSATFEDSVWKFAQK 136
Cdd:cd17945   145 VLDEADRMI-DMGFEPQVTKILDAMPvsnkkpdteeaeklaasgkhRYRQTMMFTATMPPAVEKIAKG 211
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
187-284 1.37e-09

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: 55.68  E-value: 1.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560 187 IFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPvdkdgn 266
Cdd:cd18794    35 IYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLP------ 108
                          90
                  ....*....|....*...
gi 1001624560 267 PDNETYLHRIGRTGRFGK 284
Cdd:cd18794   109 KSMESYYQESGRAGRDGL 126
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
187-289 1.43e-09

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 59.00  E-value: 1.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560 187 IFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNvcA--RGIDVEQVSVVINFDLPvdkd 264
Cdd:COG0514   235 VYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATI--AfgMGIDKPDVRFVIHYDLP---- 308
                          90       100
                  ....*....|....*....|....*
gi 1001624560 265 GNPdnETYLHRIGRTGRFGKRGLAV 289
Cdd:COG0514   309 KSI--EAYYQEIGRAGRDGLPAEAL 331
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
4-141 1.80e-09

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: 56.61  E-value: 1.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560   4 RVEPSDRyPQCLCLSPTYELALQtgkVIEQMGKFYPELKL----AY--AVRGNK---LERGQkiseQIVIGTPGTVLDWC 74
Cdd:cd17966    57 PLERGDG-PIVLVLAPTRELAQQ---IQQEANKFGGSSRLrntcVYggAPKGPQirdLRRGV----EICIATPGRLIDFL 128
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1001624560  75 SKLKfIDPKKIKVFVLDEADVMIaTQGHQDQ------SIRIQRmlprncQMLLFSATFEDSVWKFAQKVVPDP 141
Cdd:cd17966   129 DQGK-TNLRRVTYLVLDEADRML-DMGFEPQirkivdQIRPDR------QTLMWSATWPKEVRRLAEDFLKDY 193
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
10-136 3.78e-09

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: 55.62  E-value: 3.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560  10 RYPQCLCLSPTYELALQTGKVIEQMGKfypelKLAYAVRGNKLERGQKISE-----QIVIGTPGTVLDWCSKLKfIDPKK 84
Cdd:cd17944    63 RAPKVLVLAPTRELANQVTKDFKDITR-----KLSVACFYGGTPYQQQIFAirngiDILVGTPGRIKDHLQNGR-LDLTK 136
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1001624560  85 IKVFVLDEADVMI----ATQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQK 136
Cdd:cd17944   137 LKHVVLDEVDQMLdmgfAEQVEEILSVSYKKDSEDNPQTLLFSATCPDWVYNVAKK 192
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
12-125 3.95e-09

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: 54.72  E-value: 3.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560  12 PQCLCLSPTYELALQTGKVIeqMGKFYPELKLAYAVRG-NKLERGQKI--SEQIVIGTPGTVLDWCSKLKFIDPKKIKVF 88
Cdd:cd00046    31 KKVLVLVPTKALALQTAERL--RELFGPGIRVAVLVGGsSAEEREKNKlgDADIIIATPDMLLNLLLREDRLFLKDLKLI 108
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1001624560  89 VLDEADVM-IATQGHQDQSIRIQRMLPRNCQMLLFSAT 125
Cdd:cd00046   109 IVDEAHALlIDSRGALILDLAVRKAGLKNAQVILLSAT 146
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
14-145 7.69e-09

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: 54.90  E-value: 7.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560  14 CLCLSPTYELALQTGKVIEQMGKFYPELKLAYAVRGNKlergqKISEQ--------IVIGTPGTVLDWCSKLKFIDPKKI 85
Cdd:cd17949    68 ALVLVPTRELALQIYEVLEKLLKPFHWIVPGYLIGGEK-----RKSEKarlrkgvnILIATPGRLLDHLKNTQSFDVSNL 142
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1001624560  86 KVFVLDEADVMIaTQGHQDQSIRIQRML-------------PRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 145
Cdd:cd17949   143 RWLVLDEADRLL-DMGFEKDITKILELLddkrskaggekskPSRRQTVLVSATLTDGVKRLAGLSLKDPVYID 214
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
12-141 1.67e-08

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: 53.62  E-value: 1.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560  12 PQCLCLSPTYELALQtgkVIEQMGKF-YPELKlAYAVRGNKlERGQKISEQ-----IVIGTPGTVLDwCSKLKFIDPKKI 85
Cdd:cd17958    65 PGVLVLTPTRELALQ---IEAECSKYsYKGLK-SVCVYGGG-NRNEQIEDLskgvdIIIATPGRLND-LQMNNVINLKSI 138
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1001624560  86 KVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 141
Cdd:cd17958   139 TYLVLDEADRML-DMGFEPQIRKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDP 193
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
12-141 2.34e-08

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: 53.36  E-value: 2.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560  12 PQCLCLSPTYELALQTGKVIEQMGKFYPE-----LKLAYAVRGNKLERGQKISeqIVIGTPGTVLDWCSKLKfIDPKKIK 86
Cdd:cd17957    61 LRALILAPTRELASQIYRELLKLSKGTGLrivllSKSLEAKAKDGPKSITKYD--ILVSTPLRLVFLLKQGP-IDLSSVE 137
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1001624560  87 VFVLDEADVMIATqGHQDQSIRIQRMLPRNC-QMLLFSATFEDSVWKFAQKVVPDP 141
Cdd:cd17957   138 YLVLDEADKLFEP-GFREQTDEILAACTNPNlQRSLFSATIPSEVEELARSVMKDP 192
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
10-126 2.35e-08

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: 53.89  E-value: 2.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560  10 RYPQCLCLSPTYELALQtgkVIEQMGKFypelklAY--AVRGNKLERGQKISEQI---------VIGTPGTVLDWCSKLK 78
Cdd:cd18051   104 QYPLALVLAPTRELASQ---IYDEARKF------AYrsRVRPCVVYGGADIGQQMrdlergchlLVATPGRLVDMLERGK 174
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1001624560  79 fIDPKKIKVFVLDEADVMIaTQGHQDQSIRI--QRMLPRNC--QMLLFSATF 126
Cdd:cd18051   175 -IGLDYCKYLVLDEADRML-DMGFEPQIRRIveQDTMPPTGerQTLMFSATF 224
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
12-140 5.51e-08

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: 52.70  E-value: 5.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560  12 PQCLCLSPTYELALQTGKVIEQMGK--------FYPELKLAYAVRgnKLERGQkiseQIVIGTPGTVLDW--CSKLKFid 81
Cdd:cd18049    98 PICLVLAPTRELAQQVQQVAAEYGRacrlkstcIYGGAPKGPQIR--DLERGV----EICIATPGRLIDFleAGKTNL-- 169
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1001624560  82 pKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPD 140
Cdd:cd18049   170 -RRCTYLVLDEADRML-DMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKD 226
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
12-140 6.87e-08

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: 52.71  E-value: 6.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560  12 PQCLCLSPTYELALQTGKVIEQMGKfYPELKLAYAVRG-------NKLERGQkiseQIVIGTPGTVLDWCSKLKfIDPKK 84
Cdd:cd18050   136 PICLVLAPTRELAQQVQQVADDYGK-SSRLKSTCIYGGapkgpqiRDLERGV----EICIATPGRLIDFLEAGK-TNLRR 209
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1001624560  85 IKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPD 140
Cdd:cd18050   210 CTYLVLDEADRML-DMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRD 264
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
185-281 7.68e-08

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


Pssm-ID: 350188 [Multi-domain]  Cd Length: 143  Bit Score: 50.82  E-value: 7.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560 185 AMIFCHTRKTASWLAAELSKEGHQV--ALLSGE--------MMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVV 254
Cdd:cd18801    33 VIIFSEFRDSAEEIVNFLSKIRPGIraTRFIGQasgksskgMSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLI 112
                          90       100
                  ....*....|....*....|....*..
gi 1001624560 255 INFdlpvdkDGNPDNETYLHRIGRTGR 281
Cdd:cd18801   113 ICY------DASPSPIRMIQRMGRTGR 133
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
183-289 9.53e-08

ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];


Pssm-ID: 440818 [Multi-domain]  Cd Length: 758  Bit Score: 53.30  E-value: 9.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560 183 AQAMIFCHTRK----TASWLAAELSKE--GHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVIN 256
Cdd:COG1205   289 LRTLVFTRSRRgaelLARYARRALREPdlADRVAAYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVL 368
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1001624560 257 fdlpvdkDGNPDNET-YLHRIGRTGRFGKRGLAV 289
Cdd:COG1205   369 -------AGYPGTRAsFWQQAGRAGRRGQDSLVV 395
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
172-289 3.07e-07

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: 49.18  E-value: 3.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560 172 ALCNLYGAITIAqamiFCHTRKTA----SWLAAELSKEGHQVALLS---GEMMVEQRAAVIERFREGKEKVLVTTNVCAR 244
Cdd:cd18797    29 ADLVRAGVKTIV----FCRSRKLAelllRYLKARLVEEGPLASKVAsyrAGYLAEDRREIEAELFNGELLGVVATNALEL 104
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1001624560 245 GIDVEQVSVVINfdlpvdkDGNPDNET-YLHRIGRTGRFGKRGLAV 289
Cdd:cd18797   105 GIDIGGLDAVVL-------AGYPGSLAsLWQQAGRAGRRGKDSLVI 143
PRK13766 PRK13766
Hef nuclease; Provisional
132-281 1.19e-06

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 49.87  E-value: 1.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560 132 KFAQKVVPDPNVIKLKRE-----------EETLDTIKQyyVLCSSRDEKfqalcnlygaitiaqAMIFCHTRKTASWLAA 200
Cdd:PRK13766  321 KASKRLVEDPRFRKAVRKakeldiehpklEKLREIVKE--QLGKNPDSR---------------IIVFTQYRDTAEKIVD 383
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560 201 ELSKEGHQVALLSGE--------MMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVInFDLPVdkdgnPDNETY 272
Cdd:PRK13766  384 LLEKEGIKAVRFVGQaskdgdkgMSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVI-FYEPV-----PSEIRS 457

                  ....*....
gi 1001624560 273 LHRIGRTGR 281
Cdd:PRK13766  458 IQRKGRTGR 466
SF2_C_UvrB cd18790
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ...
191-311 1.36e-06

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: 47.63  E-value: 1.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560 191 TRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDlpVDKDGNPDNE 270
Cdd:cd18790    36 TKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILD--ADKEGFLRSE 113
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1001624560 271 TYL-HRIGRTGRfGKRGLAV----NMVDS-KHSMNILNR---IQEHFNKK 311
Cdd:cd18790   114 TSLiQTIGRAAR-NVNGKVIlyadKITDSmQKAIEETERrreIQMEYNEE 162
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
234-286 3.11e-06

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: 44.62  E-value: 3.11e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1001624560 234 KVLVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRIGRTGRFGKRG 286
Cdd:cd18785    24 EILVATNVLGEGIDVPSLDTVIFFDPPSSA------ASYIQRVGRAGRGGKDE 70
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
186-283 4.99e-06

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 48.17  E-value: 4.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560 186 MIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKdg 265
Cdd:PRK11057  240 IIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNI-- 317
                          90
                  ....*....|....*...
gi 1001624560 266 npdnETYLHRIGRTGRFG 283
Cdd:PRK11057  318 ----ESYYQETGRAGRDG 331
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
2-125 8.27e-06

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: 46.09  E-value: 8.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560   2 LSRVEPSDRypqCLCLSPTYELALQTGKVIEQMGKFYPeLKLAyAVRGNK-----------LERGQKISE-QIVIGTPGT 69
Cdd:cd17956    62 SKRVVPRLR---ALIVVPTKELVQQVYKVFESLCKGTG-LKVV-SLSGQKsfkkeqklllvDTSGRYLSRvDILVATPGR 136
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1001624560  70 VLDWCSKLKFIDPKKIKVFVLDEAD-------------VMIATQGHQDQ------SIRIQRMLPRNCQMLLFSAT 125
Cdd:cd17956   137 LVDHLNSTPGFTLKHLRFLVIDEADrllnqsfqdwletVMKALGRPTAPdlgsfgDANLLERSVRPLQKLLFSAT 211
PRK10917 PRK10917
ATP-dependent DNA helicase RecG; Provisional
193-255 1.74e-05

ATP-dependent DNA helicase RecG; Provisional


Pssm-ID: 236794 [Multi-domain]  Cd Length: 681  Bit Score: 46.30  E-value: 1.74e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1001624560 193 KTASWLAAELSKE--GHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSV-VI 255
Cdd:PRK10917  490 QSAEETYEELQEAfpELRVGLLHGRMKPAEKDAVMAAFKAGEIDILVATTVIEVGVDVPNATVmVI 555
SF2_C_Ski2 cd18795
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ...
184-293 1.79e-05

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: 44.08  E-value: 1.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560 184 QAMIFCHTRKTASWLAAELSKeghqVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDK 263
Cdd:cd18795    45 PVLVFCSSRKECEKTAKDLAG----IAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYDG 120
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1001624560 264 DGN---PDNEtYLHRIGRTGR--FGKRGLAVNMVD 293
Cdd:cd18795   121 KGYrelSPLE-YLQMIGRAGRpgFDTRGEAIIMTK 154
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
209-299 1.81e-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: 44.18  E-value: 1.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560 209 VALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDlpVDKDGNPDnetyLHRI-GRTGRFGKRGL 287
Cdd:cd18792    63 VALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIED--ADRFGLSQ----LHQLrGRVGRGKHQSY 136
                          90
                  ....*....|..
gi 1001624560 288 AVNMVDSKHSMN 299
Cdd:cd18792   137 CYLLYPDPKKLT 148
SF2_C_reverse_gyrase cd18798
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ...
198-325 1.83e-05

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: 44.60  E-value: 1.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560 198 LAAELSKEGHQVALLSgemmvEQRAAVIERFREGKEKVLVTT----NVCARGIDV-EQVSVVINFDLPVdkdgnpdnETY 272
Cdd:cd18798    43 LKEFLERHGIKAELAL-----SSTEKNLEKFEEGEIDVLIGVasyyGVLVRGIDLpERIKYAIFYGVPV--------TTY 109
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1001624560 273 LHRIGRTGRF--GK--RGLAVNMVDSKHSMNILNRIQEHF--NKKIERLDTDDLDEIEK 325
Cdd:cd18798   110 IQASGRTSRLyaGGltKGLSVVLVDDPELFEALKKRLKLIldEFIFKELEEVDLEELLS 168
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
209-305 5.14e-05

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


Pssm-ID: 350198 [Multi-domain]  Cd Length: 159  Bit Score: 43.10  E-value: 5.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560 209 VALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDlpVDKDGnpdnETYLHRI-GRTGRFGKRGL 287
Cdd:cd18811    64 VGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIED--AERFG----LSQLHQLrGRVGRGDHQSY 137
                          90
                  ....*....|....*...
gi 1001624560 288 AVNMVDSKHSMNILNRIQ 305
Cdd:cd18811   138 CLLVYKDPLTETAKQRLR 155
ComFA COG4098
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, ...
183-255 7.72e-05

Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, recombination and repair];


Pssm-ID: 443274 [Multi-domain]  Cd Length: 451  Bit Score: 44.09  E-value: 7.72e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1001624560 183 AQAMIFCHTRKTASWLAAELSKEGHQVALLSgemmV----EQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVI 255
Cdd:COG4098   320 RQLLIFVPTIELLEQLVALLQKLFPEERIAG----VhaedPERKEKVQAFRDGEIPILVTTTILERGVTFPNVDVAV 392
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
187-281 1.62e-04

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


Pssm-ID: 350183 [Multi-domain]  Cd Length: 150  Bit Score: 41.48  E-value: 1.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560 187 IFCHTRKTASWLAAEL------SKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFdlp 260
Cdd:cd18796    43 VFTNTRSQAERLAQRLrelcpdRVPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQI--- 119
                          90       100
                  ....*....|....*....|..
gi 1001624560 261 vdkdGNPDNET-YLHRIGRTGR 281
Cdd:cd18796   120 ----GSPKSVArLLQRLGRSGH 137
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
12-139 2.20e-04

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: 41.97  E-value: 2.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560  12 PQCLCLSPTYELALQTGKVIEQMGKFYPeLKlAYAVRGNKLERGQKISEQ----IVIGTPGTVldwcSKL---KFIDPKK 84
Cdd:cd17948    66 PRGLVITPSRELAEQIGSVAQSLTEGLG-LK-VKVITGGRTKRQIRNPHFeevdILVATPGAL----SKLltsRIYSLEQ 139
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1001624560  85 IKVFVLDEADVMI-------------ATQGHQDQSIRIQRmLPRNCQMLLFSATFEDSVWKFAQKVVP 139
Cdd:cd17948   140 LRHLVLDEADTLLddsfneklshflrRFPLASRRSENTDG-LDPGTQLVLVSATMPSGVGEVLSKVID 206
PLN03137 PLN03137
ATP-dependent DNA helicase; Q4-like; Provisional
186-289 2.26e-04

ATP-dependent DNA helicase; Q4-like; Provisional


Pssm-ID: 215597 [Multi-domain]  Cd Length: 1195  Bit Score: 42.96  E-value: 2.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560  186 MIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKDG 265
Cdd:PLN03137   684 IIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEG 763
                           90       100
                   ....*....|....*....|....
gi 1001624560  266 npdnetYLHRIGRTGRFGKRGLAV 289
Cdd:PLN03137   764 ------YHQECGRAGRDGQRSSCV 781
SF2_C_TRCF cd18810
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ...
209-299 6.99e-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: 39.63  E-value: 6.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560 209 VALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDlpVDKDGNPDnetyLHRI-GRTGRFGKRGL 287
Cdd:cd18810    54 IAIAHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIIER--ADKFGLAQ----LYQLrGRVGRSKERAY 127
                          90
                  ....*....|..
gi 1001624560 288 AVNMVDSKHSMN 299
Cdd:cd18810   128 AYFLYPDQKKLT 139
RecG COG1200
RecG-like helicase [Replication, recombination and repair];
193-248 1.14e-03

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


Pssm-ID: 440813 [Multi-domain]  Cd Length: 684  Bit Score: 40.80  E-value: 1.14e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1001624560 193 KTASWLAAELSKE--GHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDV 248
Cdd:COG1200   488 QAAEETYEELREAfpGLRVGLLHGRMKPAEKDAVMAAFKAGEIDVLVATTVIEVGVDV 545
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
87-285 1.58e-03

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: 39.72  E-value: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560  87 VFVLDEADVMIA-TQGHQDQSIRIQRmlPRNCQMLLFSATFEDSVWKFAQKVVPDpnviklkREEETLDTI---KQYYVL 162
Cdd:cd09639   126 LLIFDEVHFYDEyTLALILAVLEVLK--DNDVPILLMSATLPKFLKEYAEKIGYV-------EENEPLDLKpneRAPFIK 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624560 163 CSSRD-EKFQALCNLYGAI-TIAQAMIFCHTRKTASWLAAELSKEGHQ--VALLSGEMM----VEQRAAVIERFREGKEK 234
Cdd:cd09639   197 IESDKvGEISSLERLLEFIkKGGSVAIIVNTVDRAQEFYQQLKEKGPEeeIMLIHSRFTekdrAKKEAELLLEFKKSEKF 276
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1001624560 235 VLVTTNVCargidveQVSVVINFDLPVDKDGNPDneTYLHRIGRTGRFGKR 285
Cdd:cd09639   277 VIVATQVI-------EASLDISVDVMITELAPID--SLIQRLGRLHRYGEK 318
 
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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