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Conserved domains on  [gi|1937893951|ref|NP_001005895|]
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ATP-dependent RNA helicase DDX19B [Rattus norvegicus]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 13209184)

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

CATH:  3.40.50.300
EC:  3.6.4.-
Gene Ontology:  GO:0016887|GO:0003676|GO:0004386|GO:0005524
PubMed:  20206133|20225155

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DEAD-like_helicase_N super family cl28899
N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase ...
 75-303 9.15e-144

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


The actual alignment was detected with superfamily member cd18048:

Pssm-ID: 475120 [Multi-domain]  Cd Length: 229  Bit Score: 410.95  E-value: 9.15e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951  75 NQVEVLQRDPSSPLYSVKSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEPPQNLIAQSQSGTGKTAAFVLAMLS 154
Cdd:cd18048     1 HRVEVLQRDPTSPLFSVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADPPQNLIAQSQSGTGKTAAFVLAMLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 155 QVEPANNHPQCLCLSPTYELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKVGEQIVIGTPGTVLDWCSKMKFIDPK 234
Cdd:cd18048    81 RVDALKLYPQCLCLSPTFELALQTGKVVEEMGKFCVGIQVIYAIRGNRPGKGTDIEAQIVIGTPGTVLDWCFKLRLIDVT 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937893951 235 KIKVFVLDEADVMIATQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNIIKLKREEET 303
Cdd:cd18048   161 NISVFVLDEADVMINVQGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 307-443 6.51e-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: 171.92  E-value: 6.51e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 307 IKQYYVLCNNREEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKV 386
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1937893951 387 LVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAVNMV 443
Cdd:cd18787    81 LVATDVAARGLDIPGVDHVINYDLPRDA------EDYVHRIGRTGRAGRKGTAITFV 131
 
Name Accession Description Interval E-value
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
 75-303 9.15e-144

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: 410.95  E-value: 9.15e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951  75 NQVEVLQRDPSSPLYSVKSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEPPQNLIAQSQSGTGKTAAFVLAMLS 154
Cdd:cd18048     1 HRVEVLQRDPTSPLFSVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADPPQNLIAQSQSGTGKTAAFVLAMLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 155 QVEPANNHPQCLCLSPTYELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKVGEQIVIGTPGTVLDWCSKMKFIDPK 234
Cdd:cd18048    81 RVDALKLYPQCLCLSPTFELALQTGKVVEEMGKFCVGIQVIYAIRGNRPGKGTDIEAQIVIGTPGTVLDWCFKLRLIDVT 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937893951 235 KIKVFVLDEADVMIATQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNIIKLKREEET 303
Cdd:cd18048   161 NISVFVLDEADVMINVQGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
93-476 5.72e-123

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 365.24  E-value: 5.72e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951  93 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEP-ANNHPQCLCLSPT 171
Cdd:COG0513     3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAG--RDVLGQAQTGTGKTAAFLLPLLQRLDPsRPRAPQALILAPT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 172 YELALQTGKVIEQMGKFYPeLKLAYAVRG-------NKLERGQkvgeQIVIGTPGTVLDWCSKmKFIDPKKIKVFVLDEA 244
Cdd:COG0513    81 RELALQVAEELRKLAKYLG-LRVATVYGGvsigrqiRALKRGV----DIVVATPGRLLDLIER-GALDLSGVETLVLDEA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 245 DVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNIIKLKREEETLDTIKQYYVLCNNREeKFQAL 324
Cdd:COG0513   155 DRML-DMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRD-KLELL 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 325 CNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSV 404
Cdd:COG0513   233 RRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSH 312

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937893951 405 VINFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAVNMVdSKHSMNILNRIQEHFNKKIERLDTDDLDEIEK 476
Cdd:COG0513   313 VINYDLPEDP------EDYVHRIGRTGRAGAEGTAISLV-TPDERRLLRAIEKLIGQKIEEEELPGFEPVEE 377
PTZ00424 PTZ00424
helicase 45; Provisional
 91-469 1.98e-98

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 301.75  E-value: 1.98e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951  91 VKSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANNHPQCLCLSP 170
Cdd:PTZ00424   27 VDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDG--YDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILAP 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 171 TYELALQTGKVIEQMGKfYPELKLAYAVRG-------NKLergqKVGEQIVIGTPGTVLDWCSKmKFIDPKKIKVFVLDE 243
Cdd:PTZ00424  105 TRELAQQIQKVVLALGD-YLKVRCHACVGGtvvrddiNKL----KAGVHMVVGTPGRVYDMIDK-RHLRVDDLKLFILDE 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 244 ADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNIIKLKREEETLDTIKQYYVLCNNREEKFQA 323
Cdd:PTZ00424  179 ADEML-SRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDT 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 324 LCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVS 403
Cdd:PTZ00424  258 LCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVS 337

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937893951 404 VVINFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAVNMVDSKhSMNILNRIQEHFNKKIERLDTD 469
Cdd:PTZ00424  338 LVINYDLPASP------ENYIHRIGRSGRFGRKGVAINFVTPD-DIEQLKEIERHYNTQIEEMPME 396
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 307-443 6.51e-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: 171.92  E-value: 6.51e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 307 IKQYYVLCNNREEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKV 386
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1937893951 387 LVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAVNMV 443
Cdd:cd18787    81 LVATDVAARGLDIPGVDHVINYDLPRDA------EDYVHRIGRTGRAGRKGTAITFV 131
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 116-281 3.29e-40

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: 142.00  E-value: 3.29e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 116 SKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANNHPQCLCLSPTYELALQTGKVIEQMGKFYpELKLA 195
Cdd:pfam00270   1 TPIQAEAIPAILEG--RDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGL-GLKVA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 196 YAVRGN--KLERGQKVGEQIVIGTPGTVLDWCSKMKFIdpKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLF 273
Cdd:pfam00270  78 SLLGGDsrKEQLEKLKGPDILVGTPGRLLDLLQERKLL--KNLKLLVLDEAHRLL-DMGFGPDLEEILRRLPKKRQILLL 154


                  ....*...
gi 1937893951 274 SATFEDSV 281
Cdd:pfam00270 155 SATLPRNL 162
DEXDc smart00487
DEAD-like helicases superfamily;
107-310 3.41e-36

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 132.62  E-value: 3.41e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951  107 VYAMGFNRPSKIQENALPLMLAEPpQNLIAQSQSGTGKTAAFVLAMLSQVEPaNNHPQCLCLSPTYELALQTGKVIEQMG 186
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGL-RDVILAAPTGSGKTLAALLPALEALKR-GKGGRVLVLVPTRELAEQWAEELKKLG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951  187 KFYPELKLAYAVRGNKLERGQKVGE---QIVIGTPGTVLDwCSKMKFIDPKKIKVFVLDEADVMIAtQGHQDQSIRIQRM 263
Cdd:smart00487  79 PSLGLKVVGLYGGDSKREQLRKLESgktDILVTTPGRLLD-LLENDKLSLSNVDLVILDEAHRLLD-GGFGDQLEKLLKL 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1937893951  264 LPRNCQMLLFSATFEDSVWKFAQKVVPDPniIKLKREEETLDTIKQY 310
Cdd:smart00487 157 LPKNVQLLLLSATPPEEIENLLELFLNDP--VFIDVGFTPLEPIEQF 201
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 319-434 5.92e-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: 118.08  E-value: 5.92e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 319 EKFQALCNLYGAITIAQAMIFCHTRKTA--SWLaaeLSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARG 396
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLeaELL---LEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERG 77

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1937893951 397 IDVEQVSVVINFDLPvdkdGNPdnETYLHRIGRTGRFG 434
Cdd:pfam00271  78 LDLPDVDLVINYDLP----WNP--ASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
348-434 8.35e-27

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 103.06  E-value: 8.35e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951  348 WLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRI 427
Cdd:smart00490   2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSP------ASYIQRI 75


                   ....*..
gi 1937893951  428 GRTGRFG 434
Cdd:smart00490  76 GRAGRAG 82
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
333-435 3.53e-12

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 68.60  E-value: 3.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 333 IAQAMIFCHTRKTASWLAAELSKEGHQVALLSGE--------MMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSV 404
Cdd:COG1111   353 DSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGQaskegdkgLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDL 432

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1937893951 405 VINFDlPVdkdgnPDNETYLHRIGRTGRFGK 435
Cdd:COG1111   433 VIFYE-PV-----PSEIRSIQRKGRTGRKRE 457
PRK13766 PRK13766
Hef nuclease; Provisional
 283-432 2.84e-06

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 49.87  E-value: 2.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 283 KFAQKVVPDPNIIKLKRE-----------EETLDTIKQyyVLCNNREEKfqalcnlygaitiaqAMIFCHTRKTASWLAA 351
Cdd:PRK13766  321 KASKRLVEDPRFRKAVRKakeldiehpklEKLREIVKE--QLGKNPDSR---------------IIVFTQYRDTAEKIVD 383

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 352 ELSKEGHQVALLSGE--------MMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVInFDLPVdkdgnPDNETY 423
Cdd:PRK13766  384 LLEKEGIKAVRFVGQaskdgdkgMSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVI-FYEPV-----PSEIRS 457


                  ....*....
gi 1937893951 424 LHRIGRTGR 432
Cdd:PRK13766  458 IQRKGRTGR 466
 
Name Accession Description Interval E-value
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
 75-303 9.15e-144

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: 410.95  E-value: 9.15e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951  75 NQVEVLQRDPSSPLYSVKSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEPPQNLIAQSQSGTGKTAAFVLAMLS 154
Cdd:cd18048     1 HRVEVLQRDPTSPLFSVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADPPQNLIAQSQSGTGKTAAFVLAMLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 155 QVEPANNHPQCLCLSPTYELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKVGEQIVIGTPGTVLDWCSKMKFIDPK 234
Cdd:cd18048    81 RVDALKLYPQCLCLSPTFELALQTGKVVEEMGKFCVGIQVIYAIRGNRPGKGTDIEAQIVIGTPGTVLDWCFKLRLIDVT 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937893951 235 KIKVFVLDEADVMIATQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNIIKLKREEET 303
Cdd:cd18048   161 NISVFVLDEADVMINVQGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
 92-296 1.05e-132

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: 381.76  E-value: 1.05e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951  92 KSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEPPQNLIAQSQSGTGKTAAFVLAMLSQVEPANNHPQCLCLSPT 171
Cdd:cd18047     1 KSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEPPQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 172 YELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKVGEQIVIGTPGTVLDWCSKMKFIDPKKIKVFVLDEADVMIATQ 251
Cdd:cd18047    81 YELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKISEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIATQ 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1937893951 252 GHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNIIK 296
Cdd:cd18047   161 GHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 205
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
 99-296 3.08e-126

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: 364.97  E-value: 3.08e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951  99 LKPQLLQGVYAMGFNRPSKIQENALPLMLAEPPQNLIAQSQSGTGKTAAFVLAMLSQVEPANNHPQCLCLSPTYELALQT 178
Cdd:cd17963     1 LKPELLKGLYAMGFNKPSKIQETALPLILSDPPENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 179 GKVIEQMGKFyPELKLAYAVRGNKLERGQKVGEQIVIGTPGTVLDWCSKmKFIDPKKIKVFVLDEADVMIATQGHQDQSI 258
Cdd:cd17963    81 GEVVEKMGKF-TGVKVALAVPGNDVPRGKKITAQIVIGTPGTVLDWLKK-RQLDLKKIKILVLDEADVMLDTQGHGDQSI 158

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1937893951 259 RIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNIIK 296
Cdd:cd17963   159 RIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTIK 196
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
93-476 5.72e-123

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 365.24  E-value: 5.72e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951  93 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEP-ANNHPQCLCLSPT 171
Cdd:COG0513     3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAG--RDVLGQAQTGTGKTAAFLLPLLQRLDPsRPRAPQALILAPT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 172 YELALQTGKVIEQMGKFYPeLKLAYAVRG-------NKLERGQkvgeQIVIGTPGTVLDWCSKmKFIDPKKIKVFVLDEA 244
Cdd:COG0513    81 RELALQVAEELRKLAKYLG-LRVATVYGGvsigrqiRALKRGV----DIVVATPGRLLDLIER-GALDLSGVETLVLDEA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 245 DVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNIIKLKREEETLDTIKQYYVLCNNREeKFQAL 324
Cdd:COG0513   155 DRML-DMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRD-KLELL 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 325 CNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSV 404
Cdd:COG0513   233 RRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSH 312

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937893951 405 VINFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAVNMVdSKHSMNILNRIQEHFNKKIERLDTDDLDEIEK 476
Cdd:COG0513   313 VINYDLPEDP------EDYVHRIGRTGRAGAEGTAISLV-TPDERRLLRAIEKLIGQKIEEEELPGFEPVEE 377
PTZ00424 PTZ00424
helicase 45; Provisional
 91-469 1.98e-98

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 301.75  E-value: 1.98e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951  91 VKSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANNHPQCLCLSP 170
Cdd:PTZ00424   27 VDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDG--YDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILAP 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 171 TYELALQTGKVIEQMGKfYPELKLAYAVRG-------NKLergqKVGEQIVIGTPGTVLDWCSKmKFIDPKKIKVFVLDE 243
Cdd:PTZ00424  105 TRELAQQIQKVVLALGD-YLKVRCHACVGGtvvrddiNKL----KAGVHMVVGTPGRVYDMIDK-RHLRVDDLKLFILDE 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 244 ADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNIIKLKREEETLDTIKQYYVLCNNREEKFQA 323
Cdd:PTZ00424  179 ADEML-SRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDT 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 324 LCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVS 403
Cdd:PTZ00424  258 LCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVS 337

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937893951 404 VVINFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAVNMVDSKhSMNILNRIQEHFNKKIERLDTD 469
Cdd:PTZ00424  338 LVINYDLPASP------ENYIHRIGRSGRFGRKGVAINFVTPD-DIEQLKEIERHYNTQIEEMPME 396
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
 94-471 2.69e-73

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 237.92  E-value: 2.69e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951  94 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLamlsqvePANNH----------- 162
Cdd:PRK11192    3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDG--RDVLGSAPTGTGKTAAFLL-------PALQHlldfprrksgp 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 163 PQCLCLSPTYELALQtgkVIEQMGKFYPELKL---------AYAVRGNKLERGQkvgeQIVIGTPGTVLDWCSKMKFiDP 233
Cdd:PRK11192   74 PRILILTPTRELAMQ---VADQARELAKHTHLdiatitggvAYMNHAEVFSENQ----DIVVATPGRLLQYIKEENF-DC 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 234 KKIKVFVLDEADVMIATQGHQD-QSIRIQrmlPRNC-QMLLFSATFE-DSVWKFAQKVVPDPNIIKL---KREEETldtI 307
Cdd:PRK11192  146 RAVETLILDEADRMLDMGFAQDiETIAAE---TRWRkQTLLFSATLEgDAVQDFAERLLNDPVEVEAepsRRERKK---I 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 308 KQYYVLCNNREEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVL 387
Cdd:PRK11192  220 HQWYYRADDLEHKTALLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVL 299

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 388 VTTNVCARGIDVEQVSVVINFDLPVDKDgnpdneTYLHRIGRTGRFGKRGLAVNMVDSkHSMNILNRIQEHFNKKIERLD 467
Cdd:PRK11192  300 VATDVAARGIDIDDVSHVINFDMPRSAD------TYLHRIGRTGRAGRKGTAISLVEA-HDHLLLGKIERYIEEPLKARV 372


                  ....
gi 1937893951 468 TDDL 471
Cdd:PRK11192  373 IDEL 376
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
 90-472 1.72e-72

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 236.24  E-value: 1.72e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951  90 SVKSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANNHPQCLCLS 169
Cdd:PRK11776    2 SMTAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAG--KDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLC 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 170 PTYELALQTGKVIEQMGKFYPELKLAyavrgnKLERGQKVGEQ---------IVIGTPGTVLDWCSKmKFIDPKKIKVFV 240
Cdd:PRK11776   80 PTRELADQVAKEIRRLARFIPNIKVL------TLCGGVPMGPQidslehgahIIVGTPGRILDHLRK-GTLDLDALNTLV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 241 LDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNIIKLKrEEETLDTIKQYYVLCNNrEEK 320
Cdd:PRK11776  153 LDEADRML-DMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVE-STHDLPAIEQRFYEVSP-DER 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 321 FQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMmvEQ--RAAVIERFREGKEKVLVTTNVCARGID 398
Cdd:PRK11776  230 LPALQRLLLHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDL--EQrdRDQVLVRFANRSCSVLVATDVAARGLD 307

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937893951 399 VEQVSVVINFDLPvdkdgnPDNETYLHRIGRTGRFGKRGLAVNMVdSKHSMNILNRIQEHFNKKIERLDTDDLD 472
Cdd:PRK11776  308 IKALEAVINYELA------RDPEVHVHRIGRTGRAGSKGLALSLV-APEEMQRANAIEDYLGRKLNWEPLPSLS 374
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
 94-464 3.93e-60

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 204.38  E-value: 3.93e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951  94 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV-------EPANNHPQCL 166
Cdd:PRK01297   89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAG--HDAIGRAQTGTGKTAAFLISIINQLlqtpppkERYMGEPRAL 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 167 CLSPTYELALQTGKVIEQMGKfYPELKLAYAVRGNKLERGQKVGEQ----IVIGTPGTVLDWcSKMKFIDPKKIKVFVLD 242
Cdd:PRK01297  167 IIAPTRELVVQIAKDAAALTK-YTGLNVMTFVGGMDFDKQLKQLEArfcdILVATPGRLLDF-NQRGEVHLDMVEVMVLD 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 243 EADVMIaTQGHQDQSIRIQRMLPRNC--QMLLFSATFEDSVWKFAQKVVPDPNIIKLKREEETLDTIKQYyVLCNNREEK 320
Cdd:PRK01297  245 EADRML-DMGFIPQVRQIIRQTPRKEerQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQH-VYAVAGSDK 322

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 321 FQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVE 400
Cdd:PRK01297  323 YKLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHID 402

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937893951 401 QVSVVINFDLPVDkdgnPDNetYLHRIGRTGRFGKRGLAVNMVDSKHSMNiLNRIQEHFNKKIE 464
Cdd:PRK01297  403 GISHVINFTLPED----PDD--YVHRIGRTGRAGASGVSISFAGEDDAFQ-LPEIEELLGRKIS 459
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
 93-446 6.53e-59

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 204.70  E-value: 6.53e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951  93 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANNHPQCLCLSPTY 172
Cdd:PRK11634    7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNG--RDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAPTR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 173 ELALQTGKVIEQMGKFYPELKLAYAVRGNKLE---RGQKVGEQIVIGTPGTVLDWCsKMKFIDPKKIKVFVLDEADVMIa 249
Cdd:PRK11634   85 ELAVQVAEAMTDFSKHMRGVNVVALYGGQRYDvqlRALRQGPQIVVGTPGRLLDHL-KRGTLDLSKLSGLVLDEADEML- 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 250 TQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNIIKLKREEETLDTIKQ-YYVLCNNReeKFQALCNLY 328
Cdd:PRK11634  163 RMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQsYWTVWGMR--KNEALVRFL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 329 GAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINF 408
Cdd:PRK11634  241 EAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNY 320

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1937893951 409 DLPVdkdgnpDNETYLHRIGRTGRFGKRGLAVNMVDSK 446
Cdd:PRK11634  321 DIPM------DSESYVHRIGRTGRAGRAGRALLFVENR 352
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
 92-463 1.34e-57

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 196.35  E-value: 1.34e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951  92 KSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLA----MLSQVEPAN---NHPQ 164
Cdd:PRK04837    8 QKFSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAG--RDVAGQAQTGTGKTMAFLTAtfhyLLSHPAPEDrkvNQPR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 165 CLCLSPTYELALQTGKVIEQMGKfYPELKLAYAVRGNKLERGQKVGEQ---IVIGTPGTVLDWcSKMKFIDPKKIKVFVL 241
Cdd:PRK04837   86 ALIMAPTRELAVQIHADAEPLAQ-ATGLKLGLAYGGDGYDKQLKVLESgvdILIGTTGRLIDY-AKQNHINLGAIQVVVL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 242 DEADVMIATQGHQDqsIR--IQRMLPRNCQM-LLFSATFEDSVWKFAQKVVPDPNIIKLKREEETLDTIKQYYVLCNNrE 318
Cdd:PRK04837  164 DEADRMFDLGFIKD--IRwlFRRMPPANQRLnMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEELFYPSN-E 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 319 EKFQALCNLYGAITIAQAMIFCHTR----KTASWLAAElskeGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCA 394
Cdd:PRK04837  241 EKMRLLQTLIEEEWPDRAIIFANTKhrceEIWGHLAAD----GHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAA 316

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937893951 395 RGIDVEQVSVVINFDLPvdkdgnPDNETYLHRIGRTGRFGKRGLAVNMVDSKHSMNiLNRIQEHFNKKI 463
Cdd:PRK04837  317 RGLHIPAVTHVFNYDLP------DDCEDYVHRIGRTGRAGASGHSISLACEEYALN-LPAIETYIGHSI 378
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
 87-463 1.37e-55

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 194.40  E-value: 1.37e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951  87 PLYSVkSFEELRLKPQLLQGVYAMGFNRPSKIQenALPLMLAEPPQNLIAQSQSGTGKTAAFVLA----MLSQVEPANNH 162
Cdd:PRK04537    5 PLTDL-TFSSFDLHPALLAGLESAGFTRCTPIQ--ALTLPVALPGGDVAGQAQTGTGKTLAFLVAvmnrLLSRPALADRK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 163 PQ---CLCLSPTYELALQTGKvieQMGKFYPELKLAYA-----VRGNKLERGQKVGEQIVIGTPGTVLDWCSKMKFIDPK 234
Cdd:PRK04537   82 PEdprALILAPTRELAIQIHK---DAVKFGADLGLRFAlvyggVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVVSLH 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 235 KIKVFVLDEADVMIATQGHQDqsIR-IQRMLPRNC--QMLLFSATFEDSVWKFAQKVVPDPNiiKLKREEETLDTIK-QY 310
Cdd:PRK04537  159 ACEICVLDEADRMFDLGFIKD--IRfLLRRMPERGtrQTLLFSATLSHRVLELAYEHMNEPE--KLVVETETITAARvRQ 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 311 YVLCNNREEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTT 390
Cdd:PRK04537  235 RIYFPADEEKQTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVAT 314

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937893951 391 NVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAVNMVDSKHSMNiLNRIQEHFNKKI 463
Cdd:PRK04537  315 DVAARGLHIDGVKYVYNYDLPFDA------EDYVHRIGRTARLGEEGDAISFACERYAMS-LPDIEAYIEQKI 380
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
 103-296 2.80e-53

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: 177.63  E-value: 2.80e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 103 LLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEP----ANNHPQCLCLSPTYELALQT 178
Cdd:cd00268     1 LLKALKKLGFEKPTPIQAQAIPLILSG--RDVIGQAQTGSGKTLAFLLPILEKLLPepkkKGRGPQALVLAPTRELAMQI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 179 GKVIEQMGKfYPELKlAYAVRG----NKLERGQKVGEQIVIGTPGTVLDWCsKMKFIDPKKIKVFVLDEADVMIaTQGHQ 254
Cdd:cd00268    79 AEVARKLGK-GTGLK-VAAIYGgapiKKQIEALKKGPDIVVGTPGRLLDLI-ERGKLDLSNVKYLVLDEADRML-DMGFE 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1937893951 255 DQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNIIK 296
Cdd:cd00268   155 EDVEKILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
 93-443 8.23e-53

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 184.63  E-value: 8.23e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951  93 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANNHPQ------CL 166
Cdd:PRK10590    2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEG--RDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKgrrpvrAL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 167 CLSPTYELALQTGKVIEQMGKFYPELKLAY--AVRGN----KLeRGqkvGEQIVIGTPGTVLDwCSKMKFIDPKKIKVFV 240
Cdd:PRK10590   80 ILTPTRELAAQIGENVRDYSKYLNIRSLVVfgGVSINpqmmKL-RG---GVDVLVATPGRLLD-LEHQNAVKLDQVEILV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 241 LDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNIIKLKREEETLDTIKQYyVLCNNREEK 320
Cdd:PRK10590  155 LDEADRML-DMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQH-VHFVDKKRK 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 321 FQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVE 400
Cdd:PRK10590  233 RELLSQMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIE 312

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1937893951 401 QVSVVINFDLP-VDKDgnpdnetYLHRIGRTGRFGKRGLAVNMV 443
Cdd:PRK10590  313 ELPHVVNYELPnVPED-------YVHRIGRTGRAAATGEALSLV 349
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 307-443 6.51e-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: 171.92  E-value: 6.51e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 307 IKQYYVLCNNREEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKV 386
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1937893951 387 LVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAVNMV 443
Cdd:cd18787    81 LVATDVAARGLDIPGVDHVINYDLPRDA------EDYVHRIGRTGRAGRKGTAITFV 131
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
 96-295 2.74e-50

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: 170.20  E-value: 2.74e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951  96 ELRLKPQLLQGVYAMGFNRPSKIQENA-LPLMLAEppqNLIAQSQSGTGKTAAFVLAMLSQVEPANNHPQCLCLSPTYEL 174
Cdd:cd17939     1 DMGLSEDLLRGIYAYGFEKPSAIQQRAiVPIIKGR---DVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTREL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 175 ALQTGKVIEQMGkFYPELKLAYAVRGNKLE---RGQKVGEQIVIGTPGTVLDWCSKmKFIDPKKIKVFVLDEADVMIaTQ 251
Cdd:cd17939    78 AQQIQKVVKALG-DYMGVKVHACIGGTSVRedrRKLQYGPHIVVGTPGRVFDMLQR-RSLRTDKIKMFVLDEADEML-SR 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1937893951 252 GHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNII 295
Cdd:cd17939   155 GFKDQIYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
 94-292 5.72e-48

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: 164.16  E-value: 5.72e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951  94 FEELRLKPQLLQGVYAMGFNRPSKIQENA-LPLMLAeppQNLIAQSQSGTGKTAAFVLAMLSQVEPANNHPQCLCLSPTY 172
Cdd:cd18046     1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAiMPCIKG---YDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 173 ELALQTGKVIEQMGkFYPELKLAYAVRGNKLE---RGQKVGEQIVIGTPGTVLDWCSKmKFIDPKKIKVFVLDEADVMIa 249
Cdd:cd18046    78 ELAQQIQKVVMALG-DYMGIKCHACIGGTSVRddaQKLQAGPHIVVGTPGRVFDMINR-RYLRTDYIKMFVLDEADEML- 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1937893951 250 TQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 292
Cdd:cd18046   155 SRGFKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDP 197
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
 94-295 1.13e-47

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: 163.24  E-value: 1.13e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951  94 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANNHPQCLCLSPTYE 173
Cdd:cd17940     1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSG--RDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 174 LALQTGKVIEQMGKFypeLKLAYAV-------RGNKLERGQKVgeQIVIGTPGTVLDwCSKMKFIDPKKIKVFVLDEADV 246
Cdd:cd17940    79 LALQTSQVCKELGKH---MGVKVMVttggtslRDDIMRLYQTV--HVLVGTPGRILD-LAKKGVADLSHCKTLVLDEADK 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1937893951 247 MIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNII 295
Cdd:cd17940   153 LL-SQDFQPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
PTZ00110 PTZ00110
helicase; Provisional
 91-439 3.79e-41

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 154.55  E-value: 3.79e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951  91 VKSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLamlsqvePANNH-------- 162
Cdd:PTZ00110  129 VVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSG--RDMIGIAETGSGKTLAFLL-------PAIVHinaqpllr 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 163 ----PQCLCLSPTYELALQtgkVIEQMGKFYPELKLAYAVR-GNKLERGQ----KVGEQIVIGTPGTVLDWCSKmKFIDP 233
Cdd:PTZ00110  200 ygdgPIVLVLAPTRELAEQ---IREQCNKFGASSKIRNTVAyGGVPKRGQiyalRRGVEILIACPGRLIDFLES-NVTNL 275

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 234 KKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNI------IKLKreeeTLDTI 307
Cdd:PTZ00110  276 RRVTYLVLDEADRML-DMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEEPVhvnvgsLDLT----ACHNI 350

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 308 KQYYVLCNNREEKFQaLCNLYGAITI--AQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEK 385
Cdd:PTZ00110  351 KQEVFVVEEHEKRGK-LKMLLQRIMRdgDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSP 429

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1937893951 386 VLVTTNVCARGIDVEQVSVVINFDLPvdkdgnPDNETYLHRIGRTGRFGKRGLA 439
Cdd:PTZ00110  430 IMIATDVASRGLDVKDVKYVINFDFP------NQIEDYVHRIGRTGRAGAKGAS 477
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
 94-295 4.56e-41

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: 145.69  E-value: 4.56e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951  94 FEELRLKPQLLQGVYAMGFNRPSKIQENAL-PLMLAeppQNLIAQSQSGTGKTAAFVLAMLSQVEPANNHPQCLCLSPTY 172
Cdd:cd18045     1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIkPIIKG---RDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 173 ELALQTGKVIEQMGKFYpELKLAYAVRGNKLERGQKV---GEQIVIGTPGTVLDWCSKmKFIDPKKIKVFVLDEADVMIa 249
Cdd:cd18045    78 ELAVQIQKVLLALGDYM-NVQCHACIGGTSVGDDIRKldyGQHIVSGTPGRVFDMIRR-RSLRTRHIKMLVLDEADEML- 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1937893951 250 TQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNII 295
Cdd:cd18045   155 NKGFKEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
 67-444 1.99e-40

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 152.25  E-value: 1.99e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951  67 RSNLVDNTNQVEVLQRDPSSPlysVKSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTA 146
Cdd:PLN00206   99 QAELLRRKLEIHVKGEAVPPP---ILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSG--RSLLVSADTGSGKTA 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 147 AFVLAMLS-------QVEPANNHPQCLCLSPTYELALQTGKVIEQMGKFYPeLKLAYAVRGN----KLERGQKvGEQIVI 215
Cdd:PLN00206  174 SFLVPIISrcctirsGHPSEQRNPLAMVLTPTRELCVQVEDQAKVLGKGLP-FKTALVVGGDampqQLYRIQQ-GVELIV 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 216 GTPGTVLDWCSKMKfIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNcQMLLFSATFEDSVWKFAQKVVPDPNII 295
Cdd:PLN00206  252 GTPGRLIDLLSKHD-IELDNVSVLVLDEVDCML-ERGFRDQVMQIFQALSQP-QVLLFSATVSPEVEKFASSLAKDIILI 328

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 296 KLKREEETLDTIKQYYVLCNNREEKFQalcnLYGAITIAQ-----AMIFCHTRKTASWLAAELSK-EGHQVALLSGEMMV 369
Cdd:PLN00206  329 SIGNPNRPNKAVKQLAIWVETKQKKQK----LFDILKSKQhfkppAVVFVSSRLGADLLANAITVvTGLKALSIHGEKSM 404

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937893951 370 EQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPvdkdgNPDNEtYLHRIGRTGRFGKRGLAVNMVD 444
Cdd:PLN00206  405 KERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMP-----NTIKE-YIHQIGRASRMGEKGTAIVFVN 473
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 116-281 3.29e-40

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: 142.00  E-value: 3.29e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 116 SKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANNHPQCLCLSPTYELALQTGKVIEQMGKFYpELKLA 195
Cdd:pfam00270   1 TPIQAEAIPAILEG--RDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGL-GLKVA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 196 YAVRGN--KLERGQKVGEQIVIGTPGTVLDWCSKMKFIdpKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLF 273
Cdd:pfam00270  78 SLLGGDsrKEQLEKLKGPDILVGTPGRLLDLLQERKLL--KNLKLLVLDEAHRLL-DMGFGPDLEEILRRLPKKRQILLL 154


                  ....*...
gi 1937893951 274 SATFEDSV 281
Cdd:pfam00270 155 SATLPRNL 162
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
 93-296 8.72e-38

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: 137.05  E-value: 8.72e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951  93 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAepPQNLIAQSQSGTGKTAAFVLAMLSQVEpaNNHPQ----CLCL 168
Cdd:cd17959     2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILD--GRDVVAMARTGSGKTAAFLIPMIEKLK--AHSPTvgarALIL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 169 SPTYELALQTGKVIEQMGKFyPELKLAYAVRGNKLErgqkvgEQ---------IVIGTPGTVLDWCSKMKFiDPKKIKVF 239
Cdd:cd17959    78 SPTRELALQTLKVTKELGKF-TDLRTALLVGGDSLE------EQfealasnpdIIIATPGRLLHLLVEMNL-KLSSVEYV 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1937893951 240 VLDEADVMIAtQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNIIK 296
Cdd:cd17959   150 VFDEADRLFE-MGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLIR 205
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
 103-296 1.74e-37

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: 135.85  E-value: 1.74e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 103 LLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANNHPQCLCLSPTYELALQTGKVI 182
Cdd:cd17943     1 VLEGLKAAGFQRPSPIQLAAIPLGLAG--HDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 183 EQMGKFYPELKLAYAVRG--NKLERGQKVGEQIVIGTPGTVLDWCsKMKFIDPKKIKVFVLDEAD-VMIATqgHQDQSIR 259
Cdd:cd17943    79 KKIGKKLEGLKCEVFIGGtpVKEDKKKLKGCHIAVGTPGRIKQLI-ELGALNVSHVRLFVLDEADkLMEGS--FQKDVNW 155

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1937893951 260 IQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNIIK 296
Cdd:cd17943   156 IFSSLPKNKQVIAFSATYPKNLDNLLARYMRKPVLVR 192
DEXDc smart00487
DEAD-like helicases superfamily;
107-310 3.41e-36

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 132.62  E-value: 3.41e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951  107 VYAMGFNRPSKIQENALPLMLAEPpQNLIAQSQSGTGKTAAFVLAMLSQVEPaNNHPQCLCLSPTYELALQTGKVIEQMG 186
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGL-RDVILAAPTGSGKTLAALLPALEALKR-GKGGRVLVLVPTRELAEQWAEELKKLG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951  187 KFYPELKLAYAVRGNKLERGQKVGE---QIVIGTPGTVLDwCSKMKFIDPKKIKVFVLDEADVMIAtQGHQDQSIRIQRM 263
Cdd:smart00487  79 PSLGLKVVGLYGGDSKREQLRKLESgktDILVTTPGRLLD-LLENDKLSLSNVDLVILDEAHRLLD-GGFGDQLEKLLKL 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1937893951  264 LPRNCQMLLFSATFEDSVWKFAQKVVPDPniIKLKREEETLDTIKQY 310
Cdd:smart00487 157 LPKNVQLLLLSATPPEEIENLLELFLNDP--VFIDVGFTPLEPIEQF 201
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
 93-292 2.03e-35

DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and is required for the export of mRNA out of the nucleus. DDX39B is an essential splicing factor required for association of U2 small nuclear ribonucleoprotein with pre-mRNA, and it also plays an important role in mRNA export from the nucleus to the cytoplasm. Diseases associated with DDX39A (also called UAP56-Related Helicase, 49 kDa) include gastrointestinal stromal tumor and inflammatory bowel disease 6, while diseases associated with DDX39B (also called 56 kDa U2AF65-Associated Protein) include Plasmodium vivax malaria. DDX39 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350708 [Multi-domain]  Cd Length: 208  Bit Score: 130.93  E-value: 2.03e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951  93 SFEELRLKPQLLQGVYAMGFNRPSKIQENALP-LMLAEppqNLIAQSQSGTGKTAAFVLAMLSQVEPANNHPQCLCLSPT 171
Cdd:cd17950     3 GFRDFLLKPELLRAIVDCGFEHPSEVQHECIPqAILGM---DVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 172 YELALQTGKVIEQMGKFYPELKLAY-----AVRGNKlERGQKVGEQIVIGTPGTVLDwCSKMKFIDPKKIKVFVLDEADV 246
Cdd:cd17950    80 RELAFQISNEYERFSKYMPNVKTAVffggvPIKKDI-EVLKNKCPHIVVGTPGRILA-LVREKKLKLSHVKHFVLDECDK 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1937893951 247 MIATQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 292
Cdd:cd17950   158 MLEQLDMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDP 203
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
 99-297 1.08e-34

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: 128.86  E-value: 1.08e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951  99 LKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAML------SQVEPANNHPQCLCLSPTY 172
Cdd:cd17961     1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEG--KDILARARTGSGKTAAYALPIIqkilkaKAESGEEQGTRALILVPTR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 173 ELALQTGKVIEQMGKFY-PELKLAyAVRGNKLERGQKV--GEQ--IVIGTPGTVLDWCSKMKFIDPKKIKVFVLDEADVM 247
Cdd:cd17961    79 ELAQQVSKVLEQLTAYCrKDVRVV-NLSASSSDSVQRAllAEKpdIVVSTPARLLSHLESGSLLLLSTLKYLVIDEADLV 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1937893951 248 IaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNIIKL 297
Cdd:cd17961   158 L-SYGYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPAILKL 206
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
 93-292 2.21e-32

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: 122.43  E-value: 2.21e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951  93 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEpanNHPQ---CLCLS 169
Cdd:cd17954     1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQG--RDIIGLAETGSGKTAAFALPILQALL---ENPQrffALVLA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 170 PTYELALQTGKVIEQMGKFyPELKLAYAVRG-----NKLERGQKvgEQIVIGTPGTVLDWCSKMKFIDPKKIKVFVLDEA 244
Cdd:cd17954    76 PTRELAQQISEQFEALGSS-IGLKSAVLVGGmdmmaQAIALAKK--PHVIVATPGRLVDHLENTKGFSLKSLKFLVMDEA 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1937893951 245 DVMIatqgHQDQSIRIQRML---PRNCQMLLFSATFEDSVWKFAQKVVPDP 292
Cdd:cd17954   153 DRLL----NMDFEPEIDKILkviPRERTTYLFSATMTTKVAKLQRASLKNP 199
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 319-434 5.92e-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: 118.08  E-value: 5.92e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 319 EKFQALCNLYGAITIAQAMIFCHTRKTA--SWLaaeLSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARG 396
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLeaELL---LEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERG 77

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1937893951 397 IDVEQVSVVINFDLPvdkdGNPdnETYLHRIGRTGRFG 434
Cdd:pfam00271  78 LDLPDVDLVINYDLP----WNP--ASYIQRIGRAGRAG 109
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
 94-292 1.70e-31

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: 120.12  E-value: 1.70e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951  94 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVepannhpQCLCLSPTYE 173
Cdd:cd17938     1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGG--GDVLMAAETGSGKTGAFCLPVLQIV-------VALILEPSRE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 174 LALQTGKVIEQMGKFY--PELKLAYAVRGNKLERGQKVGEQ---IVIGTPGTVLDWCSKMKfIDPKKIKVFVLDEADVMI 248
Cdd:cd17938    72 LAEQTYNCIENFKKYLdnPKLRVALLIGGVKAREQLKRLESgvdIVVGTPGRLEDLIKTGK-LDLSSVRFFVLDEADRLL 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1937893951 249 aTQGHQDQSIRIQRMLP------RNCQMLLFSATFE-DSVWKFAQKVVPDP 292
Cdd:cd17938   151 -SQGNLETINRIYNRIPkitsdgKRLQVIVCSATLHsFEVKKLADKIMHFP 200
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
 103-285 4.56e-31

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: 118.51  E-value: 4.56e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 103 LLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV---EPANNHPQCLCLSPTYELALQTG 179
Cdd:cd17947     1 LLRALSSLGFTKPTPIQAAAIPLALLG--KDICASAVTGSGKTAAFLLPILERLlyrPKKKAATRVLVLVPTRELAMQCF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 180 KVIEQMGKFYPeLKLAYAVRGNKL---ERGQKVGEQIVIGTPGTVLDWCSKMKFIDPKKIKVFVLDEADVMIaTQGHQDQ 256
Cdd:cd17947    79 SVLQQLAQFTD-ITFALAVGGLSLkaqEAALRARPDIVIATPGRLIDHLRNSPSFDLDSIEILVLDEADRML-EEGFADE 156

                         170       180
                  ....*....|....*....|....*....
gi 1937893951 257 SIRIQRMLPRNCQMLLFSATFEDSVWKFA 285
Cdd:cd17947   157 LKEILRLCPRTRQTMLFSATMTDEVKDLA 185
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
 99-295 5.12e-30

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: 116.14  E-value: 5.12e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951  99 LKPQLLQGVYAMGFNRPSKIQENALPLMLaEPPQNLIAQSQSGTGKTAAFVL----AMLSQVEPA-NNHPQCLCLSPTYE 173
Cdd:cd17964     1 LDPSLLKALTRMGFETMTPVQQKTLKPIL-STGDDVLARAKTGTGKTLAFLLpaiqSLLNTKPAGrRSGVSALIISPTRE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 174 LALQTGKVIEQMGKFYPELKLAYAVRGNK----LERGQKVGEQIVIGTPGTVLDWCSKMKFIDP-KKIKVFVLDEADVMI 248
Cdd:cd17964    80 LALQIAAEAKKLLQGLRKLRVQSAVGGTSrraeLNRLRRGRPDILVATPGRLIDHLENPGVAKAfTDLDYLVLDEADRLL 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1937893951 249 aTQGHQDQSIRIQRMLPRNC----QMLLFSATFEDSVWKFAQKVV-PDPNII 295
Cdd:cd17964   160 -DMGFRPDLEQILRHLPEKNadprQTLLFSATVPDEVQQIARLTLkKDYKFI 210
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
 103-295 9.69e-29

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: 112.26  E-value: 9.69e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 103 LLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANNHPQCLCLSPTYELALQTGKVI 182
Cdd:cd17962     1 LSSNLKKAGYEVPTPIQMQMIPVGLLG--RDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 183 EQMGKFYPELKLAYAVRGNKLErGQ----KVGEQIVIGTPGTVLDWCSKMKfIDPKKIKVFVLDEADVMIaTQGHQDQSI 258
Cdd:cd17962    79 KELMKGLPPMKTALLVGGLPLP-PQlyrlQQGVKVIIATPGRLLDILKQSS-VELDNIKIVVVDEADTML-KMGFQQQVL 155

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1937893951 259 RIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNII 295
Cdd:cd17962   156 DILENISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
 94-292 1.65e-28

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: 111.93  E-value: 1.65e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951  94 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQ--VEPANnhPQCLCLSPT 171
Cdd:cd17955     1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAG--RDVIGGAKTGSGKTAAFALPILQRlsEDPYG--IFALVLTPT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 172 YELALQtgkVIEQM---GKFyPELKLAYAVRG-NKLERGQKVGEQ--IVIGTPGTVLDW---CSKMKFiDPKKIKVFVLD 242
Cdd:cd17955    77 RELAYQ---IAEQFralGAP-LGLRCCVIVGGmDMVKQALELSKRphIVVATPGRLADHlrsSDDTTK-VLSRVKFLVLD 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1937893951 243 EADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 292
Cdd:cd17955   152 EADRLL-TGSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKP 200
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
 93-286 8.53e-28

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: 110.27  E-value: 8.53e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951  93 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV--EPANNH-------- 162
Cdd:cd17967     1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAG--RDLMACAQTGSGKTAAFLLPIISKLleDGPPSVgrgrrkay 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 163 PQCLCLSPTYELALQTgkvieqmgkfYPE-LKLAY-------------AVRG--NKLERGQKvgeqIVIGTPGTVLDWCS 226
Cdd:cd17967    79 PSALILAPTRELAIQI----------YEEaRKFSYrsgvrsvvvyggaDVVHqqLQLLRGCD----ILVATPGRLVDFIE 144

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937893951 227 KMKfIDPKKIKVFVLDEADVMIaTQGHQDQsirIQRML-------PRNCQMLLFSATFEDSVWKFAQ 286
Cdd:cd17967   145 RGR-ISLSSIKFLVLDEADRML-DMGFEPQ---IRKIVehpdmppKGERQTLMFSATFPREIQRLAA 206
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
 103-281 3.03e-27

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: 108.43  E-value: 3.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 103 LLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV-----EPANNHPQCLCLSPTYELALQ 177
Cdd:cd17960     1 ILDVVAELGFTSMTPVQAATIPLFLSN--KDVVVEAVTGSGKTLAFLIPVLEILlkrkaNLKKGQVGALIISPTRELATQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 178 TGKVIEQMGKFY-PELKLAYAVRGNKLERGQK----VGEQIVIGTPGTVLD-WCSKMKFIDPKKIKVFVLDEADVMIATq 251
Cdd:cd17960    79 IYEVLQSFLEHHlPKLKCQLLIGGTNVEEDVKkfkrNGPNILVGTPGRLEElLSRKADKVKVKSLEVLVLDEADRLLDL- 157

                         170       180       190
                  ....*....|....*....|....*....|
gi 1937893951 252 GHQDQSIRIQRMLPRNCQMLLFSATFEDSV 281
Cdd:cd17960   158 GFEADLNRILSKLPKQRRTGLFSATQTDAV 187
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
 77-287 3.82e-27

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: 109.67  E-value: 3.82e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951  77 VEVLQRDPSSPlysVKSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQ- 155
Cdd:cd18052    31 VEVTGRNPPPA---ILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAG--RDLMACAQTGSGKTAAFLLPVLTGm 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 156 ----VEPAN----NHPQCLCLSPTYELALQTGKvieQMGKF-----------YPELKLAYAVRgnKLERGQkvgeQIVIG 216
Cdd:cd18052   106 mkegLTASSfsevQEPQALIVAPTRELANQIFL---EARKFsygtcirpvvvYGGVSVGHQIR--QIEKGC----HILVA 176

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937893951 217 TPGTVLDWCSKMKfIDPKKIKVFVLDEADVMIATQGHQDqsirIQRML-----PR--NCQMLLFSATFEDSVWKFAQK 287
Cdd:cd18052   177 TPGRLLDFIGRGK-ISLSKLKYLILDEADRMLDMGFGPE----IRKLVsepgmPSkeDRQTLMFSATFPEEIQRLAAE 249
HELICc smart00490
helicase superfamily c-terminal domain;
348-434 8.35e-27

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 103.06  E-value: 8.35e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951  348 WLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRI 427
Cdd:smart00490   2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSP------ASYIQRI 75


                   ....*..
gi 1937893951  428 GRTGRFG 434
Cdd:smart00490  76 GRAGRAG 82
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
 103-292 1.54e-22

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: 95.17  E-value: 1.54e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 103 LLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLS------QVEPANNhPQCLCLSPTYELAL 176
Cdd:cd17952     1 LLNAIRKQEYEQPTPIQAQALPVALSG--RDMIGIAKTGSGKTAAFIWPMLVhimdqrELEKGEG-PIAVIVAPTRELAQ 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 177 QTGKVIEQMGKFYPELKLAYAVRGNKLERGQ--KVGEQIVIGTPGTVLDWCsKMKFIDPKKIKVFVLDEADVMIaTQGHQ 254
Cdd:cd17952    78 QIYLEAKKFGKAYNLRVVAVYGGGSKWEQAKalQEGAEIVVATPGRLIDMV-KKKATNLQRVTYLVLDEADRMF-DMGFE 155

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1937893951 255 DQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 292
Cdd:cd17952   156 YQVRSIVGHVRPDRQTLLFSATFKKKIEQLARDILSDP 193
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
 91-292 3.64e-22

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: 94.75  E-value: 3.64e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951  91 VKSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV--EPANNH---PQC 165
Cdd:cd17953    11 IQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSG--RDVIGIAKTGSGKTLAFLLPMFRHIkdQRPVKPgegPIG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 166 LCLSPTYELALQtgkVIEQMGKFYPELKL-AYAVRGNKLERGQ----KVGEQIVIGTPGTVLDW--CSKMKFIDPKKIKV 238
Cdd:cd17953    89 LIMAPTRELALQ---IYVECKKFSKALGLrVVCVYGGSGISEQiaelKRGAEIVVCTPGRMIDIltANNGRVTNLRRVTY 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1937893951 239 FVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 292
Cdd:cd17953   166 VVLDEADRMF-DMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKP 218
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
 103-292 1.25e-21

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: 92.27  E-value: 1.25e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 103 LLQGVYAMGFNRPSKIQENALPLMLAEPpqNLIAQSQSGTGKTAAFVLAMLSQVEPANN--HPQCLCLSPTYELALQTGK 180
Cdd:cd17957     1 LLNNLEESGYREPTPIQMQAIPILLHGR--DLLACAPTGSGKTLAFLIPILQKLGKPRKkkGLRALILAPTRELASQIYR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 181 VIEQMGKFYPeLKLAYAVRGN--KLERGQKVGEQ--IVIGTPGTVLDWCsKMKFIDPKKIKVFVLDEADVMIATqGHQDQ 256
Cdd:cd17957    79 ELLKLSKGTG-LRIVLLSKSLeaKAKDGPKSITKydILVSTPLRLVFLL-KQGPIDLSSVEYLVLDEADKLFEP-GFREQ 155

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1937893951 257 SIRIQRMLPRNC-QMLLFSATFEDSVWKFAQKVVPDP 292
Cdd:cd17957   156 TDEILAACTNPNlQRSLFSATIPSEVEELARSVMKDP 192
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
 104-295 2.31e-21

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: 91.58  E-value: 2.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 104 LQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANNHPQ----CLCLSPTYELALQTG 179
Cdd:cd17941     2 LKGLKEAGFIKMTEIQRDSIPHALQG--RDILGAAKTGSGKTLAFLVPLLEKLYRERWTPEdglgALIISPTRELAMQIF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 180 KVIEQMGKfYPELKLAYAVRGN--KLERGQKVGEQIVIGTPGTVLDWCSKMKFIDPKKIKVFVLDEADvMIATQGHQDQS 257
Cdd:cd17941    80 EVLRKVGK-YHSFSAGLIIGGKdvKEEKERINRMNILVCTPGRLLQHMDETPGFDTSNLQMLVLDEAD-RILDMGFKETL 157

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1937893951 258 IRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNII 295
Cdd:cd17941   158 DAIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYI 195
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
 103-295 2.39e-21

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: 92.38  E-value: 2.39e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 103 LLQGVYAMGFNRPSKIQENALPLMLAepPQNLIAQSQSGTGKTAAFVLAMLSQV--------EPANNHPQCLCLSPTYEL 174
Cdd:cd17945     1 LLRVIRKLGYKEPTPIQRQAIPIGLQ--NRDIIGIAETGSGKTAAFLIPLLVYIsrlppldeETKDDGPYALILAPTREL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 175 ALQTGKVIEQMGKFYPeLKLAYAVRGNKLE-RGQKV--GEQIVIGTPGTVLDwCSKMKFIDPKKIKVFVLDEADVMIaTQ 251
Cdd:cd17945    79 AQQIEEETQKFAKPLG-IRVVSIVGGHSIEeQAFSLrnGCEILIATPGRLLD-CLERRLLVLNQCTYVVLDEADRMI-DM 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937893951 252 GHQDQSIRIQRMLP--------------------RNCQMLLFSATFEDSVWKFAQKVVPDPNII 295
Cdd:cd17945   156 GFEPQVTKILDAMPvsnkkpdteeaeklaasgkhRYRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
 103-295 4.72e-21

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: 90.60  E-value: 4.72e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 103 LLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLA----MLSQVEP--ANNHPQCLCLSPTYELAL 176
Cdd:cd17958     1 IMKEIKKQGFEKPSPIQSQAWPIILQG--IDLIGVAQTGTGKTLAYLLPgfihLDLQPIPreQRNGPGVLVLTPTRELAL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 177 QtgkVIEQMGKF-YPELKlAYAVRG----NKLERGQKVGEQIVIGTPGTVLDwCSKMKFIDPKKIKVFVLDEADVMIaTQ 251
Cdd:cd17958    79 Q---IEAECSKYsYKGLK-SVCVYGggnrNEQIEDLSKGVDIIIATPGRLND-LQMNNVINLKSITYLVLDEADRML-DM 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1937893951 252 GHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNII 295
Cdd:cd17958   153 GFEPQIRKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
 103-277 1.13e-20

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: 90.76  E-value: 1.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 103 LLQGVYAMGFNRPSKIQENALPLMLAEPpQNLIAQSQSGTGKTAAFVLAM----LSQVEPANN-----HPQCLCLSPTYE 173
Cdd:cd17946     1 ILRALADLGFSEPTPIQALALPAAIRDG-KDVIGAAETGSGKTLAFGIPIlerlLSQKSSNGVggkqkPLRALILTPTRE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 174 LALQTGKVIEQMGKfYPELKLAYAVRG---NKLERGQKVGEQIVIGTPGTVLDWCSKmkfiDP------KKIKVFVLDEA 244
Cdd:cd17946    80 LAVQVKDHLKAIAK-YTNIKIASIVGGlavQKQERLLKKRPEIVVATPGRLWELIQE----GNehlanlKSLRFLVLDEA 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1937893951 245 DVMIaTQGHQDQSIRIQRMLPRNC-------QMLLFSATF 277
Cdd:cd17946   155 DRML-EKGHFAELEKILELLNKDRagkkrkrQTFVFSATL 193
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
 90-277 1.80e-20

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: 90.48  E-value: 1.80e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951  90 SVKSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV------EPANN-- 161
Cdd:cd18051    19 HIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSK--RDLMACAQTGSGKTAAFLLPILSQIyeqgpgESLPSes 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 162 --------HPQCLCLSPTYELALQtgkVIEQMGKFypelklAY--AVRGNKLERGQKVGEQI---------VIGTPGTVL 222
Cdd:cd18051    97 gyygrrkqYPLALVLAPTRELASQ---IYDEARKF------AYrsRVRPCVVYGGADIGQQMrdlergchlLVATPGRLV 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1937893951 223 DWCSKMKfIDPKKIKVFVLDEADVMIaTQGHQDQSIRI--QRMLPRNC--QMLLFSATF 277
Cdd:cd18051   168 DMLERGK-IGLDYCKYLVLDEADRML-DMGFEPQIRRIveQDTMPPTGerQTLMFSATF 224
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
 110-296 4.83e-20

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: 88.41  E-value: 4.83e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 110 MGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANNH------PQCLCLSPTYELALQTGKVIE 183
Cdd:cd17949     9 MGIEKPTAIQKLAIPVLLQG--RDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRvdrsdgTLALVLVPTRELALQIYEVLE 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 184 QMGKFYPELKLAYAVRGNKLE----RGQKvGEQIVIGTPGTVLDWCSKMKFIDPKKIKVFVLDEADVMIaTQGHQDQSIR 259
Cdd:cd17949    87 KLLKPFHWIVPGYLIGGEKRKsekaRLRK-GVNILIATPGRLLDHLKNTQSFDVSNLRWLVLDEADRLL-DMGFEKDITK 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1937893951 260 IQRML-------------PRNCQMLLFSATFEDSVWKFAQKVVPDPNIIK 296
Cdd:cd17949   165 ILELLddkrskaggekskPSRRQTVLVSATLTDGVKRLAGLSLKDPVYID 214
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
 104-276 2.29e-19

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: 85.88  E-value: 2.29e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 104 LQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFV---LAMLSQVEPAN-NHPQCLCLSPTYELALQTG 179
Cdd:cd17942     2 LKAIEEMGFTKMTEIQAKSIPPLLEG--RDVLGAAKTGSGKTLAFLipaIELLYKLKFKPrNGTGVIIISPTRELALQIY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 180 KVIEQMGKFYPE---LKLAYAVRGNKLERGQKvGEQIVIGTPGTVLDWCSKMKFIDPKKIKVFVLDEADvMIATQGHQDQ 256
Cdd:cd17942    80 GVAKELLKYHSQtfgIVIGGANRKAEAEKLGK-GVNILVATPGRLLDHLQNTKGFLYKNLQCLIIDEAD-RILEIGFEEE 157

                         170       180
                  ....*....|....*....|
gi 1937893951 257 SIRIQRMLPRNCQMLLFSAT 276
Cdd:cd17942   158 MRQIIKLLPKRRQTMLFSAT 177
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
 103-295 1.57e-18

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: 83.93  E-value: 1.57e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 103 LLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQ-VEP-------ANNHPQCLCLSPTYEL 174
Cdd:cd17951     1 ILKGLKKKGIKKPTPIQMQGLPTILSG--RDMIGIAFTGSGKTLVFTLPLIMFaLEQekklpfiKGEGPYGLIVCPSREL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 175 ALQTGKVIEQMGKF-----YPELKLAYAVRGNKL---ERGQKVGEQIVIGTPGTVLDWCSKmKFIDPKKIKVFVLDEADV 246
Cdd:cd17951    79 ARQTHEVIEYYCKAlqeggYPQLRCLLCIGGMSVkeqLEVIRKGVHIVVATPGRLMDMLNK-KKINLDICRYLCLDEADR 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1937893951 247 MIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNII 295
Cdd:cd17951   158 MI-DMGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
 103-292 3.24e-18

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: 82.80  E-value: 3.24e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 103 LLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV------EPANNhPQCLCLSPTYELAL 176
Cdd:cd17966     1 VMDELKRQGFTEPTAIQAQGWPMALSG--RDMVGIAQTGSGKTLAFLLPAIVHInaqpplERGDG-PIVLVLAPTRELAQ 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 177 QtgkVIEQMGKFYPELKL----AY--AVRGNKLeRGQKVGEQIVIGTPGTVLDWCSKMKfIDPKKIKVFVLDEADVMIaT 250
Cdd:cd17966    78 Q---IQQEANKFGGSSRLrntcVYggAPKGPQI-RDLRRGVEICIATPGRLIDFLDQGK-TNLRRVTYLVLDEADRML-D 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1937893951 251 QGHQDQ------SIRIQRmlprncQMLLFSATFEDSVWKFAQKVVPDP 292
Cdd:cd17966   152 MGFEPQirkivdQIRPDR------QTLMWSATWPKEVRRLAEDFLKDY 193
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
 74-291 4.58e-15

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: 74.66  E-value: 4.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951  74 TNQVEVLQRDPSSPlysVKSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAML 153
Cdd:cd18049     9 SKEITVRGHNCPKP---VLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSG--LDMVGVAQTGSGKTLSYLLPAI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 154 SQV--EPANNH---PQCLCLSPTYELALQTGKVIEQMGK---FYPELKLAYAVRGNKLeRGQKVGEQIVIGTPGTVLDWC 225
Cdd:cd18049    84 VHInhQPFLERgdgPICLVLAPTRELAQQVQQVAAEYGRacrLKSTCIYGGAPKGPQI-RDLERGVEICIATPGRLIDFL 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937893951 226 SKMKfIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPD 291
Cdd:cd18049   163 EAGK-TNLRRCTYLVLDEADRML-DMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKD 226
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
 112-291 5.03e-15

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: 75.05  E-value: 5.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 112 FNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVepanNH---------PQCLCLSPTYELALQTGKVI 182
Cdd:cd18050    82 FKEPTPIQCQGFPLALSG--RDMVGIAQTGSGKTLAYLLPAIVHI----NHqpylergdgPICLVLAPTRELAQQVQQVA 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 183 EQMGKfYPELK----LAYAVRGNKLeRGQKVGEQIVIGTPGTVLDWCSKMKfIDPKKIKVFVLDEADVMIaTQGHQDQSI 258
Cdd:cd18050   156 DDYGK-SSRLKstciYGGAPKGPQI-RDLERGVEICIATPGRLIDFLEAGK-TNLRRCTYLVLDEADRML-DMGFEPQIR 231

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1937893951 259 RIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPD 291
Cdd:cd18050   232 KIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRD 264
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
 132-287 1.85e-14

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: 72.19  E-value: 1.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 132 QNLIAQSQSGTGKTAAFVLAML------SQVEPANNHPQCLCLSPTYELALQTGKVIEQMGKfypELKLAyAVRGNKLER 205
Cdd:cd17944    28 KDLIAQARTGTGKTFSFAIPLIeklqedQQPRKRGRAPKVLVLAPTRELANQVTKDFKDITR---KLSVA-CFYGGTPYQ 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 206 GQ----KVGEQIVIGTPGTVLDWCSKMKfIDPKKIKVFVLDEADVMI----ATQGHQDQSIRIQRMLPRNCQMLLFSATF 277
Cdd:cd17944   104 QQifaiRNGIDILVGTPGRIKDHLQNGR-LDLTKLKHVVLDEVDQMLdmgfAEQVEEILSVSYKKDSEDNPQTLLFSATC 182

                         170
                  ....*....|
gi 1937893951 278 EDSVWKFAQK 287
Cdd:cd17944   183 PDWVYNVAKK 192
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
141-477 1.93e-14

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 75.45  E-value: 1.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 141 GTGKT--AAFVLAMLSQVEPAnnhpqcLCLSPTYELALQTGKVIEQMgkfypeLKLAYAVRGNKlergqKVGEQIVIGTP 218
Cdd:COG1061   110 GTGKTvlALALAAELLRGKRV------LVLVPRRELLEQWAEELRRF------LGDPLAGGGKK-----DSDAPITVATY 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 219 GTVldwcSKMKFID--PKKIKVFVLDEAdvmiatqgHQDQSIRIQRMLPR--NCQMLLFSAT--FEDSVWKF-------- 284
Cdd:COG1061   173 QSL----ARRAHLDelGDRFGLVIIDEA--------HHAGAPSYRRILEAfpAAYRLGLTATpfRSDGREILlflfdgiv 240

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 285 ---------AQKVVPDPNII----KLKREEETLDTIKQ--YYVLCNNREEKFQALCNLYGAIT-IAQAMIFCHTRKTASW 348
Cdd:COG1061   241 yeyslkeaiEDGYLAPPEYYgirvDLTDERAEYDALSErlREALAADAERKDKILRELLREHPdDRKTLVFCSSVDHAEA 320

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 349 LAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDlPVdkdGNPDneTYLHRIG 428
Cdd:COG1061   321 LAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLR-PT---GSPR--EFIQRLG 394

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1937893951 429 R---TGRFGKRGLAVNMVDSKHSM--NILNRIQEHFNKKIERLDTDDLDEIEKI 477
Cdd:COG1061   395 RglrPAPGKEDALVYDFVGNDVPVleELAKDLRDLAGYRVEFLDEEESEELALL 448
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
 133-276 2.85e-14

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: 70.12  E-value: 2.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 133 NLIAQSQSGTGKTAAFVLAMLSQVEPAnnHPQCLCLSPTYELALQTGKVIeqMGKFYPELKLAYAVRG-NKLERGQKVG- 210
Cdd:cd00046     3 NVLITAPTGSGKTLAALLAALLLLLKK--GKKVLVLVPTKALALQTAERL--RELFGPGIRVAVLVGGsSAEEREKNKLg 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937893951 211 -EQIVIGTPGTVLDWCSKMKFIDPKKIKVFVLDEADVM-IATQGHQDQSIRIQRMLPRNCQMLLFSAT 276
Cdd:cd00046    79 dADIIIATPDMLLNLLLREDRLFLKDLKLIIVDEAHALlIDSRGALILDLAVRKAGLKNAQVILLSAT 146
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
333-435 3.53e-12

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 68.60  E-value: 3.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 333 IAQAMIFCHTRKTASWLAAELSKEGHQVALLSGE--------MMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSV 404
Cdd:COG1111   353 DSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGQaskegdkgLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDL 432

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1937893951 405 VINFDlPVdkdgnPDNETYLHRIGRTGRFGK 435
Cdd:COG1111   433 VIFYE-PV-----PSEIRSIQRKGRTGRKRE 457
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 338-434 4.18e-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: 63.26  E-value: 4.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 338 IFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEK--VLVTTNVCARGIDVEQVSVVINFDLPvdkd 415
Cdd:cd18793    32 IFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIrvFLLSTKAGGVGLNLTAANRVILYDPW---- 107

                          90
                  ....*....|....*....
gi 1937893951 416 GNPDNEtyLHRIGRTGRFG 434
Cdd:cd18793   108 WNPAVE--EQAIDRAHRIG 124
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
 103-290 3.21e-11

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: 63.15  E-value: 3.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 103 LLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV-------EPANNHPQCLCLSPTYELA 175
Cdd:cd17948     1 LVEILQRQGITKPTTVQKQGIPSILRG--RNTLCAAETGSGKTLTYLLPIIQRLlrykllaEGPFNAPRGLVITPSRELA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 176 LQTGKVIEQMGKFYP-ELKLAYAVRGNKLERGQKVGE-QIVIGTPGtVLDWCSKMKFIDPKKIKVFVLDEADVMI----- 248
Cdd:cd17948    79 EQIGSVAQSLTEGLGlKVKVITGGRTKRQIRNPHFEEvDILVATPG-ALSKLLTSRIYSLEQLRHLVLDEADTLLddsfn 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1937893951 249 --------ATQGHQDQSIRIQRmLPRNCQMLLFSATFEDSVWKFAQKVVP 290
Cdd:cd17948   158 eklshflrRFPLASRRSENTDG-LDPGTQLVLVSATMPSGVGEVLSKVID 206
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 338-434 9.44e-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: 9.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 338 IFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEK--VLVTTNVCARGIDVEQVSVVINFDLPVdkd 415
Cdd:COG0553   554 VFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEApvFLISLKAGGEGLNLTAADHVIHYDLWW--- 630

                          90
                  ....*....|....*....
gi 1937893951 416 gNPDNEtyLHRIGRTGRFG 434
Cdd:COG0553   631 -NPAVE--EQAIDRAHRIG 646
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
 317-411 2.14e-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: 58.76  E-value: 2.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 317 REEKFQALCNL----YGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMV-------------EQRA--AVIE 377
Cdd:cd18802     5 VIPKLQKLIEIlreyFPKTPDFRGIIFVERRATAVVLSRLLKEHPSTLAFIRCGFLIgrgnssqrkrslmTQRKqkETLD 84

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1937893951 378 RFREGKEKVLVTTNVCARGIDVEQVSVVINFDLP 411
Cdd:cd18802    85 KFRDGELNLLIATSVLEEGIDVPACNLVIRFDLP 118
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
 103-276 3.21e-10

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: 59.95  E-value: 3.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 103 LLQGVYAMGFNRPSKIQENALPLMLAE-------PPQNLIAQSQSGTGKTAAFVL----AMLSQVEPannHPQCLCLSPT 171
Cdd:cd17956     1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyRPGDLCVSAPTGSGKTLAYVLpivqALSKRVVP---RLRALIVVPT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 172 YELALQTGKVIEQMGK--------------FYPELKLAYAVRGNKLErgqkVGEQIVIGTPGTVLDWCSKMKFIDPKKIK 237
Cdd:cd17956    78 KELVQQVYKVFESLCKgtglkvvslsgqksFKKEQKLLLVDTSGRYL----SRVDILVATPGRLVDHLNSTPGFTLKHLR 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1937893951 238 VFVLDEAD-------------VMIATQGHQDQ------SIRIQRMLPRNCQMLLFSAT 276
Cdd:cd17956   154 FLVIDEADrllnqsfqdwletVMKALGRPTAPdlgsfgDANLLERSVRPLQKLLFSAT 211
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
 338-435 8.39e-10

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: 56.83  E-value: 8.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 338 IFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPvdkdgn 417
Cdd:cd18794    35 IYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLP------ 108

                          90
                  ....*....|....*...
gi 1937893951 418 PDNETYLHRIGRTGRFGK 435
Cdd:cd18794   109 KSMESYYQESGRAGRDGL 126
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
338-440 2.70e-09

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 59.00  E-value: 2.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 338 IFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNvcA--RGIDVEQVSVVINFDLPvdkd 415
Cdd:COG0514   235 VYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATI--AfgMGIDKPDVRFVIHYDLP---- 308

                          90       100
                  ....*....|....*....|....*
gi 1937893951 416 GNPdnETYLHRIGRTGRFGKRGLAV 440
Cdd:COG0514   309 KSI--EAYYQEIGRAGRDGLPAEAL 331
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
 336-432 4.38e-08

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


Pssm-ID: 350188 [Multi-domain]  Cd Length: 143  Bit Score: 51.97  E-value: 4.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 336 AMIFCHTRKTASWLAAELSKEGHQV--ALLSGE--------MMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVV 405
Cdd:cd18801    33 VIIFSEFRDSAEEIVNFLSKIRPGIraTRFIGQasgksskgMSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLI 112

                          90       100
                  ....*....|....*....|....*..
gi 1937893951 406 INFdlpvdkDGNPDNETYLHRIGRTGR 432
Cdd:cd18801   113 ICY------DASPSPIRMIQRMGRTGR 133
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
 132-244 1.27e-07

DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350792 [Multi-domain]  Cd Length: 200  Bit Score: 51.88  E-value: 1.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 132 QNLIAQSQSGTGKT--AAFVL-AMLSQV-EPANNHPQCLCLSPTYELALQTGKVIEQ-----MGKFYPELKLAYAVRGNK 202
Cdd:cd18034    17 RNTIVVLPTGSGKTliAVMLIkEMGELNrKEKNPKKRAVFLVPTVPLVAQQAEAIRShtdlkVGEYSGEMGVDKWTKERW 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1937893951 203 LERGQKVgeQIVIGTPGTVLDWCSKMkFIDPKKIKVFVLDEA 244
Cdd:cd18034    97 KEELEKY--DVLVMTAQILLDALRHG-FLSLSDINLLIFDEC 135
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
 334-440 2.16e-07

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


Pssm-ID: 440818 [Multi-domain]  Cd Length: 758  Bit Score: 53.30  E-value: 2.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 334 AQAMIFCHTRK----TASWLAAELSKE--GHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVIN 407
Cdd:COG1205   289 LRTLVFTRSRRgaelLARYARRALREPdlADRVAAYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVL 368

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1937893951 408 fdlpvdkDGNPDNET-YLHRIGRTGRFGKRGLAV 440
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 ...
 323-440 4.99e-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: 4.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 323 ALCNLYGAITIAqamiFCHTRKTA----SWLAAELSKEGHQVALLS---GEMMVEQRAAVIERFREGKEKVLVTTNVCAR 395
Cdd:cd18797    29 ADLVRAGVKTIV----FCRSRKLAelllRYLKARLVEEGPLASKVAsyrAGYLAEDRREIEAELFNGELLGVVATNALEL 104

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1937893951 396 GIDVEQVSVVINfdlpvdkDGNPDNET-YLHRIGRTGRFGKRGLAV 440
Cdd:cd18797   105 GIDIGGLDAVVL-------AGYPGSLAsLWQQAGRAGRRGKDSLVI 143
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
 114-276 7.62e-07

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


Pssm-ID: 350676 [Multi-domain]  Cd Length: 180  Bit Score: 49.34  E-value: 7.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 114 RPSKIQENALPL----MLAEPPQNLIAQSQSGTGKTAAFVLAMLSQVepaNNHPQCLCLSPTYELALQTGKVIEqmgKFY 189
Cdd:cd17918    15 SLTKDQAQAIKDiekdLHSPEPMDRLLSGDVGSGKTLVALGAALLAY---KNGKQVAILVPTEILAHQHYEEAR---KFL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 190 PELKLAYAVRGNKlergQKVGEQI--VIGTpGTVLDWCSKMKfidpkkikvfvldEADVMIATQGHQ---DQSIRIQRMl 264
Cdd:cd17918    89 PFINVELVTGGTK----AQILSGIslLVGT-HALLHLDVKFK-------------NLDLVIVDEQHRfgvAQREALYNL- 149

                         170
                  ....*....|..
gi 1937893951 265 pRNCQMLLFSAT 276
Cdd:cd17918   150 -GATHFLEATAT 160
SF2_C_UvrB cd18790
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ...
 342-462 8.53e-07

C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II), and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA. Its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350177 [Multi-domain]  Cd Length: 171  Bit Score: 48.78  E-value: 8.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 342 TRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDlpVDKDGNPDNE 421
Cdd:cd18790    36 TKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILD--ADKEGFLRSE 113

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1937893951 422 TYL-HRIGRTGRfGKRGLAV----NMVDS-KHSMNILNR---IQEHFNKK 462
Cdd:cd18790   114 TSLiQTIGRAAR-NVNGKVIlyadKITDSmQKAIEETERrreIQMEYNEE 162
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
 385-437 1.74e-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: 45.77  E-value: 1.74e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1937893951 385 KVLVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRIGRTGRFGKRG 437
Cdd:cd18785    24 EILVATNVLGEGIDVPSLDTVIFFDPPSSA------ASYIQRVGRAGRGGKDE 70
PRK13766 PRK13766
Hef nuclease; Provisional
 283-432 2.84e-06

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 49.87  E-value: 2.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 283 KFAQKVVPDPNIIKLKRE-----------EETLDTIKQyyVLCNNREEKfqalcnlygaitiaqAMIFCHTRKTASWLAA 351
Cdd:PRK13766  321 KASKRLVEDPRFRKAVRKakeldiehpklEKLREIVKE--QLGKNPDSR---------------IIVFTQYRDTAEKIVD 383

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 352 ELSKEGHQVALLSGE--------MMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVInFDLPVdkdgnPDNETY 423
Cdd:PRK13766  384 LLEKEGIKAVRFVGQaskdgdkgMSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVI-FYEPV-----PSEIRS 457


                  ....*....
gi 1937893951 424 LHRIGRTGR 432
Cdd:PRK13766  458 IQRKGRTGR 466
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
 337-434 1.06e-05

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 47.79  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 337 MIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKdg 416
Cdd:PRK11057  240 IIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNI-- 317

                          90
                  ....*....|....*...
gi 1937893951 417 npdnETYLHRIGRTGRFG 434
Cdd:PRK11057  318 ----ESYYQETGRAGRDG 331
SF2_C_reverse_gyrase cd18798
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ...
 349-476 1.16e-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: 45.76  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 349 LAAELSKEGHQVALLSgemmvEQRAAVIERFREGKEKVLVTT----NVCARGIDV-EQVSVVINFDLPVdkdgnpdnETY 423
Cdd:cd18798    43 LKEFLERHGIKAELAL-----SSTEKNLEKFEEGEIDVLIGVasyyGVLVRGIDLpERIKYAIFYGVPV--------TTY 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1937893951 424 LHRIGRTGRF--GK--RGLAVNMVDSKHSMNILNRIQEHF--NKKIERLDTDDLDEIEK 476
Cdd:cd18798   110 IQASGRTSRLyaGGltKGLSVVLVDDPELFEALKKRLKLIldEFIFKELEEVDLEELLS 168
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
 360-450 2.10e-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: 44.57  E-value: 2.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 360 VALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDlpVDKDGNPDnetyLHRI-GRTGRFGKRGL 438
Cdd:cd18792    63 VALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIED--ADRFGLSQ----LHQLrGRVGRGKHQSY 136

                          90
                  ....*....|..
gi 1937893951 439 AVNMVDSKHSMN 450
Cdd:cd18792   137 CYLLYPDPKKLT 148
SF2_C_Ski2 cd18795
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ...
 335-444 2.21e-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: 44.47  E-value: 2.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 335 QAMIFCHTRKTASWLAAELSKeghqVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDK 414
Cdd:cd18795    45 PVLVFCSSRKECEKTAKDLAG----IAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYDG 120

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1937893951 415 DGN---PDNEtYLHRIGRTGR--FGKRGLAVNMVD 444
Cdd:cd18795   121 KGYrelSPLE-YLQMIGRAGRpgFDTRGEAIIMTK 154
PRK10917 PRK10917
ATP-dependent DNA helicase RecG; Provisional
 344-406 3.39e-05

ATP-dependent DNA helicase RecG; Provisional


Pssm-ID: 236794 [Multi-domain]  Cd Length: 681  Bit Score: 46.30  E-value: 3.39e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937893951 344 KTASWLAAELSKE--GHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSV-VI 406
Cdd:PRK10917  490 QSAEETYEELQEAfpELRVGLLHGRMKPAEKDAVMAAFKAGEIDILVATTVIEVGVDVPNATVmVI 555
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
 360-456 5.26e-05

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


Pssm-ID: 350198 [Multi-domain]  Cd Length: 159  Bit Score: 43.49  E-value: 5.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 360 VALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDlpVDKDGnpdnETYLHRI-GRTGRFGKRGL 438
Cdd:cd18811    64 VGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIED--AERFG----LSQLHQLrGRVGRGDHQSY 137

                          90
                  ....*....|....*...
gi 1937893951 439 AVNMVDSKHSMNILNRIQ 456
Cdd:cd18811   138 CLLVYKDPLTETAKQRLR 155
ComFA COG4098
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, ...
 334-406 1.09e-04

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: 44.48  E-value: 1.09e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937893951 334 AQAMIFCHTRKTASWLAAELSKEGHQVALLSgemmV----EQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVI 406
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 ...
 338-432 2.46e-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: 2.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 338 IFCHTRKTASWLAAEL------SKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFdlp 411
Cdd:cd18796    43 VFTNTRSQAERLAQRLrelcpdRVPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQI--- 119

                          90       100
                  ....*....|....*....|..
gi 1937893951 412 vdkdGNPDNET-YLHRIGRTGR 432
Cdd:cd18796   120 ----GSPKSVArLLQRLGRSGH 137
PLN03137 PLN03137
ATP-dependent DNA helicase; Q4-like; Provisional
 337-440 4.99e-04

ATP-dependent DNA helicase; Q4-like; Provisional


Pssm-ID: 215597 [Multi-domain]  Cd Length: 1195  Bit Score: 42.96  E-value: 4.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951  337 MIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKDG 416
Cdd:PLN03137   684 IIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEG 763

                           90       100
                   ....*....|....*....|....
gi 1937893951  417 npdnetYLHRIGRTGRFGKRGLAV 440
Cdd:PLN03137   764 ------YHQECGRAGRDGQRSSCV 781
SF2_C_TRCF cd18810
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ...
 360-450 9.75e-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: 9.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 360 VALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDlpVDKDGNPDnetyLHRI-GRTGRFGKRGL 438
Cdd:cd18810    54 IAIAHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIIER--ADKFGLAQ----LYQLrGRVGRSKERAY 127

                          90
                  ....*....|..
gi 1937893951 439 AVNMVDSKHSMN 450
Cdd:cd18810   128 AYFLYPDQKKLT 139
RecG COG1200
RecG-like helicase [Replication, recombination and repair];
344-399 2.09e-03

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


Pssm-ID: 440813 [Multi-domain]  Cd Length: 684  Bit Score: 40.80  E-value: 2.09e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1937893951 344 KTASWLAAELSKE--GHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDV 399
Cdd:COG1200   488 QAAEETYEELREAfpGLRVGLLHGRMKPAEKDAVMAAFKAGEIDVLVATTVIEVGVDV 545
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
 238-436 4.57e-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: 39.34  E-value: 4.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 238 VFVLDEADVMIA-TQGHQDQSIRIQRmlPRNCQMLLFSATFEDSVWKFAQKVVPDpniiklkREEETLDTI---KQYYVL 313
Cdd:cd09639   126 LLIFDEVHFYDEyTLALILAVLEVLK--DNDVPILLMSATLPKFLKEYAEKIGYV-------EENEPLDLKpneRAPFIK 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 314 CNNRE-EKFQALCNLYGAIT-IAQAMIFCHTRKTASWLAAELSKEGHQ--VALLSGEMM----VEQRAAVIERFREGKEK 385
Cdd:cd09639   197 IESDKvGEISSLERLLEFIKkGGSVAIIVNTVDRAQEFYQQLKEKGPEeeIMLIHSRFTekdrAKKEAELLLEFKKSEKF 276

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1937893951 386 VLVTTNVCargidveQVSVVINFDLPVDKDGNPDneTYLHRIGRTGRFGKR 436
Cdd:cd09639   277 VIVATQVI-------EASLDISVDVMITELAPID--SLIQRLGRLHRYGEK 318
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
 333-412 7.71e-03

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


Pssm-ID: 350186 [Multi-domain]  Cd Length: 116  Bit Score: 36.38  E-value: 7.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937893951 333 IAQAMIFCHTRKTASWLAAELSKEG-HQVALLSGEMMVEQRAAVIER--FREGKEKVLVTTNVCARGIDVEQVSVVInFD 409
Cdd:cd18799     6 EIKTLIFCVSIEHAEFMAEAFNEAGiDAVALNSDYSDRERGDEALILlfFGELKPPILVTVDLLTTGVDIPEVDNVV-FL 84


                  ...
gi 1937893951 410 LPV 412
Cdd:cd18799    85 RPT 87
 
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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