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Conserved domains on  [gi|19112717|ref|NP_595925|]
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ATP-dependent RNA/DNA helicase [Schizosaccharomyces pombe]

Protein Classification

ATP-dependent RNA helicase( domain architecture ID 13388279)

DEAD/DEAH box containing ATP-dependent RNA helicase catalyzes the unwinding of RNA, similar to DEAH box protein 34 (DHX34) that is required for nonsense-mediated decay (NMD) degradation of mRNA transcripts containing premature stop codons

CATH:  3.40.50.300
EC:  3.6.4.13
Gene Ontology:  GO:0005524|GO:0003724|GO:0003676|GO:0016887|GO:0003723
PubMed:  34680866|19747077|22922795|20206133|21779027|20225155

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HrpA super family cl34328
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
630-1158 5.83e-106

HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];


The actual alignment was detected with superfamily member COG1643:

Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 357.08  E-value: 5.83e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  630 QLPATMFRETIIDAVNNSQLLIISGDTGCGKSTQIPAFLLENSTKNGKavKIYVTEPRRISAISLANRVSQELG---Gnp 706
Cdd:COG1643    9 DLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGWGAGG--RIGMLEPRRLAARAAAERMAEELGepvG-- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  707 psarshELVGYSVRLDSKCTPLTPLTYVTTGTFLRLLEVGNEIESVTHLIIDEVHERSIDSDlllih-vlhllKQHPHLK 785
Cdd:COG1643   85 ------ETVGYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADlllallldlqpALRPDLK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  786 IIIMSATLNAEKFQLYFEGSNLITIPGKTYPVHRFYLEDilsqfgndksfgnaagqdvieeDDYETDQQDAsisnksAED 865
Cdd:COG1643  159 LLVMSATLDAERFARLLGDAPVIESSGRTYPVEVRYRPL----------------------PADERDLEDA------VAD 210

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  866 AIVEmnlipAWYNEkainyglivyllkyiftEGDpkfskcVLVFLPGISEILRVKSLIEDmpmfRNHRKFCIYMLHSTLS 945
Cdd:COG1643  211 AVRE-----ALAEE-----------------PGD------ILVFLPGEREIRRTAEALRG----RLPPDTEILPLYGRLS 258

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  946 SAQQQSVFNIPPKGCRKIVLSTNIAETGVTIPDVTCVIDTGVHREMRYNSRRHLSRLTDTFVSKANAKQRSGRAGRVQEG 1025
Cdd:COG1643  259 AAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERISQASANQRAGRAGRLAPG 338

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717 1026 ICYHLFSKfkhdTQFLS---YQTPEILRLNLQEVVLRvkMCQMGdVQDVLGKA-LDPPSSTNIIRALEKLHQVGALSENE 1101
Cdd:COG1643  339 ICYRLWSE----EDFARrpaFTDPEILRADLASLILE--LAAWG-LGDPEDLPfLDPPPARAIADARALLQELGALDADG 411

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 19112717 1102 KLTKLGKFLSQLPVDANLGKILVLGCFYKCVDAASSIVAMLTIGSPFRKSVDNEFSA 1158
Cdd:COG1643  412 RLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDPRRGAAGSDLLA 468
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
 1266-1349 2.60e-16

Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus of the DEAD-box helicases (pfam00270). In these helicases it is apparently always found in association with pfam04408. There do seem to be a couple of instances where it occurs by itself -. The structure PDB:3i4u adopts an OB-fold. helicases (pfam00270). In these helicases it is apparently always found in association with pfam04408. This C-terminal domain of the yeast helicase contains an oligonucleotide/oligosaccharide-binding (OB)-fold which seems to be placed at the entrance of the putative nucleic acid cavity. It also constitutes the binding site for the G-patch-containing domain of Pfa1p. When found on DEAH/RHA helicases, this domain is central to the regulation of the helicase activity through its binding of both RNA and G-patch domain proteins.


:

Pssm-ID: 400182 [Multi-domain]  Cd Length: 82  Bit Score: 74.98  E-value: 2.60e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717   1266 LCGVIAASLYPNILRYDYEKRQWSTLSTNKRVRILDVSVNNRSelPNMPSKFVAYTNMMSSTRasEYVNETTMVTLRQLL 1345
Cdd:pfam07717    1 LRAALAAGLYPNVARRDPKGKGYTTLSDNQRVFIHPSSVLFNE--KTFPPEWVVYQELVETTK--VYIRTVTAISPEWLL 76


                   ....
gi 19112717   1346 MMCG 1349
Cdd:pfam07717   77 LFAP 80
 
Name Accession Description Interval E-value
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
630-1158 5.83e-106

HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 357.08  E-value: 5.83e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  630 QLPATMFRETIIDAVNNSQLLIISGDTGCGKSTQIPAFLLENSTKNGKavKIYVTEPRRISAISLANRVSQELG---Gnp 706
Cdd:COG1643    9 DLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGWGAGG--RIGMLEPRRLAARAAAERMAEELGepvG-- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  707 psarshELVGYSVRLDSKCTPLTPLTYVTTGTFLRLLEVGNEIESVTHLIIDEVHERSIDSDlllih-vlhllKQHPHLK 785
Cdd:COG1643   85 ------ETVGYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADlllallldlqpALRPDLK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  786 IIIMSATLNAEKFQLYFEGSNLITIPGKTYPVHRFYLEDilsqfgndksfgnaagqdvieeDDYETDQQDAsisnksAED 865
Cdd:COG1643  159 LLVMSATLDAERFARLLGDAPVIESSGRTYPVEVRYRPL----------------------PADERDLEDA------VAD 210

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  866 AIVEmnlipAWYNEkainyglivyllkyiftEGDpkfskcVLVFLPGISEILRVKSLIEDmpmfRNHRKFCIYMLHSTLS 945
Cdd:COG1643  211 AVRE-----ALAEE-----------------PGD------ILVFLPGEREIRRTAEALRG----RLPPDTEILPLYGRLS 258

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  946 SAQQQSVFNIPPKGCRKIVLSTNIAETGVTIPDVTCVIDTGVHREMRYNSRRHLSRLTDTFVSKANAKQRSGRAGRVQEG 1025
Cdd:COG1643  259 AAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERISQASANQRAGRAGRLAPG 338

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717 1026 ICYHLFSKfkhdTQFLS---YQTPEILRLNLQEVVLRvkMCQMGdVQDVLGKA-LDPPSSTNIIRALEKLHQVGALSENE 1101
Cdd:COG1643  339 ICYRLWSE----EDFARrpaFTDPEILRADLASLILE--LAAWG-LGDPEDLPfLDPPPARAIADARALLQELGALDADG 411

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 19112717 1102 KLTKLGKFLSQLPVDANLGKILVLGCFYKCVDAASSIVAMLTIGSPFRKSVDNEFSA 1158
Cdd:COG1643  412 RLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDPRRGAAGSDLLA 468
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
 613-1173 3.73e-71

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 262.30  E-value: 3.73e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717   613 RQQLESESAEKFKV-FRNQLPATMFRETIIDAVNNSQLLIISGDTGCGKSTQIPAFLLENstknGKAVK--IYVTEPRRI 689
Cdd:PRK11131   54 AQRVLLREAARPEItYPENLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLEL----GRGVKglIGHTQPRRL 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717   690 SAISLANRVSQELGGNPPSArshelVGYSVRLDSKCTPLTPLTYVTTGTFL------RLLevgNEIESvthLIIDEVHER 763
Cdd:PRK11131  130 AARTVANRIAEELETELGGC-----VGYKVRFNDQVSDNTMVKLMTDGILLaeiqqdRLL---MQYDT---IIIDEAHER 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717   764 SIDSDLLLIHVLHLLKQHPHLKIIIMSATLNAEKFQLYFEGSNLITIPGKTYPVHRFYledilsqfgndksfgnaagQDV 843
Cdd:PRK11131  199 SLNIDFILGYLKELLPRRPDLKVIITSATIDPERFSRHFNNAPIIEVSGRTYPVEVRY-------------------RPI 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717   844 IEE-DDYETDQQDASIsnksaeDAIVEMNlipawyNEKAinyglivyllkyifteGDpkfskcVLVFLPGISEIlRVKSl 922
Cdd:PRK11131  260 VEEaDDTERDQLQAIF------DAVDELG------REGP----------------GD------ILIFMSGEREI-RDTA- 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717   923 ieDMPMFRNHRKFCIYMLHSTLSSAQQQSVFNipPKGCRKIVLSTNIAETGVTIPDVTCVIDTGVHREMRYNSRRHLSRL 1002
Cdd:PRK11131  304 --DALNKLNLRHTEILPLYARLSNSEQNRVFQ--SHSGRRIVLATNVAETSLTVPGIKYVIDPGTARISRYSYRTKVQRL 379

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  1003 TDTFVSKANAKQRSGRAGRVQEGICYHLFSkfkhDTQFLS---YQTPEILRLNLQEVVLRVKMCQMGDVQDVlgKALDPP 1079
Cdd:PRK11131  380 PIEPISQASANQRKGRCGRVSEGICIRLYS----EDDFLSrpeFTDPEILRTNLASVILQMTALGLGDIAAF--PFVEAP 453

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  1080 SSTNI---IRALEKLhqvGALSENE-----KLTKLGKFLSQLPVDANLGKILVLGCFYKCVDAASSIVAMLTIGSPFRKS 1151
Cdd:PRK11131  454 DKRNIqdgVRLLEEL---GAITTDEqasayKLTPLGRQLAQLPVDPRLARMVLEAQKHGCVREVMIITSALSIQDPRERP 530

                         570       580
                  ....*....|....*....|..
gi 19112717  1152 VDNEFSANKARLSFAKENtrSD 1173
Cdd:PRK11131  531 MDKQQASDEKHRRFADKE--SD 550
SF2_C_RHA cd18791
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ...
 815-1031 8.42e-71

C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family members are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350178 [Multi-domain]  Cd Length: 171  Bit Score: 234.35  E-value: 8.42e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  815 YPVHRFYLEDILSQFGndksfgnaagqdvieeddyetdqqdasisnksaedaivemnliPAWYNEKAINYGLIVYLLKYI 894
Cdd:cd18791    1 FPVEVYYLEDILELLG-------------------------------------------ISSEKEDPDYVDAAVRLILQI 37

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  895 FTEGDPKfskCVLVFLPGISEILRVKSLIEDMPMFRNHRKFCIYMLHSTLSSAQQQSVFNIPPKGCRKIVLSTNIAETGV 974
Cdd:cd18791   38 HRTEEPG---DILVFLPGQEEIERLCELLREELLSPDLGKLLVLPLHSSLPPEEQQRVFEPPPPGVRKVVLATNIAETSI 114

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 19112717  975 TIPDVTCVIDTGVHREMRYNSRRHLSRLTDTFVSKANAKQRSGRAGRVQEGICYHLF 1031
Cdd:cd18791  115 TIPGVVYVIDSGLVKEKVYDPRTGLSSLVTVWISKASAEQRAGRAGRTRPGKCYRLY 171
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
 1087-1177 1.45e-20

Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in length. It is found is a diverse set of RNA helicases. Its function is unknown, however it seems likely to be involved in nucleic acid binding.


Pssm-ID: 461295 [Multi-domain]  Cd Length: 104  Bit Score: 88.06  E-value: 1.45e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717   1087 ALEKLHQVGALSENEKLTKLGKFLSQLPVDANLGKILVLGCFYKCVDAASSIVAMLTIGSPF-------------RKSVD 1153
Cdd:pfam04408    1 ALELLYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFvqpnfldprsaakAARRR 80

                           90       100
                   ....*....|....*....|....
gi 19112717   1154 NEFSANKARLSFAKENTRSDLVLM 1177
Cdd:pfam04408   81 RRAADEKARAKFARLDLEGDHLTL 104
DEXDc smart00487
DEAD-like helicases superfamily;
637-820 1.05e-18

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 86.01  E-value: 1.05e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717     637 RETIIDAVNNSQLLIISGDTGCGKSTQIPAFLLENStKNGKAVKIYVTEPRRISAISLANRVSQELGGNPPSaRSHELVG 716
Cdd:smart00487   14 KEAIEALLSGLRDVILAAPTGSGKTLAALLPALEAL-KRGKGGRVLVLVPTRELAEQWAEELKKLGPSLGLK-VVGLYGG 91

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717     717 YSVRLDSKC--TPLTPLTYVTTGTFLRLLEVGN-EIESVTHLIIDEVHERSiDSDLLLIHVLHLLKQHPHLKIIIMSATL 793
Cdd:smart00487   92 DSKREQLRKleSGKTDILVTTPGRLLDLLENDKlSLSNVDLVILDEAHRLL-DGGFGDQLEKLLKLLPKNVQLLLLSATP 170

                           170       180
                    ....*....|....*....|....*....
gi 19112717     794 --NAEKFQLYFeGSNLITIPGKTYPVHRF 820
Cdd:smart00487  171 peEIENLLELF-LNDPVFIDVGFTPLEPI 198
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
 1266-1349 2.60e-16

Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus of the DEAD-box helicases (pfam00270). In these helicases it is apparently always found in association with pfam04408. There do seem to be a couple of instances where it occurs by itself -. The structure PDB:3i4u adopts an OB-fold. helicases (pfam00270). In these helicases it is apparently always found in association with pfam04408. This C-terminal domain of the yeast helicase contains an oligonucleotide/oligosaccharide-binding (OB)-fold which seems to be placed at the entrance of the putative nucleic acid cavity. It also constitutes the binding site for the G-patch-containing domain of Pfa1p. When found on DEAH/RHA helicases, this domain is central to the regulation of the helicase activity through its binding of both RNA and G-patch domain proteins.


Pssm-ID: 400182 [Multi-domain]  Cd Length: 82  Bit Score: 74.98  E-value: 2.60e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717   1266 LCGVIAASLYPNILRYDYEKRQWSTLSTNKRVRILDVSVNNRSelPNMPSKFVAYTNMMSSTRasEYVNETTMVTLRQLL 1345
Cdd:pfam07717    1 LRAALAAGLYPNVARRDPKGKGYTTLSDNQRVFIHPSSVLFNE--KTFPPEWVVYQELVETTK--VYIRTVTAISPEWLL 76


                   ....
gi 19112717   1346 MMCG 1349
Cdd:pfam07717   77 LFAP 80
cas3_core TIGR01587
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ...
 649-824 4.97e-04

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


Pssm-ID: 273707 [Multi-domain]  Cd Length: 359  Bit Score: 43.98  E-value: 4.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717    649 LLIISGDTGCGKsTQIPAFLLENSTKNGKAVKIYVTEPRRISAISLANRVSQELG-GNPPSARSHELVGYSVRLDS---- 723
Cdd:TIGR01587    1 LLVIEAPTGYGK-TEAALLWALHSIKSQKADRVIIALPTRATINAMYRRAKELFGsELVGLHHSSSFSRIKEMGDSeefe 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717    724 KCTPL----------TPLTYVT--------TGTF----LRLLEVGNEIesvthLIIDEVH--ERSIDSDLLLIHVLHLLK 779
Cdd:TIGR01587   80 HLFPLyihsndklflDPITVCTidqvlksvFGEFghyeFTLASIANSL-----LIFDEVHfyDEYTLALILAVLEVLKDN 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 19112717    780 QHPHlkiIIMSATL------NAEKFQLYFEGSNLITIPGKTYPVHRFYLED 824
Cdd:TIGR01587  155 DVPI---LLMSATLpkflkeYAEKIGYVEFNEPLDLKEERRFENHRFILIE 202
 
Name Accession Description Interval E-value
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
630-1158 5.83e-106

HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 357.08  E-value: 5.83e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  630 QLPATMFRETIIDAVNNSQLLIISGDTGCGKSTQIPAFLLENSTKNGKavKIYVTEPRRISAISLANRVSQELG---Gnp 706
Cdd:COG1643    9 DLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGWGAGG--RIGMLEPRRLAARAAAERMAEELGepvG-- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  707 psarshELVGYSVRLDSKCTPLTPLTYVTTGTFLRLLEVGNEIESVTHLIIDEVHERSIDSDlllih-vlhllKQHPHLK 785
Cdd:COG1643   85 ------ETVGYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADlllallldlqpALRPDLK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  786 IIIMSATLNAEKFQLYFEGSNLITIPGKTYPVHRFYLEDilsqfgndksfgnaagqdvieeDDYETDQQDAsisnksAED 865
Cdd:COG1643  159 LLVMSATLDAERFARLLGDAPVIESSGRTYPVEVRYRPL----------------------PADERDLEDA------VAD 210

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  866 AIVEmnlipAWYNEkainyglivyllkyiftEGDpkfskcVLVFLPGISEILRVKSLIEDmpmfRNHRKFCIYMLHSTLS 945
Cdd:COG1643  211 AVRE-----ALAEE-----------------PGD------ILVFLPGEREIRRTAEALRG----RLPPDTEILPLYGRLS 258

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  946 SAQQQSVFNIPPKGCRKIVLSTNIAETGVTIPDVTCVIDTGVHREMRYNSRRHLSRLTDTFVSKANAKQRSGRAGRVQEG 1025
Cdd:COG1643  259 AAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERISQASANQRAGRAGRLAPG 338

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717 1026 ICYHLFSKfkhdTQFLS---YQTPEILRLNLQEVVLRvkMCQMGdVQDVLGKA-LDPPSSTNIIRALEKLHQVGALSENE 1101
Cdd:COG1643  339 ICYRLWSE----EDFARrpaFTDPEILRADLASLILE--LAAWG-LGDPEDLPfLDPPPARAIADARALLQELGALDADG 411

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 19112717 1102 KLTKLGKFLSQLPVDANLGKILVLGCFYKCVDAASSIVAMLTIGSPFRKSVDNEFSA 1158
Cdd:COG1643  412 RLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDPRRGAAGSDLLA 468
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
 613-1173 3.73e-71

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 262.30  E-value: 3.73e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717   613 RQQLESESAEKFKV-FRNQLPATMFRETIIDAVNNSQLLIISGDTGCGKSTQIPAFLLENstknGKAVK--IYVTEPRRI 689
Cdd:PRK11131   54 AQRVLLREAARPEItYPENLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLEL----GRGVKglIGHTQPRRL 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717   690 SAISLANRVSQELGGNPPSArshelVGYSVRLDSKCTPLTPLTYVTTGTFL------RLLevgNEIESvthLIIDEVHER 763
Cdd:PRK11131  130 AARTVANRIAEELETELGGC-----VGYKVRFNDQVSDNTMVKLMTDGILLaeiqqdRLL---MQYDT---IIIDEAHER 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717   764 SIDSDLLLIHVLHLLKQHPHLKIIIMSATLNAEKFQLYFEGSNLITIPGKTYPVHRFYledilsqfgndksfgnaagQDV 843
Cdd:PRK11131  199 SLNIDFILGYLKELLPRRPDLKVIITSATIDPERFSRHFNNAPIIEVSGRTYPVEVRY-------------------RPI 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717   844 IEE-DDYETDQQDASIsnksaeDAIVEMNlipawyNEKAinyglivyllkyifteGDpkfskcVLVFLPGISEIlRVKSl 922
Cdd:PRK11131  260 VEEaDDTERDQLQAIF------DAVDELG------REGP----------------GD------ILIFMSGEREI-RDTA- 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717   923 ieDMPMFRNHRKFCIYMLHSTLSSAQQQSVFNipPKGCRKIVLSTNIAETGVTIPDVTCVIDTGVHREMRYNSRRHLSRL 1002
Cdd:PRK11131  304 --DALNKLNLRHTEILPLYARLSNSEQNRVFQ--SHSGRRIVLATNVAETSLTVPGIKYVIDPGTARISRYSYRTKVQRL 379

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  1003 TDTFVSKANAKQRSGRAGRVQEGICYHLFSkfkhDTQFLS---YQTPEILRLNLQEVVLRVKMCQMGDVQDVlgKALDPP 1079
Cdd:PRK11131  380 PIEPISQASANQRKGRCGRVSEGICIRLYS----EDDFLSrpeFTDPEILRTNLASVILQMTALGLGDIAAF--PFVEAP 453

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  1080 SSTNI---IRALEKLhqvGALSENE-----KLTKLGKFLSQLPVDANLGKILVLGCFYKCVDAASSIVAMLTIGSPFRKS 1151
Cdd:PRK11131  454 DKRNIqdgVRLLEEL---GAITTDEqasayKLTPLGRQLAQLPVDPRLARMVLEAQKHGCVREVMIITSALSIQDPRERP 530

                         570       580
                  ....*....|....*....|..
gi 19112717  1152 VDNEFSANKARLSFAKENtrSD 1173
Cdd:PRK11131  531 MDKQQASDEKHRRFADKE--SD 550
SF2_C_RHA cd18791
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ...
 815-1031 8.42e-71

C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family members are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350178 [Multi-domain]  Cd Length: 171  Bit Score: 234.35  E-value: 8.42e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  815 YPVHRFYLEDILSQFGndksfgnaagqdvieeddyetdqqdasisnksaedaivemnliPAWYNEKAINYGLIVYLLKYI 894
Cdd:cd18791    1 FPVEVYYLEDILELLG-------------------------------------------ISSEKEDPDYVDAAVRLILQI 37

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  895 FTEGDPKfskCVLVFLPGISEILRVKSLIEDMPMFRNHRKFCIYMLHSTLSSAQQQSVFNIPPKGCRKIVLSTNIAETGV 974
Cdd:cd18791   38 HRTEEPG---DILVFLPGQEEIERLCELLREELLSPDLGKLLVLPLHSSLPPEEQQRVFEPPPPGVRKVVLATNIAETSI 114

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 19112717  975 TIPDVTCVIDTGVHREMRYNSRRHLSRLTDTFVSKANAKQRSGRAGRVQEGICYHLF 1031
Cdd:cd18791  115 TIPGVVYVIDSGLVKEKVYDPRTGLSSLVTVWISKASAEQRAGRAGRTRPGKCYRLY 171
DEXHc_RHA-like cd17917
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ...
 648-810 2.70e-67

DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family belongs to 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: 438707 [Multi-domain]  Cd Length: 159  Bit Score: 223.88  E-value: 2.70e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  648 QLLIISGDTGCGKSTQIPAFLLENSTKNGKAVKIYVTEPRRISAISLANRVSQELGGNPpsarsHELVGYSVRLDSKCTP 727
Cdd:cd17917    2 QVVVIVGETGSGKTTQVPQFLLEDGLAKGGKGRIVCTQPRRIAAISVAERVAEERGEKL-----GEEVGYQIRFESKTSS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  728 LTPLTYVTTGTFLRLLEVGNEIESVTHLIIDEVHERSIDSDLLLIHVLHLLKQHPHLKIIIMSATLNAEKFQLYFEGSNL 807
Cdd:cd17917   77 KTRIKFCTDGILLRELLSDPLLSGYSHVILDEAHERSLDTDFLLGLLKDLLRKRPDLKVILMSATLDAEKFSSYFGGAPV 156


                 ...
gi 19112717  808 ITI 810
Cdd:cd17917  157 IHI 159
PRK11664 PRK11664
ATP-dependent RNA helicase HrpB; Provisional
 629-1124 1.61e-62

ATP-dependent RNA helicase HrpB; Provisional


Pssm-ID: 236950 [Multi-domain]  Cd Length: 812  Bit Score: 230.20  E-value: 1.61e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717   629 NQLPATMFRETIIDAVNNSQLLIISGDTGCGKSTQIPAFLLENSTKNGKavkIYVTEPRRISAISLANRVSQELGGNPps 708
Cdd:PRK11664    2 SSLPVAAVLPELLTALKTAPQVLLKAPTGAGKSTWLPLQLLQHGGINGK---IIMLEPRRLAARNVAQRLAEQLGEKP-- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717   709 arsHELVGYSVRLDSKCTPLTPLTYVTTGTFLRLLEVGNEIESVTHLIIDEVHERSIDSDLLLIHVLHLLKQ-HPHLKII 787
Cdd:PRK11664   77 ---GETVGYRMRAESKVGPNTRLEVVTEGILTRMIQRDPELSGVGLVILDEFHERSLQADLALALLLDVQQGlRDDLKLL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717   788 IMSATLNAEKFQLYFEGSNLITIPGKTYPVHRFYLEdiLSqfgndksfgnaagqdvieeddyetdqqdasiSNKSAEDAI 867
Cdd:PRK11664  154 IMSATLDNDRLQQLLPDAPVIVSEGRSFPVERRYQP--LP-------------------------------AHQRFDEAV 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717   868 VEMnlipawynekainyglIVYLLKyiftegdpKFSKCVLVFLPGISEILRVKSLIEDmpmfRNHRKFCIYMLHSTLSSA 947
Cdd:PRK11664  201 ARA----------------TAELLR--------QESGSLLLFLPGVGEIQRVQEQLAS----RVASDVLLCPLYGALSLA 252

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717   948 QQQSVFNIPPKGCRKIVLSTNIAETGVTIPDVTCVIDTGVHREMRYNSRRHLSRLTDTFVSKANAKQRSGRAGRVQEGIC 1027
Cdd:PRK11664  253 EQQKAILPAPAGRRKVVLATNIAETSLTIEGIRLVVDSGLERVARFDPKTGLTRLVTQRISQASMTQRAGRAGRLEPGIC 332

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  1028 YHLFSKfkhdTQF---LSYQTPEILRLNLQEVVLRVKMCQMGDVQDVlgKALDPPSSTNIIRALEKLHQVGALSENEKLT 1104
Cdd:PRK11664  333 LHLYSK----EQAeraAAQSEPEILHSDLSGLLLELLQWGCHDPAQL--SWLDQPPAAALAAAKRLLQQLGALDGQGRLT 406

                         490       500
                  ....*....|....*....|
gi 19112717  1105 KLGKFLSQLPVDANLGKILV 1124
Cdd:PRK11664  407 ARGRKMAALGNDPRLAAMLV 426
DEXHc_DHX57 cd17985
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the ...
 631-810 2.42e-49

DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to 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: 350743 [Multi-domain]  Cd Length: 177  Bit Score: 173.10  E-value: 2.42e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  631 LPATMFRETIIDAVNNSQLLIISGDTGCGKSTQIPAFLLENSTKNG--KAVKIYVTEPRRISAISLANRVSQElggnpPS 708
Cdd:cd17985    1 LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFILDNSLQGPplPVANIICTQPRRISAISVAERVAQE-----RA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  709 ARSHELVGYSVRLDSKCTPLTPLTYVTTGTFLRLLEVGNEIESVTHLIIDEVHERSIDSDLLLIHVLHLLKQHPHLKIII 788
Cdd:cd17985   76 ERVGQSVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDPTLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQRPDLKVIL 155

                        170       180
                 ....*....|....*....|..
gi 19112717  789 MSATLNAEKFQLYFEGSNLITI 810
Cdd:cd17985  156 MSATLNAELFSDYFNSCPVIHI 177
DEXHc_DHX9 cd17972
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ...
 598-810 2.56e-47

DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ATP-dependent RNA helicase A or RHA and leukophysin or LKP) plays an important role in many cellular processes, including regulation of DNA replication, transcription, translation, microRNA biogenesis, RNA processing and transport, and maintenance of genomic stability. DHX9 belongs to 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: 350730 [Multi-domain]  Cd Length: 234  Bit Score: 169.63  E-value: 2.56e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  598 FSGFERPPETLLNKWRQQLESESA-EKFKVFRNQLPATMFRETIIDAVNNSQLLIISGDTGCGKSTQIPAFLLENSTKNG 676
Cdd:cd17972   25 FATPEQISMDLKNELMYQREQDHNlQQILQERELLPVKKFREEILEAISNNPVVIIRGATGCGKTTQVPQYILDDFIQND 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  677 KA--VKIYVTEPRRISAISLANRVSQELGGNPpsarsHELVGYSVRLDSKCT-PLTPLTYVTTGTFLRLLEVGneIESVT 753
Cdd:cd17972  105 RAaeCNIVVTQPRRISAVSVAERVAFERGEEV-----GKSCGYSVRFESVLPrPHASILFCTVGVLLRKLEAG--IRGIS 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 19112717  754 HLIIDEVHERSIDSDLLLIHVLHLLKQHPHLKIIIMSATLNAEKFQLYFEGSNLITI 810
Cdd:cd17972  178 HVIVDEIHERDINTDFLLVVLRDVVQAYPDLRVILMSATIDTSMFCEYFFNCPVIEV 234
DEXHc_DHX36 cd17981
DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as ...
 631-810 7.55e-45

DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as G4-resolvase 1 or G4R1, MLE-like protein 1 and RNA helicase associated with AU-rich element or RHAU) unwinds a G4-quadruplex in human telomerase RNA. DHX36 belongs to 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: 350739 [Multi-domain]  Cd Length: 180  Bit Score: 160.39  E-value: 7.55e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  631 LPATMFRETIIDAVNNSQLLIISGDTGCGKSTQIPAFLLENSTKNGKA--VKIYVTEPRRISAISLANRVSQELGGNPPS 708
Cdd:cd17981    1 LPSYGMKQEIINMIDNNQVTVISGETGCGKTTQVTQFILDDAIERGKGssCRIVCTQPRRISAISVAERVAAERAESCGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  709 ARShelVGYSVRLDS-KCTPLTPLTYVTTGTFLRLLEVGNEIESVTHLIIDEVHERSIDSDLLLIHVLHLLKQHPHLKII 787
Cdd:cd17981   81 GNS---TGYQIRLESrKPRKQGSILYCTTGIVLQWLQSDPHLSNVSHLVLDEIHERNLQSDVLMGIVKDLLPFRSDLKVI 157

                        170       180
                 ....*....|....*....|...
gi 19112717  788 IMSATLNAEKFQLYFEGSNLITI 810
Cdd:cd17981  158 LMSATLNAEKFSDYFNNCPMIHI 180
DEXHc_DHX29 cd17975
DEXH-box helicase domain of DEAH-box helicase 29; DEAH-box helicase 29 (DHX29) is a part of ...
 631-810 1.79e-44

DEXH-box helicase domain of DEAH-box helicase 29; DEAH-box helicase 29 (DHX29) is a part of the 43S pre-initiation complex involved in translation initiation of mRNAs with structured 5'-UTRs. DHX29 is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350733 [Multi-domain]  Cd Length: 183  Bit Score: 159.31  E-value: 1.79e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  631 LPATMFRETIIDAVNNSQLLIISGDTGCGKSTQIPAFLLENSTKNG---KAVKIYVTEPRRISAISLANRVSQELGGNPP 707
Cdd:cd17975    1 LPVFKHRESILETLKRHRVVVVAGETGSGKSTQVPQFLLEDLLLNGgtaQKCNIVCTQPRRISAMSLATRVCEELGCESG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  708 SARSHELVGYSVRLDSKCTPLTPLTYVTTGTFLRLLEVGNEIESVTHLIIDEVHERSIDSDLLLIHVLHLLKQHPHLKII 787
Cdd:cd17975   81 PGGKNSLCGYQIRMESRTGEATRLLYCTTGVLLRKLQEDGLLSSISHIIVDEVHERSVQSDFLLIILKEILHKRSDLHLI 160

                        170       180
                 ....*....|....*....|...
gi 19112717  788 IMSATLNAEKFQLYFEGSNLITI 810
Cdd:cd17975  161 LMSATVDCEKFSSYFTHCPILRI 183
DEXHc_DHX30 cd17976
DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an ...
 631-810 2.13e-43

DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an important role in the assembly of the mitochondrial large ribosomal subunit. DHX30 belongs to 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: 350734 [Multi-domain]  Cd Length: 178  Bit Score: 156.11  E-value: 2.13e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  631 LPATMFRETIIDAVNNSQLLIISGDTGCGKSTQIPAFLLENSTKNGKAVK--IYVTEPRRISAISLANRVSQELGgnpPS 708
Cdd:cd17976    1 LPVDSHKESILSAIEQNPVVVISGDTGCGKTTRIPQFILEDYVLRGRGARcnVVITQPRRISAVSVAQRVAHELG---PN 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  709 ARSHelVGYSVRLDSKCTPLT-PLTYVTTGTFLRLLEVGNEIESVTHLIIDEVHERSIDSDLLLIHVLHLLKQHPHLKII 787
Cdd:cd17976   78 LRRN--VGYQVRLESRPPPRGgALLFCTVGVLLKKLQSNPRLEGVSHVIVDEVHERDVNTDFLLILLKGVLQLNPELRVV 155

                        170       180
                 ....*....|....*....|...
gi 19112717  788 IMSATLNAEKFQLYFEGSNLITI 810
Cdd:cd17976  156 LMSATGDNQRLSRYFGGCPVVRV 178
DEXHc_YTHDC2 cd17987
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) ...
 631-810 8.72e-43

DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) regulates mRNA translation and stability via binding to N6-methyladenosine, a modified RNA nucleotide enriched in the stop codons and 3' UTRs of eukaryotic messenger RNAs. YTHDC2 belongs to 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: 350745 [Multi-domain]  Cd Length: 176  Bit Score: 154.22  E-value: 8.72e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  631 LPATMFRETIIDAVNNSQLLIISGDTGCGKSTQIPAFLLENSTKNGKAVKIYVTEPRRISAISLANRVSQELGgnppsAR 710
Cdd:cd17987    1 LPVFEKQEQIVRIIKENKVVLIVGETGSGKTTQIPQFLLDDCYANGIPCRIFCTQPRRLAAIAVAERVAAERG-----EK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  711 SHELVGYSVRLDSKCTPLTPLTYVTTGTFLRLLEVGNE-IESVTHLIIDEVHERSIDSDLLLIHVLHLLKQHPHLKIIIM 789
Cdd:cd17987   76 IGQTVGYQIRLESRVSPKTLLTFCTNGVLLRTLMAGDSaLSTVTHVIVDEVHERDRFSDFLLTKLRDILQKHPNLKLILS 155

                        170       180
                 ....*....|....*....|.
gi 19112717  790 SATLNAEKFQLYFEGSNLITI 810
Cdd:cd17987  156 SAALDVNLFIRYFGSCPVIYI 176
DEXHc_DHX33 cd17978
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA ...
 631-810 9.36e-41

DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA polymerase I transcription of the 47S precursor rRNA. DHX33 belongs to 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: 438710 [Multi-domain]  Cd Length: 178  Bit Score: 148.66  E-value: 9.36e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  631 LPATMFRETIIDAVNNSQLLIISGDTGCGKSTQIPAFLLENSTKNGKAvkIYVTEPRRISAISLANRVSQELGGNPpsar 710
Cdd:cd17978    1 LPIYSARKRLLEELRKHDTVIIIGETGSGKTTQIPQYLYEAGFARGGM--IGITQPRRVAAVSVAKRVAEEMGVEL---- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  711 sHELVGYSVRLDSKCTPLTPLTYVTTGTFLRllevgneiESVTH--------LIIDEVHERSIDSDL------LLIHVLH 776
Cdd:cd17978   75 -GQLVGYSVRFDDVTSEETRIKYMTDGMLLR--------EAIGDpllskysvIILDEAHERTVHTDVlfglvkSAQRRRK 145

                        170       180       190
                 ....*....|....*....|....*....|....
gi 19112717  777 LLKQHPhLKIIIMSATLNAEKFQLYFEGSNLITI 810
Cdd:cd17978  146 EQKLSP-LKVIIMSATLDADLFSEYFNGAPVLYI 178
DEXHc_DHX16 cd17974
DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably ...
 631-810 2.95e-39

DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably involved in pre-mRNA splicing. DHX16 belongs to 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: 350732 [Multi-domain]  Cd Length: 174  Bit Score: 144.18  E-value: 2.95e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  631 LPATMFRETIIDAVNNSQLLIISGDTGCGKSTQIPAFLLENS-TKNGKavKIYVTEPRRISAISLANRVSQELGGnppsa 709
Cdd:cd17974    1 LPVYPYRDDLLAAVKEHQVLIIVGETGSGKTTQIPQYLHEAGyTKGGG--KIGCTQPRRVAAMSVAARVAEEMGV----- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  710 RSHELVGYSVRLDSKCTPLTPLTYVTTGTFLRLLEVGNEIESVTHLIIDEVHERSIDSDLLLIHVLHLLKQHPHLKIIIM 789
Cdd:cd17974   74 KLGNEVGYSIRFEDCTSEKTVLKYMTDGMLLREFLTEPDLASYSVMIIDEAHERTLHTDILFGLVKDIARFRPDLKLLIS 153

                        170       180
                 ....*....|....*....|.
gi 19112717  790 SATLNAEKFQLYFEGSNLITI 810
Cdd:cd17974  154 SATMDAEKFSAFFDDAPIFRI 174
DEXHc_DHX15 cd17973
DEXH-box helicase domain of DEAH-box helicase 15; DEAH-box helicase 15 (DHX15) is a pre-mRNA ...
 628-810 4.06e-39

DEXH-box helicase domain of DEAH-box helicase 15; DEAH-box helicase 15 (DHX15) is a pre-mRNA processing factor involved in disassembly of spliceosomes after the release of mature mRNA. DHX15 belongs to 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: 438709 [Multi-domain]  Cd Length: 187  Bit Score: 144.10  E-value: 4.06e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  628 RNQLPATMFRETIIDAVNNSQLLIISGDTGCGKSTQIPAFLLENSTKNGKAVKIYVTEPRRISAISLANRVSQELggnpp 707
Cdd:cd17973   10 RRELPVWEQKEDFLKLLKNNQILVLVGETGSGKTTQIPQFVLDDELPHQPKKLVACTQPRRVAAMSVAQRVAEEM----- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  708 SARSHELVGYSVRLDSKCTPLTPLTYVTTGTFLRLLEVGNEIESVTHLIIDEVHERSIDSDLLLIHVLHLLKQHPHLKII 787
Cdd:cd17973   85 DVKLGEEVGYSIRFEDCSSAKTILKYMTDGMLLREAMSDPLLSRYSVIILDEAHERTLATDILMGLLKEVVRRRPDLKLI 164

                        170       180
                 ....*....|....*....|...
gi 19112717  788 IMSATLNAEKFQLYFEGSNLITI 810
Cdd:cd17973  165 VMSATLDAGKFQKYFDNAPLLKV 187
DEXHc_DHX34 cd17979
DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in ...
 631-810 1.04e-38

DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in the nonsense-mediated decay (NMD), a surveillance mechanism that degrades aberrant mRNAs. DHX34 belongs to 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: 350737 [Multi-domain]  Cd Length: 170  Bit Score: 142.20  E-value: 1.04e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  631 LPATMFRETIIDAVNNSQLLIISGDTGCGKSTQIPAFLLENSTKNgkavkIYVTEPRRISAISLANRVSQELGGNPPSAr 710
Cdd:cd17979    1 LPIAQYREKIIELLKTHQVVIVAGDTGCGKSTQVPQYLLAAGFRH-----IACTQPRRIACISLAKRVAFESLNQYGSK- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  711 shelVGYSVRLDSKCTPLTPLTYVTTGTFLRLLEVGNEIESVTHLIIDEVHERSIDSDLLLIHVLHLLKQHPHLKIIIMS 790
Cdd:cd17979   75 ----VAYQIRFERTRTLATKLLFLTEGLLLRQIQRDASLPQYNVLILDEVHERHLHGDFLLGVLRCLLRLRPDLKLILMS 150

                        170       180
                 ....*....|....*....|
gi 19112717  791 ATLNAEKFQLYFEGSNLITI 810
Cdd:cd17979  151 ATINIELFSGYFEGAPVVQV 170
DEXHc_DHX8 cd17971
DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as ...
 628-811 3.12e-37

DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as pre-mRNA-splicing factor ATP-dependent RNA helicase PRP22) acts late in the splicing of pre-mRNA and mediates the release of the spliced mRNA from spliceosomes. DHX8 belongs to 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: 350729 [Multi-domain]  Cd Length: 179  Bit Score: 138.38  E-value: 3.12e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  628 RNQLPATMFRETIIDAVNNSQLLIISGDTGCGKSTQIPAFLLENSTKNGKavKIYVTEPRRISAISLANRVSQELGgnpp 707
Cdd:cd17971    3 RESLPIYKLKEQLIQAVHDNQILVVIGETGSGKTTQITQYLAEAGYTSRG--KIGCTQPRRVAAMSVAKRVAEEFG---- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  708 sARSHELVGYSVRLDSKCTPLTPLTYVTTGTFLRLLEVGNEIESVTHLIIDEVHERSIDSDLLLIHVLHLLKQHPHLKII 787
Cdd:cd17971   77 -CCLGQEVGYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLSQYSVIMLDEAHERTIHTDVLFGLLKKTVQKRPDLKLI 155

                        170       180
                 ....*....|....*....|....
gi 19112717  788 IMSATLNAEKFQLYFEGSNLITIP 811
Cdd:cd17971  156 VTSATLDAVKFSQYFYEAPIFTIP 179
DEXHc_TDRD9 cd17988
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ...
 631-802 3.32e-36

DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also known as HIG-1or NET54 or C14orf75) is a part of the nuclear PIWI-interacting RNA (piRNA) pathway essential for transposon silencing and male fertility TDRD9 belongs to 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: 350746 [Multi-domain]  Cd Length: 180  Bit Score: 135.71  E-value: 3.32e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  631 LPATMFRETIIDAVNNSQLLIISGDTGCGKSTQIPAFLLENSTKNGKAVKIYVTEPRRISAISLANRVSQELGgnppsAR 710
Cdd:cd17988    1 LPIYAKREEILSLIEANSVVIIKGATGCGKTTQLPQFILDHYYKRGKYCNIVVTQPRRIAAISIARRVSQERE-----WT 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  711 SHELVGYSVRLDSKCTPLTPLTYVTTGTFLRLLEVGNEIESVTHLIIDEVHERSIDSDLLLIHVLHLLKQHP-HLKIIIM 789
Cdd:cd17988   76 LGSLVGYQVGLERPASEETRLIYCTTGVLLQKLINNKTLTEYTHIILDEVHERDQELDFLLLVVRRLLRTNSrHVKIILM 155

                        170
                 ....*....|...
gi 19112717  790 SATLNAEKFQLYF 802
Cdd:cd17988  156 SATISCKEFADYF 168
DEXHc_DHX35 cd17980
DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and ...
 631-803 1.89e-35

DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and seems to be associated with risk to thyroid cancers. It also has been shown to positively regulate poxviruses, such as Myxoma virus. DEAH-box helicase 35 (DHX35) belongs to 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: 350738 [Multi-domain]  Cd Length: 185  Bit Score: 133.75  E-value: 1.89e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  631 LPATMFRETIIDAVNNSQLLIISGDTGCGKSTQIPAFLLENS-TKNGKAvkIYVTEPRRISAISLANRVSQELGgnppsA 709
Cdd:cd17980    1 LPVFKLRNHILYLVENYQTIVIVGETGCGKSTQIPQYLAEAGwTAGGRV--VGCTQPRRVAAVTVAGRVAEEMG-----A 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  710 RSHELVGYSVRLDSKCTPL-TPLTYVTTGTFLRLLEVGNEIESVTHLIIDEVHERSIDSDLLLIHVLHLLKQHPHLKIII 788
Cdd:cd17980   74 VLGHEVGYCIRFDDCTDPQaTRIKFLTDGMLVREMMLDPLLTKYSVIMLDEAHERTLYTDILIGLLKKIQKKRGDLRLIV 153

                        170
                 ....*....|....*
gi 19112717  789 MSATLNAEKFQLYFE 803
Cdd:cd17980  154 ASATLDAEKFRDFFN 168
DEXHc_DHX37 cd17982
DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the ...
 631-798 1.15e-33

DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the human nervous system and has been linked to schizophrenia. It also negatively regulates poxviruses such as Myxoma virus. DEAH-box helicase 37 (DHX37) belongs to 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: 350740 [Multi-domain]  Cd Length: 191  Bit Score: 128.63  E-value: 1.15e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  631 LPATMFRETIIDAVNNSQLLIISGDTGCGKSTQIPAFLLE---NSTKNGKAVKIYVTEPRRISAISLANRVSQELGGNPp 707
Cdd:cd17982    1 LPILAEEQEIMEAINENPVVIICGETGSGKTTQVPQFLYEagfGSPESDNPGMIGITQPRRVAAVSMAKRVAEELNVFG- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  708 sarshELVGYSVRLDSKCTPLTPLTYVTTGTFLRLLEVGNEIESVTHLIIDEVHERSIDSD----------LLLIHVLHL 777
Cdd:cd17982   80 -----KEVSYQIRYDSTVSENTKIKFMTDGVLLKEIQTDFLLRKYSVIIIDEAHERSVNTDiligmlsrivPLRAKLYLQ 154

                        170       180
                 ....*....|....*....|.
gi 19112717  778 LKQHPHLKIIIMSATLNAEKF 798
Cdd:cd17982  155 DQTVKPLKLVIMSATLRVEDF 175
DEXHc_HrpA cd17989
DEXH-box helicase domain of ATP-dependent RNA helicase HrpA; HrpA is part of the HrpB-HrpA ...
 631-810 1.07e-31

DEXH-box helicase domain of ATP-dependent RNA helicase HrpA; HrpA is part of the HrpB-HrpA two-partner secretion (TPS) system, a secretion pathway important to the secretion of large virulence-associated proteins. HrpA belongs to 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: 350747 [Multi-domain]  Cd Length: 173  Bit Score: 122.56  E-value: 1.07e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  631 LPATMFRETIIDAVNNSQLLIISGDTGCGKSTQIPAFLLEnsTKNGKAVKIYVTEPRRISAISLANRVSQELGGNPpsar 710
Cdd:cd17989    1 LPVSQKRDEIAKAIAENQVVIIAGETGSGKTTQLPKICLE--LGRGIRGLIGHTQPRRLAARSVAERIAEELKTEL---- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  711 sHELVGYSVRLDSKCTPLTPLTYVTTGTFLRLLEVGNEIESVTHLIIDEVHERSIDSDLLLIHVLHLLKQHPHLKIIIMS 790
Cdd:cd17989   75 -GGAVGYKVRFTDQTSDETCVKLMTDGILLAETQTDRYLRAYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKVIITS 153

                        170       180
                 ....*....|....*....|
gi 19112717  791 ATLNAEKFQLYFEGSNLITI 810
Cdd:cd17989  154 ATIDAERFSRHFNNAPIIEV 173
DEXHc_DHX38 cd17983
DEXH-box helicase domain of DEAH-box helicase 38; DEAH-box helicase 38 (DHX38, also known as ...
 631-810 4.57e-30

DEXH-box helicase domain of DEAH-box helicase 38; DEAH-box helicase 38 (DHX38, also known as PRP16) is involved in pre-mRNA splicing. DHX38 belongs to 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: 350741 [Multi-domain]  Cd Length: 173  Bit Score: 117.56  E-value: 4.57e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  631 LPATMFRETIIDAVNNSQLLIISGDTGCGKSTQIPAFLLENS-TKNGKavkIYVTEPRRISAISLANRVSQELGgnppsA 709
Cdd:cd17983    1 LPIFAVRQELLNVIRDNNVVIVVGETGSGKTTQLTQYLHEDGyTDYGM---IGCTQPRRVAAMSVAKRVSEEMG-----V 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  710 RSHELVGYSVRLDSKCTPLTPLTYVTTGTFLRLLEVGNEIESVTHLIIDEVHERSIDSDLLLIHVLHLLKQHPHLKIIIM 789
Cdd:cd17983   73 ELGEEVGYAIRFEDCTSENTVIKYMTDGILLRESLRDPDLDKYSAIIMDEAHERSLNTDVLFGLLREVVARRRDLKLIVT 152

                        170       180
                 ....*....|....*....|.
gi 19112717  790 SATLNAEKFQLYFEGSNLITI 810
Cdd:cd17983  153 SATMDADKFADFFGNVPIFTI 173
DEXHc_HrpB cd17990
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ...
 631-799 1.29e-28

DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA two-partner secretion (TPS) system, a secretion pathway important to the secretion of large virulence-associated proteins. HrpB belongs to 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: 438711 [Multi-domain]  Cd Length: 174  Bit Score: 113.58  E-value: 1.29e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  631 LPATMFRETIIDAVNNSQLLIISGDTGCGKSTQIPAFLLENSTKNGKavKIYVTEPRRISAISLANRVSQELGgnppsAR 710
Cdd:cd17990    1 LPIAAVLPALRAALDAGGQVVLEAPPGAGKTTRVPLALLAELWIAGG--KIIVLEPRRVAARAAARRLATLLG-----EA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  711 SHELVGYSVRLDSKCTPLTPLTYVTTGTFLRLLEVGNEIESVTHLIIDEVHERSIDSDLLLIHVLHLLKQ-HPHLKIIIM 789
Cdd:cd17990   74 PGETVGYRVRGESRVGRRTRVEVVTEGVLLRRLQRDPELSGVGAVILDEFHERSLDADLALALLLEVQQLlRDDLRLLAM 153

                        170
                 ....*....|
gi 19112717  790 SATLNAEKFQ 799
Cdd:cd17990  154 SATLDGDGLA 163
DEXHc_DHX40 cd17984
DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to the ...
 631-810 1.69e-28

DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to 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: 350742 [Multi-domain]  Cd Length: 178  Bit Score: 113.41  E-value: 1.69e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  631 LPATMFRETIIDAVNNSQLLIISGDTGCGKSTQIPAFLLENS-TKNGkavKIYVTEPRRISAISLANRVSQELGgnppsA 709
Cdd:cd17984    1 LPIQKQRKKLVQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGfSQHG---MIGVTQPRRVAAISVAQRVAEEMK-----C 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  710 RSHELVGYSVRLDSKCTPLTPLTYVTTGTFLRLLEVGNEIESVTHLIIDEVHERSIDSDL-----LLIHVLHLLKQHPHL 784
Cdd:cd17984   73 TLGSKVGYQVRFDDCSSKETAIKYMTDGCLLRHILADPNLTKYSVIILDEAHERSLTTDIlfgllKKLFQEKSPNRKEHL 152

                        170       180
                 ....*....|....*....|....*.
gi 19112717  785 KIIIMSATLNAEKFQLYFEGSNLITI 810
Cdd:cd17984  153 KVVVMSATLELAKLSAFFGNCPVFDI 178
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
 1087-1177 1.45e-20

Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in length. It is found is a diverse set of RNA helicases. Its function is unknown, however it seems likely to be involved in nucleic acid binding.


Pssm-ID: 461295 [Multi-domain]  Cd Length: 104  Bit Score: 88.06  E-value: 1.45e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717   1087 ALEKLHQVGALSENEKLTKLGKFLSQLPVDANLGKILVLGCFYKCVDAASSIVAMLTIGSPF-------------RKSVD 1153
Cdd:pfam04408    1 ALELLYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFvqpnfldprsaakAARRR 80

                           90       100
                   ....*....|....*....|....
gi 19112717   1154 NEFSANKARLSFAKENTRSDLVLM 1177
Cdd:pfam04408   81 RRAADEKARAKFARLDLEGDHLTL 104
DEXHc_DHX32 cd17977
DEXH-box helicase domain of DEAH-box helicase 32; DEAH-box helicase 32 (DHX32) belongs to the ...
 631-808 5.97e-20

DEXH-box helicase domain of DEAH-box helicase 32; DEAH-box helicase 32 (DHX32) belongs to 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: 350735 [Multi-domain]  Cd Length: 176  Bit Score: 88.73  E-value: 5.97e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  631 LPATMFRETIIDAVNNSQLLIISGDTGCGKSTQIPA----FLLENSTKNGKAVkiyVTEPRRISAISLANRVSQELGGNP 706
Cdd:cd17977    1 LPVWEAKYEFMESLAHNQIVIVSGDAKTGKSSQIPQwcaeYCLSAHYQHGVVV---CTQVHKQTAVWLALRVADEMDVNI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  707 psarSHElVGYSVRLDSKCTPLTPLTYVTTGTFLRLLEVGNEIESVTHLIIDEVHERSIDSDLLLIHVLHLLKQHPHLKI 786
Cdd:cd17977   78 ----GHE-VGYVIPFENCCTNETILRYCTDDMLLREMMSDPLLESYGVIILDDAHERTVSTDVLLGLLKDVLLSRPELKL 152

                        170       180
                 ....*....|....*....|..
gi 19112717  787 IIMSATLNAEKFQLYFEGSNLI 808
Cdd:cd17977  153 VIITCPHLSSKLLSYYGNVPLI 174
DEXDc smart00487
DEAD-like helicases superfamily;
637-820 1.05e-18

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 86.01  E-value: 1.05e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717     637 RETIIDAVNNSQLLIISGDTGCGKSTQIPAFLLENStKNGKAVKIYVTEPRRISAISLANRVSQELGGNPPSaRSHELVG 716
Cdd:smart00487   14 KEAIEALLSGLRDVILAAPTGSGKTLAALLPALEAL-KRGKGGRVLVLVPTRELAEQWAEELKKLGPSLGLK-VVGLYGG 91

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717     717 YSVRLDSKC--TPLTPLTYVTTGTFLRLLEVGN-EIESVTHLIIDEVHERSiDSDLLLIHVLHLLKQHPHLKIIIMSATL 793
Cdd:smart00487   92 DSKREQLRKleSGKTDILVTTPGRLLDLLENDKlSLSNVDLVILDEAHRLL-DGGFGDQLEKLLKLLPKNVQLLLLSATP 170

                           170       180
                    ....*....|....*....|....*....
gi 19112717     794 --NAEKFQLYFeGSNLITIPGKTYPVHRF 820
Cdd:smart00487  171 peEIENLLELF-LNDPVFIDVGFTPLEPI 198
HA2 smart00847
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ...
 1093-1177 1.29e-17

Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino acid residues in length. It is found is a diverse set of RNA helicases. Its function is unknown, however it seems likely to be involved in nucleic acid binding.


Pssm-ID: 214852 [Multi-domain]  Cd Length: 82  Bit Score: 78.85  E-value: 1.29e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717    1093 QVGALSENEKLTKLGKFLSQLPVDANLGKILVLGCFYKCVDAASSIVAMLTIGSPFRKSVDNEfsANKARLSFAkeNTRS 1172
Cdd:smart00847    1 ELGALDDDGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPRPKEKRED--ADAARRRFA--DPES 76


                    ....*
gi 19112717    1173 DLVLM 1177
Cdd:smart00847   77 DHLTL 81
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
 1266-1349 2.60e-16

Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus of the DEAD-box helicases (pfam00270). In these helicases it is apparently always found in association with pfam04408. There do seem to be a couple of instances where it occurs by itself -. The structure PDB:3i4u adopts an OB-fold. helicases (pfam00270). In these helicases it is apparently always found in association with pfam04408. This C-terminal domain of the yeast helicase contains an oligonucleotide/oligosaccharide-binding (OB)-fold which seems to be placed at the entrance of the putative nucleic acid cavity. It also constitutes the binding site for the G-patch-containing domain of Pfa1p. When found on DEAH/RHA helicases, this domain is central to the regulation of the helicase activity through its binding of both RNA and G-patch domain proteins.


Pssm-ID: 400182 [Multi-domain]  Cd Length: 82  Bit Score: 74.98  E-value: 2.60e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717   1266 LCGVIAASLYPNILRYDYEKRQWSTLSTNKRVRILDVSVNNRSelPNMPSKFVAYTNMMSSTRasEYVNETTMVTLRQLL 1345
Cdd:pfam07717    1 LRAALAAGLYPNVARRDPKGKGYTTLSDNQRVFIHPSSVLFNE--KTFPPEWVVYQELVETTK--VYIRTVTAISPEWLL 76


                   ....
gi 19112717   1346 MMCG 1349
Cdd:pfam07717   77 LFAP 80
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 885-1022 7.81e-16

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: 74.55  E-value: 7.81e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717    885 GLIVYLLKYIFTEGDPKfskcVLVFLPGISEIlrvkslieDMPMFRNHRKFCIYMLHSTLSSAQQQSVFNIPPKGCRKIV 964
Cdd:pfam00271    1 EKLEALLELLKKERGGK----VLIFSQTKKTL--------EAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVL 68

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 19112717    965 LSTNIAETGVTIPDVTCVIDTGVHREMrynsrrhlsrltdtfvskANAKQRSGRAGRV 1022
Cdd:pfam00271   69 VATDVAERGLDLPDVDLVINYDLPWNP------------------ASYIQRIGRAGRA 108
HELICc smart00490
helicase superfamily c-terminal domain;
931-1021 1.36e-15

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 73.01  E-value: 1.36e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717     931 NHRKFCIYMLHSTLSSAQQQSVFNIPPKGCRKIVLSTNIAETGVTIPDVTCVIDtgvhremrynsrrhlsrlTDTFVSKA 1010
Cdd:smart00490    8 KELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVII------------------YDLPWSPA 69

                            90
                    ....*....|.
gi 19112717    1011 NAKQRSGRAGR 1021
Cdd:smart00490   70 SYIQRIGRAGR 80
DEXQc_DQX1 cd17986
DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 ...
 647-791 3.18e-14

DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 (DQX1) belongs to 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: 350744 [Multi-domain]  Cd Length: 177  Bit Score: 72.24  E-value: 3.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  647 SQLLIISGDTGCGKSTQIPAFLLENSTKNGKAV-KIYVTEPRRISAISLANRVSQELGGNppsaRSHElVGYSVRLDSKC 725
Cdd:cd17986   18 SGIVLVSGEPGSGKSTQVPQWCAEFALSRGFQKgQVTVTQPHPLAARSLALRVADEMDLN----LGHE-VGYSIPQEDCT 92

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19112717  726 TPLTPLTYVTTGTFLRLLEVGNEIESVTHLIIDEVHERSIDSDLLLIHVLHLLKQHPHLKIIIMSA 791
Cdd:cd17986   93 GPNTILRFCWDRLLLQEMTSTPLLGAWGVVVLDEAQERSVASDSLLGLLKDVRLQRPELRVVVVTS 158
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
 650-792 9.46e-13

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: 67.04  E-value: 9.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  650 LIISGDTGCGKSTQIPAFLLENSTKNGKavKIYVTEPRRISAISLANRVSQELGgnpPSARSHELVGYS--VRLDSKCTP 727
Cdd:cd00046    4 VLITAPTGSGKTLAALLAALLLLLKKGK--KVLVLVPTKALALQTAERLRELFG---PGIRVAVLVGGSsaEEREKNKLG 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19112717  728 LTPLTYVTTGTFLRLL--EVGNEIESVTHLIIDEVHERSIDSDLLLIHVLHLLKQHPH-LKIIIMSAT 792
Cdd:cd00046   79 DADIIIATPDMLLNLLlrEDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKnAQVILLSAT 146
PHA02653 PHA02653
RNA helicase NPH-II; Provisional
 755-1041 9.76e-10

RNA helicase NPH-II; Provisional


Pssm-ID: 177443 [Multi-domain]  Cd Length: 675  Bit Score: 63.07  E-value: 9.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717   755 LIIDEVHE----------------RSIDSdlllihvlhllkqhphlkIIIMSATL--NAEKFQLYFEGSNLITIPGKT-Y 815
Cdd:PHA02653  295 VIIDEVHEhdqigdiiiavarkhiDKIRS------------------LFLMTATLedDRDRIKEFFPNPAFVHIPGGTlF 356

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717   816 PVHRFYLEdilsqfgNDKSFGNAAgqDVIEEDDyetdqqdasisnksaedaiveMNLIPAwynekainyglivyLLKYIf 895
Cdd:PHA02653  357 PISEVYVK-------NKYNPKNKR--AYIEEEK---------------------KNIVTA--------------LKKYT- 391

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717   896 tegdPKFSKCVLVFLPGISEILRVKSLIEdmpmfRNHRKFCIYMLHSTLSSAQQ--QSVFNiPPKGCrkIVLSTNIAETG 973
Cdd:PHA02653  392 ----PPKGSSGIVFVASVSQCEEYKKYLE-----KRLPIYDFYIIHGKVPNIDEilEKVYS-SKNPS--IIISTPYLESS 459

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19112717   974 VTIPDVTCVIDTG-VHREMRYNSRrhlsrltDTFVSKANAKQRSGRAGRVQEGICYHLFSK-----FKH-DTQFL 1041
Cdd:PHA02653  460 VTIRNATHVYDTGrVYVPEPFGGK-------EMFISKSMRTQRKGRVGRVSPGTYVYFYDLdllkpIKRiDSEFL 527
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 650-796 7.02e-09

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: 56.48  E-value: 7.02e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717    650 LIISGDTGCGKST--QIPAFLLENSTKNGKavKIYVTEPRRisaiSLANRVSQELG--GNPPSARSHELV-GYSVRLDSK 724
Cdd:pfam00270   17 VLVQAPTGSGKTLafLLPALEALDKLDNGP--QALVLAPTR----ELAEQIYEELKklGKGLGLKVASLLgGDSRKEQLE 90

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19112717    725 CTPLTPLTYVTTGTFLRLLEVGNEIESVTHLIIDEVHeRSIDSDLLLIHVLHLLKQHPHLKIIIMSATLNAE 796
Cdd:pfam00270   91 KLKGPDILVGTPGRLLDLLQERKLLKNLKLLVLDEAH-RLLDMGFGPDLEEILRRLPKKRQILLLSATLPRN 161
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
 649-830 1.19e-04

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: 45.88  E-value: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  649 LLIISGDTGCGKsTQIPAFLLENSTKNGKAVKIYVTEPRRISAISLANRVSQELGGNPPSARSHELVGYSVRLDS----K 724
Cdd:cd09639    1 LLVIEAPTGYGK-TEAALLWALHSLKSQKADRVIIALPTRATINAMYRRAKEAFGETGLYHSSILSSRIKEMGDSeefeH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  725 CTPL----------TPLTYVT--------TGTF----LRLLEVGNEIesvthLIIDEVH--ERSIDSDLLLIHVLHLLKQ 780
Cdd:cd09639   80 LFPLyihsndtlflDPITVCTidqvlksvFGEFghyeFTLASIANSL-----LIFDEVHfyDEYTLALILAVLEVLKDND 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 19112717  781 HPHlkiIIMSATL------NAEKFQLYFEGSNLITIPGKTYP-VHRfyLEDILSQFG 830
Cdd:cd09639  155 VPI---LLMSATLpkflkeYAEKIGYVEENEPLDLKPNERAPfIKI--ESDKVGEIS 206
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
 962-1021 3.59e-04

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: 40.38  E-value: 3.59e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  962 KIVLSTNIAETGVTIPDVTCVIDTGVHRemrynsrrhlsrltdtfvSKANAKQRSGRAGR 1021
Cdd:cd18785   24 EILVATNVLGEGIDVPSLDTVIFFDPPS------------------SAASYIQRVGRAGR 65
cas3_core TIGR01587
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ...
 649-824 4.97e-04

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


Pssm-ID: 273707 [Multi-domain]  Cd Length: 359  Bit Score: 43.98  E-value: 4.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717    649 LLIISGDTGCGKsTQIPAFLLENSTKNGKAVKIYVTEPRRISAISLANRVSQELG-GNPPSARSHELVGYSVRLDS---- 723
Cdd:TIGR01587    1 LLVIEAPTGYGK-TEAALLWALHSIKSQKADRVIIALPTRATINAMYRRAKELFGsELVGLHHSSSFSRIKEMGDSeefe 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717    724 KCTPL----------TPLTYVT--------TGTF----LRLLEVGNEIesvthLIIDEVH--ERSIDSDLLLIHVLHLLK 779
Cdd:TIGR01587   80 HLFPLyihsndklflDPITVCTidqvlksvFGEFghyeFTLASIANSL-----LIFDEVHfyDEYTLALILAVLEVLKDN 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 19112717    780 QHPHlkiIIMSATL------NAEKFQLYFEGSNLITIPGKTYPVHRFYLED 824
Cdd:TIGR01587  155 DVPI---LLMSATLpkflkeYAEKIGYVEFNEPLDLKEERRFENHRFILIE 202
DEXHc_viral_Ns3 cd17931
DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional ...
 648-761 5.43e-03

DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional protein found in pestiviruses that contains an N-terminal protease and a C-terminal helicase. The N-terminal domain is a chymotrypsin-like serine protease, which is responsible for most of the maturation cleavages of the polyprotein precursor in the cytosolic side of the endoplasmic reticulum membrane. The C-terminal domain, about two-thirds of NS3, is a helicase belonging to superfamily 2 (SF2) thought to be important for unwinding highly structured regions of the RNA genome during replication. NS3 plays an essential role in viral polyprotein processing and genome replication. NS3 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: 350689 [Multi-domain]  Cd Length: 151  Bit Score: 39.07  E-value: 5.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112717  648 QLLIISGDTGCGKSTQIPAFLLENSTKNGKavKIYVTEPRRISAISLAnrvsQELGGNPPSARSHElvgysvrLDSKCTP 727
Cdd:cd17931    2 QLTVLDLHPGAGKTTRVLPQIIREAIKKRL--RTLVLAPTRVVAAEMY----EALRGLPIRYRTGA-------VKEEHGG 68

                         90       100       110
                 ....*....|....*....|....*....|....
gi 19112717  728 LTPLTYVTTGTFLRLLEVGNEIESVTHLIIDEVH 761
Cdd:cd17931   69 NEIVDYMCHGTFTCRLLSPKRVPNYNLIIMDEAH 102
 
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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