|
Name |
Accession |
Description |
Interval |
E-value |
| HrpA |
COG1643 |
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis]; |
208-702 |
4.76e-101 |
|
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441249 [Multi-domain] Cd Length: 836 Bit Score: 335.51 E-value: 4.76e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 208 SLPIYKQRESILNVLQRDQVLIIKGATGSGKSTQLPQYILEwaAEHRAPVRIVVSQPRRIAAISVSERISKERGEAPGTT 287
Cdd:COG1643 9 DLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLE--LGWGAGGRIGMLEPRRLAARAAAERMAEELGEPVGET 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 288 VGYNIRMNRQCSSNTVLMLTTSGCLLRALAMDKksFFKNTTHLIIDEAHERDLDTDFLL-LAtkLELQKN--PHLRLVLM 364
Cdd:COG1643 87 VGYRVRFEDKVSAATRIEVVTEGILLRELQRDP--ELEGVDTVIFDEFHERSLNADLLLaLL--LDLQPAlrPDLKLLVM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 365 SATMDLEALSNYFGGGTVMDVEGRSFEVSIYHLedilsktgymhPRmekflgkPTGKETPSELLAAyyggnTIVHpdidn 444
Cdd:COG1643 163 SATLDAERFARLLGDAPVIESSGRTYPVEVRYR-----------PL-------PADERDLEDAVAD-----AVRE----- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 445 dlivsllELLLRQGDagaVIVYLPGYSDMTSLLARLESSLPREqiTIIL-LHSQVDNSEQRKVFRTYPGVRLKIILSTNI 523
Cdd:COG1643 215 -------ALAEEPGD---ILVFLPGEREIRRTAEALRGRLPPD--TEILpLYGRLSAAEQDRAFAPAPHGRRRIVLATNI 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 524 GQTSITIPDLLYVIDTGLAKMKTYDSTIDASQLTLTWISQADAKQRAGRAGRVCHGNCYRLYDNDRMARMNLYTIPEIMR 603
Cdd:COG1643 283 AETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERISQASANQRAGRAGRLAPGICYRLWSEEDFARRPAFTDPEILR 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 604 RTLDEICL-LTKLAAPDkkIENFlALaLDTPPKDAVMQSCSRLKLLGVLDERDEVTPLGHIVAELPLGVQIGKCLVYSIY 682
Cdd:COG1643 363 ADLASLILeLAAWGLGD--PEDL-PF-LDPPPARAIADARALLQELGALDADGRLTPLGRALARLPLDPRLARMLLAAAE 438
|
490 500
....*....|....*....|
gi 665392043 683 LRCLDSMIIIAAYHSVRDPF 702
Cdd:COG1643 439 LGCLREAAILAALLSERDPR 458
|
|
| DEAH_box_HrpA |
TIGR01967 |
RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ... |
208-739 |
4.66e-79 |
|
RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ATP-dependent helicases in many Proteobacteria and a few high-GC Gram-positive bacteria. HrpA is about 1300 amino acids long, while its paralog HrpB, also uncharacterized, is about 800 amino acids long. Related characterized eukarotic proteins are RNA helicases associated with pre-mRNA processing. The HrpA/B homolog from Borrelia is 500 amino acids shorter but appears to be derived from HrpA rather than HrpB. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 273900 [Multi-domain] Cd Length: 1283 Bit Score: 281.66 E-value: 4.66e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 208 SLPIYKQRESILNVLQRDQVLIIKGATGSGKSTQLPQYILEWAAEHRApvRIVVSQPRRIAAISVSERISKERGEAPGTT 287
Cdd:TIGR01967 65 NLPVSAKREDIAEAIAENQVVIIAGETGSGKTTQLPKICLELGRGSHG--LIGHTQPRRLAARTVAQRIAEELGTPLGEK 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 288 VGYNIRMNRQCSSNTVLMLTTSGCLLRALAMDKksFFKNTTHLIIDEAHERDLDTDFLLLATKLELQKNPHLRLVLMSAT 367
Cdd:TIGR01967 143 VGYKVRFHDQVSSNTLVKLMTDGILLAETQQDR--FLSRYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKIIITSAT 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 368 MDLEALSNYFGGGTVMDVEGRSFEVSIYHledilsktgymhprmekflgKPTGKETPSEllaayyggntivhpDIDNDLI 447
Cdd:TIGR01967 221 IDPERFSRHFNNAPIIEVSGRTYPVEVRY--------------------RPLVEEQEDD--------------DLDQLEA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 448 VSLLELLLRQGDAGAVIVYLPGYSDMTSLLARLESSLPREqITIILLHSQVDNSEQRKVFRTYPGVRlkIILSTNIGQTS 527
Cdd:TIGR01967 267 ILDAVDELFAEGPGDILIFLPGEREIRDAAEILRKRNLRH-TEILPLYARLSNKEQQRVFQPHSGRR--IVLATNVAETS 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 528 ITIPDLLYVIDTGLAKMKTYDSTIDASQLTLTWISQADAKQRAGRAGRVCHGNCYRLYDNDRMARMNLYTIPEIMRRTLD 607
Cdd:TIGR01967 344 LTVPGIHYVIDTGTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVAPGICIRLYSEEDFNSRPEFTDPEILRTNLA 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 608 EIcLLTKLAAPDKKIENFlaLALDTPPKDAVMQSCSRLKLLGVLDERD---EVTPLGHIVAELPLGVQIGKCLVYSIYLR 684
Cdd:TIGR01967 424 SV-ILQMLALRLGDIAAF--PFIEAPDPRAIRDGFRLLEELGALDDDEaepQLTPIGRQLAQLPVDPRLARMLLEAHRLG 500
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 665392043 685 CLDSMIIIAAYHSVRDPFVLNIERGKKSGQQISRvlFAgDGMSDSLAVIKLYEEF 739
Cdd:TIGR01967 501 CLQEVLIIASALSIQDPRERPMEKQQAADQAHAR--FK-DPRSDFLSRVNLWRHI 552
|
|
| DEXHc_RHA-like |
cd17917 |
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ... |
226-385 |
9.54e-74 |
|
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: 239.67 E-value: 9.54e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 226 QVLIIKGATGSGKSTQLPQYILEWAAEHRAPVRIVVSQPRRIAAISVSERISKERGEAPGTTVGYNIRMNRQCSSNTVLM 305
Cdd:cd17917 2 QVVVIVGETGSGKTTQVPQFLLEDGLAKGGKGRIVCTQPRRIAAISVAERVAEERGEKLGEEVGYQIRFESKTSSKTRIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 306 LTTSGCLLRALAMDkkSFFKNTTHLIIDEAHERDLDTDFLLLATKLELQKNPHLRLVLMSATMDLEALSNYFGGGTVMDV 385
Cdd:cd17917 82 FCTDGILLRELLSD--PLLSGYSHVILDEAHERSLDTDFLLGLLKDLLRKRPDLKVILMSATLDAEKFSSYFGGAPVIHI 159
|
|
| PRK11131 |
PRK11131 |
ATP-dependent RNA helicase HrpA; Provisional |
208-737 |
2.86e-69 |
|
ATP-dependent RNA helicase HrpA; Provisional
Pssm-ID: 182986 [Multi-domain] Cd Length: 1294 Bit Score: 252.29 E-value: 2.86e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 208 SLPIYKQRESILNVLQRDQVLIIKGATGSGKSTQLPQYILEWAAEHRApvRIVVSQPRRIAAISVSERISKERGEAPGTT 287
Cdd:PRK11131 72 NLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLELGRGVKG--LIGHTQPRRLAARTVANRIAEELETELGGC 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 288 VGYNIRMNRQCSSNTVLMLTTSGCLLRALAMDKksFFKNTTHLIIDEAHERDLDTDFLLLATKLELQKNPHLRLVLMSAT 367
Cdd:PRK11131 150 VGYKVRFNDQVSDNTMVKLMTDGILLAEIQQDR--LLMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPDLKVIITSAT 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 368 MDLEALSNYFGGGTVMDVEGRSFEVSIYHledilsktgymhprmekflgKPTGKETpsellaayyggntivhPDIDNDL- 446
Cdd:PRK11131 228 IDPERFSRHFNNAPIIEVSGRTYPVEVRY--------------------RPIVEEA----------------DDTERDQl 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 447 --IVSLLELLLRQGdAGAVIVYLPG---YSDMTSLLARLEssLPREQitIILLHSQVDNSEQRKVFRTYPGVRlkIILST 521
Cdd:PRK11131 272 qaIFDAVDELGREG-PGDILIFMSGereIRDTADALNKLN--LRHTE--ILPLYARLSNSEQNRVFQSHSGRR--IVLAT 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 522 NIGQTSITIPDLLYVIDTGLAKMKTYDSTIDASQLTLTWISQADAKQRAGRAGRVCHGNCYRLYDNDRMARMNLYTIPEI 601
Cdd:PRK11131 345 NVAETSLTVPGIKYVIDPGTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVSEGICIRLYSEDDFLSRPEFTDPEI 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 602 MRRTLDEICL-LTKLAAPDkkIENFlaLALDTPPKDAVMQSCSRLKLLGVLDERD-----EVTPLGHIVAELPLGVQIGK 675
Cdd:PRK11131 425 LRTNLASVILqMTALGLGD--IAAF--PFVEAPDKRNIQDGVRLLEELGAITTDEqasayKLTPLGRQLAQLPVDPRLAR 500
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665392043 676 CLVYSIYLRCLDSMIIIAAYHSVRDPFVLNIERGKKSGQQISRvlFAgDGMSDSLAVIKLYE 737
Cdd:PRK11131 501 MVLEAQKHGCVREVMIITSALSIQDPRERPMDKQQASDEKHRR--FA-DKESDFLAFVNLWN 559
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
214-395 |
2.43e-24 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 101.80 E-value: 2.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 214 QRESILNVLQRDQVLIIKGATGSGKSTQLPQYILEWAAEHRAPvRIVVSQPRRIAAISVSERISKERGEAPGTTV----G 289
Cdd:smart00487 13 QKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGG-RVLVLVPTRELAEQWAEELKKLGPSLGLKVVglygG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 290 YNIRMNRQC--SSNTVLMLTTSGCLLRALAMDKKSfFKNTTHLIIDEAHERdLDTDFLLLATKLELQKNPHLRLVLMSAT 367
Cdd:smart00487 92 DSKREQLRKleSGKTDILVTTPGRLLDLLENDKLS-LSNVDLVILDEAHRL-LDGGFGDQLEKLLKLLPKNVQLLLLSAT 169
|
170 180 190
....*....|....*....|....*....|..
gi 665392043 368 M--DLEALSNYFGGG--TVMDVEGRSFEVSIY 395
Cdd:smart00487 170 PpeEIENLLELFLNDpvFIDVGFTPLEPIEQF 201
|
|
| HA2 |
pfam04408 |
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ... |
645-718 |
2.75e-16 |
|
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: 75.35 E-value: 2.75e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665392043 645 LKLLGVLDERDEVTPLGHIVAELPLGVQIGKCLVYSIYLRCLDSMIIIAAYHSVRDPFVLNIERGKKSGQQISR 718
Cdd:pfam04408 5 LYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPNFLDPRSAAKAAR 78
|
|
| OB_NTP_bind |
pfam07717 |
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ... |
799-884 |
2.03e-09 |
|
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: 54.95 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 799 IRLALTAGLYPKLAYMDRENKNQLVAEGDPLVQVSRSSCLRGKKKQKdlaSEWILFVEKTRTADqiSSLEHTTLVSGLMV 878
Cdd:pfam07717 1 LRAALAAGLYPNVARRDPKGKGYTTLSDNQRVFIHPSSVLFNEKTFP---PEWVVYQELVETTK--VYIRTVTAISPEWL 75
|
....*.
gi 665392043 879 ALAGGK 884
Cdd:pfam07717 76 LLFAPH 81
|
|
| R3H |
pfam01424 |
R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most ... |
67-123 |
3.48e-09 |
|
R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to be binding ssDNA.
Pssm-ID: 460206 Cd Length: 60 Bit Score: 53.65 E-value: 3.48e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 665392043 67 KMLRQLVDDFLQSCEPEKQLPGLTKAQRSHVHRLAQHRGLKTVSKGPEENRVLFISR 123
Cdd:pfam01424 4 EQLAEKLAEFVKDTGKSLELPPMSSYERRIIHELAQKYGLESESEGEEPNRRVVVYK 60
|
|
| R3H |
cd02325 |
R3H domain. The name of the R3H domain comes from the characteristic spacing of the most ... |
64-123 |
1.17e-08 |
|
R3H domain. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. R3H domains are found in proteins together with ATPase domains, SF1 helicase domains, SF2 DEAH helicase domains, Cys-rich repeats, ring-type zinc fingers, and KH domains. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.
Pssm-ID: 100064 Cd Length: 59 Bit Score: 52.23 E-value: 1.17e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 64 EDEKMLRQLVDDFLQScepEKQLPGLTKAQRSHVHRLAQHRGLKTVSKGPEENRVLFISR 123
Cdd:cd02325 3 EREEELEAFAKDAAGK---SLELPPMNSYERKLIHDLAEYYGLKSESEGEGPNRRVVITK 59
|
|
| R3H |
smart00393 |
Putative single-stranded nucleic acids-binding domain; |
57-123 |
9.10e-07 |
|
Putative single-stranded nucleic acids-binding domain;
Pssm-ID: 214647 Cd Length: 79 Bit Score: 47.29 E-value: 9.10e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 57 AGDKLKSEDEKMLRQLVDDFLQ---SCEPEKQLPGLTKAQRSHVHRLAQHRGLKTVSKGPEENRVLFISR 123
Cdd:smart00393 9 DALSYRPRRREELIELELEIARfvkSTKESVELPPMNSYERKIVHELAEKYGLESESFGEGPKRRVVISK 78
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HrpA |
COG1643 |
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis]; |
208-702 |
4.76e-101 |
|
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441249 [Multi-domain] Cd Length: 836 Bit Score: 335.51 E-value: 4.76e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 208 SLPIYKQRESILNVLQRDQVLIIKGATGSGKSTQLPQYILEwaAEHRAPVRIVVSQPRRIAAISVSERISKERGEAPGTT 287
Cdd:COG1643 9 DLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLE--LGWGAGGRIGMLEPRRLAARAAAERMAEELGEPVGET 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 288 VGYNIRMNRQCSSNTVLMLTTSGCLLRALAMDKksFFKNTTHLIIDEAHERDLDTDFLL-LAtkLELQKN--PHLRLVLM 364
Cdd:COG1643 87 VGYRVRFEDKVSAATRIEVVTEGILLRELQRDP--ELEGVDTVIFDEFHERSLNADLLLaLL--LDLQPAlrPDLKLLVM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 365 SATMDLEALSNYFGGGTVMDVEGRSFEVSIYHLedilsktgymhPRmekflgkPTGKETPSELLAAyyggnTIVHpdidn 444
Cdd:COG1643 163 SATLDAERFARLLGDAPVIESSGRTYPVEVRYR-----------PL-------PADERDLEDAVAD-----AVRE----- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 445 dlivsllELLLRQGDagaVIVYLPGYSDMTSLLARLESSLPREqiTIIL-LHSQVDNSEQRKVFRTYPGVRLKIILSTNI 523
Cdd:COG1643 215 -------ALAEEPGD---ILVFLPGEREIRRTAEALRGRLPPD--TEILpLYGRLSAAEQDRAFAPAPHGRRRIVLATNI 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 524 GQTSITIPDLLYVIDTGLAKMKTYDSTIDASQLTLTWISQADAKQRAGRAGRVCHGNCYRLYDNDRMARMNLYTIPEIMR 603
Cdd:COG1643 283 AETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERISQASANQRAGRAGRLAPGICYRLWSEEDFARRPAFTDPEILR 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 604 RTLDEICL-LTKLAAPDkkIENFlALaLDTPPKDAVMQSCSRLKLLGVLDERDEVTPLGHIVAELPLGVQIGKCLVYSIY 682
Cdd:COG1643 363 ADLASLILeLAAWGLGD--PEDL-PF-LDPPPARAIADARALLQELGALDADGRLTPLGRALARLPLDPRLARMLLAAAE 438
|
490 500
....*....|....*....|
gi 665392043 683 LRCLDSMIIIAAYHSVRDPF 702
Cdd:COG1643 439 LGCLREAAILAALLSERDPR 458
|
|
| DEAH_box_HrpA |
TIGR01967 |
RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ... |
208-739 |
4.66e-79 |
|
RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ATP-dependent helicases in many Proteobacteria and a few high-GC Gram-positive bacteria. HrpA is about 1300 amino acids long, while its paralog HrpB, also uncharacterized, is about 800 amino acids long. Related characterized eukarotic proteins are RNA helicases associated with pre-mRNA processing. The HrpA/B homolog from Borrelia is 500 amino acids shorter but appears to be derived from HrpA rather than HrpB. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 273900 [Multi-domain] Cd Length: 1283 Bit Score: 281.66 E-value: 4.66e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 208 SLPIYKQRESILNVLQRDQVLIIKGATGSGKSTQLPQYILEWAAEHRApvRIVVSQPRRIAAISVSERISKERGEAPGTT 287
Cdd:TIGR01967 65 NLPVSAKREDIAEAIAENQVVIIAGETGSGKTTQLPKICLELGRGSHG--LIGHTQPRRLAARTVAQRIAEELGTPLGEK 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 288 VGYNIRMNRQCSSNTVLMLTTSGCLLRALAMDKksFFKNTTHLIIDEAHERDLDTDFLLLATKLELQKNPHLRLVLMSAT 367
Cdd:TIGR01967 143 VGYKVRFHDQVSSNTLVKLMTDGILLAETQQDR--FLSRYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKIIITSAT 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 368 MDLEALSNYFGGGTVMDVEGRSFEVSIYHledilsktgymhprmekflgKPTGKETPSEllaayyggntivhpDIDNDLI 447
Cdd:TIGR01967 221 IDPERFSRHFNNAPIIEVSGRTYPVEVRY--------------------RPLVEEQEDD--------------DLDQLEA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 448 VSLLELLLRQGDAGAVIVYLPGYSDMTSLLARLESSLPREqITIILLHSQVDNSEQRKVFRTYPGVRlkIILSTNIGQTS 527
Cdd:TIGR01967 267 ILDAVDELFAEGPGDILIFLPGEREIRDAAEILRKRNLRH-TEILPLYARLSNKEQQRVFQPHSGRR--IVLATNVAETS 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 528 ITIPDLLYVIDTGLAKMKTYDSTIDASQLTLTWISQADAKQRAGRAGRVCHGNCYRLYDNDRMARMNLYTIPEIMRRTLD 607
Cdd:TIGR01967 344 LTVPGIHYVIDTGTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVAPGICIRLYSEEDFNSRPEFTDPEILRTNLA 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 608 EIcLLTKLAAPDKKIENFlaLALDTPPKDAVMQSCSRLKLLGVLDERD---EVTPLGHIVAELPLGVQIGKCLVYSIYLR 684
Cdd:TIGR01967 424 SV-ILQMLALRLGDIAAF--PFIEAPDPRAIRDGFRLLEELGALDDDEaepQLTPIGRQLAQLPVDPRLARMLLEAHRLG 500
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 665392043 685 CLDSMIIIAAYHSVRDPFVLNIERGKKSGQQISRvlFAgDGMSDSLAVIKLYEEF 739
Cdd:TIGR01967 501 CLQEVLIIASALSIQDPRERPMEKQQAADQAHAR--FK-DPRSDFLSRVNLWRHI 552
|
|
| DEXHc_RHA-like |
cd17917 |
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ... |
226-385 |
9.54e-74 |
|
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: 239.67 E-value: 9.54e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 226 QVLIIKGATGSGKSTQLPQYILEWAAEHRAPVRIVVSQPRRIAAISVSERISKERGEAPGTTVGYNIRMNRQCSSNTVLM 305
Cdd:cd17917 2 QVVVIVGETGSGKTTQVPQFLLEDGLAKGGKGRIVCTQPRRIAAISVAERVAEERGEKLGEEVGYQIRFESKTSSKTRIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 306 LTTSGCLLRALAMDkkSFFKNTTHLIIDEAHERDLDTDFLLLATKLELQKNPHLRLVLMSATMDLEALSNYFGGGTVMDV 385
Cdd:cd17917 82 FCTDGILLRELLSD--PLLSGYSHVILDEAHERSLDTDFLLGLLKDLLRKRPDLKVILMSATLDAEKFSSYFGGAPVIHI 159
|
|
| PRK11131 |
PRK11131 |
ATP-dependent RNA helicase HrpA; Provisional |
208-737 |
2.86e-69 |
|
ATP-dependent RNA helicase HrpA; Provisional
Pssm-ID: 182986 [Multi-domain] Cd Length: 1294 Bit Score: 252.29 E-value: 2.86e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 208 SLPIYKQRESILNVLQRDQVLIIKGATGSGKSTQLPQYILEWAAEHRApvRIVVSQPRRIAAISVSERISKERGEAPGTT 287
Cdd:PRK11131 72 NLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLELGRGVKG--LIGHTQPRRLAARTVANRIAEELETELGGC 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 288 VGYNIRMNRQCSSNTVLMLTTSGCLLRALAMDKksFFKNTTHLIIDEAHERDLDTDFLLLATKLELQKNPHLRLVLMSAT 367
Cdd:PRK11131 150 VGYKVRFNDQVSDNTMVKLMTDGILLAEIQQDR--LLMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPDLKVIITSAT 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 368 MDLEALSNYFGGGTVMDVEGRSFEVSIYHledilsktgymhprmekflgKPTGKETpsellaayyggntivhPDIDNDL- 446
Cdd:PRK11131 228 IDPERFSRHFNNAPIIEVSGRTYPVEVRY--------------------RPIVEEA----------------DDTERDQl 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 447 --IVSLLELLLRQGdAGAVIVYLPG---YSDMTSLLARLEssLPREQitIILLHSQVDNSEQRKVFRTYPGVRlkIILST 521
Cdd:PRK11131 272 qaIFDAVDELGREG-PGDILIFMSGereIRDTADALNKLN--LRHTE--ILPLYARLSNSEQNRVFQSHSGRR--IVLAT 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 522 NIGQTSITIPDLLYVIDTGLAKMKTYDSTIDASQLTLTWISQADAKQRAGRAGRVCHGNCYRLYDNDRMARMNLYTIPEI 601
Cdd:PRK11131 345 NVAETSLTVPGIKYVIDPGTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVSEGICIRLYSEDDFLSRPEFTDPEI 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 602 MRRTLDEICL-LTKLAAPDkkIENFlaLALDTPPKDAVMQSCSRLKLLGVLDERD-----EVTPLGHIVAELPLGVQIGK 675
Cdd:PRK11131 425 LRTNLASVILqMTALGLGD--IAAF--PFVEAPDKRNIQDGVRLLEELGAITTDEqasayKLTPLGRQLAQLPVDPRLAR 500
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665392043 676 CLVYSIYLRCLDSMIIIAAYHSVRDPFVLNIERGKKSGQQISRvlFAgDGMSDSLAVIKLYE 737
Cdd:PRK11131 501 MVLEAQKHGCVREVMIITSALSIQDPRERPMDKQQASDEKHRR--FA-DKESDFLAFVNLWN 559
|
|
| DEAH_box_HrpB |
TIGR01970 |
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ... |
209-669 |
9.71e-66 |
|
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but uncharacterized DEAH-box ATP-dependent helicases in many Proteobacteria, but also in a few species of other lineages. The member from Rhizobium meliloti has been designated HelO. HrpB is typically about 800 residues in length, while its paralog HrpA (TIGR01967), also uncharacterized, is about 1300 amino acids long. Related characterized eukarotic proteins are RNA helicases associated with pre-mRNA processing. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 273901 [Multi-domain] Cd Length: 819 Bit Score: 237.36 E-value: 9.71e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 209 LPIYKQRESILNVLQRDQVLIIKGATGSGKSTQLPQYILEWAAEHRapvRIVVSQPRRIAAISVSERISKERGEAPGTTV 288
Cdd:TIGR01970 1 LPIHAVLPALRDALAAHPQVVLEAPPGAGKSTAVPLALLDAPGIGG---KIIMLEPRRLAARSAAQRLASQLGEAVGQTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 289 GYNIRMNRQCSSNTVLMLTTSGCLLRALAMDKKsfFKNTTHLIIDEAHERDLDTDfLLLATKLELQK--NPHLRLVLMSA 366
Cdd:TIGR01970 78 GYRVRGENKVSRRTRLEVVTEGILTRMIQDDPE--LDGVGALIFDEFHERSLDAD-LGLALALDVQSslREDLKILAMSA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 367 TMDLEALSNYFGGGTVMDVEGRSFEVSIYHLedilsktgymhPRMEKFLGKPTGKETPSELLAAyyggntivhpdidndl 446
Cdd:TIGR01970 155 TLDGERLSSLLPDAPVVESEGRSFPVEIRYL-----------PLRGDQRLEDAVSRAVEHALAS---------------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 447 ivsllelllrqgDAGAVIVYLPGYSDMTSLLARLESSLpREQITIILLHSQVDNSEQRKVFRTYPGVRLKIILSTNIGQT 526
Cdd:TIGR01970 208 ------------ETGSILVFLPGQAEIRRVQEQLAERL-DSDVLICPLYGELSLAAQDRAIKPDPQGRRKVVLATNIAET 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 527 SITIPDLLYVIDTGLAKMKTYDSTIDASQLTLTWISQADAKQRAGRAGRVCHGNCYRLYDNDRMARMNLYTIPEIMRRTL 606
Cdd:TIGR01970 275 SLTIEGIRVVIDSGLARVARFDPKTGITRLETVRISQASATQRAGRAGRLEPGVCYRLWSEEQHQRLPAQDEPEILQADL 354
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665392043 607 DEicLLTKLAAPDKKIENFLALaLDTPPKDAVMQSCSRLKLLGVLDERDEVTPLGHIVAELPL 669
Cdd:TIGR01970 355 SG--LALELAQWGAKDPSDLRW-LDAPPSVALAAARQLLQRLGALDAQGRLTAHGKAMAALGC 414
|
|
| SF2_C_RHA |
cd18791 |
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ... |
390-585 |
7.99e-59 |
|
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: 198.91 E-value: 7.99e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 390 FEVSIYHLEDILSKTGYMhprmekflgkptgketpsellaayyggnTIVHPDIDNDLIVSLLELLLRQGDAGAVIVYLPG 469
Cdd:cd18791 1 FPVEVYYLEDILELLGIS----------------------------SEKEDPDYVDAAVRLILQIHRTEEPGDILVFLPG 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 470 YSDMTSLLARLESSLP---REQITIILLHSQVDNSEQRKVFRTYPGVRLKIILSTNIGQTSITIPDLLYVIDTGLAKMKT 546
Cdd:cd18791 53 QEEIERLCELLREELLspdLGKLLVLPLHSSLPPEEQQRVFEPPPPGVRKVVLATNIAETSITIPGVVYVIDSGLVKEKV 132
|
170 180 190
....*....|....*....|....*....|....*....
gi 665392043 547 YDSTIDASQLTLTWISQADAKQRAGRAGRVCHGNCYRLY 585
Cdd:cd18791 133 YDPRTGLSSLVTVWISKASAEQRAGRAGRTRPGKCYRLY 171
|
|
| PRK11664 |
PRK11664 |
ATP-dependent RNA helicase HrpB; Provisional |
208-667 |
2.16e-55 |
|
ATP-dependent RNA helicase HrpB; Provisional
Pssm-ID: 236950 [Multi-domain] Cd Length: 812 Bit Score: 206.70 E-value: 2.16e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 208 SLPIYKQRESILNVLQRDQVLIIKGATGSGKSTQLPQYILewaAEHRAPVRIVVSQPRRIAAISVSERISKERGEAPGTT 287
Cdd:PRK11664 3 SLPVAAVLPELLTALKTAPQVLLKAPTGAGKSTWLPLQLL---QHGGINGKIIMLEPRRLAARNVAQRLAEQLGEKPGET 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 288 VGYNIRMNRQCSSNTVLMLTTSGCLLRALAMDKKsfFKNTTHLIIDEAHERDLDTDfLLLATKLELQK--NPHLRLVLMS 365
Cdd:PRK11664 80 VGYRMRAESKVGPNTRLEVVTEGILTRMIQRDPE--LSGVGLVILDEFHERSLQAD-LALALLLDVQQglRDDLKLLIMS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 366 ATMDLEALSNYFGGGTVMDVEGRSFEVSI-YHledILSKtgymHPRMEKFLGKPTgketpSELLaayyggntivhpdidn 444
Cdd:PRK11664 157 ATLDNDRLQQLLPDAPVIVSEGRSFPVERrYQ---PLPA----HQRFDEAVARAT-----AELL---------------- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 445 dlivsllelllrQGDAGAVIVYLPGYSDMTSLLARLESSLPrEQITIILLHSQVDNSEQRKVFRTYPGVRLKIILSTNIG 524
Cdd:PRK11664 209 ------------RQESGSLLLFLPGVGEIQRVQEQLASRVA-SDVLLCPLYGALSLAEQQKAILPAPAGRRKVVLATNIA 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 525 QTSITIPDLLYVIDTGLAKMKTYDSTIDASQLTLTWISQADAKQRAGRAGRVCHGNCYRLYDNDRMARMNLYTIPEIMRR 604
Cdd:PRK11664 276 ETSLTIEGIRLVVDSGLERVARFDPKTGLTRLVTQRISQASMTQRAGRAGRLEPGICLHLYSKEQAERAAAQSEPEILHS 355
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665392043 605 TLDEICL-LTKLAAPDKKIENFlalaLDTPPKDAVMQSCSRLKLLGVLDERDEVTPLGHIVAEL 667
Cdd:PRK11664 356 DLSGLLLeLLQWGCHDPAQLSW----LDQPPAAALAAAKRLLQQLGALDGQGRLTARGRKMAAL 415
|
|
| DEXHc_YTHDC2 |
cd17987 |
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) ... |
209-385 |
2.89e-54 |
|
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: 186.57 E-value: 2.89e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 209 LPIYKQRESILNVLQRDQVLIIKGATGSGKSTQLPQYILEWAAEHRAPVRIVVSQPRRIAAISVSERISKERGEAPGTTV 288
Cdd:cd17987 1 LPVFEKQEQIVRIIKENKVVLIVGETGSGKTTQIPQFLLDDCYANGIPCRIFCTQPRRLAAIAVAERVAAERGEKIGQTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 289 GYNIRMNRQCSSNTVLMLTTSGCLLRALaMDKKSFFKNTTHLIIDEAHERDLDTDFLLLATKLELQKNPHLRLVLMSATM 368
Cdd:cd17987 81 GYQIRLESRVSPKTLLTFCTNGVLLRTL-MAGDSALSTVTHVIVDEVHERDRFSDFLLTKLRDILQKHPNLKLILSSAAL 159
|
170
....*....|....*..
gi 665392043 369 DLEALSNYFGGGTVMDV 385
Cdd:cd17987 160 DVNLFIRYFGSCPVIYI 176
|
|
| DEXHc_DHX9 |
cd17972 |
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ... |
195-385 |
4.52e-50 |
|
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: 176.56 E-value: 4.52e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 195 QSNRNRNIQHERRSLPIYKQRESILNVLQRDQVLIIKGATGSGKSTQLPQYILE--WAAEHRAPVRIVVSQPRRIAAISV 272
Cdd:cd17972 45 QDHNLQQILQERELLPVKKFREEILEAISNNPVVIIRGATGCGKTTQVPQYILDdfIQNDRAAECNIVVTQPRRISAVSV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 273 SERISKERGEAPGTTVGYNIRMN----RQCSSntvLMLTTSGCLLRALamdkKSFFKNTTHLIIDEAHERDLDTDFLLLA 348
Cdd:cd17972 125 AERVAFERGEEVGKSCGYSVRFEsvlpRPHAS---ILFCTVGVLLRKL----EAGIRGISHVIVDEIHERDINTDFLLVV 197
|
170 180 190
....*....|....*....|....*....|....*..
gi 665392043 349 TKLELQKNPHLRLVLMSATMDLEALSNYFGGGTVMDV 385
Cdd:cd17972 198 LRDVVQAYPDLRVILMSATIDTSMFCEYFFNCPVIEV 234
|
|
| DEXHc_DHX57 |
cd17985 |
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the ... |
209-385 |
2.80e-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: 172.33 E-value: 2.80e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 209 LPIYKQRESILNVLQRDQVLIIKGATGSGKSTQLPQYILEwAAEHRAP---VRIVVSQPRRIAAISVSERISKERGEAPG 285
Cdd:cd17985 1 LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFILD-NSLQGPPlpvANIICTQPRRISAISVAERVAQERAERVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 286 TTVGYNIRMNRQCSSNTVLMLTTSGCLLRALAMDkkSFFKNTTHLIIDEAHERDLDTDFLLLATKLELQKNPHLRLVLMS 365
Cdd:cd17985 80 QSVGYQIRLESVKSSATRLLYCTTGVLLRRLEGD--PTLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQRPDLKVILMS 157
|
170 180
....*....|....*....|
gi 665392043 366 ATMDLEALSNYFGGGTVMDV 385
Cdd:cd17985 158 ATLNAELFSDYFNSCPVIHI 177
|
|
| DEXHc_TDRD9 |
cd17988 |
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ... |
209-378 |
1.75e-48 |
|
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: 169.99 E-value: 1.75e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 209 LPIYKQRESILNVLQRDQVLIIKGATGSGKSTQLPQYILEWAAEHRAPVRIVVSQPRRIAAISVSERISKERGEAPGTTV 288
Cdd:cd17988 1 LPIYAKREEILSLIEANSVVIIKGATGCGKTTQLPQFILDHYYKRGKYCNIVVTQPRRIAAISIARRVSQEREWTLGSLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 289 GYNIRMNRQCSSNTVLMLTTSGCLLRALAMDKKsfFKNTTHLIIDEAHERDLDTDFLLLATKLELQKNP-HLRLVLMSAT 367
Cdd:cd17988 81 GYQVGLERPASEETRLIYCTTGVLLQKLINNKT--LTEYTHIILDEVHERDQELDFLLLVVRRLLRTNSrHVKIILMSAT 158
|
170
....*....|.
gi 665392043 368 MDLEALSNYFG 378
Cdd:cd17988 159 ISCKEFADYFT 169
|
|
| DEXHc_DHX29 |
cd17975 |
DEXH-box helicase domain of DEAH-box helicase 29; DEAH-box helicase 29 (DHX29) is a part of ... |
209-377 |
6.64e-47 |
|
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: 165.86 E-value: 6.64e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 209 LPIYKQRESILNVLQRDQVLIIKGATGSGKSTQLPQYILE---WAAEHRAPVRIVVSQPRRIAAISVSERISKERG--EA 283
Cdd:cd17975 1 LPVFKHRESILETLKRHRVVVVAGETGSGKSTQVPQFLLEdllLNGGTAQKCNIVCTQPRRISAMSLATRVCEELGceSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 284 PG---TTVGYNIRMNRQCSSNTVLMLTTSGCLLRALAMDkkSFFKNTTHLIIDEAHERDLDTDFLLLATKLELQKNPHLR 360
Cdd:cd17975 81 PGgknSLCGYQIRMESRTGEATRLLYCTTGVLLRKLQED--GLLSSISHIIVDEVHERSVQSDFLLIILKEILHKRSDLH 158
|
170
....*....|....*..
gi 665392043 361 LVLMSATMDLEALSNYF 377
Cdd:cd17975 159 LILMSATVDCEKFSSYF 175
|
|
| DEXHc_DHX33 |
cd17978 |
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA ... |
209-383 |
1.19e-45 |
|
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: 162.14 E-value: 1.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 209 LPIYKQRESILNVLQRDQVLIIKGATGSGKSTQLPQYILEwAAEHRAPVrIVVSQPRRIAAISVSERISKERGEAPGTTV 288
Cdd:cd17978 1 LPIYSARKRLLEELRKHDTVIIIGETGSGKTTQIPQYLYE-AGFARGGM-IGITQPRRVAAVSVAKRVAEEMGVELGQLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 289 GYNIRMNRQCSSNTVLMLTTSGCLLRALAMDkkSFFKNTTHLIIDEAHERDLDTDFLLLATK-----LELQKNPHLRLVL 363
Cdd:cd17978 79 GYSVRFDDVTSEETRIKYMTDGMLLREAIGD--PLLSKYSVIILDEAHERTVHTDVLFGLVKsaqrrRKEQKLSPLKVII 156
|
170 180
....*....|....*....|
gi 665392043 364 MSATMDLEALSNYFGGGTVM 383
Cdd:cd17978 157 MSATLDADLFSEYFNGAPVL 176
|
|
| DEXHc_DHX30 |
cd17976 |
DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an ... |
209-385 |
1.27e-45 |
|
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: 161.88 E-value: 1.27e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 209 LPIYKQRESILNVLQRDQVLIIKGATGSGKSTQLPQYILE-WAAEHR-APVRIVVSQPRRIAAISVSERISKERGEAPGT 286
Cdd:cd17976 1 LPVDSHKESILSAIEQNPVVVISGDTGCGKTTRIPQFILEdYVLRGRgARCNVVITQPRRISAVSVAQRVAHELGPNLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 287 TVGYNIRM-NRQCSSNTVLMLTTSGCLLRALAMDKKsfFKNTTHLIIDEAHERDLDTDFLLLATKLELQKNPHLRLVLMS 365
Cdd:cd17976 81 NVGYQVRLeSRPPPRGGALLFCTVGVLLKKLQSNPR--LEGVSHVIVDEVHERDVNTDFLLILLKGVLQLNPELRVVLMS 158
|
170 180
....*....|....*....|
gi 665392043 366 ATMDLEALSNYFGGGTVMDV 385
Cdd:cd17976 159 ATGDNQRLSRYFGGCPVVRV 178
|
|
| DEXHc_DHX15 |
cd17973 |
DEXH-box helicase domain of DEAH-box helicase 15; DEAH-box helicase 15 (DHX15) is a pre-mRNA ... |
197-385 |
1.49e-44 |
|
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: 159.12 E-value: 1.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 197 NRNRNIQHERRSLPIYKQRESILNVLQRDQVLIIKGATGSGKSTQLPQYILEWAAEHRAPVRIVVSQPRRIAAISVSERI 276
Cdd:cd17973 1 QRYFEILEKRRELPVWEQKEDFLKLLKNNQILVLVGETGSGKTTQIPQFVLDDELPHQPKKLVACTQPRRVAAMSVAQRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 277 SKERGEAPGTTVGYNIRMNRQCSSNTVLMLTTSGCLLRAlAMDKKSFFKNTThLIIDEAHERDLDTDFLLLATKLELQKN 356
Cdd:cd17973 81 AEEMDVKLGEEVGYSIRFEDCSSAKTILKYMTDGMLLRE-AMSDPLLSRYSV-IILDEAHERTLATDILMGLLKEVVRRR 158
|
170 180
....*....|....*....|....*....
gi 665392043 357 PHLRLVLMSATMDLEALSNYFGGGTVMDV 385
Cdd:cd17973 159 PDLKLIVMSATLDAGKFQKYFDNAPLLKV 187
|
|
| DEXHc_DHX36 |
cd17981 |
DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as ... |
209-378 |
3.46e-42 |
|
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: 152.30 E-value: 3.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 209 LPIYKQRESILNVLQRDQVLIIKGATGSGKSTQLPQYILEWAAEH--RAPVRIVVSQPRRIAAISVSERISKERGEAP-- 284
Cdd:cd17981 1 LPSYGMKQEIINMIDNNQVTVISGETGCGKTTQVTQFILDDAIERgkGSSCRIVCTQPRRISAISVAERVAAERAESCgl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 285 GTTVGYNIRMNRQCSSNTVLML-TTSGCLLRALAMDKksFFKNTTHLIIDEAHERDLDTDFLLLATKLELQKNPHLRLVL 363
Cdd:cd17981 81 GNSTGYQIRLESRKPRKQGSILyCTTGIVLQWLQSDP--HLSNVSHLVLDEIHERNLQSDVLMGIVKDLLPFRSDLKVIL 158
|
170
....*....|....*
gi 665392043 364 MSATMDLEALSNYFG 378
Cdd:cd17981 159 MSATLNAEKFSDYFN 173
|
|
| DEXHc_DHX35 |
cd17980 |
DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and ... |
209-377 |
2.20e-41 |
|
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: 149.93 E-value: 2.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 209 LPIYKQRESILNVLQRDQVLIIKGATGSGKSTQLPQYILE--WAAEHRApvrIVVSQPRRIAAISVSERISKERGEAPGT 286
Cdd:cd17980 1 LPVFKLRNHILYLVENYQTIVIVGETGCGKSTQIPQYLAEagWTAGGRV---VGCTQPRRVAAVTVAGRVAEEMGAVLGH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 287 TVGYNIRMNRQCSS-NTVLMLTTSGCLLRALAMDkkSFFKNTTHLIIDEAHERDLDTDFLLLATKLELQKNPHLRLVLMS 365
Cdd:cd17980 78 EVGYCIRFDDCTDPqATRIKFLTDGMLVREMMLD--PLLTKYSVIMLDEAHERTLYTDILIGLLKKIQKKRGDLRLIVAS 155
|
170
....*....|..
gi 665392043 366 ATMDLEALSNYF 377
Cdd:cd17980 156 ATLDAEKFRDFF 167
|
|
| DEXHc_HrpA |
cd17989 |
DEXH-box helicase domain of ATP-dependent RNA helicase HrpA; HrpA is part of the HrpB-HrpA ... |
209-385 |
5.23e-41 |
|
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: 148.37 E-value: 5.23e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 209 LPIYKQRESILNVLQRDQVLIIKGATGSGKSTQLPQYILEWAAEHRApvRIVVSQPRRIAAISVSERISKERGEAPGTTV 288
Cdd:cd17989 1 LPVSQKRDEIAKAIAENQVVIIAGETGSGKTTQLPKICLELGRGIRG--LIGHTQPRRLAARSVAERIAEELKTELGGAV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 289 GYNIRMNRQCSSNTVLMLTTSGCLLRALAMDKksFFKNTTHLIIDEAHERDLDTDFLLLATKLELQKNPHLRLVLMSATM 368
Cdd:cd17989 79 GYKVRFTDQTSDETCVKLMTDGILLAETQTDR--YLRAYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKVIITSATI 156
|
170
....*....|....*..
gi 665392043 369 DLEALSNYFGGGTVMDV 385
Cdd:cd17989 157 DAERFSRHFNNAPIIEV 173
|
|
| DEXHc_DHX34 |
cd17979 |
DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in ... |
209-385 |
1.09e-40 |
|
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: 147.59 E-value: 1.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 209 LPIYKQRESILNVLQRDQVLIIKGATGSGKSTQLPQYILEWAAEHrapvrIVVSQPRRIAAISVSERISKERGEAPGTTV 288
Cdd:cd17979 1 LPIAQYREKIIELLKTHQVVIVAGDTGCGKSTQVPQYLLAAGFRH-----IACTQPRRIACISLAKRVAFESLNQYGSKV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 289 GYNIRMNRQCSSNTVLMLTTSGCLLRALAMDkkSFFKNTTHLIIDEAHERDLDTDFLLLATKLELQKNPHLRLVLMSATM 368
Cdd:cd17979 76 AYQIRFERTRTLATKLLFLTEGLLLRQIQRD--ASLPQYNVLILDEVHERHLHGDFLLGVLRCLLRLRPDLKLILMSATI 153
|
170
....*....|....*..
gi 665392043 369 DLEALSNYFGGGTVMDV 385
Cdd:cd17979 154 NIELFSGYFEGAPVVQV 170
|
|
| DEXHc_DHX40 |
cd17984 |
DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to the ... |
209-385 |
1.74e-40 |
|
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: 147.31 E-value: 1.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 209 LPIYKQRESILNVLQRDQVLIIKGATGSGKSTQLPQYILEWAAEHRApvRIVVSQPRRIAAISVSERISKERGEAPGTTV 288
Cdd:cd17984 1 LPIQKQRKKLVQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGFSQHG--MIGVTQPRRVAAISVAQRVAEEMKCTLGSKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 289 GYNIRMNRQCSSNTVLMLTTSGCLLRALAMDkKSFFKNTThLIIDEAHERDLDTDFLL-LATKLELQKNP----HLRLVL 363
Cdd:cd17984 79 GYQVRFDDCSSKETAIKYMTDGCLLRHILAD-PNLTKYSV-IILDEAHERSLTTDILFgLLKKLFQEKSPnrkeHLKVVV 156
|
170 180
....*....|....*....|..
gi 665392043 364 MSATMDLEALSNYFGGGTVMDV 385
Cdd:cd17984 157 MSATLELAKLSAFFGNCPVFDI 178
|
|
| DEXHc_DHX16 |
cd17974 |
DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably ... |
209-385 |
5.23e-40 |
|
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: 145.72 E-value: 5.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 209 LPIYKQRESILNVLQRDQVLIIKGATGSGKSTQLPQYILEwAAEHRAPVRIVVSQPRRIAAISVSERISKERGEAPGTTV 288
Cdd:cd17974 1 LPVYPYRDDLLAAVKEHQVLIIVGETGSGKTTQIPQYLHE-AGYTKGGGKIGCTQPRRVAAMSVAARVAEEMGVKLGNEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 289 GYNIRMNRQCSSNTVLMLTTSGCLLRAL--AMDKKSFfkntTHLIIDEAHERDLDTDFLLLATKLELQKNPHLRLVLMSA 366
Cdd:cd17974 80 GYSIRFEDCTSEKTVLKYMTDGMLLREFltEPDLASY----SVMIIDEAHERTLHTDILFGLVKDIARFRPDLKLLISSA 155
|
170
....*....|....*....
gi 665392043 367 TMDLEALSNYFGGGTVMDV 385
Cdd:cd17974 156 TMDAEKFSAFFDDAPIFRI 174
|
|
| DEXHc_DHX8 |
cd17971 |
DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as ... |
205-377 |
3.01e-38 |
|
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: 140.70 E-value: 3.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 205 ERRSLPIYKQRESILNVLQRDQVLIIKGATGSGKSTQLPQYILEWAAEHRApvRIVVSQPRRIAAISVSERISKERGEAP 284
Cdd:cd17971 2 QRESLPIYKLKEQLIQAVHDNQILVVIGETGSGKTTQITQYLAEAGYTSRG--KIGCTQPRRVAAMSVAKRVAEEFGCCL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 285 GTTVGYNIRMNRQCSSNTVLMLTTSGCLLRALAMDKKsfFKNTTHLIIDEAHERDLDTDFLLLATKLELQKNPHLRLVLM 364
Cdd:cd17971 80 GQEVGYTIRFEDCTSPETVIKYMTDGMLLRECLIDPD--LSQYSVIMLDEAHERTIHTDVLFGLLKKTVQKRPDLKLIVT 157
|
170
....*....|...
gi 665392043 365 SATMDLEALSNYF 377
Cdd:cd17971 158 SATLDAVKFSQYF 170
|
|
| DEXHc_DHX38 |
cd17983 |
DEXH-box helicase domain of DEAH-box helicase 38; DEAH-box helicase 38 (DHX38, also known as ... |
209-379 |
3.83e-38 |
|
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: 140.29 E-value: 3.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 209 LPIYKQRESILNVLQRDQVLIIKGATGSGKSTQLPQYILEWAAEHRApvRIVVSQPRRIAAISVSERISKERGEAPGTTV 288
Cdd:cd17983 1 LPIFAVRQELLNVIRDNNVVIVVGETGSGKTTQLTQYLHEDGYTDYG--MIGCTQPRRVAAMSVAKRVSEEMGVELGEEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 289 GYNIRMNRQCSSNTVLMLTTSGCLLRALAMDkkSFFKNTTHLIIDEAHERDLDTDFLLLATKLELQKNPHLRLVLMSATM 368
Cdd:cd17983 79 GYAIRFEDCTSENTVIKYMTDGILLRESLRD--PDLDKYSAIIMDEAHERSLNTDVLFGLLREVVARRRDLKLIVTSATM 156
|
170
....*....|.
gi 665392043 369 DLEALSNYFGG 379
Cdd:cd17983 157 DADKFADFFGN 167
|
|
| DEXHc_HrpB |
cd17990 |
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ... |
209-382 |
8.17e-36 |
|
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: 133.61 E-value: 8.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 209 LPIYKQRESILNVLQRDQVLIIKGATGSGKSTQLPQYILEWAAEhrAPVRIVVSQPRRIAAISVSERISKERGEAPGTTV 288
Cdd:cd17990 1 LPIAAVLPALRAALDAGGQVVLEAPPGAGKTTRVPLALLAELWI--AGGKIIVLEPRRVAARAAARRLATLLGEAPGETV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 289 GYNIRMNRQCSSNTVLMLTTSGCLLRALAMDKKsfFKNTTHLIIDEAHERDLDTDfLLLATKLELQK--NPHLRLVLMSA 366
Cdd:cd17990 79 GYRVRGESRVGRRTRVEVVTEGVLLRRLQRDPE--LSGVGAVILDEFHERSLDAD-LALALLLEVQQllRDDLRLLAMSA 155
|
170
....*....|....*.
gi 665392043 367 TMDLEALSNYFGGGTV 382
Cdd:cd17990 156 TLDGDGLAALLPEAPV 171
|
|
| DEXHc_DHX37 |
cd17982 |
DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the ... |
209-371 |
3.12e-34 |
|
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: 129.78 E-value: 3.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 209 LPIYKQRESILNVLQRDQVLIIKGATGSGKSTQLPQYILEWAAEHRAPVR---IVVSQPRRIAAISVSERISKERGeAPG 285
Cdd:cd17982 1 LPILAEEQEIMEAINENPVVIICGETGSGKTTQVPQFLYEAGFGSPESDNpgmIGITQPRRVAAVSMAKRVAEELN-VFG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 286 TTVGYNIRMNRQCSSNTVLMLTTSGCLLRALAMDkksfFKNTTH--LIIDEAHERDLDTDFLL--------LATKLELQK 355
Cdd:cd17982 80 KEVSYQIRYDSTVSENTKIKFMTDGVLLKEIQTD----FLLRKYsvIIIDEAHERSVNTDILIgmlsrivpLRAKLYLQD 155
|
170
....*....|....*...
gi 665392043 356 NPH--LRLVLMSATMDLE 371
Cdd:cd17982 156 QTVkpLKLVIMSATLRVE 173
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
214-395 |
2.43e-24 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 101.80 E-value: 2.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 214 QRESILNVLQRDQVLIIKGATGSGKSTQLPQYILEWAAEHRAPvRIVVSQPRRIAAISVSERISKERGEAPGTTV----G 289
Cdd:smart00487 13 QKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGG-RVLVLVPTRELAEQWAEELKKLGPSLGLKVVglygG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 290 YNIRMNRQC--SSNTVLMLTTSGCLLRALAMDKKSfFKNTTHLIIDEAHERdLDTDFLLLATKLELQKNPHLRLVLMSAT 367
Cdd:smart00487 92 DSKREQLRKleSGKTDILVTTPGRLLDLLENDKLS-LSNVDLVILDEAHRL-LDGGFGDQLEKLLKLLPKNVQLLLLSAT 169
|
170 180 190
....*....|....*....|....*....|..
gi 665392043 368 M--DLEALSNYFGGG--TVMDVEGRSFEVSIY 395
Cdd:smart00487 170 PpeEIENLLELFLNDpvFIDVGFTPLEPIEQF 201
|
|
| DEXHc_DHX32 |
cd17977 |
DEXH-box helicase domain of DEAH-box helicase 32; DEAH-box helicase 32 (DHX32) belongs to the ... |
209-385 |
5.65e-21 |
|
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: 91.04 E-value: 5.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 209 LPIYKQRESILNVLQRDQVLIIKGATGSGKSTQLPQYILEW--AAEHRAPVrIVVSQPRRIAAISVSERISKERGEAPGT 286
Cdd:cd17977 1 LPVWEAKYEFMESLAHNQIVIVSGDAKTGKSSQIPQWCAEYclSAHYQHGV-VVCTQVHKQTAVWLALRVADEMDVNIGH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 287 TVGYNIRMNRQCSSNTVLMLTTSGCLLRALAMDkkSFFKNTTHLIIDEAHERDLDTDFLLLATKLELQKNPHLRLVLMSA 366
Cdd:cd17977 80 EVGYVIPFENCCTNETILRYCTDDMLLREMMSD--PLLESYGVIILDDAHERTVSTDVLLGLLKDVLLSRPELKLVIITC 157
|
170
....*....|....*....
gi 665392043 367 TMDLEALSNYFGGGTVMDV 385
Cdd:cd17977 158 PHLSSKLLSYYGNVPLIEV 176
|
|
| DEXQc_DQX1 |
cd17986 |
DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 ... |
209-385 |
2.97e-19 |
|
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: 86.10 E-value: 2.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 209 LPIYKQRESILNVLQRDQ-VLIIKGATGSGKSTQLPQYILEWAAEHR-APVRIVVSQPRRIAAISVSERISKERGEAPGT 286
Cdd:cd17986 1 LPIWAAKFTFLEQLESPSgIVLVSGEPGSGKSTQVPQWCAEFALSRGfQKGQVTVTQPHPLAARSLALRVADEMDLNLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 287 TVGYNIRMNRQCSSNTVLMLTTSGCLLRALAMDKksFFKNTTHLIIDEAHERDLDTDFLLLATKLELQKNPHLRLVLMSA 366
Cdd:cd17986 81 EVGYSIPQEDCTGPNTILRFCWDRLLLQEMTSTP--LLGAWGVVVLDEAQERSVASDSLLGLLKDVRLQRPELRVVVVTS 158
|
170
....*....|....*....
gi 665392043 367 TMDLEALSNYFGGGTVMDV 385
Cdd:cd17986 159 PALEPKLRAFWGNPPVVHV 177
|
|
| HA2 |
pfam04408 |
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ... |
645-718 |
2.75e-16 |
|
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: 75.35 E-value: 2.75e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665392043 645 LKLLGVLDERDEVTPLGHIVAELPLGVQIGKCLVYSIYLRCLDSMIIIAAYHSVRDPFVLNIERGKKSGQQISR 718
Cdd:pfam04408 5 LYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPNFLDPRSAAKAAR 78
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
228-367 |
8.84e-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: 69.74 E-value: 8.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 228 LIIKGATGSGKSTQLPQyILEWAAEHRAPvRIVVSQPRRIAAISVSERISKERGeaPGTTVGYNIRMNRQCS------SN 301
Cdd:cd00046 4 VLITAPTGSGKTLAALL-AALLLLLKKGK-KVLVLVPTKALALQTAERLRELFG--PGIRVAVLVGGSSAEEreknklGD 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665392043 302 TVLMLTTSGCLLRALAMDKKSFFKNTTHLIIDEAHERDLDTDFLLLATKLELQKNPH-LRLVLMSAT 367
Cdd:cd00046 80 ADIIIATPDMLLNLLLREDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKnAQVILLSAT 146
|
|
| HA2 |
smart00847 |
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ... |
648-733 |
4.54e-13 |
|
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: 65.37 E-value: 4.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 648 LGVLDERDEVTPLGHIVAELPLGVQIGKCLVYSIYLRCLDSMIIIAAYHSVRDPFvlniERGKKSGQQISRVLFAgDGMS 727
Cdd:smart00847 2 LGALDDDGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPR----PKEKREDADAARRRFA-DPES 76
|
....*.
gi 665392043 728 DSLAVI 733
Cdd:smart00847 77 DHLTLL 82
|
|
| PHA02653 |
PHA02653 |
RNA helicase NPH-II; Provisional |
207-591 |
3.11e-12 |
|
RNA helicase NPH-II; Provisional
Pssm-ID: 177443 [Multi-domain] Cd Length: 675 Bit Score: 70.39 E-value: 3.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 207 RSLPIYKQREsILNVLQRDQVLIIKGATGSGKSTQLPQYIL----------EWAAEHR--APVRIVVSQPRRIAAISVSE 274
Cdd:PHA02653 162 ASLQPDVQLK-IFEAWISRKPVVLTGGTGVGKTSQVPKLLLwfnylfggfdNLDKIDPnfIERPIVLSLPRVALVRLHSI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 275 RISKERG--EAPGTTV--GY-----NIRMNRQcsSNTVLMLTTSGCLLRALamdkksffKNTTHLIIDEAHERDLDTDfL 345
Cdd:PHA02653 241 TLLKSLGfdEIDGSPIslKYgsipdELINTNP--KPYGLVFSTHKLTLNKL--------FDYGTVIIDEVHEHDQIGD-I 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 346 LLATkleLQKNPHL--RLVLMSATM--DLEALSNYFGGGTVMDVEGRS-FEVS-IYHLEDILSKTGYMHPRMEKflgkpt 419
Cdd:PHA02653 310 IIAV---ARKHIDKirSLFLMTATLedDRDRIKEFFPNPAFVHIPGGTlFPISeVYVKNKYNPKNKRAYIEEEK------ 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 420 gketpsellaayyggntivhPDIDNDLivslLELLLRQGDAGavIVYLPGYSDMTSLLARLESSLPREQITIIllHSQVD 499
Cdd:PHA02653 381 --------------------KNIVTAL----KKYTPPKGSSG--IVFVASVSQCEEYKKYLEKRLPIYDFYII--HGKVP 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 500 NSEQ--RKVfrtYPGVRLKIILSTNIGQTSITIPDLLYVIDTGlakmKTY-DSTIDASQltlTWISQADAKQRAGRAGRV 576
Cdd:PHA02653 433 NIDEilEKV---YSSKNPSIIISTPYLESSVTIRNATHVYDTG----RVYvPEPFGGKE---MFISKSMRTQRKGRVGRV 502
|
410
....*....|....*
gi 665392043 577 CHGNCYRLYDNDRMA 591
Cdd:PHA02653 503 SPGTYVYFYDLDLLK 517
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
479-575 |
7.47e-12 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 61.84 E-value: 7.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 479 RLESSLPREQITIILLHSQVDNSEQRKVFRTYPGVRLKIILSTNIGQTSITIPDLLYVIDTGLakmktydstidasqltl 558
Cdd:smart00490 2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDL----------------- 64
|
90
....*....|....*..
gi 665392043 559 tWISQADAKQRAGRAGR 575
Cdd:smart00490 65 -PWSPASYIQRIGRAGR 80
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
214-369 |
1.97e-10 |
|
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: 60.33 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 214 QRESILNVLQRDQVLIIkGATGSGKST--QLPqyILEWAAEHRAPVRIVVSQPRRIAAISVSERIsKERGEAPGTTV--- 288
Cdd:pfam00270 4 QAEAIPAILEGRDVLVQ-APTGSGKTLafLLP--ALEALDKLDNGPQALVLAPTRELAEQIYEEL-KKLGKGLGLKVasl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 289 --GYNIRMNRQCSSNTVLMLTTSGCLLRALamDKKSFFKNTTHLIIDEAHeRDLDTDFLLLATKLELQKNPHLRLVLMSA 366
Cdd:pfam00270 80 lgGDSRKEQLEKLKGPDILVGTPGRLLDLL--QERKLLKNLKLLVLDEAH-RLLDMGFGPDLEEILRRLPKKRQILLLSA 156
|
...
gi 665392043 367 TMD 369
Cdd:pfam00270 157 TLP 159
|
|
| OB_NTP_bind |
pfam07717 |
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ... |
799-884 |
2.03e-09 |
|
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: 54.95 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 799 IRLALTAGLYPKLAYMDRENKNQLVAEGDPLVQVSRSSCLRGKKKQKdlaSEWILFVEKTRTADqiSSLEHTTLVSGLMV 878
Cdd:pfam07717 1 LRAALAAGLYPNVARRDPKGKGYTTLSDNQRVFIHPSSVLFNEKTFP---PEWVVYQELVETTK--VYIRTVTAISPEWL 75
|
....*.
gi 665392043 879 ALAGGK 884
Cdd:pfam07717 76 LLFAPH 81
|
|
| R3H |
pfam01424 |
R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most ... |
67-123 |
3.48e-09 |
|
R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to be binding ssDNA.
Pssm-ID: 460206 Cd Length: 60 Bit Score: 53.65 E-value: 3.48e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 665392043 67 KMLRQLVDDFLQSCEPEKQLPGLTKAQRSHVHRLAQHRGLKTVSKGPEENRVLFISR 123
Cdd:pfam01424 4 EQLAEKLAEFVKDTGKSLELPPMSSYERRIIHELAQKYGLESESEGEEPNRRVVVYK 60
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
461-576 |
1.08e-08 |
|
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: 53.75 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 461 GAVIVYLPGYSdmtslLARLESSLPREQITIILLHSQVDNSEQRKVFRTYPGVRLKIILSTNIGQTSITIPDLLYVIDtg 540
Cdd:pfam00271 16 GKVLIFSQTKK-----TLEAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDLVIN-- 88
|
90 100 110
....*....|....*....|....*....|....*.
gi 665392043 541 lakmktYDSTIDASQLtltwisqadaKQRAGRAGRV 576
Cdd:pfam00271 89 ------YDLPWNPASY----------IQRIGRAGRA 108
|
|
| R3H |
cd02325 |
R3H domain. The name of the R3H domain comes from the characteristic spacing of the most ... |
64-123 |
1.17e-08 |
|
R3H domain. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. R3H domains are found in proteins together with ATPase domains, SF1 helicase domains, SF2 DEAH helicase domains, Cys-rich repeats, ring-type zinc fingers, and KH domains. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.
Pssm-ID: 100064 Cd Length: 59 Bit Score: 52.23 E-value: 1.17e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 64 EDEKMLRQLVDDFLQScepEKQLPGLTKAQRSHVHRLAQHRGLKTVSKGPEENRVLFISR 123
Cdd:cd02325 3 EREEELEAFAKDAAGK---SLELPPMNSYERKLIHDLAEYYGLKSESEGEGPNRRVVITK 59
|
|
| R3H |
smart00393 |
Putative single-stranded nucleic acids-binding domain; |
57-123 |
9.10e-07 |
|
Putative single-stranded nucleic acids-binding domain;
Pssm-ID: 214647 Cd Length: 79 Bit Score: 47.29 E-value: 9.10e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 57 AGDKLKSEDEKMLRQLVDDFLQ---SCEPEKQLPGLTKAQRSHVHRLAQHRGLKTVSKGPEENRVLFISR 123
Cdd:smart00393 9 DALSYRPRRREELIELELEIARfvkSTKESVELPPMNSYERKIVHELAEKYGLESESFGEGPKRRVVISK 78
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
214-533 |
1.61e-06 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 51.95 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 214 QRESILNVL----QRDQVLIIKGATGSGKSTqlpqYILEWAAEHRAPVRIVVSQPRRIAAISVSERISKERGEAPGttVG 289
Cdd:COG1061 85 QQEALEALLaaleRGGGRGLVVAPTGTGKTV----LALALAAELLRGKRVLVLVPRRELLEQWAEELRRFLGDPLA--GG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 290 YNIRMNRQCssnTVLMLTTsgcLLRALAMDKksFFKNTTHLIIDEAHerdldtdfLLLATKLE--LQKNPHLRLVLMSAT 367
Cdd:COG1061 159 GKKDSDAPI---TVATYQS---LARRAHLDE--LGDRFGLVIIDEAH--------HAGAPSYRriLEAFPAAYRLGLTAT 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 368 ---MD-LEALSNYFgggtvmdvEGRSFEVSIYHL--EDILSKTGYmHPRMEKFLGKPTGKETPSELLAayyggNTIVHPD 441
Cdd:COG1061 223 pfrSDgREILLFLF--------DGIVYEYSLKEAieDGYLAPPEY-YGIRVDLTDERAEYDALSERLR-----EALAADA 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 442 IDNDLIVSllELLLRQGDAGAVIVYLPGysdmTSLLARLESSLPREQITIILLHSQVDNSEQRKVFRTYPGVRLKIILST 521
Cdd:COG1061 289 ERKDKILR--ELLREHPDDRKTLVFCSS----VDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTV 362
|
330
....*....|..
gi 665392043 522 NIGQTSITIPDL 533
Cdd:COG1061 363 DVLNEGVDVPRL 374
|
|
| DEXHc_viral_Ns3 |
cd17931 |
DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional ... |
226-367 |
5.76e-06 |
|
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: 47.16 E-value: 5.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 226 QVLIIKGATGSGKSTQLPQYILEWAAEHRapVRIVVSQPRRIAAISVSERIskeRGEAPgttvgyNIR---MNRQCSSNT 302
Cdd:cd17931 2 QLTVLDLHPGAGKTTRVLPQIIREAIKKR--LRTLVLAPTRVVAAEMYEAL---RGLPI------RYRtgaVKEEHGGNE 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665392043 303 VLMLTTSGCLLRALAMDKKSffKNTTHLIIDEAHERDlDTDFLLLATKLELQKNPHLRLVLMSAT 367
Cdd:cd17931 71 IVDYMCHGTFTCRLLSPKRV--PNYNLIIMDEAHFTD-PASIAARGYIHTRVEMGEAAVIFMTAT 132
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
210-384 |
3.45e-05 |
|
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: 45.66 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 210 PIykQRESILNVLQRDQVLIIkGATGSGK--STQLPqyILEWAAEHR----------APVRIVVSQ------------PR 265
Cdd:cd17957 15 PI--QMQAIPILLHGRDLLAC-APTGSGKtlAFLIP--ILQKLGKPRkkkglralilAPTRELASQiyrellklskgtGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 266 RIAAISVSERISKERGEAPGTtvGYNIrmnrqcssntvlMLTTSGCLLRALAMDKKSFfKNTTHLIIDEAhERDLDTDFL 345
Cdd:cd17957 90 RIVLLSKSLEAKAKDGPKSIT--KYDI------------LVSTPLRLVFLLKQGPIDL-SSVEYLVLDEA-DKLFEPGFR 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 665392043 346 -LLATKLELQKNPHLRLVLMSATM--DLEALSNyfgggTVMD 384
Cdd:cd17957 154 eQTDEILAACTNPNLQRSLFSATIpsEVEELAR-----SVMK 190
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
514-575 |
8.87e-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: 38.84 E-value: 8.87e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665392043 514 RLKIILSTNIGQTSITIPDLLYVIDTGlakmktydstidasqltlTWISQADAKQRAGRAGR 575
Cdd:cd18785 22 SLEILVATNVLGEGIDVPSLDTVIFFD------------------PPSSAASYIQRVGRAGR 65
|
|
| R3H_NRF |
cd02640 |
R3H domain of the NF-kappaB-repression factor (NRF). NRF is a nuclear inhibitor of NF-kappaB ... |
70-123 |
9.49e-04 |
|
R3H domain of the NF-kappaB-repression factor (NRF). NRF is a nuclear inhibitor of NF-kappaB proteins that can silence the IFNbeta promoter via binding to a negative regulatory element (NRE). Beside R3H NRF also contains a G-patch domain. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.
Pssm-ID: 100069 Cd Length: 60 Bit Score: 38.15 E-value: 9.49e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 665392043 70 RQLVDDFLQScEPEKQL---PGLTKAQRSHVHRLAQHRGLKTVSKGPEENRVLFISR 123
Cdd:cd02640 5 RQIIQNYAHS-DDIRDMvfsPEFSKEERALIHQIAQKYGLKSRSYGSGNDRYLVISK 60
|
|
| R3H_DEXH_helicase |
cd06007 |
R3H domain of a group of proteins which also contain a DEXH-box helicase domain, and may ... |
73-123 |
4.25e-03 |
|
R3H domain of a group of proteins which also contain a DEXH-box helicase domain, and may function as ATP-dependent DNA or RNA helicases. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.
Pssm-ID: 100077 Cd Length: 59 Bit Score: 36.52 E-value: 4.25e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 665392043 73 VDDFLQSCEPEKQLP-GLTKAQRSHVHRLAQHRGLKTVSKGPEENRVLFISR 123
Cdd:cd06007 8 LEDFRASDNEEYEFPsSLTNHERAVIHRLCRKLGLKSKSKGKGSNRRLSVYK 59
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| R3H_Smubp-2_like |
cd02641 |
R3H domain of Smubp-2_like proteins. Smubp-2_like proteins also contain a helicase_like and ... |
67-123 |
7.02e-03 |
|
R3H domain of Smubp-2_like proteins. Smubp-2_like proteins also contain a helicase_like and an AN1-like Zinc finger domain and have been shown to bind single-stranded DNA. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA.
Pssm-ID: 100070 Cd Length: 60 Bit Score: 35.79 E-value: 7.02e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392043 67 KMLRQLVDDFLQSCEPEkQL---PGLTKAQRSHVHRLAQHRGLKTVSKGPEENRVLFISR 123
Cdd:cd02641 2 KHLKAMVKAFMKDPKAT-ELefpPTLSSHDRLLVHELAEELGLRHESTGEGSDRVITVSK 60
|
|
| R3H_NF-X1 |
cd02643 |
R3H domain of the X1 box binding protein (NF-X1) and related proteins. Human NF-X1 is a ... |
66-117 |
7.30e-03 |
|
R3H domain of the X1 box binding protein (NF-X1) and related proteins. Human NF-X1 is a transcription factor that regulates the expression of class II major histocompatibility complex (MHC) genes. The Drosophila homolog shuttle craft (STC) has been shown to be a DNA- or RNA-binding protein required for proper axon guidance in the central nervous system and, the yeast homolog FAP1 encodes a dosage suppressor of rapamycin toxicity. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.
Pssm-ID: 100072 Cd Length: 74 Bit Score: 36.18 E-value: 7.30e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 665392043 66 EKMLRQLVDDFLQSCEPEKQ--LPGLTKAQRSHVHRLAQHRGLKTVSKGPEENR 117
Cdd:cd02643 15 EKDLIELVESVNKGKQTSRShsFPPMNREKRRIVHELAEHFGIESVSYDQEPKR 68
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|
| AAA_19 |
pfam13245 |
AAA domain; |
214-279 |
8.06e-03 |
|
AAA domain;
Pssm-ID: 433059 [Multi-domain] Cd Length: 136 Bit Score: 37.58 E-value: 8.06e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665392043 214 QRESILNVLQRDQVLIIKGAtGSGKSTQLPQYILEWAAEHRAPVRIVVSQPRRIAAISVSERISKE 279
Cdd:pfam13245 1 QREAVRTALPSKVVLLTGGP-GTGKTTTIRHIVALLVALGGVSFPILLAAPTGRAAKRLSERTGLP 65
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