|
Name |
Accession |
Description |
Interval |
E-value |
| HrpA |
COG1643 |
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis]; |
316-943 |
1.47e-120 |
|
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441249 [Multi-domain] Cd Length: 836 Bit Score: 392.14 E-value: 1.47e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 316 LPAWEERETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSLnGPPERvanIICTQPRRISAISVAERVAKERAERVGL 395
Cdd:COG1643 10 LPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGW-GAGGR---IGMLEPRRLAARAAAERMAEELGEPVGE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 396 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIvmQRAT---LQVILMS 472
Cdd:COG1643 86 TVGYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDL--QPALrpdLKLLVMS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 473 ATLDAGLFSKYFSYCPVITIPGRAFPVDqffledalavTRYvlqdgspymrsmkqiakeklkarhnrtaqeeveedLRLS 552
Cdd:COG1643 164 ATLDAERFARLLGDAPVIESSGRTYPVE----------VRY-----------------------------------RPLP 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 553 LHLQDEEESVKDTIpdqqldfkqllirykgvsksviktmsvmdfekvnlelIEALLEwivdgkhayPPGAVLVFLPGLAE 632
Cdd:COG1643 199 ADERDLEDAVADAV-------------------------------------REALAE---------EPGDILVFLPGERE 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 633 IKMLYEQLQsnslfnNRRSHRCVIHPLHSSLSSEEQQAVFVKPPMGVTKIIISTNIAETSITIDDVVYVIDSGKMKEKRY 712
Cdd:COG1643 233 IRRTAEALR------GRLPPDTEILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRY 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 713 DAGKGMESLEDTFVSQANALQRKGRAGRVASGVCFHLFTSHHYNhQLLKQQLPEIQRVPLEQLclrikILEMFS--THNL 790
Cdd:COG1643 307 DPRSGVTRLPTERISQASANQRAGRAGRLAPGICYRLWSEEDFA-RRPAFTDPEILRADLASL-----ILELAAwgLGDP 380
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 791 QSVfsRLIEPPHIDSLRASKVRLRDLGALTPDEKLTPLGYHLASLPVDVRIGKLMLLGSIFRCLDPALTIAASLAFKSPF 870
Cdd:COG1643 381 EDL--PFLDPPPARAIADARALLQELGALDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDPR 458
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720388776 871 VSPwdkkeeanqkklefafANSDYLALLcayKGWQlstkesaraSYNYCRQNFLSGRTLQEMASLKRQFTELL 943
Cdd:COG1643 459 RGA----------------AGSDLLARL---NLWR---------RLREQQREFLSYLRLREWRDLARQLRRLL 503
|
|
| DEXHc_DHX57 |
cd17985 |
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the ... |
316-492 |
2.78e-110 |
|
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: 341.43 E-value: 2.78e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 316 LPAWEERETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSLNGPPERVANIICTQPRRISAISVAERVAKERAERVGL 395
Cdd:cd17985 1 LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFILDNSLQGPPLPVANIICTQPRRISAISVAERVAQERAERVGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 396 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIVMQRATLQVILMSATL 475
Cdd:cd17985 81 SVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDPTLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQRPDLKVILMSATL 160
|
170
....*....|....*..
gi 1720388776 476 DAGLFSKYFSYCPVITI 492
Cdd:cd17985 161 NAELFSDYFNSCPVIHI 177
|
|
| PRK11131 |
PRK11131 |
ATP-dependent RNA helicase HrpA; Provisional |
314-948 |
4.52e-77 |
|
ATP-dependent RNA helicase HrpA; Provisional
Pssm-ID: 182986 [Multi-domain] Cd Length: 1294 Bit Score: 278.48 E-value: 4.52e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 314 QLLPAWEERETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSLNgppeRVANIICTQPRRISAISVAERVAKERAERV 393
Cdd:PRK11131 71 ENLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLELGRG----VKGLIGHTQPRRLAARTVANRIAEELETEL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 394 GLTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIVMQRATLQVILMSA 473
Cdd:PRK11131 147 GGCVGYKVRFNDQVSDNTMVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPDLKVIITSA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 474 TLDAGLFSKYFSYCPVITIPGRAFPVDqffledalavTRYvlqdgspymrsmkqiakeklkarhnRTAQEEVEedlrlsl 553
Cdd:PRK11131 227 TIDPERFSRHFNNAPIIEVSGRTYPVE----------VRY-------------------------RPIVEEAD------- 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 554 hlqdeeesvkDTIPDQqldfkqllirykgvsksviktmsvmdfekvnlelIEALLEwIVDGKHAYPPGAVLVFLPGLAEI 633
Cdd:PRK11131 265 ----------DTERDQ----------------------------------LQAIFD-AVDELGREGPGDILIFMSGEREI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 634 KMLYEQLQSNSLFNNRrshrcvIHPLHSSLSSEEQQAVFvkPPMGVTKIIISTNIAETSITIDDVVYVIDSGKMKEKRYD 713
Cdd:PRK11131 300 RDTADALNKLNLRHTE------ILPLYARLSNSEQNRVF--QSHSGRRIVLATNVAETSLTVPGIKYVIDPGTARISRYS 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 714 AGKGMESLEDTFVSQANALQRKGRAGRVASGVCFHLFTSHHYNHqllKQQL--PEIQRVPLEQLclrikILEMFSThNLQ 791
Cdd:PRK11131 372 YRTKVQRLPIEPISQASANQRKGRCGRVSEGICIRLYSEDDFLS---RPEFtdPEILRTNLASV-----ILQMTAL-GLG 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 792 --SVFSrLIEPP---HI-DSLRAskvrLRDLGALTPDE-----KLTPLGYHLASLPVDVRIGKLMLLGSIFRCLDPALTI 860
Cdd:PRK11131 443 diAAFP-FVEAPdkrNIqDGVRL----LEELGAITTDEqasayKLTPLGRQLAQLPVDPRLARMVLEAQKHGCVREVMII 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 861 AASLAFKSPFVSPWDKKEEANQKKLEFAFANSDYLALLcayKGWQ-LSTKESARASYNY---CRQNFLSGRTLQEMASLK 936
Cdd:PRK11131 518 TSALSIQDPRERPMDKQQASDEKHRRFADKESDFLAFV---NLWNyLQEQQKALSSNQFrrlCRTDYLNYLRVREWQDIY 594
|
650
....*....|..
gi 1720388776 937 RQFTELLSDIGF 948
Cdd:PRK11131 595 TQLRQVVKELGI 606
|
|
| DEAH_box_HrpB |
TIGR01970 |
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ... |
315-864 |
7.87e-76 |
|
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: 268.17 E-value: 7.87e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 315 LLPAweeretILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSLNGppervANIICTQPRRISAISVAERVAKERAERVG 394
Cdd:TIGR01970 6 VLPA------LRDALAAHPQVVLEAPPGAGKSTAVPLALLDAPGIG-----GKIIMLEPRRLAARSAAQRLASQLGEAVG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 395 LTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIVMQ-RATLQVILMSA 473
Cdd:TIGR01970 75 QTVGYRVRGENKVSRRTRLEVVTEGILTRMIQDDPELDGVGALIFDEFHERSLDADLGLALALDVQSSlREDLKILAMSA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 474 TLDAGLFSKYFSYCPVITIPGRAFPVDqffledalavTRYvlqdgspymrsmkqiakeklkarhnRTAQeeveedlrlsl 553
Cdd:TIGR01970 155 TLDGERLSSLLPDAPVVESEGRSFPVE----------IRY-------------------------LPLR----------- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 554 hlqdeeesvkdtiPDQQLDfkqllirykgvsksviktmsvmdfEKVNLELIEALlewivdgkhAYPPGAVLVFLPGLAEI 633
Cdd:TIGR01970 189 -------------GDQRLE------------------------DAVSRAVEHAL---------ASETGSILVFLPGQAEI 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 634 KMLYEQLQSnslfnnRRSHRCVIHPLHSSLSSEEQQAVFVKPPMGVTKIIISTNIAETSITIDDVVYVIDSGKMKEKRYD 713
Cdd:TIGR01970 223 RRVQEQLAE------RLDSDVLICPLYGELSLAAQDRAIKPDPQGRRKVVLATNIAETSLTIEGIRVVIDSGLARVARFD 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 714 AGKGMESLEDTFVSQANALQRKGRAGRVASGVCFHLFtSHHYNHQLLKQQLPEIQRVPLEQLCLRIKILEMFSTHNLqsv 793
Cdd:TIGR01970 297 PKTGITRLETVRISQASATQRAGRAGRLEPGVCYRLW-SEEQHQRLPAQDEPEILQADLSGLALELAQWGAKDPSDL--- 372
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720388776 794 fsRLIEPPHIDSLRASKVRLRDLGALTPDEKLTPLGYHLASLPVDVRIGKLMLLGSIFRCLDPALTIAASL 864
Cdd:TIGR01970 373 --RWLDAPPSVALAAARQLLQRLGALDAQGRLTAHGKAMAALGCHPRLAAMLLSAHSTGLAALACDLAALL 441
|
|
| RWD_DHX57 |
cd23825 |
RWD domain of DEAH box protein 57 (DHX57) and related proteins; DHX57 (EC 3.6.4.13) is a ... |
14-196 |
1.51e-48 |
|
RWD domain of DEAH box protein 57 (DHX57) and related proteins; DHX57 (EC 3.6.4.13) is a putative ATP-dependent RNA helicase. A genome-wide association study (GWAS) of cerebellar epigenetic age acceleration identified significant SNPs (single nucleotide polymorphisms) in a loci 2p22.1 inside the DHX57 gene, suggesting that variants in DHX57 are associated with epigenetic age in the cerebellum.
Pssm-ID: 467661 Cd Length: 115 Bit Score: 168.14 E-value: 1.51e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 14 ECVEQRQEETLALKSICGEKFIERIQNRVWTIGLELDYLTNkfckskqkessknvrdtspetckfylkgnckfgskckfk 93
Cdd:cd23825 2 ELLEQRQEEAMALESIYGEAFSERIPNKVWTIKLDLPYLPW--------------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 94 hevpphqmigraernvndphldadddttfmYELQIRFSKDHKYPYQAPLVAFYSTNENLPLACRLHISEFLYGKALEFAK 173
Cdd:cd23825 43 ------------------------------FELEIRFPKGNKYPYEPPIVAFSSTNENFPKAVCLNITERLMEEALELAE 92
|
170 180
....*....|....*....|...
gi 1720388776 174 TSEPVVYSLITLLEEESEIVKLL 196
Cdd:cd23825 93 DGEPVVFSLVSLLEDEEEILELL 115
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
322-502 |
3.59e-24 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 101.41 E-value: 3.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 322 RETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSLNGPPERVaniICTQPRRISAISVAERVAKE----RAERVGLTV 397
Cdd:smart00487 14 KEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRV---LVLVPTRELAEQWAEELKKLgpslGLKVVGLYG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 398 GYQIR--LESVKSSATRLLYCTTGVLLRRLE-GDATLQGVTHIIVDEVHERTEES--DFLLLVLKDIvmqRATLQVILMS 472
Cdd:smart00487 91 GDSKReqLRKLESGKTDILVTTPGRLLDLLEnDKLSLSNVDLVILDEAHRLLDGGfgDQLEKLLKLL---PKNVQLLLLS 167
|
170 180 190
....*....|....*....|....*....|....
gi 1720388776 473 ATLDAGL--FSKYFSYCPVITIPGRA--FPVDQF 502
Cdd:smart00487 168 ATPPEEIenLLELFLNDPVFIDVGFTplEPIEQF 201
|
|
| HA2 |
pfam04408 |
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ... |
813-892 |
3.46e-23 |
|
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: 95.38 E-value: 3.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 813 LRDLGALTPDEKLTPLGYHLASLPVDVRIGKLMLLGSIFRCLDPALTIAASLAFKSPFVSP----WDKKEEANQKKLEFA 888
Cdd:pfam04408 5 LYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPnfldPRSAAKAARRRRRAA 84
|
....
gi 1720388776 889 FANS 892
Cdd:pfam04408 85 DEKA 88
|
|
| OB_NTP_bind |
pfam07717 |
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ... |
986-1083 |
5.46e-22 |
|
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: 91.16 E-value: 5.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 986 ISAVLCAALYPNVVqvktpegkfqktssgvvRLQPKSAELKFVtKNDGYVHIHPSSVNYQVRHFDSPYLLYHEKIKTSRV 1065
Cdd:pfam07717 1 LRAALAAGLYPNVA-----------------RRDPKGKGYTTL-SDNQRVFIHPSSVLFNEKTFPPEWVVYQELVETTKV 62
|
90
....*....|....*...
gi 1720388776 1066 FIRDCSMVSVYPLVLFGG 1083
Cdd:pfam07717 63 YIRTVTAISPEWLLLFAP 80
|
|
| RWD |
pfam05773 |
RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. ... |
17-190 |
3.51e-07 |
|
RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. The function of this domain is unknown. GCN2 is the alpha-subunit of the only translation initiation factor (eIF2 alpha) kinase that appears in all eukaryotes. Its function requires an interaction with GCN1 via the domain at its N-terminus, which is termed the RWD domain after three major RWD-containing proteins: RING finger-containing proteins, WD-repeat-containing proteins, and yeast DEAD (DEXD)-like helicases. The structure forms an alpha + beta sandwich fold consisting of two layers: a four-stranded antiparallel beta-sheet, and three side-by-side alpha-helices.
Pssm-ID: 399058 Cd Length: 111 Bit Score: 49.63 E-value: 3.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 17 EQRQEETLALKSICGEKFiERIQNRVWtigleldyltnkfckskqkessknvrdtspetckfylkgnckfgskCKFKHEV 96
Cdd:pfam05773 1 EEQEEELEALESIYPDEF-EVISDSPY----------------------------------------------ESLEIEI 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 97 PPHqmigraernvnDPHLDADDDTTFMYELQIRFSKDhkYPYQAPLVAFySTNENLPLACRLHISEFLYGKALEFakTSE 176
Cdd:pfam05773 34 KLS-----------LDSDESDSSHLPPLVLKFTLPED--YPDEPPKISL-SSPWNLSDEQVLSLLEELEELAEEN--LGE 97
|
170
....*....|....
gi 1720388776 177 PVVYSLITLLEEES 190
Cdd:pfam05773 98 VMIFELIEWLQENL 111
|
|
| zf_CCCH_4 |
pfam18345 |
Zinc finger domain; This is a zinc finger domain found in Zinc finger CCCH-type with G patch ... |
76-94 |
1.47e-06 |
|
Zinc finger domain; This is a zinc finger domain found in Zinc finger CCCH-type with G patch domain-containing proteins such as ZIP. Functional studies indicate that ZIP specifically targets EGFR and represses its transcription, and that the zinc finger and the coiled-coil domains are central to that process.
Pssm-ID: 465719 [Multi-domain] Cd Length: 19 Bit Score: 45.49 E-value: 1.47e-06
|
| ZnF_C3H1 |
smart00356 |
zinc finger; |
73-94 |
2.36e-06 |
|
zinc finger;
Pssm-ID: 214632 [Multi-domain] Cd Length: 27 Bit Score: 44.93 E-value: 2.36e-06
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HrpA |
COG1643 |
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis]; |
316-943 |
1.47e-120 |
|
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441249 [Multi-domain] Cd Length: 836 Bit Score: 392.14 E-value: 1.47e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 316 LPAWEERETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSLnGPPERvanIICTQPRRISAISVAERVAKERAERVGL 395
Cdd:COG1643 10 LPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGW-GAGGR---IGMLEPRRLAARAAAERMAEELGEPVGE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 396 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIvmQRAT---LQVILMS 472
Cdd:COG1643 86 TVGYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDL--QPALrpdLKLLVMS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 473 ATLDAGLFSKYFSYCPVITIPGRAFPVDqffledalavTRYvlqdgspymrsmkqiakeklkarhnrtaqeeveedLRLS 552
Cdd:COG1643 164 ATLDAERFARLLGDAPVIESSGRTYPVE----------VRY-----------------------------------RPLP 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 553 LHLQDEEESVKDTIpdqqldfkqllirykgvsksviktmsvmdfekvnlelIEALLEwivdgkhayPPGAVLVFLPGLAE 632
Cdd:COG1643 199 ADERDLEDAVADAV-------------------------------------REALAE---------EPGDILVFLPGERE 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 633 IKMLYEQLQsnslfnNRRSHRCVIHPLHSSLSSEEQQAVFVKPPMGVTKIIISTNIAETSITIDDVVYVIDSGKMKEKRY 712
Cdd:COG1643 233 IRRTAEALR------GRLPPDTEILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRY 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 713 DAGKGMESLEDTFVSQANALQRKGRAGRVASGVCFHLFTSHHYNhQLLKQQLPEIQRVPLEQLclrikILEMFS--THNL 790
Cdd:COG1643 307 DPRSGVTRLPTERISQASANQRAGRAGRLAPGICYRLWSEEDFA-RRPAFTDPEILRADLASL-----ILELAAwgLGDP 380
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 791 QSVfsRLIEPPHIDSLRASKVRLRDLGALTPDEKLTPLGYHLASLPVDVRIGKLMLLGSIFRCLDPALTIAASLAFKSPF 870
Cdd:COG1643 381 EDL--PFLDPPPARAIADARALLQELGALDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDPR 458
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720388776 871 VSPwdkkeeanqkklefafANSDYLALLcayKGWQlstkesaraSYNYCRQNFLSGRTLQEMASLKRQFTELL 943
Cdd:COG1643 459 RGA----------------AGSDLLARL---NLWR---------RLREQQREFLSYLRLREWRDLARQLRRLL 503
|
|
| DEXHc_DHX57 |
cd17985 |
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the ... |
316-492 |
2.78e-110 |
|
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: 341.43 E-value: 2.78e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 316 LPAWEERETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSLNGPPERVANIICTQPRRISAISVAERVAKERAERVGL 395
Cdd:cd17985 1 LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFILDNSLQGPPLPVANIICTQPRRISAISVAERVAQERAERVGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 396 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIVMQRATLQVILMSATL 475
Cdd:cd17985 81 SVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDPTLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQRPDLKVILMSATL 160
|
170
....*....|....*..
gi 1720388776 476 DAGLFSKYFSYCPVITI 492
Cdd:cd17985 161 NAELFSDYFNSCPVIHI 177
|
|
| DEXHc_RHA-like |
cd17917 |
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ... |
332-492 |
4.91e-86 |
|
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: 275.11 E-value: 4.91e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 332 HQVVVISGMTGCGKTTQIPQFILDNSLNGPPErvANIICTQPRRISAISVAERVAKERAERVGLTVGYQIRLESVKSSAT 411
Cdd:cd17917 1 NQVVVIVGETGSGKTTQVPQFLLEDGLAKGGK--GRIVCTQPRRIAAISVAERVAEERGEKLGEEVGYQIRFESKTSSKT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 412 RLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIVMQRATLQVILMSATLDAGLFSKYFSYCPVIT 491
Cdd:cd17917 79 RIKFCTDGILLRELLSDPLLSGYSHVILDEAHERSLDTDFLLGLLKDLLRKRPDLKVILMSATLDAEKFSSYFGGAPVIH 158
|
.
gi 1720388776 492 I 492
Cdd:cd17917 159 I 159
|
|
| PRK11131 |
PRK11131 |
ATP-dependent RNA helicase HrpA; Provisional |
314-948 |
4.52e-77 |
|
ATP-dependent RNA helicase HrpA; Provisional
Pssm-ID: 182986 [Multi-domain] Cd Length: 1294 Bit Score: 278.48 E-value: 4.52e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 314 QLLPAWEERETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSLNgppeRVANIICTQPRRISAISVAERVAKERAERV 393
Cdd:PRK11131 71 ENLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLELGRG----VKGLIGHTQPRRLAARTVANRIAEELETEL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 394 GLTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIVMQRATLQVILMSA 473
Cdd:PRK11131 147 GGCVGYKVRFNDQVSDNTMVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPDLKVIITSA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 474 TLDAGLFSKYFSYCPVITIPGRAFPVDqffledalavTRYvlqdgspymrsmkqiakeklkarhnRTAQEEVEedlrlsl 553
Cdd:PRK11131 227 TIDPERFSRHFNNAPIIEVSGRTYPVE----------VRY-------------------------RPIVEEAD------- 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 554 hlqdeeesvkDTIPDQqldfkqllirykgvsksviktmsvmdfekvnlelIEALLEwIVDGKHAYPPGAVLVFLPGLAEI 633
Cdd:PRK11131 265 ----------DTERDQ----------------------------------LQAIFD-AVDELGREGPGDILIFMSGEREI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 634 KMLYEQLQSNSLFNNRrshrcvIHPLHSSLSSEEQQAVFvkPPMGVTKIIISTNIAETSITIDDVVYVIDSGKMKEKRYD 713
Cdd:PRK11131 300 RDTADALNKLNLRHTE------ILPLYARLSNSEQNRVF--QSHSGRRIVLATNVAETSLTVPGIKYVIDPGTARISRYS 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 714 AGKGMESLEDTFVSQANALQRKGRAGRVASGVCFHLFTSHHYNHqllKQQL--PEIQRVPLEQLclrikILEMFSThNLQ 791
Cdd:PRK11131 372 YRTKVQRLPIEPISQASANQRKGRCGRVSEGICIRLYSEDDFLS---RPEFtdPEILRTNLASV-----ILQMTAL-GLG 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 792 --SVFSrLIEPP---HI-DSLRAskvrLRDLGALTPDE-----KLTPLGYHLASLPVDVRIGKLMLLGSIFRCLDPALTI 860
Cdd:PRK11131 443 diAAFP-FVEAPdkrNIqDGVRL----LEELGAITTDEqasayKLTPLGRQLAQLPVDPRLARMVLEAQKHGCVREVMII 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 861 AASLAFKSPFVSPWDKKEEANQKKLEFAFANSDYLALLcayKGWQ-LSTKESARASYNY---CRQNFLSGRTLQEMASLK 936
Cdd:PRK11131 518 TSALSIQDPRERPMDKQQASDEKHRRFADKESDFLAFV---NLWNyLQEQQKALSSNQFrrlCRTDYLNYLRVREWQDIY 594
|
650
....*....|..
gi 1720388776 937 RQFTELLSDIGF 948
Cdd:PRK11131 595 TQLRQVVKELGI 606
|
|
| DEAH_box_HrpB |
TIGR01970 |
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ... |
315-864 |
7.87e-76 |
|
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: 268.17 E-value: 7.87e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 315 LLPAweeretILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSLNGppervANIICTQPRRISAISVAERVAKERAERVG 394
Cdd:TIGR01970 6 VLPA------LRDALAAHPQVVLEAPPGAGKSTAVPLALLDAPGIG-----GKIIMLEPRRLAARSAAQRLASQLGEAVG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 395 LTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIVMQ-RATLQVILMSA 473
Cdd:TIGR01970 75 QTVGYRVRGENKVSRRTRLEVVTEGILTRMIQDDPELDGVGALIFDEFHERSLDADLGLALALDVQSSlREDLKILAMSA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 474 TLDAGLFSKYFSYCPVITIPGRAFPVDqffledalavTRYvlqdgspymrsmkqiakeklkarhnRTAQeeveedlrlsl 553
Cdd:TIGR01970 155 TLDGERLSSLLPDAPVVESEGRSFPVE----------IRY-------------------------LPLR----------- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 554 hlqdeeesvkdtiPDQQLDfkqllirykgvsksviktmsvmdfEKVNLELIEALlewivdgkhAYPPGAVLVFLPGLAEI 633
Cdd:TIGR01970 189 -------------GDQRLE------------------------DAVSRAVEHAL---------ASETGSILVFLPGQAEI 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 634 KMLYEQLQSnslfnnRRSHRCVIHPLHSSLSSEEQQAVFVKPPMGVTKIIISTNIAETSITIDDVVYVIDSGKMKEKRYD 713
Cdd:TIGR01970 223 RRVQEQLAE------RLDSDVLICPLYGELSLAAQDRAIKPDPQGRRKVVLATNIAETSLTIEGIRVVIDSGLARVARFD 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 714 AGKGMESLEDTFVSQANALQRKGRAGRVASGVCFHLFtSHHYNHQLLKQQLPEIQRVPLEQLCLRIKILEMFSTHNLqsv 793
Cdd:TIGR01970 297 PKTGITRLETVRISQASATQRAGRAGRLEPGVCYRLW-SEEQHQRLPAQDEPEILQADLSGLALELAQWGAKDPSDL--- 372
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720388776 794 fsRLIEPPHIDSLRASKVRLRDLGALTPDEKLTPLGYHLASLPVDVRIGKLMLLGSIFRCLDPALTIAASL 864
Cdd:TIGR01970 373 --RWLDAPPSVALAAARQLLQRLGALDAQGRLTAHGKAMAALGCHPRLAAMLLSAHSTGLAALACDLAALL 441
|
|
| SF2_C_RHA |
cd18791 |
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ... |
591-750 |
1.14e-72 |
|
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: 238.59 E-value: 1.14e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 591 MSVMDFEKVNLELIEALLEWIVdgkHAYPPGAVLVFLPGLAEIKMLYEQLQSNSLFNNrrSHRCVIHPLHSSLSSEEQQA 670
Cdd:cd18791 17 ISSEKEDPDYVDAAVRLILQIH---RTEEPGDILVFLPGQEEIERLCELLREELLSPD--LGKLLVLPLHSSLPPEEQQR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 671 VFVKPPMGVTKIIISTNIAETSITIDDVVYVIDSGKMKEKRYDAGKGMESLEDTFVSQANALQRKGRAGRVASGVCFHLF 750
Cdd:cd18791 92 VFEPPPPGVRKVVLATNIAETSITIPGVVYVIDSGLVKEKVYDPRTGLSSLVTVWISKASAEQRAGRAGRTRPGKCYRLY 171
|
|
| DEXHc_YTHDC2 |
cd17987 |
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) ... |
316-492 |
6.91e-69 |
|
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: 228.56 E-value: 6.91e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 316 LPAWEERETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSL-NGPPERvanIICTQPRRISAISVAERVAKERAERVG 394
Cdd:cd17987 1 LPVFEKQEQIVRIIKENKVVLIVGETGSGKTTQIPQFLLDDCYaNGIPCR---IFCTQPRRLAAIAVAERVAAERGEKIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 395 LTVGYQIRLESVKSSATRLLYCTTGVLLRRL-EGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIVMQRATLQVILMSA 473
Cdd:cd17987 78 QTVGYQIRLESRVSPKTLLTFCTNGVLLRTLmAGDSALSTVTHVIVDEVHERDRFSDFLLTKLRDILQKHPNLKLILSSA 157
|
170
....*....|....*....
gi 1720388776 474 TLDAGLFSKYFSYCPVITI 492
Cdd:cd17987 158 ALDVNLFIRYFGSCPVIYI 176
|
|
| DEXHc_DHX9 |
cd17972 |
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ... |
300-492 |
1.54e-67 |
|
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: 227.02 E-value: 1.54e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 300 KQASRQFHAILQERQLLPAWEERETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSLNGPPERVANIICTQPRRISAI 379
Cdd:cd17972 43 REQDHNLQQILQERELLPVKKFREEILEAISNNPVVIIRGATGCGKTTQVPQYILDDFIQNDRAAECNIVVTQPRRISAV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 380 SVAERVAKERAERVGLTVGYQIRLESV-KSSATRLLYCTTGVLLRRLEgdATLQGVTHIIVDEVHERTEESDFLLLVLKD 458
Cdd:cd17972 123 SVAERVAFERGEEVGKSCGYSVRFESVlPRPHASILFCTVGVLLRKLE--AGIRGISHVIVDEIHERDINTDFLLVVLRD 200
|
170 180 190
....*....|....*....|....*....|....
gi 1720388776 459 IVMQRATLQVILMSATLDAGLFSKYFSYCPVITI 492
Cdd:cd17972 201 VVQAYPDLRVILMSATIDTSMFCEYFFNCPVIEV 234
|
|
| DEXHc_DHX29 |
cd17975 |
DEXH-box helicase domain of DEAH-box helicase 29; DEAH-box helicase 29 (DHX29) is a part of ... |
316-492 |
1.71e-66 |
|
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: 222.10 E-value: 1.71e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 316 LPAWEERETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSL-NGPPERVANIICTQPRRISAISVAERVAKERAERVG 394
Cdd:cd17975 1 LPVFKHRESILETLKRHRVVVVAGETGSGKSTQVPQFLLEDLLlNGGTAQKCNIVCTQPRRISAMSLATRVCEELGCESG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 395 -----LTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIVMQRATLQVI 469
Cdd:cd17975 81 pggknSLCGYQIRMESRTGEATRLLYCTTGVLLRKLQEDGLLSSISHIIVDEVHERSVQSDFLLIILKEILHKRSDLHLI 160
|
170 180
....*....|....*....|...
gi 1720388776 470 LMSATLDAGLFSKYFSYCPVITI 492
Cdd:cd17975 161 LMSATVDCEKFSSYFTHCPILRI 183
|
|
| DEXHc_DHX36 |
cd17981 |
DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as ... |
316-492 |
9.61e-65 |
|
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: 217.02 E-value: 9.61e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 316 LPAWEERETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSLNGPPERVANIICTQPRRISAISVAERVAKERAERVGL 395
Cdd:cd17981 1 LPSYGMKQEIINMIDNNQVTVISGETGCGKTTQVTQFILDDAIERGKGSSCRIVCTQPRRISAISVAERVAAERAESCGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 396 --TVGYQIRLESVKS-SATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIVMQRATLQVILMS 472
Cdd:cd17981 81 gnSTGYQIRLESRKPrKQGSILYCTTGIVLQWLQSDPHLSNVSHLVLDEIHERNLQSDVLMGIVKDLLPFRSDLKVILMS 160
|
170 180
....*....|....*....|
gi 1720388776 473 ATLDAGLFSKYFSYCPVITI 492
Cdd:cd17981 161 ATLNAEKFSDYFNNCPMIHI 180
|
|
| PRK11664 |
PRK11664 |
ATP-dependent RNA helicase HrpB; Provisional |
315-865 |
1.53e-63 |
|
ATP-dependent RNA helicase HrpB; Provisional
Pssm-ID: 236950 [Multi-domain] Cd Length: 812 Bit Score: 232.12 E-value: 1.53e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 315 LLPAWEERETILKLLSKHQVVVISGMTGCGKTTQIP-QFILDNSLNGppervaNIICTQPRRISAISVAERVAKERAERV 393
Cdd:PRK11664 3 SLPVAAVLPELLTALKTAPQVLLKAPTGAGKSTWLPlQLLQHGGING------KIIMLEPRRLAARNVAQRLAEQLGEKP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 394 GLTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDiVMQ--RATLQVILM 471
Cdd:PRK11664 77 GETVGYRMRAESKVGPNTRLEVVTEGILTRMIQRDPELSGVGLVILDEFHERSLQADLALALLLD-VQQglRDDLKLLIM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 472 SATLDAGLFSKYFSYCPVITIPGRAFPVDqffledalavTRYvlqdgspymrsmkqiakeklkarhnrtaqeeveEDLRL 551
Cdd:PRK11664 156 SATLDNDRLQQLLPDAPVIVSEGRSFPVE----------RRY---------------------------------QPLPA 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 552 SLHLqdeEESVKDTIpdqqldfKQLLIRykgvsksviktmsvmdfekvnlelieallewivdgkhayPPGAVLVFLPGLA 631
Cdd:PRK11664 193 HQRF---DEAVARAT-------AELLRQ---------------------------------------ESGSLLLFLPGVG 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 632 EIKMLYEQLQsnslfnNRRSHRCVIHPLHSSLSSEEQQAVFVKPPMGVTKIIISTNIAETSITIDDVVYVIDSGKMKEKR 711
Cdd:PRK11664 224 EIQRVQEQLA------SRVASDVLLCPLYGALSLAEQQKAILPAPAGRRKVVLATNIAETSLTIEGIRLVVDSGLERVAR 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 712 YDAGKGMESLEDTFVSQANALQRKGRAGRVASGVCFHLFTSHHYNHQLLkQQLPEIQRVPLEQLCLRikiLEMFSTHNLQ 791
Cdd:PRK11664 298 FDPKTGLTRLVTQRISQASMTQRAGRAGRLEPGICLHLYSKEQAERAAA-QSEPEILHSDLSGLLLE---LLQWGCHDPA 373
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720388776 792 SVfsRLIEPPHIDSLRASKVRLRDLGALTPDEKLTPLGYHLASLPVDVRIGKLMLLGSIFRclDPALTIAASLA 865
Cdd:PRK11664 374 QL--SWLDQPPAAALAAAKRLLQQLGALDGQGRLTARGRKMAALGNDPRLAAMLVAAKEDD--EAALATAAKLA 443
|
|
| DEXHc_DHX30 |
cd17976 |
DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an ... |
316-492 |
1.96e-61 |
|
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: 207.34 E-value: 1.96e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 316 LPAWEERETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSLNGPPERVANIICTQPRRISAISVAERVAKERAERVGL 395
Cdd:cd17976 1 LPVDSHKESILSAIEQNPVVVISGDTGCGKTTRIPQFILEDYVLRGRGARCNVVITQPRRISAVSVAQRVAHELGPNLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 396 TVGYQIRLES-VKSSATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIVMQRATLQVILMSAT 474
Cdd:cd17976 81 NVGYQVRLESrPPPRGGALLFCTVGVLLKKLQSNPRLEGVSHVIVDEVHERDVNTDFLLILLKGVLQLNPELRVVLMSAT 160
|
170
....*....|....*...
gi 1720388776 475 LDAGLFSKYFSYCPVITI 492
Cdd:cd17976 161 GDNQRLSRYFGGCPVVRV 178
|
|
| DEXHc_DHX15 |
cd17973 |
DEXH-box helicase domain of DEAH-box helicase 15; DEAH-box helicase 15 (DHX15) is a pre-mRNA ... |
305-492 |
2.98e-59 |
|
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: 201.49 E-value: 2.98e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 305 QFHAILQERQLLPAWEERETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSLNGPPERVanIICTQPRRISAISVAER 384
Cdd:cd17973 2 RYFEILEKRRELPVWEQKEDFLKLLKNNQILVLVGETGSGKTTQIPQFVLDDELPHQPKKL--VACTQPRRVAAMSVAQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 385 VAKERAERVGLTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIVMQRA 464
Cdd:cd17973 80 VAEEMDVKLGEEVGYSIRFEDCSSAKTILKYMTDGMLLREAMSDPLLSRYSVIILDEAHERTLATDILMGLLKEVVRRRP 159
|
170 180
....*....|....*....|....*...
gi 1720388776 465 TLQVILMSATLDAGLFSKYFSYCPVITI 492
Cdd:cd17973 160 DLKLIVMSATLDAGKFQKYFDNAPLLKV 187
|
|
| DEXHc_DHX34 |
cd17979 |
DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in ... |
316-492 |
1.32e-55 |
|
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: 190.35 E-value: 1.32e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 316 LPAWEERETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSLNgppervaNIICTQPRRISAISVAERVAKERAERVGL 395
Cdd:cd17979 1 LPIAQYREKIIELLKTHQVVIVAGDTGCGKSTQVPQYLLAAGFR-------HIACTQPRRIACISLAKRVAFESLNQYGS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 396 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIVMQRATLQVILMSATL 475
Cdd:cd17979 74 KVAYQIRFERTRTLATKLLFLTEGLLLRQIQRDASLPQYNVLILDEVHERHLHGDFLLGVLRCLLRLRPDLKLILMSATI 153
|
170
....*....|....*..
gi 1720388776 476 DAGLFSKYFSYCPVITI 492
Cdd:cd17979 154 NIELFSGYFEGAPVVQV 170
|
|
| DEXHc_DHX33 |
cd17978 |
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA ... |
316-492 |
1.23e-53 |
|
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: 185.25 E-value: 1.23e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 316 LPAWEERETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSLNgppeRVANIICTQPRRISAISVAERVAKERAERVGL 395
Cdd:cd17978 1 LPIYSARKRLLEELRKHDTVIIIGETGSGKTTQIPQYLYEAGFA----RGGMIGITQPRRVAAVSVAKRVAEEMGVELGQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 396 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIVMQR-----ATLQVIL 470
Cdd:cd17978 77 LVGYSVRFDDVTSEETRIKYMTDGMLLREAIGDPLLSKYSVIILDEAHERTVHTDVLFGLVKSAQRRRkeqklSPLKVII 156
|
170 180
....*....|....*....|..
gi 1720388776 471 MSATLDAGLFSKYFSYCPVITI 492
Cdd:cd17978 157 MSATLDADLFSEYFNGAPVLYI 178
|
|
| DEXHc_TDRD9 |
cd17988 |
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ... |
316-485 |
1.54e-53 |
|
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: 185.01 E-value: 1.54e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 316 LPAWEERETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSLNgpPERVANIICTQPRRISAISVAERVAKERAERVGL 395
Cdd:cd17988 1 LPIYAKREEILSLIEANSVVIIKGATGCGKTTQLPQFILDHYYK--RGKYCNIVVTQPRRIAAISIARRVSQEREWTLGS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 396 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIVMQRAT-LQVILMSAT 474
Cdd:cd17988 79 LVGYQVGLERPASEETRLIYCTTGVLLQKLINNKTLTEYTHIILDEVHERDQELDFLLLVVRRLLRTNSRhVKIILMSAT 158
|
170
....*....|.
gi 1720388776 475 LDAGLFSKYFS 485
Cdd:cd17988 159 ISCKEFADYFT 169
|
|
| RWD_DHX57 |
cd23825 |
RWD domain of DEAH box protein 57 (DHX57) and related proteins; DHX57 (EC 3.6.4.13) is a ... |
14-196 |
1.51e-48 |
|
RWD domain of DEAH box protein 57 (DHX57) and related proteins; DHX57 (EC 3.6.4.13) is a putative ATP-dependent RNA helicase. A genome-wide association study (GWAS) of cerebellar epigenetic age acceleration identified significant SNPs (single nucleotide polymorphisms) in a loci 2p22.1 inside the DHX57 gene, suggesting that variants in DHX57 are associated with epigenetic age in the cerebellum.
Pssm-ID: 467661 Cd Length: 115 Bit Score: 168.14 E-value: 1.51e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 14 ECVEQRQEETLALKSICGEKFIERIQNRVWTIGLELDYLTNkfckskqkessknvrdtspetckfylkgnckfgskckfk 93
Cdd:cd23825 2 ELLEQRQEEAMALESIYGEAFSERIPNKVWTIKLDLPYLPW--------------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 94 hevpphqmigraernvndphldadddttfmYELQIRFSKDHKYPYQAPLVAFYSTNENLPLACRLHISEFLYGKALEFAK 173
Cdd:cd23825 43 ------------------------------FELEIRFPKGNKYPYEPPIVAFSSTNENFPKAVCLNITERLMEEALELAE 92
|
170 180
....*....|....*....|...
gi 1720388776 174 TSEPVVYSLITLLEEESEIVKLL 196
Cdd:cd23825 93 DGEPVVFSLVSLLEDEEEILELL 115
|
|
| DEXHc_DHX8 |
cd17971 |
DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as ... |
311-493 |
3.41e-48 |
|
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: 169.59 E-value: 3.41e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 311 QERQLLPAWEERETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSLNgppeRVANIICTQPRRISAISVAERVAKERA 390
Cdd:cd17971 1 EQRESLPIYKLKEQLIQAVHDNQILVVIGETGSGKTTQITQYLAEAGYT----SRGKIGCTQPRRVAAMSVAKRVAEEFG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 391 ERVGLTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIVMQRATLQVIL 470
Cdd:cd17971 77 CCLGQEVGYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLSQYSVIMLDEAHERTIHTDVLFGLLKKTVQKRPDLKLIV 156
|
170 180
....*....|....*....|...
gi 1720388776 471 MSATLDAGLFSKYFSYCPVITIP 493
Cdd:cd17971 157 TSATLDAVKFSQYFYEAPIFTIP 179
|
|
| DEXHc_DHX35 |
cd17980 |
DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and ... |
316-486 |
4.95e-47 |
|
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: 166.49 E-value: 4.95e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 316 LPAWEERETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNslnGPPERVANIICTQPRRISAISVAERVAKERAERVGL 395
Cdd:cd17980 1 LPVFKLRNHILYLVENYQTIVIVGETGCGKSTQIPQYLAEA---GWTAGGRVVGCTQPRRVAAVTVAGRVAEEMGAVLGH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 396 TVGYQIRLESVKSS-ATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIVMQRATLQVILMSAT 474
Cdd:cd17980 78 EVGYCIRFDDCTDPqATRIKFLTDGMLVREMMLDPLLTKYSVIMLDEAHERTLYTDILIGLLKKIQKKRGDLRLIVASAT 157
|
170
....*....|..
gi 1720388776 475 LDAGLFSKYFSY 486
Cdd:cd17980 158 LDAEKFRDFFNQ 169
|
|
| DEXHc_DHX16 |
cd17974 |
DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably ... |
316-492 |
5.60e-47 |
|
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: 165.75 E-value: 5.60e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 316 LPAWEERETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNslnGPPERVANIICTQPRRISAISVAERVAKERAERVGL 395
Cdd:cd17974 1 LPVYPYRDDLLAAVKEHQVLIIVGETGSGKTTQIPQYLHEA---GYTKGGGKIGCTQPRRVAAMSVAARVAEEMGVKLGN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 396 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIVMQRATLQVILMSATL 475
Cdd:cd17974 78 EVGYSIRFEDCTSEKTVLKYMTDGMLLREFLTEPDLASYSVMIIDEAHERTLHTDILFGLVKDIARFRPDLKLLISSATM 157
|
170
....*....|....*..
gi 1720388776 476 DAGLFSKYFSYCPVITI 492
Cdd:cd17974 158 DAEKFSAFFDDAPIFRI 174
|
|
| DEXHc_DHX38 |
cd17983 |
DEXH-box helicase domain of DEAH-box helicase 38; DEAH-box helicase 38 (DHX38, also known as ... |
316-492 |
1.03e-43 |
|
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: 156.47 E-value: 1.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 316 LPAWEERETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSLNgppeRVANIICTQPRRISAISVAERVAKERAERVGL 395
Cdd:cd17983 1 LPIFAVRQELLNVIRDNNVVIVVGETGSGKTTQLTQYLHEDGYT----DYGMIGCTQPRRVAAMSVAKRVSEEMGVELGE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 396 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIVMQRATLQVILMSATL 475
Cdd:cd17983 77 EVGYAIRFEDCTSENTVIKYMTDGILLRESLRDPDLDKYSAIIMDEAHERSLNTDVLFGLLREVVARRRDLKLIVTSATM 156
|
170
....*....|....*..
gi 1720388776 476 DAGLFSKYFSYCPVITI 492
Cdd:cd17983 157 DADKFADFFGNVPIFTI 173
|
|
| DEXHc_HrpB |
cd17990 |
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ... |
316-490 |
1.32e-41 |
|
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: 150.56 E-value: 1.32e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 316 LPAWEERETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSLNGPpervANIICTQPRRISAISVAERVAKERAERVGL 395
Cdd:cd17990 1 LPIAAVLPALRAALDAGGQVVLEAPPGAGKTTRVPLALLAELWIAG----GKIIVLEPRRVAARAAARRLATLLGEAPGE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 396 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIV-MQRATLQVILMSAT 474
Cdd:cd17990 77 TVGYRVRGESRVGRRTRVEVVTEGVLLRRLQRDPELSGVGAVILDEFHERSLDADLALALLLEVQqLLRDDLRLLAMSAT 156
|
170
....*....|....*.
gi 1720388776 475 LDAGLFSKYFSYCPVI 490
Cdd:cd17990 157 LDGDGLAALLPEAPVV 172
|
|
| DEXHc_HrpA |
cd17989 |
DEXH-box helicase domain of ATP-dependent RNA helicase HrpA; HrpA is part of the HrpB-HrpA ... |
316-492 |
2.01e-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: 149.91 E-value: 2.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 316 LPAWEERETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSLNgppeRVANIICTQPRRISAISVAERVAKERAERVGL 395
Cdd:cd17989 1 LPVSQKRDEIAKAIAENQVVIIAGETGSGKTTQLPKICLELGRG----IRGLIGHTQPRRLAARSVAERIAEELKTELGG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 396 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIVMQRATLQVILMSATL 475
Cdd:cd17989 77 AVGYKVRFTDQTSDETCVKLMTDGILLAETQTDRYLRAYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKVIITSATI 156
|
170
....*....|....*..
gi 1720388776 476 DAGLFSKYFSYCPVITI 492
Cdd:cd17989 157 DAERFSRHFNNAPIIEV 173
|
|
| DEXHc_DHX37 |
cd17982 |
DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the ... |
316-475 |
5.02e-39 |
|
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: 143.65 E-value: 5.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 316 LPAWEERETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSLNGP-PERVANIICTQPRRISAISVAERVAKERAErVG 394
Cdd:cd17982 1 LPILAEEQEIMEAINENPVVIICGETGSGKTTQVPQFLYEAGFGSPeSDNPGMIGITQPRRVAAVSMAKRVAEELNV-FG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 395 LTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIVMQRAT--------- 465
Cdd:cd17982 80 KEVSYQIRYDSTVSENTKIKFMTDGVLLKEIQTDFLLRKYSVIIIDEAHERSVNTDILIGMLSRIVPLRAKlylqdqtvk 159
|
170
....*....|.
gi 1720388776 466 -LQVILMSATL 475
Cdd:cd17982 160 pLKLVIMSATL 170
|
|
| DEXHc_DHX40 |
cd17984 |
DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to the ... |
316-492 |
1.00e-36 |
|
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: 136.91 E-value: 1.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 316 LPAWEERETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSLNgppeRVANIICTQPRRISAISVAERVAKERAERVGL 395
Cdd:cd17984 1 LPIQKQRKKLVQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGFS----QHGMIGVTQPRRVAAISVAQRVAEEMKCTLGS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 396 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIVMQRAT-----LQVIL 470
Cdd:cd17984 77 KVGYQVRFDDCSSKETAIKYMTDGCLLRHILADPNLTKYSVIILDEAHERSLTTDILFGLLKKLFQEKSPnrkehLKVVV 156
|
170 180
....*....|....*....|..
gi 1720388776 471 MSATLDAGLFSKYFSYCPVITI 492
Cdd:cd17984 157 MSATLELAKLSAFFGNCPVFDI 178
|
|
| DEXHc_DHX32 |
cd17977 |
DEXH-box helicase domain of DEAH-box helicase 32; DEAH-box helicase 32 (DHX32) belongs to the ... |
316-490 |
1.90e-32 |
|
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: 124.55 E-value: 1.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 316 LPAWEERETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSLNGPpERVANIICTQPRRISAISVAERVAKERAERVGL 395
Cdd:cd17977 1 LPVWEAKYEFMESLAHNQIVIVSGDAKTGKSSQIPQWCAEYCLSAH-YQHGVVVCTQVHKQTAVWLALRVADEMDVNIGH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 396 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIVMQRATLQVILMSATL 475
Cdd:cd17977 80 EVGYVIPFENCCTNETILRYCTDDMLLREMMSDPLLESYGVIILDDAHERTVSTDVLLGLLKDVLLSRPELKLVIITCPH 159
|
170
....*....|....*
gi 1720388776 476 DAGLFSKYFSYCPVI 490
Cdd:cd17977 160 LSSKLLSYYGNVPLI 174
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
322-502 |
3.59e-24 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 101.41 E-value: 3.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 322 RETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSLNGPPERVaniICTQPRRISAISVAERVAKE----RAERVGLTV 397
Cdd:smart00487 14 KEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRV---LVLVPTRELAEQWAEELKKLgpslGLKVVGLYG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 398 GYQIR--LESVKSSATRLLYCTTGVLLRRLE-GDATLQGVTHIIVDEVHERTEES--DFLLLVLKDIvmqRATLQVILMS 472
Cdd:smart00487 91 GDSKReqLRKLESGKTDILVTTPGRLLDLLEnDKLSLSNVDLVILDEAHRLLDGGfgDQLEKLLKLL---PKNVQLLLLS 167
|
170 180 190
....*....|....*....|....*....|....
gi 1720388776 473 ATLDAGL--FSKYFSYCPVITIPGRA--FPVDQF 502
Cdd:smart00487 168 ATPPEEIenLLELFLNDPVFIDVGFTplEPIEQF 201
|
|
| DEXQc_DQX1 |
cd17986 |
DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 ... |
316-492 |
6.22e-24 |
|
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: 99.97 E-value: 6.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 316 LPAWEERETIL-KLLSKHQVVVISGMTGCGKTTQIPQFILDNSLNGPPERvANIICTQPRRISAISVAERVAKERAERVG 394
Cdd:cd17986 1 LPIWAAKFTFLeQLESPSGIVLVSGEPGSGKSTQVPQWCAEFALSRGFQK-GQVTVTQPHPLAARSLALRVADEMDLNLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 395 LTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIVMQRATLQVILMSat 474
Cdd:cd17986 80 HEVGYSIPQEDCTGPNTILRFCWDRLLLQEMTSTPLLGAWGVVVLDEAQERSVASDSLLGLLKDVRLQRPELRVVVVT-- 157
|
170 180
....*....|....*....|.
gi 1720388776 475 lDAGLFSKYFSYC---PVITI 492
Cdd:cd17986 158 -SPALEPKLRAFWgnpPVVHV 177
|
|
| HA2 |
smart00847 |
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ... |
816-898 |
3.37e-23 |
|
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: 94.26 E-value: 3.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 816 LGALTPDEKLTPLGYHLASLPVDVRIGKLMLLGSIFRCLDPALTIAASLAFKSPFvsPWDKKEEANQKKLEFAFANSDYL 895
Cdd:smart00847 2 LGALDDDGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPR--PKEKREDADAARRRFADPESDHL 79
|
...
gi 1720388776 896 ALL 898
Cdd:smart00847 80 TLL 82
|
|
| HA2 |
pfam04408 |
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ... |
813-892 |
3.46e-23 |
|
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: 95.38 E-value: 3.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 813 LRDLGALTPDEKLTPLGYHLASLPVDVRIGKLMLLGSIFRCLDPALTIAASLAFKSPFVSP----WDKKEEANQKKLEFA 888
Cdd:pfam04408 5 LYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPnfldPRSAAKAARRRRRAA 84
|
....
gi 1720388776 889 FANS 892
Cdd:pfam04408 85 DEKA 88
|
|
| OB_NTP_bind |
pfam07717 |
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ... |
986-1083 |
5.46e-22 |
|
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: 91.16 E-value: 5.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 986 ISAVLCAALYPNVVqvktpegkfqktssgvvRLQPKSAELKFVtKNDGYVHIHPSSVNYQVRHFDSPYLLYHEKIKTSRV 1065
Cdd:pfam07717 1 LRAALAAGLYPNVA-----------------RRDPKGKGYTTL-SDNQRVFIHPSSVLFNEKTFPPEWVVYQELVETTKV 62
|
90
....*....|....*...
gi 1720388776 1066 FIRDCSMVSVYPLVLFGG 1083
Cdd:pfam07717 63 YIRTVTAISPEWLLLFAP 80
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
602-741 |
1.36e-13 |
|
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: 68.01 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 602 ELIEALLEWIvdgkHAYPPGAVLVFLPGlaeIKMLYEQLqsnslFNNRRSHRCVihPLHSSLSSEEQQAVFVKPPMGVTK 681
Cdd:pfam00271 1 EKLEALLELL----KKERGGKVLIFSQT---KKTLEAEL-----LLEKEGIKVA--RLHGDLSQEEREEILEDFRKGKID 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 682 IIISTNIAETSITIDDVVYVIDsgkmkekrYDAGKGMESLedtfvsqanaLQRKGRAGRV 741
Cdd:pfam00271 67 VLVATDVAERGLDLPDVDLVIN--------YDLPWNPASY----------IQRIGRAGRA 108
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
650-740 |
6.79e-13 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 64.93 E-value: 6.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 650 RSHRCVIHPLHSSLSSEEQQAVFVKPPMGVTKIIISTNIAETSITIDDVVYVIDSgkmkekrydagkgmesleDTFVSQA 729
Cdd:smart00490 8 KELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIY------------------DLPWSPA 69
|
90
....*....|.
gi 1720388776 730 NALQRKGRAGR 740
Cdd:smart00490 70 SYIQRIGRAGR 80
|
|
| PHA02653 |
PHA02653 |
RNA helicase NPH-II; Provisional |
325-744 |
2.04e-12 |
|
RNA helicase NPH-II; Provisional
Pssm-ID: 177443 [Multi-domain] Cd Length: 675 Bit Score: 71.55 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 325 ILKLLSKHQVVVISGMTGCGKTTQIPQFIL-DNSLNG---------PPERVANIICTQPR----RISAISVAERVAKERA 390
Cdd:PHA02653 172 IFEAWISRKPVVLTGGTGVGKTSQVPKLLLwFNYLFGgfdnldkidPNFIERPIVLSLPRvalvRLHSITLLKSLGFDEI 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 391 ERVGLTVGY---QIRLESVKSSATRLLYCTTGVLLRRLEGDATlqgvthIIVDEVHERTEESDFLLLVL-KDIVMQRAtl 466
Cdd:PHA02653 252 DGSPISLKYgsiPDELINTNPKPYGLVFSTHKLTLNKLFDYGT------VIIDEVHEHDQIGDIIIAVArKHIDKIRS-- 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 467 qVILMSATL--DAGLFSKYFSYCPVITIPGRA-FPVDQFfledalavtrYVLQDGSPYMRSMKqiakeklkarhnrtaqe 543
Cdd:PHA02653 324 -LFLMTATLedDRDRIKEFFPNPAFVHIPGGTlFPISEV----------YVKNKYNPKNKRAY----------------- 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 544 eVEEDLRLSLHlqdeeeSVKDTIPDQQldfkqllirykgvsKSVI---KTMSVMDFEKVNLE-LIEALLEWIVDGKhayp 619
Cdd:PHA02653 376 -IEEEKKNIVT------ALKKYTPPKG--------------SSGIvfvASVSQCEEYKKYLEkRLPIYDFYIIHGK---- 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 620 pgavlvfLPGLAEIkmlyeqlqSNSLFNNRRSHrcvihplhsslsseeqqavfvkppmgvtkIIISTNIAETSITIDDVV 699
Cdd:PHA02653 431 -------VPNIDEI--------LEKVYSSKNPS-----------------------------IIISTPYLESSVTIRNAT 466
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1720388776 700 YVIDSGKMKEKRYDAGKgmesleDTFVSQANALQRKGRAGRVASG 744
Cdd:PHA02653 467 HVYDTGRVYVPEPFGGK------EMFISKSMRTQRKGRVGRVSPG 505
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
335-474 |
4.34e-12 |
|
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: 65.12 E-value: 4.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 335 VVISGMTGCGKTTQIPQFILDNSLNGPPERVanIICtqPRRISAISVAERVAKERAE--RVGLTVGY---QIRLESVKSS 409
Cdd:cd00046 4 VLITAPTGSGKTLAALLAALLLLLKKGKKVL--VLV--PTKALALQTAERLRELFGPgiRVAVLVGGssaEEREKNKLGD 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720388776 410 AtRLLYCTTGVLLRRLEGDA--TLQGVTHIIVDEVHERTEESDFLLLV-LKDIVMQRATLQVILMSAT 474
Cdd:cd00046 80 A-DIIIATPDMLLNLLLREDrlFLKDLKLIIVDEAHALLIDSRGALILdLAVRKAGLKNAQVILLSAT 146
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
322-476 |
3.47e-11 |
|
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: 63.03 E-value: 3.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 322 RETILKLLSKHQVVVISGmTGCGKTT--QIPqfILDNSLNGPPERVANIICtqPRRISAISVAERvAKERAERVGLTV-- 397
Cdd:pfam00270 5 AEAIPAILEGRDVLVQAP-TGSGKTLafLLP--ALEALDKLDNGPQALVLA--PTRELAEQIYEE-LKKLGKGLGLKVas 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 398 ---GYQIRLESVKSSATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHeRTEESDF---LLLVLKDIvmqRATLQVILM 471
Cdd:pfam00270 79 llgGDSRKEQLEKLKGPDILVGTPGRLLDLLQERKLLKNLKLLVLDEAH-RLLDMGFgpdLEEILRRL---PKKRQILLL 154
|
....*
gi 1720388776 472 SATLD 476
Cdd:pfam00270 155 SATLP 159
|
|
| RWD |
pfam05773 |
RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. ... |
17-190 |
3.51e-07 |
|
RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. The function of this domain is unknown. GCN2 is the alpha-subunit of the only translation initiation factor (eIF2 alpha) kinase that appears in all eukaryotes. Its function requires an interaction with GCN1 via the domain at its N-terminus, which is termed the RWD domain after three major RWD-containing proteins: RING finger-containing proteins, WD-repeat-containing proteins, and yeast DEAD (DEXD)-like helicases. The structure forms an alpha + beta sandwich fold consisting of two layers: a four-stranded antiparallel beta-sheet, and three side-by-side alpha-helices.
Pssm-ID: 399058 Cd Length: 111 Bit Score: 49.63 E-value: 3.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 17 EQRQEETLALKSICGEKFiERIQNRVWtigleldyltnkfckskqkessknvrdtspetckfylkgnckfgskCKFKHEV 96
Cdd:pfam05773 1 EEQEEELEALESIYPDEF-EVISDSPY----------------------------------------------ESLEIEI 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 97 PPHqmigraernvnDPHLDADDDTTFMYELQIRFSKDhkYPYQAPLVAFySTNENLPLACRLHISEFLYGKALEFakTSE 176
Cdd:pfam05773 34 KLS-----------LDSDESDSSHLPPLVLKFTLPED--YPDEPPKISL-SSPWNLSDEQVLSLLEELEELAEEN--LGE 97
|
170
....*....|....
gi 1720388776 177 PVVYSLITLLEEES 190
Cdd:pfam05773 98 VMIFELIEWLQENL 111
|
|
| zf_CCCH_4 |
pfam18345 |
Zinc finger domain; This is a zinc finger domain found in Zinc finger CCCH-type with G patch ... |
76-94 |
1.47e-06 |
|
Zinc finger domain; This is a zinc finger domain found in Zinc finger CCCH-type with G patch domain-containing proteins such as ZIP. Functional studies indicate that ZIP specifically targets EGFR and represses its transcription, and that the zinc finger and the coiled-coil domains are central to that process.
Pssm-ID: 465719 [Multi-domain] Cd Length: 19 Bit Score: 45.49 E-value: 1.47e-06
|
| ZnF_C3H1 |
smart00356 |
zinc finger; |
73-94 |
2.36e-06 |
|
zinc finger;
Pssm-ID: 214632 [Multi-domain] Cd Length: 27 Bit Score: 44.93 E-value: 2.36e-06
|
| zf-CCCH |
pfam00642 |
Zinc finger C-x8-C-x5-C-x3-H type (and similar); |
74-94 |
3.13e-05 |
|
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
Pssm-ID: 459885 [Multi-domain] Cd Length: 27 Bit Score: 41.80 E-value: 3.13e-05
|
| zf-CCCH_4 |
pfam18044 |
CCCH-type zinc finger; This short zinc binding domain has the pattern of three cysteines and ... |
75-94 |
3.35e-05 |
|
CCCH-type zinc finger; This short zinc binding domain has the pattern of three cysteines and one histidine to coordinate the zinc ion. This domain is found in a wide variety of proteins such as E3 ligases.
Pssm-ID: 465626 Cd Length: 22 Bit Score: 41.81 E-value: 3.35e-05
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
322-493 |
2.95e-04 |
|
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350679 [Multi-domain] Cd Length: 181 Bit Score: 43.02 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 322 RETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSLNGPPervaNIICTQPRRisAIsVAERVA--KERAERVGLTVGY 399
Cdd:cd17921 7 REALRALYLSGDSVLVSAPTSSGKTLIAELAILRALATSGG----KAVYIAPTR--AL-VNQKEAdlRERFGPLGKNVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388776 400 QIRLESV---KSSATRLLYCTT---GVLLRRLeGDATLQGVTHIIVDEVH--ERTEESDFLLLVLKDIVMQRATLQVILM 471
Cdd:cd17921 80 LTGDPSVnklLLAEADILVATPeklDLLLRNG-GERLIQDVRLVVVDEAHliGDGERGVVLELLLSRLLRINKNARFVGL 158
|
170 180
....*....|....*....|...
gi 1720388776 472 SATLD-AGLFSKYFSYCPVITIP 493
Cdd:cd17921 159 SATLPnAEDLAEWLGVEDLIRFD 181
|
|
| zf-CCCH_2 |
pfam14608 |
RNA-binding, Nab2-type zinc finger; This is an unusual zinc-finger family, and is represented ... |
76-94 |
5.86e-04 |
|
RNA-binding, Nab2-type zinc finger; This is an unusual zinc-finger family, and is represented by fingers 5-7 of Nab2. Nab2 ZnF5-7 are zinc-fingers of the type C-x8-C-x5-C-x3-H. Nab2 ZnFs function in the generation of export-competent mRNPs. Mab2 is a conserved polyadenosine-RNA-binding Zn finger protein required for both mRNA export and polyadenylation regulation and becomes attached to the mRNP after splicing and during or immediately after polyadenylation. The three ZnFs, 5-7, have almost identical folds and, most unusually, associate with one another to form a single coherent structural unit. ZnF5-7 bind to eight consecutive adenines, and chemical shift perturbations identify residues on each finger that interact with RNA.
Pssm-ID: 464217 Cd Length: 19 Bit Score: 38.26 E-value: 5.86e-04
|
| |
