|
Name |
Accession |
Description |
Interval |
E-value |
| HrpA |
COG1643 |
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis]; |
476-1103 |
2.45e-119 |
|
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441249 [Multi-domain] Cd Length: 836 Bit Score: 392.14 E-value: 2.45e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 476 LPAWEERETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSLnGPPERvanIICTQPRRISAISVAERVAKERAERVGL 555
Cdd:COG1643 10 LPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGW-GAGGR---IGMLEPRRLAARAAAERMAEELGEPVGE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 556 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIvmQRAT---LQVILMS 632
Cdd:COG1643 86 TVGYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDL--QPALrpdLKLLVMS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 633 ATLDAGLFSKYFSYCPVITIPGRAFPVDqffledalavTRYvlqdgspymrsmkqiakeklkarhnrtaqeeveedLRLS 712
Cdd:COG1643 164 ATLDAERFARLLGDAPVIESSGRTYPVE----------VRY-----------------------------------RPLP 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 713 LHLQDEEESVKDTIpdqqldfkqllirykgvsksviktmsvmdfekvnlelIEALLEwivdgkhayPPGAVLVFLPGLAE 792
Cdd:COG1643 199 ADERDLEDAVADAV-------------------------------------REALAE---------EPGDILVFLPGERE 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 793 IKMLYEQLQsnslfnNRRSHRCVIHPLHSSLSSEEQQAVFVKPPMGVTKIIISTNIAETSITIDDVVYVIDSGKMKEKRY 872
Cdd:COG1643 233 IRRTAEALR------GRLPPDTEILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRY 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 873 DAGKGMESLEDTFVSQANALQRKGRAGRVASGVCFHLFTSHHYNhQLLKQQLPEIQRVPLEQLclrikILEMFS--THNL 950
Cdd:COG1643 307 DPRSGVTRLPTERISQASANQRAGRAGRLAPGICYRLWSEEDFA-RRPAFTDPEILRADLASL-----ILELAAwgLGDP 380
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 951 QSVfsRLIEPPHIDSLRASKVRLRDLGALTPDEKLTPLGYHLASLPVDVRIGKLMLLGSIFRCLDPALTIAASLAFKSPF 1030
Cdd:COG1643 381 EDL--PFLDPPPARAIADARALLQELGALDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDPR 458
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720388772 1031 VSPwdkkeeanqkklefafANSDYLALLcayKGWQlstkesaraSYNYCRQNFLSGRTLQEMASLKRQFTELL 1103
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 ... |
476-652 |
5.31e-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: 343.36 E-value: 5.31e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 476 LPAWEERETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSLNGPPERVANIICTQPRRISAISVAERVAKERAERVGL 555
Cdd:cd17985 1 LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFILDNSLQGPPLPVANIICTQPRRISAISVAERVAQERAERVGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 556 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIVMQRATLQVILMSATL 635
Cdd:cd17985 81 SVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDPTLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQRPDLKVILMSATL 160
|
170
....*....|....*..
gi 1720388772 636 DAGLFSKYFSYCPVITI 652
Cdd:cd17985 161 NAELFSDYFNSCPVIHI 177
|
|
| PRK11131 |
PRK11131 |
ATP-dependent RNA helicase HrpA; Provisional |
474-1108 |
1.02e-76 |
|
ATP-dependent RNA helicase HrpA; Provisional
Pssm-ID: 182986 [Multi-domain] Cd Length: 1294 Bit Score: 278.87 E-value: 1.02e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 474 QLLPAWEERETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSLNgppeRVANIICTQPRRISAISVAERVAKERAERV 553
Cdd:PRK11131 71 ENLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLELGRG----VKGLIGHTQPRRLAARTVANRIAEELETEL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 554 GLTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIVMQRATLQVILMSA 633
Cdd:PRK11131 147 GGCVGYKVRFNDQVSDNTMVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPDLKVIITSA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 634 TLDAGLFSKYFSYCPVITIPGRAFPVDqffledalavTRYvlqdgspymrsmkqiakeklkarhnRTAQEEVEEDLRlsl 713
Cdd:PRK11131 227 TIDPERFSRHFNNAPIIEVSGRTYPVE----------VRY-------------------------RPIVEEADDTER--- 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 714 hlqdeeesvkdtipDQqldfkqllirykgvsksviktmsvmdfekvnlelIEALLEwIVDGKHAYPPGAVLVFLPGLAEI 793
Cdd:PRK11131 269 --------------DQ----------------------------------LQAIFD-AVDELGREGPGDILIFMSGEREI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 794 KMLYEQLQSNSLFNNRrshrcvIHPLHSSLSSEEQQAVFvkPPMGVTKIIISTNIAETSITIDDVVYVIDSGKMKEKRYD 873
Cdd:PRK11131 300 RDTADALNKLNLRHTE------ILPLYARLSNSEQNRVF--QSHSGRRIVLATNVAETSLTVPGIKYVIDPGTARISRYS 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 874 AGKGMESLEDTFVSQANALQRKGRAGRVASGVCFHLFTSHHYNHqllKQQL--PEIQRVPLEQLclrikILEMFSThNLQ 951
Cdd:PRK11131 372 YRTKVQRLPIEPISQASANQRKGRCGRVSEGICIRLYSEDDFLS---RPEFtdPEILRTNLASV-----ILQMTAL-GLG 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 952 --SVFSrLIEPP---HI-DSLRAskvrLRDLGALTPDE-----KLTPLGYHLASLPVDVRIGKLMLLGSIFRCLDPALTI 1020
Cdd:PRK11131 443 diAAFP-FVEAPdkrNIqDGVRL----LEELGAITTDEqasayKLTPLGRQLAQLPVDPRLARMVLEAQKHGCVREVMII 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 1021 AASLAFKSPFVSPWDKKEEANQKKLEFAFANSDYLALLcayKGWQ-LSTKESARASYNY---CRQNFLSGRTLQEMASLK 1096
Cdd:PRK11131 518 TSALSIQDPRERPMDKQQASDEKHRRFADKESDFLAFV---NLWNyLQEQQKALSSNQFrrlCRTDYLNYLRVREWQDIY 594
|
650
....*....|..
gi 1720388772 1097 RQFTELLSDIGF 1108
Cdd:PRK11131 595 TQLRQVVKELGI 606
|
|
| DEAH_box_HrpB |
TIGR01970 |
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ... |
475-1024 |
6.53e-75 |
|
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: 267.02 E-value: 6.53e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 475 LLPAweeretILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSLNGppervANIICTQPRRISAISVAERVAKERAERVG 554
Cdd:TIGR01970 6 VLPA------LRDALAAHPQVVLEAPPGAGKSTAVPLALLDAPGIG-----GKIIMLEPRRLAARSAAQRLASQLGEAVG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 555 LTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIVMQ-RATLQVILMSA 633
Cdd:TIGR01970 75 QTVGYRVRGENKVSRRTRLEVVTEGILTRMIQDDPELDGVGALIFDEFHERSLDADLGLALALDVQSSlREDLKILAMSA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 634 TLDAGLFSKYFSYCPVITIPGRAFPVDqffledalavTRYvlqdgspymrsmkqiakeklkarhnRTAQeeveedlrlsl 713
Cdd:TIGR01970 155 TLDGERLSSLLPDAPVVESEGRSFPVE----------IRY-------------------------LPLR----------- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 714 hlqdeeesvkdtiPDQQLDfkqllirykgvsksviktmsvmdfEKVNLELIEALlewivdgkhAYPPGAVLVFLPGLAEI 793
Cdd:TIGR01970 189 -------------GDQRLE------------------------DAVSRAVEHAL---------ASETGSILVFLPGQAEI 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 794 KMLYEQLQSnslfnnRRSHRCVIHPLHSSLSSEEQQAVFVKPPMGVTKIIISTNIAETSITIDDVVYVIDSGKMKEKRYD 873
Cdd:TIGR01970 223 RRVQEQLAE------RLDSDVLICPLYGELSLAAQDRAIKPDPQGRRKVVLATNIAETSLTIEGIRVVIDSGLARVARFD 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 874 AGKGMESLEDTFVSQANALQRKGRAGRVASGVCFHLFtSHHYNHQLLKQQLPEIQRVPLEQLCLRIKILEMFSTHNLqsv 953
Cdd:TIGR01970 297 PKTGITRLETVRISQASATQRAGRAGRLEPGVCYRLW-SEEQHQRLPAQDEPEILQADLSGLALELAQWGAKDPSDL--- 372
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720388772 954 fsRLIEPPHIDSLRASKVRLRDLGALTPDEKLTPLGYHLASLPVDVRIGKLMLLGSIFRCLDPALTIAASL 1024
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 ... |
174-356 |
1.45e-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: 1.45e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 174 ECVEQRQEETLALKSICGEKFIERIQNRVWTIGLELDYLTNkfckskqkessknvrdtspetckfylkgnckfgskckfk 253
Cdd:cd23825 2 ELLEQRQEEAMALESIYGEAFSERIPNKVWTIKLDLPYLPW--------------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 254 hevpphqmigraernvndphldadddttfmYELQIRFSKDHKYPYQAPLVAFYSTNENLPLACRLHISEFLYGKALEFAK 333
Cdd:cd23825 43 ------------------------------FELEIRFPKGNKYPYEPPIVAFSSTNENFPKAVCLNITERLMEEALELAE 92
|
170 180
....*....|....*....|...
gi 1720388772 334 TSEPVVYSLITLLEEESEIVKLL 356
Cdd:cd23825 93 DGEPVVFSLVSLLEDEEEILELL 115
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
482-662 |
1.07e-24 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 102.96 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 482 RETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSLNGPPERVaniICTQPRRISAISVAERVAKE----RAERVGLTV 557
Cdd:smart00487 14 KEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRV---LVLVPTRELAEQWAEELKKLgpslGLKVVGLYG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 558 GYQIR--LESVKSSATRLLYCTTGVLLRRLE-GDATLQGVTHIIVDEVHERTEES--DFLLLVLKDIvmqRATLQVILMS 632
Cdd:smart00487 91 GDSKReqLRKLESGKTDILVTTPGRLLDLLEnDKLSLSNVDLVILDEAHRLLDGGfgDQLEKLLKLL---PKNVQLLLLS 167
|
170 180 190
....*....|....*....|....*....|....
gi 1720388772 633 ATLDAGL--FSKYFSYCPVITIPGRA--FPVDQF 662
Cdd:smart00487 168 ATPPEEIenLLELFLNDPVFIDVGFTplEPIEQF 201
|
|
| HA2 |
pfam04408 |
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ... |
973-1052 |
3.10e-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: 3.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 973 LRDLGALTPDEKLTPLGYHLASLPVDVRIGKLMLLGSIFRCLDPALTIAASLAFKSPFVSP----WDKKEEANQKKLEFA 1048
Cdd:pfam04408 5 LYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPnfldPRSAAKAARRRRRAA 84
|
....
gi 1720388772 1049 FANS 1052
Cdd:pfam04408 85 DEKA 88
|
|
| OB_NTP_bind |
pfam07717 |
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ... |
1146-1243 |
2.75e-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: 91.93 E-value: 2.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 1146 ISAVLCAALYPNVVqvktpegkfqktssgvvRLQPKSAELKFVtKNDGYVHIHPSSVNYQVRHFDSPYLLYHEKIKTSRV 1225
Cdd:pfam07717 1 LRAALAAGLYPNVA-----------------RRDPKGKGYTTL-SDNQRVFIHPSSVLFNEKTFPPEWVVYQELVETTKV 62
|
90
....*....|....*...
gi 1720388772 1226 FIRDCSMVSVYPLVLFGG 1243
Cdd:pfam07717 63 YIRTVTAISPEWLLLFAP 80
|
|
| UBA_DHX57 |
cd14317 |
UBA domain found in putative ATP-dependent RNA helicase DHX57 and similar proteins; DHX57, ... |
112-149 |
3.82e-13 |
|
UBA domain found in putative ATP-dependent RNA helicase DHX57 and similar proteins; DHX57, also called DEAH box protein 57, is a multi-domain protein with an N-terminal ubiquitin-association (UBA) domain, a Zinc finger domain, a RWD domain, a DEAD-like helicase domain and two C-terminal helicase associated domains. Although the precise biological function of DHX57 remains unclear, it may function as a putative ATP-dependent RNA helicase.
Pssm-ID: 270502 Cd Length: 38 Bit Score: 64.64 E-value: 3.82e-13
10 20 30
....*....|....*....|....*....|....*...
gi 1720388772 112 VSPLAVQKLSRYGFHTEHCQLALRICDGDLGAALEHLL 149
Cdd:cd14317 1 VSPFAVGKLSRYGFDKERCIQALRSNDGDIGAALEHLL 38
|
|
| RWD |
pfam05773 |
RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. ... |
177-350 |
3.18e-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: 50.01 E-value: 3.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 177 EQRQEETLALKSICGEKFiERIQNRVWtigleldyltnkfckskqkessknvrdtspetckfylkgnckfgskCKFKHEV 256
Cdd:pfam05773 1 EEQEEELEALESIYPDEF-EVISDSPY----------------------------------------------ESLEIEI 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 257 PPHqmigraernvnDPHLDADDDTTFMYELQIRFSKDhkYPYQAPLVAFySTNENLPLACRLHISEFLYGKALEFakTSE 336
Cdd:pfam05773 34 KLS-----------LDSDESDSSHLPPLVLKFTLPED--YPDEPPKISL-SSPWNLSDEQVLSLLEELEELAEEN--LGE 97
|
170
....*....|....
gi 1720388772 337 PVVYSLITLLEEES 350
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 ... |
236-254 |
3.15e-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: 44.72 E-value: 3.15e-06
|
| ZnF_C3H1 |
smart00356 |
zinc finger; |
233-254 |
4.88e-06 |
|
zinc finger;
Pssm-ID: 214632 [Multi-domain] Cd Length: 27 Bit Score: 44.16 E-value: 4.88e-06
|
| UBA |
smart00165 |
Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 ... |
116-149 |
3.75e-03 |
|
Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 is known to bind ubiquitin.
Pssm-ID: 197551 [Multi-domain] Cd Length: 37 Bit Score: 36.31 E-value: 3.75e-03
10 20 30
....*....|....*....|....*....|....
gi 1720388772 116 AVQKLSRYGFHTEHCQLALRICDGDLGAALEHLL 149
Cdd:smart00165 4 KIDQLLEMGFSREEALKALRAANGNVERAAEYLL 37
|
|
| UBA |
pfam00627 |
UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes ... |
112-148 |
7.28e-03 |
|
UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes the previously defined UBA and TS-N domains. The UBA-domain (ubiquitin associated domain) is a novel sequence motif found in several proteins having connections to ubiquitin and the ubiquitination pathway. The structure of the UBA domain consists of a compact three helix bundle. This domain is found at the N terminus of EF-TS hence the name TS-N. The structure of EF-TS is known and this domain is implicated in its interaction with EF-TU. The domain has been found in non EF-TS proteins such as alpha-NAC and MJ0280.
Pssm-ID: 395502 [Multi-domain] Cd Length: 37 Bit Score: 35.49 E-value: 7.28e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1720388772 112 VSPLAVQKLSRYGFHTEHCQLALRICDGDLGAALEHL 148
Cdd:pfam00627 1 EDEEAIQRLVEMGFDREQVREALRATGNNVERAAEYL 37
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HrpA |
COG1643 |
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis]; |
476-1103 |
2.45e-119 |
|
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441249 [Multi-domain] Cd Length: 836 Bit Score: 392.14 E-value: 2.45e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 476 LPAWEERETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSLnGPPERvanIICTQPRRISAISVAERVAKERAERVGL 555
Cdd:COG1643 10 LPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGW-GAGGR---IGMLEPRRLAARAAAERMAEELGEPVGE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 556 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIvmQRAT---LQVILMS 632
Cdd:COG1643 86 TVGYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDL--QPALrpdLKLLVMS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 633 ATLDAGLFSKYFSYCPVITIPGRAFPVDqffledalavTRYvlqdgspymrsmkqiakeklkarhnrtaqeeveedLRLS 712
Cdd:COG1643 164 ATLDAERFARLLGDAPVIESSGRTYPVE----------VRY-----------------------------------RPLP 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 713 LHLQDEEESVKDTIpdqqldfkqllirykgvsksviktmsvmdfekvnlelIEALLEwivdgkhayPPGAVLVFLPGLAE 792
Cdd:COG1643 199 ADERDLEDAVADAV-------------------------------------REALAE---------EPGDILVFLPGERE 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 793 IKMLYEQLQsnslfnNRRSHRCVIHPLHSSLSSEEQQAVFVKPPMGVTKIIISTNIAETSITIDDVVYVIDSGKMKEKRY 872
Cdd:COG1643 233 IRRTAEALR------GRLPPDTEILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRY 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 873 DAGKGMESLEDTFVSQANALQRKGRAGRVASGVCFHLFTSHHYNhQLLKQQLPEIQRVPLEQLclrikILEMFS--THNL 950
Cdd:COG1643 307 DPRSGVTRLPTERISQASANQRAGRAGRLAPGICYRLWSEEDFA-RRPAFTDPEILRADLASL-----ILELAAwgLGDP 380
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 951 QSVfsRLIEPPHIDSLRASKVRLRDLGALTPDEKLTPLGYHLASLPVDVRIGKLMLLGSIFRCLDPALTIAASLAFKSPF 1030
Cdd:COG1643 381 EDL--PFLDPPPARAIADARALLQELGALDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDPR 458
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720388772 1031 VSPwdkkeeanqkklefafANSDYLALLcayKGWQlstkesaraSYNYCRQNFLSGRTLQEMASLKRQFTELL 1103
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 ... |
476-652 |
5.31e-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: 343.36 E-value: 5.31e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 476 LPAWEERETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSLNGPPERVANIICTQPRRISAISVAERVAKERAERVGL 555
Cdd:cd17985 1 LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFILDNSLQGPPLPVANIICTQPRRISAISVAERVAQERAERVGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 556 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIVMQRATLQVILMSATL 635
Cdd:cd17985 81 SVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDPTLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQRPDLKVILMSATL 160
|
170
....*....|....*..
gi 1720388772 636 DAGLFSKYFSYCPVITI 652
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) ... |
492-652 |
4.12e-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: 276.65 E-value: 4.12e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 492 HQVVVISGMTGCGKTTQIPQFILDNSLNGPPErvANIICTQPRRISAISVAERVAKERAERVGLTVGYQIRLESVKSSAT 571
Cdd:cd17917 1 NQVVVIVGETGSGKTTQVPQFLLEDGLAKGGK--GRIVCTQPRRIAAISVAERVAEERGEKLGEEVGYQIRFESKTSSKT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 572 RLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIVMQRATLQVILMSATLDAGLFSKYFSYCPVIT 651
Cdd:cd17917 79 RIKFCTDGILLRELLSDPLLSGYSHVILDEAHERSLDTDFLLGLLKDLLRKRPDLKVILMSATLDAEKFSSYFGGAPVIH 158
|
.
gi 1720388772 652 I 652
Cdd:cd17917 159 I 159
|
|
| PRK11131 |
PRK11131 |
ATP-dependent RNA helicase HrpA; Provisional |
474-1108 |
1.02e-76 |
|
ATP-dependent RNA helicase HrpA; Provisional
Pssm-ID: 182986 [Multi-domain] Cd Length: 1294 Bit Score: 278.87 E-value: 1.02e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 474 QLLPAWEERETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSLNgppeRVANIICTQPRRISAISVAERVAKERAERV 553
Cdd:PRK11131 71 ENLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLELGRG----VKGLIGHTQPRRLAARTVANRIAEELETEL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 554 GLTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIVMQRATLQVILMSA 633
Cdd:PRK11131 147 GGCVGYKVRFNDQVSDNTMVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPDLKVIITSA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 634 TLDAGLFSKYFSYCPVITIPGRAFPVDqffledalavTRYvlqdgspymrsmkqiakeklkarhnRTAQEEVEEDLRlsl 713
Cdd:PRK11131 227 TIDPERFSRHFNNAPIIEVSGRTYPVE----------VRY-------------------------RPIVEEADDTER--- 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 714 hlqdeeesvkdtipDQqldfkqllirykgvsksviktmsvmdfekvnlelIEALLEwIVDGKHAYPPGAVLVFLPGLAEI 793
Cdd:PRK11131 269 --------------DQ----------------------------------LQAIFD-AVDELGREGPGDILIFMSGEREI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 794 KMLYEQLQSNSLFNNRrshrcvIHPLHSSLSSEEQQAVFvkPPMGVTKIIISTNIAETSITIDDVVYVIDSGKMKEKRYD 873
Cdd:PRK11131 300 RDTADALNKLNLRHTE------ILPLYARLSNSEQNRVF--QSHSGRRIVLATNVAETSLTVPGIKYVIDPGTARISRYS 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 874 AGKGMESLEDTFVSQANALQRKGRAGRVASGVCFHLFTSHHYNHqllKQQL--PEIQRVPLEQLclrikILEMFSThNLQ 951
Cdd:PRK11131 372 YRTKVQRLPIEPISQASANQRKGRCGRVSEGICIRLYSEDDFLS---RPEFtdPEILRTNLASV-----ILQMTAL-GLG 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 952 --SVFSrLIEPP---HI-DSLRAskvrLRDLGALTPDE-----KLTPLGYHLASLPVDVRIGKLMLLGSIFRCLDPALTI 1020
Cdd:PRK11131 443 diAAFP-FVEAPdkrNIqDGVRL----LEELGAITTDEqasayKLTPLGRQLAQLPVDPRLARMVLEAQKHGCVREVMII 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 1021 AASLAFKSPFVSPWDKKEEANQKKLEFAFANSDYLALLcayKGWQ-LSTKESARASYNY---CRQNFLSGRTLQEMASLK 1096
Cdd:PRK11131 518 TSALSIQDPRERPMDKQQASDEKHRRFADKESDFLAFV---NLWNyLQEQQKALSSNQFrrlCRTDYLNYLRVREWQDIY 594
|
650
....*....|..
gi 1720388772 1097 RQFTELLSDIGF 1108
Cdd:PRK11131 595 TQLRQVVKELGI 606
|
|
| DEAH_box_HrpB |
TIGR01970 |
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ... |
475-1024 |
6.53e-75 |
|
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: 267.02 E-value: 6.53e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 475 LLPAweeretILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSLNGppervANIICTQPRRISAISVAERVAKERAERVG 554
Cdd:TIGR01970 6 VLPA------LRDALAAHPQVVLEAPPGAGKSTAVPLALLDAPGIG-----GKIIMLEPRRLAARSAAQRLASQLGEAVG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 555 LTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIVMQ-RATLQVILMSA 633
Cdd:TIGR01970 75 QTVGYRVRGENKVSRRTRLEVVTEGILTRMIQDDPELDGVGALIFDEFHERSLDADLGLALALDVQSSlREDLKILAMSA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 634 TLDAGLFSKYFSYCPVITIPGRAFPVDqffledalavTRYvlqdgspymrsmkqiakeklkarhnRTAQeeveedlrlsl 713
Cdd:TIGR01970 155 TLDGERLSSLLPDAPVVESEGRSFPVE----------IRY-------------------------LPLR----------- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 714 hlqdeeesvkdtiPDQQLDfkqllirykgvsksviktmsvmdfEKVNLELIEALlewivdgkhAYPPGAVLVFLPGLAEI 793
Cdd:TIGR01970 189 -------------GDQRLE------------------------DAVSRAVEHAL---------ASETGSILVFLPGQAEI 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 794 KMLYEQLQSnslfnnRRSHRCVIHPLHSSLSSEEQQAVFVKPPMGVTKIIISTNIAETSITIDDVVYVIDSGKMKEKRYD 873
Cdd:TIGR01970 223 RRVQEQLAE------RLDSDVLICPLYGELSLAAQDRAIKPDPQGRRKVVLATNIAETSLTIEGIRVVIDSGLARVARFD 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 874 AGKGMESLEDTFVSQANALQRKGRAGRVASGVCFHLFtSHHYNHQLLKQQLPEIQRVPLEQLCLRIKILEMFSTHNLqsv 953
Cdd:TIGR01970 297 PKTGITRLETVRISQASATQRAGRAGRLEPGVCYRLW-SEEQHQRLPAQDEPEILQADLSGLALELAQWGAKDPSDL--- 372
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720388772 954 fsRLIEPPHIDSLRASKVRLRDLGALTPDEKLTPLGYHLASLPVDVRIGKLMLLGSIFRCLDPALTIAASL 1024
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 ... |
751-910 |
7.11e-73 |
|
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: 240.13 E-value: 7.11e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 751 MSVMDFEKVNLELIEALLEWIVdgkHAYPPGAVLVFLPGLAEIKMLYEQLQSNSLFNNrrSHRCVIHPLHSSLSSEEQQA 830
Cdd:cd18791 17 ISSEKEDPDYVDAAVRLILQIH---RTEEPGDILVFLPGQEEIERLCELLREELLSPD--LGKLLVLPLHSSLPPEEQQR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 831 VFVKPPMGVTKIIISTNIAETSITIDDVVYVIDSGKMKEKRYDAGKGMESLEDTFVSQANALQRKGRAGRVASGVCFHLF 910
Cdd:cd18791 92 VFEPPPPGVRKVVLATNIAETSITIPGVVYVIDSGLVKEKVYDPRTGLSSLVTVWISKASAEQRAGRAGRTRPGKCYRLY 171
|
|
| DEXHc_YTHDC2 |
cd17987 |
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) ... |
476-652 |
3.78e-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: 229.72 E-value: 3.78e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 476 LPAWEERETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSL-NGPPERvanIICTQPRRISAISVAERVAKERAERVG 554
Cdd:cd17987 1 LPVFEKQEQIVRIIKENKVVLIVGETGSGKTTQIPQFLLDDCYaNGIPCR---IFCTQPRRLAAIAVAERVAAERGEKIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 555 LTVGYQIRLESVKSSATRLLYCTTGVLLRRL-EGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIVMQRATLQVILMSA 633
Cdd:cd17987 78 QTVGYQIRLESRVSPKTLLTFCTNGVLLRTLmAGDSALSTVTHVIVDEVHERDRFSDFLLTKLRDILQKHPNLKLILSSA 157
|
170
....*....|....*....
gi 1720388772 634 TLDAGLFSKYFSYCPVITI 652
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 ... |
460-652 |
1.30e-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: 227.79 E-value: 1.30e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 460 KQASRQFHAILQERQLLPAWEERETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSLNGPPERVANIICTQPRRISAI 539
Cdd:cd17972 43 REQDHNLQQILQERELLPVKKFREEILEAISNNPVVIIRGATGCGKTTQVPQYILDDFIQNDRAAECNIVVTQPRRISAV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 540 SVAERVAKERAERVGLTVGYQIRLESV-KSSATRLLYCTTGVLLRRLEgdATLQGVTHIIVDEVHERTEESDFLLLVLKD 618
Cdd:cd17972 123 SVAERVAFERGEEVGKSCGYSVRFESVlPRPHASILFCTVGVLLRKLE--AGIRGISHVIVDEIHERDINTDFLLVVLRD 200
|
170 180 190
....*....|....*....|....*....|....
gi 1720388772 619 IVMQRATLQVILMSATLDAGLFSKYFSYCPVITI 652
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 ... |
476-652 |
1.70e-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: 222.48 E-value: 1.70e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 476 LPAWEERETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSL-NGPPERVANIICTQPRRISAISVAERVAKERAERVG 554
Cdd:cd17975 1 LPVFKHRESILETLKRHRVVVVAGETGSGKSTQVPQFLLEDLLlNGGTAQKCNIVCTQPRRISAMSLATRVCEELGCESG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 555 -----LTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIVMQRATLQVI 629
Cdd:cd17975 81 pggknSLCGYQIRMESRTGEATRLLYCTTGVLLRKLQEDGLLSSISHIIVDEVHERSVQSDFLLIILKEILHKRSDLHLI 160
|
170 180
....*....|....*....|...
gi 1720388772 630 LMSATLDAGLFSKYFSYCPVITI 652
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 ... |
476-652 |
8.56e-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: 217.40 E-value: 8.56e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 476 LPAWEERETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSLNGPPERVANIICTQPRRISAISVAERVAKERAERVGL 555
Cdd:cd17981 1 LPSYGMKQEIINMIDNNQVTVISGETGCGKTTQVTQFILDDAIERGKGSSCRIVCTQPRRISAISVAERVAAERAESCGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 556 --TVGYQIRLESVKS-SATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIVMQRATLQVILMS 632
Cdd:cd17981 81 gnSTGYQIRLESRKPrKQGSILYCTTGIVLQWLQSDPHLSNVSHLVLDEIHERNLQSDVLMGIVKDLLPFRSDLKVILMS 160
|
170 180
....*....|....*....|
gi 1720388772 633 ATLDAGLFSKYFSYCPVITI 652
Cdd:cd17981 161 ATLNAEKFSDYFNNCPMIHI 180
|
|
| PRK11664 |
PRK11664 |
ATP-dependent RNA helicase HrpB; Provisional |
475-1025 |
3.43e-63 |
|
ATP-dependent RNA helicase HrpB; Provisional
Pssm-ID: 236950 [Multi-domain] Cd Length: 812 Bit Score: 231.74 E-value: 3.43e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 475 LLPAWEERETILKLLSKHQVVVISGMTGCGKTTQIP-QFILDNSLNGppervaNIICTQPRRISAISVAERVAKERAERV 553
Cdd:PRK11664 3 SLPVAAVLPELLTALKTAPQVLLKAPTGAGKSTWLPlQLLQHGGING------KIIMLEPRRLAARNVAQRLAEQLGEKP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 554 GLTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDiVMQ--RATLQVILM 631
Cdd:PRK11664 77 GETVGYRMRAESKVGPNTRLEVVTEGILTRMIQRDPELSGVGLVILDEFHERSLQADLALALLLD-VQQglRDDLKLLIM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 632 SATLDAGLFSKYFSYCPVITIPGRAFPVDqffledalavTRYvlqdgspymrsmkqiakeklkarhnrtaqeeveEDLRL 711
Cdd:PRK11664 156 SATLDNDRLQQLLPDAPVIVSEGRSFPVE----------RRY---------------------------------QPLPA 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 712 SLHLqdeEESVKDTIpdqqldfKQLLIRykgvsksviktmsvmdfekvnlelieallewivdgkhayPPGAVLVFLPGLA 791
Cdd:PRK11664 193 HQRF---DEAVARAT-------AELLRQ---------------------------------------ESGSLLLFLPGVG 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 792 EIKMLYEQLQsnslfnNRRSHRCVIHPLHSSLSSEEQQAVFVKPPMGVTKIIISTNIAETSITIDDVVYVIDSGKMKEKR 871
Cdd:PRK11664 224 EIQRVQEQLA------SRVASDVLLCPLYGALSLAEQQKAILPAPAGRRKVVLATNIAETSLTIEGIRLVVDSGLERVAR 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 872 YDAGKGMESLEDTFVSQANALQRKGRAGRVASGVCFHLFTSHHYNHQLLkQQLPEIQRVPLEQLCLRikiLEMFSTHNLQ 951
Cdd:PRK11664 298 FDPKTGLTRLVTQRISQASMTQRAGRAGRLEPGICLHLYSKEQAERAAA-QSEPEILHSDLSGLLLE---LLQWGCHDPA 373
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720388772 952 SVfsRLIEPPHIDSLRASKVRLRDLGALTPDEKLTPLGYHLASLPVDVRIGKLMLLGSIFRclDPALTIAASLA 1025
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 ... |
476-652 |
2.09e-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: 207.72 E-value: 2.09e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 476 LPAWEERETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSLNGPPERVANIICTQPRRISAISVAERVAKERAERVGL 555
Cdd:cd17976 1 LPVDSHKESILSAIEQNPVVVISGDTGCGKTTRIPQFILEDYVLRGRGARCNVVITQPRRISAVSVAQRVAHELGPNLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 556 TVGYQIRLES-VKSSATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIVMQRATLQVILMSAT 634
Cdd:cd17976 81 NVGYQVRLESrPPPRGGALLFCTVGVLLKKLQSNPRLEGVSHVIVDEVHERDVNTDFLLILLKGVLQLNPELRVVLMSAT 160
|
170
....*....|....*...
gi 1720388772 635 LDAGLFSKYFSYCPVITI 652
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 ... |
465-652 |
1.37e-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: 202.65 E-value: 1.37e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 465 QFHAILQERQLLPAWEERETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSLNGPPERVanIICTQPRRISAISVAER 544
Cdd:cd17973 2 RYFEILEKRRELPVWEQKEDFLKLLKNNQILVLVGETGSGKTTQIPQFVLDDELPHQPKKL--VACTQPRRVAAMSVAQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 545 VAKERAERVGLTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIVMQRA 624
Cdd:cd17973 80 VAEEMDVKLGEEVGYSIRFEDCSSAKTILKYMTDGMLLREAMSDPLLSRYSVIILDEAHERTLATDILMGLLKEVVRRRP 159
|
170 180
....*....|....*....|....*...
gi 1720388772 625 TLQVILMSATLDAGLFSKYFSYCPVITI 652
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 ... |
476-652 |
5.44e-56 |
|
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: 191.89 E-value: 5.44e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 476 LPAWEERETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSLNgppervaNIICTQPRRISAISVAERVAKERAERVGL 555
Cdd:cd17979 1 LPIAQYREKIIELLKTHQVVIVAGDTGCGKSTQVPQYLLAAGFR-------HIACTQPRRIACISLAKRVAFESLNQYGS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 556 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIVMQRATLQVILMSATL 635
Cdd:cd17979 74 KVAYQIRFERTRTLATKLLFLTEGLLLRQIQRDASLPQYNVLILDEVHERHLHGDFLLGVLRCLLRLRPDLKLILMSATI 153
|
170
....*....|....*..
gi 1720388772 636 DAGLFSKYFSYCPVITI 652
Cdd:cd17979 154 NIELFSGYFEGAPVVQV 170
|
|
| DEXHc_TDRD9 |
cd17988 |
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ... |
476-645 |
4.21e-54 |
|
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: 186.94 E-value: 4.21e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 476 LPAWEERETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSLNgpPERVANIICTQPRRISAISVAERVAKERAERVGL 555
Cdd:cd17988 1 LPIYAKREEILSLIEANSVVIIKGATGCGKTTQLPQFILDHYYK--RGKYCNIVVTQPRRIAAISIARRVSQEREWTLGS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 556 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIVMQRAT-LQVILMSAT 634
Cdd:cd17988 79 LVGYQVGLERPASEETRLIYCTTGVLLQKLINNKTLTEYTHIILDEVHERDQELDFLLLVVRRLLRTNSRhVKIILMSAT 158
|
170
....*....|.
gi 1720388772 635 LDAGLFSKYFS 645
Cdd:cd17988 159 ISCKEFADYFT 169
|
|
| DEXHc_DHX33 |
cd17978 |
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA ... |
476-652 |
4.77e-54 |
|
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: 186.41 E-value: 4.77e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 476 LPAWEERETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSLNgppeRVANIICTQPRRISAISVAERVAKERAERVGL 555
Cdd:cd17978 1 LPIYSARKRLLEELRKHDTVIIIGETGSGKTTQIPQYLYEAGFA----RGGMIGITQPRRVAAVSVAKRVAEEMGVELGQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 556 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIVMQR-----ATLQVIL 630
Cdd:cd17978 77 LVGYSVRFDDVTSEETRIKYMTDGMLLREAIGDPLLSKYSVIILDEAHERTVHTDVLFGLVKSAQRRRkeqklSPLKVII 156
|
170 180
....*....|....*....|..
gi 1720388772 631 MSATLDAGLFSKYFSYCPVITI 652
Cdd:cd17978 157 MSATLDADLFSEYFNGAPVLYI 178
|
|
| RWD_DHX57 |
cd23825 |
RWD domain of DEAH box protein 57 (DHX57) and related proteins; DHX57 (EC 3.6.4.13) is a ... |
174-356 |
1.45e-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: 1.45e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 174 ECVEQRQEETLALKSICGEKFIERIQNRVWTIGLELDYLTNkfckskqkessknvrdtspetckfylkgnckfgskckfk 253
Cdd:cd23825 2 ELLEQRQEEAMALESIYGEAFSERIPNKVWTIKLDLPYLPW--------------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 254 hevpphqmigraernvndphldadddttfmYELQIRFSKDHKYPYQAPLVAFYSTNENLPLACRLHISEFLYGKALEFAK 333
Cdd:cd23825 43 ------------------------------FELEIRFPKGNKYPYEPPIVAFSSTNENFPKAVCLNITERLMEEALELAE 92
|
170 180
....*....|....*....|...
gi 1720388772 334 TSEPVVYSLITLLEEESEIVKLL 356
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 ... |
471-653 |
2.57e-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: 169.97 E-value: 2.57e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 471 QERQLLPAWEERETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSLNgppeRVANIICTQPRRISAISVAERVAKERA 550
Cdd:cd17971 1 EQRESLPIYKLKEQLIQAVHDNQILVVIGETGSGKTTQITQYLAEAGYT----SRGKIGCTQPRRVAAMSVAKRVAEEFG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 551 ERVGLTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIVMQRATLQVIL 630
Cdd:cd17971 77 CCLGQEVGYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLSQYSVIMLDEAHERTIHTDVLFGLLKKTVQKRPDLKLIV 156
|
170 180
....*....|....*....|...
gi 1720388772 631 MSATLDAGLFSKYFSYCPVITIP 653
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 ... |
476-646 |
2.79e-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: 167.26 E-value: 2.79e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 476 LPAWEERETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNslnGPPERVANIICTQPRRISAISVAERVAKERAERVGL 555
Cdd:cd17980 1 LPVFKLRNHILYLVENYQTIVIVGETGCGKSTQIPQYLAEA---GWTAGGRVVGCTQPRRVAAVTVAGRVAEEMGAVLGH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 556 TVGYQIRLESVKSS-ATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIVMQRATLQVILMSAT 634
Cdd:cd17980 78 EVGYCIRFDDCTDPqATRIKFLTDGMLVREMMLDPLLTKYSVIMLDEAHERTLYTDILIGLLKKIQKKRGDLRLIVASAT 157
|
170
....*....|..
gi 1720388772 635 LDAGLFSKYFSY 646
Cdd:cd17980 158 LDAEKFRDFFNQ 169
|
|
| DEXHc_DHX16 |
cd17974 |
DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably ... |
476-652 |
4.26e-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: 166.52 E-value: 4.26e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 476 LPAWEERETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNslnGPPERVANIICTQPRRISAISVAERVAKERAERVGL 555
Cdd:cd17974 1 LPVYPYRDDLLAAVKEHQVLIIVGETGSGKTTQIPQYLHEA---GYTKGGGKIGCTQPRRVAAMSVAARVAEEMGVKLGN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 556 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIVMQRATLQVILMSATL 635
Cdd:cd17974 78 EVGYSIRFEDCTSEKTVLKYMTDGMLLREFLTEPDLASYSVMIIDEAHERTLHTDILFGLVKDIARFRPDLKLLISSATM 157
|
170
....*....|....*..
gi 1720388772 636 DAGLFSKYFSYCPVITI 652
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 ... |
476-652 |
5.36e-44 |
|
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: 157.62 E-value: 5.36e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 476 LPAWEERETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSLNgppeRVANIICTQPRRISAISVAERVAKERAERVGL 555
Cdd:cd17983 1 LPIFAVRQELLNVIRDNNVVIVVGETGSGKTTQLTQYLHEDGYT----DYGMIGCTQPRRVAAMSVAKRVSEEMGVELGE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 556 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIVMQRATLQVILMSATL 635
Cdd:cd17983 77 EVGYAIRFEDCTSENTVIKYMTDGILLRESLRDPDLDKYSAIIMDEAHERSLNTDVLFGLLREVVARRRDLKLIVTSATM 156
|
170
....*....|....*..
gi 1720388772 636 DAGLFSKYFSYCPVITI 652
Cdd:cd17983 157 DADKFADFFGNVPIFTI 173
|
|
| DEXHc_HrpB |
cd17990 |
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ... |
476-650 |
1.39e-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: 1.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 476 LPAWEERETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSLNGPpervANIICTQPRRISAISVAERVAKERAERVGL 555
Cdd:cd17990 1 LPIAAVLPALRAALDAGGQVVLEAPPGAGKTTRVPLALLAELWIAG----GKIIVLEPRRVAARAAARRLATLLGEAPGE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 556 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIV-MQRATLQVILMSAT 634
Cdd:cd17990 77 TVGYRVRGESRVGRRTRVEVVTEGVLLRRLQRDPELSGVGAVILDEFHERSLDADLALALLLEVQqLLRDDLRLLAMSAT 156
|
170
....*....|....*.
gi 1720388772 635 LDAGLFSKYFSYCPVI 650
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 ... |
476-652 |
1.75e-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: 150.30 E-value: 1.75e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 476 LPAWEERETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSLNgppeRVANIICTQPRRISAISVAERVAKERAERVGL 555
Cdd:cd17989 1 LPVSQKRDEIAKAIAENQVVIIAGETGSGKTTQLPKICLELGRG----IRGLIGHTQPRRLAARSVAERIAEELKTELGG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 556 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIVMQRATLQVILMSATL 635
Cdd:cd17989 77 AVGYKVRFTDQTSDETCVKLMTDGILLAETQTDRYLRAYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKVIITSATI 156
|
170
....*....|....*..
gi 1720388772 636 DAGLFSKYFSYCPVITI 652
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 ... |
476-635 |
2.48e-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: 144.80 E-value: 2.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 476 LPAWEERETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSLNGP-PERVANIICTQPRRISAISVAERVAKERAErVG 554
Cdd:cd17982 1 LPILAEEQEIMEAINENPVVIICGETGSGKTTQVPQFLYEAGFGSPeSDNPGMIGITQPRRVAAVSMAKRVAEELNV-FG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 555 LTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIVMQRAT--------- 625
Cdd:cd17982 80 KEVSYQIRYDSTVSENTKIKFMTDGVLLKEIQTDFLLRKYSVIIIDEAHERSVNTDILIGMLSRIVPLRAKlylqdqtvk 159
|
170
....*....|.
gi 1720388772 626 -LQVILMSATL 635
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 ... |
476-652 |
6.98e-37 |
|
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: 137.29 E-value: 6.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 476 LPAWEERETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSLNgppeRVANIICTQPRRISAISVAERVAKERAERVGL 555
Cdd:cd17984 1 LPIQKQRKKLVQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGFS----QHGMIGVTQPRRVAAISVAQRVAEEMKCTLGS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 556 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIVMQRAT-----LQVIL 630
Cdd:cd17984 77 KVGYQVRFDDCSSKETAIKYMTDGCLLRHILADPNLTKYSVIILDEAHERSLTTDILFGLLKKLFQEKSPnrkehLKVVV 156
|
170 180
....*....|....*....|..
gi 1720388772 631 MSATLDAGLFSKYFSYCPVITI 652
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 ... |
476-650 |
1.95e-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: 1.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 476 LPAWEERETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSLNGPpERVANIICTQPRRISAISVAERVAKERAERVGL 555
Cdd:cd17977 1 LPVWEAKYEFMESLAHNQIVIVSGDAKTGKSSQIPQWCAEYCLSAH-YQHGVVVCTQVHKQTAVWLALRVADEMDVNIGH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 556 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIVMQRATLQVILMSATL 635
Cdd:cd17977 80 EVGYVIPFENCCTNETILRYCTDDMLLREMMSDPLLESYGVIILDDAHERTVSTDVLLGLLKDVLLSRPELKLVIITCPH 159
|
170
....*....|....*
gi 1720388772 636 DAGLFSKYFSYCPVI 650
Cdd:cd17977 160 LSSKLLSYYGNVPLI 174
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
482-662 |
1.07e-24 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 102.96 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 482 RETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSLNGPPERVaniICTQPRRISAISVAERVAKE----RAERVGLTV 557
Cdd:smart00487 14 KEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRV---LVLVPTRELAEQWAEELKKLgpslGLKVVGLYG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 558 GYQIR--LESVKSSATRLLYCTTGVLLRRLE-GDATLQGVTHIIVDEVHERTEES--DFLLLVLKDIvmqRATLQVILMS 632
Cdd:smart00487 91 GDSKReqLRKLESGKTDILVTTPGRLLDLLEnDKLSLSNVDLVILDEAHRLLDGGfgDQLEKLLKLL---PKNVQLLLLS 167
|
170 180 190
....*....|....*....|....*....|....
gi 1720388772 633 ATLDAGL--FSKYFSYCPVITIPGRA--FPVDQF 662
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 ... |
476-652 |
1.12e-23 |
|
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: 99.59 E-value: 1.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 476 LPAWEERETIL-KLLSKHQVVVISGMTGCGKTTQIPQFILDNSLNGPPERvANIICTQPRRISAISVAERVAKERAERVG 554
Cdd:cd17986 1 LPIWAAKFTFLeQLESPSGIVLVSGEPGSGKSTQVPQWCAEFALSRGFQK-GQVTVTQPHPLAARSLALRVADEMDLNLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 555 LTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHERTEESDFLLLVLKDIVMQRATLQVILMSat 634
Cdd:cd17986 80 HEVGYSIPQEDCTGPNTILRFCWDRLLLQEMTSTPLLGAWGVVVLDEAQERSVASDSLLGLLKDVRLQRPELRVVVVT-- 157
|
170 180
....*....|....*....|.
gi 1720388772 635 lDAGLFSKYFSYC---PVITI 652
Cdd:cd17986 158 -SPALEPKLRAFWgnpPVVHV 177
|
|
| HA2 |
pfam04408 |
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ... |
973-1052 |
3.10e-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: 3.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 973 LRDLGALTPDEKLTPLGYHLASLPVDVRIGKLMLLGSIFRCLDPALTIAASLAFKSPFVSP----WDKKEEANQKKLEFA 1048
Cdd:pfam04408 5 LYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPnfldPRSAAKAARRRRRAA 84
|
....
gi 1720388772 1049 FANS 1052
Cdd:pfam04408 85 DEKA 88
|
|
| HA2 |
smart00847 |
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ... |
976-1058 |
3.63e-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: 94.64 E-value: 3.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 976 LGALTPDEKLTPLGYHLASLPVDVRIGKLMLLGSIFRCLDPALTIAASLAFKSPFvsPWDKKEEANQKKLEFAFANSDYL 1055
Cdd:smart00847 2 LGALDDDGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPR--PKEKREDADAARRRFADPESDHL 79
|
...
gi 1720388772 1056 ALL 1058
Cdd:smart00847 80 TLL 82
|
|
| OB_NTP_bind |
pfam07717 |
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ... |
1146-1243 |
2.75e-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: 91.93 E-value: 2.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 1146 ISAVLCAALYPNVVqvktpegkfqktssgvvRLQPKSAELKFVtKNDGYVHIHPSSVNYQVRHFDSPYLLYHEKIKTSRV 1225
Cdd:pfam07717 1 LRAALAAGLYPNVA-----------------RRDPKGKGYTTL-SDNQRVFIHPSSVLFNEKTFPPEWVVYQELVETTKV 62
|
90
....*....|....*...
gi 1720388772 1226 FIRDCSMVSVYPLVLFGG 1243
Cdd:pfam07717 63 YIRTVTAISPEWLLLFAP 80
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
762-901 |
6.23e-14 |
|
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: 69.16 E-value: 6.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 762 ELIEALLEWIvdgkHAYPPGAVLVFLPGlaeIKMLYEQLqsnslFNNRRSHRCVihPLHSSLSSEEQQAVFVKPPMGVTK 841
Cdd:pfam00271 1 EKLEALLELL----KKERGGKVLIFSQT---KKTLEAEL-----LLEKEGIKVA--RLHGDLSQEEREEILEDFRKGKID 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 842 IIISTNIAETSITIDDVVYVIDsgkmkekrYDAGKGMESLedtfvsqanaLQRKGRAGRV 901
Cdd:pfam00271 67 VLVATDVAERGLDLPDVDLVIN--------YDLPWNPASY----------IQRIGRAGRA 108
|
|
| UBA_DHX57 |
cd14317 |
UBA domain found in putative ATP-dependent RNA helicase DHX57 and similar proteins; DHX57, ... |
112-149 |
3.82e-13 |
|
UBA domain found in putative ATP-dependent RNA helicase DHX57 and similar proteins; DHX57, also called DEAH box protein 57, is a multi-domain protein with an N-terminal ubiquitin-association (UBA) domain, a Zinc finger domain, a RWD domain, a DEAD-like helicase domain and two C-terminal helicase associated domains. Although the precise biological function of DHX57 remains unclear, it may function as a putative ATP-dependent RNA helicase.
Pssm-ID: 270502 Cd Length: 38 Bit Score: 64.64 E-value: 3.82e-13
10 20 30
....*....|....*....|....*....|....*...
gi 1720388772 112 VSPLAVQKLSRYGFHTEHCQLALRICDGDLGAALEHLL 149
Cdd:cd14317 1 VSPFAVGKLSRYGFDKERCIQALRSNDGDIGAALEHLL 38
|
|
| PHA02653 |
PHA02653 |
RNA helicase NPH-II; Provisional |
485-904 |
4.10e-13 |
|
RNA helicase NPH-II; Provisional
Pssm-ID: 177443 [Multi-domain] Cd Length: 675 Bit Score: 73.86 E-value: 4.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 485 ILKLLSKHQVVVISGMTGCGKTTQIPQFIL-DNSLNG---------PPERVANIICTQPR----RISAISVAERVAKERA 550
Cdd:PHA02653 172 IFEAWISRKPVVLTGGTGVGKTSQVPKLLLwFNYLFGgfdnldkidPNFIERPIVLSLPRvalvRLHSITLLKSLGFDEI 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 551 ERVGLTVGY---QIRLESVKSSATRLLYCTTGVLLRRLEGDATlqgvthIIVDEVHERTEESDFLLLVL-KDIVMQRAtl 626
Cdd:PHA02653 252 DGSPISLKYgsiPDELINTNPKPYGLVFSTHKLTLNKLFDYGT------VIIDEVHEHDQIGDIIIAVArKHIDKIRS-- 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 627 qVILMSATL--DAGLFSKYFSYCPVITIPGRA-FPVDQFfledalavtrYVLQDGSPYMRSMKqiakeklkarhnrtaqe 703
Cdd:PHA02653 324 -LFLMTATLedDRDRIKEFFPNPAFVHIPGGTlFPISEV----------YVKNKYNPKNKRAY----------------- 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 704 eVEEDLRLSLHlqdeeeSVKDTIPDQQldfkqllirykgvsKSVI---KTMSVMDFEKVNLE-LIEALLEWIVDGKhayp 779
Cdd:PHA02653 376 -IEEEKKNIVT------ALKKYTPPKG--------------SSGIvfvASVSQCEEYKKYLEkRLPIYDFYIIHGK---- 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 780 pgavlvfLPGLAEIkmlyeqlqSNSLFNNRRSHrcvihplhsslsseeqqavfvkppmgvtkIIISTNIAETSITIDDVV 859
Cdd:PHA02653 431 -------VPNIDEI--------LEKVYSSKNPS-----------------------------IIISTPYLESSVTIRNAT 466
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1720388772 860 YVIDSGKMKEKRYDAGKgmesleDTFVSQANALQRKGRAGRVASG 904
Cdd:PHA02653 467 HVYDTGRVYVPEPFGGK------EMFISKSMRTQRKGRVGRVSPG 505
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
810-900 |
4.62e-13 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 65.70 E-value: 4.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 810 RSHRCVIHPLHSSLSSEEQQAVFVKPPMGVTKIIISTNIAETSITIDDVVYVIDSgkmkekrydagkgmesleDTFVSQA 889
Cdd:smart00490 8 KELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIY------------------DLPWSPA 69
|
90
....*....|.
gi 1720388772 890 NALQRKGRAGR 900
Cdd:smart00490 70 SYIQRIGRAGR 80
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
495-634 |
2.54e-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: 65.89 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 495 VVISGMTGCGKTTQIPQFILDNSLNGPPERVanIICtqPRRISAISVAERVAKERAE--RVGLTVGY---QIRLESVKSS 569
Cdd:cd00046 4 VLITAPTGSGKTLAALLAALLLLLKKGKKVL--VLV--PTKALALQTAERLRELFGPgiRVAVLVGGssaEEREKNKLGD 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720388772 570 AtRLLYCTTGVLLRRLEGDA--TLQGVTHIIVDEVHERTEESDFLLLV-LKDIVMQRATLQVILMSAT 634
Cdd:cd00046 80 A-DIIIATPDMLLNLLLREDrlFLKDLKLIIVDEAHALLIDSRGALILdLAVRKAGLKNAQVILLSAT 146
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
482-636 |
2.02e-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: 63.80 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 482 RETILKLLSKHQVVVISGmTGCGKTT--QIPqfILDNSLNGPPERVANIICtqPRRISAISVAERvAKERAERVGLTV-- 557
Cdd:pfam00270 5 AEAIPAILEGRDVLVQAP-TGSGKTLafLLP--ALEALDKLDNGPQALVLA--PTRELAEQIYEE-LKKLGKGLGLKVas 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 558 ---GYQIRLESVKSSATRLLYCTTGVLLRRLEGDATLQGVTHIIVDEVHeRTEESDF---LLLVLKDIvmqRATLQVILM 631
Cdd:pfam00270 79 llgGDSRKEQLEKLKGPDILVGTPGRLLDLLQERKLLKNLKLLVLDEAH-RLLDMGFgpdLEEILRRL---PKKRQILLL 154
|
....*
gi 1720388772 632 SATLD 636
Cdd:pfam00270 155 SATLP 159
|
|
| RWD |
pfam05773 |
RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. ... |
177-350 |
3.18e-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: 50.01 E-value: 3.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 177 EQRQEETLALKSICGEKFiERIQNRVWtigleldyltnkfckskqkessknvrdtspetckfylkgnckfgskCKFKHEV 256
Cdd:pfam05773 1 EEQEEELEALESIYPDEF-EVISDSPY----------------------------------------------ESLEIEI 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 257 PPHqmigraernvnDPHLDADDDTTFMYELQIRFSKDhkYPYQAPLVAFySTNENLPLACRLHISEFLYGKALEFakTSE 336
Cdd:pfam05773 34 KLS-----------LDSDESDSSHLPPLVLKFTLPED--YPDEPPKISL-SSPWNLSDEQVLSLLEELEELAEEN--LGE 97
|
170
....*....|....
gi 1720388772 337 PVVYSLITLLEEES 350
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 ... |
236-254 |
3.15e-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: 44.72 E-value: 3.15e-06
|
| ZnF_C3H1 |
smart00356 |
zinc finger; |
233-254 |
4.88e-06 |
|
zinc finger;
Pssm-ID: 214632 [Multi-domain] Cd Length: 27 Bit Score: 44.16 E-value: 4.88e-06
|
| zf-CCCH |
pfam00642 |
Zinc finger C-x8-C-x5-C-x3-H type (and similar); |
234-254 |
6.16e-05 |
|
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
Pssm-ID: 459885 [Multi-domain] Cd Length: 27 Bit Score: 41.02 E-value: 6.16e-05
|
| zf-CCCH_4 |
pfam18044 |
CCCH-type zinc finger; This short zinc binding domain has the pattern of three cysteines and ... |
235-254 |
6.40e-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: 41.03 E-value: 6.40e-05
|
| UBA_VP13D |
cd14306 |
UBA domain found in vacuolar protein sorting-associated protein 13D (VP13D) and similar ... |
117-149 |
2.00e-04 |
|
UBA domain found in vacuolar protein sorting-associated protein 13D (VP13D) and similar proteins; VP13D is a chorea-acanthocytosis (CHAC)-similar protein encoded by gene VPS13D. it contains two putative domains, ubiquitin-associated (UBA) domain and lectin domain of ricin B chain profile (ricin-B-lectin), suggesting it may interact with, and be involved in the trafficking of, proteins modified with ubiquitin and/or carbohydrate molecules. Further investigation is required.
Pssm-ID: 270491 Cd Length: 36 Bit Score: 39.73 E-value: 2.00e-04
10 20 30
....*....|....*....|....*....|...
gi 1720388772 117 VQKLSRYGFHTEHCQLALRICDGDLGAALEHLL 149
Cdd:cd14306 1 VAKLMELGFPEEDCIRALRACGGNVEEAANWLL 33
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
482-653 |
2.05e-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: 43.79 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 482 RETILKLLSKHQVVVISGMTGCGKTTQIPQFILDNSLNGPPervaNIICTQPRRisAIsVAERVA--KERAERVGLTVGY 559
Cdd:cd17921 7 REALRALYLSGDSVLVSAPTSSGKTLIAELAILRALATSGG----KAVYIAPTR--AL-VNQKEAdlRERFGPLGKNVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388772 560 QIRLESV---KSSATRLLYCTT---GVLLRRLeGDATLQGVTHIIVDEVH--ERTEESDFLLLVLKDIVMQRATLQVILM 631
Cdd:cd17921 80 LTGDPSVnklLLAEADILVATPeklDLLLRNG-GERLIQDVRLVVVDEAHliGDGERGVVLELLLSRLLRINKNARFVGL 158
|
170 180
....*....|....*....|...
gi 1720388772 632 SATLD-AGLFSKYFSYCPVITIP 653
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 ... |
236-254 |
9.86e-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: 37.49 E-value: 9.86e-04
|
| UBA |
smart00165 |
Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 ... |
116-149 |
3.75e-03 |
|
Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 is known to bind ubiquitin.
Pssm-ID: 197551 [Multi-domain] Cd Length: 37 Bit Score: 36.31 E-value: 3.75e-03
10 20 30
....*....|....*....|....*....|....
gi 1720388772 116 AVQKLSRYGFHTEHCQLALRICDGDLGAALEHLL 149
Cdd:smart00165 4 KIDQLLEMGFSREEALKALRAANGNVERAAEYLL 37
|
|
| UBA |
cd14270 |
UBA domain found in proteins involved in ubiquitin-mediated proteolysis; The ... |
117-146 |
6.22e-03 |
|
UBA domain found in proteins involved in ubiquitin-mediated proteolysis; The ubiquitin-associated (UBA) domains are commonly occurring sequence motifs found in proteins involved in ubiquitin-mediated proteolysis. They contribute to ubiquitin (Ub) binding or ubiquitin-like (UbL) domain binding. However, some kinds of UBA domains can only the bind UbL domain, but not the Ub domain. UBA domains are normally comprised of compact three-helix bundles which contain a conserved GF/Y-loop. They can bind polyubiquitin with high affinity. They also bind monoubiquitin and other proteins. Most UBA domain-containing proteins have one UBA domain, but some harbor two or three UBA domains.
Pssm-ID: 270456 [Multi-domain] Cd Length: 30 Bit Score: 35.40 E-value: 6.22e-03
10 20 30
....*....|....*....|....*....|
gi 1720388772 117 VQKLSRYGFHTEHCQLALRICDGDLGAALE 146
Cdd:cd14270 1 LAQLVEMGFSREQARRALRATNGDVEAAVE 30
|
|
| UBA |
pfam00627 |
UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes ... |
112-148 |
7.28e-03 |
|
UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes the previously defined UBA and TS-N domains. The UBA-domain (ubiquitin associated domain) is a novel sequence motif found in several proteins having connections to ubiquitin and the ubiquitination pathway. The structure of the UBA domain consists of a compact three helix bundle. This domain is found at the N terminus of EF-TS hence the name TS-N. The structure of EF-TS is known and this domain is implicated in its interaction with EF-TU. The domain has been found in non EF-TS proteins such as alpha-NAC and MJ0280.
Pssm-ID: 395502 [Multi-domain] Cd Length: 37 Bit Score: 35.49 E-value: 7.28e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1720388772 112 VSPLAVQKLSRYGFHTEHCQLALRICDGDLGAALEHL 148
Cdd:pfam00627 1 EDEEAIQRLVEMGFDREQVREALRATGNNVERAAEYL 37
|
|
| |
