|
Name |
Accession |
Description |
Interval |
E-value |
| DEXHc_YTHDC2 |
cd17987 |
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) ... |
193-368 |
2.85e-119 |
|
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: 369.54 E-value: 2.85e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 193 LPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFLLDDCFKNGIPCRIFCTQPRRLAAIAVAERVAAERRERIGQTI 272
Cdd:cd17987 1 LPVFEKQEQIVRIIKENKVVLIVGETGSGKTTQIPQFLLDDCYANGIPCRIFCTQPRRLAAIAVAERVAAERGEKIGQTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 273 GYQIRLESRVSPKTLLTFCTNGVLLRTLMAGDSTLSTVTHVIVDEVHERDRFSDFLLTKLRDLLQKHPTLKLILSSAALD 352
Cdd:cd17987 81 GYQIRLESRVSPKTLLTFCTNGVLLRTLMAGDSALSTVTHVIVDEVHERDRFSDFLLTKLRDILQKHPNLKLILSSAALD 160
|
170
....*....|....*.
gi 1622946379 353 VNLFLRYFGSCPVIYI 368
Cdd:cd17987 161 VNLFIRYFGSCPVIYI 176
|
|
| HrpA |
COG1643 |
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis]; |
188-948 |
1.31e-82 |
|
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441249 [Multi-domain] Cd Length: 836 Bit Score: 290.44 E-value: 1.31e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 188 SFRQSLPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFLLD-DCFKNGipcRIFCTQPRRLAAIAVAERVAAERRE 266
Cdd:COG1643 5 TYPPDLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLElGWGAGG---RIGMLEPRRLAARAAAERMAEELGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 267 RIGQTIGYQIRLESRVSPKTLLTFCTNGVLLRTLMAgDSTLSTVTHVIVDEVHERDRFSDFLLTKLRDLLQKhptlklil 346
Cdd:COG1643 82 PVGETVGYRVRFEDKVSAATRIEVVTEGILLRELQR-DPELEGVDTVIFDEFHERSLNADLLLALLLDLQPA-------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 347 ssaaldvnlfLRyfgscpviyiqgrpfevkemflEDilrttgytnkemLKykkekqqeekqqttltewysaqentfkpes 426
Cdd:COG1643 153 ----------LR----------------------PD------------LK------------------------------ 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 427 qrqrtvpnvtdeydllddggdavfsqltekdvnclepwlikemdaclsdiwlhkdidafaqvfhLILTenvsvdyrhset 506
Cdd:COG1643 159 ----------------------------------------------------------------LLVM------------ 162
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 507 SATalmvaagrgfasqveqlismganvhskasngwmaLD---WAKHFGQTEIVdllesysaslefgnldESS----LVQT 579
Cdd:COG1643 163 SAT----------------------------------LDaerFARLLGDAPVI----------------ESSgrtyPVEV 192
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 580 NGSDLSAEDRELLKAyhhsfddekVdLDLIMHLLYNichscDAGAVLIFLPGYDEIVGLRDRIlfdDKRFADSThryQVF 659
Cdd:COG1643 193 RYRPLPADERDLEDA---------V-ADAVREALAE-----EPGDILVFLPGEREIRRTAEAL---RGRLPPDT---EIL 251
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 660 MLHSNMQTSDQKKVLKNPPAGVRKIILSTNIAETSITVNDVVFVIDSGKVKEKSFDALNFVTMLKMVWISKASAIQRKGR 739
Cdd:COG1643 252 PLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERISQASANQRAGR 331
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 740 AGRCRPGICFRLFSRLRFQNMLEFQTPELLRMPLQELCLHTKLLapvNCP-IADFLMkaPEPPPALIVRNAVQMLKTIDA 818
Cdd:COG1643 332 AGRLAPGICYRLWSEEDFARRPAFTDPEILRADLASLILELAAW---GLGdPEDLPF--LDPPPARAIADARALLQELGA 406
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 819 MDTWEDLTELGYHLADLPVEPHLGKMVLCAVVLKCLDPILTIACTLAYRDPFvlptqasqkraamlcrkRFTAGafSDHM 898
Cdd:COG1643 407 LDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDPR-----------------RGAAG--SDLL 467
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 1622946379 899 ALLRAFQAWQKARsdgwerafceKNFLSQATMEIIIGMRTQLLGQLRASG 948
Cdd:COG1643 468 ARLNLWRRLREQQ----------REFLSYLRLREWRDLARQLRRLLGEGA 507
|
|
| SF2_C_RHA |
cd18791 |
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ... |
597-752 |
3.06e-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: 238.20 E-value: 3.06e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 597 HSFDDEKVDLDLIMHLLYNICHSCDAGAVLIFLPGYDEIVGLRDRILfdDKRFADSTHRYQVFMLHSNMQTSDQKKVLKN 676
Cdd:cd18791 18 SSEKEDPDYVDAAVRLILQIHRTEEPGDILVFLPGQEEIERLCELLR--EELLSPDLGKLLVLPLHSSLPPEEQQRVFEP 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622946379 677 PPAGVRKIILSTNIAETSITVNDVVFVIDSGKVKEKSFDALNFVTMLKMVWISKASAIQRKGRAGRCRPGICFRLF 752
Cdd:cd18791 96 PPPGVRKVVLATNIAETSITIPGVVYVIDSGLVKEKVYDPRTGLSSLVTVWISKASAEQRAGRAGRTRPGKCYRLY 171
|
|
| PRK11131 |
PRK11131 |
ATP-dependent RNA helicase HrpA; Provisional |
155-1018 |
1.12e-65 |
|
ATP-dependent RNA helicase HrpA; Provisional
Pssm-ID: 182986 [Multi-domain] Cd Length: 1294 Bit Score: 244.97 E-value: 1.12e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 155 AVEAE-NREMSKTSGRLNN---GIPQIpvkrgesefdSFRQSLPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFL 230
Cdd:PRK11131 41 AIFQEiAKEIAQAAQRVLLreaARPEI----------TYPENLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKIC 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 231 LDdcFKNGIPCRIFCTQPRRLAAIAVAERVAAERRERIGQTIGYQIRLESRVSPKTLLTFCTNGVLL------RTLMAGD 304
Cdd:PRK11131 111 LE--LGRGVKGLIGHTQPRRLAARTVANRIAEELETELGGCVGYKVRFNDQVSDNTMVKLMTDGILLaeiqqdRLLMQYD 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 305 StlstvthVIVDEVHERDRFSDFLLTKLRDLLQKHPTLKLILSSAALDVNLFLRYFGSCPVIYIQGR--PFEVkemfled 382
Cdd:PRK11131 189 T-------IIIDEAHERSLNIDFILGYLKELLPRRPDLKVIITSATIDPERFSRHFNNAPIIEVSGRtyPVEV------- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 383 ilrttgytnkemlkykkekqqeekqqttltewysaqentfkpesqRQRtvPNVTDEYDLLDDGGDAVFsqltekdvncle 462
Cdd:PRK11131 255 ---------------------------------------------RYR--PIVEEADDTERDQLQAIF------------ 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 463 pwlikemDAclsdiwlhkdidafaqvfhliltenvsVDYRHSEtsatalmvaaGRGfasqvEQLISMGanvhskasngwm 542
Cdd:PRK11131 276 -------DA---------------------------VDELGRE----------GPG-----DILIFMS------------ 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 543 aldwakhfGQTEIVDLLESysaslefgnLDESSLVQTngsdlsaedrellkayhhsfddekvdldlimhllynichscda 622
Cdd:PRK11131 295 --------GEREIRDTADA---------LNKLNLRHT------------------------------------------- 314
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 623 gavliflpgydEIVGLRDRIlfddkrfadsthryqvfmlhSNmqtSDQKKVLKnpPAGVRKIILSTNIAETSITVNDVVF 702
Cdd:PRK11131 315 -----------EILPLYARL--------------------SN---SEQNRVFQ--SHSGRRIVLATNVAETSLTVPGIKY 358
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 703 VIDSGKVKEKSFDALNFVTMLKMVWISKASAIQRKGRAGRCRPGICFRLFSRLRFQNMLEFQTPELLRMPLQELCLHTKL 782
Cdd:PRK11131 359 VIDPGTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVSEGICIRLYSEDDFLSRPEFTDPEILRTNLASVILQMTA 438
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 783 LAPVNcpIADFlmkaP--EPPPALIVRNAVQMLKTIDAMDTWED-----LTELGYHLADLPVEPHLGKMVLCAVVLKCLD 855
Cdd:PRK11131 439 LGLGD--IAAF----PfvEAPDKRNIQDGVRLLEELGAITTDEQasaykLTPLGRQLAQLPVDPRLARMVLEAQKHGCVR 512
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 856 PILTIACTLAYRDPFVLPT---QASQKRaamlcRKRFtAGAFSDHMALLRAF---QAWQKARSDGWERAFCEKNFLSQAT 929
Cdd:PRK11131 513 EVMIITSALSIQDPRERPMdkqQASDEK-----HRRF-ADKESDFLAFVNLWnylQEQQKALSSNQFRRLCRTDYLNYLR 586
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 930 MEIIIGMRTQLLGQLRASGFvrargggdirDVNTNSENWAVVKAALVAGMypnLVHV---DRENLVLTGPkeKKVRFH-- 1004
Cdd:PRK11131 587 VREWQDIYTQLRQVVKELGI----------PVNSEPAEYREIHTALLTGL---LSHIgmkDAEKQEYTGA--RNARFSif 651
|
890
....*....|....
gi 1622946379 1005 PASVLsqpqYKKIP 1018
Cdd:PRK11131 652 PGSGL----FKKPP 661
|
|
| YTH |
cd21134 |
YTH (YT521-B homology) domains are RNA-binding domains that belong to the PUA superfamily; ... |
1289-1418 |
4.06e-64 |
|
YTH (YT521-B homology) domains are RNA-binding domains that belong to the PUA superfamily; Individual members of the YTH family have been shown to selectively remove transcripts of meiosis-specific genes expressed in mitotic cells. In general, eukaryotic YTH-family members may be involved in similar mechanisms to suppress gene regulation during gametogenesis or in other forms of silencing. The YTH domain is a novel RNA-binding domain that has been shown to bind to short, degenerate, single-stranded RNA motifs that loosely follow a consensus sequence. It belongs to the larger PUA superfamily.
Pssm-ID: 410979 Cd Length: 133 Bit Score: 213.58 E-value: 4.06e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 1289 RYFIMKSSNLRNLEISQQKGIWSTTPSNERKLNRAFWESSMVYLVFSVQGSGHFQGFSRMSSEIGREKS---QDWGSAGL 1365
Cdd:cd21134 1 RFFIIKSNNEENIHLSIKYGVWATQPHNEKKLNQAFRESGNVYLIFSVNGSGHFQGYARMTSPPDPNRSpswPWWSQDKL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1622946379 1366 GGVFKVEWIRKESLPFQFAHHLLNPWNDNKKVQISRDGQELEPQVGEQLLQLW 1418
Cdd:cd21134 81 GGPFKVEWLRVKDLPFSKLRHLKNPLNENKPVTISRDGQEIEPEVGEQLLKLF 133
|
|
| YTH |
pfam04146 |
YT521-B-like domain; A protein of the YTH family has been shown to selectively remove ... |
1288-1419 |
5.34e-60 |
|
YT521-B-like domain; A protein of the YTH family has been shown to selectively remove transcripts of meiosis-specific genes expressed in mitotic cells. It has been speculated that in higher eukaryotic YTH-family members may be involved in similar mechanisms to suppress gene regulation during gametogenesis or general silencing. The rat protein YT521-B is a tyrosine-phosphorylated nuclear protein, that interacts with the nuclear transcriptosomal component scaffold attachment factor B, and the 68-kDa Src substrate associated during mitosis, Sam68. In vivo splicing assays demonstrated that YT521-B modulates alternative splice site selection in a concentration-dependent manner. The YTH domain has been identified as part of the PUA superfamily.
Pssm-ID: 461195 Cd Length: 135 Bit Score: 201.96 E-value: 5.34e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 1288 VRYFIMKSSNLRNLEISQQKGIWSTTPSNERKLNRAFWESSMVYLVFSVQGSGHFQGFSRMSSEIGREKSQ-DWGSAGL- 1365
Cdd:pfam04146 1 ARFFIIKSLNEENIHLSIKYGIWATQPHNNKRLNEAFKESKNVYLIFSVNKSGHFQGYARMTSPVDFDPSFiFWEADSDk 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1622946379 1366 -GGVFKVEWIRKESLPFQFAHHLLNPWNDNKKVQISRDGQELEPQVGEQLLQLWE 1419
Cdd:pfam04146 81 wGGPFKVEWLSVKDLPFSRLRHLRNPLNENKPVKISRDGQEIEPEVGRQLLKLFD 135
|
|
| R3H_DEXH_helicase |
cd06007 |
R3H domain of a group of proteins which also contain a DEXH-box helicase domain, and may ... |
46-104 |
7.98e-28 |
|
R3H domain of a group of proteins which also contain a DEXH-box helicase domain, and may function as ATP-dependent DNA or RNA helicases. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.
Pssm-ID: 100077 Cd Length: 59 Bit Score: 107.01 E-value: 7.98e-28
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622946379 46 KIAVNIALERFRYGDQREMEFPSSLTSTERAFIHRLSQSLGLVSKSKGKGANRYLTVKK 104
Cdd:cd06007 1 RIAINKALEDFRASDNEEYEFPSSLTNHERAVIHRLCRKLGLKSKSKGKGSNRRLSVYK 59
|
|
| HA2 |
pfam04408 |
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ... |
809-900 |
1.69e-27 |
|
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: 107.71 E-value: 1.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 809 AVQMLKTIDAMDTWEDLTELGYHLADLPVEPHLGKMVLCAVVLKCLDPILTIACTLAYRDPFVLPTQASQKRAAMLCRKR 888
Cdd:pfam04408 1 ALELLYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPNFLDPRSAAKAARRR 80
|
90 100
....*....|....*....|....
gi 1622946379 889 FTA------------GAFSDHMAL 900
Cdd:pfam04408 81 RRAadekarakfarlDLEGDHLTL 104
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
199-372 |
8.84e-23 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 97.56 E-value: 8.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 199 QEEIVKIIKEN-KVVLIVGETGSGKTTQIPQFLLdDCFKNGIPCRIFCTQPRRLAAIAVAERVAAERRERIGQTIGY--- 274
Cdd:smart00487 13 QKEAIEALLSGlRDVILAAPTGSGKTLAALLPAL-EALKRGKGGRVLVLVPTRELAEQWAEELKKLGPSLGLKVVGLygg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 275 ---QIRLESRVSPKTLLTFCTNGVLLRTLMAGDSTLSTVTHVIVDEVHERDR--FSDFLLTKLRDLlqkHPTLKLILSSA 349
Cdd:smart00487 92 dskREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDggFGDQLEKLLKLL---PKNVQLLLLSA 168
|
170 180
....*....|....*....|....*
gi 1622946379 350 ALDVNL--FLRYFGSCPVIYIQGRP 372
Cdd:smart00487 169 TPPEEIenLLELFLNDPVFIDVGFT 193
|
|
| HA2 |
smart00847 |
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ... |
816-901 |
5.77e-18 |
|
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: 79.62 E-value: 5.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 816 IDAMDTWEDLTELGYHLADLPVEPHLGKMVLCAVVLKCLDPILTIACTLAYRDPFvlptQASQKRAAMLCRKRFtAGAFS 895
Cdd:smart00847 2 LGALDDDGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPR----PKEKREDADAARRRF-ADPES 76
|
....*.
gi 1622946379 896 DHMALL 901
Cdd:smart00847 77 DHLTLL 82
|
|
| OB_NTP_bind |
pfam07717 |
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ... |
971-1066 |
4.13e-12 |
|
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: 63.04 E-value: 4.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 971 VKAALVAGMYPNLVHVDRENLVLTGPKEK-KVRFHPASVLSQPqyKKIPPAngqaaaikalptdWLIYDEMTRAHRIAnI 1049
Cdd:pfam07717 1 LRAALAAGLYPNVARRDPKGKGYTTLSDNqRVFIHPSSVLFNE--KTFPPE-------------WVVYQELVETTKVY-I 64
|
90
....*....|....*..
gi 1622946379 1050 RCCSAVTPVTILVFCGP 1066
Cdd:pfam07717 65 RTVTAISPEWLLLFAPH 81
|
|
| R3H |
pfam01424 |
R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most ... |
44-104 |
1.62e-09 |
|
R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to be binding ssDNA.
Pssm-ID: 460206 Cd Length: 60 Bit Score: 55.19 E-value: 1.62e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622946379 44 EVKIAVNIALERFRYGDQREMEFPSsLTSTERAFIHRLSQSLGLVSKSKGKGANRYLTVKK 104
Cdd:pfam01424 1 EFLEQLAEKLAEFVKDTGKSLELPP-MSSYERRIIHELAQKYGLESESEGEEPNRRVVVYK 60
|
|
| PHA02653 |
PHA02653 |
RNA helicase NPH-II; Provisional |
156-379 |
1.99e-08 |
|
RNA helicase NPH-II; Provisional
Pssm-ID: 177443 [Multi-domain] Cd Length: 675 Bit Score: 58.84 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 156 VEAENR-------EMSKTS--GRLNNGIPQIPVKrgesefdsFRQSLPvfEKQEEIVKIIKENKVVLIVGETGSGKTTQI 226
Cdd:PHA02653 127 VEGGNAlgifsnnVGSKKDtiGILGNPEPFSKIP--------LASLQP--DVQLKIFEAWISRKPVVLTGGTGVGKTSQV 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 227 PQFL-----LDDCFKN-GIPCRIFCTQPRRLAAiavaERVAAERRERIG--QTIGYQIRLESRVSPK------------- 285
Cdd:PHA02653 197 PKLLlwfnyLFGGFDNlDKIDPNFIERPIVLSL----PRVALVRLHSITllKSLGFDEIDGSPISLKygsipdelintnp 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 286 --TLLTFCTNGVLLRTLMAGDStlstvthVIVDEVHERDRFSDFLLTKLRdllqKHPTL--KLILSSAAL--DVNLFLRY 359
Cdd:PHA02653 273 kpYGLVFSTHKLTLNKLFDYGT-------VIIDEVHEHDQIGDIIIAVAR----KHIDKirSLFLMTATLedDRDRIKEF 341
|
250 260
....*....|....*....|.
gi 1622946379 360 FGSCPVIYIQGRP-FEVKEMF 379
Cdd:PHA02653 342 FPNPAFVHIPGGTlFPISEVY 362
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
199-355 |
9.35e-08 |
|
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: 53.02 E-value: 9.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 199 QEEIVKIIKENKVVLIVGETGSGKTT--QIPqfLLDDCFKNGIPCRIFCTQPRR-LAA--IAVAERVAAERRERI----- 268
Cdd:pfam00270 4 QAEAIPAILEGRDVLVQAPTGSGKTLafLLP--ALEALDKLDNGPQALVLAPTReLAEqiYEELKKLGKGLGLKVasllg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 269 GQTIGYQIRLESRVSpktlLTFCTNGVLLrTLMAGDSTLSTVTHVIVDEVHE--RDRFSDFLLTKLRDLLQKHPTLKLil 346
Cdd:pfam00270 82 GDSRKEQLEKLKGPD----ILVGTPGRLL-DLLQERKLLKNLKLLVLDEAHRllDMGFGPDLEEILRRLPKKRQILLL-- 154
|
....*....
gi 1622946379 347 sSAALDVNL 355
Cdd:pfam00270 155 -SATLPRNL 162
|
|
| R3H |
smart00393 |
Putative single-stranded nucleic acids-binding domain; |
51-105 |
2.22e-06 |
|
Putative single-stranded nucleic acids-binding domain;
Pssm-ID: 214647 Cd Length: 79 Bit Score: 46.91 E-value: 2.22e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1622946379 51 IALERFRYGDQREMEFPSsLTSTERAFIHRLSQSLGLVSKSKGKGANRYLTVKKK 105
Cdd:smart00393 26 LEIARFVKSTKESVELPP-MNSYERKIVHELAEKYGLESESFGEGPKRRVVISKK 79
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DEXHc_YTHDC2 |
cd17987 |
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) ... |
193-368 |
2.85e-119 |
|
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: 369.54 E-value: 2.85e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 193 LPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFLLDDCFKNGIPCRIFCTQPRRLAAIAVAERVAAERRERIGQTI 272
Cdd:cd17987 1 LPVFEKQEQIVRIIKENKVVLIVGETGSGKTTQIPQFLLDDCYANGIPCRIFCTQPRRLAAIAVAERVAAERGEKIGQTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 273 GYQIRLESRVSPKTLLTFCTNGVLLRTLMAGDSTLSTVTHVIVDEVHERDRFSDFLLTKLRDLLQKHPTLKLILSSAALD 352
Cdd:cd17987 81 GYQIRLESRVSPKTLLTFCTNGVLLRTLMAGDSALSTVTHVIVDEVHERDRFSDFLLTKLRDILQKHPNLKLILSSAALD 160
|
170
....*....|....*.
gi 1622946379 353 VNLFLRYFGSCPVIYI 368
Cdd:cd17987 161 VNLFIRYFGSCPVIYI 176
|
|
| DEXHc_RHA-like |
cd17917 |
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ... |
209-368 |
5.78e-87 |
|
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: 279.73 E-value: 5.78e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 209 NKVVLIVGETGSGKTTQIPQFLLDDCFKNGIPCRIFCTQPRRLAAIAVAERVAAERRERIGQTIGYQIRLESRVSPKTLL 288
Cdd:cd17917 1 NQVVVIVGETGSGKTTQVPQFLLEDGLAKGGKGRIVCTQPRRIAAISVAERVAEERGEKLGEEVGYQIRFESKTSSKTRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 289 TFCTNGVLLRTLMaGDSTLSTVTHVIVDEVHERDRFSDFLLTKLRDLLQKHPTLKLILSSAALDVNLFLRYFGSCPVIYI 368
Cdd:cd17917 81 KFCTDGILLRELL-SDPLLSGYSHVILDEAHERSLDTDFLLGLLKDLLRKRPDLKVILMSATLDAEKFSSYFGGAPVIHI 159
|
|
| HrpA |
COG1643 |
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis]; |
188-948 |
1.31e-82 |
|
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441249 [Multi-domain] Cd Length: 836 Bit Score: 290.44 E-value: 1.31e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 188 SFRQSLPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFLLD-DCFKNGipcRIFCTQPRRLAAIAVAERVAAERRE 266
Cdd:COG1643 5 TYPPDLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLElGWGAGG---RIGMLEPRRLAARAAAERMAEELGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 267 RIGQTIGYQIRLESRVSPKTLLTFCTNGVLLRTLMAgDSTLSTVTHVIVDEVHERDRFSDFLLTKLRDLLQKhptlklil 346
Cdd:COG1643 82 PVGETVGYRVRFEDKVSAATRIEVVTEGILLRELQR-DPELEGVDTVIFDEFHERSLNADLLLALLLDLQPA-------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 347 ssaaldvnlfLRyfgscpviyiqgrpfevkemflEDilrttgytnkemLKykkekqqeekqqttltewysaqentfkpes 426
Cdd:COG1643 153 ----------LR----------------------PD------------LK------------------------------ 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 427 qrqrtvpnvtdeydllddggdavfsqltekdvnclepwlikemdaclsdiwlhkdidafaqvfhLILTenvsvdyrhset 506
Cdd:COG1643 159 ----------------------------------------------------------------LLVM------------ 162
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 507 SATalmvaagrgfasqveqlismganvhskasngwmaLD---WAKHFGQTEIVdllesysaslefgnldESS----LVQT 579
Cdd:COG1643 163 SAT----------------------------------LDaerFARLLGDAPVI----------------ESSgrtyPVEV 192
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 580 NGSDLSAEDRELLKAyhhsfddekVdLDLIMHLLYNichscDAGAVLIFLPGYDEIVGLRDRIlfdDKRFADSThryQVF 659
Cdd:COG1643 193 RYRPLPADERDLEDA---------V-ADAVREALAE-----EPGDILVFLPGEREIRRTAEAL---RGRLPPDT---EIL 251
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 660 MLHSNMQTSDQKKVLKNPPAGVRKIILSTNIAETSITVNDVVFVIDSGKVKEKSFDALNFVTMLKMVWISKASAIQRKGR 739
Cdd:COG1643 252 PLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERISQASANQRAGR 331
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 740 AGRCRPGICFRLFSRLRFQNMLEFQTPELLRMPLQELCLHTKLLapvNCP-IADFLMkaPEPPPALIVRNAVQMLKTIDA 818
Cdd:COG1643 332 AGRLAPGICYRLWSEEDFARRPAFTDPEILRADLASLILELAAW---GLGdPEDLPF--LDPPPARAIADARALLQELGA 406
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 819 MDTWEDLTELGYHLADLPVEPHLGKMVLCAVVLKCLDPILTIACTLAYRDPFvlptqasqkraamlcrkRFTAGafSDHM 898
Cdd:COG1643 407 LDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDPR-----------------RGAAG--SDLL 467
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 1622946379 899 ALLRAFQAWQKARsdgwerafceKNFLSQATMEIIIGMRTQLLGQLRASG 948
Cdd:COG1643 468 ARLNLWRRLREQQ----------REFLSYLRLREWRDLARQLRRLLGEGA 507
|
|
| SF2_C_RHA |
cd18791 |
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ... |
597-752 |
3.06e-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: 238.20 E-value: 3.06e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 597 HSFDDEKVDLDLIMHLLYNICHSCDAGAVLIFLPGYDEIVGLRDRILfdDKRFADSTHRYQVFMLHSNMQTSDQKKVLKN 676
Cdd:cd18791 18 SSEKEDPDYVDAAVRLILQIHRTEEPGDILVFLPGQEEIERLCELLR--EELLSPDLGKLLVLPLHSSLPPEEQQRVFEP 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622946379 677 PPAGVRKIILSTNIAETSITVNDVVFVIDSGKVKEKSFDALNFVTMLKMVWISKASAIQRKGRAGRCRPGICFRLF 752
Cdd:cd18791 96 PPPGVRKVVLATNIAETSITIPGVVYVIDSGLVKEKVYDPRTGLSSLVTVWISKASAEQRAGRAGRTRPGKCYRLY 171
|
|
| DEXHc_DHX57 |
cd17985 |
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the ... |
193-368 |
1.42e-69 |
|
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: 230.88 E-value: 1.42e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 193 LPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFLLDDCFKNGIP--CRIFCTQPRRLAAIAVAERVAAERRERIGQ 270
Cdd:cd17985 1 LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFILDNSLQGPPLpvANIICTQPRRISAISVAERVAQERAERVGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 271 TIGYQIRLESRVSPKTLLTFCTNGVLLRTLmAGDSTLSTVTHVIVDEVHERDRFSDFLLTKLRDLLQKHPTLKLILSSAA 350
Cdd:cd17985 81 SVGYQIRLESVKSSATRLLYCTTGVLLRRL-EGDPTLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQRPDLKVILMSAT 159
|
170
....*....|....*...
gi 1622946379 351 LDVNLFLRYFGSCPVIYI 368
Cdd:cd17985 160 LNAELFSDYFNSCPVIHI 177
|
|
| PRK11131 |
PRK11131 |
ATP-dependent RNA helicase HrpA; Provisional |
155-1018 |
1.12e-65 |
|
ATP-dependent RNA helicase HrpA; Provisional
Pssm-ID: 182986 [Multi-domain] Cd Length: 1294 Bit Score: 244.97 E-value: 1.12e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 155 AVEAE-NREMSKTSGRLNN---GIPQIpvkrgesefdSFRQSLPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFL 230
Cdd:PRK11131 41 AIFQEiAKEIAQAAQRVLLreaARPEI----------TYPENLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKIC 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 231 LDdcFKNGIPCRIFCTQPRRLAAIAVAERVAAERRERIGQTIGYQIRLESRVSPKTLLTFCTNGVLL------RTLMAGD 304
Cdd:PRK11131 111 LE--LGRGVKGLIGHTQPRRLAARTVANRIAEELETELGGCVGYKVRFNDQVSDNTMVKLMTDGILLaeiqqdRLLMQYD 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 305 StlstvthVIVDEVHERDRFSDFLLTKLRDLLQKHPTLKLILSSAALDVNLFLRYFGSCPVIYIQGR--PFEVkemfled 382
Cdd:PRK11131 189 T-------IIIDEAHERSLNIDFILGYLKELLPRRPDLKVIITSATIDPERFSRHFNNAPIIEVSGRtyPVEV------- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 383 ilrttgytnkemlkykkekqqeekqqttltewysaqentfkpesqRQRtvPNVTDEYDLLDDGGDAVFsqltekdvncle 462
Cdd:PRK11131 255 ---------------------------------------------RYR--PIVEEADDTERDQLQAIF------------ 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 463 pwlikemDAclsdiwlhkdidafaqvfhliltenvsVDYRHSEtsatalmvaaGRGfasqvEQLISMGanvhskasngwm 542
Cdd:PRK11131 276 -------DA---------------------------VDELGRE----------GPG-----DILIFMS------------ 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 543 aldwakhfGQTEIVDLLESysaslefgnLDESSLVQTngsdlsaedrellkayhhsfddekvdldlimhllynichscda 622
Cdd:PRK11131 295 --------GEREIRDTADA---------LNKLNLRHT------------------------------------------- 314
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 623 gavliflpgydEIVGLRDRIlfddkrfadsthryqvfmlhSNmqtSDQKKVLKnpPAGVRKIILSTNIAETSITVNDVVF 702
Cdd:PRK11131 315 -----------EILPLYARL--------------------SN---SEQNRVFQ--SHSGRRIVLATNVAETSLTVPGIKY 358
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 703 VIDSGKVKEKSFDALNFVTMLKMVWISKASAIQRKGRAGRCRPGICFRLFSRLRFQNMLEFQTPELLRMPLQELCLHTKL 782
Cdd:PRK11131 359 VIDPGTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVSEGICIRLYSEDDFLSRPEFTDPEILRTNLASVILQMTA 438
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 783 LAPVNcpIADFlmkaP--EPPPALIVRNAVQMLKTIDAMDTWED-----LTELGYHLADLPVEPHLGKMVLCAVVLKCLD 855
Cdd:PRK11131 439 LGLGD--IAAF----PfvEAPDKRNIQDGVRLLEELGAITTDEQasaykLTPLGRQLAQLPVDPRLARMVLEAQKHGCVR 512
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 856 PILTIACTLAYRDPFVLPT---QASQKRaamlcRKRFtAGAFSDHMALLRAF---QAWQKARSDGWERAFCEKNFLSQAT 929
Cdd:PRK11131 513 EVMIITSALSIQDPRERPMdkqQASDEK-----HRRF-ADKESDFLAFVNLWnylQEQQKALSSNQFRRLCRTDYLNYLR 586
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 930 MEIIIGMRTQLLGQLRASGFvrargggdirDVNTNSENWAVVKAALVAGMypnLVHV---DRENLVLTGPkeKKVRFH-- 1004
Cdd:PRK11131 587 VREWQDIYTQLRQVVKELGI----------PVNSEPAEYREIHTALLTGL---LSHIgmkDAEKQEYTGA--RNARFSif 651
|
890
....*....|....
gi 1622946379 1005 PASVLsqpqYKKIP 1018
Cdd:PRK11131 652 PGSGL----FKKPP 661
|
|
| YTH |
cd21134 |
YTH (YT521-B homology) domains are RNA-binding domains that belong to the PUA superfamily; ... |
1289-1418 |
4.06e-64 |
|
YTH (YT521-B homology) domains are RNA-binding domains that belong to the PUA superfamily; Individual members of the YTH family have been shown to selectively remove transcripts of meiosis-specific genes expressed in mitotic cells. In general, eukaryotic YTH-family members may be involved in similar mechanisms to suppress gene regulation during gametogenesis or in other forms of silencing. The YTH domain is a novel RNA-binding domain that has been shown to bind to short, degenerate, single-stranded RNA motifs that loosely follow a consensus sequence. It belongs to the larger PUA superfamily.
Pssm-ID: 410979 Cd Length: 133 Bit Score: 213.58 E-value: 4.06e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 1289 RYFIMKSSNLRNLEISQQKGIWSTTPSNERKLNRAFWESSMVYLVFSVQGSGHFQGFSRMSSEIGREKS---QDWGSAGL 1365
Cdd:cd21134 1 RFFIIKSNNEENIHLSIKYGVWATQPHNEKKLNQAFRESGNVYLIFSVNGSGHFQGYARMTSPPDPNRSpswPWWSQDKL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1622946379 1366 GGVFKVEWIRKESLPFQFAHHLLNPWNDNKKVQISRDGQELEPQVGEQLLQLW 1418
Cdd:cd21134 81 GGPFKVEWLRVKDLPFSKLRHLKNPLNENKPVTISRDGQEIEPEVGEQLLKLF 133
|
|
| DEXHc_DHX9 |
cd17972 |
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ... |
185-366 |
3.33e-62 |
|
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: 212.39 E-value: 3.33e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 185 EFDSFRQSLPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFLLDDCFKN--GIPCRIFCTQPRRLAAIAVAERVAA 262
Cdd:cd17972 51 QILQERELLPVKKFREEILEAISNNPVVIIRGATGCGKTTQVPQYILDDFIQNdrAAECNIVVTQPRRISAVSVAERVAF 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 263 ERRERIGQTIGYQIRLESRV-SPKTLLTFCTNGVLLRTLMAGdstLSTVTHVIVDEVHERDRFSDFLLTKLRDLLQKHPT 341
Cdd:cd17972 131 ERGEEVGKSCGYSVRFESVLpRPHASILFCTVGVLLRKLEAG---IRGISHVIVDEIHERDINTDFLLVVLRDVVQAYPD 207
|
170 180
....*....|....*....|....*
gi 1622946379 342 LKLILSSAALDVNLFLRYFGSCPVI 366
Cdd:cd17972 208 LRVILMSATIDTSMFCEYFFNCPVI 232
|
|
| DEXHc_DHX36 |
cd17981 |
DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as ... |
193-368 |
4.27e-61 |
|
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: 207.00 E-value: 4.27e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 193 LPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFLLDDCFKNGI--PCRIFCTQPRRLAAIAVAERVAAERRE--RI 268
Cdd:cd17981 1 LPSYGMKQEIINMIDNNQVTVISGETGCGKTTQVTQFILDDAIERGKgsSCRIVCTQPRRISAISVAERVAAERAEscGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 269 GQTIGYQIRLESRVSPK-TLLTFCTNGVLLRTLMAgDSTLSTVTHVIVDEVHERDRFSDFLLTKLRDLLQKHPTLKLILS 347
Cdd:cd17981 81 GNSTGYQIRLESRKPRKqGSILYCTTGIVLQWLQS-DPHLSNVSHLVLDEIHERNLQSDVLMGIVKDLLPFRSDLKVILM 159
|
170 180
....*....|....*....|.
gi 1622946379 348 SAALDVNLFLRYFGSCPVIYI 368
Cdd:cd17981 160 SATLNAEKFSDYFNNCPMIHI 180
|
|
| YTH |
pfam04146 |
YT521-B-like domain; A protein of the YTH family has been shown to selectively remove ... |
1288-1419 |
5.34e-60 |
|
YT521-B-like domain; A protein of the YTH family has been shown to selectively remove transcripts of meiosis-specific genes expressed in mitotic cells. It has been speculated that in higher eukaryotic YTH-family members may be involved in similar mechanisms to suppress gene regulation during gametogenesis or general silencing. The rat protein YT521-B is a tyrosine-phosphorylated nuclear protein, that interacts with the nuclear transcriptosomal component scaffold attachment factor B, and the 68-kDa Src substrate associated during mitosis, Sam68. In vivo splicing assays demonstrated that YT521-B modulates alternative splice site selection in a concentration-dependent manner. The YTH domain has been identified as part of the PUA superfamily.
Pssm-ID: 461195 Cd Length: 135 Bit Score: 201.96 E-value: 5.34e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 1288 VRYFIMKSSNLRNLEISQQKGIWSTTPSNERKLNRAFWESSMVYLVFSVQGSGHFQGFSRMSSEIGREKSQ-DWGSAGL- 1365
Cdd:pfam04146 1 ARFFIIKSLNEENIHLSIKYGIWATQPHNNKRLNEAFKESKNVYLIFSVNKSGHFQGYARMTSPVDFDPSFiFWEADSDk 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1622946379 1366 -GGVFKVEWIRKESLPFQFAHHLLNPWNDNKKVQISRDGQELEPQVGEQLLQLWE 1419
Cdd:pfam04146 81 wGGPFKVEWLSVKDLPFSRLRHLRNPLNENKPVKISRDGQEIEPEVGRQLLKLFD 135
|
|
| DEXHc_DHX29 |
cd17975 |
DEXH-box helicase domain of DEAH-box helicase 29; DEAH-box helicase 29 (DHX29) is a part of ... |
193-368 |
2.74e-57 |
|
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: 196.29 E-value: 2.74e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 193 LPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFLLDDCFKNG---IPCRIFCTQPRRLAAIAVAERVAAERRERIG 269
Cdd:cd17975 1 LPVFKHRESILETLKRHRVVVVAGETGSGKSTQVPQFLLEDLLLNGgtaQKCNIVCTQPRRISAMSLATRVCEELGCESG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 270 -----QTIGYQIRLESRVSPKTLLTFCTNGVLLRTLMAgDSTLSTVTHVIVDEVHERDRFSDFLLTKLRDLLQKHPTLKL 344
Cdd:cd17975 81 pggknSLCGYQIRMESRTGEATRLLYCTTGVLLRKLQE-DGLLSSISHIIVDEVHERSVQSDFLLIILKEILHKRSDLHL 159
|
170 180
....*....|....*....|....
gi 1622946379 345 ILSSAALDVNLFLRYFGSCPVIYI 368
Cdd:cd17975 160 ILMSATVDCEKFSSYFTHCPILRI 183
|
|
| DEXHc_DHX30 |
cd17976 |
DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an ... |
193-368 |
1.02e-55 |
|
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: 191.54 E-value: 1.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 193 LPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFLLDDCF--KNGIPCRIFCTQPRRLAAIAVAERVAAERRERIGQ 270
Cdd:cd17976 1 LPVDSHKESILSAIEQNPVVVISGDTGCGKTTRIPQFILEDYVlrGRGARCNVVITQPRRISAVSVAQRVAHELGPNLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 271 TIGYQIRLESRVSPKT-LLTFCTNGVLLRTLMaGDSTLSTVTHVIVDEVHERDRFSDFLLTKLRDLLQKHPTLKLILSSA 349
Cdd:cd17976 81 NVGYQVRLESRPPPRGgALLFCTVGVLLKKLQ-SNPRLEGVSHVIVDEVHERDVNTDFLLILLKGVLQLNPELRVVLMSA 159
|
170
....*....|....*....
gi 1622946379 350 ALDVNLFLRYFGSCPVIYI 368
Cdd:cd17976 160 TGDNQRLSRYFGGCPVVRV 178
|
|
| DEXHc_DHX33 |
cd17978 |
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA ... |
193-368 |
4.09e-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: 186.79 E-value: 4.09e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 193 LPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFLLDDCF-KNGIpcrIFCTQPRRLAAIAVAERVAAERRERIGQT 271
Cdd:cd17978 1 LPIYSARKRLLEELRKHDTVIIIGETGSGKTTQIPQYLYEAGFaRGGM---IGITQPRRVAAVSVAKRVAEEMGVELGQL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 272 IGYQIRLESRVSPKTLLTFCTNGVLLRTLMaGDSTLSTVTHVIVDEVHERDRFSDFLLTKLRD-----LLQKHPTLKLIL 346
Cdd:cd17978 78 VGYSVRFDDVTSEETRIKYMTDGMLLREAI-GDPLLSKYSVIILDEAHERTVHTDVLFGLVKSaqrrrKEQKLSPLKVII 156
|
170 180
....*....|....*....|..
gi 1622946379 347 SSAALDVNLFLRYFGSCPVIYI 368
Cdd:cd17978 157 MSATLDADLFSEYFNGAPVLYI 178
|
|
| DEXHc_DHX15 |
cd17973 |
DEXH-box helicase domain of DEAH-box helicase 15; DEAH-box helicase 15 (DHX15) is a pre-mRNA ... |
190-368 |
8.02e-54 |
|
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: 186.47 E-value: 8.02e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 190 RQSLPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFLLDDCFKNGIPCRIFCTQPRRLAAIAVAERVAAERRERIG 269
Cdd:cd17973 10 RRELPVWEQKEDFLKLLKNNQILVLVGETGSGKTTQIPQFVLDDELPHQPKKLVACTQPRRVAAMSVAQRVAEEMDVKLG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 270 QTIGYQIRLESRVSPKTLLTFCTNGVLLRTLMAgDSTLSTVTHVIVDEVHERDRFSDFLLTKLRDLLQKHPTLKLILSSA 349
Cdd:cd17973 90 EEVGYSIRFEDCSSAKTILKYMTDGMLLREAMS-DPLLSRYSVIILDEAHERTLATDILMGLLKEVVRRRPDLKLIVMSA 168
|
170
....*....|....*....
gi 1622946379 350 ALDVNLFLRYFGSCPVIYI 368
Cdd:cd17973 169 TLDAGKFQKYFDNAPLLKV 187
|
|
| DEXHc_DHX34 |
cd17979 |
DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in ... |
193-366 |
3.47e-53 |
|
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: 183.80 E-value: 3.47e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 193 LPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFLLDDCFKNgipcrIFCTQPRRLAAIAVAERVAAERRERIGQTI 272
Cdd:cd17979 1 LPIAQYREKIIELLKTHQVVIVAGDTGCGKSTQVPQYLLAAGFRH-----IACTQPRRIACISLAKRVAFESLNQYGSKV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 273 GYQIRLESRVSPKTLLTFCTNGVLLRTlMAGDSTLSTVTHVIVDEVHERDRFSDFLLTKLRDLLQKHPTLKLILSSAALD 352
Cdd:cd17979 76 AYQIRFERTRTLATKLLFLTEGLLLRQ-IQRDASLPQYNVLILDEVHERHLHGDFLLGVLRCLLRLRPDLKLILMSATIN 154
|
170
....*....|....
gi 1622946379 353 VNLFLRYFGSCPVI 366
Cdd:cd17979 155 IELFSGYFEGAPVV 168
|
|
| DEXHc_DHX38 |
cd17983 |
DEXH-box helicase domain of DEAH-box helicase 38; DEAH-box helicase 38 (DHX38, also known as ... |
193-368 |
1.97e-51 |
|
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: 178.81 E-value: 1.97e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 193 LPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFLLDDCF-KNGIpcrIFCTQPRRLAAIAVAERVAAERRERIGQT 271
Cdd:cd17983 1 LPIFAVRQELLNVIRDNNVVIVVGETGSGKTTQLTQYLHEDGYtDYGM---IGCTQPRRVAAMSVAKRVSEEMGVELGEE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 272 IGYQIRLESRVSPKTLLTFCTNGVLLRTLMaGDSTLSTVTHVIVDEVHERDRFSDFLLTKLRDLLQKHPTLKLILSSAAL 351
Cdd:cd17983 78 VGYAIRFEDCTSENTVIKYMTDGILLRESL-RDPDLDKYSAIIMDEAHERSLNTDVLFGLLREVVARRRDLKLIVTSATM 156
|
170
....*....|....*..
gi 1622946379 352 DVNLFLRYFGSCPVIYI 368
Cdd:cd17983 157 DADKFADFFGNVPIFTI 173
|
|
| DEXHc_TDRD9 |
cd17988 |
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ... |
193-362 |
3.25e-51 |
|
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: 178.46 E-value: 3.25e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 193 LPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFLLDDCFKNGIPCRIFCTQPRRLAAIAVAERVAAERRERIGQTI 272
Cdd:cd17988 1 LPIYAKREEILSLIEANSVVIIKGATGCGKTTQLPQFILDHYYKRGKYCNIVVTQPRRIAAISIARRVSQEREWTLGSLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 273 GYQIRLESRVSPKTLLTFCTNGVLLRTLMAgDSTLSTVTHVIVDEVHERDRFSDFLLTKLRDLLQKHPT-LKLILSSAAL 351
Cdd:cd17988 81 GYQVGLERPASEETRLIYCTTGVLLQKLIN-NKTLTEYTHIILDEVHERDQELDFLLLVVRRLLRTNSRhVKIILMSATI 159
|
170
....*....|.
gi 1622946379 352 DVNLFLRYFGS 362
Cdd:cd17988 160 SCKEFADYFTT 170
|
|
| DEXHc_DHX8 |
cd17971 |
DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as ... |
190-368 |
7.99e-50 |
|
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: 174.59 E-value: 7.99e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 190 RQSLPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFLLDDCFKNgiPCRIFCTQPRRLAAIAVAERVAAERRERIG 269
Cdd:cd17971 3 RESLPIYKLKEQLIQAVHDNQILVVIGETGSGKTTQITQYLAEAGYTS--RGKIGCTQPRRVAAMSVAKRVAEEFGCCLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 270 QTIGYQIRLESRVSPKTLLTFCTNGVLLRTLMAgDSTLSTVTHVIVDEVHERDRFSDFLLTKLRDLLQKHPTLKLILSSA 349
Cdd:cd17971 81 QEVGYTIRFEDCTSPETVIKYMTDGMLLRECLI-DPDLSQYSVIMLDEAHERTIHTDVLFGLLKKTVQKRPDLKLIVTSA 159
|
170
....*....|....*....
gi 1622946379 350 ALDVNLFLRYFGSCPVIYI 368
Cdd:cd17971 160 TLDAVKFSQYFYEAPIFTI 178
|
|
| DEXHc_DHX16 |
cd17974 |
DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably ... |
193-368 |
1.36e-49 |
|
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: 173.84 E-value: 1.36e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 193 LPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFLLDDCFKNGIPcRIFCTQPRRLAAIAVAERVAAERRERIGQTI 272
Cdd:cd17974 1 LPVYPYRDDLLAAVKEHQVLIIVGETGSGKTTQIPQYLHEAGYTKGGG-KIGCTQPRRVAAMSVAARVAEEMGVKLGNEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 273 GYQIRLESRVSPKTLLTFCTNGVLLRTLMaGDSTLSTVTHVIVDEVHERDRFSDFLLTKLRDLLQKHPTLKLILSSAALD 352
Cdd:cd17974 80 GYSIRFEDCTSEKTVLKYMTDGMLLREFL-TEPDLASYSVMIIDEAHERTLHTDILFGLVKDIARFRPDLKLLISSATMD 158
|
170
....*....|....*.
gi 1622946379 353 VNLFLRYFGSCPVIYI 368
Cdd:cd17974 159 AEKFSAFFDDAPIFRI 174
|
|
| DEXHc_HrpA |
cd17989 |
DEXH-box helicase domain of ATP-dependent RNA helicase HrpA; HrpA is part of the HrpB-HrpA ... |
193-366 |
4.11e-48 |
|
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: 169.56 E-value: 4.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 193 LPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFLLDdcFKNGIPCRIFCTQPRRLAAIAVAERVAAERRERIGQTI 272
Cdd:cd17989 1 LPVSQKRDEIAKAIAENQVVIIAGETGSGKTTQLPKICLE--LGRGIRGLIGHTQPRRLAARSVAERIAEELKTELGGAV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 273 GYQIRLESRVSPKTLLTFCTNGVLLRTlMAGDSTLSTVTHVIVDEVHERDRFSDFLLTKLRDLLQKHPTLKLILSSAALD 352
Cdd:cd17989 79 GYKVRFTDQTSDETCVKLMTDGILLAE-TQTDRYLRAYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKVIITSATID 157
|
170
....*....|....
gi 1622946379 353 VNLFLRYFGSCPVI 366
Cdd:cd17989 158 AERFSRHFNNAPII 171
|
|
| DEXHc_DHX35 |
cd17980 |
DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and ... |
193-360 |
1.30e-45 |
|
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: 162.64 E-value: 1.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 193 LPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFLLDDCFKNGIPCrIFCTQPRRLAAIAVAERVAAERRERIGQTI 272
Cdd:cd17980 1 LPVFKLRNHILYLVENYQTIVIVGETGCGKSTQIPQYLAEAGWTAGGRV-VGCTQPRRVAAVTVAGRVAEEMGAVLGHEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 273 GYQIRLESRVSP-KTLLTFCTNGVLLRTLMAgDSTLSTVTHVIVDEVHERDRFSDFLLTKLRDLLQKHPTLKLILSSAAL 351
Cdd:cd17980 80 GYCIRFDDCTDPqATRIKFLTDGMLVREMML-DPLLTKYSVIMLDEAHERTLYTDILIGLLKKIQKKRGDLRLIVASATL 158
|
....*....
gi 1622946379 352 DVNLFLRYF 360
Cdd:cd17980 159 DAEKFRDFF 167
|
|
| DEXHc_DHX37 |
cd17982 |
DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the ... |
193-357 |
9.53e-43 |
|
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: 154.82 E-value: 9.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 193 LPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFLLDDCF---KNGIPCRIFCTQPRRLAAIAVAERVAAErRERIG 269
Cdd:cd17982 1 LPILAEEQEIMEAINENPVVIICGETGSGKTTQVPQFLYEAGFgspESDNPGMIGITQPRRVAAVSMAKRVAEE-LNVFG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 270 QTIGYQIRLESRVSPKTLLTFCTNGVLLRTlMAGDSTLSTVTHVIVDEVHERDRFSDFLL----------TKLRDLLQKH 339
Cdd:cd17982 80 KEVSYQIRYDSTVSENTKIKFMTDGVLLKE-IQTDFLLRKYSVIIIDEAHERSVNTDILIgmlsrivplrAKLYLQDQTV 158
|
170
....*....|....*...
gi 1622946379 340 PTLKLILSSAALDVNLFL 357
Cdd:cd17982 159 KPLKLVIMSATLRVEDFT 176
|
|
| PRK11664 |
PRK11664 |
ATP-dependent RNA helicase HrpB; Provisional |
192-848 |
1.11e-39 |
|
ATP-dependent RNA helicase HrpB; Provisional
Pssm-ID: 236950 [Multi-domain] Cd Length: 812 Bit Score: 159.70 E-value: 1.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 192 SLPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIP-QFLLddcfKNGIPCRIFCTQPRRLAAIAVAERVAAERRERIGQ 270
Cdd:PRK11664 3 SLPVAAVLPELLTALKTAPQVLLKAPTGAGKSTWLPlQLLQ----HGGINGKIIMLEPRRLAARNVAQRLAEQLGEKPGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 271 TIGYQIRLESRVSPKTLLTFCTNGVLLRTLMAgDSTLSTVTHVIVDEVHErdrfsdflltklRDLlqkHPTLKLILssaA 350
Cdd:PRK11664 79 TVGYRMRAESKVGPNTRLEVVTEGILTRMIQR-DPELSGVGLVILDEFHE------------RSL---QADLALAL---L 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 351 LDVNLFLRyfgscpviyiqgrpfevkemflEDilrttgytnkemLKYkkekqqeekqqttltewysaqentfkpesqrqr 430
Cdd:PRK11664 140 LDVQQGLR----------------------DD------------LKL--------------------------------- 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 431 tvpnvtdeydllddggdavfsqltekdvnclepwLIkeMDACLsdiwlhkDIDAFAQvfhlILTEnvsvdyrhsetsaTA 510
Cdd:PRK11664 153 ----------------------------------LI--MSATL-------DNDRLQQ----LLPD-------------AP 172
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 511 LMVAAGRGFAsqVE-QLISMGANVHskasngwmaldwakhfgqteivdllesysaslefgnLDESSLVQTngsdlsaedR 589
Cdd:PRK11664 173 VIVSEGRSFP--VErRYQPLPAHQR------------------------------------FDEAVARAT---------A 205
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 590 ELLKAyhhsfddekvdldlimhllynichscDAGAVLIFLPGYDEIVGLRDRIlfdDKRFADSThryQVFMLHSNMQTSD 669
Cdd:PRK11664 206 ELLRQ--------------------------ESGSLLLFLPGVGEIQRVQEQL---ASRVASDV---LLCPLYGALSLAE 253
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 670 QKKVLKNPPAGVRKIILSTNIAETSITVNDVVFVIDSGKVKEKSFDALNFVTMLKMVWISKASAIQRKGRAGRCRPGICF 749
Cdd:PRK11664 254 QQKAILPAPAGRRKVVLATNIAETSLTIEGIRLVVDSGLERVARFDPKTGLTRLVTQRISQASMTQRAGRAGRLEPGICL 333
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 750 RLFSRLRFQNMLEFQTPELLRMPLQELCLHtklLAPVNCPIADFLMKAPEPPPALIvRNAVQMLKTIDAMDTWEDLTELG 829
Cdd:PRK11664 334 HLYSKEQAERAAAQSEPEILHSDLSGLLLE---LLQWGCHDPAQLSWLDQPPAAAL-AAAKRLLQQLGALDGQGRLTARG 409
|
650
....*....|....*....
gi 1622946379 830 YHLADLPVEPHLGKMVLCA 848
Cdd:PRK11664 410 RKMAALGNDPRLAAMLVAA 428
|
|
| DEXHc_DHX40 |
cd17984 |
DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to the ... |
193-368 |
2.61e-39 |
|
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: 144.23 E-value: 2.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 193 LPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFLLDDCF-KNGipcRIFCTQPRRLAAIAVAERVAAERRERIGQT 271
Cdd:cd17984 1 LPIQKQRKKLVQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGFsQHG---MIGVTQPRRVAAISVAQRVAEEMKCTLGSK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 272 IGYQIRLESRVSPKTLLTFCTNGVLLRTLMAgDSTLSTVTHVIVDEVHERDRFSDFLLTKLRDLLQKHPT-----LKLIL 346
Cdd:cd17984 78 VGYQVRFDDCSSKETAIKYMTDGCLLRHILA-DPNLTKYSVIILDEAHERSLTTDILFGLLKKLFQEKSPnrkehLKVVV 156
|
170 180
....*....|....*....|..
gi 1622946379 347 SSAALDVNLFLRYFGSCPVIYI 368
Cdd:cd17984 157 MSATLELAKLSAFFGNCPVFDI 178
|
|
| DEXHc_HrpB |
cd17990 |
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ... |
193-366 |
2.69e-39 |
|
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: 144.01 E-value: 2.69e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 193 LPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFLLD-DCFKNGipcRIFCTQPRRLAAIAVAERVAAERRERIGQT 271
Cdd:cd17990 1 LPIAAVLPALRAALDAGGQVVLEAPPGAGKTTRVPLALLAeLWIAGG---KIIVLEPRRVAARAAARRLATLLGEAPGET 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 272 IGYQIRLESRVSPKTLLTFCTNGVLLRTLMAgDSTLSTVTHVIVDEVHERDRFSDFLLTKLRDLLQ-KHPTLKLILSSAA 350
Cdd:cd17990 78 VGYRVRGESRVGRRTRVEVVTEGVLLRRLQR-DPELSGVGAVILDEFHERSLDADLALALLLEVQQlLRDDLRLLAMSAT 156
|
170
....*....|....*.
gi 1622946379 351 LDVNLFLRYFGSCPVI 366
Cdd:cd17990 157 LDGDGLAALLPEAPVV 172
|
|
| DEXHc_DHX32 |
cd17977 |
DEXH-box helicase domain of DEAH-box helicase 32; DEAH-box helicase 32 (DHX32) belongs to the ... |
193-366 |
1.84e-29 |
|
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: 116.08 E-value: 1.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 193 LPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQ----FLLDDCFKNGIpcrIFCTQPRRLAAIAVAERVAAERRERI 268
Cdd:cd17977 1 LPVWEAKYEFMESLAHNQIVIVSGDAKTGKSSQIPQwcaeYCLSAHYQHGV---VVCTQVHKQTAVWLALRVADEMDVNI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 269 GQTIGYQIRLESRVSPKTLLTFCTNGVLLRTLMAgDSTLSTVTHVIVDEVHERDRFSDFLLTKLRDLLQKHPTLKLILSS 348
Cdd:cd17977 78 GHEVGYVIPFENCCTNETILRYCTDDMLLREMMS-DPLLESYGVIILDDAHERTVSTDVLLGLLKDVLLSRPELKLVIIT 156
|
170
....*....|....*...
gi 1622946379 349 AALDVNLFLRYFGSCPVI 366
Cdd:cd17977 157 CPHLSSKLLSYYGNVPLI 174
|
|
| R3H_DEXH_helicase |
cd06007 |
R3H domain of a group of proteins which also contain a DEXH-box helicase domain, and may ... |
46-104 |
7.98e-28 |
|
R3H domain of a group of proteins which also contain a DEXH-box helicase domain, and may function as ATP-dependent DNA or RNA helicases. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.
Pssm-ID: 100077 Cd Length: 59 Bit Score: 107.01 E-value: 7.98e-28
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622946379 46 KIAVNIALERFRYGDQREMEFPSSLTSTERAFIHRLSQSLGLVSKSKGKGANRYLTVKK 104
Cdd:cd06007 1 RIAINKALEDFRASDNEEYEFPSSLTNHERAVIHRLCRKLGLKSKSKGKGSNRRLSVYK 59
|
|
| HA2 |
pfam04408 |
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ... |
809-900 |
1.69e-27 |
|
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: 107.71 E-value: 1.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 809 AVQMLKTIDAMDTWEDLTELGYHLADLPVEPHLGKMVLCAVVLKCLDPILTIACTLAYRDPFVLPTQASQKRAAMLCRKR 888
Cdd:pfam04408 1 ALELLYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPNFLDPRSAAKAARRR 80
|
90 100
....*....|....*....|....
gi 1622946379 889 FTA------------GAFSDHMAL 900
Cdd:pfam04408 81 RRAadekarakfarlDLEGDHLTL 104
|
|
| DEXQc_DQX1 |
cd17986 |
DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 ... |
211-368 |
7.25e-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: 7.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 211 VVLIVGETGSGKTTQIPQFLLDDCFKNGIPC-RIFCTQPRRLAAIAVAERVAAERRERIGQTIGYQIRLESRVSPKTLLT 289
Cdd:cd17986 20 IVLVSGEPGSGKSTQVPQWCAEFALSRGFQKgQVTVTQPHPLAARSLALRVADEMDLNLGHEVGYSIPQEDCTGPNTILR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 290 FCTNGVLLRTlMAGDSTLSTVTHVIVDEVHERDRFSDFLLTKLRDLLQKHPTLKL-ILSSAALDVNLfLRYFGSCPVIYI 368
Cdd:cd17986 100 FCWDRLLLQE-MTSTPLLGAWGVVVLDEAQERSVASDSLLGLLKDVRLQRPELRVvVVTSPALEPKL-RAFWGNPPVVHV 177
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
199-372 |
8.84e-23 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 97.56 E-value: 8.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 199 QEEIVKIIKEN-KVVLIVGETGSGKTTQIPQFLLdDCFKNGIPCRIFCTQPRRLAAIAVAERVAAERRERIGQTIGY--- 274
Cdd:smart00487 13 QKEAIEALLSGlRDVILAAPTGSGKTLAALLPAL-EALKRGKGGRVLVLVPTRELAEQWAEELKKLGPSLGLKVVGLygg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 275 ---QIRLESRVSPKTLLTFCTNGVLLRTLMAGDSTLSTVTHVIVDEVHERDR--FSDFLLTKLRDLlqkHPTLKLILSSA 349
Cdd:smart00487 92 dskREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDggFGDQLEKLLKLL---PKNVQLLLLSA 168
|
170 180
....*....|....*....|....*
gi 1622946379 350 ALDVNL--FLRYFGSCPVIYIQGRP 372
Cdd:smart00487 169 TPPEEIenLLELFLNDPVFIDVGFT 193
|
|
| HA2 |
smart00847 |
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ... |
816-901 |
5.77e-18 |
|
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: 79.62 E-value: 5.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 816 IDAMDTWEDLTELGYHLADLPVEPHLGKMVLCAVVLKCLDPILTIACTLAYRDPFvlptQASQKRAAMLCRKRFtAGAFS 895
Cdd:smart00847 2 LGALDDDGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPR----PKEKREDADAARRRF-ADPES 76
|
....*.
gi 1622946379 896 DHMALL 901
Cdd:smart00847 77 DHLTLL 82
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
654-742 |
3.18e-14 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 69.16 E-value: 3.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 654 HRYQVFMLHSNMQTSDQKKVLKNPPAGVRKIILSTNIAETSITVNDVVFVIDSGkvkeksfdalnfvtmlkmVWISKASA 733
Cdd:smart00490 10 LGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYD------------------LPWSPASY 71
|
....*....
gi 1622946379 734 IQRKGRAGR 742
Cdd:smart00490 72 IQRIGRAGR 80
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
610-742 |
4.21e-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: 69.93 E-value: 4.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 610 MHLLYNICHSCDAGAVLIFLPGYDEIvglrdrilfdDKRFADSTHRYQVFMLHSNMQTSDQKKVLKNPPAGVRKIILSTN 689
Cdd:pfam00271 3 LEALLELLKKERGGKVLIFSQTKKTL----------EAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATD 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1622946379 690 IAETSITVNDVVFVIDsgkvkeksFDAlnfvtmlkmvWISKASAIQRKGRAGR 742
Cdd:pfam00271 73 VAERGLDLPDVDLVIN--------YDL----------PWNPASYIQRIGRAGR 107
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
209-349 |
5.60e-14 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 70.51 E-value: 5.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 209 NKVVLIVGETGSGKTTQIPQFLLDDCFKNGipCRIFCTQPRRLAAIAVAERVAaeRRERIGQTIGYqirLESRVSPKTL- 287
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLLKKG--KKVLVLVPTKALALQTAERLR--ELFGPGIRVAV---LVGGSSAEERe 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622946379 288 --------LTFCTNGVLLRTLMAGD-STLSTVTHVIVDEVHERDRFSDFLLTKLRDLLQKH-PTLKLILSSA 349
Cdd:cd00046 74 knklgdadIIIATPDMLLNLLLREDrLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGlKNAQVILLSA 145
|
|
| OB_NTP_bind |
pfam07717 |
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ... |
971-1066 |
4.13e-12 |
|
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: 63.04 E-value: 4.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 971 VKAALVAGMYPNLVHVDRENLVLTGPKEK-KVRFHPASVLSQPqyKKIPPAngqaaaikalptdWLIYDEMTRAHRIAnI 1049
Cdd:pfam07717 1 LRAALAAGLYPNVARRDPKGKGYTTLSDNqRVFIHPSSVLFNE--KTFPPE-------------WVVYQELVETTKVY-I 64
|
90
....*....|....*..
gi 1622946379 1050 RCCSAVTPVTILVFCGP 1066
Cdd:pfam07717 65 RTVTAISPEWLLLFAPH 81
|
|
| R3H_NRF |
cd02640 |
R3H domain of the NF-kappaB-repression factor (NRF). NRF is a nuclear inhibitor of NF-kappaB ... |
60-104 |
8.10e-10 |
|
R3H domain of the NF-kappaB-repression factor (NRF). NRF is a nuclear inhibitor of NF-kappaB proteins that can silence the IFNbeta promoter via binding to a negative regulatory element (NRE). Beside R3H NRF also contains a G-patch domain. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.
Pssm-ID: 100069 Cd Length: 60 Bit Score: 55.87 E-value: 8.10e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1622946379 60 DQREMEFPSSLTSTERAFIHRLSQSLGLVSKSKGKGANRYLTVKK 104
Cdd:cd02640 16 DIRDMVFSPEFSKEERALIHQIAQKYGLKSRSYGSGNDRYLVISK 60
|
|
| R3H |
pfam01424 |
R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most ... |
44-104 |
1.62e-09 |
|
R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to be binding ssDNA.
Pssm-ID: 460206 Cd Length: 60 Bit Score: 55.19 E-value: 1.62e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622946379 44 EVKIAVNIALERFRYGDQREMEFPSsLTSTERAFIHRLSQSLGLVSKSKGKGANRYLTVKK 104
Cdd:pfam01424 1 EFLEQLAEKLAEFVKDTGKSLELPP-MSSYERRIIHELAQKYGLESESEGEEPNRRVVVYK 60
|
|
| PHA02653 |
PHA02653 |
RNA helicase NPH-II; Provisional |
684-753 |
1.82e-09 |
|
RNA helicase NPH-II; Provisional
Pssm-ID: 177443 [Multi-domain] Cd Length: 675 Bit Score: 62.30 E-value: 1.82e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622946379 684 IILSTNIAETSITVNDVVFVIDSGKVKEKS-FDAlnfvtmlKMVWISKASAIQRKGRAGRCRPGICFRLFS 753
Cdd:PHA02653 449 IIISTPYLESSVTIRNATHVYDTGRVYVPEpFGG-------KEMFISKSMRTQRKGRVGRVSPGTYVYFYD 512
|
|
| R3H |
cd02325 |
R3H domain. The name of the R3H domain comes from the characteristic spacing of the most ... |
52-104 |
2.14e-09 |
|
R3H domain. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. R3H domains are found in proteins together with ATPase domains, SF1 helicase domains, SF2 DEAH helicase domains, Cys-rich repeats, ring-type zinc fingers, and KH domains. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.
Pssm-ID: 100064 Cd Length: 59 Bit Score: 54.54 E-value: 2.14e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1622946379 52 ALERFRYGD-QREMEFPSsLTSTERAFIHRLSQSLGLVSKSKGKGANRYLTVKK 104
Cdd:cd02325 7 ELEAFAKDAaGKSLELPP-MNSYERKLIHDLAEYYGLKSESEGEGPNRRVVITK 59
|
|
| R3H_Smubp-2_like |
cd02641 |
R3H domain of Smubp-2_like proteins. Smubp-2_like proteins also contain a helicase_like and ... |
59-104 |
2.58e-09 |
|
R3H domain of Smubp-2_like proteins. Smubp-2_like proteins also contain a helicase_like and an AN1-like Zinc finger domain and have been shown to bind single-stranded DNA. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA.
Pssm-ID: 100070 Cd Length: 60 Bit Score: 54.67 E-value: 2.58e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1622946379 59 GDQREMEFPSSLTSTERAFIHRLSQSLGLVSKSKGKGANRYLTVKK 104
Cdd:cd02641 15 PKATELEFPPTLSSHDRLLVHELAEELGLRHESTGEGSDRVITVSK 60
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
509-564 |
5.69e-09 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 59.20 E-value: 5.69e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622946379 509 TALMVAAGRGFASQVEQLISMGANVHSKASNGWMALDWAKHFGQTEIVDLLESYSA 564
Cdd:COG0666 155 TPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA 210
|
|
| PHA02653 |
PHA02653 |
RNA helicase NPH-II; Provisional |
156-379 |
1.99e-08 |
|
RNA helicase NPH-II; Provisional
Pssm-ID: 177443 [Multi-domain] Cd Length: 675 Bit Score: 58.84 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 156 VEAENR-------EMSKTS--GRLNNGIPQIPVKrgesefdsFRQSLPvfEKQEEIVKIIKENKVVLIVGETGSGKTTQI 226
Cdd:PHA02653 127 VEGGNAlgifsnnVGSKKDtiGILGNPEPFSKIP--------LASLQP--DVQLKIFEAWISRKPVVLTGGTGVGKTSQV 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 227 PQFL-----LDDCFKN-GIPCRIFCTQPRRLAAiavaERVAAERRERIG--QTIGYQIRLESRVSPK------------- 285
Cdd:PHA02653 197 PKLLlwfnyLFGGFDNlDKIDPNFIERPIVLSL----PRVALVRLHSITllKSLGFDEIDGSPISLKygsipdelintnp 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 286 --TLLTFCTNGVLLRTLMAGDStlstvthVIVDEVHERDRFSDFLLTKLRdllqKHPTL--KLILSSAAL--DVNLFLRY 359
Cdd:PHA02653 273 kpYGLVFSTHKLTLNKLFDYGT-------VIIDEVHEHDQIGDIIIAVAR----KHIDKirSLFLMTATLedDRDRIKEF 341
|
250 260
....*....|....*....|.
gi 1622946379 360 FGSCPVIYIQGRP-FEVKEMF 379
Cdd:PHA02653 342 FPNPAFVHIPGGTlFPISEVY 362
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
199-355 |
9.35e-08 |
|
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: 53.02 E-value: 9.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 199 QEEIVKIIKENKVVLIVGETGSGKTT--QIPqfLLDDCFKNGIPCRIFCTQPRR-LAA--IAVAERVAAERRERI----- 268
Cdd:pfam00270 4 QAEAIPAILEGRDVLVQAPTGSGKTLafLLP--ALEALDKLDNGPQALVLAPTReLAEqiYEELKKLGKGLGLKVasllg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 269 GQTIGYQIRLESRVSpktlLTFCTNGVLLrTLMAGDSTLSTVTHVIVDEVHE--RDRFSDFLLTKLRDLLQKHPTLKLil 346
Cdd:pfam00270 82 GDSRKEQLEKLKGPD----ILVGTPGRLL-DLLQERKLLKNLKLLVLDEAHRllDMGFGPDLEEILRRLPKKRQILLL-- 154
|
....*....
gi 1622946379 347 sSAALDVNL 355
Cdd:pfam00270 155 -SATLPRNL 162
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
486-647 |
2.10e-07 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 54.19 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 486 AQVFHLILTENVSVDYRhSETSATALMVAAGRGFASQVEQLISMGANVHSKASNGWMALDWAKHFGQTEIVDLLESYSAS 565
Cdd:COG0666 100 LEIVKLLLEAGADVNAR-DKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGAD 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 566 L---------------EFGNLDessLVQT---NGSDLSAEDRE----LLKAYHHSFDDEKVDLDLIMHLLYNICHSCDAG 623
Cdd:COG0666 179 VnardndgetplhlaaENGHLE---IVKLlleAGADVNAKDNDgktaLDLAAENGNLEIVKLLLEAGADLNAKDKDGLTA 255
|
170 180
....*....|....*....|....
gi 1622946379 624 AVLIFLPGYDEIVGLRDRILFDDK 647
Cdd:COG0666 256 LLLAAAAGAALIVKLLLLALLLLA 279
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
509-610 |
3.80e-07 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 53.42 E-value: 3.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 509 TALMVAAGRGFASQVEQLISMGANVHSKASNGWMALDWAKHFGQTEIVDLLESYSASLEFGNLDESSLVQTNGSDLSAED 588
Cdd:COG0666 188 TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALI 267
|
90 100
....*....|....*....|..
gi 1622946379 589 RELLKAYHHSFDDEKVDLDLIM 610
Cdd:COG0666 268 VKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
465-559 |
5.49e-07 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 53.03 E-value: 5.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 465 LIKEMDACLSDIWLHKDIDAFAQVFHLILTENVSVDYRhSETSATALMVAAGRGFASQVEQLISMGANVHSKASNGWMAL 544
Cdd:COG0666 46 ALALADALGALLLLAAALAGDLLVALLLLAAGADINAK-DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPL 124
|
90
....*....|....*
gi 1622946379 545 DWAKHFGQTEIVDLL 559
Cdd:COG0666 125 HLAAYNGNLEIVKLL 139
|
|
| R3H |
smart00393 |
Putative single-stranded nucleic acids-binding domain; |
51-105 |
2.22e-06 |
|
Putative single-stranded nucleic acids-binding domain;
Pssm-ID: 214647 Cd Length: 79 Bit Score: 46.91 E-value: 2.22e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1622946379 51 IALERFRYGDQREMEFPSsLTSTERAFIHRLSQSLGLVSKSKGKGANRYLTVKKK 105
Cdd:smart00393 26 LEIARFVKSTKESVELPP-MNSYERKIVHELAEKYGLESESFGEGPKRRVVISKK 79
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
511-579 |
2.86e-06 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 47.03 E-value: 2.86e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622946379 511 LMVAAGRGFASQVEQLISMGANVHSKASNGWMALDWAKHFGQTEIVDLLesysasLEFGNLDESSLVQT 579
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL------LEHADVNLKDNGRT 63
|
|
| R3H_RRM |
cd02639 |
R3H domain of mainly fungal proteins which are associated with a RNA recognition motif (RRM) ... |
56-104 |
1.03e-04 |
|
R3H domain of mainly fungal proteins which are associated with a RNA recognition motif (RRM) domain. Present in this group is the RNA-binding post-transcriptional regulator Cip2 (Csx1-interacting protein 2) involved in counteracting Csx1 function. Csx1 plays a central role in controlling gene expression during oxidative stress. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.
Pssm-ID: 100068 Cd Length: 60 Bit Score: 41.51 E-value: 1.03e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1622946379 56 FRYGDQR-EMEFPSSLTSTERAFIHRLSQSLGLVSKSKGKGANRYLTVKK 104
Cdd:cd02639 11 FKDDRMRdELAFPSSLSPAERRIVHLLASRLGLNHVSDGTGERRQVQITK 60
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
681-751 |
1.98e-04 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350172 [Multi-domain] Cd Length: 77 Bit Score: 41.15 E-value: 1.98e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622946379 681 VRKIILSTNIAETSITVNDVVFVIdSGKVKEKSFD--ALNFVTMLkMVWISKASAIQRKGRAGR--CRPGICFRL 751
Cdd:cd18785 4 VKIIVFTNSIEHAEEIASSLEILV-ATNVLGEGIDvpSLDTVIFF-DPPSSAASYIQRVGRAGRggKDEGEVILF 76
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
211-347 |
2.00e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 39.63 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 211 VVLIVGETGSGKTTQIPQFLlddcfkngipcRIFCTQPRRLAAIAVAERV-AAERRERIGQTIGyqIRLESRVSPKTLLT 289
Cdd:pfam13401 7 ILVLTGESGTGKTTLLRRLL-----------EQLPEVRDSVVFVDLPSGTsPKDLLRALLRALG--LPLSGRLSKEELLA 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622946379 290 FCTNGVLlrtlmagdsTLSTVTHVIVDEVHerdRFSDFLLTKLRDLLQKHPT-LKLILS 347
Cdd:pfam13401 74 ALQQLLL---------ALAVAVVLIIDEAQ---HLSLEALEELRDLLNLSSKlLQLILV 120
|
|
| R3H_unknown_2 |
cd06006 |
R3H domain of a group of fungal proteins with unknown function. The name of the R3H domain ... |
61-104 |
3.20e-03 |
|
R3H domain of a group of fungal proteins with unknown function. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.
Pssm-ID: 100076 Cd Length: 59 Bit Score: 37.35 E-value: 3.20e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1622946379 61 QREMEFPSsLTSTERAFIHRLSQSLGLVSKSKGKGANRYLTVKK 104
Cdd:cd06006 17 KRSLRFPP-MRSPQRAFIHELAKDYGLYSESQDPEPKRSVFVKK 59
|
|
| AAA_19 |
pfam13245 |
AAA domain; |
199-318 |
4.19e-03 |
|
AAA domain;
Pssm-ID: 433059 [Multi-domain] Cd Length: 136 Bit Score: 39.12 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946379 199 QEEIVKIIKENKVVLIVGETGSGKTTQIpqfllddcfkNGIpCRIFC---TQPRRLAAIAVAERVAAERRERIG---QTI 272
Cdd:pfam13245 1 QREAVRTALPSKVVLLTGGPGTGKTTTI----------RHI-VALLValgGVSFPILLAAPTGRAAKRLSERTGlpaSTI 69
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1622946379 273 GYqirlesrvspktLLTFctNGVLLRTLMAGDSTLSTVTHVIVDEV 318
Cdd:pfam13245 70 HR------------LLGF--DDLEAGGFLRDEEEPLDGDLLIVDEF 101
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
488-559 |
4.70e-03 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 37.79 E-value: 4.70e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622946379 488 VFHLILTENVSVDyRHSETSATALMVAAGRGFASQVEQLIS-MGANVhskASNGWMALDWAKHFGQTEIVDLL 559
Cdd:pfam12796 12 LVKLLLENGADAN-LQDKNGRTALHLAAKNGHLEIVKLLLEhADVNL---KDNGRTALHYAARSGHLEIVKLL 80
|
|
| R3H_G-patch |
cd02646 |
R3H domain of a group of fungal and plant proteins with unknown function, who also contain a ... |
49-104 |
5.92e-03 |
|
R3H domain of a group of fungal and plant proteins with unknown function, who also contain a G-patch domain. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the R3H domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.
Pssm-ID: 100075 Cd Length: 58 Bit Score: 36.39 E-value: 5.92e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622946379 49 VNIALERFRYGDQREMEFPSsLTSTERAFIHRLSQSLGLVSKSKGKGANRYLTVKK 104
Cdd:cd02646 4 IKDEIEAFLLDSRDSLSFPP-MDKHGRKTIHKLANCYNLKSKSRGKGKKRFVTVTK 58
|
|
| |
