|
Name |
Accession |
Description |
Interval |
E-value |
| HrpA |
COG1643 |
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis]; |
401-1028 |
0e+00 |
|
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441249 [Multi-domain] Cd Length: 836 Bit Score: 559.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 401 SLPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGYTKKGmKIACTQPRRVAAMSVAARVAREMGVKLGNEV 480
Cdd:COG1643 9 DLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGWGAGG-RIGMLEPRRLAARAAAERMAEELGEPVGETV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 481 GYSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDV-ARFRPELKVLVASATLD 559
Cdd:COG1643 88 GYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLqPALRPDLKLLVMSATLD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 560 TARFSAFFDDAPVFRIPGRRFPVDIFYT--KAPEADYLEACVVSVLQIHvTQPPGDILVFLTGQEEIEAACEMLQDRCRR 637
Cdd:COG1643 168 AERFARLLGDAPVIESSGRTYPVEVRYRplPADERDLEDAVADAVREAL-AEEPGDILVFLPGEREIRRTAEALRGRLPP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 638 lgskirELLVLPIYANLPSDMQARIFQPTPPGARKVVVATNIAETSLTIEGIIYVLDPGFCKQKSYNPRTGMESLTVTPC 717
Cdd:COG1643 247 ------DTEILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 718 SKASANQRAGRAGRVAAGKCFRLYTAwAYQHELEETTVPEIQRTSLGNVVLLLKSLGIHDLMHFDFLDPPPYETLLLALE 797
Cdd:COG1643 321 SQASANQRAGRAGRLAPGICYRLWSE-EDFARRPAFTDPEILRADLASLILELAAWGLGDPEDLPFLDPPPARAIADARA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 798 QLYALGALNHLGELTTSGRKMAELPVDPMLSKMILASEKYSCSEEILTVAAMLSVnnsifyrpKDKVVHAdnarvnfflP 877
Cdd:COG1643 400 LLQELGALDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSE--------RDPRRGA---------A 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 878 GGDHLVLLNVYTQWAESGyssqwcyENFVQFRSMRRARDVREQlegLLERVEVGLTSCQGDYVRVRKAITSGYFYHTARL 957
Cdd:COG1643 463 GSDLLARLNLWRRLREQQ-------REFLSYLRLREWRDLARQ---LRRLLGEGANEEPADYEAIGLLLALAYPDRIARR 532
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226246667 958 TRSG--YRTVKQQQtVFIHPNSSLFEQqpRWLLYHELVLTTKE-FMRQVLEIESSWLLEVAPHyyKAKELEDPH 1028
Cdd:COG1643 533 RGEGgrYLLARGRG-AALFPGSPLAKK--EWLVAAELVGGAAEaRIRLAAPIDPEWLEELAAH--LIKRYSEPH 601
|
|
| DEAH_box_HrpA |
TIGR01967 |
RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ... |
401-1031 |
2.22e-145 |
|
RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ATP-dependent helicases in many Proteobacteria and a few high-GC Gram-positive bacteria. HrpA is about 1300 amino acids long, while its paralog HrpB, also uncharacterized, is about 800 amino acids long. Related characterized eukarotic proteins are RNA helicases associated with pre-mRNA processing. The HrpA/B homolog from Borrelia is 500 amino acids shorter but appears to be derived from HrpA rather than HrpB. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 273900 [Multi-domain] Cd Length: 1283 Bit Score: 467.32 E-value: 2.22e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 401 SLPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGYTKKGMkIACTQPRRVAAMSVAARVAREMGVKLGNEV 480
Cdd:TIGR01967 65 NLPVSAKREDIAEAIAENQVVIIAGETGSGKTTQLPKICLELGRGSHGL-IGHTQPRRLAARTVAQRIAEELGTPLGEKV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 481 GYSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVLVASATLDT 560
Cdd:TIGR01967 144 GYKVRFHDQVSSNTLVKLMTDGILLAETQQDRFLSRYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKIIITSATIDP 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 561 ARFSAFFDDAPVFRIPGRRFPVDIFY------TKAPEADYLEACVVSVLQIhVTQPPGDILVFLTGQEEIEAACEMLQDR 634
Cdd:TIGR01967 224 ERFSRHFNNAPIIEVSGRTYPVEVRYrplveeQEDDDLDQLEAILDAVDEL-FAEGPGDILIFLPGEREIRDAAEILRKR 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 635 crrlgsKIRELLVLPIYANLPSDMQARIFQPTppGARKVVVATNIAETSLTIEGIIYVLDPGFCKQKSYNPRTGMESLTV 714
Cdd:TIGR01967 303 ------NLRHTEILPLYARLSNKEQQRVFQPH--SGRRIVLATNVAETSLTVPGIHYVIDTGTARISRYSYRTKVQRLPI 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 715 TPCSKASANQRAGRAGRVAAGKCFRLYTAWAYQHElEETTVPEIQRTSLGNVVLLLKSLGIHDLMHFDFLDPPPYETL-- 792
Cdd:TIGR01967 375 EPISQASANQRKGRCGRVAPGICIRLYSEEDFNSR-PEFTDPEILRTNLASVILQMLALRLGDIAAFPFIEAPDPRAIrd 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 793 -LLALEQLYALGALNHLGELTTSGRKMAELPVDPMLSKMILASEKYSCSEEILTVAAMLSVNNsIFYRPKDKVVHADNAR 871
Cdd:TIGR01967 454 gFRLLEELGALDDDEAEPQLTPIGRQLAQLPVDPRLARMLLEAHRLGCLQEVLIIASALSIQD-PRERPMEKQQAADQAH 532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 872 VNFFLPGGDHLVLLNVY-----TQWAESGYS-SQWCYENFVQFRSMRRARDVREQLEGLLERVEVGLTSCQGDYVRVRKA 945
Cdd:TIGR01967 533 ARFKDPRSDFLSRVNLWrhieeQRQALSANQfRNACRKQYLNYLRVREWQDIYRQLTQVVKELGLKLNEEPADYDAIHKA 612
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 946 ITSGYFYHTARLTRSGYRTVKQQQTVFIHPNSSLFEQQPRWLLYHELVLTTKEFMRQVLEIESSWLLEVAPHYYKaKELE 1025
Cdd:TIGR01967 613 LLSGLLSQIGMKDEKHEYDGARGRKFHIFPGSPLFKKPPKWVMAAELVETSKLYARLVAKIEPEWVEPVAGHLIK-KNYF 691
|
....*.
gi 226246667 1026 DPHAKK 1031
Cdd:TIGR01967 692 EPHWEK 697
|
|
| PRK11131 |
PRK11131 |
ATP-dependent RNA helicase HrpA; Provisional |
387-1031 |
2.68e-143 |
|
ATP-dependent RNA helicase HrpA; Provisional
Pssm-ID: 182986 [Multi-domain] Cd Length: 1294 Bit Score: 462.22 E-value: 2.68e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 387 AQAQQK-ESIQAVR------RSLPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGYTKKGMkIACTQPRRV 459
Cdd:PRK11131 51 AQAAQRvLLREAARpeitypENLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLELGRGVKGL-IGHTQPRRL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 460 AAMSVAARVAREMGVKLGNEVGYSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLI 539
Cdd:PRK11131 130 AARTVANRIAEELETELGGCVGYKVRFNDQVSDNTMVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDFILGYL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 540 KDVARFRPELKVLVASATLDTARFSAFFDDAPVFRIPGRRFPVDIFY------TKAPEADYLEACVVSVLQIHVtQPPGD 613
Cdd:PRK11131 210 KELLPRRPDLKVIITSATIDPERFSRHFNNAPIIEVSGRTYPVEVRYrpiveeADDTERDQLQAIFDAVDELGR-EGPGD 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 614 ILVFLTGQEEIEAACEMLQDRcrrlgsKIRELLVLPIYANLPSDMQARIFQPTppGARKVVVATNIAETSLTIEGIIYVL 693
Cdd:PRK11131 289 ILIFMSGEREIRDTADALNKL------NLRHTEILPLYARLSNSEQNRVFQSH--SGRRIVLATNVAETSLTVPGIKYVI 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 694 DPGFCKQKSYNPRTGMESLTVTPCSKASANQRAGRAGRVAAGKCFRLYTAWAYQHElEETTVPEIQRTSLGNVVLLLKSL 773
Cdd:PRK11131 361 DPGTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVSEGICIRLYSEDDFLSR-PEFTDPEILRTNLASVILQMTAL 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 774 GIHDLMHFDFLDPPPYETLLLALEQLYALGALN-----HLGELTTSGRKMAELPVDPMLSKMILASEKYSCSEEILTVAA 848
Cdd:PRK11131 440 GLGDIAAFPFVEAPDKRNIQDGVRLLEELGAITtdeqaSAYKLTPLGRQLAQLPVDPRLARMVLEAQKHGCVREVMIITS 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 849 MLSVNNSiFYRPKDKVVHADNARVNFFLPGGDHLVLLNV--YTQWAESGYSS----QWCYENFVQFRSMRRARDVREQLE 922
Cdd:PRK11131 520 ALSIQDP-RERPMDKQQASDEKHRRFADKESDFLAFVNLwnYLQEQQKALSSnqfrRLCRTDYLNYLRVREWQDIYTQLR 598
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 923 GLLERVEVGLTSCQGDYVRVRKAITSGYFYHTarltrsGYRTVKQQQTV-------FIHPNSSLFEQQPRWLLYHELVLT 995
Cdd:PRK11131 599 QVVKELGIPVNSEPAEYREIHTALLTGLLSHI------GMKDAEKQEYTgarnarfSIFPGSGLFKKPPKWVMVAELVET 672
|
650 660 670
....*....|....*....|....*....|....*.
gi 226246667 996 TKEFMRQVLEIESSWLLEVAPHYYKaKELEDPHAKK 1031
Cdd:PRK11131 673 SRLWGRIAARIEPEWIEPLAQHLIK-RSYSEPHWEK 707
|
|
| DEXHc_DHX16 |
cd17974 |
DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably ... |
402-575 |
3.40e-121 |
|
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: 367.98 E-value: 3.40e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 402 LPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGYTKKGMKIACTQPRRVAAMSVAARVAREMGVKLGNEVG 481
Cdd:cd17974 1 LPVYPYRDDLLAAVKEHQVLIIVGETGSGKTTQIPQYLHEAGYTKGGGKIGCTQPRRVAAMSVAARVAEEMGVKLGNEVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 482 YSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVLVASATLDTA 561
Cdd:cd17974 81 YSIRFEDCTSEKTVLKYMTDGMLLREFLTEPDLASYSVMIIDEAHERTLHTDILFGLVKDIARFRPDLKLLISSATMDAE 160
|
170
....*....|....
gi 226246667 562 RFSAFFDDAPVFRI 575
Cdd:cd17974 161 KFSAFFDDAPIFRI 174
|
|
| DEAH_box_HrpB |
TIGR01970 |
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ... |
402-850 |
6.63e-105 |
|
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: 347.14 E-value: 6.63e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 402 LPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGYTkkGMKIACTQPRRVAAMSVAARVAREMGVKLGNEVG 481
Cdd:TIGR01970 1 LPIHAVLPALRDALAAHPQVVLEAPPGAGKSTAVPLALLDAPGI--GGKIIMLEPRRLAARSAAQRLASQLGEAVGQTVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 482 YSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDV-ARFRPELKVLVASATLDT 560
Cdd:TIGR01970 79 YRVRGENKVSRRTRLEVVTEGILTRMIQDDPELDGVGALIFDEFHERSLDADLGLALALDVqSSLREDLKILAMSATLDG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 561 ARFSAFFDDAPVFRIPGRRFPVDIFYTKAPEADYLEACVVSVLQIHVTQPPGDILVFLTGQEEIEAACEMLQDrcrRLGS 640
Cdd:TIGR01970 159 ERLSSLLPDAPVVESEGRSFPVEIRYLPLRGDQRLEDAVSRAVEHALASETGSILVFLPGQAEIRRVQEQLAE---RLDS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 641 kirELLVLPIYANLPSDMQARIFQPTPPGARKVVVATNIAETSLTIEGIIYVLDPGFCKQKSYNPRTGMESLTVTPCSKA 720
Cdd:TIGR01970 236 ---DVLICPLYGELSLAAQDRAIKPDPQGRRKVVLATNIAETSLTIEGIRVVIDSGLARVARFDPKTGITRLETVRISQA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 721 SANQRAGRAGRVAAGKCFRLYtAWAYQHELEETTVPEIQRTSLGNVVLLLKSLGIHDLMHFDFLDPPPYETLLLALEQLY 800
Cdd:TIGR01970 313 SATQRAGRAGRLEPGVCYRLW-SEEQHQRLPAQDEPEILQADLSGLALELAQWGAKDPSDLRWLDAPPSVALAAARQLLQ 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 226246667 801 ALGALNHLGELTTSGRKMAELPVDPMLSKMILASEKYSCSEEILTVAAML 850
Cdd:TIGR01970 392 RLGALDAQGRLTAHGKAMAALGCHPRLAAMLLSAHSTGLAALACDLAALL 441
|
|
| PRK11664 |
PRK11664 |
ATP-dependent RNA helicase HrpB; Provisional |
401-850 |
1.55e-92 |
|
ATP-dependent RNA helicase HrpB; Provisional
Pssm-ID: 236950 [Multi-domain] Cd Length: 812 Bit Score: 313.40 E-value: 1.55e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 401 SLPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGyTKKGmKIACTQPRRVAAMSVAARVAREMGVKLGNEV 480
Cdd:PRK11664 3 SLPVAAVLPELLTALKTAPQVLLKAPTGAGKSTWLPLQLLQHG-GING-KIIMLEPRRLAARNVAQRLAEQLGEKPGETV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 481 GYSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDV-ARFRPELKVLVASATLD 559
Cdd:PRK11664 81 GYRMRAESKVGPNTRLEVVTEGILTRMIQRDPELSGVGLVILDEFHERSLQADLALALLLDVqQGLRDDLKLLIMSATLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 560 TARFSAFFDDAPVFRIPGRRFPVDIFYTKAPEADYL-EACVVSVLQIhVTQPPGDILVFLTGQEEIEAACEMLQDRcrrL 638
Cdd:PRK11664 161 NDRLQQLLPDAPVIVSEGRSFPVERRYQPLPAHQRFdEAVARATAEL-LRQESGSLLLFLPGVGEIQRVQEQLASR---V 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 639 GSkirELLVLPIYANLPSDMQARIFQPTPPGARKVVVATNIAETSLTIEGIIYVLDPGFCKQKSYNPRTGMESLTVTPCS 718
Cdd:PRK11664 237 AS---DVLLCPLYGALSLAEQQKAILPAPAGRRKVVLATNIAETSLTIEGIRLVVDSGLERVARFDPKTGLTRLVTQRIS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 719 KASANQRAGRAGRVAAGKCFRLYTAWAYQhELEETTVPEIQRTSLGNVVLLLKSLGIHDLMHFDFLDPPPYETLLLALEQ 798
Cdd:PRK11664 314 QASMTQRAGRAGRLEPGICLHLYSKEQAE-RAAAQSEPEILHSDLSGLLLELLQWGCHDPAQLSWLDQPPAAALAAAKRL 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 226246667 799 LYALGALNHLGELTTSGRKMAELPVDPMLSKMILASEKYscSEEILTVAAML 850
Cdd:PRK11664 393 LQQLGALDGQGRLTARGRKMAALGNDPRLAAMLVAAKED--DEAALATAAKL 442
|
|
| DEXHc_DHX8 |
cd17971 |
DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as ... |
399-576 |
3.00e-90 |
|
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: 285.92 E-value: 3.00e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 399 RRSLPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGYTKKGmKIACTQPRRVAAMSVAARVAREMGVKLGN 478
Cdd:cd17971 3 RESLPIYKLKEQLIQAVHDNQILVVIGETGSGKTTQITQYLAEAGYTSRG-KIGCTQPRRVAAMSVAKRVAEEFGCCLGQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 479 EVGYSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVLVASATL 558
Cdd:cd17971 82 EVGYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLSQYSVIMLDEAHERTIHTDVLFGLLKKTVQKRPDLKLIVTSATL 161
|
170
....*....|....*...
gi 226246667 559 DTARFSAFFDDAPVFRIP 576
Cdd:cd17971 162 DAVKFSQYFYEAPIFTIP 179
|
|
| DEXHc_RHA-like |
cd17917 |
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ... |
418-575 |
5.37e-88 |
|
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: 279.34 E-value: 5.37e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 418 HQVLIIEGETGSGKTTQIPQYLFEEGYTK-KGMKIACTQPRRVAAMSVAARVAREMGVKLGNEVGYSIRFEDCTSERTVL 496
Cdd:cd17917 1 NQVVVIVGETGSGKTTQVPQFLLEDGLAKgGKGRIVCTQPRRIAAISVAERVAEERGEKLGEEVGYQIRFESKTSSKTRI 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226246667 497 RYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVLVASATLDTARFSAFFDDAPVFRI 575
Cdd:cd17917 81 KFCTDGILLRELLSDPLLSGYSHVILDEAHERSLDTDFLLGLLKDLLRKRPDLKVILMSATLDAEKFSSYFGGAPVIHI 159
|
|
| DEXHc_DHX38 |
cd17983 |
DEXH-box helicase domain of DEAH-box helicase 38; DEAH-box helicase 38 (DHX38, also known as ... |
402-575 |
1.08e-84 |
|
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: 270.87 E-value: 1.08e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 402 LPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGYTKKGMkIACTQPRRVAAMSVAARVAREMGVKLGNEVG 481
Cdd:cd17983 1 LPIFAVRQELLNVIRDNNVVIVVGETGSGKTTQLTQYLHEDGYTDYGM-IGCTQPRRVAAMSVAKRVSEEMGVELGEEVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 482 YSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVLVASATLDTA 561
Cdd:cd17983 80 YAIRFEDCTSENTVIKYMTDGILLRESLRDPDLDKYSAIIMDEAHERSLNTDVLFGLLREVVARRRDLKLIVTSATMDAD 159
|
170
....*....|....
gi 226246667 562 RFSAFFDDAPVFRI 575
Cdd:cd17983 160 KFADFFGNVPIFTI 173
|
|
| DEXHc_DHX33 |
cd17978 |
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA ... |
402-575 |
4.06e-84 |
|
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: 269.61 E-value: 4.06e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 402 LPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGYTKKGMkIACTQPRRVAAMSVAARVAREMGVKLGNEVG 481
Cdd:cd17978 1 LPIYSARKRLLEELRKHDTVIIIGETGSGKTTQIPQYLYEAGFARGGM-IGITQPRRVAAVSVAKRVAEEMGVELGQLVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 482 YSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFR-----PELKVLVASA 556
Cdd:cd17978 80 YSVRFDDVTSEETRIKYMTDGMLLREAIGDPLLSKYSVIILDEAHERTVHTDVLFGLVKSAQRRRkeqklSPLKVIIMSA 159
|
170
....*....|....*....
gi 226246667 557 TLDTARFSAFFDDAPVFRI 575
Cdd:cd17978 160 TLDADLFSEYFNGAPVLYI 178
|
|
| DEXHc_DHX15 |
cd17973 |
DEXH-box helicase domain of DEAH-box helicase 15; DEAH-box helicase 15 (DHX15) is a pre-mRNA ... |
399-575 |
5.98e-84 |
|
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: 269.29 E-value: 5.98e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 399 RRSLPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGYTKKGMK-IACTQPRRVAAMSVAARVAREMGVKLG 477
Cdd:cd17973 10 RRELPVWEQKEDFLKLLKNNQILVLVGETGSGKTTQIPQFVLDDELPHQPKKlVACTQPRRVAAMSVAQRVAEEMDVKLG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 478 NEVGYSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVLVASAT 557
Cdd:cd17973 90 EEVGYSIRFEDCSSAKTILKYMTDGMLLREAMSDPLLSRYSVIILDEAHERTLATDILMGLLKEVVRRRPDLKLIVMSAT 169
|
170
....*....|....*...
gi 226246667 558 LDTARFSAFFDDAPVFRI 575
Cdd:cd17973 170 LDAGKFQKYFDNAPLLKV 187
|
|
| SF2_C_RHA |
cd18791 |
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ... |
580-741 |
3.01e-79 |
|
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: 255.92 E-value: 3.01e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 580 FPVDIFYTKAP-----------EADYLEACVVSVLQIHVTQPPGDILVFLTGQEEIEAACEMLQDRCRRLGSKirELLVL 648
Cdd:cd18791 1 FPVEVYYLEDIlellgissekeDPDYVDAAVRLILQIHRTEEPGDILVFLPGQEEIERLCELLREELLSPDLG--KLLVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 649 PIYANLPSDMQARIFQPTPPGARKVVVATNIAETSLTIEGIIYVLDPGFCKQKSYNPRTGMESLTVTPCSKASANQRAGR 728
Cdd:cd18791 79 PLHSSLPPEEQQRVFEPPPPGVRKVVLATNIAETSITIPGVVYVIDSGLVKEKVYDPRTGLSSLVTVWISKASAEQRAGR 158
|
170
....*....|...
gi 226246667 729 AGRVAAGKCFRLY 741
Cdd:cd18791 159 AGRTRPGKCYRLY 171
|
|
| DEXHc_DHX35 |
cd17980 |
DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and ... |
402-568 |
1.14e-74 |
|
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: 243.92 E-value: 1.14e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 402 LPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGYTKKGMKIACTQPRRVAAMSVAARVAREMGVKLGNEVG 481
Cdd:cd17980 1 LPVFKLRNHILYLVENYQTIVIVGETGCGKSTQIPQYLAEAGWTAGGRVVGCTQPRRVAAVTVAGRVAEEMGAVLGHEVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 482 YSIRFEDCTSE-RTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVLVASATLDT 560
Cdd:cd17980 81 YCIRFDDCTDPqATRIKFLTDGMLVREMMLDPLLTKYSVIMLDEAHERTLYTDILIGLLKKIQKKRGDLRLIVASATLDA 160
|
....*...
gi 226246667 561 ARFSAFFD 568
Cdd:cd17980 161 EKFRDFFN 168
|
|
| DEXHc_DHX40 |
cd17984 |
DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to the ... |
402-575 |
3.20e-67 |
|
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: 223.19 E-value: 3.20e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 402 LPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGYTKKGMkIACTQPRRVAAMSVAARVAREMGVKLGNEVG 481
Cdd:cd17984 1 LPIQKQRKKLVQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGFSQHGM-IGVTQPRRVAAISVAQRVAEEMKCTLGSKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 482 YSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDV-----ARFRPELKVLVASA 556
Cdd:cd17984 80 YQVRFDDCSSKETAIKYMTDGCLLRHILADPNLTKYSVIILDEAHERSLTTDILFGLLKKLfqeksPNRKEHLKVVVMSA 159
|
170
....*....|....*....
gi 226246667 557 TLDTARFSAFFDDAPVFRI 575
Cdd:cd17984 160 TLELAKLSAFFGNCPVFDI 178
|
|
| DEXHc_HrpA |
cd17989 |
DEXH-box helicase domain of ATP-dependent RNA helicase HrpA; HrpA is part of the HrpB-HrpA ... |
402-575 |
1.62e-58 |
|
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: 198.45 E-value: 1.62e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 402 LPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGYTKKGMkIACTQPRRVAAMSVAARVAREMGVKLGNEVG 481
Cdd:cd17989 1 LPVSQKRDEIAKAIAENQVVIIAGETGSGKTTQLPKICLELGRGIRGL-IGHTQPRRLAARSVAERIAEELKTELGGAVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 482 YSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVLVASATLDTA 561
Cdd:cd17989 80 YKVRFTDQTSDETCVKLMTDGILLAETQTDRYLRAYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKVIITSATIDAE 159
|
170
....*....|....
gi 226246667 562 RFSAFFDDAPVFRI 575
Cdd:cd17989 160 RFSRHFNNAPIIEV 173
|
|
| DEXHc_DHX37 |
cd17982 |
DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the ... |
402-576 |
2.53e-56 |
|
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: 192.95 E-value: 2.53e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 402 LPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGYTKK-----GMkIACTQPRRVAAMSVAARVAREMGVkL 476
Cdd:cd17982 1 LPILAEEQEIMEAINENPVVIICGETGSGKTTQVPQFLYEAGFGSPesdnpGM-IGITQPRRVAAVSMAKRVAEELNV-F 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 477 GNEVGYSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPE-------- 548
Cdd:cd17982 79 GKEVSYQIRYDSTVSENTKIKFMTDGVLLKEIQTDFLLRKYSVIIIDEAHERSVNTDILIGMLSRIVPLRAKlylqdqtv 158
|
170 180 190
....*....|....*....|....*....|
gi 226246667 549 --LKVLVASATLdtaRFSAFFDDAPVFRIP 576
Cdd:cd17982 159 kpLKLVIMSATL---RVEDFTENKLLFPRP 185
|
|
| DEXHc_DHX34 |
cd17979 |
DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in ... |
402-575 |
4.45e-55 |
|
DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in the nonsense-mediated decay (NMD), a surveillance mechanism that degrades aberrant mRNAs. DHX34 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350737 [Multi-domain] Cd Length: 170 Bit Score: 188.81 E-value: 4.45e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 402 LPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGYTKkgmkIACTQPRRVAAMSVAARVAREMGVKLGNEVG 481
Cdd:cd17979 1 LPIAQYREKIIELLKTHQVVIVAGDTGCGKSTQVPQYLLAAGFRH----IACTQPRRIACISLAKRVAFESLNQYGSKVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 482 YSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVLVASATLDTA 561
Cdd:cd17979 77 YQIRFERTRTLATKLLFLTEGLLLRQIQRDASLPQYNVLILDEVHERHLHGDFLLGVLRCLLRLRPDLKLILMSATINIE 156
|
170
....*....|....
gi 226246667 562 RFSAFFDDAPVFRI 575
Cdd:cd17979 157 LFSGYFEGAPVVQV 170
|
|
| DEXHc_DHX36 |
cd17981 |
DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as ... |
402-575 |
1.51e-52 |
|
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: 181.96 E-value: 1.51e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 402 LPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEgYTKKGM----KIACTQPRRVAAMSVAARVAREMG--VK 475
Cdd:cd17981 1 LPSYGMKQEIINMIDNNQVTVISGETGCGKTTQVTQFILDD-AIERGKgsscRIVCTQPRRISAISVAERVAAERAesCG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 476 LGNEVGYSIRFED-CTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVLVA 554
Cdd:cd17981 80 LGNSTGYQIRLESrKPRKQGSILYCTTGIVLQWLQSDPHLSNVSHLVLDEIHERNLQSDVLMGIVKDLLPFRSDLKVILM 159
|
170 180
....*....|....*....|.
gi 226246667 555 SATLDTARFSAFFDDAPVFRI 575
Cdd:cd17981 160 SATLNAEKFSDYFNNCPMIHI 180
|
|
| DEXHc_DHX32 |
cd17977 |
DEXH-box helicase domain of DEAH-box helicase 32; DEAH-box helicase 32 (DHX32) belongs to the ... |
402-575 |
2.13e-49 |
|
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: 172.70 E-value: 2.13e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 402 LPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFE---EGYTKKGMkIACTQPRRVAAMSVAARVAREMGVKLGN 478
Cdd:cd17977 1 LPVWEAKYEFMESLAHNQIVIVSGDAKTGKSSQIPQWCAEyclSAHYQHGV-VVCTQVHKQTAVWLALRVADEMDVNIGH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 479 EVGYSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVLVASATL 558
Cdd:cd17977 80 EVGYVIPFENCCTNETILRYCTDDMLLREMMSDPLLESYGVIILDDAHERTVSTDVLLGLLKDVLLSRPELKLVIITCPH 159
|
170
....*....|....*..
gi 226246667 559 DTARFSAFFDDAPVFRI 575
Cdd:cd17977 160 LSSKLLSYYGNVPLIEV 176
|
|
| DEXHc_DHX57 |
cd17985 |
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the ... |
402-575 |
3.04e-48 |
|
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: 169.64 E-value: 3.04e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 402 LPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFE---EGYTKKGMKIACTQPRRVAAMSVAARVAREMGVKLGN 478
Cdd:cd17985 1 LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFILDnslQGPPLPVANIICTQPRRISAISVAERVAQERAERVGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 479 EVGYSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVLVASATL 558
Cdd:cd17985 81 SVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDPTLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQRPDLKVILMSATL 160
|
170
....*....|....*..
gi 226246667 559 DTARFSAFFDDAPVFRI 575
Cdd:cd17985 161 NAELFSDYFNSCPVIHI 177
|
|
| DEXHc_DHX29 |
cd17975 |
DEXH-box helicase domain of DEAH-box helicase 29; DEAH-box helicase 29 (DHX29) is a part of ... |
402-575 |
3.16e-48 |
|
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: 169.71 E-value: 3.16e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 402 LPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEE----GYTKKGMKIACTQPRRVAAMSVAARVAREMGVKLG 477
Cdd:cd17975 1 LPVFKHRESILETLKRHRVVVVAGETGSGKSTQVPQFLLEDlllnGGTAQKCNIVCTQPRRISAMSLATRVCEELGCESG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 478 ----NEV-GYSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVL 552
Cdd:cd17975 81 pggkNSLcGYQIRMESRTGEATRLLYCTTGVLLRKLQEDGLLSSISHIIVDEVHERSVQSDFLLIILKEILHKRSDLHLI 160
|
170 180
....*....|....*....|...
gi 226246667 553 VASATLDTARFSAFFDDAPVFRI 575
Cdd:cd17975 161 LMSATVDCEKFSSYFTHCPILRI 183
|
|
| DEXHc_YTHDC2 |
cd17987 |
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) ... |
402-575 |
1.18e-47 |
|
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: 167.70 E-value: 1.18e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 402 LPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGYTK-KGMKIACTQPRRVAAMSVAARVAREMGVKLGNEV 480
Cdd:cd17987 1 LPVFEKQEQIVRIIKENKVVLIVGETGSGKTTQIPQFLLDDCYANgIPCRIFCTQPRRLAAIAVAERVAAERGEKIGQTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 481 GYSIRFEDCTSERTVLRYMTDGMLLREFLS-EPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVLVASATLD 559
Cdd:cd17987 81 GYQIRLESRVSPKTLLTFCTNGVLLRTLMAgDSALSTVTHVIVDEVHERDRFSDFLLTKLRDILQKHPNLKLILSSAALD 160
|
170
....*....|....*.
gi 226246667 560 TARFSAFFDDAPVFRI 575
Cdd:cd17987 161 VNLFIRYFGSCPVIYI 176
|
|
| DEXHc_HrpB |
cd17990 |
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ... |
402-574 |
1.69e-47 |
|
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: 167.12 E-value: 1.69e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 402 LPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGYTKKGmKIACTQPRRVAAMSVAARVAREMGVKLGNEVG 481
Cdd:cd17990 1 LPIAAVLPALRAALDAGGQVVLEAPPGAGKTTRVPLALLAELWIAGG-KIIVLEPRRVAARAAARRLATLLGEAPGETVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 482 YSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVAR-FRPELKVLVASATLDT 560
Cdd:cd17990 80 YRVRGESRVGRRTRVEVVTEGVLLRRLQRDPELSGVGAVILDEFHERSLDADLALALLLEVQQlLRDDLRLLAMSATLDG 159
|
170
....*....|....
gi 226246667 561 ARFSAFFDDAPVFR 574
Cdd:cd17990 160 DGLAALLPEAPVVE 173
|
|
| DEXHc_DHX30 |
cd17976 |
DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an ... |
402-575 |
2.58e-47 |
|
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: 166.89 E-value: 2.58e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 402 LPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGYTK-KGMK--IACTQPRRVAAMSVAARVAREMGVKLGN 478
Cdd:cd17976 1 LPVDSHKESILSAIEQNPVVVISGDTGCGKTTRIPQFILEDYVLRgRGARcnVVITQPRRISAVSVAQRVAHELGPNLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 479 EVGYSIRFEDCTSERT-VLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVLVASAT 557
Cdd:cd17976 81 NVGYQVRLESRPPPRGgALLFCTVGVLLKKLQSNPRLEGVSHVIVDEVHERDVNTDFLLILLKGVLQLNPELRVVLMSAT 160
|
170
....*....|....*...
gi 226246667 558 LDTARFSAFFDDAPVFRI 575
Cdd:cd17976 161 GDNQRLSRYFGGCPVVRV 178
|
|
| DEXHc_DHX9 |
cd17972 |
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ... |
388-575 |
9.75e-46 |
|
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: 164.62 E-value: 9.75e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 388 QAQQKESIQAV---RRSLPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEgYTKKGMKIAC----TQPRRVA 460
Cdd:cd17972 42 QREQDHNLQQIlqeRELLPVKKFREEILEAISNNPVVIIRGATGCGKTTQVPQYILDD-FIQNDRAAECnivvTQPRRIS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 461 AMSVAARVAREMGVKLGNEVGYSIRFEDCTSE-RTVLRYMTDGMLLREFlsEPDLASYSVVMVDEAHERTLHTDILFGLI 539
Cdd:cd17972 121 AVSVAERVAFERGEEVGKSCGYSVRFESVLPRpHASILFCTVGVLLRKL--EAGIRGISHVIVDEIHERDINTDFLLVVL 198
|
170 180 190
....*....|....*....|....*....|....*.
gi 226246667 540 KDVARFRPELKVLVASATLDTARFSAFFDDAPVFRI 575
Cdd:cd17972 199 RDVVQAYPDLRVILMSATIDTSMFCEYFFNCPVIEV 234
|
|
| DEXQc_DQX1 |
cd17986 |
DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 ... |
402-575 |
6.30e-43 |
|
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: 154.29 E-value: 6.30e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 402 LPVFPFREELLAAI-ANHQVLIIEGETGSGKTTQIPQYLFEEGYTKKGMK--IACTQPRRVAAMSVAARVAREMGVKLGN 478
Cdd:cd17986 1 LPIWAAKFTFLEQLeSPSGIVLVSGEPGSGKSTQVPQWCAEFALSRGFQKgqVTVTQPHPLAARSLALRVADEMDLNLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 479 EVGYSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVLVASATL 558
Cdd:cd17986 81 EVGYSIPQEDCTGPNTILRFCWDRLLLQEMTSTPLLGAWGVVVLDEAQERSVASDSLLGLLKDVRLQRPELRVVVVTSPA 160
|
170
....*....|....*..
gi 226246667 559 DTARFSAFFDDAPVFRI 575
Cdd:cd17986 161 LEPKLRAFWGNPPVVHV 177
|
|
| DEXHc_TDRD9 |
cd17988 |
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ... |
402-573 |
2.05e-40 |
|
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: 147.26 E-value: 2.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 402 LPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEgYTKKGM--KIACTQPRRVAAMSVAARVAREMGVKLGNE 479
Cdd:cd17988 1 LPIYAKREEILSLIEANSVVIIKGATGCGKTTQLPQFILDH-YYKRGKycNIVVTQPRRIAAISIARRVSQEREWTLGSL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 480 VGYSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRP-ELKVLVASATL 558
Cdd:cd17988 80 VGYQVGLERPASEETRLIYCTTGVLLQKLINNKTLTEYTHIILDEVHERDQELDFLLLVVRRLLRTNSrHVKIILMSATI 159
|
170
....*....|....*....
gi 226246667 559 DTARFSAFF----DDAPVF 573
Cdd:cd17988 160 SCKEFADYFttpnNPAYVF 178
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
402-584 |
1.24e-27 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 111.43 E-value: 1.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 402 LPVFPFREELLAAI-ANHQVLIIEGETGSGKTTQIPQYLFEEGYTKKGMKIACTQPRRVAAMSVAARVAREMGVKLGNEV 480
Cdd:smart00487 7 EPLRPYQKEAIEALlSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELKKLGPSLGLKVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 481 GY------SIRFEDCTSERTVLRYMTDGMLLREFLSEP-DLASYSVVMVDEAHERT--LHTDILFGLIKdvaRFRPELKV 551
Cdd:smart00487 87 GLyggdskREQLRKLESGKTDILVTTPGRLLDLLENDKlSLSNVDLVILDEAHRLLdgGFGDQLEKLLK---LLPKNVQL 163
|
170 180 190
....*....|....*....|....*....|....*
gi 226246667 552 LVASATL--DTARFSAFFDDAPVFRIPGRRFPVDI 584
Cdd:smart00487 164 LLLSATPpeEIENLLELFLNDPVFIDVGFTPLEPI 198
|
|
| HA2 |
smart00847 |
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ... |
801-885 |
1.20e-25 |
|
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: 101.19 E-value: 1.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 801 ALGALNHLGELTTSGRKMAELPVDPMLSKMILASEKYSCSEEILTVAAMLSVNNsifYRPKDKVVHADNARVNFFLPGGD 880
Cdd:smart00847 1 ELGALDDDGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGD---PRPKEKREDADAARRRFADPESD 77
|
....*
gi 226246667 881 HLVLL 885
Cdd:smart00847 78 HLTLL 82
|
|
| OB_NTP_bind |
pfam07717 |
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ... |
942-1018 |
5.73e-25 |
|
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: 99.25 E-value: 5.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 942 VRKAITSGYFYHTARLTRSG--YRTVKQQQTVFIHPNSSLF---EQQPRWLLYHELVLTTKEFMRQVLEIESSWLLEVAP 1016
Cdd:pfam07717 1 LRAALAAGLYPNVARRDPKGkgYTTLSDNQRVFIHPSSVLFnekTFPPEWVVYQELVETTKVYIRTVTAISPEWLLLFAP 80
|
..
gi 226246667 1017 HY 1018
Cdd:pfam07717 81 HI 82
|
|
| HA2 |
pfam04408 |
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ... |
795-884 |
5.83e-25 |
|
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: 100.00 E-value: 5.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 795 ALEQLYALGALNHLGELTTSGRKMAELPVDPMLSKMILASEKYSCSEEILTVAAMLSVNNsIFYRP-------------- 860
Cdd:pfam04408 1 ALELLYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRD-PFVQPnfldprsaakaarr 79
|
90 100
....*....|....*....|....*...
gi 226246667 861 ----KDKVVHADNARVNFFlpgGDHLVL 884
Cdd:pfam04408 80 rrraADEKARAKFARLDLE---GDHLTL 104
|
|
| PHA02653 |
PHA02653 |
RNA helicase NPH-II; Provisional |
410-742 |
2.30e-14 |
|
RNA helicase NPH-II; Provisional
Pssm-ID: 177443 [Multi-domain] Cd Length: 675 Bit Score: 77.71 E-value: 2.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 410 ELLAAIANHQVLIIEGETGSGKTTQIPQ------YLFeeGYTKKGMKIACTQPRRVAAMSVAaRVA--REMGVKLGNEVG 481
Cdd:PHA02653 171 KIFEAWISRKPVVLTGGTGVGKTSQVPKlllwfnYLF--GGFDNLDKIDPNFIERPIVLSLP-RVAlvRLHSITLLKSLG 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 482 Y--------SIRFEDCTSERTVLRYMTDGMLLREF-LSEPDLASYSVVMVDEAHERTLHTDILFG-LIKDVARFRpelKV 551
Cdd:PHA02653 248 FdeidgspiSLKYGSIPDELINTNPKPYGLVFSTHkLTLNKLFDYGTVIIDEVHEHDQIGDIIIAvARKHIDKIR---SL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 552 LVASATL--DTARFSAFFDDAPVFRIPG-RRFPVDIFYTKAP-----EADYLEA---CVVSVLQIHVTQPPGDILVFLtg 620
Cdd:PHA02653 325 FLMTATLedDRDRIKEFFPNPAFVHIPGgTLFPISEVYVKNKynpknKRAYIEEekkNIVTALKKYTPPKGSSGIVFV-- 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 621 qeEIEAACEMLQdrcRRLGSKIRELLVLPIYANLPS--DMQARIFQPTPPgarKVVVATNIAETSLTIEGIIYVLDPGFC 698
Cdd:PHA02653 403 --ASVSQCEEYK---KYLEKRLPIYDFYIIHGKVPNidEILEKVYSSKNP---SIIISTPYLESSVTIRNATHVYDTGRV 474
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 226246667 699 KQKSynPRTGMESLTvtpcSKASANQRAGRAGRVAAGKCFRLYT 742
Cdd:PHA02653 475 YVPE--PFGGKEMFI----SKSMRTQRKGRVGRVSPGTYVYFYD 512
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
629-731 |
3.43e-11 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 60.30 E-value: 3.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 629 EMLQDRCRRLGSKirellVLPIYANLPSDMQARIFQPTPPGARKVVVATNIAETSLTIEGIIYVLDPGFckqksynprtg 708
Cdd:smart00490 1 EELAELLKELGIK-----VARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDL----------- 64
|
90 100
....*....|....*....|...
gi 226246667 709 mesltvtPCSKASANQRAGRAGR 731
Cdd:smart00490 65 -------PWSPASYIQRIGRAGR 80
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
602-732 |
6.06e-11 |
|
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: 60.30 E-value: 6.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 602 VLQIHVTQPPGDILVFLTGQEEIEaaCEMLQDRcrrlgskiRELLVLPIYANLPSDMQARIFQPTPPGARKVVVATNIAE 681
Cdd:pfam00271 6 LLELLKKERGGKVLIFSQTKKTLE--AELLLEK--------EGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAE 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 226246667 682 TSLTIEGIIYVLDpgfckqksYNPrtgmesltvtPCSKASANQRAGRAGRV 732
Cdd:pfam00271 76 RGLDLPDVDLVIN--------YDL----------PWNPASYIQRIGRAGRA 108
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
147-410 |
3.22e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.78 E-value: 3.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 147 KRKAGGSKSPTEEKPASEDEWERTERERlQDLEERDAFAERVRQRDKDRTRnvleRSDKKAYEEAQKRlkmAEEDRKAmv 226
Cdd:PTZ00121 1390 KKKADEAKKKAEEDKKKADELKKAAAAK-KKADEAKKKAEEKKKADEAKKK----AEEAKKADEAKKK---AEEAKKA-- 1459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 227 PELRKKSRREYLAKREREKLEdlEAELADEevLFGDVELSRHERRELKYKRRVRDLAREYRAAGEQEKLEATNRYHMPKE 306
Cdd:PTZ00121 1460 EEAKKKAEEAKKADEAKKKAE--EAKKADE--AKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKK 1535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 307 T----RGQPARTVDIVEE-ESGAPGEEQRRWEEAQLGAASLKFGARDA----AAQEAKYQLVLEEDETIEFVRAAQLQGD 377
Cdd:PTZ00121 1536 AdeakKAEEKKKADELKKaEELKKAEEKKKAEEAKKAEEDKNMALRKAeeakKAEEARIEEVMKLYEEEKKMKAEEAKKA 1615
|
250 260 270
....*....|....*....|....*....|...
gi 226246667 378 EEPsgpplSAQAQQKESIQAVRRSLPVFPFREE 410
Cdd:PTZ00121 1616 EEA-----KIKAEELKKAEEEKKKVEQLKKKEA 1643
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
147-379 |
6.02e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.62 E-value: 6.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 147 KRKAGGSKSPTEEKPASEDEWERTERERlqDLEERDAFAERVRQRDKDRTRnvLERSDKKAyEEAQKRL---KMAEEDRK 223
Cdd:PTZ00121 1443 AKKADEAKKKAEEAKKAEEAKKKAEEAK--KADEAKKKAEEAKKADEAKKK--AEEAKKKA-DEAKKAAeakKKADEAKK 1517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 224 A----MVPELRK--KSRREYLAKREREKLEDLEAELADEEVLFGDVELSRHERRELKYKRRVRDLAREYRAAGEQEKLEA 297
Cdd:PTZ00121 1518 AeeakKADEAKKaeEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEV 1597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 298 TNRYHMPKETRGQPARTvdivEEESGAPGEEQRRWEEAQLGAASLKfgarDAAAQEAKYQLVLEEDETIEFVRAAQLQGD 377
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAKK----AEEAKIKAEELKKAEEEKKKVEQLK----KKEAEEKKKAEELKKAEEENKIKAAEEAKK 1669
|
..
gi 226246667 378 EE 379
Cdd:PTZ00121 1670 AE 1671
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
147-379 |
1.14e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.85 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 147 KRKAGGSKSPTEEKPASEDEWERTERERLQDLEERDA----FAERVRQRDKDRTRNVLERSD-KKAYEEAQK--RLKMAE 219
Cdd:PTZ00121 1482 AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAeeakKADEAKKAEEAKKADEAKKAEeKKKADELKKaeELKKAE 1561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 220 EDRKamVPELRKKSRREYLAKREREKLEDLEaELADEEVLFGDVELSRHERRELKYKRRVRDLAREYRAAGEQEKLEATN 299
Cdd:PTZ00121 1562 EKKK--AEEAKKAEEDKNMALRKAEEAKKAE-EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQL 1638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 300 RYHMPKETRgqPARTVDIVEEESGA-PGEEQRRWEEAQLGAASLKFGARDAAAQEAKYQLVLEEDETIEFVR-------- 370
Cdd:PTZ00121 1639 KKKEAEEKK--KAEELKKAEEENKIkAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKkkeaeekk 1716
|
250
....*....|
gi 226246667 371 -AAQLQGDEE 379
Cdd:PTZ00121 1717 kAEELKKAEE 1726
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
139-393 |
2.58e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.61 E-value: 2.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 139 EEEV--SESGKRKAGGSKSPTEEKPASEDEWERTErerlqdlEERDAFAERVRQRDKDRTRNVLERS-DKKAYEEAQKRl 215
Cdd:PTZ00121 1407 ADELkkAAAAKKKADEAKKKAEEKKKADEAKKKAE-------EAKKADEAKKKAEEAKKAEEAKKKAeEAKKADEAKKK- 1478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 216 kmAEEDRKAmvPELRKKS-----RREYLAKREREKLEDLEAELADE-----EVLFGDVELSRHERRELKYKRRVRDL--A 283
Cdd:PTZ00121 1479 --AEEAKKA--DEAKKKAeeakkKADEAKKAAEAKKKADEAKKAEEakkadEAKKAEEAKKADEAKKAEEKKKADELkkA 1554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 284 REYRAAGEQEKLEATNRyhmPKETRGQPARTVDIV---------------EEESGAPGEEQRRWEEAQLGAASLKfgard 348
Cdd:PTZ00121 1555 EELKKAEEKKKAEEAKK---AEEDKNMALRKAEEAkkaeearieevmklyEEEKKMKAEEAKKAEEAKIKAEELK----- 1626
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 226246667 349 AAAQEAKYQLVLEEDETIEFVRAAQLQGDEEPSGPPLSAQAQQKE 393
Cdd:PTZ00121 1627 KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAE 1671
|
|
| DEXHc_viral_Ns3 |
cd17931 |
DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional ... |
419-557 |
4.31e-08 |
|
DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional protein found in pestiviruses that contains an N-terminal protease and a C-terminal helicase. The N-terminal domain is a chymotrypsin-like serine protease, which is responsible for most of the maturation cleavages of the polyprotein precursor in the cytosolic side of the endoplasmic reticulum membrane. The C-terminal domain, about two-thirds of NS3, is a helicase belonging to superfamily 2 (SF2) thought to be important for unwinding highly structured regions of the RNA genome during replication. NS3 plays an essential role in viral polyprotein processing and genome replication. NS3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350689 [Multi-domain] Cd Length: 151 Bit Score: 53.32 E-value: 4.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 419 QVLIIEGETGSGKTTQIPQYLFEEGYtKKGMKIACTQPRRVAAMSVAARVaREMGVKLGNEVgysIRFEDctSERTVLRY 498
Cdd:cd17931 2 QLTVLDLHPGAGKTTRVLPQIIREAI-KKRLRTLVLAPTRVVAAEMYEAL-RGLPIRYRTGA---VKEEH--GGNEIVDY 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 226246667 499 MTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFrPELKVLVASAT 557
Cdd:cd17931 75 MCHGTFTCRLLSPKRVPNYNLIIMDEAHFTDPASIAARGYIHTRVEM-GEAAVIFMTAT 132
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
421-557 |
2.20e-07 |
|
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: 51.25 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 421 LIIEGETGSGKTTQIPQYLFEEGyTKKGMKIACTQPRRVAAMSVAARVAREMgvKLGNEVGYSIRFEDcTSERTVLR--- 497
Cdd:cd00046 4 VLITAPTGSGKTLAALLAALLLL-LKKGKKVLVLVPTKALALQTAERLRELF--GPGIRVAVLVGGSS-AEEREKNKlgd 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226246667 498 ----YMTDGMLLREFLSE--PDLASYSVVMVDEAHERT-LHTDILFGLIKDVARFRPELKVLVASAT 557
Cdd:cd00046 80 adiiIATPDMLLNLLLREdrLFLKDLKLIIVDEAHALLiDSRGALILDLAVRKAGLKNAQVILLSAT 146
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
144-300 |
4.33e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 53.97 E-value: 4.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 144 ESGKRKAGGSKSPTEEKPASEDEWERTERERLQdlEERDAFAERVRQRDKDRTRNVlERSDKKAYEEAQKRLKMAEEDR- 222
Cdd:pfam17380 409 EERQRKIQQQKVEMEQIRAEQEEARQREVRRLE--EERAREMERVRLEEQERQQQV-ERLRQQEEERKRKKLELEKEKRd 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 223 KAMVPELRKKSRREYLAKREREKLED------LEAELAD------EEVLFGDVELSRHERRELKYKRRVRDLAReyRAAG 290
Cdd:pfam17380 486 RKRAEEQRRKILEKELEERKQAMIEEerkrklLEKEMEErqkaiyEEERRREAEEERRKQQEMEERRRIQEQMR--KATE 563
|
170
....*....|
gi 226246667 291 EQEKLEATNR 300
Cdd:pfam17380 564 ERSRLEAMER 573
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
147-401 |
4.69e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.38 E-value: 4.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 147 KRKAGGSKSPTEEKPASEDEWERTER-----ERLQDLEERDAFAERVRQRDKDRTRNVLERSDKKAyeEAQKrLKMAEED 221
Cdd:PTZ00121 1301 KKKADEAKKKAEEAKKADEAKKKAEEakkkaDAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA--EAAE-KKKEEAK 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 222 RKAmvPELRKKS---RREYLAKREREKLEDLEAELADEEVLFGDVELSRHERRELKYKRRVRDLAREYRAAGEQEKLEAT 298
Cdd:PTZ00121 1378 KKA--DAAKKKAeekKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEE 1455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 299 NRYHMPKETRGQPARTVDiveeESGAPGEEQRRWEEAQLGAASLKFGARDAAAQEAKYQLVLEEDETIEFVRAAQLQGDE 378
Cdd:PTZ00121 1456 AKKAEEAKKKAEEAKKAD----EAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAE 1531
|
250 260
....*....|....*....|...
gi 226246667 379 EPSGPPLSAQAQQKESIQAVRRS 401
Cdd:PTZ00121 1532 EAKKADEAKKAEEKKKADELKKA 1554
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
406-559 |
5.78e-07 |
|
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: 50.32 E-value: 5.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 406 PFREELLAAIANHQVLIIEGETGSGKTT--QIPqyLFEE-GYTKKGMKIACTQPRRVAAMSVaARVAREMGVKLGNEVGY 482
Cdd:pfam00270 2 PIQAEAIPAILEGRDVLVQAPTGSGKTLafLLP--ALEAlDKLDNGPQALVLAPTRELAEQI-YEELKKLGKGLGLKVAS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 483 SIRFEDCTSERTVLR-----YMTDGMLLREFLSEPDLASYSVVMVDEAHErtlHTDILFG--LIKDVARFRPELKVLVAS 555
Cdd:pfam00270 79 LLGGDSRKEQLEKLKgpdilVGTPGRLLDLLQERKLLKNLKLLVLDEAHR---LLDMGFGpdLEEILRRLPKKRQILLLS 155
|
....
gi 226246667 556 ATLD 559
Cdd:pfam00270 156 ATLP 159
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
158-274 |
8.00e-07 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 53.22 E-value: 8.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 158 EEKPASEDEWERTERERLQDLEERDAFAERVRQRDKDRtrnvlERSDKKAYEEAQKRLKMAEEDRKAMVPELRKKSRREY 237
Cdd:COG1193 525 RERRELEEEREEAERLREELEKLREELEEKLEELEEEK-----EEILEKAREEAEEILREARKEAEELIRELREAQAEEE 599
|
90 100 110
....*....|....*....|....*....|....*..
gi 226246667 238 LAKREREKLEDLEAELADEEVLFGDVELSRHERRELK 274
Cdd:COG1193 600 ELKEARKKLEELKQELEEKLEKPKKKAKPAKPPEELK 636
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
147-364 |
4.74e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 4.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 147 KRKAGGSKSPTEEKPASE---DEWERTERERLQDL-----EERDAFAERVRQRDKDRTR-NVLERSDKKAYEEAQKRLKM 217
Cdd:PTZ00121 1563 KKKAEEAKKAEEDKNMALrkaEEAKKAEEARIEEVmklyeEEKKMKAEEAKKAEEAKIKaEELKKAEEEKKKVEQLKKKE 1642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 218 AEEDRKAmvPELRK-----KSRREYLAKR-EREKLEDLEAELADEEVLFGDVELSRHERRELKYKRRVRDLAREYRAAGE 291
Cdd:PTZ00121 1643 AEEKKKA--EELKKaeeenKIKAAEEAKKaEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEE 1720
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226246667 292 QEKLEatnryhmpkETRGQPARTVDIVEEESGAPGEEQRRWEEAQLGAASLKFGARDAAAQEAKYQLVLEEDE 364
Cdd:PTZ00121 1721 LKKAE---------EENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEE 1784
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
171-397 |
5.18e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 5.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 171 ERERLQDLEERDAFAERVRQRDKDRtrnvlERSDKKAYEEAQKRLKMAEEDRKAMVPELRKKSRREYLAKREREKLEDLE 250
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEE-----LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 251 AELADEEVLFGDVELSRHERRELKYKRRVRDLAREYRAAGEQEKLEATNRyhmpkETRGQPARTVDIVEEESGAPGEEQR 330
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA-----ELEEEEEEEEEALEEAAEEEAELEE 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226246667 331 RWEEAQLGAASLKfgaRDAAAQEAKYQLVLEEDETIEFVRAAQLQGDEEPSGPPLSAQAQQKESIQA 397
Cdd:COG1196 457 EEEALLELLAELL---EEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
160-373 |
3.25e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 160 KPASED-EWERTERERLQD-LEERDAFAERVRQRDKDRtrnvLERSDKKayEEAQKR---LKMAEEDRKAMVPELRKKSR 234
Cdd:PTZ00121 1073 KPSYKDfDFDAKEDNRADEaTEEAFGKAEEAKKTETGK----AEEARKA--EEAKKKaedARKAEEARKAEDARKAEEAR 1146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 235 REYLAKREREKLEDLEAELADEEVLFGDVELSRHERRELKYKRrvrdlAREYRAAGEQEKLEATNRYHMPKET----RGQ 310
Cdd:PTZ00121 1147 KAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRK-----AEELRKAEDARKAEAARKAEEERKAeearKAE 1221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 226246667 311 PARTVDIVE--EESGAPGEEQRRWEEAQLGAASLKF-GARDAAAQEAKYQLVLEEDETIEFVRAAQ 373
Cdd:PTZ00121 1222 DAKKAEAVKkaEEAKKDAEEAKKAEEERNNEEIRKFeEARMAHFARRQAAIKAEEARKADELKKAE 1287
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
157-347 |
5.92e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 46.38 E-value: 5.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 157 TEEKPASEDEWERTERERLQDLEERDAFAERVRQRDKDRTRNVLERSDKKAYEEAQKRlkmAEEDRKAMVPELRKKSRRE 236
Cdd:TIGR02794 94 LEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQ---AEEEAKAKAAAEAKKKAEE 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 237 YLAKREREKLEDLEAEL-ADEEVLFGDVElsrherrELKYKRRVRDLAREYRAAGEQEKLEAtnryhmpkETRGQPARTV 315
Cdd:TIGR02794 171 AKKKAEAEAKAKAEAEAkAKAEEAKAKAE-------AAKAKAAAEAAAKAEAEAAAAAAAEA--------ERKADEAELG 235
|
170 180 190
....*....|....*....|....*....|..
gi 226246667 316 DIVEEESGAPGEEQRRWEEAQLGAASLKFGAR 347
Cdd:TIGR02794 236 DIFGLASGSNAEKQGGARGAAAGSEVDKYAAI 267
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
143-384 |
7.37e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 7.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 143 SESGKRKAGGSKSPTEEKPASEDEWERTERERLQDLEERDAFAERVRQRDKDRTRnvlERSDKKAYEEAQKRlkmAEEDR 222
Cdd:PTZ00121 1670 AEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKA---EEENKIKAEEAKKE---AEEDK 1743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 223 KAmVPELRK----KSRREYLAKREREKLEDLEAElaDEEVLFGDVElSRHERRELKYKRRVRDLAREYRAAGEQEKlEAT 298
Cdd:PTZ00121 1744 KK-AEEAKKdeeeKKKIAHLKKEEEKKAEEIRKE--KEAVIEEELD-EEDEKRRMEVDKKIKDIFDNFANIIEGGK-EGN 1818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 299 NRYHMPKETRGQPARTVDIveeESGAPGEEQRRWEEAQLGAASL--KFGARDAAAQEAKYQLVLEEDETIEFVRAAQLQG 376
Cdd:PTZ00121 1819 LVINDSKEMEDSAIKEVAD---SKNMQLEEADAFEKHKFNKNNEngEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDK 1895
|
....*...
gi 226246667 377 DEEPSGPP 384
Cdd:PTZ00121 1896 DDIEREIP 1903
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
158-400 |
1.88e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 158 EEKPASEDEW-----ERTERERLQDLEERDAFAER----VRQRDKDRTRNVLERSDKKAYEEAQK--RLKMAEEDRKAmv 226
Cdd:PTZ00121 1215 EEARKAEDAKkaeavKKAEEAKKDAEEAKKAEEERnneeIRKFEEARMAHFARRQAAIKAEEARKadELKKAEEKKKA-- 1292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 227 PELRKKsrrEYLAKREREKLEDLEAELADEevLFGDVELSRHERRELKYK---RRVRDLAREYRAAGEQEKLEATNRYHM 303
Cdd:PTZ00121 1293 DEAKKA---EEKKKADEAKKKAEEAKKADE--AKKKAEEAKKKADAAKKKaeeAKKAAEAAKAEAEAAADEAEAAEEKAE 1367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 304 PKETRGQPARTvdiVEEESGAPGEEQRRWEEAQLGAASLKFGARDAAAQEAKYQLVLEEDETIEFVRAA---QLQGDEEP 380
Cdd:PTZ00121 1368 AAEKKKEEAKK---KADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKAdeaKKKAEEAK 1444
|
250 260
....*....|....*....|
gi 226246667 381 SGPPLSAQAQQKESIQAVRR 400
Cdd:PTZ00121 1445 KADEAKKKAEEAKKAEEAKK 1464
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
144-355 |
2.80e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 144 ESGKRKAGGSKSPTEEKpaSEDEWERTERERLQDLEERDAF--------AERVRQRDKDRTRNVLERSD-KKAYEEAQKR 214
Cdd:PTZ00121 1233 EEAKKDAEEAKKAEEER--NNEEIRKFEEARMAHFARRQAAikaeearkADELKKAEEKKKADEAKKAEeKKKADEAKKK 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 215 lkmAEEDRKAmvPELRKKSrREYLAKREREKLEDLEAELADEEvlfgdvelsrhERRELKYKRRVRDLAREYRAAGEQEK 294
Cdd:PTZ00121 1311 ---AEEAKKA--DEAKKKA-EEAKKKADAAKKKAEEAKKAAEA-----------AKAEAEAAADEAEAAEEKAEAAEKKK 1373
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 226246667 295 LEATNRYHMPKEtRGQPARTVDIVE---EESGAPGEEQRRWEEAQLGAASLKFGARDA-AAQEAK 355
Cdd:PTZ00121 1374 EEAKKKADAAKK-KAEEKKKADEAKkkaEEDKKKADELKKAAAAKKKADEAKKKAEEKkKADEAK 1437
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
157-379 |
5.93e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 5.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 157 TEEKPASEDEWERTERERLQdlEERDAFAERVRQRDKDRTRNVLERSDKKAYEEAQK--------RLKMAEEDRKAmvpe 228
Cdd:PTZ00121 1093 TEEAFGKAEEAKKTETGKAE--EARKAEEAKKKAEDARKAEEARKAEDARKAEEARKaedakrveIARKAEDARKA---- 1166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 229 lrKKSRREYLAKREREKLEDLEAELADEEVLFGDVELSRHERRELKYKRrvrdlAREYRAAGEQEKLEATNRYHMPKETr 308
Cdd:PTZ00121 1167 --EEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERK-----AEEARKAEDAKKAEAVKKAEEAKKD- 1238
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226246667 309 gqpartvdivEEESGAPGEEQRRWEEAQLGAASLKFGARDAAAQEAKYQLVLEEDETIEFVRAA-QLQGDEE 379
Cdd:PTZ00121 1239 ----------AEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAdEAKKAEE 1300
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
162-330 |
6.58e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.90 E-value: 6.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 162 ASEDEWERTERERLQDLEERDAFAERVRQRDKD------RTRNVLERSDKKAYEEAQKRLKMAEEDRKA----------- 224
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIDKLLAEIEELEREieeerkRRDKLTEEYAELKEELEDLRAELEEVDKEFaetrdelkdyr 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 225 ---------MVPELRKKSRREYLAKREREKLEDLEAELADEEVLFGDVELSRHERR-ELKYKRRVRDLAREYRAAGEQEK 294
Cdd:TIGR02169 392 ekleklkreINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAlEIKKQEWKLEQLAADLSKYEQEL 471
|
170 180 190
....*....|....*....|....*....|....*.
gi 226246667 295 LEATNRYHMPKETRGQPARTVDIVEEESGAPGEEQR 330
Cdd:TIGR02169 472 YDLKEEYDRVEKELSKLQRELAEAEAQARASEERVR 507
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
148-355 |
6.96e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 6.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 148 RKAGGSKSPTEEKPASEDE----WERTERERLQDLEERDAFAERV----RQRDKDRTRNVLERSDKKAYEEAQK--RLKM 217
Cdd:PTZ00121 1134 RKAEDARKAEEARKAEDAKrveiARKAEDARKAEEARKAEDAKKAeaarKAEEVRKAEELRKAEDARKAEAARKaeEERK 1213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 218 AEEDRKAMVPELRKKSRREYLAKREREKLEDLEAELADEEVL-FGDVELSRHERRELKYKRRVRDLAREYRAAGEQEKLE 296
Cdd:PTZ00121 1214 AEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRkFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD 1293
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226246667 297 ATNRYHMPKETrgqpartvdiveEESGAPGEEQRRWEEAQLGAASLKFGARDA--AAQEAK 355
Cdd:PTZ00121 1294 EAKKAEEKKKA------------DEAKKKAEEAKKADEAKKKAEEAKKKADAAkkKAEEAK 1342
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
144-334 |
9.68e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 9.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 144 ESGKRKAGGSKSPTEEKPASEDEWERTERERLQDLEERDAFAERVRQRDKDRTrnvlERSDKKAYEEAQKRlkMAEEDRK 223
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK----AEEDEKKAAEALKK--EAEEAKK 1703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 224 amVPELRKKSrreylaKREREKLEDLEAEladEEVLFGDVELSRHERRELKYKrrvrdlAREYRAAGEQEKLEATNRYHM 303
Cdd:PTZ00121 1704 --AEELKKKE------AEEKKKAEELKKA---EEENKIKAEEAKKEAEEDKKK------AEEAKKDEEEKKKIAHLKKEE 1766
|
170 180 190
....*....|....*....|....*....|.
gi 226246667 304 PKETRGQPARTVDIVEEESGAPGEEQRRWEE 334
Cdd:PTZ00121 1767 EKKAEEIRKEKEAVIEEELDEEDEKRRMEVD 1797
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
168-297 |
2.15e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 41.78 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 168 ERTERERLQDLEERDAFAERVRQRDKDRTRNVLERSDKK-AYEEAQKRLKMAEEDRKAMvpELRKKSRREYL---AKRER 243
Cdd:COG2268 200 DARIAEAEAERETEIAIAQANREAEEAELEQEREIETARiAEAEAELAKKKAEERREAE--TARAEAEAAYEiaeANAER 277
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 226246667 244 EKLEDLEAELADEEVlfgDVELSRHERRELKYKRRVRDLAR-EYRAAGEQEKLEA 297
Cdd:COG2268 278 EVQRQLEIAEREREI---ELQEKEAEREEAELEADVRKPAEaEKQAAEAEAEAEA 329
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
168-331 |
4.02e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 41.09 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 168 ERTERERLQDLEERDAFAERVRQRDK-----DRTRNVLERSDKKAYEEAQKRLKMAEEDRKAMVPELRKKSRREYLAKRE 242
Cdd:pfam15709 341 ERAEMRRLEVERKRREQEEQRRLQQEqleraEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQER 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 243 --------REKLEDLEAELADEEVLFGDVELSRHERRELKY---KRRVRDLAREYRAAGEQEKLEATNRYHMPKETRGQP 311
Cdd:pfam15709 421 arqqqeefRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLaeeQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERRQK 500
|
170 180
....*....|....*....|.
gi 226246667 312 AR-TVDIVEEESGAPGEEQRR 331
Cdd:pfam15709 501 EEeAARLALEEAMKQAQEQAR 521
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
156-400 |
4.08e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 40.60 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 156 PTEEKPAsedewERTERERLQDLEERDAFAERVRQRDKDRTRNVLERsdKKAYEEAQKrlkmAEEDRKAMvpELRKKSRR 235
Cdd:TIGR02794 56 QQQKKPA-----AKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQR--AAAEKAAKQ----AEQAAKQA--EEKQKQAE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 236 EYLAKREREKLEDLEAEladeevlfgdvelsrherRELKYKRRVRDLAREYRAAGEQEKLEAtnryhmpketRGQPARTV 315
Cdd:TIGR02794 123 EAKAKQAAEAKAKAEAE------------------AERKAKEEAAKQAEEEAKAKAAAEAKK----------KAEEAKKK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 316 DIVEEESGAPGEEQRRWEEAQLGAASLKFGAR-DA---AAQEAKYQLVLEEDETIEFVRAAQLQGDEEPSGPPLSAQAQQ 391
Cdd:TIGR02794 175 AEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAaEAaakAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARG 254
|
....*....
gi 226246667 392 KESIQAVRR 400
Cdd:TIGR02794 255 AAAGSEVDK 263
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
164-252 |
4.70e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 40.71 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 164 EDEWERTERERLQDLEERDAFAERVRQRDKDRTRNVLERSDKKAYEEA---------QKRLKM--AEEDRKAMvpELRKK 232
Cdd:pfam15709 397 EEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAeraeaekqrQKELEMqlAEEQKRLM--EMAEE 474
|
90 100
....*....|....*....|.
gi 226246667 233 SRREYL-AKREREKLEDLEAE 252
Cdd:pfam15709 475 ERLEYQrQKQEAEEKARLEAE 495
|
|
| U2AF_lg |
TIGR01642 |
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ... |
165-300 |
5.01e-03 |
|
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of an N-terminal arginine-rich low complexity domain followed by three tandem RNA recognition motifs (pfam00076). The well-characterized members of this family are auxilliary components of the U2 small nuclear ribonuclearprotein splicing factor (U2AF). These proteins are closely related to the CC1-like subfamily of splicing factors (TIGR01622). Members of this subfamily are found in plants, metazoa and fungi.
Pssm-ID: 273727 [Multi-domain] Cd Length: 509 Bit Score: 40.65 E-value: 5.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 165 DEWERTERERLQD-----LEERDAFAERVRQRDKDRTRNVLERSdkkAYEEAQKRLKMAEEDRKamvpelrKKSRREYLA 239
Cdd:TIGR01642 2 DEEPDREREKSRGrdrdrSSERPRRRSRDRSRFRDRHRRSRERS---YREDSRPRDRRRYDSRS-------PRSLRYSSV 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226246667 240 KREREKledleaeladeevlfgDVELSRHERRELKYKRRVRDlareyRAAGEQEKLEATNR 300
Cdd:TIGR01642 72 RRSRDR----------------PRRRSRSVRSIEQHRRRLRD-----RSPSNQWRKDDKKR 111
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
168-253 |
6.30e-03 |
|
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.
Pssm-ID: 405931 [Multi-domain] Cd Length: 151 Bit Score: 38.49 E-value: 6.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 168 ERTERERLQDLEERDAFAERVRQRDKDRTRNVLERSDKkaYEEAQKRLkmaEEDRKAMVPELRKKSRREYLAKREREKLE 247
Cdd:pfam15346 56 EELEREREAELEEERRKEEEERKKREELERILEENNRK--IEEAQRKE---AEERLAMLEEQRRMKEERQRREKEEEERE 130
|
....*.
gi 226246667 248 DLEAEL 253
Cdd:pfam15346 131 KREQQK 136
|
|
| SF-CC1 |
TIGR01622 |
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ... |
171-247 |
8.77e-03 |
|
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors including the Pad-1 protein (N. crassa), CAPER (M. musculus) and CC1.3 (H.sapiens). These proteins are characterized by an N-terminal arginine-rich, low complexity domain followed by three (or in the case of 4 H. sapiens paralogs, two) RNA recognition domains (rrm: pfam00706). These splicing factors are closely related to the U2AF splicing factor family (TIGR01642). A homologous gene from Plasmodium falciparum was identified in the course of the analysis of that genome at TIGR and was included in the seed.
Pssm-ID: 273721 [Multi-domain] Cd Length: 494 Bit Score: 39.90 E-value: 8.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246667 171 ERERLQDLE-------ERDAFAERVRQRDKDRTRNVLERSDKKAYEEAQK-RLKMAEEDRKAMVPELRKKSRREYLAKRE 242
Cdd:TIGR01622 6 ERERLRDSSsagdrdrRRDKGRERSRDRSRDRERSRSRRRDRHRDRDYYRgRERRSRSRRPNRRYRPREKRRRRGDSYRR 85
|
....*
gi 226246667 243 REKLE 247
Cdd:TIGR01622 86 RRDDR 90
|
|
| |
