|
Name |
Accession |
Description |
Interval |
E-value |
| HrpA |
COG1643 |
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis]; |
338-965 |
0e+00 |
|
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441249 [Multi-domain] Cd Length: 836 Bit Score: 559.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 338 SLPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGYTNKGmKIACTQPRRVAAMSVAARVAREMGVKLGNEV 417
Cdd:COG1643 9 DLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGWGAGG-RIGMLEPRRLAARAAAERMAEELGEPVGETV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 418 GYSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDV-ARFRPELKVLVASATMD 496
Cdd:COG1643 88 GYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLqPALRPDLKLLVMSATLD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 497 TARFSTFFDDAPVFRIPGRRFPVDIFYT--KAPEADYLEACVVSVLQIHvTQPPGDILVFLTGQEEIEAACEMLQDRCRR 574
Cdd:COG1643 168 AERFARLLGDAPVIESSGRTYPVEVRYRplPADERDLEDAVADAVREAL-AEEPGDILVFLPGEREIRRTAEALRGRLPP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 575 lgskirELLVLPIYANLPSDMQARIFQPTPPGARKVVVATNIAETSLTIEGIIYVLDPGFCKQKSYNPRTGMESLTVTPC 654
Cdd:COG1643 247 ------DTEILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 655 SKASANQRAGRAGRVAAGKCFRLYTAwAYQHELEETTVPEIQRTSLGNVVLLLKSLGIHDLMHFDFLDPPPYETLLLALE 734
Cdd:COG1643 321 SQASANQRAGRAGRLAPGICYRLWSE-EDFARRPAFTDPEILRADLASLILELAAWGLGDPEDLPFLDPPPARAIADARA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 735 QLYALGALNHLGELTTSGRKMAELPVDPMLSKMILASEKYSCSEEILTVAAMLSVnnsifyrpKDKVVHAdnarvnfflP 814
Cdd:COG1643 400 LLQELGALDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSE--------RDPRRGA---------A 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 815 GGDHLVLLNVYTQWAESGyssqwcyENFVQFRSMRRARDVREQlegLLERVEVGLSSCQGDYIRVRKAITAGYFYHTARL 894
Cdd:COG1643 463 GSDLLARLNLWRRLREQQ-------REFLSYLRLREWRDLARQ---LRRLLGEGANEEPADYEAIGLLLALAYPDRIARR 532
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 256000749 895 TRSG--YRTVKQQQtVFIHPNSSLFEQqpRWLLYHELVLTTKE-FMRQVLEIESSWLLEVAPHyyKAKELEDPH 965
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 ... |
338-968 |
3.49e-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: 465.01 E-value: 3.49e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 338 SLPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGYTNKGMkIACTQPRRVAAMSVAARVAREMGVKLGNEV 417
Cdd:TIGR01967 65 NLPVSAKREDIAEAIAENQVVIIAGETGSGKTTQLPKICLELGRGSHGL-IGHTQPRRLAARTVAQRIAEELGTPLGEKV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 418 GYSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVLVASATMDT 497
Cdd:TIGR01967 144 GYKVRFHDQVSSNTLVKLMTDGILLAETQQDRFLSRYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKIIITSATIDP 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 498 ARFSTFFDDAPVFRIPGRRFPVDIFY------TKAPEADYLEACVVSVLQIhVTQPPGDILVFLTGQEEIEAACEMLQDR 571
Cdd:TIGR01967 224 ERFSRHFNNAPIIEVSGRTYPVEVRYrplveeQEDDDLDQLEAILDAVDEL-FAEGPGDILIFLPGEREIRDAAEILRKR 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 572 crrlgsKIRELLVLPIYANLPSDMQARIFQPTppGARKVVVATNIAETSLTIEGIIYVLDPGFCKQKSYNPRTGMESLTV 651
Cdd:TIGR01967 303 ------NLRHTEILPLYARLSNKEQQRVFQPH--SGRRIVLATNVAETSLTVPGIHYVIDTGTARISRYSYRTKVQRLPI 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 652 TPCSKASANQRAGRAGRVAAGKCFRLYTAWAYQHElEETTVPEIQRTSLGNVVLLLKSLGIHDLMHFDFLDPPPYETL-- 729
Cdd:TIGR01967 375 EPISQASANQRKGRCGRVAPGICIRLYSEEDFNSR-PEFTDPEILRTNLASVILQMLALRLGDIAAFPFIEAPDPRAIrd 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 730 -LLALEQLYALGALNHLGELTTSGRKMAELPVDPMLSKMILASEKYSCSEEILTVAAMLSVNNsIFYRPKDKVVHADNAR 808
Cdd:TIGR01967 454 gFRLLEELGALDDDEAEPQLTPIGRQLAQLPVDPRLARMLLEAHRLGCLQEVLIIASALSIQD-PRERPMEKQQAADQAH 532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 809 VNFFLPGGDHLVLLNVY-----TQWAESGYS-SQWCYENFVQFRSMRRARDVREQLEGLLERVEVGLSSCQGDYIRVRKA 882
Cdd:TIGR01967 533 ARFKDPRSDFLSRVNLWrhieeQRQALSANQfRNACRKQYLNYLRVREWQDIYRQLTQVVKELGLKLNEEPADYDAIHKA 612
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 883 ITAGYFYHTARLTRSGYRTVKQQQTVFIHPNSSLFEQQPRWLLYHELVLTTKEFMRQVLEIESSWLLEVAPHYYKaKELE 962
Cdd:TIGR01967 613 LLSGLLSQIGMKDEKHEYDGARGRKFHIFPGSPLFKKPPKWVMAAELVETSKLYARLVAKIEPEWVEPVAGHLIK-KNYF 691
|
....*.
gi 256000749 963 DPHAKK 968
Cdd:TIGR01967 692 EPHWEK 697
|
|
| PRK11131 |
PRK11131 |
ATP-dependent RNA helicase HrpA; Provisional |
338-968 |
5.86e-143 |
|
ATP-dependent RNA helicase HrpA; Provisional
Pssm-ID: 182986 [Multi-domain] Cd Length: 1294 Bit Score: 459.53 E-value: 5.86e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 338 SLPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGYTNKGMkIACTQPRRVAAMSVAARVAREMGVKLGNEV 417
Cdd:PRK11131 72 NLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLELGRGVKGL-IGHTQPRRLAARTVANRIAEELETELGGCV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 418 GYSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVLVASATMDT 497
Cdd:PRK11131 151 GYKVRFNDQVSDNTMVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPDLKVIITSATIDP 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 498 ARFSTFFDDAPVFRIPGRRFPVDIFY------TKAPEADYLEACVVSVLQIHVtQPPGDILVFLTGQEEIEAACEMLQDR 571
Cdd:PRK11131 231 ERFSRHFNNAPIIEVSGRTYPVEVRYrpiveeADDTERDQLQAIFDAVDELGR-EGPGDILIFMSGEREIRDTADALNKL 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 572 crrlgsKIRELLVLPIYANLPSDMQARIFQPTppGARKVVVATNIAETSLTIEGIIYVLDPGFCKQKSYNPRTGMESLTV 651
Cdd:PRK11131 310 ------NLRHTEILPLYARLSNSEQNRVFQSH--SGRRIVLATNVAETSLTVPGIKYVIDPGTARISRYSYRTKVQRLPI 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 652 TPCSKASANQRAGRAGRVAAGKCFRLYTAWAYQHElEETTVPEIQRTSLGNVVLLLKSLGIHDLMHFDFLDPPPYETLLL 731
Cdd:PRK11131 382 EPISQASANQRKGRCGRVSEGICIRLYSEDDFLSR-PEFTDPEILRTNLASVILQMTALGLGDIAAFPFVEAPDKRNIQD 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 732 ALEQLYALGALN-----HLGELTTSGRKMAELPVDPMLSKMILASEKYSCSEEILTVAAMLSVNNSiFYRPKDKVVHADN 806
Cdd:PRK11131 461 GVRLLEELGAITtdeqaSAYKLTPLGRQLAQLPVDPRLARMVLEAQKHGCVREVMIITSALSIQDP-RERPMDKQQASDE 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 807 ARVNFFLPGGDHLVLLNV--YTQWAESGYSS----QWCYENFVQFRSMRRARDVREQLEGLLERVEVGLSSCQGDYIRVR 880
Cdd:PRK11131 540 KHRRFADKESDFLAFVNLwnYLQEQQKALSSnqfrRLCRTDYLNYLRVREWQDIYTQLRQVVKELGIPVNSEPAEYREIH 619
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 881 KAITAGYFYHTarltrsGYRTVKQQQTV-------FIHPNSSLFEQQPRWLLYHELVLTTKEFMRQVLEIESSWLLEVAP 953
Cdd:PRK11131 620 TALLTGLLSHI------GMKDAEKQEYTgarnarfSIFPGSGLFKKPPKWVMVAELVETSRLWGRIAARIEPEWIEPLAQ 693
|
650
....*....|....*
gi 256000749 954 HYYKaKELEDPHAKK 968
Cdd:PRK11131 694 HLIK-RSYSEPHWEK 707
|
|
| DEXHc_DHX16 |
cd17974 |
DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably ... |
339-512 |
2.83e-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: 366.83 E-value: 2.83e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 339 LPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGYTNKGMKIACTQPRRVAAMSVAARVAREMGVKLGNEVG 418
Cdd:cd17974 1 LPVYPYRDDLLAAVKEHQVLIIVGETGSGKTTQIPQYLHEAGYTKGGGKIGCTQPRRVAAMSVAARVAEEMGVKLGNEVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 419 YSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVLVASATMDTA 498
Cdd:cd17974 81 YSIRFEDCTSEKTVLKYMTDGMLLREFLTEPDLASYSVMIIDEAHERTLHTDILFGLVKDIARFRPDLKLLISSATMDAE 160
|
170
....*....|....
gi 256000749 499 RFSTFFDDAPVFRI 512
Cdd:cd17974 161 KFSAFFDDAPIFRI 174
|
|
| DEAH_box_HrpB |
TIGR01970 |
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ... |
339-787 |
1.51e-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: 347.52 E-value: 1.51e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 339 LPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGYTNKgmKIACTQPRRVAAMSVAARVAREMGVKLGNEVG 418
Cdd:TIGR01970 1 LPIHAVLPALRDALAAHPQVVLEAPPGAGKSTAVPLALLDAPGIGG--KIIMLEPRRLAARSAAQRLASQLGEAVGQTVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 419 YSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDV-ARFRPELKVLVASATMDT 497
Cdd:TIGR01970 79 YRVRGENKVSRRTRLEVVTEGILTRMIQDDPELDGVGALIFDEFHERSLDADLGLALALDVqSSLREDLKILAMSATLDG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 498 ARFSTFFDDAPVFRIPGRRFPVDIFYTKAPEADYLEACVVSVLQIHVTQPPGDILVFLTGQEEIEAACEMLQDrcrRLGS 577
Cdd:TIGR01970 159 ERLSSLLPDAPVVESEGRSFPVEIRYLPLRGDQRLEDAVSRAVEHALASETGSILVFLPGQAEIRRVQEQLAE---RLDS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 578 kirELLVLPIYANLPSDMQARIFQPTPPGARKVVVATNIAETSLTIEGIIYVLDPGFCKQKSYNPRTGMESLTVTPCSKA 657
Cdd:TIGR01970 236 ---DVLICPLYGELSLAAQDRAIKPDPQGRRKVVLATNIAETSLTIEGIRVVIDSGLARVARFDPKTGITRLETVRISQA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 658 SANQRAGRAGRVAAGKCFRLYTawAYQHE-LEETTVPEIQRTSLGNVVLLLKSLGIHDLMHFDFLDPPPYETLLLALEQL 736
Cdd:TIGR01970 313 SATQRAGRAGRLEPGVCYRLWS--EEQHQrLPAQDEPEILQADLSGLALELAQWGAKDPSDLRWLDAPPSVALAAARQLL 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 256000749 737 YALGALNHLGELTTSGRKMAELPVDPMLSKMILASEKYSCSEEILTVAAML 787
Cdd:TIGR01970 391 QRLGALDAQGRLTAHGKAMAALGCHPRLAAMLLSAHSTGLAALACDLAALL 441
|
|
| PRK11664 |
PRK11664 |
ATP-dependent RNA helicase HrpB; Provisional |
338-787 |
1.71e-92 |
|
ATP-dependent RNA helicase HrpB; Provisional
Pssm-ID: 236950 [Multi-domain] Cd Length: 812 Bit Score: 311.86 E-value: 1.71e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 338 SLPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGYTNKgmKIACTQPRRVAAMSVAARVAREMGVKLGNEV 417
Cdd:PRK11664 3 SLPVAAVLPELLTALKTAPQVLLKAPTGAGKSTWLPLQLLQHGGING--KIIMLEPRRLAARNVAQRLAEQLGEKPGETV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 418 GYSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDV-ARFRPELKVLVASATMD 496
Cdd:PRK11664 81 GYRMRAESKVGPNTRLEVVTEGILTRMIQRDPELSGVGLVILDEFHERSLQADLALALLLDVqQGLRDDLKLLIMSATLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 497 TARFSTFFDDAPVFRIPGRRFPVDIFYTKAPEADYL-EACVVSVLQIhVTQPPGDILVFLTGQEEIEAACEMLQDRcrrL 575
Cdd:PRK11664 161 NDRLQQLLPDAPVIVSEGRSFPVERRYQPLPAHQRFdEAVARATAEL-LRQESGSLLLFLPGVGEIQRVQEQLASR---V 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 576 GSkirELLVLPIYANLPSDMQARIFQPTPPGARKVVVATNIAETSLTIEGIIYVLDPGFCKQKSYNPRTGMESLTVTPCS 655
Cdd:PRK11664 237 AS---DVLLCPLYGALSLAEQQKAILPAPAGRRKVVLATNIAETSLTIEGIRLVVDSGLERVARFDPKTGLTRLVTQRIS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 656 KASANQRAGRAGRVAAGKCFRLYTAWAYQhELEETTVPEIQRTSLGNVVLLLKSLGIHDLMHFDFLDPPPYETLLLALEQ 735
Cdd:PRK11664 314 QASMTQRAGRAGRLEPGICLHLYSKEQAE-RAAAQSEPEILHSDLSGLLLELLQWGCHDPAQLSWLDQPPAAALAAAKRL 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 256000749 736 LYALGALNHLGELTTSGRKMAELPVDPMLSKMILASEKYscSEEILTVAAML 787
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 ... |
336-513 |
4.01e-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: 284.76 E-value: 4.01e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 336 RRSLPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGYTNKGmKIACTQPRRVAAMSVAARVAREMGVKLGN 415
Cdd:cd17971 3 RESLPIYKLKEQLIQAVHDNQILVVIGETGSGKTTQITQYLAEAGYTSRG-KIGCTQPRRVAAMSVAKRVAEEFGCCLGQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 416 EVGYSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVLVASATM 495
Cdd:cd17971 82 EVGYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLSQYSVIMLDEAHERTIHTDVLFGLLKKTVQKRPDLKLIVTSATL 161
|
170
....*....|....*...
gi 256000749 496 DTARFSTFFDDAPVFRIP 513
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) ... |
355-512 |
4.05e-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: 278.57 E-value: 4.05e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 355 HQVLIIEGETGSGKTTQIPQYLFEEGYTN-KGMKIACTQPRRVAAMSVAARVAREMGVKLGNEVGYSIRFEDCTSERTVL 433
Cdd:cd17917 1 NQVVVIVGETGSGKTTQVPQFLLEDGLAKgGKGRIVCTQPRRIAAISVAERVAEERGEKLGEEVGYQIRFESKTSSKTRI 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 256000749 434 RYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVLVASATMDTARFSTFFDDAPVFRI 512
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 ... |
339-512 |
5.71e-86 |
|
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: 273.57 E-value: 5.71e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 339 LPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGYTNKGMkIACTQPRRVAAMSVAARVAREMGVKLGNEVG 418
Cdd:cd17983 1 LPIFAVRQELLNVIRDNNVVIVVGETGSGKTTQLTQYLHEDGYTDYGM-IGCTQPRRVAAMSVAKRVSEEMGVELGEEVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 419 YSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVLVASATMDTA 498
Cdd:cd17983 80 YAIRFEDCTSENTVIKYMTDGILLRESLRDPDLDKYSAIIMDEAHERSLNTDVLFGLLREVVARRRDLKLIVTSATMDAD 159
|
170
....*....|....
gi 256000749 499 RFSTFFDDAPVFRI 512
Cdd:cd17983 160 KFADFFGNVPIFTI 173
|
|
| DEXHc_DHX33 |
cd17978 |
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA ... |
339-512 |
3.92e-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: 268.45 E-value: 3.92e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 339 LPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGYTNKGMkIACTQPRRVAAMSVAARVAREMGVKLGNEVG 418
Cdd:cd17978 1 LPIYSARKRLLEELRKHDTVIIIGETGSGKTTQIPQYLYEAGFARGGM-IGITQPRRVAAVSVAKRVAEEMGVELGQLVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 419 YSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFR-----PELKVLVASA 493
Cdd:cd17978 80 YSVRFDDVTSEETRIKYMTDGMLLREAIGDPLLSKYSVIILDEAHERTVHTDVLFGLVKSAQRRRkeqklSPLKVIIMSA 159
|
170
....*....|....*....
gi 256000749 494 TMDTARFSTFFDDAPVFRI 512
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 ... |
336-512 |
4.93e-83 |
|
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: 266.20 E-value: 4.93e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 336 RRSLPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGYTNKGMK-IACTQPRRVAAMSVAARVAREMGVKLG 414
Cdd:cd17973 10 RRELPVWEQKEDFLKLLKNNQILVLVGETGSGKTTQIPQFVLDDELPHQPKKlVACTQPRRVAAMSVAQRVAEEMDVKLG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 415 NEVGYSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVLVASAT 494
Cdd:cd17973 90 EEVGYSIRFEDCSSAKTILKYMTDGMLLREAMSDPLLSRYSVIILDEAHERTLATDILMGLLKEVVRRRPDLKLIVMSAT 169
|
170
....*....|....*...
gi 256000749 495 MDTARFSTFFDDAPVFRI 512
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 ... |
517-678 |
3.12e-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: 255.15 E-value: 3.12e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 517 FPVDIFYTKAP-----------EADYLEACVVSVLQIHVTQPPGDILVFLTGQEEIEAACEMLQDRCRRLGSKirELLVL 585
Cdd:cd18791 1 FPVEVYYLEDIlellgissekeDPDYVDAAVRLILQIHRTEEPGDILVFLPGQEEIERLCELLREELLSPDLG--KLLVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 586 PIYANLPSDMQARIFQPTPPGARKVVVATNIAETSLTIEGIIYVLDPGFCKQKSYNPRTGMESLTVTPCSKASANQRAGR 665
Cdd:cd18791 79 PLHSSLPPEEQQRVFEPPPPGVRKVVLATNIAETSITIPGVVYVIDSGLVKEKVYDPRTGLSSLVTVWISKASAEQRAGR 158
|
170
....*....|...
gi 256000749 666 AGRVAAGKCFRLY 678
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 ... |
339-505 |
5.44e-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: 241.60 E-value: 5.44e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 339 LPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGYTNKGMKIACTQPRRVAAMSVAARVAREMGVKLGNEVG 418
Cdd:cd17980 1 LPVFKLRNHILYLVENYQTIVIVGETGCGKSTQIPQYLAEAGWTAGGRVVGCTQPRRVAAVTVAGRVAEEMGAVLGHEVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 419 YSIRFEDCTSE-RTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVLVASATMDT 497
Cdd:cd17980 81 YCIRFDDCTDPqATRIKFLTDGMLVREMMLDPLLTKYSVIMLDEAHERTLYTDILIGLLKKIQKKRGDLRLIVASATLDA 160
|
....*...
gi 256000749 498 ARFSTFFD 505
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 ... |
339-512 |
2.18e-66 |
|
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: 220.50 E-value: 2.18e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 339 LPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGYTNKGMkIACTQPRRVAAMSVAARVAREMGVKLGNEVG 418
Cdd:cd17984 1 LPIQKQRKKLVQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGFSQHGM-IGVTQPRRVAAISVAQRVAEEMKCTLGSKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 419 YSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDV-----ARFRPELKVLVASA 493
Cdd:cd17984 80 YQVRFDDCSSKETAIKYMTDGCLLRHILADPNLTKYSVIILDEAHERSLTTDILFGLLKKLfqeksPNRKEHLKVVVMSA 159
|
170
....*....|....*....
gi 256000749 494 TMDTARFSTFFDDAPVFRI 512
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 ... |
339-512 |
7.06e-59 |
|
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: 199.22 E-value: 7.06e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 339 LPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGYTNKGMkIACTQPRRVAAMSVAARVAREMGVKLGNEVG 418
Cdd:cd17989 1 LPVSQKRDEIAKAIAENQVVIIAGETGSGKTTQLPKICLELGRGIRGL-IGHTQPRRLAARSVAERIAEELKTELGGAVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 419 YSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVLVASATMDTA 498
Cdd:cd17989 80 YKVRFTDQTSDETCVKLMTDGILLAETQTDRYLRAYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKVIITSATIDAE 159
|
170
....*....|....
gi 256000749 499 RFSTFFDDAPVFRI 512
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 ... |
339-513 |
5.75e-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: 191.80 E-value: 5.75e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 339 LPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGYTNK-----GMkIACTQPRRVAAMSVAARVAREMGVkL 413
Cdd:cd17982 1 LPILAEEQEIMEAINENPVVIICGETGSGKTTQVPQFLYEAGFGSPesdnpGM-IGITQPRRVAAVSMAKRVAEELNV-F 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 414 GNEVGYSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPE-------- 485
Cdd:cd17982 79 GKEVSYQIRYDSTVSENTKIKFMTDGVLLKEIQTDFLLRKYSVIIIDEAHERSVNTDILIGMLSRIVPLRAKlylqdqtv 158
|
170 180 190
....*....|....*....|....*....|
gi 256000749 486 --LKVLVASATMdtaRFSTFFDDAPVFRIP 513
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 ... |
339-512 |
2.84e-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: 189.19 E-value: 2.84e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 339 LPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGYTNkgmkIACTQPRRVAAMSVAARVAREMGVKLGNEVG 418
Cdd:cd17979 1 LPIAQYREKIIELLKTHQVVIVAGDTGCGKSTQVPQYLLAAGFRH----IACTQPRRIACISLAKRVAFESLNQYGSKVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 419 YSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVLVASATMDTA 498
Cdd:cd17979 77 YQIRFERTRTLATKLLFLTEGLLLRQIQRDASLPQYNVLILDEVHERHLHGDFLLGVLRCLLRLRPDLKLILMSATINIE 156
|
170
....*....|....
gi 256000749 499 RFSTFFDDAPVFRI 512
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 ... |
339-512 |
1.48e-51 |
|
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: 178.88 E-value: 1.48e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 339 LPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEgYTNKGM----KIACTQPRRVAAMSVAARVAREMG--VK 412
Cdd:cd17981 1 LPSYGMKQEIINMIDNNQVTVISGETGCGKTTQVTQFILDD-AIERGKgsscRIVCTQPRRISAISVAERVAAERAesCG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 413 LGNEVGYSIRFED-CTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVLVA 491
Cdd:cd17981 80 LGNSTGYQIRLESrKPRKQGSILYCTTGIVLQWLQSDPHLSNVSHLVLDEIHERNLQSDVLMGIVKDLLPFRSDLKVILM 159
|
170 180
....*....|....*....|.
gi 256000749 492 SATMDTARFSTFFDDAPVFRI 512
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 ... |
339-512 |
9.39e-50 |
|
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: 173.47 E-value: 9.39e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 339 LPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFE---EGYTNKGMkIACTQPRRVAAMSVAARVAREMGVKLGN 415
Cdd:cd17977 1 LPVWEAKYEFMESLAHNQIVIVSGDAKTGKSSQIPQWCAEyclSAHYQHGV-VVCTQVHKQTAVWLALRVADEMDVNIGH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 416 EVGYSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVLVASATM 495
Cdd:cd17977 80 EVGYVIPFENCCTNETILRYCTDDMLLREMMSDPLLESYGVIILDDAHERTVSTDVLLGLLKDVLLSRPELKLVIITCPH 159
|
170
....*....|....*..
gi 256000749 496 DTARFSTFFDDAPVFRI 512
Cdd:cd17977 160 LSSKLLSYYGNVPLIEV 176
|
|
| DEXHc_DHX29 |
cd17975 |
DEXH-box helicase domain of DEAH-box helicase 29; DEAH-box helicase 29 (DHX29) is a part of ... |
339-512 |
1.60e-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: 170.48 E-value: 1.60e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 339 LPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEE----GYTNKGMKIACTQPRRVAAMSVAARVAREMGVKLG 414
Cdd:cd17975 1 LPVFKHRESILETLKRHRVVVVAGETGSGKSTQVPQFLLEDlllnGGTAQKCNIVCTQPRRISAMSLATRVCEELGCESG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 415 ----NEV-GYSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVL 489
Cdd:cd17975 81 pggkNSLcGYQIRMESRTGEATRLLYCTTGVLLRKLQEDGLLSSISHIIVDEVHERSVQSDFLLIILKEILHKRSDLHLI 160
|
170 180
....*....|....*....|...
gi 256000749 490 VASATMDTARFSTFFDDAPVFRI 512
Cdd:cd17975 161 LMSATVDCEKFSSYFTHCPILRI 183
|
|
| DEXHc_DHX57 |
cd17985 |
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the ... |
339-512 |
2.87e-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: 2.87e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 339 LPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFE---EGYTNKGMKIACTQPRRVAAMSVAARVAREMGVKLGN 415
Cdd:cd17985 1 LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFILDnslQGPPLPVANIICTQPRRISAISVAERVAQERAERVGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 416 EVGYSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVLVASATM 495
Cdd:cd17985 81 SVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDPTLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQRPDLKVILMSATL 160
|
170
....*....|....*..
gi 256000749 496 DTARFSTFFDDAPVFRI 512
Cdd:cd17985 161 NAELFSDYFNSCPVIHI 177
|
|
| DEXHc_YTHDC2 |
cd17987 |
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) ... |
339-512 |
1.30e-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: 1.30e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 339 LPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGY-TNKGMKIACTQPRRVAAMSVAARVAREMGVKLGNEV 417
Cdd:cd17987 1 LPVFEKQEQIVRIIKENKVVLIVGETGSGKTTQIPQFLLDDCYaNGIPCRIFCTQPRRLAAIAVAERVAAERGEKIGQTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 418 GYSIRFEDCTSERTVLRYMTDGMLLREFLS-EPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVLVASATMD 496
Cdd:cd17987 81 GYQIRLESRVSPKTLLTFCTNGVLLRTLMAgDSALSTVTHVIVDEVHERDRFSDFLLTKLRDILQKHPNLKLILSSAALD 160
|
170
....*....|....*.
gi 256000749 497 TARFSTFFDDAPVFRI 512
Cdd:cd17987 161 VNLFIRYFGSCPVIYI 176
|
|
| DEXHc_HrpB |
cd17990 |
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ... |
339-511 |
1.95e-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: 1.95e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 339 LPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEgYTNKGMKIACTQPRRVAAMSVAARVAREMGVKLGNEVG 418
Cdd:cd17990 1 LPIAAVLPALRAALDAGGQVVLEAPPGAGKTTRVPLALLAE-LWIAGGKIIVLEPRRVAARAAARRLATLLGEAPGETVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 419 YSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVAR-FRPELKVLVASATMDT 497
Cdd:cd17990 80 YRVRGESRVGRRTRVEVVTEGVLLRRLQRDPELSGVGAVILDEFHERSLDADLALALLLEVQQlLRDDLRLLAMSATLDG 159
|
170
....*....|....
gi 256000749 498 ARFSTFFDDAPVFR 511
Cdd:cd17990 160 DGLAALLPEAPVVE 173
|
|
| DEXHc_DHX30 |
cd17976 |
DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an ... |
339-512 |
2.50e-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: 2.50e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 339 LPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGYTN-KGMK--IACTQPRRVAAMSVAARVAREMGVKLGN 415
Cdd:cd17976 1 LPVDSHKESILSAIEQNPVVVISGDTGCGKTTRIPQFILEDYVLRgRGARcnVVITQPRRISAVSVAQRVAHELGPNLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 416 EVGYSIRFEDCTSERT-VLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVLVASAT 494
Cdd:cd17976 81 NVGYQVRLESRPPPRGgALLFCTVGVLLKKLQSNPRLEGVSHVIVDEVHERDVNTDFLLILLKGVLQLNPELRVVLMSAT 160
|
170
....*....|....*...
gi 256000749 495 MDTARFSTFFDDAPVFRI 512
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 ... |
299-512 |
1.33e-45 |
|
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: 163.85 E-value: 1.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 299 EEETIEFVRATQLQGDEEPSAPPTSTQAQQKESIQAVRRSLPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFE 378
Cdd:cd17972 19 DEGPLAFATPEQISMDLKNELMYQREQDHNLQQILQERELLPVKKFREEILEAISNNPVVIIRGATGCGKTTQVPQYILD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 379 E-------GYTNkgmkIACTQPRRVAAMSVAARVAREMGVKLGNEVGYSIRFEDCTSE-RTVLRYMTDGMLLREFlsEPD 450
Cdd:cd17972 99 DfiqndraAECN----IVVTQPRRISAVSVAERVAFERGEEVGKSCGYSVRFESVLPRpHASILFCTVGVLLRKL--EAG 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256000749 451 LASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVLVASATMDTARFSTFFDDAPVFRI 512
Cdd:cd17972 173 IRGISHVIVDEIHERDINTDFLLVVLRDVVQAYPDLRVILMSATIDTSMFCEYFFNCPVIEV 234
|
|
| DEXQc_DQX1 |
cd17986 |
DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 ... |
339-512 |
2.28e-42 |
|
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: 152.74 E-value: 2.28e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 339 LPVFPFREELLAAI-ANHQVLIIEGETGSGKTTQIPQYLFEEGYTNKGMK--IACTQPRRVAAMSVAARVAREMGVKLGN 415
Cdd:cd17986 1 LPIWAAKFTFLEQLeSPSGIVLVSGEPGSGKSTQVPQWCAEFALSRGFQKgqVTVTQPHPLAARSLALRVADEMDLNLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 416 EVGYSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVLVASATM 495
Cdd:cd17986 81 EVGYSIPQEDCTGPNTILRFCWDRLLLQEMTSTPLLGAWGVVVLDEAQERSVASDSLLGLLKDVRLQRPELRVVVVTSPA 160
|
170
....*....|....*..
gi 256000749 496 DTARFSTFFDDAPVFRI 512
Cdd:cd17986 161 LEPKLRAFWGNPPVVHV 177
|
|
| DEXHc_TDRD9 |
cd17988 |
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ... |
339-504 |
5.62e-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: 145.72 E-value: 5.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 339 LPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGY-TNKGMKIACTQPRRVAAMSVAARVAREMGVKLGNEV 417
Cdd:cd17988 1 LPIYAKREEILSLIEANSVVIIKGATGCGKTTQLPQFILDHYYkRGKYCNIVVTQPRRIAAISIARRVSQEREWTLGSLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 418 GYSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRP-ELKVLVASATMD 496
Cdd:cd17988 81 GYQVGLERPASEETRLIYCTTGVLLQKLINNKTLTEYTHIILDEVHERDQELDFLLLVVRRLLRTNSrHVKIILMSATIS 160
|
....*...
gi 256000749 497 TARFSTFF 504
Cdd:cd17988 161 CKEFADYF 168
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
339-521 |
1.48e-27 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 111.04 E-value: 1.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 339 LPVFPFREELLAAI-ANHQVLIIEGETGSGKTTQIPQYLFEEGYTNKGMKIACTQPRRVAAMSVAARVAREMGVKLGNEV 417
Cdd:smart00487 7 EPLRPYQKEAIEALlSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELKKLGPSLGLKVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 418 GY------SIRFEDCTSERTVLRYMTDGMLLREFLSEP-DLASYSVVMVDEAHERT--LHTDILFGLIKdvaRFRPELKV 488
Cdd:smart00487 87 GLyggdskREQLRKLESGKTDILVTTPGRLLDLLENDKlSLSNVDLVILDEAHRLLdgGFGDQLEKLLK---LLPKNVQL 163
|
170 180 190
....*....|....*....|....*....|....*
gi 256000749 489 LVASATM--DTARFSTFFDDAPVFRIPGRRFPVDI 521
Cdd:smart00487 164 LLLSATPpeEIENLLELFLNDPVFIDVGFTPLEPI 198
|
|
| HA2 |
smart00847 |
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ... |
738-822 |
7.91e-26 |
|
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: 101.58 E-value: 7.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 738 ALGALNHLGELTTSGRKMAELPVDPMLSKMILASEKYSCSEEILTVAAMLSVNNsifYRPKDKVVHADNARVNFFLPGGD 817
Cdd:smart00847 1 ELGALDDDGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGD---PRPKEKREDADAARRRFADPESD 77
|
....*
gi 256000749 818 HLVLL 822
Cdd:smart00847 78 HLTLL 82
|
|
| OB_NTP_bind |
pfam07717 |
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ... |
879-955 |
4.02e-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: 99.63 E-value: 4.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 879 VRKAITAGYFYHTARLTRSG--YRTVKQQQTVFIHPNSSLF---EQQPRWLLYHELVLTTKEFMRQVLEIESSWLLEVAP 953
Cdd:pfam07717 1 LRAALAAGLYPNVARRDPKGkgYTTLSDNQRVFIHPSSVLFnekTFPPEWVVYQELVETTKVYIRTVTAISPEWLLLFAP 80
|
..
gi 256000749 954 HY 955
Cdd:pfam07717 81 HI 82
|
|
| HA2 |
pfam04408 |
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ... |
732-821 |
4.37e-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: 100.39 E-value: 4.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 732 ALEQLYALGALNHLGELTTSGRKMAELPVDPMLSKMILASEKYSCSEEILTVAAMLSVNNsIFYRP-------------- 797
Cdd:pfam04408 1 ALELLYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRD-PFVQPnfldprsaakaarr 79
|
90 100
....*....|....*....|....*...
gi 256000749 798 ----KDKVVHADNARVNFFlpgGDHLVL 821
Cdd:pfam04408 80 rrraADEKARAKFARLDLE---GDHLTL 104
|
|
| PHA02653 |
PHA02653 |
RNA helicase NPH-II; Provisional |
347-679 |
4.55e-14 |
|
RNA helicase NPH-II; Provisional
Pssm-ID: 177443 [Multi-domain] Cd Length: 675 Bit Score: 76.55 E-value: 4.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 347 ELLAAIANHQVLIIEGETGSGKTTQIPQ------YLFEeGYTNKGmKIACTQPRRVAAMSVAaRVA--REMGVKLGNEVG 418
Cdd:PHA02653 171 KIFEAWISRKPVVLTGGTGVGKTSQVPKlllwfnYLFG-GFDNLD-KIDPNFIERPIVLSLP-RVAlvRLHSITLLKSLG 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 419 Y--------SIRFEDCTSERTVLRYMTDGMLLREF-LSEPDLASYSVVMVDEAHERTLHTDILFG-LIKDVARFRpelKV 488
Cdd:PHA02653 248 FdeidgspiSLKYGSIPDELINTNPKPYGLVFSTHkLTLNKLFDYGTVIIDEVHEHDQIGDIIIAvARKHIDKIR---SL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 489 LVASATM--DTARFSTFFDDAPVFRIPG-RRFPVDIFYTKAP-----EADYLEA---CVVSVLQIHVTQPPGDILVFLtg 557
Cdd:PHA02653 325 FLMTATLedDRDRIKEFFPNPAFVHIPGgTLFPISEVYVKNKynpknKRAYIEEekkNIVTALKKYTPPKGSSGIVFV-- 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 558 qeEIEAACEMLQdrcRRLGSKIRELLVLPIYANLPS--DMQARIFQPTPPgarKVVVATNIAETSLTIEGIIYVLDPGFC 635
Cdd:PHA02653 403 --ASVSQCEEYK---KYLEKRLPIYDFYIIHGKVPNidEILEKVYSSKNP---SIIISTPYLESSVTIRNATHVYDTGRV 474
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 256000749 636 KQKSynPRTGMESLTvtpcSKASANQRAGRAGRVAAGKCFRLYT 679
Cdd:PHA02653 475 YVPE--PFGGKEMFI----SKSMRTQRKGRVGRVSPGTYVYFYD 512
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
566-668 |
3.47e-11 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 59.92 E-value: 3.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 566 EMLQDRCRRLGSKirellVLPIYANLPSDMQARIFQPTPPGARKVVVATNIAETSLTIEGIIYVLDPGFckqksynprtg 645
Cdd:smart00490 1 EELAELLKELGIK-----VARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDL----------- 64
|
90 100
....*....|....*....|...
gi 256000749 646 mesltvtPCSKASANQRAGRAGR 668
Cdd:smart00490 65 -------PWSPASYIQRIGRAGR 80
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
539-669 |
6.14e-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: 6.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 539 VLQIHVTQPPGDILVFLTGQEEIEaaCEMLQDRcrrlgskiRELLVLPIYANLPSDMQARIFQPTPPGARKVVVATNIAE 618
Cdd:pfam00271 6 LLELLKKERGGKVLIFSQTKKTLE--AELLLEK--------EGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAE 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 256000749 619 TSLTIEGIIYVLDpgfckqksYNPrtgmesltvtPCSKASANQRAGRAGRV 669
Cdd:pfam00271 76 RGLDLPDVDLVIN--------YDL----------PWNPASYIQRIGRAGRA 108
|
|
| DEXHc_viral_Ns3 |
cd17931 |
DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional ... |
356-494 |
1.09e-07 |
|
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: 52.17 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 356 QVLIIEGETGSGKTTQIPQYLFEEGYtNKGMKIACTQPRRVAAMSVAARVaREMGVKLGNEVgysIRFEDctSERTVLRY 435
Cdd:cd17931 2 QLTVLDLHPGAGKTTRVLPQIIREAI-KKRLRTLVLAPTRVVAAEMYEAL-RGLPIRYRTGA---VKEEH--GGNEIVDY 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 256000749 436 MTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFrPELKVLVASAT 494
Cdd:cd17931 75 MCHGTFTCRLLSPKRVPNYNLIIMDEAHFTDPASIAARGYIHTRVEM-GEAAVIFMTAT 132
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
88-316 |
1.37e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.92 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 88 TGGSKQQTEKPESEDEWERTERERLQDLEERDAFAERVRQRDKDRTRNVLERSD--KKAYEEAQK--RLKMAEEDRKAmv 163
Cdd:PTZ00121 1447 DEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADeaKKAAEAKKKadEAKKAEEAKKA-- 1524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 164 PELRK--KSRREYLAKREREKLEDLEAELADEEFLFGDVELSRHERQELKYKRRVRDLAREYRAAGEQEKLEATNRYHMP 241
Cdd:PTZ00121 1525 DEAKKaeEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEE 1604
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256000749 242 KETRGQPARAvdlvEEESGAPGEEQRRWEEARLGAASLKfgarDAASQEPKYQLVLEEEETIEFVRATQLQGDEE 316
Cdd:PTZ00121 1605 KKMKAEEAKK----AEEAKIKAEELKKAEEEKKKVEQLK----KKEAEEKKKAEELKKAEEENKIKAAEEAKKAE 1671
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
96-301 |
3.01e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.76 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 96 EKPESEDEWERTERERLQDLEERDAFAERVRQRDKDRTRnvLERSDKKAYEEAQKrlkmAEEDRKAmvpELRKKSRREYL 175
Cdd:PTZ00121 1596 EVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKK--VEQLKKKEAEEKKK----AEELKKA---EEENKIKAAEE 1666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 176 AKR-EREKLEDLEAELADEEFLFGDVELSRHERQELKYKRRVRDLAREYRAAGEQEKLEatnryhmpkETRGQPARAVDL 254
Cdd:PTZ00121 1667 AKKaEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAE---------EENKIKAEEAKK 1737
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 256000749 255 VEEESGAPGEEQRRWEEARLGAASLKFGARDAASQEPKYQLVLEEEE 301
Cdd:PTZ00121 1738 EAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEE 1784
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
96-347 |
3.30e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.76 E-value: 3.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 96 EKPESEDEWERTERERlQDLEERDAFAERVRQRDKDRTRnvleRSDKKAYEEAQKRlkmAEEDRKAmvPELRKKSRREYL 175
Cdd:PTZ00121 1402 EDKKKADELKKAAAAK-KKADEAKKKAEEKKKADEAKKK----AEEAKKADEAKKK---AEEAKKA--EEAKKKAEEAKK 1471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 176 AKREREKLEdlEAELADEefLFGDVELSRHERQELKYKRRVRDLAREYRAAGEQEKL-------EATNRYHMPKETRGQP 248
Cdd:PTZ00121 1472 ADEAKKKAE--EAKKADE--AKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKAdeakkaeEAKKADEAKKAEEKKK 1547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 249 ARAVDLVEE----ESGAPGEEQRRWEEARLGAASLKFGARDAasQEPKYQLVLEEEETIEFVRATQLQGDEEpsappTST 324
Cdd:PTZ00121 1548 ADELKKAEElkkaEEKKKAEEAKKAEEDKNMALRKAEEAKKA--EEARIEEVMKLYEEEKKMKAEEAKKAEE-----AKI 1620
|
250 260
....*....|....*....|...
gi 256000749 325 QAQQKESIQAVRRSLPVFPFREE 347
Cdd:PTZ00121 1621 KAEELKKAEEEKKKVEQLKKKEA 1643
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
343-496 |
4.86e-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: 50.70 E-value: 4.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 343 PFREELLAAIANHQVLIIEGETGSGKTT--QIPqyLFEE-GYTNKGMKIACTQPRRVAAMSVaARVAREMGVKLGNEVGY 419
Cdd:pfam00270 2 PIQAEAIPAILEGRDVLVQAPTGSGKTLafLLP--ALEAlDKLDNGPQALVLAPTRELAEQI-YEELKKLGKGLGLKVAS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 420 SIRFEDCTSERTVLR-----YMTDGMLLREFLSEPDLASYSVVMVDEAHErtlHTDILFG--LIKDVARFRPELKVLVAS 492
Cdd:pfam00270 79 LLGGDSRKEQLEKLKgpdilVGTPGRLLDLLQERKLLKNLKLLVLDEAHR---LLDMGFGpdLEEILRRLPKKRQILLLS 155
|
....
gi 256000749 493 ATMD 496
Cdd:pfam00270 156 ATLP 159
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
358-494 |
8.19e-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: 49.32 E-value: 8.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 358 LIIEGETGSGKTTQIPQYLFEEGyTNKGMKIACTQPRRVAAMSVAARVAREMgvKLGNEVGYSIRFEDcTSERTVLR--- 434
Cdd:cd00046 4 VLITAPTGSGKTLAALLAALLLL-LKKGKKVLVLVPTKALALQTAERLRELF--GPGIRVAVLVGGSS-AEEREKNKlgd 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 256000749 435 ----YMTDGMLLREFLSE--PDLASYSVVMVDEAHERT-LHTDILFGLIKDVARFRPELKVLVASAT 494
Cdd:cd00046 80 adiiIATPDMLLNLLLREdrLFLKDLKLIIVDEAHALLiDSRGALILDLAVRKAGLKNAQVILLSAT 146
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
94-211 |
1.37e-06 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 52.45 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 94 QTEKPESEDEWERTERERLQDLEERDAFAERVRQRDKDRtrnvlERSDKKAYEEAQKRLKMAEEDRKAMVPELRKKSRRE 173
Cdd:COG1193 524 ERERRELEEEREEAERLREELEKLREELEEKLEELEEEK-----EEILEKAREEAEEILREARKEAEELIRELREAQAEE 598
|
90 100 110
....*....|....*....|....*....|....*...
gi 256000749 174 YLAKREREKLEDLEAELADEEFLFGDVELSRHERQELK 211
Cdd:COG1193 599 EELKEARKKLEELKQELEEKLEKPKKKAKPAKPPEELK 636
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
93-237 |
1.52e-06 |
|
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: 52.05 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 93 QQTEKPESEDEWERTERERLQDLEE-RDAFAERVRQRDKDRTRNVlERSDKKAYEEAQKRLKMAEEDR-KAMVPELRKKS 170
Cdd:pfam17380 418 QKVEMEQIRAEQEEARQREVRRLEEeRAREMERVRLEEQERQQQV-ERLRQQEEERKRKKLELEKEKRdRKRAEEQRRKI 496
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 256000749 171 RREYLAKREREKLED------LEAELAD------EEFLFGDVELSRHERQELKYKRRVRDLAReyRAAGEQEKLEATNR 237
Cdd:pfam17380 497 LEKELEERKQAMIEEerkrklLEKEMEErqkaiyEEERRREAEEERRKQQEMEERRRIQEQMR--KATEERSRLEAMER 573
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
88-338 |
4.65e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 4.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 88 TGGSKQQTEKPESEDEWERTERERLQDLEERdafAERVRQRDKDRTrnvlERSDKKAyEEAQKRlkmAEEDRKAmvPELR 167
Cdd:PTZ00121 1331 ADAAKKKAEEAKKAAEAAKAEAEAAADEAEA---AEEKAEAAEKKK----EEAKKKA-DAAKKK---AEEKKKA--DEAK 1397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 168 KKSRREylaKREREKLEDLEAELADEEFLFGDVELSRhERQELKYKRRVRDLAREYRAAGEqEKLEATNRYHMPKETRGQ 247
Cdd:PTZ00121 1398 KKAEED---KKKADELKKAAAAKKKADEAKKKAEEKK-KADEAKKKAEEAKKADEAKKKAE-EAKKAEEAKKKAEEAKKA 1472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 248 paravdlveEESGAPGEEQRRWEEARLGAASLKFGARDAASQEPKYQLVLEEEETIEFVRATQLQGDEEPSAPPTSTQAQ 327
Cdd:PTZ00121 1473 ---------DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAE 1543
|
250
....*....|.
gi 256000749 328 QKESIQAVRRS 338
Cdd:PTZ00121 1544 EKKKADELKKA 1554
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
82-316 |
1.96e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 82 EKGKKKTGGSKQQTEKPESEDEWERtERERLQDLEERDAFAERVRQRDKDRTRNVLERS-DKKAYEEAQK--------RL 152
Cdd:PTZ00121 1473 DEAKKKAEEAKKADEAKKKAEEAKK-KADEAKKAAEAKKKADEAKKAEEAKKADEAKKAeEAKKADEAKKaeekkkadEL 1551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 153 KMAEEDRKA----MVPELRKKSRREYLAKREREKLEDLEaELADEEFLFGDVELSRHERQELKYKRRVRDLAREYRAAGE 228
Cdd:PTZ00121 1552 KKAEELKKAeekkKAEEAKKAEEDKNMALRKAEEAKKAE-EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEE 1630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 229 QEKLEATNRYHMPKETRgqPARAVDLVEEESGA-PGEEQRRWEEARLGAASLKFGARDAASQEPKYQLVLEEEETIEFVR 307
Cdd:PTZ00121 1631 EKKKVEQLKKKEAEEKK--KAEELKKAEEENKIkAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELK 1708
|
250
....*....|....*...
gi 256000749 308 ---------ATQLQGDEE 316
Cdd:PTZ00121 1709 kkeaeekkkAEELKKAEE 1726
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
93-284 |
4.30e-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: 46.76 E-value: 4.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 93 QQTEKPESEDEWERTERERLQDLEERDAFAERVRQRDKDRTRNVLERSDKKAYEEAQKRlkmAEEDRKAMVPELRKKSRR 172
Cdd:TIGR02794 93 ELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQ---AEEEAKAKAAAEAKKKAE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 173 EYLAKREREKLEDLEAEL-ADEEFLFGDVElsrherqELKYKRRVRDLAREYRAAGEQEKLEAtnryhmpkETRGQPARA 251
Cdd:TIGR02794 170 EAKKKAEAEAKAKAEAEAkAKAEEAKAKAE-------AAKAKAAAEAAAKAEAEAAAAAAAEA--------ERKADEAEL 234
|
170 180 190
....*....|....*....|....*....|...
gi 256000749 252 VDLVEEESGAPGEEQRRWEEARLGAASLKFGAR 284
Cdd:TIGR02794 235 GDIFGLASGSNAEKQGGARGAAAGSEVDKYAAI 267
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
93-290 |
5.32e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 5.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 93 QQTEKPESEDEWERTERERLQDLEERDAF--------AERVRQRDKDRTRNVLERSD-KKAYEEAQKRlkmAEEDRKAmv 163
Cdd:PTZ00121 1243 KKAEEERNNEEIRKFEEARMAHFARRQAAikaeearkADELKKAEEKKKADEAKKAEeKKKADEAKKK---AEEAKKA-- 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 164 PELRKKSrREYLAKREREKLEDLEAELADEEflfgdvelsrhERQELKYKRRVRDLAREYRAAGEQEKLEATNRYHMPKE 243
Cdd:PTZ00121 1318 DEAKKKA-EEAKKKADAAKKKAEEAKKAAEA-----------AKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKK 1385
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 256000749 244 TRGQPARAVDLVE--EESGAPGEEQRRWEEARLGAASLKFGARDAASQE 290
Cdd:PTZ00121 1386 KAEEKKKADEAKKkaEEDKKKADELKKAAAAKKKADEAKKKAEEKKKAD 1434
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
103-337 |
6.69e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 6.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 103 EWERTERERLQDLEERDAFAERVRQRDKDRTRNVLERSDKKAYEEAQKrlkmAEEDRKAMVPELRKKSRREYLAKREREK 182
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARK----AEEARKAEDAKRVEIARKAEDARKAEEA 1169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 183 LEDLEAELADEeflfgdvelsrhERQELKYKRrvrdlAREYRAAGEQEKLEATNRYHMPKET----RGQPARAVDLVE-- 256
Cdd:PTZ00121 1170 RKAEDAKKAEA------------ARKAEEVRK-----AEELRKAEDARKAEAARKAEEERKAeearKAEDAKKAEAVKka 1232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 257 EESGAPGEEQRRWEEARLGAASLKFGARDAASQEPKYQLVLEEEETiefvRATQLQGDEEPSAPPTSTQAQQKESIQAVR 336
Cdd:PTZ00121 1233 EEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEAR----KADELKKAEEKKKADEAKKAEEKKKADEAK 1308
|
.
gi 256000749 337 R 337
Cdd:PTZ00121 1309 K 1309
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
99-267 |
1.20e-03 |
|
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: 42.75 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 99 ESEDEWERTERERLQDLEERDAFAERVRQRDKD------RTRNVLERSDKKAYEEAQKRLKMAEEDRKA----------- 161
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIDKLLAEIEELEREieeerkRRDKLTEEYAELKEELEDLRAELEEVDKEFaetrdelkdyr 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 162 ---------MVPELRKKSRREYLAKREREKLEDLEAELADEEFLFGDVELSRHERQ-ELKYKRRVRDLAREYRAAGEQEK 231
Cdd:TIGR02169 392 ekleklkreINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAlEIKKQEWKLEQLAADLSKYEQEL 471
|
170 180 190
....*....|....*....|....*....|....*.
gi 256000749 232 LEATNRYHMPKETRGQPARAVDLVEEESGAPGEEQR 267
Cdd:TIGR02169 472 YDLKEEYDRVEKELSKLQRELAEAEAQARASEERVR 507
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
97-273 |
1.34e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 97 KPESEDEWERTERERLQDLEErdafAERVRQRDKDRTRNVLERS-DKKAYEEAQK--RLKMAEEDRKAM----VPELRK- 168
Cdd:PTZ00121 1121 KKKAEDARKAEEARKAEDARK----AEEARKAEDAKRVEIARKAeDARKAEEARKaeDAKKAEAARKAEevrkAEELRKa 1196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 169 -KSRREYLAKREREKLEDLEAELADEEFLFGDVELSRHERQELKYKRRvrdlAREYRAAGEQEKLEATNRYHMPKETRGQ 247
Cdd:PTZ00121 1197 eDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKK----AEEERNNEEIRKFEEARMAHFARRQAAI 1272
|
170 180
....*....|....*....|....*.
gi 256000749 248 PARAVDLVEEESGApgEEQRRWEEAR 273
Cdd:PTZ00121 1273 KAEEARKADELKKA--EEKKKADEAK 1296
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
139-237 |
2.70e-03 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 41.65 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 139 RSDKKAYEEAqkRLKMAEEDRKAMVPELRKKSRREYLAKREREKLEDLEAELADEEflfgDVELSRHERQELKYKRRVRD 218
Cdd:PTZ00266 429 RVDKDHAERA--RIEKENAHRKALEMKILEKKRIERLEREERERLERERMERIERE----RLERERLERERLERDRLERD 502
|
90 100
....*....|....*....|...
gi 256000749 219 ----LAREYRAAGEQEKLEATNR 237
Cdd:PTZ00266 503 rldrLERERVDRLERDRLEKARR 525
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
97-268 |
2.82e-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: 41.48 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 97 KPESEDEWERTERERLQDLEERDAFAERVRQRDKDRTRNVLERSDKKAYEEAQKrlkmaeedrkamvpelrkksrreylA 176
Cdd:pfam15709 393 KQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAER-------------------------A 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 177 KREREKLEDLEAELADEEFLFgdVELSRHERqeLKYKRRVRDlareyraAGEQEKLEAtnryhmpKETRGQPARAVDLVE 256
Cdd:pfam15709 448 EAEKQRQKELEMQLAEEQKRL--MEMAEEER--LEYQRQKQE-------AEEKARLEA-------EERRQKEEEAARLAL 509
|
170
....*....|..
gi 256000749 257 EESGAPGEEQRR 268
Cdd:pfam15709 510 EEAMKQAQEQAR 521
|
|
| SF-CC1 |
TIGR01622 |
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ... |
108-227 |
3.09e-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: 41.06 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 108 ERERLQDLE-------ERDAFAERVRQRDKDRTRNVLERSDKKAYEEAQK-RLKMAEEDRKAMVPELRKKSRREYLAKRE 179
Cdd:TIGR01622 6 ERERLRDSSsagdrdrRRDKGRERSRDRSRDRERSRSRRRDRHRDRDYYRgRERRSRSRRPNRRYRPREKRRRRGDSYRR 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 256000749 180 REKLEDLEAELADEEFLFGDvELSRHER-------QELKYKRRVRDLAREYRAAG 227
Cdd:TIGR01622 86 RRDDRRSRREKPRARDGTPE-PLTEDERdrrtvfvQQLAARARERDLYEFFSKVG 139
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
52-316 |
3.50e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 52 SRAGSSLQKKrkkrKHLRKKREEEEEEEASEKGKKKTGGSKQQTEKPESEDEWERTERERLQDLEErdafAERVRQRDKD 131
Cdd:PTZ00121 1521 AKKADEAKKA----EEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRK----AEEAKKAEEA 1592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 132 RTRNVL---ERSDKKAYEEAQK----RLKmAEEDRKAmvpELRKKSRREYLAKREREKLEDLEAELADEEFLFGDVELSR 204
Cdd:PTZ00121 1593 RIEEVMklyEEEKKMKAEEAKKaeeaKIK-AEELKKA---EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK 1668
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 205 HERQELKYKRRVRDLAREYRAAGEQEKLEATNRYHMpKETRGQPARAVDLVEEESGAPGEEQRRWEEARLGAASLKFGAR 284
Cdd:PTZ00121 1669 KAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKA-EELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAE 1747
|
250 260 270
....*....|....*....|....*....|....*.
gi 256000749 285 DAASQEPK----YQLVLEEEETIEFVRATQLQGDEE 316
Cdd:PTZ00121 1748 EAKKDEEEkkkiAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
78-357 |
3.85e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 78 EEASEKGKKKTGGSKQQTEKPE----------SEDEWERTERERLQDLEERDAFAERVRQRDKDRTRNVLERSDKKAYEE 147
Cdd:COG1196 324 ELAELEEELEELEEELEELEEEleeaeeeleeAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 148 AQKRLKMAEEDRKAMVpELRKKSRREYLAKREREKLEDLEAELADEEFLFGDVELSRHERQELKYKRRVRDLAREYRAAG 227
Cdd:COG1196 404 ELEEAEEALLERLERL-EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 228 EQEKLEATNRYHMPK------ETRGQPARAVDLVEEESGAPGE--EQRRWEEARLGAASLkfgARDAASQEPKYQLVLEE 299
Cdd:COG1196 483 LEELAEAAARLLLLLeaeadyEGFLEGVKAALLLAGLRGLAGAvaVLIGVEAAYEAALEA---ALAAALQNIVVEDDEVA 559
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 256000749 300 EETIEFV------RATQLQGDEEPSAPPTSTQAQQKESIQAVRRSLPVFPFREELLAAIANHQV 357
Cdd:COG1196 560 AAAIEYLkaakagRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLL 623
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
93-334 |
5.50e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 5.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 93 QQTEKPESEDEwERTERERLQDLEERDAFAERVRQRDKDRTRNVLERSD-KKAYEEAQKRLKMAEEDRkamvpeLRKKSR 171
Cdd:COG1196 301 EQDIARLEERR-RELEERLEELEEELAELEEELEELEEELEELEEELEEaEEELEEAEAELAEAEEAL------LEAEAE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 172 REYLAKREREKLEDLEAELADEEflfgdVELSRHERQELKYKRRVRDLAREYRAAGEQEKLEAtnryhmpkETRGQPARA 251
Cdd:COG1196 374 LAEAEEELEELAEELLEALRAAA-----ELAAQLEELEEAEEALLERLERLEEELEELEEALA--------ELEEEEEEE 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 252 VDLVEEESGAPGEEQRRWEEARLGAASLKFGARDAASQEpkyQLVLEEEETIEFVRATQLQGDEEPSAPPTSTQAQQKES 331
Cdd:COG1196 441 EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL---AELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLA 517
|
...
gi 256000749 332 IQA 334
Cdd:COG1196 518 GLR 520
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
105-190 |
6.98e-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: 38.11 E-value: 6.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 105 ERTERERLQDLEERDAFAERVRQRDKDRTRNVLERSDKkaYEEAQKRLkmaEEDRKAMVPELRKKSRREYLAKREREKLE 184
Cdd:pfam15346 56 EELEREREAELEEERRKEEEERKKREELERILEENNRK--IEEAQRKE---AEERLAMLEEQRRMKEERQRREKEEEERE 130
|
....*.
gi 256000749 185 DLEAEL 190
Cdd:pfam15346 131 KREQQK 136
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
114-274 |
7.46e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.31 E-value: 7.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 114 DLEERDAFAER------VRQRDKDRTRNVLERSDKKAYEEAQKRLKMAEEDRKAMVPELRKKSRREyLAKREREKLEDLE 187
Cdd:COG1196 607 DLREADARYYVlgdtllGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLA-ALLEAEAELEELA 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 188 AELADEEFLFGDVELSRHERQELKYKRRVRDLAREYRAAGEQEKLEATNRYHMPKETRGQPARAVDLVEEESGAPGEEQR 267
Cdd:COG1196 686 ERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEEL 765
|
....*..
gi 256000749 268 RWEEARL 274
Cdd:COG1196 766 ERELERL 772
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
95-235 |
8.34e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 8.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 95 TEKPESEDEWERTER--ERLQDLEERDAFAERVRQRDKDRTRNVLERSDKKAyEEAQKRLKMAEEDRKAMVPELRKKSRR 172
Cdd:PRK02224 579 SKLAELKERIESLERirTLLAAIADAEDEIERLREKREALAELNDERRERLA-EKRERKRELEAEFDEARIEEAREDKER 657
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000749 173 --EYLAKRErEKLEDLEAELADEEFLFGDVELSRHERQELKYKR-----RVRDLAREYraaGEQEKLEAT 235
Cdd:PRK02224 658 aeEYLEQVE-EKLDELREERDDLQAEIGAVENELEELEELRERRealenRVEALEALY---DEAEELESM 723
|
|
| |
