|
Name |
Accession |
Description |
Interval |
E-value |
| HrpA |
COG1643 |
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis]; |
398-1025 |
0e+00 |
|
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441249 [Multi-domain] Cd Length: 836 Bit Score: 556.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 398 SLPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGYTNKGmKIACTQPRRVAAMSVAARVAREMGVKLGNEV 477
Cdd:COG1643 9 DLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGWGAGG-RIGMLEPRRLAARAAAERMAEELGEPVGETV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 478 GYSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDV-ARFRPELKVLVASATMD 556
Cdd:COG1643 88 GYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLqPALRPDLKLLVMSATLD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 557 TARFSTFFDDAPVFRIPGRRFPVDIFYT--KAPEADYLEACVVSVLQIHvTQPPGDILVFLTGQEEIEAACEMLQDRCRR 634
Cdd:COG1643 168 AERFARLLGDAPVIESSGRTYPVEVRYRplPADERDLEDAVADAVREAL-AEEPGDILVFLPGEREIRRTAEALRGRLPP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 635 lgskirELLVLPIYANLPSDMQARIFQPTPPGARKVVVATNIAETSLTIEGIIYVLDPGFCKQKSYNPRTGMESLTVTPC 714
Cdd:COG1643 247 ------DTEILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 715 SKASANQRAGRAGRVAAGKCFRLYTAwAYQHELEETTVPEIQRTSLGNVVLLLKSLGIHDLMHFDFLDPPPYETLLLALE 794
Cdd:COG1643 321 SQASANQRAGRAGRLAPGICYRLWSE-EDFARRPAFTDPEILRADLASLILELAAWGLGDPEDLPFLDPPPARAIADARA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 795 QLYALGALNHLGELTTSGRKMAELPVDPMLSKMILASEKYSCSEEILTVAAMLSVnnsifyrpKDKVVHAdnarvnfflP 874
Cdd:COG1643 400 LLQELGALDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSE--------RDPRRGA---------A 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 875 GGDHLVLLNVYTQWAESGyssqwcyENFVQFRSMRRARDVREQlegLLERVEVGLSSCQGDYIRVRKAITAGYFYHTARL 954
Cdd:COG1643 463 GSDLLARLNLWRRLREQQ-------REFLSYLRLREWRDLARQ---LRRLLGEGANEEPADYEAIGLLLALAYPDRIARR 532
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255982614 955 TRSG--YRTVKQQQtVFIHPNSSLFEQqpRWLLYHELVLTTKE-FMRQVLEIESSWLLEVAPHyyKAKELEDPH 1025
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 ... |
398-1028 |
1.86e-144 |
|
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: 1.86e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 398 SLPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGYTNKGMkIACTQPRRVAAMSVAARVAREMGVKLGNEV 477
Cdd:TIGR01967 65 NLPVSAKREDIAEAIAENQVVIIAGETGSGKTTQLPKICLELGRGSHGL-IGHTQPRRLAARTVAQRIAEELGTPLGEKV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 478 GYSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVLVASATMDT 557
Cdd:TIGR01967 144 GYKVRFHDQVSSNTLVKLMTDGILLAETQQDRFLSRYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKIIITSATIDP 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 558 ARFSTFFDDAPVFRIPGRRFPVDIFY------TKAPEADYLEACVVSVLQIhVTQPPGDILVFLTGQEEIEAACEMLQDR 631
Cdd:TIGR01967 224 ERFSRHFNNAPIIEVSGRTYPVEVRYrplveeQEDDDLDQLEAILDAVDEL-FAEGPGDILIFLPGEREIRDAAEILRKR 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 632 crrlgsKIRELLVLPIYANLPSDMQARIFQPTppGARKVVVATNIAETSLTIEGIIYVLDPGFCKQKSYNPRTGMESLTV 711
Cdd:TIGR01967 303 ------NLRHTEILPLYARLSNKEQQRVFQPH--SGRRIVLATNVAETSLTVPGIHYVIDTGTARISRYSYRTKVQRLPI 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 712 TPCSKASANQRAGRAGRVAAGKCFRLYTAWAYQHElEETTVPEIQRTSLGNVVLLLKSLGIHDLMHFDFLDPPPYETL-- 789
Cdd:TIGR01967 375 EPISQASANQRKGRCGRVAPGICIRLYSEEDFNSR-PEFTDPEILRTNLASVILQMLALRLGDIAAFPFIEAPDPRAIrd 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 790 -LLALEQLYALGALNHLGELTTSGRKMAELPVDPMLSKMILASEKYSCSEEILTVAAMLSVNNsIFYRPKDKVVHADNAR 868
Cdd:TIGR01967 454 gFRLLEELGALDDDEAEPQLTPIGRQLAQLPVDPRLARMLLEAHRLGCLQEVLIIASALSIQD-PRERPMEKQQAADQAH 532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 869 VNFFLPGGDHLVLLNVY-----TQWAESGYS-SQWCYENFVQFRSMRRARDVREQLEGLLERVEVGLSSCQGDYIRVRKA 942
Cdd:TIGR01967 533 ARFKDPRSDFLSRVNLWrhieeQRQALSANQfRNACRKQYLNYLRVREWQDIYRQLTQVVKELGLKLNEEPADYDAIHKA 612
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 943 ITAGYFYHTARLTRSGYRTVKQQQTVFIHPNSSLFEQQPRWLLYHELVLTTKEFMRQVLEIESSWLLEVAPHYYKaKELE 1022
Cdd:TIGR01967 613 LLSGLLSQIGMKDEKHEYDGARGRKFHIFPGSPLFKKPPKWVMAAELVETSKLYARLVAKIEPEWVEPVAGHLIK-KNYF 691
|
....*.
gi 255982614 1023 DPHAKK 1028
Cdd:TIGR01967 692 EPHWEK 697
|
|
| PRK11131 |
PRK11131 |
ATP-dependent RNA helicase HrpA; Provisional |
398-1028 |
2.78e-142 |
|
ATP-dependent RNA helicase HrpA; Provisional
Pssm-ID: 182986 [Multi-domain] Cd Length: 1294 Bit Score: 459.14 E-value: 2.78e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 398 SLPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGYTNKGMkIACTQPRRVAAMSVAARVAREMGVKLGNEV 477
Cdd:PRK11131 72 NLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLELGRGVKGL-IGHTQPRRLAARTVANRIAEELETELGGCV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 478 GYSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVLVASATMDT 557
Cdd:PRK11131 151 GYKVRFNDQVSDNTMVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPDLKVIITSATIDP 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 558 ARFSTFFDDAPVFRIPGRRFPVDIFY------TKAPEADYLEACVVSVLQIHVtQPPGDILVFLTGQEEIEAACEMLQDR 631
Cdd:PRK11131 231 ERFSRHFNNAPIIEVSGRTYPVEVRYrpiveeADDTERDQLQAIFDAVDELGR-EGPGDILIFMSGEREIRDTADALNKL 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 632 crrlgsKIRELLVLPIYANLPSDMQARIFQPTppGARKVVVATNIAETSLTIEGIIYVLDPGFCKQKSYNPRTGMESLTV 711
Cdd:PRK11131 310 ------NLRHTEILPLYARLSNSEQNRVFQSH--SGRRIVLATNVAETSLTVPGIKYVIDPGTARISRYSYRTKVQRLPI 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 712 TPCSKASANQRAGRAGRVAAGKCFRLYTAWAYQHElEETTVPEIQRTSLGNVVLLLKSLGIHDLMHFDFLDPPPYETLLL 791
Cdd:PRK11131 382 EPISQASANQRKGRCGRVSEGICIRLYSEDDFLSR-PEFTDPEILRTNLASVILQMTALGLGDIAAFPFVEAPDKRNIQD 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 792 ALEQLYALGALN-----HLGELTTSGRKMAELPVDPMLSKMILASEKYSCSEEILTVAAMLSVNNSiFYRPKDKVVHADN 866
Cdd:PRK11131 461 GVRLLEELGAITtdeqaSAYKLTPLGRQLAQLPVDPRLARMVLEAQKHGCVREVMIITSALSIQDP-RERPMDKQQASDE 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 867 ARVNFFLPGGDHLVLLNV--YTQWAESGYSS----QWCYENFVQFRSMRRARDVREQLEGLLERVEVGLSSCQGDYIRVR 940
Cdd:PRK11131 540 KHRRFADKESDFLAFVNLwnYLQEQQKALSSnqfrRLCRTDYLNYLRVREWQDIYTQLRQVVKELGIPVNSEPAEYREIH 619
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 941 KAITAGYFYHTarltrsGYRTVKQQQTV-------FIHPNSSLFEQQPRWLLYHELVLTTKEFMRQVLEIESSWLLEVAP 1013
Cdd:PRK11131 620 TALLTGLLSHI------GMKDAEKQEYTgarnarfSIFPGSGLFKKPPKWVMVAELVETSRLWGRIAARIEPEWIEPLAQ 693
|
650
....*....|....*
gi 255982614 1014 HYYKaKELEDPHAKK 1028
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 ... |
399-572 |
6.79e-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: 367.21 E-value: 6.79e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 399 LPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGYTNKGMKIACTQPRRVAAMSVAARVAREMGVKLGNEVG 478
Cdd:cd17974 1 LPVYPYRDDLLAAVKEHQVLIIVGETGSGKTTQIPQYLHEAGYTKGGGKIGCTQPRRVAAMSVAARVAEEMGVKLGNEVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 479 YSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVLVASATMDTA 558
Cdd:cd17974 81 YSIRFEDCTSEKTVLKYMTDGMLLREFLTEPDLASYSVMIIDEAHERTLHTDILFGLVKDIARFRPDLKLLISSATMDAE 160
|
170
....*....|....
gi 255982614 559 RFSTFFDDAPVFRI 572
Cdd:cd17974 161 KFSAFFDDAPIFRI 174
|
|
| DEAH_box_HrpB |
TIGR01970 |
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ... |
399-847 |
1.71e-104 |
|
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: 345.98 E-value: 1.71e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 399 LPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGYTNKgmKIACTQPRRVAAMSVAARVAREMGVKLGNEVG 478
Cdd:TIGR01970 1 LPIHAVLPALRDALAAHPQVVLEAPPGAGKSTAVPLALLDAPGIGG--KIIMLEPRRLAARSAAQRLASQLGEAVGQTVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 479 YSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDV-ARFRPELKVLVASATMDT 557
Cdd:TIGR01970 79 YRVRGENKVSRRTRLEVVTEGILTRMIQDDPELDGVGALIFDEFHERSLDADLGLALALDVqSSLREDLKILAMSATLDG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 558 ARFSTFFDDAPVFRIPGRRFPVDIFYTKAPEADYLEACVVSVLQIHVTQPPGDILVFLTGQEEIEAACEMLQDrcrRLGS 637
Cdd:TIGR01970 159 ERLSSLLPDAPVVESEGRSFPVEIRYLPLRGDQRLEDAVSRAVEHALASETGSILVFLPGQAEIRRVQEQLAE---RLDS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 638 kirELLVLPIYANLPSDMQARIFQPTPPGARKVVVATNIAETSLTIEGIIYVLDPGFCKQKSYNPRTGMESLTVTPCSKA 717
Cdd:TIGR01970 236 ---DVLICPLYGELSLAAQDRAIKPDPQGRRKVVLATNIAETSLTIEGIRVVIDSGLARVARFDPKTGITRLETVRISQA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 718 SANQRAGRAGRVAAGKCFRLYtAWAYQHELEETTVPEIQRTSLGNVVLLLKSLGIHDLMHFDFLDPPPYETLLLALEQLY 797
Cdd:TIGR01970 313 SATQRAGRAGRLEPGVCYRLW-SEEQHQRLPAQDEPEILQADLSGLALELAQWGAKDPSDLRWLDAPPSVALAAARQLLQ 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 255982614 798 ALGALNHLGELTTSGRKMAELPVDPMLSKMILASEKYSCSEEILTVAAML 847
Cdd:TIGR01970 392 RLGALDAQGRLTAHGKAMAALGCHPRLAAMLLSAHSTGLAALACDLAALL 441
|
|
| PRK11664 |
PRK11664 |
ATP-dependent RNA helicase HrpB; Provisional |
398-847 |
1.34e-91 |
|
ATP-dependent RNA helicase HrpB; Provisional
Pssm-ID: 236950 [Multi-domain] Cd Length: 812 Bit Score: 310.70 E-value: 1.34e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 398 SLPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGYTNKgmKIACTQPRRVAAMSVAARVAREMGVKLGNEV 477
Cdd:PRK11664 3 SLPVAAVLPELLTALKTAPQVLLKAPTGAGKSTWLPLQLLQHGGING--KIIMLEPRRLAARNVAQRLAEQLGEKPGETV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 478 GYSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDV-ARFRPELKVLVASATMD 556
Cdd:PRK11664 81 GYRMRAESKVGPNTRLEVVTEGILTRMIQRDPELSGVGLVILDEFHERSLQADLALALLLDVqQGLRDDLKLLIMSATLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 557 TARFSTFFDDAPVFRIPGRRFPVDIFYTKAPEADYL-EACVVSVLQIhVTQPPGDILVFLTGQEEIEAACEMLQDRcrrL 635
Cdd:PRK11664 161 NDRLQQLLPDAPVIVSEGRSFPVERRYQPLPAHQRFdEAVARATAEL-LRQESGSLLLFLPGVGEIQRVQEQLASR---V 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 636 GSkirELLVLPIYANLPSDMQARIFQPTPPGARKVVVATNIAETSLTIEGIIYVLDPGFCKQKSYNPRTGMESLTVTPCS 715
Cdd:PRK11664 237 AS---DVLLCPLYGALSLAEQQKAILPAPAGRRKVVLATNIAETSLTIEGIRLVVDSGLERVARFDPKTGLTRLVTQRIS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 716 KASANQRAGRAGRVAAGKCFRLYTAWAYQhELEETTVPEIQRTSLGNVVLLLKSLGIHDLMHFDFLDPPPYETLLLALEQ 795
Cdd:PRK11664 314 QASMTQRAGRAGRLEPGICLHLYSKEQAE-RAAAQSEPEILHSDLSGLLLELLQWGCHDPAQLSWLDQPPAAALAAAKRL 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 255982614 796 LYALGALNHLGELTTSGRKMAELPVDPMLSKMILASEKYscSEEILTVAAML 847
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 ... |
396-573 |
6.38e-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: 285.15 E-value: 6.38e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 396 RRSLPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGYTNKGmKIACTQPRRVAAMSVAARVAREMGVKLGN 475
Cdd:cd17971 3 RESLPIYKLKEQLIQAVHDNQILVVIGETGSGKTTQITQYLAEAGYTSRG-KIGCTQPRRVAAMSVAKRVAEEFGCCLGQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 476 EVGYSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVLVASATM 555
Cdd:cd17971 82 EVGYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLSQYSVIMLDEAHERTIHTDVLFGLLKKTVQKRPDLKLIVTSATL 161
|
170
....*....|....*...
gi 255982614 556 DTARFSTFFDDAPVFRIP 573
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) ... |
415-572 |
1.24e-87 |
|
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 438707 [Multi-domain] Cd Length: 159 Bit Score: 278.19 E-value: 1.24e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 415 HQVLIIEGETGSGKTTQIPQYLFEEGYTN-KGMKIACTQPRRVAAMSVAARVAREMGVKLGNEVGYSIRFEDCTSERTVL 493
Cdd:cd17917 1 NQVVVIVGETGSGKTTQVPQFLLEDGLAKgGKGRIVCTQPRRIAAISVAERVAEERGEKLGEEVGYQIRFESKTSSKTRI 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255982614 494 RYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVLVASATMDTARFSTFFDDAPVFRI 572
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 ... |
399-572 |
1.10e-85 |
|
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: 1.10e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 399 LPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGYTNKGMkIACTQPRRVAAMSVAARVAREMGVKLGNEVG 478
Cdd:cd17983 1 LPIFAVRQELLNVIRDNNVVIVVGETGSGKTTQLTQYLHEDGYTDYGM-IGCTQPRRVAAMSVAKRVSEEMGVELGEEVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 479 YSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVLVASATMDTA 558
Cdd:cd17983 80 YAIRFEDCTSENTVIKYMTDGILLRESLRDPDLDKYSAIIMDEAHERSLNTDVLFGLLREVVARRRDLKLIVTSATMDAD 159
|
170
....*....|....
gi 255982614 559 RFSTFFDDAPVFRI 572
Cdd:cd17983 160 KFADFFGNVPIFTI 173
|
|
| DEXHc_DHX33 |
cd17978 |
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA ... |
399-572 |
6.68e-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: 268.84 E-value: 6.68e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 399 LPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGYTNKGMkIACTQPRRVAAMSVAARVAREMGVKLGNEVG 478
Cdd:cd17978 1 LPIYSARKRLLEELRKHDTVIIIGETGSGKTTQIPQYLYEAGFARGGM-IGITQPRRVAAVSVAKRVAEEMGVELGQLVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 479 YSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFR-----PELKVLVASA 553
Cdd:cd17978 80 YSVRFDDVTSEETRIKYMTDGMLLREAIGDPLLSKYSVIILDEAHERTVHTDVLFGLVKSAQRRRkeqklSPLKVIIMSA 159
|
170
....*....|....*....
gi 255982614 554 TMDTARFSTFFDDAPVFRI 572
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 ... |
396-572 |
7.45e-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: 266.59 E-value: 7.45e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 396 RRSLPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGYTNKGMK-IACTQPRRVAAMSVAARVAREMGVKLG 474
Cdd:cd17973 10 RRELPVWEQKEDFLKLLKNNQILVLVGETGSGKTTQIPQFVLDDELPHQPKKlVACTQPRRVAAMSVAQRVAEEMDVKLG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 475 NEVGYSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVLVASAT 554
Cdd:cd17973 90 EEVGYSIRFEDCSSAKTILKYMTDGMLLREAMSDPLLSRYSVIILDEAHERTLATDILMGLLKEVVRRRPDLKLIVMSAT 169
|
170
....*....|....*...
gi 255982614 555 MDTARFSTFFDDAPVFRI 572
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 ... |
577-738 |
5.39e-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: 5.39e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 577 FPVDIFYTKAP-----------EADYLEACVVSVLQIHVTQPPGDILVFLTGQEEIEAACEMLQDRCRRLGSKirELLVL 645
Cdd:cd18791 1 FPVEVYYLEDIlellgissekeDPDYVDAAVRLILQIHRTEEPGDILVFLPGQEEIERLCELLREELLSPDLG--KLLVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 646 PIYANLPSDMQARIFQPTPPGARKVVVATNIAETSLTIEGIIYVLDPGFCKQKSYNPRTGMESLTVTPCSKASANQRAGR 725
Cdd:cd18791 79 PLHSSLPPEEQQRVFEPPPPGVRKVVLATNIAETSITIPGVVYVIDSGLVKEKVYDPRTGLSSLVTVWISKASAEQRAGR 158
|
170
....*....|...
gi 255982614 726 AGRVAAGKCFRLY 738
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 ... |
399-565 |
1.01e-73 |
|
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: 241.22 E-value: 1.01e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 399 LPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGYTNKGMKIACTQPRRVAAMSVAARVAREMGVKLGNEVG 478
Cdd:cd17980 1 LPVFKLRNHILYLVENYQTIVIVGETGCGKSTQIPQYLAEAGWTAGGRVVGCTQPRRVAAVTVAGRVAEEMGAVLGHEVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 479 YSIRFEDCTSE-RTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVLVASATMDT 557
Cdd:cd17980 81 YCIRFDDCTDPqATRIKFLTDGMLVREMMLDPLLTKYSVIMLDEAHERTLYTDILIGLLKKIQKKRGDLRLIVASATLDA 160
|
....*...
gi 255982614 558 ARFSTFFD 565
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 ... |
399-572 |
2.09e-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: 220.88 E-value: 2.09e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 399 LPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGYTNKGMkIACTQPRRVAAMSVAARVAREMGVKLGNEVG 478
Cdd:cd17984 1 LPIQKQRKKLVQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGFSQHGM-IGVTQPRRVAAISVAQRVAEEMKCTLGSKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 479 YSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDV-----ARFRPELKVLVASA 553
Cdd:cd17984 80 YQVRFDDCSSKETAIKYMTDGCLLRHILADPNLTKYSVIILDEAHERSLTTDILFGLLKKLfqeksPNRKEHLKVVVMSA 159
|
170
....*....|....*....
gi 255982614 554 TMDTARFSTFFDDAPVFRI 572
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 ... |
399-572 |
9.43e-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: 9.43e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 399 LPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGYTNKGMkIACTQPRRVAAMSVAARVAREMGVKLGNEVG 478
Cdd:cd17989 1 LPVSQKRDEIAKAIAENQVVIIAGETGSGKTTQLPKICLELGRGIRGL-IGHTQPRRLAARSVAERIAEELKTELGGAVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 479 YSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVLVASATMDTA 558
Cdd:cd17989 80 YKVRFTDQTSDETCVKLMTDGILLAETQTDRYLRAYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKVIITSATIDAE 159
|
170
....*....|....
gi 255982614 559 RFSTFFDDAPVFRI 572
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 ... |
399-573 |
4.42e-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: 192.18 E-value: 4.42e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 399 LPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGYTNK-----GMkIACTQPRRVAAMSVAARVAREMGVkL 473
Cdd:cd17982 1 LPILAEEQEIMEAINENPVVIICGETGSGKTTQVPQFLYEAGFGSPesdnpGM-IGITQPRRVAAVSMAKRVAEELNV-F 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 474 GNEVGYSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPE-------- 545
Cdd:cd17982 79 GKEVSYQIRYDSTVSENTKIKFMTDGVLLKEIQTDFLLRKYSVIIIDEAHERSVNTDILIGMLSRIVPLRAKlylqdqtv 158
|
170 180 190
....*....|....*....|....*....|
gi 255982614 546 --LKVLVASATMdtaRFSTFFDDAPVFRIP 573
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 ... |
399-572 |
4.78e-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: 188.42 E-value: 4.78e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 399 LPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGYTNkgmkIACTQPRRVAAMSVAARVAREMGVKLGNEVG 478
Cdd:cd17979 1 LPIAQYREKIIELLKTHQVVIVAGDTGCGKSTQVPQYLLAAGFRH----IACTQPRRIACISLAKRVAFESLNQYGSKVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 479 YSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVLVASATMDTA 558
Cdd:cd17979 77 YQIRFERTRTLATKLLFLTEGLLLRQIQRDASLPQYNVLILDEVHERHLHGDFLLGVLRCLLRLRPDLKLILMSATINIE 156
|
170
....*....|....
gi 255982614 559 RFSTFFDDAPVFRI 572
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 ... |
399-572 |
1.67e-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: 1.67e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 399 LPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEgYTNKGM----KIACTQPRRVAAMSVAARVAREMG--VK 472
Cdd:cd17981 1 LPSYGMKQEIINMIDNNQVTVISGETGCGKTTQVTQFILDD-AIERGKgsscRIVCTQPRRISAISVAERVAAERAesCG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 473 LGNEVGYSIRFED-CTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVLVA 551
Cdd:cd17981 80 LGNSTGYQIRLESrKPRKQGSILYCTTGIVLQWLQSDPHLSNVSHLVLDEIHERNLQSDVLMGIVKDLLPFRSDLKVILM 159
|
170 180
....*....|....*....|.
gi 255982614 552 SATMDTARFSTFFDDAPVFRI 572
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 ... |
399-572 |
1.11e-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: 173.47 E-value: 1.11e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 399 LPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFE---EGYTNKGMkIACTQPRRVAAMSVAARVAREMGVKLGN 475
Cdd:cd17977 1 LPVWEAKYEFMESLAHNQIVIVSGDAKTGKSSQIPQWCAEyclSAHYQHGV-VVCTQVHKQTAVWLALRVADEMDVNIGH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 476 EVGYSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVLVASATM 555
Cdd:cd17977 80 EVGYVIPFENCCTNETILRYCTDDMLLREMMSDPLLESYGVIILDDAHERTVSTDVLLGLLKDVLLSRPELKLVIITCPH 159
|
170
....*....|....*..
gi 255982614 556 DTARFSTFFDDAPVFRI 572
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 ... |
399-572 |
2.04e-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: 170.10 E-value: 2.04e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 399 LPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEE----GYTNKGMKIACTQPRRVAAMSVAARVAREMGVKLG 474
Cdd:cd17975 1 LPVFKHRESILETLKRHRVVVVAGETGSGKSTQVPQFLLEDlllnGGTAQKCNIVCTQPRRISAMSLATRVCEELGCESG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 475 ----NEV-GYSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVL 549
Cdd:cd17975 81 pggkNSLcGYQIRMESRTGEATRLLYCTTGVLLRKLQEDGLLSSISHIIVDEVHERSVQSDFLLIILKEILHKRSDLHLI 160
|
170 180
....*....|....*....|...
gi 255982614 550 VASATMDTARFSTFFDDAPVFRI 572
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 ... |
399-572 |
4.51e-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: 168.87 E-value: 4.51e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 399 LPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFE---EGYTNKGMKIACTQPRRVAAMSVAARVAREMGVKLGN 475
Cdd:cd17985 1 LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFILDnslQGPPLPVANIICTQPRRISAISVAERVAQERAERVGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 476 EVGYSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVLVASATM 555
Cdd:cd17985 81 SVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDPTLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQRPDLKVILMSATL 160
|
170
....*....|....*..
gi 255982614 556 DTARFSTFFDDAPVFRI 572
Cdd:cd17985 161 NAELFSDYFNSCPVIHI 177
|
|
| DEXHc_YTHDC2 |
cd17987 |
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) ... |
399-572 |
1.49e-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: 167.31 E-value: 1.49e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 399 LPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGY-TNKGMKIACTQPRRVAAMSVAARVAREMGVKLGNEV 477
Cdd:cd17987 1 LPVFEKQEQIVRIIKENKVVLIVGETGSGKTTQIPQFLLDDCYaNGIPCRIFCTQPRRLAAIAVAERVAAERGEKIGQTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 478 GYSIRFEDCTSERTVLRYMTDGMLLREFLS-EPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVLVASATMD 556
Cdd:cd17987 81 GYQIRLESRVSPKTLLTFCTNGVLLRTLMAgDSALSTVTHVIVDEVHERDRFSDFLLTKLRDILQKHPNLKLILSSAALD 160
|
170
....*....|....*.
gi 255982614 557 TARFSTFFDDAPVFRI 572
Cdd:cd17987 161 VNLFIRYFGSCPVIYI 176
|
|
| DEXHc_DHX30 |
cd17976 |
DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an ... |
399-572 |
2.78e-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: 2.78e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 399 LPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGYTN-KGMK--IACTQPRRVAAMSVAARVAREMGVKLGN 475
Cdd:cd17976 1 LPVDSHKESILSAIEQNPVVVISGDTGCGKTTRIPQFILEDYVLRgRGARcnVVITQPRRISAVSVAQRVAHELGPNLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 476 EVGYSIRFEDCTSERT-VLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVLVASAT 554
Cdd:cd17976 81 NVGYQVRLESRPPPRGgALLFCTVGVLLKKLQSNPRLEGVSHVIVDEVHERDVNTDFLLILLKGVLQLNPELRVVLMSAT 160
|
170
....*....|....*...
gi 255982614 555 MDTARFSTFFDDAPVFRI 572
Cdd:cd17976 161 GDNQRLSRYFGGCPVVRV 178
|
|
| DEXHc_HrpB |
cd17990 |
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ... |
399-571 |
3.87e-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: 166.35 E-value: 3.87e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 399 LPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEgYTNKGMKIACTQPRRVAAMSVAARVAREMGVKLGNEVG 478
Cdd:cd17990 1 LPIAAVLPALRAALDAGGQVVLEAPPGAGKTTRVPLALLAE-LWIAGGKIIVLEPRRVAARAAARRLATLLGEAPGETVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 479 YSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVAR-FRPELKVLVASATMDT 557
Cdd:cd17990 80 YRVRGESRVGRRTRVEVVTEGVLLRRLQRDPELSGVGAVILDEFHERSLDADLALALLLEVQQlLRDDLRLLAMSATLDG 159
|
170
....*....|....
gi 255982614 558 ARFSTFFDDAPVFR 571
Cdd:cd17990 160 DGLAALLPEAPVVE 173
|
|
| DEXHc_DHX9 |
cd17972 |
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ... |
359-572 |
1.19e-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: 164.24 E-value: 1.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 359 EEETIEFVRATQLQGDEEPSAPPTSTQAQQKESIQAVRRSLPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFE 438
Cdd:cd17972 19 DEGPLAFATPEQISMDLKNELMYQREQDHNLQQILQERELLPVKKFREEILEAISNNPVVIIRGATGCGKTTQVPQYILD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 439 E-------GYTNkgmkIACTQPRRVAAMSVAARVAREMGVKLGNEVGYSIRFEDCTSE-RTVLRYMTDGMLLREFlsEPD 510
Cdd:cd17972 99 DfiqndraAECN----IVVTQPRRISAVSVAERVAFERGEEVGKSCGYSVRFESVLPRpHASILFCTVGVLLRKL--EAG 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255982614 511 LASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVLVASATMDTARFSTFFDDAPVFRI 572
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 ... |
399-572 |
2.87e-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: 152.36 E-value: 2.87e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 399 LPVFPFREELLAAI-ANHQVLIIEGETGSGKTTQIPQYLFEEGYTNKGMK--IACTQPRRVAAMSVAARVAREMGVKLGN 475
Cdd:cd17986 1 LPIWAAKFTFLEQLeSPSGIVLVSGEPGSGKSTQVPQWCAEFALSRGFQKgqVTVTQPHPLAARSLALRVADEMDLNLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 476 EVGYSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVLVASATM 555
Cdd:cd17986 81 EVGYSIPQEDCTGPNTILRFCWDRLLLQEMTSTPLLGAWGVVVLDEAQERSVASDSLLGLLKDVRLQRPELRVVVVTSPA 160
|
170
....*....|....*..
gi 255982614 556 DTARFSTFFDDAPVFRI 572
Cdd:cd17986 161 LEPKLRAFWGNPPVVHV 177
|
|
| DEXHc_TDRD9 |
cd17988 |
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ... |
399-564 |
5.52e-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: 146.11 E-value: 5.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 399 LPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGY-TNKGMKIACTQPRRVAAMSVAARVAREMGVKLGNEV 477
Cdd:cd17988 1 LPIYAKREEILSLIEANSVVIIKGATGCGKTTQLPQFILDHYYkRGKYCNIVVTQPRRIAAISIARRVSQEREWTLGSLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 478 GYSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRP-ELKVLVASATMD 556
Cdd:cd17988 81 GYQVGLERPASEETRLIYCTTGVLLQKLINNKTLTEYTHIILDEVHERDQELDFLLLVVRRLLRTNSrHVKIILMSATIS 160
|
....*...
gi 255982614 557 TARFSTFF 564
Cdd:cd17988 161 CKEFADYF 168
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
399-581 |
1.62e-27 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 111.04 E-value: 1.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 399 LPVFPFREELLAAI-ANHQVLIIEGETGSGKTTQIPQYLFEEGYTNKGMKIACTQPRRVAAMSVAARVAREMGVKLGNEV 477
Cdd:smart00487 7 EPLRPYQKEAIEALlSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELKKLGPSLGLKVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 478 GY------SIRFEDCTSERTVLRYMTDGMLLREFLSEP-DLASYSVVMVDEAHERT--LHTDILFGLIKdvaRFRPELKV 548
Cdd:smart00487 87 GLyggdskREQLRKLESGKTDILVTTPGRLLDLLENDKlSLSNVDLVILDEAHRLLdgGFGDQLEKLLK---LLPKNVQL 163
|
170 180 190
....*....|....*....|....*....|....*
gi 255982614 549 LVASATM--DTARFSTFFDDAPVFRIPGRRFPVDI 581
Cdd:smart00487 164 LLLSATPpeEIENLLELFLNDPVFIDVGFTPLEPI 198
|
|
| HA2 |
smart00847 |
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ... |
798-882 |
1.34e-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: 1.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 798 ALGALNHLGELTTSGRKMAELPVDPMLSKMILASEKYSCSEEILTVAAMLSVNNsifYRPKDKVVHADNARVNFFLPGGD 877
Cdd:smart00847 1 ELGALDDDGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGD---PRPKEKREDADAARRRFADPESD 77
|
....*
gi 255982614 878 HLVLL 882
Cdd:smart00847 78 HLTLL 82
|
|
| OB_NTP_bind |
pfam07717 |
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ... |
939-1015 |
4.27e-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: 4.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 939 VRKAITAGYFYHTARLTRSG--YRTVKQQQTVFIHPNSSLF---EQQPRWLLYHELVLTTKEFMRQVLEIESSWLLEVAP 1013
Cdd:pfam07717 1 LRAALAAGLYPNVARRDPKGkgYTTLSDNQRVFIHPSSVLFnekTFPPEWVVYQELVETTKVYIRTVTAISPEWLLLFAP 80
|
..
gi 255982614 1014 HY 1015
Cdd:pfam07717 81 HI 82
|
|
| HA2 |
pfam04408 |
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ... |
792-881 |
5.70e-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: 5.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 792 ALEQLYALGALNHLGELTTSGRKMAELPVDPMLSKMILASEKYSCSEEILTVAAMLSVNNsIFYRP-------------- 857
Cdd:pfam04408 1 ALELLYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRD-PFVQPnfldprsaakaarr 79
|
90 100
....*....|....*....|....*...
gi 255982614 858 ----KDKVVHADNARVNFFlpgGDHLVL 881
Cdd:pfam04408 80 rrraADEKARAKFARLDLE---GDHLTL 104
|
|
| PHA02653 |
PHA02653 |
RNA helicase NPH-II; Provisional |
407-739 |
4.95e-14 |
|
RNA helicase NPH-II; Provisional
Pssm-ID: 177443 [Multi-domain] Cd Length: 675 Bit Score: 76.55 E-value: 4.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 407 ELLAAIANHQVLIIEGETGSGKTTQIPQ------YLFEeGYTNKGmKIACTQPRRVAAMSVAaRVA--REMGVKLGNEVG 478
Cdd:PHA02653 171 KIFEAWISRKPVVLTGGTGVGKTSQVPKlllwfnYLFG-GFDNLD-KIDPNFIERPIVLSLP-RVAlvRLHSITLLKSLG 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 479 Y--------SIRFEDCTSERTVLRYMTDGMLLREF-LSEPDLASYSVVMVDEAHERTLHTDILFG-LIKDVARFRpelKV 548
Cdd:PHA02653 248 FdeidgspiSLKYGSIPDELINTNPKPYGLVFSTHkLTLNKLFDYGTVIIDEVHEHDQIGDIIIAvARKHIDKIR---SL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 549 LVASATM--DTARFSTFFDDAPVFRIPG-RRFPVDIFYTKAP-----EADYLEA---CVVSVLQIHVTQPPGDILVFLtg 617
Cdd:PHA02653 325 FLMTATLedDRDRIKEFFPNPAFVHIPGgTLFPISEVYVKNKynpknKRAYIEEekkNIVTALKKYTPPKGSSGIVFV-- 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 618 qeEIEAACEMLQdrcRRLGSKIRELLVLPIYANLPS--DMQARIFQPTPPgarKVVVATNIAETSLTIEGIIYVLDPGFC 695
Cdd:PHA02653 403 --ASVSQCEEYK---KYLEKRLPIYDFYIIHGKVPNidEILEKVYSSKNP---SIIISTPYLESSVTIRNATHVYDTGRV 474
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 255982614 696 KQKSynPRTGMESLTvtpcSKASANQRAGRAGRVAAGKCFRLYT 739
Cdd:PHA02653 475 YVPE--PFGGKEMFI----SKSMRTQRKGRVGRVSPGTYVYFYD 512
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
626-728 |
4.32e-11 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 59.92 E-value: 4.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 626 EMLQDRCRRLGSKirellVLPIYANLPSDMQARIFQPTPPGARKVVVATNIAETSLTIEGIIYVLDPGFckqksynprtg 705
Cdd:smart00490 1 EELAELLKELGIK-----VARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDL----------- 64
|
90 100
....*....|....*....|...
gi 255982614 706 mesltvtPCSKASANQRAGRAGR 728
Cdd:smart00490 65 -------PWSPASYIQRIGRAGR 80
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
599-729 |
6.99e-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: 6.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 599 VLQIHVTQPPGDILVFLTGQEEIEaaCEMLQDRcrrlgskiRELLVLPIYANLPSDMQARIFQPTPPGARKVVVATNIAE 678
Cdd:pfam00271 6 LLELLKKERGGKVLIFSQTKKTLE--AELLLEK--------EGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAE 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 255982614 679 TSLTIEGIIYVLDpgfckqksYNPrtgmesltvtPCSKASANQRAGRAGRV 729
Cdd:pfam00271 76 RGLDLPDVDLVIN--------YDL----------PWNPASYIQRIGRAGRA 108
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
148-376 |
8.55e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.69 E-value: 8.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 148 TGGSKQQTEKPESEDEWERTERERLQDLEERDAFAERVRQRDKDRTRNVLERSD--KKAYEEAQK--RLKMAEEDRKAmv 223
Cdd:PTZ00121 1447 DEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADeaKKAAEAKKKadEAKKAEEAKKA-- 1524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 224 PELRK--KSRREYLAKREREKLEDLEAELADEEFLFGDVELSRHERQELKYKRRVRDLAREYRAAGEQEKLEATNRYHMP 301
Cdd:PTZ00121 1525 DEAKKaeEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEE 1604
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255982614 302 KETRGQPARAvdlvEEESGAPGEEQRRWEEARLGAASLKfgarDAASQEPKYQLVLEEEETIEFVRATQLQGDEE 376
Cdd:PTZ00121 1605 KKMKAEEAKK----AEEAKIKAEELKKAEEEKKKVEQLK----KKEAEEKKKAEELKKAEEENKIKAAEEAKKAE 1671
|
|
| DEXHc_viral_Ns3 |
cd17931 |
DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional ... |
416-554 |
9.62e-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: 52.55 E-value: 9.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 416 QVLIIEGETGSGKTTQIPQYLFEEGYtNKGMKIACTQPRRVAAMSVAARVaREMGVKLGNEVgysIRFEDctSERTVLRY 495
Cdd:cd17931 2 QLTVLDLHPGAGKTTRVLPQIIREAI-KKRLRTLVLAPTRVVAAEMYEAL-RGLPIRYRTGA---VKEEH--GGNEIVDY 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 255982614 496 MTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFrPELKVLVASAT 554
Cdd:cd17931 75 MCHGTFTCRLLSPKRVPNYNLIIMDEAHFTDPASIAARGYIHTRVEM-GEAAVIFMTAT 132
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
156-407 |
1.58e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.92 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 156 EKPESEDEWERTERERlQDLEERDAFAERVRQRDKDRTRnvleRSDKKAYEEAQKRlkmAEEDRKAmvPELRKKSRREYL 235
Cdd:PTZ00121 1402 EDKKKADELKKAAAAK-KKADEAKKKAEEKKKADEAKKK----AEEAKKADEAKKK---AEEAKKA--EEAKKKAEEAKK 1471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 236 AKREREKLEdlEAELADEefLFGDVELSRHERQELKYKRRVRDLAREYRAAGEQEKL-------EATNRYHMPKETRGQP 308
Cdd:PTZ00121 1472 ADEAKKKAE--EAKKADE--AKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKAdeakkaeEAKKADEAKKAEEKKK 1547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 309 ARAVDLVEE----ESGAPGEEQRRWEEARLGAASLKFGARDAasQEPKYQLVLEEEETIEFVRATQLQGDEEpsappTST 384
Cdd:PTZ00121 1548 ADELKKAEElkkaEEKKKAEEAKKAEEDKNMALRKAEEAKKA--EEARIEEVMKLYEEEKKMKAEEAKKAEE-----AKI 1620
|
250 260
....*....|....*....|...
gi 255982614 385 QAQQKESIQAVRRSLPVFPFREE 407
Cdd:PTZ00121 1621 KAEELKKAEEEKKKVEQLKKKEA 1643
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
156-361 |
1.87e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.53 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 156 EKPESEDEWERTERERLQDLEERDAFAERVRQRDKDRTRnvLERSDKKAYEEAQKrlkmAEEDRKAmvpELRKKSRREYL 235
Cdd:PTZ00121 1596 EVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKK--VEQLKKKEAEEKKK----AEELKKA---EEENKIKAAEE 1666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 236 AKR-EREKLEDLEAELADEEFLFGDVELSRHERQELKYKRRVRDLAREYRAAGEQEKLEatnryhmpkETRGQPARAVDL 314
Cdd:PTZ00121 1667 AKKaEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAE---------EENKIKAEEAKK 1737
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 255982614 315 VEEESGAPGEEQRRWEEARLGAASLKFGARDAASQEPKYQLVLEEEE 361
Cdd:PTZ00121 1738 EAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEE 1784
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
403-556 |
5.93e-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: 5.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 403 PFREELLAAIANHQVLIIEGETGSGKTT--QIPqyLFEE-GYTNKGMKIACTQPRRVAAMSVaARVAREMGVKLGNEVGY 479
Cdd:pfam00270 2 PIQAEAIPAILEGRDVLVQAPTGSGKTLafLLP--ALEAlDKLDNGPQALVLAPTRELAEQI-YEELKKLGKGLGLKVAS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 480 SIRFEDCTSERTVLR-----YMTDGMLLREFLSEPDLASYSVVMVDEAHErtlHTDILFG--LIKDVARFRPELKVLVAS 552
Cdd:pfam00270 79 LLGGDSRKEQLEKLKgpdilVGTPGRLLDLLQERKLLKNLKLLVLDEAHR---LLDMGFGpdLEEILRRLPKKRQILLLS 155
|
....
gi 255982614 553 ATMD 556
Cdd:pfam00270 156 ATLP 159
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
418-554 |
9.90e-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: 9.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 418 LIIEGETGSGKTTQIPQYLFEEGyTNKGMKIACTQPRRVAAMSVAARVAREMgvKLGNEVGYSIRFEDcTSERTVLR--- 494
Cdd:cd00046 4 VLITAPTGSGKTLAALLAALLLL-LKKGKKVLVLVPTKALALQTAERLRELF--GPGIRVAVLVGGSS-AEEREKNKlgd 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255982614 495 ----YMTDGMLLREFLSE--PDLASYSVVMVDEAHERT-LHTDILFGLIKDVARFRPELKVLVASAT 554
Cdd:cd00046 80 adiiIATPDMLLNLLLREdrLFLKDLKLIIVDEAHALLiDSRGALILDLAVRKAGLKNAQVILLSAT 146
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
153-297 |
1.05e-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: 52.82 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 153 QQTEKPESEDEWERTERERLQDLEE-RDAFAERVRQRDKDRTRNVlERSDKKAYEEAQKRLKMAEEDR-KAMVPELRKKS 230
Cdd:pfam17380 418 QKVEMEQIRAEQEEARQREVRRLEEeRAREMERVRLEEQERQQQV-ERLRQQEEERKRKKLELEKEKRdRKRAEEQRRKI 496
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255982614 231 RREYLAKREREKLED------LEAELAD------EEFLFGDVELSRHERQELKYKRRVRDLAReyRAAGEQEKLEATNR 297
Cdd:pfam17380 497 LEKELEERKQAMIEEerkrklLEKEMEErqkaiyEEERRREAEEERRKQQEMEERRRIQEQMR--KATEERSRLEAMER 573
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
154-271 |
1.41e-06 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 52.45 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 154 QTEKPESEDEWERTERERLQDLEERDAFAERVRQRDKDRtrnvlERSDKKAYEEAQKRLKMAEEDRKAMVPELRKKSRRE 233
Cdd:COG1193 524 ERERRELEEEREEAERLREELEKLREELEEKLEELEEEK-----EEILEKAREEAEEILREARKEAEELIRELREAQAEE 598
|
90 100 110
....*....|....*....|....*....|....*...
gi 255982614 234 YLAKREREKLEDLEAELADEEFLFGDVELSRHERQELK 271
Cdd:COG1193 599 EELKEARKKLEELKQELEEKLEKPKKKAKPAKPPEELK 636
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
148-398 |
2.10e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 148 TGGSKQQTEKPESEDEWERTERERLQDLEERdafAERVRQRDKDRTrnvlERSDKKAyEEAQKRlkmAEEDRKAmvPELR 227
Cdd:PTZ00121 1331 ADAAKKKAEEAKKAAEAAKAEAEAAADEAEA---AEEKAEAAEKKK----EEAKKKA-DAAKKK---AEEKKKA--DEAK 1397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 228 KKS-----RREYLAKREREKLEDLEAELADEEflfgdvelsRHERQELKYKRRVRDLAREYRAAGEqEKLEATNRYHMPK 302
Cdd:PTZ00121 1398 KKAeedkkKADELKKAAAAKKKADEAKKKAEE---------KKKADEAKKKAEEAKKADEAKKKAE-EAKKAEEAKKKAE 1467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 303 ETRGQparavdlveEESGAPGEEQRRWEEARLGAASLKFGARDAASQEPKYQLVLEEEETIEFVRATQLQGDEEPSAPPT 382
Cdd:PTZ00121 1468 EAKKA---------DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADE 1538
|
250
....*....|....*.
gi 255982614 383 STQAQQKESIQAVRRS 398
Cdd:PTZ00121 1539 AKKAEEKKKADELKKA 1554
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
142-376 |
1.27e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 142 EKGKKKTGGSKQQTEKPESEDEWERtERERLQDLEERDAFAERVRQRDKDRTRNVLERS-DKKAYEEAQK--------RL 212
Cdd:PTZ00121 1473 DEAKKKAEEAKKADEAKKKAEEAKK-KADEAKKAAEAKKKADEAKKAEEAKKADEAKKAeEAKKADEAKKaeekkkadEL 1551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 213 KMAEEDRKA----MVPELRKKSRREYLAKREREKLEDLEaELADEEFLFGDVELSRHERQELKYKRRVRDLAREYRAAGE 288
Cdd:PTZ00121 1552 KKAEELKKAeekkKAEEAKKAEEDKNMALRKAEEAKKAE-EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEE 1630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 289 QEKLEATNRYHMPKETRgqPARAVDLVEEESGA-PGEEQRRWEEARLGAASLKFGARDAASQEPKYQLVLEEEETIEFVR 367
Cdd:PTZ00121 1631 EKKKVEQLKKKEAEEKK--KAEELKKAEEENKIkAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELK 1708
|
250
....*....|....*...
gi 255982614 368 ---------ATQLQGDEE 376
Cdd:PTZ00121 1709 kkeaeekkkAEELKKAEE 1726
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
153-344 |
3.71e-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: 47.15 E-value: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 153 QQTEKPESEDEWERTERERLQDLEERDAFAERVRQRDKDRTRNVLERSDKKAYEEAQKRlkmAEEDRKAMVPELRKKSRR 232
Cdd:TIGR02794 93 ELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQ---AEEEAKAKAAAEAKKKAE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 233 EYLAKREREKLEDLEAEL-ADEEFLFGDVElsrherqELKYKRRVRDLAREYRAAGEQEKLEAtnryhmpkETRGQPARA 311
Cdd:TIGR02794 170 EAKKKAEAEAKAKAEAEAkAKAEEAKAKAE-------AAKAKAAAEAAAKAEAEAAAAAAAEA--------ERKADEAEL 234
|
170 180 190
....*....|....*....|....*....|...
gi 255982614 312 VDLVEEESGAPGEEQRRWEEARLGAASLKFGAR 344
Cdd:TIGR02794 235 GDIFGLASGSNAEKQGGARGAAAGSEVDKYAAI 267
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
158-349 |
7.45e-05 |
|
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: 46.48 E-value: 7.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 158 PESEDEWERTERERLQDLEERDAFAERVRQRDKDRTRNVLERsdKKAYEEAQKRLKMAEEDR-KAMVPELRKKSRREYLA 236
Cdd:pfam15709 311 SEEERSEEDPSKALLEKREQEKASRDRLRAERAEMRRLEVER--KRREQEEQRRLQQEQLERaEKMREELELEQQRRFEE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 237 KRER-EKLEDLEAELADEE---FLFGDVELSRHERQELKYKRRVRDLAREY------RAAGEQEKL---------EATNR 297
Cdd:pfam15709 389 IRLRkQRLEEERQRQEEEErkqRLQLQAAQERARQQQEEFRRKLQELQRKKqqeeaeRAEAEKQRQkelemqlaeEQKRL 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 255982614 298 YHMPKETRGQPARAVDLVEEESGAPGEEQRRWEE--ARLGAASLKFGARDAASQ 349
Cdd:pfam15709 469 MEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEeaARLALEEAMKQAQEQARQ 522
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
156-397 |
8.77e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 8.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 156 EKPESEDEWERTERERLQdleerdafaERVRQRDKDRTRNVLERSDKKAYEEAQK--RLKMAEEDRKAmvPELRKKsrrE 233
Cdd:PTZ00121 1234 EAKKDAEEAKKAEEERNN---------EEIRKFEEARMAHFARRQAAIKAEEARKadELKKAEEKKKA--DEAKKA---E 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 234 YLAKREREKLEDLEAELADEefLFGDVELSRHERQELKYK---RRVRDLAREYRAAGEQEKLEATNRYHMPKETRGQPAR 310
Cdd:PTZ00121 1300 EKKKADEAKKKAEEAKKADE--AKKKAEEAKKKADAAKKKaeeAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAK 1377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 311 AvdlVEEESGAPGEEQRRWEEARLGAASLKFGA---RDAASQEPKYQLVLEEEETIEFVRATQLQGDEEPSAPPTSTQAQ 387
Cdd:PTZ00121 1378 K---KADAAKKKAEEKKKADEAKKKAEEDKKKAdelKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAE 1454
|
250
....*....|
gi 255982614 388 QKESIQAVRR 397
Cdd:PTZ00121 1455 EAKKAEEAKK 1464
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
153-407 |
1.78e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 153 QQTEKPESEDEWERTERERLQDLEERDAfAERVRQRDKDRTRnvLERSDKKAYEEAQK--RLKMAEEDRKAmVPELRKKS 230
Cdd:PTZ00121 1352 AEAAADEAEAAEEKAEAAEKKKEEAKKK-ADAAKKKAEEKKK--ADEAKKKAEEDKKKadELKKAAAAKKK-ADEAKKKA 1427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 231 ----RREYLAKREREKLEDLEAELADEEflFGDVELSRHERQELKYKRRVRDLAREYRAAGEQEKL--EATNRYHMPKET 304
Cdd:PTZ00121 1428 eekkKADEAKKKAEEAKKADEAKKKAEE--AKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKaeEAKKKADEAKKA 1505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 305 RGQPARAVDLVEEESGAPGEEQRRWEEARLGAASLKFGARDAASQEPKYQLVLEEEEtiefVRATQLQGDEEPSAPPTST 384
Cdd:PTZ00121 1506 AEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEE----KKKAEEAKKAEEDKNMALR 1581
|
250 260
....*....|....*....|...
gi 255982614 385 QAQQKESIQAVRRSLPVFPFREE 407
Cdd:PTZ00121 1582 KAEEAKKAEEARIEEVMKLYEEE 1604
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
153-350 |
2.86e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 153 QQTEKPESEDEWERTERERLQDLEERDAF--------AERVRQRDKDRTRNVLERSD-KKAYEEAQKRlkmAEEDRKAmv 223
Cdd:PTZ00121 1243 KKAEEERNNEEIRKFEEARMAHFARRQAAikaeearkADELKKAEEKKKADEAKKAEeKKKADEAKKK---AEEAKKA-- 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 224 PELRKKSrREYLAKREREKLEDLEAELADEEflfgdvelsrhERQELKYKRRVRDLAREYRAAGEQEKLEATNRYHMPKE 303
Cdd:PTZ00121 1318 DEAKKKA-EEAKKKADAAKKKAEEAKKAAEA-----------AKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKK 1385
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 255982614 304 TRGQPARAVDLVE--EESGAPGEEQRRWEEARLGAASLKFGARDAASQE 350
Cdd:PTZ00121 1386 KAEEKKKADEAKKkaEEDKKKADELKKAAAAKKKADEAKKKAEEKKKAD 1434
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
163-397 |
3.84e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 163 EWERTERERLQDLEERDAFAERVRQRDKDRTRNVLERSDKKAYEEAQKrlkmAEEDRKAMVPELRKKSRREYLAKREREK 242
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARK----AEEARKAEDAKRVEIARKAEDARKAEEA 1169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 243 LEDLEAELADEeflfgdvelsrhERQELKYKRrvrdlAREYRAAGEQEKLEATNRYHMPKET----RGQPARAVDLVE-- 316
Cdd:PTZ00121 1170 RKAEDAKKAEA------------ARKAEEVRK-----AEELRKAEDARKAEAARKAEEERKAeearKAEDAKKAEAVKka 1232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 317 EESGAPGEEQRRWEEARLGAASLKFGARDAASQEPKYQLVLEEEETiefvRATQLQGDEEPSAPPTSTQAQQKESIQAVR 396
Cdd:PTZ00121 1233 EEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEAR----KADELKKAEEKKKADEAKKAEEKKKADEAK 1308
|
.
gi 255982614 397 R 397
Cdd:PTZ00121 1309 K 1309
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
153-331 |
5.57e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 5.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 153 QQTEKPESE----DEWERTERERLQDLEERDAFAERVRQ----RDKDRTRNVLERSDKKAYEEAQKR---LKMAEEDRKA 221
Cdd:PTZ00121 1610 EEAKKAEEAkikaEELKKAEEEKKKVEQLKKKEAEEKKKaeelKKAEEENKIKAAEEAKKAEEDKKKaeeAKKAEEDEKK 1689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 222 MVPELRKKS----RREYLAKREREKLEDLEAELADEEFLFGDVELSRHERQELKYKrrvrdlAREYRAAGEQEKLEATNR 297
Cdd:PTZ00121 1690 AAEALKKEAeeakKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKK------AEEAKKDEEEKKKIAHLK 1763
|
170 180 190
....*....|....*....|....*....|....
gi 255982614 298 YHMPKETRGQPARAVDLVEEESGAPGEEQRRWEE 331
Cdd:PTZ00121 1764 KEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD 1797
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
157-333 |
8.72e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 8.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 157 KPESEDEWERTERERLQDLEErdafAERVRQRDKDRTRNVLERS-DKKAYEEAQK--RLKMAEEDRKAM----VPELRK- 228
Cdd:PTZ00121 1121 KKKAEDARKAEEARKAEDARK----AEEARKAEDAKRVEIARKAeDARKAEEARKaeDAKKAEAARKAEevrkAEELRKa 1196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 229 -KSRREYLAKREREKLEDLEAELADEEFLFGDVELSRHERQELKYKRRvrdlAREYRAAGEQEKLEATNRYHMPKETRGQ 307
Cdd:PTZ00121 1197 eDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKK----AEEERNNEEIRKFEEARMAHFARRQAAI 1272
|
170 180
....*....|....*....|....*.
gi 255982614 308 PARAVDLVEEESGApgEEQRRWEEAR 333
Cdd:PTZ00121 1273 KAEEARKADELKKA--EEKKKADEAK 1296
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
159-358 |
1.02e-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: 43.13 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 159 ESEDEWERTERERLQDLEERDAFAERVRQRDKD------RTRNVLERSDKKAYEEAQKRLKMAEEDRKA----------- 221
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIDKLLAEIEELEREieeerkRRDKLTEEYAELKEELEDLRAELEEVDKEFaetrdelkdyr 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 222 ---------MVPELRKKSRREYLAKREREKLEDLEAELADEEFLFGDVELSRHERQ-ELKYKRRVRDLAREYRAAGEQEK 291
Cdd:TIGR02169 392 ekleklkreINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAlEIKKQEWKLEQLAADLSKYEQEL 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255982614 292 LEATNRYHMPKETRGQPARAVDLVEEESGAPGEEQRRWEearlgAASLKFGA---------RDAASQEPKYQLVLE 358
Cdd:TIGR02169 472 YDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGR-----AVEEVLKAsiqgvhgtvAQLGSVGERYATAIE 542
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
157-328 |
2.11e-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: 41.86 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 157 KPESEDEWERTERERLQDLEERDAFAERVRQRDKDRTRNVLERSDKKAYEEAQKrlkmaeedrkamvpelrkksrreylA 236
Cdd:pfam15709 393 KQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAER-------------------------A 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 237 KREREKLEDLEAELADEEFLFgdVELSRHERqeLKYKRRVRDlareyraAGEQEKLEAtnryhmpKETRGQPARAVDLVE 316
Cdd:pfam15709 448 EAEKQRQKELEMQLAEEQKRL--MEMAEEER--LEYQRQKQE-------AEEKARLEA-------EERRQKEEEAARLAL 509
|
170
....*....|..
gi 255982614 317 EESGAPGEEQRR 328
Cdd:pfam15709 510 EEAMKQAQEQAR 521
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
112-376 |
2.32e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 112 SRAGSSLQKKrkkrKHLRKKREEEEEEEASEKGKKKTGGSKQQTEKPESEDEWERTERERLQDLEErdafAERVRQRDKD 191
Cdd:PTZ00121 1521 AKKADEAKKA----EEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRK----AEEAKKAEEA 1592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 192 RTRNVL---ERSDKKAYEEAQK----RLKmAEEDRKAmvpELRKKSRREYLAKREREKLEDLEAELADEEFLFGDVELSR 264
Cdd:PTZ00121 1593 RIEEVMklyEEEKKMKAEEAKKaeeaKIK-AEELKKA---EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK 1668
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 265 HERQELKYKRRVRDLAREYRAAGEQEKLEATNRYHMpKETRGQPARAVDLVEEESGAPGEEQRRWEEARLGAASLKFGAR 344
Cdd:PTZ00121 1669 KAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKA-EELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAE 1747
|
250 260 270
....*....|....*....|....*....|....*.
gi 255982614 345 DAASQEPK----YQLVLEEEETIEFVRATQLQGDEE 376
Cdd:PTZ00121 1748 EAKKDEEEkkkiAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
199-297 |
2.53e-03 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 42.03 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 199 RSDKKAYEEAqkRLKMAEEDRKAMVPELRKKSRREYLAKREREKLEDLEAELADEEflfgDVELSRHERQELKYKRRVRD 278
Cdd:PTZ00266 429 RVDKDHAERA--RIEKENAHRKALEMKILEKKRIERLEREERERLERERMERIERE----RLERERLERERLERDRLERD 502
|
90 100
....*....|....*....|...
gi 255982614 279 ----LAREYRAAGEQEKLEATNR 297
Cdd:PTZ00266 503 rldrLERERVDRLERDRLEKARR 525
|
|
| SF-CC1 |
TIGR01622 |
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ... |
168-287 |
2.79e-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: 41.44 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 168 ERERLQDLE-------ERDAFAERVRQRDKDRTRNVLERSDKKAYEEAQK-RLKMAEEDRKAMVPELRKKSRREYLAKRE 239
Cdd:TIGR01622 6 ERERLRDSSsagdrdrRRDKGRERSRDRSRDRERSRSRRRDRHRDRDYYRgRERRSRSRRPNRRYRPREKRRRRGDSYRR 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 255982614 240 REKLEDLEAELADEEFLFGDvELSRHER-------QELKYKRRVRDLAREYRAAG 287
Cdd:TIGR01622 86 RRDDRRSRREKPRARDGTPE-PLTEDERdrrtvfvQQLAARARERDLYEFFSKVG 139
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
138-417 |
4.24e-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: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 138 EEASEKGKKKTGGSKQQTEKPE----------SEDEWERTERERLQDLEERDAFAERVRQRDKDRTRNVLERSDKKAYEE 207
Cdd:COG1196 324 ELAELEEELEELEEELEELEEEleeaeeeleeAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 208 AQKRLKMAEEDRKAMVpELRKKSRREYLAKREREKLEDLEAELADEEFLFGDVELSRHERQELKYKRRVRDLAREYRAAG 287
Cdd:COG1196 404 ELEEAEEALLERLERL-EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 288 EQEKLEATNRYHMPK------ETRGQPARAVDLVEEESGAPGE--EQRRWEEARLGAASLkfgARDAASQEPKYQLVLEE 359
Cdd:COG1196 483 LEELAEAAARLLLLLeaeadyEGFLEGVKAALLLAGLRGLAGAvaVLIGVEAAYEAALEA---ALAAALQNIVVEDDEVA 559
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255982614 360 EETIEFV------RATQLQGDEEPSAPPTSTQAQQKESIQAVRRSLPVFPFREELLAAIANHQV 417
Cdd:COG1196 560 AAAIEYLkaakagRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLL 623
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
165-250 |
5.14e-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: 5.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 165 ERTERERLQDLEERDAFAERVRQRDKDRTRNVLERSDKkaYEEAQKRLkmaEEDRKAMVPELRKKSRREYLAKREREKLE 244
Cdd:pfam15346 56 EELEREREAELEEERRKEEEERKKREELERILEENNRK--IEEAQRKE---AEERLAMLEEQRRMKEERQRREKEEEERE 130
|
....*.
gi 255982614 245 DLEAEL 250
Cdd:pfam15346 131 KREQQK 136
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
153-394 |
6.42e-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: 6.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 153 QQTEKPESEDEwERTERERLQDLEERDAFAERVRQRDKDRTRNVLERSD-KKAYEEAQKRLKMAEEDRkamvpeLRKKSR 231
Cdd:COG1196 301 EQDIARLEERR-RELEERLEELEEELAELEEELEELEEELEELEEELEEaEEELEEAEAELAEAEEAL------LEAEAE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 232 REYLAKREREKLEDLEAELADEEflfgdVELSRHERQELKYKRRVRDLAREYRAAGEQEKLEAtnryhmpkETRGQPARA 311
Cdd:COG1196 374 LAEAEEELEELAEELLEALRAAA-----ELAAQLEELEEAEEALLERLERLEEELEELEEALA--------ELEEEEEEE 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 312 VDLVEEESGAPGEEQRRWEEARLGAASLKFGARDAASQEpkyQLVLEEEETIEFVRATQLQGDEEPSAPPTSTQAQQKES 391
Cdd:COG1196 441 EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL---AELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLA 517
|
...
gi 255982614 392 IQA 394
Cdd:COG1196 518 GLR 520
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
174-334 |
8.49e-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: 8.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 174 DLEERDAFAER------VRQRDKDRTRNVLERSDKKAYEEAQKRLKMAEEDRKAMVPELRKKSRREyLAKREREKLEDLE 247
Cdd:COG1196 607 DLREADARYYVlgdtllGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLA-ALLEAEAELEELA 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 248 AELADEEFLFGDVELSRHERQELKYKRRVRDLAREYRAAGEQEKLEATNRYHMPKETRGQPARAVDLVEEESGAPGEEQR 327
Cdd:COG1196 686 ERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEEL 765
|
....*..
gi 255982614 328 RWEEARL 334
Cdd:COG1196 766 ERELERL 772
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
153-294 |
8.65e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 39.79 E-value: 8.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 153 QQTEKPESEDEWERTERERLQDL-EERDAFAERVRQRDKDRtrnVLERSDKKAYEEAQKRL----KMAEEDRKAMVPELR 227
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAEELqQKQAAEQERLKQLEKER---LAAQEQKKQAEEAAKQAalkqKQAEEAAAKAAAAAK 146
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255982614 228 KKsrreylAKREREKLEDLEAELADEEFLFGDVElsRHERQELKYKRRVRDLAREYRAAGEQEKLEA 294
Cdd:PRK09510 147 AK------AEAEAKRAAAAAKKAAAEAKKKAEAE--AAKKAAAEAKKKAEAEAAAKAAAEAKKKAEA 205
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
155-295 |
8.79e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 8.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 155 TEKPESEDEWERTER--ERLQDLEERDAFAERVRQRDKDRTRNVLERSDKKAyEEAQKRLKMAEEDRKAMVPELRKKSRR 232
Cdd:PRK02224 579 SKLAELKERIESLERirTLLAAIADAEDEIERLREKREALAELNDERRERLA-EKRERKRELEAEFDEARIEEAREDKER 657
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 233 --EYLAKRErEKLEDLEAELADEEFLFGDVELSRHERQELKYKR-----RVRDLAREYraaGEQEKLEAT 295
Cdd:PRK02224 658 aeEYLEQVE-EKLDELREERDDLQAEIGAVENELEELEELRERRealenRVEALEALY---DEAEELESM 723
|
|
| U2AF_lg |
TIGR01642 |
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ... |
162-275 |
9.49e-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: 39.88 E-value: 9.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982614 162 DEWERTERERLQD-----LEERDAFAERVRQRDKDRTRNVLERSdkkAYEEAQKRLKMAEEDRKamvpelrKKSRREYLA 236
Cdd:TIGR01642 2 DEEPDREREKSRGrdrdrSSERPRRRSRDRSRFRDRHRRSRERS---YREDSRPRDRRRYDSRS-------PRSLRYSSV 71
|
90 100 110
....*....|....*....|....*....|....*....
gi 255982614 237 KREREKLEDLEAELADEEflfgdvelsRHERQELKYKRR 275
Cdd:TIGR01642 72 RRSRDRPRRRSRSVRSIE---------QHRRRLRDRSPS 101
|
|
| |
