|
Name |
Accession |
Description |
Interval |
E-value |
| HrpA |
COG1643 |
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis]; |
631-1253 |
1.36e-167 |
|
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441249 [Multi-domain] Cd Length: 836 Bit Score: 520.41 E-value: 1.36e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 631 LPIYNLKNDLMKAIEKNNVLIVIGETGSGKTTQIPQYLHEANYTEKGIVGCTQPRRVAAMSIAKRVSEEFGCILGQEVGY 710
Cdd:COG1643 10 LPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGWGAGGRIGMLEPRRLAARAAAERMAEELGEPVGETVGY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 711 SIRFDDCTSNDTIIKYLTDGMLLRETLSDTLLTKYSFIILDEAHERTISTDILFCLLKDVVRK-RADFKLIVTSATLDAE 789
Cdd:COG1643 90 RVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQPAlRPDLKLLVMSATLDAE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 790 KFSTYFFNSPIFTIPGKIFPVEILH--SKEPESDYVEASLITVLNIhLNEHPGDILVFLTGQDEINTACEILHERMkkle 867
Cdd:COG1643 170 RFARLLGDAPVIESSGRTYPVEVRYrpLPADERDLEDAVADAVREA-LAEEPGDILVFLPGEREIRRTAEALRGRL---- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 868 smsPPPLIILPIYSSLPSEMQSVIFEPAPPGCRKCILATNIAEASLTIDGIFFVIDPGFCKIKKYDSKRDMDSLIVAPIS 947
Cdd:COG1643 245 ---PPDTEILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERIS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 948 KANAKQRAGRAGRTGPGKCYRLYTEEAYKNeMSEMSVPEIQRINLGSIVLLLKALGINDFLHFDFMDSPSVETLIHSLEN 1027
Cdd:COG1643 322 QASANQRAGRAGRLAPGICYRLWSEEDFAR-RPAFTDPEILRADLASLILELAAWGLGDPEDLPFLDPPPARAIADARAL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 1028 LYYLGALDDNGYLTKLGKKMANFPMEPNLSKILLTSLNFNCTDDVVTIVSMLSVQNIFyRPQNKAlladkkknkfimpqg 1107
Cdd:COG1643 401 LQELGALDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDPR-RGAAGS--------------- 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 1108 DLITYLNIYNKWKENSfsnywchENFIQSRALKRAQDVRKQMLSIFekynyqvkKSTSKNDATKYVNICKSICSGYFNHV 1187
Cdd:COG1643 465 DLLARLNLWRRLREQQ-------REFLSYLRLREWRDLARQLRRLL--------GEGANEEPADYEAIGLLLALAYPDRI 529
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124802732 1188 CKRDTQQG-YttLLTN-QQVFIHPSSTLFNKNplFVVYHELVLTNKEY-IRDCTIIQPQWLIQLAPNLF 1253
Cdd:COG1643 530 ARRRGEGGrY--LLARgRGAALFPGSPLAKKE--WLVAAELVGGAAEArIRLAAPIDPEWLEELAAHLI 594
|
|
| PRK11131 |
PRK11131 |
ATP-dependent RNA helicase HrpA; Provisional |
631-1252 |
5.08e-136 |
|
ATP-dependent RNA helicase HrpA; Provisional
Pssm-ID: 182986 [Multi-domain] Cd Length: 1294 Bit Score: 448.74 E-value: 5.08e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 631 LPIYNLKNDLMKAIEKNNVLIVIGETGSGKTTQIPQYLHEANYTEKGIVGCTQPRRVAAMSIAKRVSEEFGCILGQEVGY 710
Cdd:PRK11131 73 LPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLELGRGVKGLIGHTQPRRLAARTVANRIAEELETELGGCVGY 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 711 SIRFDDCTSNDTIIKYLTDGMLLRETLSDTLLTKYSFIILDEAHERTISTDILFCLLKDVVRKRADFKLIVTSATLDAEK 790
Cdd:PRK11131 153 KVRFNDQVSDNTMVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPDLKVIITSATIDPER 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 791 FSTYFFNSPIFTIPGKIFPVEILH------SKEPESDYVEASLITVLNIHlNEHPGDILVFLTGQDEINTACEILHER-M 863
Cdd:PRK11131 233 FSRHFNNAPIIEVSGRTYPVEVRYrpiveeADDTERDQLQAIFDAVDELG-REGPGDILIFMSGEREIRDTADALNKLnL 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 864 KKLEsmspppliILPIYSSLPSEMQSVIFEPAppGCRKCILATNIAEASLTIDGIFFVIDPGFCKIKKYDSKRDMDSLIV 943
Cdd:PRK11131 312 RHTE--------ILPLYARLSNSEQNRVFQSH--SGRRIVLATNVAETSLTVPGIKYVIDPGTARISRYSYRTKVQRLPI 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 944 APISKANAKQRAGRAGRTGPGKCYRLYTEEAYkNEMSEMSVPEIQRINLGSIVLLLKALGINDFLHFDFMDSPSVETLIH 1023
Cdd:PRK11131 382 EPISQASANQRKGRCGRVSEGICIRLYSEDDF-LSRPEFTDPEILRTNLASVILQMTALGLGDIAAFPFVEAPDKRNIQD 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 1024 SLENLYYLGALDDNG-----YLTKLGKKMANFPMEPNLSKILLTSLNFNCTDDVVTIVSMLSVQNIFYRPQNKALLADKK 1098
Cdd:PRK11131 461 GVRLLEELGAITTDEqasayKLTPLGRQLAQLPVDPRLARMVLEAQKHGCVREVMIITSALSIQDPRERPMDKQQASDEK 540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 1099 KNKFIMPQGDLITYLNIYNKWKE-------NSFSNYwCHENFIQSRALKRAQDVRKQMLSIFEKYNYQVkkstsKNDATK 1171
Cdd:PRK11131 541 HRRFADKESDFLAFVNLWNYLQEqqkalssNQFRRL-CRTDYLNYLRVREWQDIYTQLRQVVKELGIPV-----NSEPAE 614
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 1172 YVNICKSICSGYFNHVCKRDTQQGYTTLLTNQQVFIHPSSTLFNKNPLFVVYHELVLTNKEYIRDCTIIQPQWLIQLAPN 1251
Cdd:PRK11131 615 YREIHTALLTGLLSHIGMKDAEKQEYTGARNARFSIFPGSGLFKKPPKWVMVAELVETSRLWGRIAARIEPEWIEPLAQH 694
|
.
gi 124802732 1252 L 1252
Cdd:PRK11131 695 L 695
|
|
| DEXHc_DHX8 |
cd17971 |
DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as ... |
626-804 |
5.84e-105 |
|
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: 329.06 E-value: 5.84e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 626 EQRSKLPIYNLKNDLMKAIEKNNVLIVIGETGSGKTTQIPQYLHEANYTEKGIVGCTQPRRVAAMSIAKRVSEEFGCILG 705
Cdd:cd17971 1 EQRESLPIYKLKEQLIQAVHDNQILVVIGETGSGKTTQITQYLAEAGYTSRGKIGCTQPRRVAAMSVAKRVAEEFGCCLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 706 QEVGYSIRFDDCTSNDTIIKYLTDGMLLRETLSDTLLTKYSFIILDEAHERTISTDILFCLLKDVVRKRADFKLIVTSAT 785
Cdd:cd17971 81 QEVGYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLSQYSVIMLDEAHERTIHTDVLFGLLKKTVQKRPDLKLIVTSAT 160
|
170
....*....|....*....
gi 124802732 786 LDAEKFSTYFFNSPIFTIP 804
Cdd:cd17971 161 LDAVKFSQYFYEAPIFTIP 179
|
|
| DEAH_box_HrpB |
TIGR01970 |
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ... |
631-1065 |
3.70e-92 |
|
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: 316.32 E-value: 3.70e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 631 LPIYNLKNDLMKAIEKNNVLIVIGETGSGKTTQIP-QYLHEANYTEKGIVgcTQPRRVAAMSIAKRVSEEFGCILGQEVG 709
Cdd:TIGR01970 1 LPIHAVLPALRDALAAHPQVVLEAPPGAGKSTAVPlALLDAPGIGGKIIM--LEPRRLAARSAAQRLASQLGEAVGQTVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 710 YSIRFDDCTSNDTIIKYLTDGMLLRETLSDTLLTKYSFIILDEAHERTISTDILFCLLKDVVRK-RADFKLIVTSATLDA 788
Cdd:TIGR01970 79 YRVRGENKVSRRTRLEVVTEGILTRMIQDDPELDGVGALIFDEFHERSLDADLGLALALDVQSSlREDLKILAMSATLDG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 789 EKFSTYFFNSPIFTIPGKIFPVEILHSKEPESDYVEASLITVLNIHLNEHPGDILVFLTGQDEINTACEILHERMKkles 868
Cdd:TIGR01970 159 ERLSSLLPDAPVVESEGRSFPVEIRYLPLRGDQRLEDAVSRAVEHALASETGSILVFLPGQAEIRRVQEQLAERLD---- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 869 mspPPLIILPIYSSLPSEMQSVIFEPAPPGCRKCILATNIAEASLTIDGIFFVIDPGFCKIKKYDSKRDMDSLIVAPISK 948
Cdd:TIGR01970 235 ---SDVLICPLYGELSLAAQDRAIKPDPQGRRKVVLATNIAETSLTIEGIRVVIDSGLARVARFDPKTGITRLETVRISQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 949 ANAKQRAGRAGRTGPGKCYRLYTEEAYKnEMSEMSVPEIQRINLGSIVLLLKALGINDFLHFDFMDSPSVETLIHSLENL 1028
Cdd:TIGR01970 312 ASATQRAGRAGRLEPGVCYRLWSEEQHQ-RLPAQDEPEILQADLSGLALELAQWGAKDPSDLRWLDAPPSVALAAARQLL 390
|
410 420 430
....*....|....*....|....*....|....*..
gi 124802732 1029 YYLGALDDNGYLTKLGKKMANFPMEPNLSKILLTSLN 1065
Cdd:TIGR01970 391 QRLGALDAQGRLTAHGKAMAALGCHPRLAAMLLSAHS 427
|
|
| S1_DHX8_helicase |
cd05684 |
S1_DHX8_helicase: The N-terminal S1 domain of human ATP-dependent RNA helicase DHX8, a DEAH ... |
329-408 |
2.40e-32 |
|
S1_DHX8_helicase: The N-terminal S1 domain of human ATP-dependent RNA helicase DHX8, a DEAH (Asp-Glu-Ala-His) box polypeptide. The DEAH-box RNA helicases are thought to play key roles in pre-mRNA splicing and DHX8 facilitates nuclear export of spliced mRNA by releasing the RNA from the spliceosome. DHX8 is also known as HRH1 (human RNA helicase 1) in Homo sapiens and PRP22 in Saccharomyces cerevisiae.
Pssm-ID: 240189 [Multi-domain] Cd Length: 79 Bit Score: 120.42 E-value: 2.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 329 NNIFNGTINKITDFGLFVSFKTNEGYKEGLVHATDILPNRkRVVNMNEKFKRNMKVKVKVKGIFNQKISLNMSEVDQKTG 408
Cdd:cd05684 1 GKIYKGKVTSIMDFGCFVQLEGLKGRKEGLVHISQLSFEG-RVANPSDVVKRGQKVKVKVISIQNGKISLSMKDVDQDTG 79
|
|
| HA2 |
pfam04408 |
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ... |
1024-1112 |
5.61e-29 |
|
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: 111.95 E-value: 5.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 1024 SLENLYYLGALDDNGYLTKLGKKMANFPMEPNLSKILLTSLNFNCTDDVVTIVSMLSVQNIFYRPQN------------- 1090
Cdd:pfam04408 1 ALELLYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPNFldprsaakaarrr 80
|
90 100
....*....|....*....|....
gi 124802732 1091 KALLADKKKNKFIMPQ--GDLITY 1112
Cdd:pfam04408 81 RRAADEKARAKFARLDleGDHLTL 104
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
640-812 |
4.50e-27 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 109.89 E-value: 4.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 640 LMKAIEKNNVLIVIGETGSGKTTQIPQYLHEANYTEKGI-VGCTQPRRVAAMSIAKRVSEEFGCILGQEVGY------SI 712
Cdd:smart00487 17 IEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGrVLVLVPTRELAEQWAEELKKLGPSLGLKVVGLyggdskRE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 713 RFDDCTSNDTIIKYLTDGMLLRETLSDTL-LTKYSFIILDEAHERTIS--TDILFCLLKdvvRKRADFKLIVTSATL--D 787
Cdd:smart00487 97 QLRKLESGKTDILVTTPGRLLDLLENDKLsLSNVDLVILDEAHRLLDGgfGDQLEKLLK---LLPKNVQLLLLSATPpeE 173
|
170 180
....*....|....*....|....*
gi 124802732 788 AEKFSTYFFNSPIFTIPGKIFPVEI 812
Cdd:smart00487 174 IENLLELFLNDPVFIDVGFTPLEPI 198
|
|
| PRK11824 |
PRK11824 |
polynucleotide phosphorylase/polyadenylase; Provisional |
331-404 |
1.97e-10 |
|
polynucleotide phosphorylase/polyadenylase; Provisional
Pssm-ID: 236995 [Multi-domain] Cd Length: 693 Bit Score: 65.07 E-value: 1.97e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124802732 331 IFNGTINKITDFGLFVSFKtneGYKEGLVHATDIlpNRKRVVNMNEKFKRNMKVKVKVKGIFNQ-KISLNMSEVD 404
Cdd:PRK11824 624 IYEGKVVRIVDFGAFVEIL---PGKDGLVHISEI--ADERVEKVEDVLKEGDEVKVKVLEIDKRgRIRLSRKAVL 693
|
|
| S1 |
smart00316 |
Ribosomal protein S1-like RNA-binding domain; |
327-401 |
6.54e-08 |
|
Ribosomal protein S1-like RNA-binding domain;
Pssm-ID: 197648 [Multi-domain] Cd Length: 72 Bit Score: 50.68 E-value: 6.54e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124802732 327 KLNNIFNGTINKITDFGLFVSFktnEGYKEGLVHATDIlpNRKRVVNMNEKFKRNMKVKVKVKGIFNQKISLNMS 401
Cdd:smart00316 1 EVGDVVEGTVTEITPGGAFVDL---GNGVEGLIPISEL--SDKRVKDPEEVLKVGDEVKVKVLSVDEEKGRIILS 70
|
|
| YabR |
COG1098 |
Predicted RNA-binding protein, contains ribosomal protein S1 (RPS1) domain [General function ... |
324-406 |
2.11e-07 |
|
Predicted RNA-binding protein, contains ribosomal protein S1 (RPS1) domain [General function prediction only];
Pssm-ID: 440715 [Multi-domain] Cd Length: 130 Bit Score: 50.95 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 324 MALKLNNIFNGTINKITDFGLFVSFktnEGYKEGLVHATDIlpNRKRVVNMNEKFKRNMKVKVKVKGI-FNQKISLNMSE 402
Cdd:COG1098 1 MSIEVGDIVEGKVTGITPFGAFVEL---PEGTTGLVHISEI--ADGYVKDINDYLKVGDEVKVKVLSIdEDGKISLSIKQ 75
|
....
gi 124802732 403 VDQK 406
Cdd:COG1098 76 AEEK 79
|
|
| GH2-like_DHX8 |
cd21691 |
GIPC-homology 2 (GH2)-like domain found in DEAH box protein 8 (DHX8) and similar proteins; ... |
4-54 |
1.03e-06 |
|
GIPC-homology 2 (GH2)-like domain found in DEAH box protein 8 (DHX8) and similar proteins; DHX8 (a human homolog of yeast Prp22), also called RNA helicase HRH1, is an ATP-dependent RNA helicase involved in pre-mRNA splicing as a component of the spliceosome. It facilitates nuclear export of spliced mRNA by releasing the RNA from the spliceosome. This model corresponds to the GH2-like domain that shows high sequence similarity with the GH2 domain found in GIPC (GAIP C-terminus-interacting protein) family of proteins, which mediate endocytosis by tethering cargo proteins to the motor myosin VI.
Pssm-ID: 409668 Cd Length: 68 Bit Score: 47.15 E-value: 1.03e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 124802732 4 LSKINLIRKVNEELYNSIGVEDDNLSEFLIYLCEKSTSLEEFCKDVFENGG 54
Cdd:cd21691 1 LEYLSLVSKVCTELENHLGISDKDLAEFIIDLAEKSKTLDEFKKALKENGA 51
|
|
| rpsA |
TIGR00717 |
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found ... |
334-405 |
9.92e-04 |
|
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found in most bacterial genomes in a single copy, but is not present in the Mycoplasmas. It is heterogeneous with respect to the number of repeats of the S1 RNA binding domain described by pfam00575: six repeats in E. coli and most other bacteria, four in Bacillus subtilis and some other species. rpsA is an essential gene in E. coli but not in B. subtilis. It is associated with the cytidylate kinase gene cmk in many species, and fused to it in Treponema pallidum. RpsA is proposed (Medline:97323001) to assist in mRNA degradation. This model provides trusted hits to most long form (6 repeat) examples of RpsA. Among homologs with only four repeats are some to which other (perhaps secondary) functions have been assigned. [Protein synthesis, Ribosomal proteins: synthesis and modification]
Pssm-ID: 273232 [Multi-domain] Cd Length: 516 Bit Score: 43.18 E-value: 9.92e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124802732 334 GTINKITDFGLFVsfktNEGYKEGLVHATDIlpNRKRVVNMNEKFKRNMKVKVKVKGIFNQK--ISLNMSEVDQ 405
Cdd:TIGR00717 193 GVVKNITDFGAFV----DLGGVDGLLHITDM--SWKRVKHPSEYVKVGQEVKVKVIKFDKEKgrISLSLKQLGE 260
|
|
| S1 |
pfam00575 |
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ... |
326-400 |
2.06e-03 |
|
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is structurally similar to cold shock protein which binds nucleic acids. The S1 domain has an OB-fold structure.
Pssm-ID: 425760 [Multi-domain] Cd Length: 72 Bit Score: 38.04 E-value: 2.06e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124802732 326 LKLNNIFNGTINKITDFGLFVSFktnEGYKEGLVHATDIlpNRKRVVNMNEKFKRNMKVKVKVKGIFNQK--ISLNM 400
Cdd:pfam00575 1 PEKGDVVEGEVTRVTKGGAFVDL---GNGVEGFIPISEL--SDDHVEDPDEVIKVGDEVKVKVLKVDKDRrrIILSI 72
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HrpA |
COG1643 |
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis]; |
631-1253 |
1.36e-167 |
|
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441249 [Multi-domain] Cd Length: 836 Bit Score: 520.41 E-value: 1.36e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 631 LPIYNLKNDLMKAIEKNNVLIVIGETGSGKTTQIPQYLHEANYTEKGIVGCTQPRRVAAMSIAKRVSEEFGCILGQEVGY 710
Cdd:COG1643 10 LPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGWGAGGRIGMLEPRRLAARAAAERMAEELGEPVGETVGY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 711 SIRFDDCTSNDTIIKYLTDGMLLRETLSDTLLTKYSFIILDEAHERTISTDILFCLLKDVVRK-RADFKLIVTSATLDAE 789
Cdd:COG1643 90 RVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQPAlRPDLKLLVMSATLDAE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 790 KFSTYFFNSPIFTIPGKIFPVEILH--SKEPESDYVEASLITVLNIhLNEHPGDILVFLTGQDEINTACEILHERMkkle 867
Cdd:COG1643 170 RFARLLGDAPVIESSGRTYPVEVRYrpLPADERDLEDAVADAVREA-LAEEPGDILVFLPGEREIRRTAEALRGRL---- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 868 smsPPPLIILPIYSSLPSEMQSVIFEPAPPGCRKCILATNIAEASLTIDGIFFVIDPGFCKIKKYDSKRDMDSLIVAPIS 947
Cdd:COG1643 245 ---PPDTEILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERIS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 948 KANAKQRAGRAGRTGPGKCYRLYTEEAYKNeMSEMSVPEIQRINLGSIVLLLKALGINDFLHFDFMDSPSVETLIHSLEN 1027
Cdd:COG1643 322 QASANQRAGRAGRLAPGICYRLWSEEDFAR-RPAFTDPEILRADLASLILELAAWGLGDPEDLPFLDPPPARAIADARAL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 1028 LYYLGALDDNGYLTKLGKKMANFPMEPNLSKILLTSLNFNCTDDVVTIVSMLSVQNIFyRPQNKAlladkkknkfimpqg 1107
Cdd:COG1643 401 LQELGALDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDPR-RGAAGS--------------- 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 1108 DLITYLNIYNKWKENSfsnywchENFIQSRALKRAQDVRKQMLSIFekynyqvkKSTSKNDATKYVNICKSICSGYFNHV 1187
Cdd:COG1643 465 DLLARLNLWRRLREQQ-------REFLSYLRLREWRDLARQLRRLL--------GEGANEEPADYEAIGLLLALAYPDRI 529
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124802732 1188 CKRDTQQG-YttLLTN-QQVFIHPSSTLFNKNplFVVYHELVLTNKEY-IRDCTIIQPQWLIQLAPNLF 1253
Cdd:COG1643 530 ARRRGEGGrY--LLARgRGAALFPGSPLAKKE--WLVAAELVGGAAEArIRLAAPIDPEWLEELAAHLI 594
|
|
| PRK11131 |
PRK11131 |
ATP-dependent RNA helicase HrpA; Provisional |
631-1252 |
5.08e-136 |
|
ATP-dependent RNA helicase HrpA; Provisional
Pssm-ID: 182986 [Multi-domain] Cd Length: 1294 Bit Score: 448.74 E-value: 5.08e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 631 LPIYNLKNDLMKAIEKNNVLIVIGETGSGKTTQIPQYLHEANYTEKGIVGCTQPRRVAAMSIAKRVSEEFGCILGQEVGY 710
Cdd:PRK11131 73 LPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLELGRGVKGLIGHTQPRRLAARTVANRIAEELETELGGCVGY 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 711 SIRFDDCTSNDTIIKYLTDGMLLRETLSDTLLTKYSFIILDEAHERTISTDILFCLLKDVVRKRADFKLIVTSATLDAEK 790
Cdd:PRK11131 153 KVRFNDQVSDNTMVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPDLKVIITSATIDPER 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 791 FSTYFFNSPIFTIPGKIFPVEILH------SKEPESDYVEASLITVLNIHlNEHPGDILVFLTGQDEINTACEILHER-M 863
Cdd:PRK11131 233 FSRHFNNAPIIEVSGRTYPVEVRYrpiveeADDTERDQLQAIFDAVDELG-REGPGDILIFMSGEREIRDTADALNKLnL 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 864 KKLEsmspppliILPIYSSLPSEMQSVIFEPAppGCRKCILATNIAEASLTIDGIFFVIDPGFCKIKKYDSKRDMDSLIV 943
Cdd:PRK11131 312 RHTE--------ILPLYARLSNSEQNRVFQSH--SGRRIVLATNVAETSLTVPGIKYVIDPGTARISRYSYRTKVQRLPI 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 944 APISKANAKQRAGRAGRTGPGKCYRLYTEEAYkNEMSEMSVPEIQRINLGSIVLLLKALGINDFLHFDFMDSPSVETLIH 1023
Cdd:PRK11131 382 EPISQASANQRKGRCGRVSEGICIRLYSEDDF-LSRPEFTDPEILRTNLASVILQMTALGLGDIAAFPFVEAPDKRNIQD 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 1024 SLENLYYLGALDDNG-----YLTKLGKKMANFPMEPNLSKILLTSLNFNCTDDVVTIVSMLSVQNIFYRPQNKALLADKK 1098
Cdd:PRK11131 461 GVRLLEELGAITTDEqasayKLTPLGRQLAQLPVDPRLARMVLEAQKHGCVREVMIITSALSIQDPRERPMDKQQASDEK 540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 1099 KNKFIMPQGDLITYLNIYNKWKE-------NSFSNYwCHENFIQSRALKRAQDVRKQMLSIFEKYNYQVkkstsKNDATK 1171
Cdd:PRK11131 541 HRRFADKESDFLAFVNLWNYLQEqqkalssNQFRRL-CRTDYLNYLRVREWQDIYTQLRQVVKELGIPV-----NSEPAE 614
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 1172 YVNICKSICSGYFNHVCKRDTQQGYTTLLTNQQVFIHPSSTLFNKNPLFVVYHELVLTNKEYIRDCTIIQPQWLIQLAPN 1251
Cdd:PRK11131 615 YREIHTALLTGLLSHIGMKDAEKQEYTGARNARFSIFPGSGLFKKPPKWVMVAELVETSRLWGRIAARIEPEWIEPLAQH 694
|
.
gi 124802732 1252 L 1252
Cdd:PRK11131 695 L 695
|
|
| DEXHc_DHX8 |
cd17971 |
DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as ... |
626-804 |
5.84e-105 |
|
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: 329.06 E-value: 5.84e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 626 EQRSKLPIYNLKNDLMKAIEKNNVLIVIGETGSGKTTQIPQYLHEANYTEKGIVGCTQPRRVAAMSIAKRVSEEFGCILG 705
Cdd:cd17971 1 EQRESLPIYKLKEQLIQAVHDNQILVVIGETGSGKTTQITQYLAEAGYTSRGKIGCTQPRRVAAMSVAKRVAEEFGCCLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 706 QEVGYSIRFDDCTSNDTIIKYLTDGMLLRETLSDTLLTKYSFIILDEAHERTISTDILFCLLKDVVRKRADFKLIVTSAT 785
Cdd:cd17971 81 QEVGYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLSQYSVIMLDEAHERTIHTDVLFGLLKKTVQKRPDLKLIVTSAT 160
|
170
....*....|....*....
gi 124802732 786 LDAEKFSTYFFNSPIFTIP 804
Cdd:cd17971 161 LDAVKFSQYFYEAPIFTIP 179
|
|
| DEAH_box_HrpB |
TIGR01970 |
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ... |
631-1065 |
3.70e-92 |
|
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: 316.32 E-value: 3.70e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 631 LPIYNLKNDLMKAIEKNNVLIVIGETGSGKTTQIP-QYLHEANYTEKGIVgcTQPRRVAAMSIAKRVSEEFGCILGQEVG 709
Cdd:TIGR01970 1 LPIHAVLPALRDALAAHPQVVLEAPPGAGKSTAVPlALLDAPGIGGKIIM--LEPRRLAARSAAQRLASQLGEAVGQTVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 710 YSIRFDDCTSNDTIIKYLTDGMLLRETLSDTLLTKYSFIILDEAHERTISTDILFCLLKDVVRK-RADFKLIVTSATLDA 788
Cdd:TIGR01970 79 YRVRGENKVSRRTRLEVVTEGILTRMIQDDPELDGVGALIFDEFHERSLDADLGLALALDVQSSlREDLKILAMSATLDG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 789 EKFSTYFFNSPIFTIPGKIFPVEILHSKEPESDYVEASLITVLNIHLNEHPGDILVFLTGQDEINTACEILHERMKkles 868
Cdd:TIGR01970 159 ERLSSLLPDAPVVESEGRSFPVEIRYLPLRGDQRLEDAVSRAVEHALASETGSILVFLPGQAEIRRVQEQLAERLD---- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 869 mspPPLIILPIYSSLPSEMQSVIFEPAPPGCRKCILATNIAEASLTIDGIFFVIDPGFCKIKKYDSKRDMDSLIVAPISK 948
Cdd:TIGR01970 235 ---SDVLICPLYGELSLAAQDRAIKPDPQGRRKVVLATNIAETSLTIEGIRVVIDSGLARVARFDPKTGITRLETVRISQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 949 ANAKQRAGRAGRTGPGKCYRLYTEEAYKnEMSEMSVPEIQRINLGSIVLLLKALGINDFLHFDFMDSPSVETLIHSLENL 1028
Cdd:TIGR01970 312 ASATQRAGRAGRLEPGVCYRLWSEEQHQ-RLPAQDEPEILQADLSGLALELAQWGAKDPSDLRWLDAPPSVALAAARQLL 390
|
410 420 430
....*....|....*....|....*....|....*..
gi 124802732 1029 YYLGALDDNGYLTKLGKKMANFPMEPNLSKILLTSLN 1065
Cdd:TIGR01970 391 QRLGALDAQGRLTAHGKAMAALGCHPRLAAMLLSAHS 427
|
|
| DEXHc_DHX38 |
cd17983 |
DEXH-box helicase domain of DEAH-box helicase 38; DEAH-box helicase 38 (DHX38, also known as ... |
631-803 |
6.39e-90 |
|
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: 287.82 E-value: 6.39e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 631 LPIYNLKNDLMKAIEKNNVLIVIGETGSGKTTQIPQYLHEANYTEKGIVGCTQPRRVAAMSIAKRVSEEFGCILGQEVGY 710
Cdd:cd17983 1 LPIFAVRQELLNVIRDNNVVIVVGETGSGKTTQLTQYLHEDGYTDYGMIGCTQPRRVAAMSVAKRVSEEMGVELGEEVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 711 SIRFDDCTSNDTIIKYLTDGMLLRETLSDTLLTKYSFIILDEAHERTISTDILFCLLKDVVRKRADFKLIVTSATLDAEK 790
Cdd:cd17983 81 AIRFEDCTSENTVIKYMTDGILLRESLRDPDLDKYSAIIMDEAHERSLNTDVLFGLLREVVARRRDLKLIVTSATMDADK 160
|
170
....*....|...
gi 124802732 791 FSTYFFNSPIFTI 803
Cdd:cd17983 161 FADFFGNVPIFTI 173
|
|
| DEXHc_RHA-like |
cd17917 |
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ... |
647-803 |
7.48e-89 |
|
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: 284.35 E-value: 7.48e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 647 NNVLIVIGETGSGKTTQIPQYLHEANYT--EKGIVGCTQPRRVAAMSIAKRVSEEFGCILGQEVGYSIRFDDCTSNDTII 724
Cdd:cd17917 1 NQVVVIVGETGSGKTTQVPQFLLEDGLAkgGKGRIVCTQPRRIAAISVAERVAEERGEKLGEEVGYQIRFESKTSSKTRI 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124802732 725 KYLTDGMLLRETLSDTLLTKYSFIILDEAHERTISTDILFCLLKDVVRKRADFKLIVTSATLDAEKFSTYFFNSPIFTI 803
Cdd:cd17917 81 KFCTDGILLRELLSDPLLSGYSHVILDEAHERSLDTDFLLGLLKDLLRKRPDLKVILMSATLDAEKFSSYFGGAPVIHI 159
|
|
| DEXHc_DHX15 |
cd17973 |
DEXH-box helicase domain of DEAH-box helicase 15; DEAH-box helicase 15 (DHX15) is a pre-mRNA ... |
624-803 |
9.16e-88 |
|
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: 282.38 E-value: 9.16e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 624 INEQRSKLPIYNLKNDLMKAIEKNNVLIVIGETGSGKTTQIPQYLHEANYTE--KGIVGCTQPRRVAAMSIAKRVSEEFG 701
Cdd:cd17973 6 ILEKRRELPVWEQKEDFLKLLKNNQILVLVGETGSGKTTQIPQFVLDDELPHqpKKLVACTQPRRVAAMSVAQRVAEEMD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 702 CILGQEVGYSIRFDDCTSNDTIIKYLTDGMLLRETLSDTLLTKYSFIILDEAHERTISTDILFCLLKDVVRKRADFKLIV 781
Cdd:cd17973 86 VKLGEEVGYSIRFEDCSSAKTILKYMTDGMLLREAMSDPLLSRYSVIILDEAHERTLATDILMGLLKEVVRRRPDLKLIV 165
|
170 180
....*....|....*....|..
gi 124802732 782 TSATLDAEKFSTYFFNSPIFTI 803
Cdd:cd17973 166 MSATLDAGKFQKYFDNAPLLKV 187
|
|
| DEXHc_DHX16 |
cd17974 |
DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably ... |
631-803 |
5.48e-87 |
|
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: 279.77 E-value: 5.48e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 631 LPIYNLKNDLMKAIEKNNVLIVIGETGSGKTTQIPQYLHEANYTEKGI-VGCTQPRRVAAMSIAKRVSEEFGCILGQEVG 709
Cdd:cd17974 1 LPVYPYRDDLLAAVKEHQVLIIVGETGSGKTTQIPQYLHEAGYTKGGGkIGCTQPRRVAAMSVAARVAEEMGVKLGNEVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 710 YSIRFDDCTSNDTIIKYLTDGMLLRETLSDTLLTKYSFIILDEAHERTISTDILFCLLKDVVRKRADFKLIVTSATLDAE 789
Cdd:cd17974 81 YSIRFEDCTSEKTVLKYMTDGMLLREFLTEPDLASYSVMIIDEAHERTLHTDILFGLVKDIARFRPDLKLLISSATMDAE 160
|
170
....*....|....
gi 124802732 790 KFSTYFFNSPIFTI 803
Cdd:cd17974 161 KFSAFFDDAPIFRI 174
|
|
| DEXHc_DHX33 |
cd17978 |
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA ... |
631-803 |
6.76e-87 |
|
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: 279.62 E-value: 6.76e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 631 LPIYNLKNDLMKAIEKNNVLIVIGETGSGKTTQIPQYLHEANYTEKGIVGCTQPRRVAAMSIAKRVSEEFGCILGQEVGY 710
Cdd:cd17978 1 LPIYSARKRLLEELRKHDTVIIIGETGSGKTTQIPQYLYEAGFARGGMIGITQPRRVAAVSVAKRVAEEMGVELGQLVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 711 SIRFDDCTSNDTIIKYLTDGMLLRETLSDTLLTKYSFIILDEAHERTISTDILFCLLKDVVRKR-----ADFKLIVTSAT 785
Cdd:cd17978 81 SVRFDDVTSEETRIKYMTDGMLLREAIGDPLLSKYSVIILDEAHERTVHTDVLFGLVKSAQRRRkeqklSPLKVIIMSAT 160
|
170
....*....|....*...
gi 124802732 786 LDAEKFSTYFFNSPIFTI 803
Cdd:cd17978 161 LDADLFSEYFNGAPVLYI 178
|
|
| SF2_C_RHA |
cd18791 |
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ... |
808-970 |
5.94e-81 |
|
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: 262.85 E-value: 5.94e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 808 FPVEILHSKEPES-----------DYVEASLITVLNIHLNEHPGDILVFLTGQDEINTACEILherMKKLESMSPPPLII 876
Cdd:cd18791 1 FPVEVYYLEDILEllgissekedpDYVDAAVRLILQIHRTEEPGDILVFLPGQEEIERLCELL---REELLSPDLGKLLV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 877 LPIYSSLPSEMQSVIFEPAPPGCRKCILATNIAEASLTIDGIFFVIDPGFCKIKKYDSKRDMDSLIVAPISKANAKQRAG 956
Cdd:cd18791 78 LPLHSSLPPEEQQRVFEPPPPGVRKVVLATNIAETSITIPGVVYVIDSGLVKEKVYDPRTGLSSLVTVWISKASAEQRAG 157
|
170
....*....|....
gi 124802732 957 RAGRTGPGKCYRLY 970
Cdd:cd18791 158 RAGRTRPGKCYRLY 171
|
|
| PRK11664 |
PRK11664 |
ATP-dependent RNA helicase HrpB; Provisional |
629-1061 |
8.30e-79 |
|
ATP-dependent RNA helicase HrpB; Provisional
Pssm-ID: 236950 [Multi-domain] Cd Length: 812 Bit Score: 277.96 E-value: 8.30e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 629 SKLPIYNLKNDLMKAIEKNNVLIVIGETGSGKTTQIP-QYLHEANYTEKGIVgcTQPRRVAAMSIAKRVSEEFGCILGQE 707
Cdd:PRK11664 2 SSLPVAAVLPELLTALKTAPQVLLKAPTGAGKSTWLPlQLLQHGGINGKIIM--LEPRRLAARNVAQRLAEQLGEKPGET 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 708 VGYSIRFDDCTSNDTIIKYLTDGMLLRETLSDTLLTKYSFIILDEAHERTISTDILFCLLKDVVRK-RADFKLIVTSATL 786
Cdd:PRK11664 80 VGYRMRAESKVGPNTRLEVVTEGILTRMIQRDPELSGVGLVILDEFHERSLQADLALALLLDVQQGlRDDLKLLIMSATL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 787 DAEKFSTYFFNSPIFTIPGKIFPVEI----LHSKEPesdYVEASLITVLNIhLNEHPGDILVFLTGQDEINTACEILHER 862
Cdd:PRK11664 160 DNDRLQQLLPDAPVIVSEGRSFPVERryqpLPAHQR---FDEAVARATAEL-LRQESGSLLLFLPGVGEIQRVQEQLASR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 863 MkklesmsPPPLIILPIYSSLP-SEMQSVIfEPAPPGCRKCILATNIAEASLTIDGIFFVIDPGFCKIKKYDSKRDMDSL 941
Cdd:PRK11664 236 V-------ASDVLLCPLYGALSlAEQQKAI-LPAPAGRRKVVLATNIAETSLTIEGIRLVVDSGLERVARFDPKTGLTRL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 942 IVAPISKANAKQRAGRAGRTGPGKCYRLYTEEAYKnEMSEMSVPEIQRINLGSIVLLLKALGINDFLHFDFMDSPSVETL 1021
Cdd:PRK11664 308 VTQRISQASMTQRAGRAGRLEPGICLHLYSKEQAE-RAAAQSEPEILHSDLSGLLLELLQWGCHDPAQLSWLDQPPAAAL 386
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 124802732 1022 IHSLENLYYLGALDDNGYLTKLGKKMANFPMEPNLSKILL 1061
Cdd:PRK11664 387 AAAKRLLQQLGALDGQGRLTARGRKMAALGNDPRLAAMLV 426
|
|
| DEXHc_DHX35 |
cd17980 |
DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and ... |
631-798 |
4.49e-78 |
|
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: 255.09 E-value: 4.49e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 631 LPIYNLKNDLMKAIEKNNVLIVIGETGSGKTTQIPQYLHEANYTEKG-IVGCTQPRRVAAMSIAKRVSEEFGCILGQEVG 709
Cdd:cd17980 1 LPVFKLRNHILYLVENYQTIVIVGETGCGKSTQIPQYLAEAGWTAGGrVVGCTQPRRVAAVTVAGRVAEEMGAVLGHEVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 710 YSIRFDDCTSND-TIIKYLTDGMLLRETLSDTLLTKYSFIILDEAHERTISTDILFCLLKDVVRKRADFKLIVTSATLDA 788
Cdd:cd17980 81 YCIRFDDCTDPQaTRIKFLTDGMLVREMMLDPLLTKYSVIMLDEAHERTLYTDILIGLLKKIQKKRGDLRLIVASATLDA 160
|
170
....*....|
gi 124802732 789 EKFSTyFFNS 798
Cdd:cd17980 161 EKFRD-FFNQ 169
|
|
| DEXHc_DHX40 |
cd17984 |
DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to the ... |
631-803 |
4.37e-73 |
|
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: 240.91 E-value: 4.37e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 631 LPIYNLKNDLMKAIEKNNVLIVIGETGSGKTTQIPQYLHEANYTEKGIVGCTQPRRVAAMSIAKRVSEEFGCILGQEVGY 710
Cdd:cd17984 1 LPIQKQRKKLVQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGFSQHGMIGVTQPRRVAAISVAQRVAEEMKCTLGSKVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 711 SIRFDDCTSNDTIIKYLTDGMLLRETLSDTLLTKYSFIILDEAHERTISTDILFCLLKDVVRKRA-----DFKLIVTSAT 785
Cdd:cd17984 81 QVRFDDCSSKETAIKYMTDGCLLRHILADPNLTKYSVIILDEAHERSLTTDILFGLLKKLFQEKSpnrkeHLKVVVMSAT 160
|
170
....*....|....*...
gi 124802732 786 LDAEKFSTYFFNSPIFTI 803
Cdd:cd17984 161 LELAKLSAFFGNCPVFDI 178
|
|
| DEXHc_DHX37 |
cd17982 |
DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the ... |
631-804 |
5.64e-63 |
|
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: 212.60 E-value: 5.64e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 631 LPIYNLKNDLMKAIEKNNVLIVIGETGSGKTTQIPQYLHEANYTEK-----GIVGCTQPRRVAAMSIAKRVSEEFGcILG 705
Cdd:cd17982 1 LPILAEEQEIMEAINENPVVIICGETGSGKTTQVPQFLYEAGFGSPesdnpGMIGITQPRRVAAVSMAKRVAEELN-VFG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 706 QEVGYSIRFDDCTSNDTIIKYLTDGMLLRETLSDTLLTKYSFIILDEAHERTISTDILFCLLKDVVRKRADF-------- 777
Cdd:cd17982 80 KEVSYQIRYDSTVSENTKIKFMTDGVLLKEIQTDFLLRKYSVIIIDEAHERSVNTDILIGMLSRIVPLRAKLylqdqtvk 159
|
170 180
....*....|....*....|....*....
gi 124802732 778 --KLIVTSATLDAEKFSTyffNSPIFTIP 804
Cdd:cd17982 160 plKLVIMSATLRVEDFTE---NKLLFPRP 185
|
|
| DEXHc_HrpA |
cd17989 |
DEXH-box helicase domain of ATP-dependent RNA helicase HrpA; HrpA is part of the HrpB-HrpA ... |
631-800 |
4.04e-61 |
|
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: 206.54 E-value: 4.04e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 631 LPIYNLKNDLMKAIEKNNVLIVIGETGSGKTTQIPQYLHEANYTEKGIVGCTQPRRVAAMSIAKRVSEEFGCILGQEVGY 710
Cdd:cd17989 1 LPVSQKRDEIAKAIAENQVVIIAGETGSGKTTQLPKICLELGRGIRGLIGHTQPRRLAARSVAERIAEELKTELGGAVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 711 SIRFDDCTSNDTIIKYLTDGMLLRETLSDTLLTKYSFIILDEAHERTISTDILFCLLKDVVRKRADFKLIVTSATLDAEK 790
Cdd:cd17989 81 KVRFTDQTSDETCVKLMTDGILLAETQTDRYLRAYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKVIITSATIDAER 160
|
170
....*....|
gi 124802732 791 FSTYFFNSPI 800
Cdd:cd17989 161 FSRHFNNAPI 170
|
|
| DEXHc_DHX34 |
cd17979 |
DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in ... |
631-800 |
3.95e-52 |
|
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: 180.72 E-value: 3.95e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 631 LPIYNLKNDLMKAIEKNNVLIVIGETGSGKTTQIPQYLHEANYTEkgiVGCTQPRRVAAMSIAKRVSEEFGCILGQEVGY 710
Cdd:cd17979 1 LPIAQYREKIIELLKTHQVVIVAGDTGCGKSTQVPQYLLAAGFRH---IACTQPRRIACISLAKRVAFESLNQYGSKVAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 711 SIRFDDCTSNDTIIKYLTDGMLLRETLSDTLLTKYSFIILDEAHERTISTDILFCLLKDVVRKRADFKLIVTSATLDAEK 790
Cdd:cd17979 78 QIRFERTRTLATKLLFLTEGLLLRQIQRDASLPQYNVLILDEVHERHLHGDFLLGVLRCLLRLRPDLKLILMSATINIEL 157
|
170
....*....|
gi 124802732 791 FSTYFFNSPI 800
Cdd:cd17979 158 FSGYFEGAPV 167
|
|
| DEXHc_DHX29 |
cd17975 |
DEXH-box helicase domain of DEAH-box helicase 29; DEAH-box helicase 29 (DHX29) is a part of ... |
631-803 |
2.16e-50 |
|
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: 176.26 E-value: 2.16e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 631 LPIYNLKNDLMKAIEKNNVLIVIGETGSGKTTQIPQYLHE-----ANYTEKGIVGCTQPRRVAAMSIAKRVSEEFGCILG 705
Cdd:cd17975 1 LPVFKHRESILETLKRHRVVVVAGETGSGKSTQVPQFLLEdlllnGGTAQKCNIVCTQPRRISAMSLATRVCEELGCESG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 706 -----QEVGYSIRFDDCTSNDTIIKYLTDGMLLRETLSDTLLTKYSFIILDEAHERTISTDILFCLLKDVVRKRADFKLI 780
Cdd:cd17975 81 pggknSLCGYQIRMESRTGEATRLLYCTTGVLLRKLQEDGLLSSISHIIVDEVHERSVQSDFLLIILKEILHKRSDLHLI 160
|
170 180
....*....|....*....|...
gi 124802732 781 VTSATLDAEKFSTYFFNSPIFTI 803
Cdd:cd17975 161 LMSATVDCEKFSSYFTHCPILRI 183
|
|
| DEXHc_DHX36 |
cd17981 |
DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as ... |
631-803 |
9.97e-49 |
|
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: 171.18 E-value: 9.97e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 631 LPIYNLKNDLMKAIEKNNVLIVIGETGSGKTTQIPQYLHEaNYTEKG------IVgCTQPRRVAAMSIAKRVSEEFG--C 702
Cdd:cd17981 1 LPSYGMKQEIINMIDNNQVTVISGETGCGKTTQVTQFILD-DAIERGkgsscrIV-CTQPRRISAISVAERVAAERAesC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 703 ILGQEVGYSIRFDD-CTSNDTIIKYLTDGMLLRETLSDTLLTKYSFIILDEAHERTISTDILFCLLKDVVRKRADFKLIV 781
Cdd:cd17981 79 GLGNSTGYQIRLESrKPRKQGSILYCTTGIVLQWLQSDPHLSNVSHLVLDEIHERNLQSDVLMGIVKDLLPFRSDLKVIL 158
|
170 180
....*....|....*....|..
gi 124802732 782 TSATLDAEKFSTYFFNSPIFTI 803
Cdd:cd17981 159 MSATLNAEKFSDYFNNCPMIHI 180
|
|
| DEXHc_YTHDC2 |
cd17987 |
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) ... |
631-803 |
6.13e-48 |
|
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: 168.85 E-value: 6.13e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 631 LPIYNLKNDLMKAIEKNNVLIVIGETGSGKTTQIPQYLHEANYtEKGI---VGCTQPRRVAAMSIAKRVSEEFGCILGQE 707
Cdd:cd17987 1 LPVFEKQEQIVRIIKENKVVLIVGETGSGKTTQIPQFLLDDCY-ANGIpcrIFCTQPRRLAAIAVAERVAAERGEKIGQT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 708 VGYSIRFDDCTSNDTIIKYLTDGMLLRETLS-DTLLTKYSFIILDEAHERTISTDILFCLLKDVVRKRADFKLIVTSATL 786
Cdd:cd17987 80 VGYQIRLESRVSPKTLLTFCTNGVLLRTLMAgDSALSTVTHVIVDEVHERDRFSDFLLTKLRDILQKHPNLKLILSSAAL 159
|
170
....*....|....*..
gi 124802732 787 DAEKFSTYFFNSPIFTI 803
Cdd:cd17987 160 DVNLFIRYFGSCPVIYI 176
|
|
| DEXHc_DHX32 |
cd17977 |
DEXH-box helicase domain of DEAH-box helicase 32; DEAH-box helicase 32 (DHX32) belongs to the ... |
631-800 |
3.34e-47 |
|
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: 166.92 E-value: 3.34e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 631 LPIYNLKNDLMKAIEKNNVLIVIGETGSGKTTQIPQYLHE---ANYTEKGIVGCTQPRRVAAMSIAKRVSEEFGCILGQE 707
Cdd:cd17977 1 LPVWEAKYEFMESLAHNQIVIVSGDAKTGKSSQIPQWCAEyclSAHYQHGVVVCTQVHKQTAVWLALRVADEMDVNIGHE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 708 VGYSIRFDDCTSNDTIIKYLTDGMLLRETLSDTLLTKYSFIILDEAHERTISTDILFCLLKDVVRKRADFKLIVTSATLD 787
Cdd:cd17977 81 VGYVIPFENCCTNETILRYCTDDMLLREMMSDPLLESYGVIILDDAHERTVSTDVLLGLLKDVLLSRPELKLVIITCPHL 160
|
170
....*....|...
gi 124802732 788 AEKFSTYFFNSPI 800
Cdd:cd17977 161 SSKLLSYYGNVPL 173
|
|
| DEXHc_DHX57 |
cd17985 |
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the ... |
631-803 |
1.08e-45 |
|
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: 162.70 E-value: 1.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 631 LPIYNLKNDLMKAIEKNNVLIVIGETGSGKTTQIPQYLHEANYTEK-----GIVgCTQPRRVAAMSIAKRVSEEFGCILG 705
Cdd:cd17985 1 LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFILDNSLQGPplpvaNII-CTQPRRISAISVAERVAQERAERVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 706 QEVGYSIRFDDCTSNDTIIKYLTDGMLLRETLSDTLLTKYSFIILDEAHERTISTDILFCLLKDVVRKRADFKLIVTSAT 785
Cdd:cd17985 80 QSVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDPTLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQRPDLKVILMSAT 159
|
170
....*....|....*...
gi 124802732 786 LDAEKFSTYFFNSPIFTI 803
Cdd:cd17985 160 LNAELFSDYFNSCPVIHI 177
|
|
| DEXHc_DHX9 |
cd17972 |
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ... |
624-803 |
8.03e-43 |
|
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: 156.53 E-value: 8.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 624 INEQRSKLPIYNLKNDLMKAIEKNNVLIVIGETGSGKTTQIPQYLHEaNYTEKGIVG-----CTQPRRVAAMSIAKRVSE 698
Cdd:cd17972 52 ILQERELLPVKKFREEILEAISNNPVVIIRGATGCGKTTQVPQYILD-DFIQNDRAAecnivVTQPRRISAVSVAERVAF 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 699 EFGCILGQEVGYSIRFDDCTSND-TIIKYLTDGMLLRETLSDtlLTKYSFIILDEAHERTISTDILFCLLKDVVRKRADF 777
Cdd:cd17972 131 ERGEEVGKSCGYSVRFESVLPRPhASILFCTVGVLLRKLEAG--IRGISHVIVDEIHERDINTDFLLVVLRDVVQAYPDL 208
|
170 180
....*....|....*....|....*.
gi 124802732 778 KLIVTSATLDAEKFSTYFFNSPIFTI 803
Cdd:cd17972 209 RVILMSATIDTSMFCEYFFNCPVIEV 234
|
|
| DEXQc_DQX1 |
cd17986 |
DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 ... |
631-803 |
1.08e-41 |
|
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: 151.20 E-value: 1.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 631 LPIYNLKNDLMKAIEK-NNVLIVIGETGSGKTTQIPQYLHE---ANYTEKGIVGCTQPRRVAAMSIAKRVSEEFGCILGQ 706
Cdd:cd17986 1 LPIWAAKFTFLEQLESpSGIVLVSGEPGSGKSTQVPQWCAEfalSRGFQKGQVTVTQPHPLAARSLALRVADEMDLNLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 707 EVGYSIRFDDCTSNDTIIKYLTDGMLLRETLSDTLLTKYSFIILDEAHERTISTDILFCLLKDVVRKRADFKLIVTSATL 786
Cdd:cd17986 81 EVGYSIPQEDCTGPNTILRFCWDRLLLQEMTSTPLLGAWGVVVLDEAQERSVASDSLLGLLKDVRLQRPELRVVVVTSPA 160
|
170
....*....|....*..
gi 124802732 787 DAEKFSTYFFNSPIFTI 803
Cdd:cd17986 161 LEPKLRAFWGNPPVVHV 177
|
|
| DEXHc_TDRD9 |
cd17988 |
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ... |
631-810 |
9.95e-41 |
|
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: 148.42 E-value: 9.95e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 631 LPIYNLKNDLMKAIEKNNVLIVIGETGSGKTTQIPQYLHEaNYTEKGI---VGCTQPRRVAAMSIAKRVSEEFGCILGQE 707
Cdd:cd17988 1 LPIYAKREEILSLIEANSVVIIKGATGCGKTTQLPQFILD-HYYKRGKycnIVVTQPRRIAAISIARRVSQEREWTLGSL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 708 VGYSIRFDDCTSNDTIIKYLTDGMLLRETLSDTLLTKYSFIILDEAHERTISTDILFCLLKDVVRKRADF-KLIVTSATL 786
Cdd:cd17988 80 VGYQVGLERPASEETRLIYCTTGVLLQKLINNKTLTEYTHIILDEVHERDQELDFLLLVVRRLLRTNSRHvKIILMSATI 159
|
170 180
....*....|....*....|....
gi 124802732 787 DAEKFSTYfFNSPIftIPGKIFPV 810
Cdd:cd17988 160 SCKEFADY-FTTPN--NPAYVFEV 180
|
|
| DEXHc_HrpB |
cd17990 |
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ... |
631-801 |
2.10e-40 |
|
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: 147.09 E-value: 2.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 631 LPIYNLKNDLMKAIEKNNVLIVIGETGSGKTTQIPQYL--HEANYTEKGIVgcTQPRRVAAMSIAKRVSEEFGCILGQEV 708
Cdd:cd17990 1 LPIAAVLPALRAALDAGGQVVLEAPPGAGKTTRVPLALlaELWIAGGKIIV--LEPRRVAARAAARRLATLLGEAPGETV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 709 GYSIRFDDCTSNDTIIKYLTDGMLLRETLSDTLLTKYSFIILDEAHERTISTDILFCLLKDVVR-KRADFKLIVTSATLD 787
Cdd:cd17990 79 GYRVRGESRVGRRTRVEVVTEGVLLRRLQRDPELSGVGAVILDEFHERSLDADLALALLLEVQQlLRDDLRLLAMSATLD 158
|
170
....*....|....
gi 124802732 788 AEKFSTYFFNSPIF 801
Cdd:cd17990 159 GDGLAALLPEAPVV 172
|
|
| DEXHc_DHX30 |
cd17976 |
DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an ... |
631-800 |
2.17e-38 |
|
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: 141.47 E-value: 2.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 631 LPIYNLKNDLMKAIEKNNVLIVIGETGSGKTTQIPQYLHEANYTEKGIVGC----TQPRRVAAMSIAKRVSEEFGCILGQ 706
Cdd:cd17976 1 LPVDSHKESILSAIEQNPVVVISGDTGCGKTTRIPQFILEDYVLRGRGARCnvviTQPRRISAVSVAQRVAHELGPNLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 707 EVGYSIRFDD-CTSNDTIIKYLTDGMLLRETLSDTLLTKYSFIILDEAHERTISTDILFCLLKDVVRKRADFKLIVTSAT 785
Cdd:cd17976 81 NVGYQVRLESrPPPRGGALLFCTVGVLLKKLQSNPRLEGVSHVIVDEVHERDVNTDFLLILLKGVLQLNPELRVVLMSAT 160
|
170
....*....|....*
gi 124802732 786 LDAEKFSTYFFNSPI 800
Cdd:cd17976 161 GDNQRLSRYFGGCPV 175
|
|
| S1_DHX8_helicase |
cd05684 |
S1_DHX8_helicase: The N-terminal S1 domain of human ATP-dependent RNA helicase DHX8, a DEAH ... |
329-408 |
2.40e-32 |
|
S1_DHX8_helicase: The N-terminal S1 domain of human ATP-dependent RNA helicase DHX8, a DEAH (Asp-Glu-Ala-His) box polypeptide. The DEAH-box RNA helicases are thought to play key roles in pre-mRNA splicing and DHX8 facilitates nuclear export of spliced mRNA by releasing the RNA from the spliceosome. DHX8 is also known as HRH1 (human RNA helicase 1) in Homo sapiens and PRP22 in Saccharomyces cerevisiae.
Pssm-ID: 240189 [Multi-domain] Cd Length: 79 Bit Score: 120.42 E-value: 2.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 329 NNIFNGTINKITDFGLFVSFKTNEGYKEGLVHATDILPNRkRVVNMNEKFKRNMKVKVKVKGIFNQKISLNMSEVDQKTG 408
Cdd:cd05684 1 GKIYKGKVTSIMDFGCFVQLEGLKGRKEGLVHISQLSFEG-RVANPSDVVKRGQKVKVKVISIQNGKISLSMKDVDQDTG 79
|
|
| HA2 |
pfam04408 |
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ... |
1024-1112 |
5.61e-29 |
|
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: 111.95 E-value: 5.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 1024 SLENLYYLGALDDNGYLTKLGKKMANFPMEPNLSKILLTSLNFNCTDDVVTIVSMLSVQNIFYRPQN------------- 1090
Cdd:pfam04408 1 ALELLYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPNFldprsaakaarrr 80
|
90 100
....*....|....*....|....
gi 124802732 1091 KALLADKKKNKFIMPQ--GDLITY 1112
Cdd:pfam04408 81 RRAADEKARAKFARLDleGDHLTL 104
|
|
| OB_NTP_bind |
pfam07717 |
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ... |
1175-1252 |
6.94e-29 |
|
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: 110.81 E-value: 6.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 1175 ICKSICSGYFNHVCKRD-TQQGYTTLLTNQQVFIHPSSTLFN---KNPLFVVYHELVLTNKEYIRDCTIIQPQWLIQLAP 1250
Cdd:pfam07717 1 LRAALAAGLYPNVARRDpKGKGYTTLSDNQRVFIHPSSVLFNektFPPEWVVYQELVETTKVYIRTVTAISPEWLLLFAP 80
|
..
gi 124802732 1251 NL 1252
Cdd:pfam07717 81 HI 82
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
640-812 |
4.50e-27 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 109.89 E-value: 4.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 640 LMKAIEKNNVLIVIGETGSGKTTQIPQYLHEANYTEKGI-VGCTQPRRVAAMSIAKRVSEEFGCILGQEVGY------SI 712
Cdd:smart00487 17 IEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGrVLVLVPTRELAEQWAEELKKLGPSLGLKVVGLyggdskRE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 713 RFDDCTSNDTIIKYLTDGMLLRETLSDTL-LTKYSFIILDEAHERTIS--TDILFCLLKdvvRKRADFKLIVTSATL--D 787
Cdd:smart00487 97 QLRKLESGKTDILVTTPGRLLDLLENDKLsLSNVDLVILDEAHRLLDGgfGDQLEKLLK---LLPKNVQLLLLSATPpeE 173
|
170 180
....*....|....*....|....*
gi 124802732 788 AEKFSTYFFNSPIFTIPGKIFPVEI 812
Cdd:smart00487 174 IENLLELFLNDPVFIDVGFTPLEPI 198
|
|
| HA2 |
smart00847 |
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ... |
1030-1113 |
3.20e-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: 103.12 E-value: 3.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 1030 YLGALDDNGYLTKLGKKMANFPMEPNLSKILLTSLNFNCTDDVVTIVSMLSVQNIFYRPQNKAllADKKKNKFIMPQGDL 1109
Cdd:smart00847 1 ELGALDDDGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPRPKEKRED--ADAARRRFADPESDH 78
|
....
gi 124802732 1110 ITYL 1113
Cdd:smart00847 79 LTLL 82
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
857-962 |
1.28e-12 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 64.54 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 857 EILHERMKKLEsmspppLIILPIYSSLPSEMQSVIFEPAPPGCRKCILATNIAEASLTIDGIFFVIDpgfckikkYDskr 936
Cdd:smart00490 1 EELAELLKELG------IKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVII--------YD--- 63
|
90 100
....*....|....*....|....*.
gi 124802732 937 dmdslivAPISKANAKQRAGRAGRTG 962
Cdd:smart00490 64 -------LPWSPASYIQRIGRAGRAG 82
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
827-962 |
6.23e-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: 60.69 E-value: 6.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 827 LITVLNIHLNEHPGDILVFLTGQDEINtaCEILHERMKklesmspppLIILPIYSSLPSEMQSVIFEPAPPGCRKCILAT 906
Cdd:pfam00271 3 LEALLELLKKERGGKVLIFSQTKKTLE--AELLLEKEG---------IKVARLHGDLSQEEREEILEDFRKGKIDVLVAT 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 124802732 907 NIAEASLTIDGIFFVIDpgfckikkYDSKRDMDSLIvapiskanakQRAGRAGRTG 962
Cdd:pfam00271 72 DVAERGLDLPDVDLVIN--------YDLPWNPASYI----------QRIGRAGRAG 109
|
|
| PRK11824 |
PRK11824 |
polynucleotide phosphorylase/polyadenylase; Provisional |
331-404 |
1.97e-10 |
|
polynucleotide phosphorylase/polyadenylase; Provisional
Pssm-ID: 236995 [Multi-domain] Cd Length: 693 Bit Score: 65.07 E-value: 1.97e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124802732 331 IFNGTINKITDFGLFVSFKtneGYKEGLVHATDIlpNRKRVVNMNEKFKRNMKVKVKVKGIFNQ-KISLNMSEVD 404
Cdd:PRK11824 624 IYEGKVVRIVDFGAFVEIL---PGKDGLVHISEI--ADERVEKVEDVLKEGDEVKVKVLEIDKRgRIRLSRKAVL 693
|
|
| PHA02653 |
PHA02653 |
RNA helicase NPH-II; Provisional |
646-971 |
2.09e-10 |
|
RNA helicase NPH-II; Provisional
Pssm-ID: 177443 [Multi-domain] Cd Length: 675 Bit Score: 65.00 E-value: 2.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 646 KNNVLIVIGETGSGKTTQIPQ------YLH---------EANYTEKGIVgCTQPRR--VAAMSIAKRVSEEFGCILGQEV 708
Cdd:PHA02653 178 SRKPVVLTGGTGVGKTSQVPKlllwfnYLFggfdnldkiDPNFIERPIV-LSLPRValVRLHSITLLKSLGFDEIDGSPI 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 709 gySIRFDDCTS---NDTIIKYltdGMLL---RETLSDtlLTKYSFIILDEAHERTISTDILFCllkdVVRKRADF--KLI 780
Cdd:PHA02653 257 --SLKYGSIPDeliNTNPKPY---GLVFsthKLTLNK--LFDYGTVIIDEVHEHDQIGDIIIA----VARKHIDKirSLF 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 781 VTSATL-DAEKFSTYFFNSPIFT-IPG-KIFPVEILHSKEPES-----DYVEASLITVLNIHLNEHPGD---ILVFLTGQ 849
Cdd:PHA02653 326 LMTATLeDDRDRIKEFFPNPAFVhIPGgTLFPISEVYVKNKYNpknkrAYIEEEKKNIVTALKKYTPPKgssGIVFVASV 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 850 DEINTACEILHERMkklesmspPPLIILPIYSSLPS--EMQSVIFEPAPPgcrKCILATNIAEASLTIDGIFFVIDPGFC 927
Cdd:PHA02653 406 SQCEEYKKYLEKRL--------PIYDFYIIHGKVPNidEILEKVYSSKNP---SIIISTPYLESSVTIRNATHVYDTGRV 474
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 124802732 928 KIKKYDSKRDMdslivaPISKANAKQRAGRAGRTGPGKCYRLYT 971
Cdd:PHA02653 475 YVPEPFGGKEM------FISKSMRTQRKGRVGRVSPGTYVYFYD 512
|
|
| PRK05807 |
PRK05807 |
RNA-binding protein S1; |
324-439 |
2.99e-10 |
|
RNA-binding protein S1;
Pssm-ID: 235614 [Multi-domain] Cd Length: 136 Bit Score: 59.37 E-value: 2.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 324 MALKLNNIFNGTINKITDFGLFVSFktnEGyKEGLVHATDILPNrkRVVNMNEKFKRNMKVKVKVKGI-FNQKISLNMSE 402
Cdd:PRK05807 1 MTLKAGSILEGTVVNITNFGAFVEV---EG-KTGLVHISEVADT--YVKDIREHLKEQDKVKVKVISIdDNGKISLSIKQ 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 124802732 403 -VDQKTGKNLVNDDMNKE---------EDNYISLFDDINEDFNDLKK 439
Cdd:PRK05807 75 aMKQKKSVKPAEIDWQKEknknnngnfEDRLSKFLKDSEERFQDLKK 121
|
|
| S1 |
smart00316 |
Ribosomal protein S1-like RNA-binding domain; |
327-401 |
6.54e-08 |
|
Ribosomal protein S1-like RNA-binding domain;
Pssm-ID: 197648 [Multi-domain] Cd Length: 72 Bit Score: 50.68 E-value: 6.54e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124802732 327 KLNNIFNGTINKITDFGLFVSFktnEGYKEGLVHATDIlpNRKRVVNMNEKFKRNMKVKVKVKGIFNQKISLNMS 401
Cdd:smart00316 1 EVGDVVEGTVTEITPGGAFVDL---GNGVEGLIPISEL--SDKRVKDPEEVLKVGDEVKVKVLSVDEEKGRIILS 70
|
|
| S1_like |
cd00164 |
S1_like: Ribosomal protein S1-like RNA-binding domain. Found in a wide variety of ... |
334-401 |
7.54e-08 |
|
S1_like: Ribosomal protein S1-like RNA-binding domain. Found in a wide variety of RNA-associated proteins. Originally identified in S1 ribosomal protein. This superfamily also contains the Cold Shock Domain (CSD), which is a homolog of the S1 domain. Both domains are members of the Oligonucleotide/oligosaccharide Binding (OB) fold.
Pssm-ID: 238094 [Multi-domain] Cd Length: 65 Bit Score: 50.46 E-value: 7.54e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124802732 334 GTINKITDFGLFVSFktnEGYKEGLVHATDIlpNRKRVVNMNEKFKRNMKVKVKVKGIFNQKISLNMS 401
Cdd:cd00164 3 GKVVSITKFGVFVEL---EDGVEGLVHISEL--SDKFVKDPSEVFKVGDEVEVKVLEVDPEKGRISLS 65
|
|
| YabR |
COG1098 |
Predicted RNA-binding protein, contains ribosomal protein S1 (RPS1) domain [General function ... |
324-406 |
2.11e-07 |
|
Predicted RNA-binding protein, contains ribosomal protein S1 (RPS1) domain [General function prediction only];
Pssm-ID: 440715 [Multi-domain] Cd Length: 130 Bit Score: 50.95 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 324 MALKLNNIFNGTINKITDFGLFVSFktnEGYKEGLVHATDIlpNRKRVVNMNEKFKRNMKVKVKVKGI-FNQKISLNMSE 402
Cdd:COG1098 1 MSIEVGDIVEGKVTGITPFGAFVEL---PEGTTGLVHISEI--ADGYVKDINDYLKVGDEVKVKVLSIdEDGKISLSIKQ 75
|
....
gi 124802732 403 VDQK 406
Cdd:COG1098 76 AEEK 79
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
641-789 |
2.19e-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: 51.86 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 641 MKAIEKNNVLIVIGETGSGKTT--QIP--QYLHEANYTEKGIVgcTQPRRVAAMSIAKRVsEEFGCILGQEV-----GYS 711
Cdd:pfam00270 8 IPAILEGRDVLVQAPTGSGKTLafLLPalEALDKLDNGPQALV--LAPTRELAEQIYEEL-KKLGKGLGLKVasllgGDS 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124802732 712 IRFDDCTSNDTIIKYLTDGMLLRETLSDTLLTKYSFIILDEAHErtISTDILFCLLKDVVRK-RADFKLIVTSATLDAE 789
Cdd:pfam00270 85 RKEQLEKLKGPDILVGTPGRLLDLLQERKLLKNLKLLVLDEAHR--LLDMGFGPDLEEILRRlPKKRQILLLSATLPRN 161
|
|
| rpsA |
PRK06676 |
30S ribosomal protein S1; Reviewed |
326-439 |
3.90e-07 |
|
30S ribosomal protein S1; Reviewed
Pssm-ID: 235851 [Multi-domain] Cd Length: 390 Bit Score: 54.11 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 326 LKLNNIFNGTINKITDFGLFVSFKtnEGYkEGLVHATDIlpNRKRVVNMNEKFKRNMKVKVKVKGI--FNQKISLNM--- 400
Cdd:PRK06676 275 LPEGDVIEGTVKRLTDFGAFVEVL--PGV-EGLVHISQI--SHKHIATPSEVLEEGQEVKVKVLEVneEEKRISLSIkal 349
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 124802732 401 ---SEVDQKTGKNLVNDDMNKEEDNYiSLFDDINEDFNDLKK 439
Cdd:PRK06676 350 eeaPAEEEDRREEYRQYELPEEETGF-SLGDLIGDKLKKLKL 390
|
|
| S1_RPS1_repeat_hs4 |
cd05692 |
S1_RPS1_repeat_hs4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ... |
334-400 |
5.81e-07 |
|
S1_RPS1_repeat_hs4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ribosomal subunit thought to be involved in the recognition and binding of mRNA's during translation initiation. The bacterial RPS1 domain architecture consists of 4-6 tandem S1 domains. In some bacteria, the tandem S1 array is located C-terminal to a 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (HMBPP reductase) domain. While RPS1 is found primarily in bacteria, proteins with tandem RPS1-like domains have been identified in plants and humans, however these lack the N-terminal HMBPP reductase domain. This CD includes S1 repeat 4 (hs4) of the H. sapiens RPS1 homolog. Autoantibodies to double-stranded DNA from patients with systemic lupus erythematosus cross-react with the human RPS1 homolog.
Pssm-ID: 240197 [Multi-domain] Cd Length: 69 Bit Score: 48.05 E-value: 5.81e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124802732 334 GTINKITDFGLFVSFktnEGYKEGLVHATDIlpNRKRVVNMNEKFKRNMKVKVKVKGI-FNQKISLNM 400
Cdd:cd05692 6 GTVTRLKPFGAFVEL---GGGISGLVHISQI--AHKRVKDVKDVLKEGDKVKVKVLSIdARGRISLSI 68
|
|
| RpsA |
COG0539 |
Ribosomal protein S1 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S1 ... |
326-400 |
1.01e-06 |
|
Ribosomal protein S1 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S1 is part of the Pathway/BioSystem: Ribosome 30S subunit
Pssm-ID: 440305 [Multi-domain] Cd Length: 348 Bit Score: 52.35 E-value: 1.01e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124802732 326 LKLNNIFNGTINKITDFGLFVSFktneGYKEGLVHATDIlpNRKRVVNMNEKFKRNMKVKVKVKGI--FNQKISLNM 400
Cdd:COG0539 187 LEEGDVVEGTVKNITDFGAFVDL----GGVDGLLHISEI--SWGRVKHPSEVLKVGDEVEVKVLKIdrEKERISLSL 257
|
|
| GH2-like_DHX8 |
cd21691 |
GIPC-homology 2 (GH2)-like domain found in DEAH box protein 8 (DHX8) and similar proteins; ... |
4-54 |
1.03e-06 |
|
GIPC-homology 2 (GH2)-like domain found in DEAH box protein 8 (DHX8) and similar proteins; DHX8 (a human homolog of yeast Prp22), also called RNA helicase HRH1, is an ATP-dependent RNA helicase involved in pre-mRNA splicing as a component of the spliceosome. It facilitates nuclear export of spliced mRNA by releasing the RNA from the spliceosome. This model corresponds to the GH2-like domain that shows high sequence similarity with the GH2 domain found in GIPC (GAIP C-terminus-interacting protein) family of proteins, which mediate endocytosis by tethering cargo proteins to the motor myosin VI.
Pssm-ID: 409668 Cd Length: 68 Bit Score: 47.15 E-value: 1.03e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 124802732 4 LSKINLIRKVNEELYNSIGVEDDNLSEFLIYLCEKSTSLEEFCKDVFENGG 54
Cdd:cd21691 1 LEYLSLVSKVCTELENHLGISDKDLAEFIIDLAEKSKTLDEFKKALKENGA 51
|
|
| S1_PNPase |
cd04472 |
S1_PNPase: Polynucleotide phosphorylase (PNPase), ), S1-like RNA-binding domain. PNPase is a ... |
331-398 |
2.49e-06 |
|
S1_PNPase: Polynucleotide phosphorylase (PNPase), ), S1-like RNA-binding domain. PNPase is a polyribonucleotide nucleotidyl transferase that degrades mRNA. It is a trimeric multidomain protein. The C-terminus contains the S1 domain which binds ssRNA. This family is classified based on the S1 domain. PNPase nonspecifically removes the 3' nucleotides from mRNA, but is stalled by double-stranded RNA structures such as a stem-loop. Evidence shows that a minimum of 7-10 unpaired nucleotides at the 3' end, is required for PNPase degradation. It is suggested that PNPase also dephosphorylates the RNA 5' end. This additional activity may regulate the 5'-dependent activity of RNaseE in vivo.
Pssm-ID: 239918 [Multi-domain] Cd Length: 68 Bit Score: 46.00 E-value: 2.49e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124802732 331 IFNGTINKITDFGLFVSFKtneGYKEGLVHATDIlpNRKRVVNMNEKFKRNMKVKVKVKGIFNQ-KISL 398
Cdd:cd04472 3 IYEGKVVKIKDFGAFVEIL---PGKDGLVHISEL--SDERVEKVEDVLKVGDEVKVKVIEVDDRgRISL 66
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
647-785 |
3.90e-06 |
|
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: 47.78 E-value: 3.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 647 NNVLIViGETGSGKTTQIPQYLHEANYTEKGIVGCTQPRRVAAMSIAKRVSEEFGC-----ILGQEVGYSIRFDDCTSND 721
Cdd:cd00046 2 ENVLIT-APTGSGKTLAALLAALLLLLKKGKKVLVLVPTKALALQTAERLRELFGPgirvaVLVGGSSAEEREKNKLGDA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124802732 722 TIIkYLTDGMLLRETLSDTLLT--KYSFIILDEAHERTISTD-ILFCLLKDVVRKRADFKLIVTSAT 785
Cdd:cd00046 81 DII-IATPDMLLNLLLREDRLFlkDLKLIIVDEAHALLIDSRgALILDLAVRKAGLKNAQVILLSAT 146
|
|
| RpsA |
COG0539 |
Ribosomal protein S1 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S1 ... |
326-403 |
7.96e-06 |
|
Ribosomal protein S1 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S1 is part of the Pathway/BioSystem: Ribosome 30S subunit
Pssm-ID: 440305 [Multi-domain] Cd Length: 348 Bit Score: 49.66 E-value: 7.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 326 LKLNNIFNGTINKITDFGLFVSFKtnEGYkEGLVHATDILPNrKRVVNMNEKFKRNMKVKVKVKGI--FNQKISLNMSEV 403
Cdd:COG0539 272 YPVGDVVKGKVTRLTDFGAFVELE--PGV-EGLVHISEMSWT-KRVAHPSDVVKVGDEVEVKVLDIdpEERRISLSIKQL 347
|
|
| rpsA |
PRK06299 |
30S ribosomal protein S1; Reviewed |
315-440 |
8.36e-06 |
|
30S ribosomal protein S1; Reviewed
Pssm-ID: 235775 [Multi-domain] Cd Length: 565 Bit Score: 50.16 E-value: 8.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 315 EEDKsYDDYMA-LKLNNIFNGTINKITDFGLFVSFktNEGYkEGLVHATDILpnRKRVVNMNEKFKRNMKVKVKVKGI-- 391
Cdd:PRK06299 447 EEDP-FEEFAKkHKKGSIVTGTVTEVKDKGAFVEL--EDGV-EGLIRASELS--RDRVEDATEVLKVGDEVEAKVINIdr 520
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 124802732 392 FNQKISLNMSEVDQKTGKNLVNdDMNKEEDNYISLFDDINEdfnDLKKK 440
Cdd:PRK06299 521 KNRRISLSIKALDEAEEKEAIA-EYNSASDSKTTLGDLLKA---ALKGK 565
|
|
| DEXHc_viral_Ns3 |
cd17931 |
DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional ... |
656-754 |
1.06e-05 |
|
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: 46.77 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 656 TGSGKTTQI-PQYLHEAnYTEKGIVGCTQPRRVAAMSIAKRVSeefgcilGQEVGYSI-RFDDCTSNDTIIKYLTDGMLL 733
Cdd:cd17931 10 PGAGKTTRVlPQIIREA-IKKRLRTLVLAPTRVVAAEMYEALR-------GLPIRYRTgAVKEEHGGNEIVDYMCHGTFT 81
|
90 100
....*....|....*....|.
gi 124802732 734 RETLSDTLLTKYSFIILDEAH 754
Cdd:cd17931 82 CRLLSPKRVPNYNLIIMDEAH 102
|
|
| S1_RPS1_repeat_ec3 |
cd05688 |
S1_RPS1_repeat_ec3: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ... |
331-398 |
1.24e-05 |
|
S1_RPS1_repeat_ec3: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ribosomal subunit thought to be involved in the recognition and binding of mRNA's during translation initiation. The bacterial RPS1 domain architecture consists of 4-6 tandem S1 domains. In some bacteria, the tandem S1 array is located C-terminal to a 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (HMBPP reductase) domain. While RPS1 is found primarily in bacteria, proteins with tandem RPS1-like domains have been identified in plants and humans, however these lack the N-terminal HMBPP reductase domain. This CD includes S1 repeat 3 (ec3) of the Escherichia coli RPS1. Autoantibodies to double-stranded DNA from patients with systemic lupus erythematosus cross-react with the human RPS1 homolog.
Pssm-ID: 240193 [Multi-domain] Cd Length: 68 Bit Score: 44.16 E-value: 1.24e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 331 IFNGTINKITDFGLFVSFktneGYKEGLVHATDIlpNRKRVVNMNEKFKRNMKVKVKVKGI--FNQKISL 398
Cdd:cd05688 4 VVEGTVKSITDFGAFVDL----GGVDGLLHISDM--SWGRVKHPSEVVNVGDEVEVKVLKIdkERKRISL 67
|
|
| S1_RPS1_repeat_ec5 |
cd05690 |
S1_RPS1_repeat_ec5: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ... |
334-398 |
1.59e-05 |
|
S1_RPS1_repeat_ec5: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ribosomal subunit thought to be involved in the recognition and binding of mRNA's during translation initiation. The bacterial RPS1 domain architecture consists of 4-6 tandem S1 domains. In some bacteria, the tandem S1 array is located C-terminal to a 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (HMBPP reductase) domain. While RPS1 is found primarily in bacteria, proteins with tandem RPS1-like domains have been identified in plants and humans, however these lack the N-terminal HMBPP reductase domain. This CD includes S1 repeat 5 (ec5) of the Escherichia coli RPS1. Autoantibodies to double-stranded DNA from patients with systemic lupus erythematosus cross-react with the human RPS1 homolog.
Pssm-ID: 240195 [Multi-domain] Cd Length: 69 Bit Score: 44.02 E-value: 1.59e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124802732 334 GTINKITDFGLFVSFktnEGYKEGLVHATDILPNrKRVVNMNEKFKRNMKVKVKVKGIFN--QKISL 398
Cdd:cd05690 6 GKIKSITDFGIFVGL---DGGIDGLVHISDISWT-QRVRHPSEIYKKGQEVEAVVLNIDVerERISL 68
|
|
| rpsA |
PRK06676 |
30S ribosomal protein S1; Reviewed |
310-403 |
2.40e-05 |
|
30S ribosomal protein S1; Reviewed
Pssm-ID: 235851 [Multi-domain] Cd Length: 390 Bit Score: 48.33 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 310 RDKKNEEDKSyddymALKLNNIFNGTINKITDFGLFVSFktneGYKEGLVHATDIlpNRKRVVNMNEKFKRNMKVKVKVK 389
Cdd:PRK06676 179 RAAKKEELLS-----SLKEGDVVEGTVARLTDFGAFVDI----GGVDGLVHISEL--SHERVEKPSEVVSVGQEVEVKVL 247
|
90
....*....|....*.
gi 124802732 390 GI--FNQKISLNMSEV 403
Cdd:PRK06676 248 SIdwETERISLSLKDT 263
|
|
| rpsA |
PRK06299 |
30S ribosomal protein S1; Reviewed |
334-398 |
2.54e-05 |
|
30S ribosomal protein S1; Reviewed
Pssm-ID: 235775 [Multi-domain] Cd Length: 565 Bit Score: 48.62 E-value: 2.54e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124802732 334 GTINKITDFGLFVSFktnEGYKEGLVHATDILPNRKrVVNMNEKFKRNMKVKVKVKGI--FNQKISL 398
Cdd:PRK06299 379 GKVKNITDFGAFVGL---EGGIDGLVHLSDISWDKK-GEEAVELYKKGDEVEAVVLKVdvEKERISL 441
|
|
| rpsA |
PRK06299 |
30S ribosomal protein S1; Reviewed |
331-400 |
2.96e-05 |
|
30S ribosomal protein S1; Reviewed
Pssm-ID: 235775 [Multi-domain] Cd Length: 565 Bit Score: 48.24 E-value: 2.96e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124802732 331 IFNGTINKITDFGLFVSFktneGYKEGLVHATDIlpNRKRVVNMNEKFKRNMKVKVKVKGI--FNQKISLNM 400
Cdd:PRK06299 204 VVEGVVKNITDYGAFVDL----GGVDGLLHITDI--SWKRVNHPSEVVNVGDEVKVKVLKFdkEKKRVSLGL 269
|
|
| PRK00087 |
PRK00087 |
bifunctional 4-hydroxy-3-methylbut-2-enyl diphosphate reductase/30S ribosomal protein S1; |
327-408 |
5.10e-05 |
|
bifunctional 4-hydroxy-3-methylbut-2-enyl diphosphate reductase/30S ribosomal protein S1;
Pssm-ID: 234623 [Multi-domain] Cd Length: 647 Bit Score: 47.63 E-value: 5.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 327 KLNNIFNGTINKITDFGLFVSFktnEGYKEGLVHATDIlpNRKRVVNMNEKFKRNMKVKVKVKGI--FNQKISLNMSEVD 404
Cdd:PRK00087 561 PVGSIVLGKVVRIAPFGAFVEL---EPGVDGLVHISQI--SWKRIDKPEDVLSEGEEVKAKILEVdpEEKRIRLSIKEVE 635
|
....
gi 124802732 405 QKTG 408
Cdd:PRK00087 636 EEPG 639
|
|
| GH2_like |
cd21690 |
GIPC homology 2 (GH2) domain-like family; The GIPC (GAIP C-terminus-interacting protein) ... |
9-68 |
6.39e-05 |
|
GIPC homology 2 (GH2) domain-like family; The GIPC (GAIP C-terminus-interacting protein) family of proteins mediate endocytosis by tethering cargo proteins to the motor myosin VI. This model represents the C-terminal GIPC homology 2 or GH2 domain (plus the linker to the PDZ domain located N-terminally of GH2), which mediates the interaction with myosin VI and is involved in homodimerization in the autoinhibited state. The family also includes DEAH box protein 8 (DHX8) and similar proteins. DHX8 (a human homolog of yeast Prp22), also called RNA helicase HRH1, is an ATP-dependent RNA helicase involved in pre-mRNA splicing as a component of the spliceosome. It facilitates nuclear export of spliced mRNA by releasing the RNA from the spliceosome. DHX8 contains a GH2-like domain at the N-terminus, which shows high sequence similarity with the GH2 domain found in GIPC proteins.
Pssm-ID: 409667 Cd Length: 62 Bit Score: 42.07 E-value: 6.39e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 9 LIRKVNEELYNSIGVEDDNLSEFLIYLCEKSTSLEEFCKDVFENGGVIEQAVLKYIYNMI 68
Cdd:cd21690 3 AIEKVDDLLKNYLGIDDPELAEFVISLAKKKKNPDEFAEALDENDAAFPDEFVFDLYRAI 62
|
|
| VacB |
COG0557 |
Exoribonuclease R [Transcription]; |
323-389 |
1.02e-04 |
|
Exoribonuclease R [Transcription];
Pssm-ID: 440323 [Multi-domain] Cd Length: 711 Bit Score: 46.64 E-value: 1.02e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124802732 323 YMALKLNNIFNGTINKITDFGLFVsfKTNEGYKEGLVHATDiLPN--------RKRVVnmNEKFKR----NMKVKVKVK 389
Cdd:COG0557 617 YMKDRVGEEFEGVISGVTSFGLFV--ELDELGVEGLVHVSS-LGDdyyeyderRQALV--GERTGKryrlGDRVEVRVV 690
|
|
| rpsA |
TIGR00717 |
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found ... |
334-405 |
9.92e-04 |
|
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found in most bacterial genomes in a single copy, but is not present in the Mycoplasmas. It is heterogeneous with respect to the number of repeats of the S1 RNA binding domain described by pfam00575: six repeats in E. coli and most other bacteria, four in Bacillus subtilis and some other species. rpsA is an essential gene in E. coli but not in B. subtilis. It is associated with the cytidylate kinase gene cmk in many species, and fused to it in Treponema pallidum. RpsA is proposed (Medline:97323001) to assist in mRNA degradation. This model provides trusted hits to most long form (6 repeat) examples of RpsA. Among homologs with only four repeats are some to which other (perhaps secondary) functions have been assigned. [Protein synthesis, Ribosomal proteins: synthesis and modification]
Pssm-ID: 273232 [Multi-domain] Cd Length: 516 Bit Score: 43.18 E-value: 9.92e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124802732 334 GTINKITDFGLFVsfktNEGYKEGLVHATDIlpNRKRVVNMNEKFKRNMKVKVKVKGIFNQK--ISLNMSEVDQ 405
Cdd:TIGR00717 193 GVVKNITDFGAFV----DLGGVDGLLHITDM--SWKRVKHPSEYVKVGQEVKVKVIKFDKEKgrISLSLKQLGE 260
|
|
| S1 |
pfam00575 |
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ... |
326-400 |
2.06e-03 |
|
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is structurally similar to cold shock protein which binds nucleic acids. The S1 domain has an OB-fold structure.
Pssm-ID: 425760 [Multi-domain] Cd Length: 72 Bit Score: 38.04 E-value: 2.06e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124802732 326 LKLNNIFNGTINKITDFGLFVSFktnEGYKEGLVHATDIlpNRKRVVNMNEKFKRNMKVKVKVKGIFNQK--ISLNM 400
Cdd:pfam00575 1 PEKGDVVEGEVTRVTKGGAFVDL---GNGVEGFIPISEL--SDDHVEDPDEVIKVGDEVKVKVLKVDKDRrrIILSI 72
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
649-781 |
2.12e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 39.63 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 649 VLIVIGETGSGKTTQIPQYLHEANYTEKGIVGCTQPRRVAAMSIAKRVSEEFGcilgqevgysirfddctsndTIIKYLT 728
Cdd:pfam13401 7 ILVLTGESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSGTSPKDLLRALLRALG--------------------LPLSGRL 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 124802732 729 DGMLLRETLSDTLLTKYS--FIILDEAHErtISTDILFCLLKDVVRKRADFKLIV 781
Cdd:pfam13401 67 SKEELLAALQQLLLALAVavVLIIDEAQH--LSLEALEELRDLLNLSSKLLQLIL 119
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
903-970 |
2.80e-03 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350172 [Multi-domain] Cd Length: 77 Bit Score: 37.68 E-value: 2.80e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 903 ILATNIAEASLTIDGIFFVIDPGFckikkydskrdmdslivaPISKANAKQRAGRAGRTG--PGKCYRLY 970
Cdd:cd18785 26 LVATNVLGEGIDVPSLDTVIFFDP------------------PSSAASYIQRVGRAGRGGkdEGEVILFV 77
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
646-783 |
5.41e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 38.89 E-value: 5.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802732 646 KNNVLIVIGETGSGKTTQIPQYLHEANYTEKGIVgctqprRVAAMSIAKRVSEEFGCILGQEVGYSirfddctsndtiik 725
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVI------YIDGEDILEEVLDQLLLIIVGGKKAS-------------- 60
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124802732 726 yLTDGMLLRETLSDTLLTKYSFIILDEAH------ERTISTDILFCLLKDVVRKRADFKLIVTS 783
Cdd:smart00382 61 -GSGELRLRLALALARKLKPDVLILDEITslldaeQEALLLLLEELRLLLLLKSEKNLTVILTT 123
|
|
| |
