|
Name |
Accession |
Description |
Interval |
E-value |
| HrpA |
COG1643 |
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis]; |
600-1219 |
9.33e-100 |
|
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441249 [Multi-domain] Cd Length: 836 Bit Score: 339.75 E-value: 9.33e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 600 VREQLPAwkkqkvIIDIINKNEVVLITGETGSGKSTQVVQFILDflqkeKGDFGKTKIVCTQPRRISAIGLAERVSDERC 679
Cdd:COG1643 12 VSAVLPE------LLAALRAHQVVVLAAPPGAGKTTQLPLALLE-----LGWGAGGRIGMLEPRRLAARAAAERMAEELG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 680 VTCGEEVGYVIRGVNKTKASTRIKFMTTGVLVRLLQNARtMLENT-IVVIDEVHERSIDTDLIVTLMKNLLHRVRG-MKI 757
Cdd:COG1643 81 EPVGETVGYRVRFEDKVSAATRIEVVTEGILLRELQRDP-ELEGVdTVIFDEFHERSLNADLLLALLLDLQPALRPdLKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 758 VLMSATVNVDLFKKFFPGLATCHIEGRTFPitdyfledilsdldfkikrekalsydddsVDERnnddqYLKPRADSKFFT 837
Cdd:COG1643 160 LVMSATLDAERFARLLGDAPVIESSGRTYP-----------------------------VEVR-----YRPLPADERDLE 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 838 sgqinyDLLCQVVEYVHkrlkaANDNGSIIVFLPGVGEINKCCNLLAnKSNEADFMVLPLHSALTPEDQKRVFK-KYHGK 916
Cdd:COG1643 206 ------DAVADAVREAL-----AEEPGDILVFLPGEREIRRTAEALR-GRLPPDTEILPLYGRLSAAEQDRAFApAPHGR 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 917 RKVVVSTNIAETSITIDD--CVatIDTGRAKSMFYNPKDNTTKL-IESfISKAEVKQRRGRAGRVREGLSYKLFSKNLYE 993
Cdd:COG1643 274 RRIVLATNIAETSLTVPGirYV--IDSGLARIPRYDPRSGVTRLpTER-ISQASANQRAGRAGRLAPGICYRLWSEEDFA 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 994 NdMISMPIPEIKRIPLESLYLSVKAMGIKDVKAFlsTALDAPPLPALQKAERILTTIGLVDEsDKSLTQLGQFISLMPVm 1073
Cdd:COG1643 351 R-RPAFTDPEILRADLASLILELAAWGLGDPEDL--PFLDPPPARAIADARALLQELGALDA-DGRLTPLGRALARLPL- 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 1074 DSKHGKLLIYGILFGCTDISVLLVSILGIGVlPFIGGfenrekikkllckyeSRGDLFAVLEIVRDYfkikdssikrKYL 1153
Cdd:COG1643 426 DPRLARMLLAAAELGCLREAAILAALLSERD-PRRGA---------------AGSDLLARLNLWRRL----------REQ 479
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398366185 1154 RDNLLSYNKINEIKSSTAQYYSILKDvgflpmdykvgsisDLNRNERNFDIL-RAILTGafYP-HIAR 1219
Cdd:COG1643 480 QREFLSYLRLREWRDLARQLRRLLGE--------------GANEEPADYEAIgLLLALA--YPdRIAR 531
|
|
| DEXHc_RHA-like |
cd17917 |
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ... |
620-781 |
1.34e-72 |
|
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: 238.90 E-value: 1.34e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 620 NEVVLITGETGSGKSTQVVQFILDFLQKEKGdfgKTKIVCTQPRRISAIGLAERVSDERCVTCGEEVGYVIRGVNKTKAS 699
Cdd:cd17917 1 NQVVVIVGETGSGKTTQVPQFLLEDGLAKGG---KGRIVCTQPRRIAAISVAERVAEERGEKLGEEVGYQIRFESKTSSK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 700 TRIKFMTTGVLVRLLQNARTMLENTIVVIDEVHERSIDTDLIVTLMKNLLHRVRGMKIVLMSATVNVDLFKKFFPGLATC 779
Cdd:cd17917 78 TRIKFCTDGILLRELLSDPLLSGYSHVILDEAHERSLDTDFLLGLLKDLLRKRPDLKVILMSATLDAEKFSSYFGGAPVI 157
|
..
gi 398366185 780 HI 781
Cdd:cd17917 158 HI 159
|
|
| PRK11131 |
PRK11131 |
ATP-dependent RNA helicase HrpA; Provisional |
555-1102 |
9.74e-67 |
|
ATP-dependent RNA helicase HrpA; Provisional
Pssm-ID: 182986 [Multi-domain] Cd Length: 1294 Bit Score: 248.44 E-value: 9.74e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 555 NGKRSINNSSSRKFTKTTISEDtLSVLREEYTKR---IKSSEYKsmqlvrEQLPAWKKQKVIIDIINKNEVVLITGETGS 631
Cdd:PRK11131 28 HGAKKIKNPDAQQAIFQEIAKE-IAQAAQRVLLReaaRPEITYP------ENLPVSQKKQDILEAIRDHQVVIVAGETGS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 632 GKSTQVVQFILDFLQKEKGDFGKTkivctQPRRISAIGLAERVSDERCVTCGEEVGYVIRGVNKTKASTRIKFMTTGVLV 711
Cdd:PRK11131 101 GKTTQLPKICLELGRGVKGLIGHT-----QPRRLAARTVANRIAEELETELGGCVGYKVRFNDQVSDNTMVKLMTDGILL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 712 RLLQNARTMLENTIVVIDEVHERSIDTDLIVTLMKNLLHRVRGMKIVLMSATVNVDLFKKFFPGLATCHIEGRTFPITdy 791
Cdd:PRK11131 176 AEIQQDRLLMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPDLKVIITSATIDPERFSRHFNNAPIIEVSGRTYPVE-- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 792 fledilsdldfkiKREKALSYDDDSVDErnndDQylkpradskffTSGQIN-YDLLCqvveyvhkrlkaANDNGSIIVFL 870
Cdd:PRK11131 254 -------------VRYRPIVEEADDTER----DQ-----------LQAIFDaVDELG------------REGPGDILIFM 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 871 PGVGEINKCCNLLaNKSNEADFMVLPLHSALTPEDQKRVFKKYHGKRkVVVSTNIAETSITIDDCVATIDTGRAKSMFYN 950
Cdd:PRK11131 294 SGEREIRDTADAL-NKLNLRHTEILPLYARLSNSEQNRVFQSHSGRR-IVLATNVAETSLTVPGIKYVIDPGTARISRYS 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 951 PKDNTTKL-IESfISKAEVKQRRGRAGRVREGLSYKLFSknlyENDMISMPI---PEIKRIPLESLYLSVKAMGIKDVKA 1026
Cdd:PRK11131 372 YRTKVQRLpIEP-ISQASANQRKGRCGRVSEGICIRLYS----EDDFLSRPEftdPEILRTNLASVILQMTALGLGDIAA 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 1027 FlsTALDAPPLPALQKAERILTTIGLVDESDK----SLTQLGQFISLMPVmDSKHGKLLIYGILFGCTDISVLLVSILGI 1102
Cdd:PRK11131 447 F--PFVEAPDKRNIQDGVRLLEELGAITTDEQasayKLTPLGRQLAQLPV-DPRLARMVLEAQKHGCVREVMIITSALSI 523
|
|
| DEAH_box_HrpB |
TIGR01970 |
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ... |
616-1072 |
1.83e-66 |
|
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: 241.98 E-value: 1.83e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 616 IINKNEVVLiTGETGSGKSTQVVQFILDflqkeKGDFGKtKIVCTQPRRISAIGLAERVSDERCVTCGEEVGYVIRGVNK 695
Cdd:TIGR01970 14 LAAHPQVVL-EAPPGAGKSTAVPLALLD-----APGIGG-KIIMLEPRRLAARSAAQRLASQLGEAVGQTVGYRVRGENK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 696 TKASTRIKFMTTGVLVRLLQNaRTMLENTIVVI-DEVHERSIDTDLIVTLMKNLLHRVR-GMKIVLMSATVNVDLFKKFF 773
Cdd:TIGR01970 87 VSRRTRLEVVTEGILTRMIQD-DPELDGVGALIfDEFHERSLDADLGLALALDVQSSLReDLKILAMSATLDGERLSSLL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 774 PGLATCHIEGRTFPItdyfledilsdldfkikrekalsydddsvdernnDDQYLKPRADSKFFTsgqinydllcQVVEYV 853
Cdd:TIGR01970 166 PDAPVVESEGRSFPV----------------------------------EIRYLPLRGDQRLED----------AVSRAV 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 854 HKRLkaANDNGSIIVFLPGVGEINKCCNLLANKSNeADFMVLPLHSALTPEDQKRVFK-KYHGKRKVVVSTNIAETSITI 932
Cdd:TIGR01970 202 EHAL--ASETGSILVFLPGQAEIRRVQEQLAERLD-SDVLICPLYGELSLAAQDRAIKpDPQGRRKVVLATNIAETSLTI 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 933 DDCVATIDTGRAKSMFYNPKDNTTKLIESFISKAEVKQRRGRAGRVREGLSYKLFSKNLYENdMISMPIPEIKRIPLESL 1012
Cdd:TIGR01970 279 EGIRVVIDSGLARVARFDPKTGITRLETVRISQASATQRAGRAGRLEPGVCYRLWSEEQHQR-LPAQDEPEILQADLSGL 357
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 1013 YLSVKAMGIKDVKAFlsTALDAPPLPALQKAERILTTIGLVDESDKsLTQLGQFISLMPV 1072
Cdd:TIGR01970 358 ALELAQWGAKDPSDL--RWLDAPPSVALAAARQLLQRLGALDAQGR-LTAHGKAMAALGC 414
|
|
| RWD_YLR419W-like |
cd23827 |
RWD domain of Saccharomyces cerevisiae putative ATP-dependent RNA helicase YLR419W and related ... |
428-532 |
1.64e-33 |
|
RWD domain of Saccharomyces cerevisiae putative ATP-dependent RNA helicase YLR419W and related proteins; YLR419W (EC 3.6.4.13) may act as an ATP-binding RNA helicase. The RWD domain may mediate protein-protein interactions.
Pssm-ID: 467662 Cd Length: 104 Bit Score: 125.05 E-value: 1.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 428 WNQELESLESIYeGCVMDAKEDSHYTLNLI----EKLKIKLKVYRTKNYPASLPGIVVSTFDKnykLPDYIKKQILTRLL 503
Cdd:cd23827 1 WDEEIEALEAIY-GEKFEVISDDSCEITLNsptkTKPSLKLKFYKSSSYPNSLPGIFISSSDK---LPAYIKLAIIRQLL 76
|
90 100
....*....|....*....|....*....
gi 398366185 504 HYLQEgNLIGDMLVYHIYEWLKENISKII 532
Cdd:cd23827 77 QYARD-NLLGDPMIFSIVEWLEENIEEII 104
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
610-787 |
4.13e-21 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 92.94 E-value: 4.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 610 QKVIIDIINKNE-VVLITGETGSGKSTQVVQFILDFLQKEKGdfgkTKIVCTQPRRISAIGLAERVSdERCVTCGEEVGY 688
Cdd:smart00487 13 QKEAIEALLSGLrDVILAAPTGSGKTLAALLPALEALKRGKG----GRVLVLVPTRELAEQWAEELK-KLGPSLGLKVVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 689 VIRGVNK-------TKASTRIKFMTTGVLVRLLQNARTMLEN-TIVVIDEVHERSiDTDLIVTLMKNLLHRVRGMKIVLM 760
Cdd:smart00487 88 LYGGDSKreqlrklESGKTDILVTTPGRLLDLLENDKLSLSNvDLVILDEAHRLL-DGGFGDQLEKLLKLLPKNVQLLLL 166
|
170 180 190
....*....|....*....|....*....|
gi 398366185 761 SATVNVD---LFKKFFPGLATCHIEGRTFP 787
Cdd:smart00487 167 SATPPEEienLLELFLNDPVFIDVGFTPLE 196
|
|
| RWD |
pfam05773 |
RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. ... |
426-528 |
6.13e-18 |
|
RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. The function of this domain is unknown. GCN2 is the alpha-subunit of the only translation initiation factor (eIF2 alpha) kinase that appears in all eukaryotes. Its function requires an interaction with GCN1 via the domain at its N-terminus, which is termed the RWD domain after three major RWD-containing proteins: RING finger-containing proteins, WD-repeat-containing proteins, and yeast DEAD (DEXD)-like helicases. The structure forms an alpha + beta sandwich fold consisting of two layers: a four-stranded antiparallel beta-sheet, and three side-by-side alpha-helices.
Pssm-ID: 399058 Cd Length: 111 Bit Score: 80.83 E-value: 6.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 426 ECWNQELESLESIYEGCVMDaKEDSHYTLNLIE--------------KLKIKLKVYRTKNYPASLPGIVVSTFdknYKLP 491
Cdd:pfam05773 1 EEQEEELEALESIYPDEFEV-ISDSPYESLEIEiklsldsdesdsshLPPLVLKFTLPEDYPDEPPKISLSSP---WNLS 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 398366185 492 DYIKKQILTRLLHYLQEgnLIGDMLVYHIYEWLKENI 528
Cdd:pfam05773 77 DEQVLSLLEELEELAEE--NLGEVMIFELIEWLQENL 111
|
|
| UBA_YLR419W_like |
cd14271 |
UBA domain found in Saccharomyces cerevisiae putative ATP-dependent RNA helicase YLR419W and ... |
369-409 |
6.85e-18 |
|
UBA domain found in Saccharomyces cerevisiae putative ATP-dependent RNA helicase YLR419W and similar proteins; The group includes some uncharacterized hypothetical proteins which show a high level of sequence similarity with Saccharomyces cerevisiae putative ATP-dependent RNA helicase YLR419W. All family members contain a ubiquitin-associated (UBA) domain, RWD domain, DEAD-box (DEXDc), helicase superfamily c-terminal domain (HELICc), Helicase associated domain (HA2), and a C-terminal oligonucleotide/oligosaccharide-binding (OB)-fold.
Pssm-ID: 270457 Cd Length: 41 Bit Score: 78.20 E-value: 6.85e-18
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 398366185 369 RMIVERLTEIGVSSDEALLALQQNDMNENEAAGFLTREILP 409
Cdd:cd14271 1 RNMIERLTESGVSKDEALLALEECNFNEAEAAGKLTRSILP 41
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
848-978 |
3.13e-12 |
|
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: 64.54 E-value: 3.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 848 QVVEYVHKRLKAANdNGSIIVFLPGVGEINkcCNLLANKSNeadFMVLPLHSALTPEDQKRVFKKY-HGKRKVVVSTNIA 926
Cdd:pfam00271 1 EKLEALLELLKKER-GGKVLIFSQTKKTLE--AELLLEKEG---IKVARLHGDLSQEEREEILEDFrKGKIDVLVATDVA 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 398366185 927 ETSITIDDCVATIDtgraksmfYNPKDNTTKLIesfiskaevkQRRGRAGRV 978
Cdd:pfam00271 75 ERGLDLPDVDLVIN--------YDLPWNPASYI----------QRIGRAGRA 108
|
|
| RWD |
smart00591 |
domain in RING finger and WD repeat containing proteins and DEXDc-like helicases subfamily ... |
431-529 |
2.32e-11 |
|
domain in RING finger and WD repeat containing proteins and DEXDc-like helicases subfamily related to the UBCc domain;
Pssm-ID: 214735 Cd Length: 107 Bit Score: 61.99 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 431 ELESLESIYEGCVMDAKEDSH---YTLNLIEK--------LKIKLKVYRTKNYPASLPGIVVSTFdknYKLPDYIKKQIL 499
Cdd:smart00591 1 ELEALESIYPEDFEVIDEDARipeITIKLSPSsdegedqyVSLTLQVKLPENYPDEAPPISLLNS---EGLSDEQLAELL 77
|
90 100 110
....*....|....*....|....*....|
gi 398366185 500 TRLLHYLQEgnLIGDMLVYHIYEWLKENIS 529
Cdd:smart00591 78 KKLEEIAEE--NLGEVMIFELVEKLQEFLS 105
|
|
| OB_NTP_bind |
pfam07717 |
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ... |
1205-1342 |
6.53e-05 |
|
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: 42.62 E-value: 6.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 1205 LRAILTGAFYPHIARvqlpdvkylstssgaveKDPEAKmikywirseeyqdkleEYKTKISQEtqkvdledlplpatRAF 1284
Cdd:pfam07717 1 LRAALAAGLYPNVAR-----------------RDPKGK----------------GYTTLSDNQ--------------RVF 33
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 398366185 1285 IHPSSVLFStnsvnledakllsevdgpisrqskiPTVVKYPFVLFTTSQVTNKLYLRD 1342
Cdd:pfam07717 34 IHPSSVLFN-------------------------EKTFPPEWVVYQELVETTKVYIRT 66
|
|
| UBA |
smart00165 |
Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 ... |
369-403 |
5.43e-04 |
|
Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 is known to bind ubiquitin.
Pssm-ID: 197551 [Multi-domain] Cd Length: 37 Bit Score: 38.62 E-value: 5.43e-04
10 20 30
....*....|....*....|....*....|....*
gi 398366185 369 RMIVERLTEIGVSSDEALLALQQNDMNENEAAGFL 403
Cdd:smart00165 2 EEKIDQLLEMGFSREEALKALRAANGNVERAAEYL 36
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HrpA |
COG1643 |
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis]; |
600-1219 |
9.33e-100 |
|
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441249 [Multi-domain] Cd Length: 836 Bit Score: 339.75 E-value: 9.33e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 600 VREQLPAwkkqkvIIDIINKNEVVLITGETGSGKSTQVVQFILDflqkeKGDFGKTKIVCTQPRRISAIGLAERVSDERC 679
Cdd:COG1643 12 VSAVLPE------LLAALRAHQVVVLAAPPGAGKTTQLPLALLE-----LGWGAGGRIGMLEPRRLAARAAAERMAEELG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 680 VTCGEEVGYVIRGVNKTKASTRIKFMTTGVLVRLLQNARtMLENT-IVVIDEVHERSIDTDLIVTLMKNLLHRVRG-MKI 757
Cdd:COG1643 81 EPVGETVGYRVRFEDKVSAATRIEVVTEGILLRELQRDP-ELEGVdTVIFDEFHERSLNADLLLALLLDLQPALRPdLKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 758 VLMSATVNVDLFKKFFPGLATCHIEGRTFPitdyfledilsdldfkikrekalsydddsVDERnnddqYLKPRADSKFFT 837
Cdd:COG1643 160 LVMSATLDAERFARLLGDAPVIESSGRTYP-----------------------------VEVR-----YRPLPADERDLE 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 838 sgqinyDLLCQVVEYVHkrlkaANDNGSIIVFLPGVGEINKCCNLLAnKSNEADFMVLPLHSALTPEDQKRVFK-KYHGK 916
Cdd:COG1643 206 ------DAVADAVREAL-----AEEPGDILVFLPGEREIRRTAEALR-GRLPPDTEILPLYGRLSAAEQDRAFApAPHGR 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 917 RKVVVSTNIAETSITIDD--CVatIDTGRAKSMFYNPKDNTTKL-IESfISKAEVKQRRGRAGRVREGLSYKLFSKNLYE 993
Cdd:COG1643 274 RRIVLATNIAETSLTVPGirYV--IDSGLARIPRYDPRSGVTRLpTER-ISQASANQRAGRAGRLAPGICYRLWSEEDFA 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 994 NdMISMPIPEIKRIPLESLYLSVKAMGIKDVKAFlsTALDAPPLPALQKAERILTTIGLVDEsDKSLTQLGQFISLMPVm 1073
Cdd:COG1643 351 R-RPAFTDPEILRADLASLILELAAWGLGDPEDL--PFLDPPPARAIADARALLQELGALDA-DGRLTPLGRALARLPL- 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 1074 DSKHGKLLIYGILFGCTDISVLLVSILGIGVlPFIGGfenrekikkllckyeSRGDLFAVLEIVRDYfkikdssikrKYL 1153
Cdd:COG1643 426 DPRLARMLLAAAELGCLREAAILAALLSERD-PRRGA---------------AGSDLLARLNLWRRL----------REQ 479
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398366185 1154 RDNLLSYNKINEIKSSTAQYYSILKDvgflpmdykvgsisDLNRNERNFDIL-RAILTGafYP-HIAR 1219
Cdd:COG1643 480 QREFLSYLRLREWRDLARQLRRLLGE--------------GANEEPADYEAIgLLLALA--YPdRIAR 531
|
|
| DEXHc_RHA-like |
cd17917 |
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ... |
620-781 |
1.34e-72 |
|
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: 238.90 E-value: 1.34e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 620 NEVVLITGETGSGKSTQVVQFILDFLQKEKGdfgKTKIVCTQPRRISAIGLAERVSDERCVTCGEEVGYVIRGVNKTKAS 699
Cdd:cd17917 1 NQVVVIVGETGSGKTTQVPQFLLEDGLAKGG---KGRIVCTQPRRIAAISVAERVAEERGEKLGEEVGYQIRFESKTSSK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 700 TRIKFMTTGVLVRLLQNARTMLENTIVVIDEVHERSIDTDLIVTLMKNLLHRVRGMKIVLMSATVNVDLFKKFFPGLATC 779
Cdd:cd17917 78 TRIKFCTDGILLRELLSDPLLSGYSHVILDEAHERSLDTDFLLGLLKDLLRKRPDLKVILMSATLDAEKFSSYFGGAPVI 157
|
..
gi 398366185 780 HI 781
Cdd:cd17917 158 HI 159
|
|
| PRK11131 |
PRK11131 |
ATP-dependent RNA helicase HrpA; Provisional |
555-1102 |
9.74e-67 |
|
ATP-dependent RNA helicase HrpA; Provisional
Pssm-ID: 182986 [Multi-domain] Cd Length: 1294 Bit Score: 248.44 E-value: 9.74e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 555 NGKRSINNSSSRKFTKTTISEDtLSVLREEYTKR---IKSSEYKsmqlvrEQLPAWKKQKVIIDIINKNEVVLITGETGS 631
Cdd:PRK11131 28 HGAKKIKNPDAQQAIFQEIAKE-IAQAAQRVLLReaaRPEITYP------ENLPVSQKKQDILEAIRDHQVVIVAGETGS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 632 GKSTQVVQFILDFLQKEKGDFGKTkivctQPRRISAIGLAERVSDERCVTCGEEVGYVIRGVNKTKASTRIKFMTTGVLV 711
Cdd:PRK11131 101 GKTTQLPKICLELGRGVKGLIGHT-----QPRRLAARTVANRIAEELETELGGCVGYKVRFNDQVSDNTMVKLMTDGILL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 712 RLLQNARTMLENTIVVIDEVHERSIDTDLIVTLMKNLLHRVRGMKIVLMSATVNVDLFKKFFPGLATCHIEGRTFPITdy 791
Cdd:PRK11131 176 AEIQQDRLLMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPDLKVIITSATIDPERFSRHFNNAPIIEVSGRTYPVE-- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 792 fledilsdldfkiKREKALSYDDDSVDErnndDQylkpradskffTSGQIN-YDLLCqvveyvhkrlkaANDNGSIIVFL 870
Cdd:PRK11131 254 -------------VRYRPIVEEADDTER----DQ-----------LQAIFDaVDELG------------REGPGDILIFM 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 871 PGVGEINKCCNLLaNKSNEADFMVLPLHSALTPEDQKRVFKKYHGKRkVVVSTNIAETSITIDDCVATIDTGRAKSMFYN 950
Cdd:PRK11131 294 SGEREIRDTADAL-NKLNLRHTEILPLYARLSNSEQNRVFQSHSGRR-IVLATNVAETSLTVPGIKYVIDPGTARISRYS 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 951 PKDNTTKL-IESfISKAEVKQRRGRAGRVREGLSYKLFSknlyENDMISMPI---PEIKRIPLESLYLSVKAMGIKDVKA 1026
Cdd:PRK11131 372 YRTKVQRLpIEP-ISQASANQRKGRCGRVSEGICIRLYS----EDDFLSRPEftdPEILRTNLASVILQMTALGLGDIAA 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 1027 FlsTALDAPPLPALQKAERILTTIGLVDESDK----SLTQLGQFISLMPVmDSKHGKLLIYGILFGCTDISVLLVSILGI 1102
Cdd:PRK11131 447 F--PFVEAPDKRNIQDGVRLLEELGAITTDEQasayKLTPLGRQLAQLPV-DPRLARMVLEAQKHGCVREVMIITSALSI 523
|
|
| DEAH_box_HrpB |
TIGR01970 |
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ... |
616-1072 |
1.83e-66 |
|
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: 241.98 E-value: 1.83e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 616 IINKNEVVLiTGETGSGKSTQVVQFILDflqkeKGDFGKtKIVCTQPRRISAIGLAERVSDERCVTCGEEVGYVIRGVNK 695
Cdd:TIGR01970 14 LAAHPQVVL-EAPPGAGKSTAVPLALLD-----APGIGG-KIIMLEPRRLAARSAAQRLASQLGEAVGQTVGYRVRGENK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 696 TKASTRIKFMTTGVLVRLLQNaRTMLENTIVVI-DEVHERSIDTDLIVTLMKNLLHRVR-GMKIVLMSATVNVDLFKKFF 773
Cdd:TIGR01970 87 VSRRTRLEVVTEGILTRMIQD-DPELDGVGALIfDEFHERSLDADLGLALALDVQSSLReDLKILAMSATLDGERLSSLL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 774 PGLATCHIEGRTFPItdyfledilsdldfkikrekalsydddsvdernnDDQYLKPRADSKFFTsgqinydllcQVVEYV 853
Cdd:TIGR01970 166 PDAPVVESEGRSFPV----------------------------------EIRYLPLRGDQRLED----------AVSRAV 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 854 HKRLkaANDNGSIIVFLPGVGEINKCCNLLANKSNeADFMVLPLHSALTPEDQKRVFK-KYHGKRKVVVSTNIAETSITI 932
Cdd:TIGR01970 202 EHAL--ASETGSILVFLPGQAEIRRVQEQLAERLD-SDVLICPLYGELSLAAQDRAIKpDPQGRRKVVLATNIAETSLTI 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 933 DDCVATIDTGRAKSMFYNPKDNTTKLIESFISKAEVKQRRGRAGRVREGLSYKLFSKNLYENdMISMPIPEIKRIPLESL 1012
Cdd:TIGR01970 279 EGIRVVIDSGLARVARFDPKTGITRLETVRISQASATQRAGRAGRLEPGVCYRLWSEEQHQR-LPAQDEPEILQADLSGL 357
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 1013 YLSVKAMGIKDVKAFlsTALDAPPLPALQKAERILTTIGLVDESDKsLTQLGQFISLMPV 1072
Cdd:TIGR01970 358 ALELAQWGAKDPSDL--RWLDAPPSVALAAARQLLQRLGALDAQGR-LTAHGKAMAALGC 414
|
|
| SF2_C_RHA |
cd18791 |
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ... |
786-987 |
9.72e-64 |
|
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: 213.93 E-value: 9.72e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 786 FPITDYFLEDILSDLDFKIKREKalsydddsvdernnddqylkpradskfftsgQINYDLLCQVVEYVHKRlkaaNDNGS 865
Cdd:cd18791 1 FPVEVYYLEDILELLGISSEKED-------------------------------PDYVDAAVRLILQIHRT----EEPGD 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 866 IIVFLPGVGEINKCCNLLANKS---NEADFMVLPLHSALTPEDQKRVFKKYH-GKRKVVVSTNIAETSITIDDCVATIDT 941
Cdd:cd18791 46 ILVFLPGQEEIERLCELLREELlspDLGKLLVLPLHSSLPPEEQQRVFEPPPpGVRKVVLATNIAETSITIPGVVYVIDS 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 398366185 942 GRAKSMFYNPKDNTTKLIESFISKAEVKQRRGRAGRVREGLSYKLF 987
Cdd:cd18791 126 GLVKEKVYDPRTGLSSLVTVWISKASAEQRAGRAGRTRPGKCYRLY 171
|
|
| PRK11664 |
PRK11664 |
ATP-dependent RNA helicase HrpB; Provisional |
623-1065 |
3.42e-59 |
|
ATP-dependent RNA helicase HrpB; Provisional
Pssm-ID: 236950 [Multi-domain] Cd Length: 812 Bit Score: 220.18 E-value: 3.42e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 623 VLITGETGSGKSTQvvqFILDFLQkEKGDFGKtkIVCTQPRRISAIGLAERVSDERCVTCGEEVGYVIRGVNKTKASTRI 702
Cdd:PRK11664 23 VLLKAPTGAGKSTW---LPLQLLQ-HGGINGK--IIMLEPRRLAARNVAQRLAEQLGEKPGETVGYRMRAESKVGPNTRL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 703 KFMTTGVLVRLLQNArTMLENTIVVI-DEVHERSIDTDLIVTLMKNLLHRVR-GMKIVLMSATVNVDLFKKFFPGLATCH 780
Cdd:PRK11664 97 EVVTEGILTRMIQRD-PELSGVGLVIlDEFHERSLQADLALALLLDVQQGLRdDLKLLIMSATLDNDRLQQLLPDAPVIV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 781 IEGRTFPITdyfledilsdldfkiKREKALSydddsVDERnnddqylkpradskfftsgqinydlLCQVVEYVHKRLkAA 860
Cdd:PRK11664 176 SEGRSFPVE---------------RRYQPLP-----AHQR-------------------------FDEAVARATAEL-LR 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 861 NDNGSIIVFLPGVGEINKCCNLLANKSNEaDFMVLPLHSALTPEDQKR-VFKKYHGKRKVVVSTNIAETSITIDDCVATI 939
Cdd:PRK11664 210 QESGSLLLFLPGVGEIQRVQEQLASRVAS-DVLLCPLYGALSLAEQQKaILPAPAGRRKVVLATNIAETSLTIEGIRLVV 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 940 DTGRAKSMFYNPKDNTTKLIESFISKAEVKQRRGRAGRVREGLSYKLFSKNLYENdMISMPIPEIKRIPLESLYLSVKAM 1019
Cdd:PRK11664 289 DSGLERVARFDPKTGLTRLVTQRISQASMTQRAGRAGRLEPGICLHLYSKEQAER-AAAQSEPEILHSDLSGLLLELLQW 367
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 398366185 1020 GIKDVKAFlsTALDAPPLPALQKAERILTTIGLVDESDKsLTQLGQ 1065
Cdd:PRK11664 368 GCHDPAQL--SWLDQPPAAALAAAKRLLQQLGALDGQGR-LTARGR 410
|
|
| DEXHc_DHX57 |
cd17985 |
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the ... |
604-781 |
1.42e-50 |
|
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: 176.57 E-value: 1.42e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 604 LPAWKKQKVIIDIINKNEVVLITGETGSGKSTQVVQFILD-FLQKekGDFGKTKIVCTQPRRISAIGLAERVSDERCVTC 682
Cdd:cd17985 1 LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFILDnSLQG--PPLPVANIICTQPRRISAISVAERVAQERAERV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 683 GEEVGYVIRGVNKTKASTRIKFMTTGVLVRLLQNARTMLENTIVVIDEVHERSIDTDLIVTLMKNLLHRVRGMKIVLMSA 762
Cdd:cd17985 79 GQSVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDPTLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQRPDLKVILMSA 158
|
170
....*....|....*....
gi 398366185 763 TVNVDLFKKFFPGLATCHI 781
Cdd:cd17985 159 TLNAELFSDYFNSCPVIHI 177
|
|
| DEXHc_DHX36 |
cd17981 |
DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as ... |
604-781 |
1.18e-48 |
|
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: 1.18e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 604 LPAWKKQKVIIDIINKNEVVLITGETGSGKSTQVVQFILD-FLQKEKGDfgKTKIVCTQPRRISAIGLAERVSDERCVTC 682
Cdd:cd17981 1 LPSYGMKQEIINMIDNNQVTVISGETGCGKTTQVTQFILDdAIERGKGS--SCRIVCTQPRRISAISVAERVAAERAESC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 683 --GEEVGYVIR-GVNKTKASTRIKFMTTGVLVRLLQNARTMLENTIVVIDEVHERSIDTDLIVTLMKNLLHRVRGMKIVL 759
Cdd:cd17981 79 glGNSTGYQIRlESRKPRKQGSILYCTTGIVLQWLQSDPHLSNVSHLVLDEIHERNLQSDVLMGIVKDLLPFRSDLKVIL 158
|
170 180
....*....|....*....|..
gi 398366185 760 MSATVNVDLFKKFFPGLATCHI 781
Cdd:cd17981 159 MSATLNAEKFSDYFNNCPMIHI 180
|
|
| DEXHc_DHX15 |
cd17973 |
DEXH-box helicase domain of DEAH-box helicase 15; DEAH-box helicase 15 (DHX15) is a pre-mRNA ... |
601-773 |
5.94e-48 |
|
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: 169.52 E-value: 5.94e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 601 REQLPAWKKQKVIIDIINKNEVVLITGETGSGKSTQVVQFILDFlqkEKGDFGKTKIVCTQPRRISAIGLAERVSDERCV 680
Cdd:cd17973 10 RRELPVWEQKEDFLKLLKNNQILVLVGETGSGKTTQIPQFVLDD---ELPHQPKKLVACTQPRRVAAMSVAQRVAEEMDV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 681 TCGEEVGYVIRGVNKTKASTRIKFMTTGVLVRLLQNARTMLENTIVVIDEVHERSIDTDLIVTLMKNLLHRVRGMKIVLM 760
Cdd:cd17973 87 KLGEEVGYSIRFEDCSSAKTILKYMTDGMLLREAMSDPLLSRYSVIILDEAHERTLATDILMGLLKEVVRRRPDLKLIVM 166
|
170
....*....|...
gi 398366185 761 SATVNVDLFKKFF 773
Cdd:cd17973 167 SATLDAGKFQKYF 179
|
|
| DEXHc_DHX9 |
cd17972 |
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ... |
571-773 |
1.04e-46 |
|
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ATP-dependent RNA helicase A or RHA and leukophysin or LKP) plays an important role in many cellular processes, including regulation of DNA replication, transcription, translation, microRNA biogenesis, RNA processing and transport, and maintenance of genomic stability. DHX9 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350730 [Multi-domain] Cd Length: 234 Bit Score: 167.70 E-value: 1.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 571 TTISEDTLSVLREEYTKRIKSSEYKSMQLVREQLPAWKKQKVIIDIINKNEVVLITGETGSGKSTQVVQFILD-FLQKEK 649
Cdd:cd17972 26 ATPEQISMDLKNELMYQREQDHNLQQILQERELLPVKKFREEILEAISNNPVVIIRGATGCGKTTQVPQYILDdFIQNDR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 650 GdfGKTKIVCTQPRRISAIGLAERVSDERCVTCGEEVGYVIRGVNKT-KASTRIKFMTTGVLVRLLQNARTMLENtiVVI 728
Cdd:cd17972 106 A--AECNIVVTQPRRISAVSVAERVAFERGEEVGKSCGYSVRFESVLpRPHASILFCTVGVLLRKLEAGIRGISH--VIV 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 398366185 729 DEVHERSIDTDLIVTLMKNLLHRVRGMKIVLMSATVNVDLFKKFF 773
Cdd:cd17972 182 DEIHERDINTDFLLVVLRDVVQAYPDLRVILMSATIDTSMFCEYF 226
|
|
| DEXHc_DHX29 |
cd17975 |
DEXH-box helicase domain of DEAH-box helicase 29; DEAH-box helicase 29 (DHX29) is a part of ... |
604-773 |
4.44e-45 |
|
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: 161.24 E-value: 4.44e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 604 LPAWKKQKVIIDIINKNEVVLITGETGSGKSTQVVQFILDFLQKEKGDFGKTKIVCTQPRRISAIGLAERVSDERCVTCG 683
Cdd:cd17975 1 LPVFKHRESILETLKRHRVVVVAGETGSGKSTQVPQFLLEDLLLNGGTAQKCNIVCTQPRRISAMSLATRVCEELGCESG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 684 -----EEVGYVIRGVNKTKASTRIKFMTTGVLVRLLQNARTMLENTIVVIDEVHERSIDTDLIVTLMKNLLHRVRGMKIV 758
Cdd:cd17975 81 pggknSLCGYQIRMESRTGEATRLLYCTTGVLLRKLQEDGLLSSISHIIVDEVHERSVQSDFLLIILKEILHKRSDLHLI 160
|
170
....*....|....*
gi 398366185 759 LMSATVNVDLFKKFF 773
Cdd:cd17975 161 LMSATVDCEKFSSYF 175
|
|
| DEXHc_YTHDC2 |
cd17987 |
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) ... |
604-781 |
1.69e-44 |
|
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: 159.22 E-value: 1.69e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 604 LPAWKKQKVIIDIINKNEVVLITGETGSGKSTQVVQFILDFLQKEKGdfgKTKIVCTQPRRISAIGLAERVSDERCVTCG 683
Cdd:cd17987 1 LPVFEKQEQIVRIIKENKVVLIVGETGSGKTTQIPQFLLDDCYANGI---PCRIFCTQPRRLAAIAVAERVAAERGEKIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 684 EEVGYVIRGVNKTKASTRIKFMTTGVLVRLLQNARTMLEN-TIVVIDEVHERSIDTDLIVTLMKNLLHRVRGMKIVLMSA 762
Cdd:cd17987 78 QTVGYQIRLESRVSPKTLLTFCTNGVLLRTLMAGDSALSTvTHVIVDEVHERDRFSDFLLTKLRDILQKHPNLKLILSSA 157
|
170
....*....|....*....
gi 398366185 763 TVNVDLFKKFFPGLATCHI 781
Cdd:cd17987 158 ALDVNLFIRYFGSCPVIYI 176
|
|
| DEXHc_DHX33 |
cd17978 |
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA ... |
604-781 |
2.25e-44 |
|
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: 159.06 E-value: 2.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 604 LPAWKKQKVIIDIINKNEVVLITGETGSGKSTQVVQFILDflqkekGDFGKTKIV-CTQPRRISAIGLAERVSDERCVTC 682
Cdd:cd17978 1 LPIYSARKRLLEELRKHDTVIIIGETGSGKTTQIPQYLYE------AGFARGGMIgITQPRRVAAVSVAKRVAEEMGVEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 683 GEEVGYVIRGVNKTKASTRIKFMTTGVLVRLLQNARTMLENTIVVIDEVHERSIDTDLIVTLMKNLLHRVRG-----MKI 757
Cdd:cd17978 75 GQLVGYSVRFDDVTSEETRIKYMTDGMLLREAIGDPLLSKYSVIILDEAHERTVHTDVLFGLVKSAQRRRKEqklspLKV 154
|
170 180
....*....|....*....|....
gi 398366185 758 VLMSATVNVDLFKKFFPGLATCHI 781
Cdd:cd17978 155 IIMSATLDADLFSEYFNGAPVLYI 178
|
|
| DEXHc_DHX37 |
cd17982 |
DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the ... |
604-775 |
2.83e-43 |
|
DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the human nervous system and has been linked to schizophrenia. It also negatively regulates poxviruses such as Myxoma virus. DEAH-box helicase 37 (DHX37) belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350740 [Multi-domain] Cd Length: 191 Bit Score: 156.36 E-value: 2.83e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 604 LPAWKKQKVIIDIINKNEVVLITGETGSGKSTQVVQFILD--FLQKEKGDFGKtkIVCTQPRRISAIGLAERVSDERCVT 681
Cdd:cd17982 1 LPILAEEQEIMEAINENPVVIICGETGSGKTTQVPQFLYEagFGSPESDNPGM--IGITQPRRVAAVSMAKRVAEELNVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 682 cGEEVGYVIRGVNKTKASTRIKFMTTGVLVRLLQNARTMLENTIVVIDEVHERSIDTDL-------IVTLMKNL---LHR 751
Cdd:cd17982 79 -GKEVSYQIRYDSTVSENTKIKFMTDGVLLKEIQTDFLLRKYSVIIIDEAHERSVNTDIligmlsrIVPLRAKLylqDQT 157
|
170 180
....*....|....*....|....*..
gi 398366185 752 VRGMKIVLMSATVNVDLF---KKFFPG 775
Cdd:cd17982 158 VKPLKLVIMSATLRVEDFtenKLLFPR 184
|
|
| DEXHc_DHX38 |
cd17983 |
DEXH-box helicase domain of DEAH-box helicase 38; DEAH-box helicase 38 (DHX38, also known as ... |
604-781 |
1.38e-42 |
|
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: 153.77 E-value: 1.38e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 604 LPAWKKQKVIIDIINKNEVVLITGETGSGKSTQVVQFILdflqkEKGDFGKTKIVCTQPRRISAIGLAERVSDERCVTCG 683
Cdd:cd17983 1 LPIFAVRQELLNVIRDNNVVIVVGETGSGKTTQLTQYLH-----EDGYTDYGMIGCTQPRRVAAMSVAKRVSEEMGVELG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 684 EEVGYVIRGVNKTKASTRIKFMTTGVLVRLLQNARTMLENTIVVIDEVHERSIDTDLIVTLMKNLLHRVRGMKIVLMSAT 763
Cdd:cd17983 76 EEVGYAIRFEDCTSENTVIKYMTDGILLRESLRDPDLDKYSAIIMDEAHERSLNTDVLFGLLREVVARRRDLKLIVTSAT 155
|
170
....*....|....*...
gi 398366185 764 VNVDLFKKFFPGLATCHI 781
Cdd:cd17983 156 MDADKFADFFGNVPIFTI 173
|
|
| DEXHc_DHX34 |
cd17979 |
DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in ... |
604-775 |
1.65e-42 |
|
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: 153.37 E-value: 1.65e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 604 LPAWKKQKVIIDIINKNEVVLITGETGSGKSTQVVQFILDFlqkekgdfGKTKIVCTQPRRISAIGLAERVSDERCVTCG 683
Cdd:cd17979 1 LPIAQYREKIIELLKTHQVVIVAGDTGCGKSTQVPQYLLAA--------GFRHIACTQPRRIACISLAKRVAFESLNQYG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 684 EEVGYVIRGVNKTKASTRIKFMTTGVLVRLLQNARTMLENTIVVIDEVHERSIDTDLIVTLMKNLLHRVRGMKIVLMSAT 763
Cdd:cd17979 73 SKVAYQIRFERTRTLATKLLFLTEGLLLRQIQRDASLPQYNVLILDEVHERHLHGDFLLGVLRCLLRLRPDLKLILMSAT 152
|
170
....*....|..
gi 398366185 764 VNVDLFKKFFPG 775
Cdd:cd17979 153 INIELFSGYFEG 164
|
|
| DEXHc_DHX8 |
cd17971 |
DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as ... |
601-773 |
6.02e-40 |
|
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: 146.09 E-value: 6.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 601 REQLPAWKKQKVIIDIINKNEVVLITGETGSGKSTQVVQFIldflqKEKGDFGKTKIVCTQPRRISAIGLAERVSDERCV 680
Cdd:cd17971 3 RESLPIYKLKEQLIQAVHDNQILVVIGETGSGKTTQITQYL-----AEAGYTSRGKIGCTQPRRVAAMSVAKRVAEEFGC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 681 TCGEEVGYVIRGVNKTKASTRIKFMTTGVLVRLLQNARTMLENTIVVIDEVHERSIDTDLIVTLMKNLLHRVRGMKIVLM 760
Cdd:cd17971 78 CLGQEVGYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLSQYSVIMLDEAHERTIHTDVLFGLLKKTVQKRPDLKLIVT 157
|
170
....*....|...
gi 398366185 761 SATVNVDLFKKFF 773
Cdd:cd17971 158 SATLDAVKFSQYF 170
|
|
| DEXHc_DHX35 |
cd17980 |
DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and ... |
604-773 |
6.96e-40 |
|
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: 146.46 E-value: 6.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 604 LPAWKKQKVIIDIINKNEVVLITGETGSGKSTQVVQFIldflqKEKG--DFGKTkIVCTQPRRISAIGLAERVSDERCVT 681
Cdd:cd17980 1 LPVFKLRNHILYLVENYQTIVIVGETGCGKSTQIPQYL-----AEAGwtAGGRV-VGCTQPRRVAAVTVAGRVAEEMGAV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 682 CGEEVGYVIRGVNKT-KASTRIKFMTTGVLVRLLQNARTMLENTIVVIDEVHERSIDTDLIVTLMKNLLHRVRGMKIVLM 760
Cdd:cd17980 75 LGHEVGYCIRFDDCTdPQATRIKFLTDGMLVREMMLDPLLTKYSVIMLDEAHERTLYTDILIGLLKKIQKKRGDLRLIVA 154
|
170
....*....|...
gi 398366185 761 SATVNVDLFKKFF 773
Cdd:cd17980 155 SATLDAEKFRDFF 167
|
|
| DEXHc_TDRD9 |
cd17988 |
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ... |
604-773 |
1.37e-38 |
|
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: 142.26 E-value: 1.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 604 LPAWKKQKVIIDIINKNEVVLITGETGSGKSTQVVQFILDFLQKEKGDfgkTKIVCTQPRRISAIGLAERVSDERCVTCG 683
Cdd:cd17988 1 LPIYAKREEILSLIEANSVVIIKGATGCGKTTQLPQFILDHYYKRGKY---CNIVVTQPRRIAAISIARRVSQEREWTLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 684 EEVGYVIRGVNKTKASTRIKFMTTGVLVRLLQNARTMLENTIVVIDEVHERSIDTDLIVTLMKNLLH-RVRGMKIVLMSA 762
Cdd:cd17988 78 SLVGYQVGLERPASEETRLIYCTTGVLLQKLINNKTLTEYTHIILDEVHERDQELDFLLLVVRRLLRtNSRHVKIILMSA 157
|
170
....*....|.
gi 398366185 763 TVNVDLFKKFF 773
Cdd:cd17988 158 TISCKEFADYF 168
|
|
| DEXHc_HrpA |
cd17989 |
DEXH-box helicase domain of ATP-dependent RNA helicase HrpA; HrpA is part of the HrpB-HrpA ... |
604-775 |
1.69e-36 |
|
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: 136.05 E-value: 1.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 604 LPAWKKQKVIIDIINKNEVVLITGETGSGKSTQVVQFILDFLQKEKGDFGKTkivctQPRRISAIGLAERVSDERCVTCG 683
Cdd:cd17989 1 LPVSQKRDEIAKAIAENQVVIIAGETGSGKTTQLPKICLELGRGIRGLIGHT-----QPRRLAARSVAERIAEELKTELG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 684 EEVGYVIRGVNKTKASTRIKFMTTGVLVRLLQNARTMLENTIVVIDEVHERSIDTDLIVTLMKNLLHRVRGMKIVLMSAT 763
Cdd:cd17989 76 GAVGYKVRFTDQTSDETCVKLMTDGILLAETQTDRYLRAYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKVIITSAT 155
|
170
....*....|..
gi 398366185 764 VNVDLFKKFFPG 775
Cdd:cd17989 156 IDAERFSRHFNN 167
|
|
| DEXHc_DHX16 |
cd17974 |
DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably ... |
604-773 |
9.07e-36 |
|
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: 134.17 E-value: 9.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 604 LPAWKKQKVIIDIINKNEVVLITGETGSGKSTQVVQFildfLQKEKGDFGKTKIVCTQPRRISAIGLAERVSDERCVTCG 683
Cdd:cd17974 1 LPVYPYRDDLLAAVKEHQVLIIVGETGSGKTTQIPQY----LHEAGYTKGGGKIGCTQPRRVAAMSVAARVAEEMGVKLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 684 EEVGYVIRGVNKTKASTRIKFMTTGVLVRLLQNARTMLENTIVVIDEVHERSIDTDLIVTLMKNLLHRVRGMKIVLMSAT 763
Cdd:cd17974 77 NEVGYSIRFEDCTSEKTVLKYMTDGMLLREFLTEPDLASYSVMIIDEAHERTLHTDILFGLVKDIARFRPDLKLLISSAT 156
|
170
....*....|
gi 398366185 764 VNVDLFKKFF 773
Cdd:cd17974 157 MDAEKFSAFF 166
|
|
| RWD_YLR419W-like |
cd23827 |
RWD domain of Saccharomyces cerevisiae putative ATP-dependent RNA helicase YLR419W and related ... |
428-532 |
1.64e-33 |
|
RWD domain of Saccharomyces cerevisiae putative ATP-dependent RNA helicase YLR419W and related proteins; YLR419W (EC 3.6.4.13) may act as an ATP-binding RNA helicase. The RWD domain may mediate protein-protein interactions.
Pssm-ID: 467662 Cd Length: 104 Bit Score: 125.05 E-value: 1.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 428 WNQELESLESIYeGCVMDAKEDSHYTLNLI----EKLKIKLKVYRTKNYPASLPGIVVSTFDKnykLPDYIKKQILTRLL 503
Cdd:cd23827 1 WDEEIEALEAIY-GEKFEVISDDSCEITLNsptkTKPSLKLKFYKSSSYPNSLPGIFISSSDK---LPAYIKLAIIRQLL 76
|
90 100
....*....|....*....|....*....
gi 398366185 504 HYLQEgNLIGDMLVYHIYEWLKENISKII 532
Cdd:cd23827 77 QYARD-NLLGDPMIFSIVEWLEENIEEII 104
|
|
| DEXHc_DHX30 |
cd17976 |
DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an ... |
604-781 |
3.55e-33 |
|
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: 126.83 E-value: 3.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 604 LPAWKKQKVIIDIINKNEVVLITGETGSGKSTQVVQFIL-DFLQKEKGdfGKTKIVCTQPRRISAIGLAERVSDERCVTC 682
Cdd:cd17976 1 LPVDSHKESILSAIEQNPVVVISGDTGCGKTTRIPQFILeDYVLRGRG--ARCNVVITQPRRISAVSVAQRVAHELGPNL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 683 GEEVGYVIRGVNKTKAST-RIKFMTTGVLVRLLQNARTMLENTIVVIDEVHERSIDTDLIVTLMKNLLHRVRGMKIVLMS 761
Cdd:cd17976 79 RRNVGYQVRLESRPPPRGgALLFCTVGVLLKKLQSNPRLEGVSHVIVDEVHERDVNTDFLLILLKGVLQLNPELRVVLMS 158
|
170 180
....*....|....*....|
gi 398366185 762 ATVNVDLFKKFFPGLATCHI 781
Cdd:cd17976 159 ATGDNQRLSRYFGGCPVVRV 178
|
|
| DEXHc_DHX40 |
cd17984 |
DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to the ... |
604-781 |
7.28e-32 |
|
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: 123.04 E-value: 7.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 604 LPAWKKQKVIIDIINKNEVVLITGETGSGKSTQVVQFILdflqkeKGDFGKT-KIVCTQPRRISAIGLAERVSDERCVTC 682
Cdd:cd17984 1 LPIQKQRKKLVQAVRDNSFLIVTGNTGSGKTTQLPKYLY------EAGFSQHgMIGVTQPRRVAAISVAQRVAEEMKCTL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 683 GEEVGYVIRGVNKTKASTRIKFMTTGVLVRLLQNARTMLENTIVVIDEVHERSIDTDLIVTLMKNLL-----HRVRGMKI 757
Cdd:cd17984 75 GSKVGYQVRFDDCSSKETAIKYMTDGCLLRHILADPNLTKYSVIILDEAHERSLTTDILFGLLKKLFqekspNRKEHLKV 154
|
170 180
....*....|....*....|....
gi 398366185 758 VLMSATVNVDLFKKFFPGLATCHI 781
Cdd:cd17984 155 VVMSATLELAKLSAFFGNCPVFDI 178
|
|
| DEXHc_HrpB |
cd17990 |
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ... |
600-778 |
1.07e-30 |
|
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: 119.36 E-value: 1.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 600 VREQLPAwkkqkvIIDIINKNEVVLITGETGSGKSTQVVQFILDFLqkekgDFGKTKIVCTQPRRISAIGLAERVSDERC 679
Cdd:cd17990 3 IAAVLPA------LRAALDAGGQVVLEAPPGAGKTTRVPLALLAEL-----WIAGGKIIVLEPRRVAARAAARRLATLLG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 680 VTCGEEVGYVIRGVNKTKASTRIKFMTTGVLVRLLQNARTMLENTIVVIDEVHERSIDTDLIVTlmknLLHRVRG----- 754
Cdd:cd17990 72 EAPGETVGYRVRGESRVGRRTRVEVVTEGVLLRRLQRDPELSGVGAVILDEFHERSLDADLALA----LLLEVQQllrdd 147
|
170 180
....*....|....*....|....
gi 398366185 755 MKIVLMSATVNVDLFKKFFPGLAT 778
Cdd:cd17990 148 LRLLAMSATLDGDGLAALLPEAPV 171
|
|
| DEXHc_DHX32 |
cd17977 |
DEXH-box helicase domain of DEAH-box helicase 32; DEAH-box helicase 32 (DHX32) belongs to the ... |
604-762 |
3.91e-23 |
|
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: 97.97 E-value: 3.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 604 LPAWKKQKVIIDIINKNEVVLITGETGSGKSTQVVQFILDF---LQKEKGdfgktKIVCTQPRRISAIGLAERVSDERCV 680
Cdd:cd17977 1 LPVWEAKYEFMESLAHNQIVIVSGDAKTGKSSQIPQWCAEYclsAHYQHG-----VVVCTQVHKQTAVWLALRVADEMDV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 681 TCGEEVGYVIRGVNKTKASTRIKFMTTGVLVRLLQNARTMLENTIVVIDEVHERSIDTDLIVTLMKNLLHRVRGMKIVLM 760
Cdd:cd17977 76 NIGHEVGYVIPFENCCTNETILRYCTDDMLLREMMSDPLLESYGVIILDDAHERTVSTDVLLGLLKDVLLSRPELKLVII 155
|
..
gi 398366185 761 SA 762
Cdd:cd17977 156 TC 157
|
|
| DEXQc_DQX1 |
cd17986 |
DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 ... |
604-781 |
2.41e-22 |
|
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: 95.73 E-value: 2.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 604 LPAWKKQKVIIDII-NKNEVVLITGETGSGKSTQVVQFILDFLQKEKgdFGKTKIVCTQPRRISAIGLAERVSDERCVTC 682
Cdd:cd17986 1 LPIWAAKFTFLEQLeSPSGIVLVSGEPGSGKSTQVPQWCAEFALSRG--FQKGQVTVTQPHPLAARSLALRVADEMDLNL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 683 GEEVGYVIRGVNKTKASTRIKFMTTGVLVRLLQNARTMLENTIVVIDEVHERSIDTDLIVTLMKNLLHRVRGMKIVLMSA 762
Cdd:cd17986 79 GHEVGYSIPQEDCTGPNTILRFCWDRLLLQEMTSTPLLGAWGVVVLDEAQERSVASDSLLGLLKDVRLQRPELRVVVVTS 158
|
170
....*....|....*....
gi 398366185 763 TVNVDLFKKFFPGLATCHI 781
Cdd:cd17986 159 PALEPKLRAFWGNPPVVHV 177
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
610-787 |
4.13e-21 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 92.94 E-value: 4.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 610 QKVIIDIINKNE-VVLITGETGSGKSTQVVQFILDFLQKEKGdfgkTKIVCTQPRRISAIGLAERVSdERCVTCGEEVGY 688
Cdd:smart00487 13 QKEAIEALLSGLrDVILAAPTGSGKTLAALLPALEALKRGKG----GRVLVLVPTRELAEQWAEELK-KLGPSLGLKVVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 689 VIRGVNK-------TKASTRIKFMTTGVLVRLLQNARTMLEN-TIVVIDEVHERSiDTDLIVTLMKNLLHRVRGMKIVLM 760
Cdd:smart00487 88 LYGGDSKreqlrklESGKTDILVTTPGRLLDLLENDKLSLSNvDLVILDEAHRLL-DGGFGDQLEKLLKLLPKNVQLLLL 166
|
170 180 190
....*....|....*....|....*....|
gi 398366185 761 SATVNVD---LFKKFFPGLATCHIEGRTFP 787
Cdd:smart00487 167 SATPPEEienLLELFLNDPVFIDVGFTPLE 196
|
|
| PHA02653 |
PHA02653 |
RNA helicase NPH-II; Provisional |
610-1013 |
2.32e-20 |
|
RNA helicase NPH-II; Provisional
Pssm-ID: 177443 [Multi-domain] Cd Length: 675 Bit Score: 97.36 E-value: 2.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 610 QKVIIDIINKNEVVLITGETGSGKSTQVVQFIL---------DFLQKEKGDFGKTKIVCTQPRR----------ISAIGL 670
Cdd:PHA02653 169 QLKIFEAWISRKPVVLTGGTGVGKTSQVPKLLLwfnylfggfDNLDKIDPNFIERPIVLSLPRValvrlhsitlLKSLGF 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 671 AErvSDERCVTcgeevgyvIRGVNKTKASTRIKFMTTGVLV---RLLQNArtMLENTIVVIDEVHERSIDTDLIVTLMKN 747
Cdd:PHA02653 249 DE--IDGSPIS--------LKYGSIPDELINTNPKPYGLVFsthKLTLNK--LFDYGTVIIDEVHEHDQIGDIIIAVARK 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 748 LLHRVRgmKIVLMSATV--NVDLFKKFFPGLATCHIEGRT-FPITDYFledILSDLDFKIKREkalsYDDDsvdERNNDD 824
Cdd:PHA02653 317 HIDKIR--SLFLMTATLedDRDRIKEFFPNPAFVHIPGGTlFPISEVY---VKNKYNPKNKRA----YIEE---EKKNIV 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 825 QYLK---PRADSkfftsgqinydllcqvveyvhkrlkaandngSIIVFLPGVGEINKCCNLLANKSNEADFMVLplHSAL 901
Cdd:PHA02653 385 TALKkytPPKGS-------------------------------SGIVFVASVSQCEEYKKYLEKRLPIYDFYII--HGKV 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 902 TPEDQkrVFKKYHGKRK--VVVSTNIAETSITIDDCVATIDTGRAksmfYNPKDNTTKliESFISKAEVKQRRGRAGRVR 979
Cdd:PHA02653 432 PNIDE--ILEKVYSSKNpsIIISTPYLESSVTIRNATHVYDTGRV----YVPEPFGGK--EMFISKSMRTQRKGRVGRVS 503
|
410 420 430
....*....|....*....|....*....|....
gi 398366185 980 EGLSYKLFSKNLyendmismpIPEIKRIPLESLY 1013
Cdd:PHA02653 504 PGTYVYFYDLDL---------LKPIKRIDSEFLH 528
|
|
| RWD |
pfam05773 |
RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. ... |
426-528 |
6.13e-18 |
|
RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. The function of this domain is unknown. GCN2 is the alpha-subunit of the only translation initiation factor (eIF2 alpha) kinase that appears in all eukaryotes. Its function requires an interaction with GCN1 via the domain at its N-terminus, which is termed the RWD domain after three major RWD-containing proteins: RING finger-containing proteins, WD-repeat-containing proteins, and yeast DEAD (DEXD)-like helicases. The structure forms an alpha + beta sandwich fold consisting of two layers: a four-stranded antiparallel beta-sheet, and three side-by-side alpha-helices.
Pssm-ID: 399058 Cd Length: 111 Bit Score: 80.83 E-value: 6.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 426 ECWNQELESLESIYEGCVMDaKEDSHYTLNLIE--------------KLKIKLKVYRTKNYPASLPGIVVSTFdknYKLP 491
Cdd:pfam05773 1 EEQEEELEALESIYPDEFEV-ISDSPYESLEIEiklsldsdesdsshLPPLVLKFTLPEDYPDEPPKISLSSP---WNLS 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 398366185 492 DYIKKQILTRLLHYLQEgnLIGDMLVYHIYEWLKENI 528
Cdd:pfam05773 77 DEQVLSLLEELEELAEE--NLGEVMIFELIEWLQENL 111
|
|
| UBA_YLR419W_like |
cd14271 |
UBA domain found in Saccharomyces cerevisiae putative ATP-dependent RNA helicase YLR419W and ... |
369-409 |
6.85e-18 |
|
UBA domain found in Saccharomyces cerevisiae putative ATP-dependent RNA helicase YLR419W and similar proteins; The group includes some uncharacterized hypothetical proteins which show a high level of sequence similarity with Saccharomyces cerevisiae putative ATP-dependent RNA helicase YLR419W. All family members contain a ubiquitin-associated (UBA) domain, RWD domain, DEAD-box (DEXDc), helicase superfamily c-terminal domain (HELICc), Helicase associated domain (HA2), and a C-terminal oligonucleotide/oligosaccharide-binding (OB)-fold.
Pssm-ID: 270457 Cd Length: 41 Bit Score: 78.20 E-value: 6.85e-18
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 398366185 369 RMIVERLTEIGVSSDEALLALQQNDMNENEAAGFLTREILP 409
Cdd:cd14271 1 RNMIERLTESGVSKDEALLALEECNFNEAEAAGKLTRSILP 41
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
883-977 |
9.22e-13 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 64.93 E-value: 9.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 883 LANKSNEADFMVLPLHSALTPEDQKRVFKKY-HGKRKVVVSTNIAETSITIDDCVATIDTGraksmfynpkdnttklieS 961
Cdd:smart00490 3 LAELLKELGIKVARLHGGLSQEEREEILDKFnNGKIKVLVATDVAERGLDLPGVDLVIIYD------------------L 64
|
90
....*....|....*.
gi 398366185 962 FISKAEVKQRRGRAGR 977
Cdd:smart00490 65 PWSPASYIQRIGRAGR 80
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
848-978 |
3.13e-12 |
|
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: 64.54 E-value: 3.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 848 QVVEYVHKRLKAANdNGSIIVFLPGVGEINkcCNLLANKSNeadFMVLPLHSALTPEDQKRVFKKY-HGKRKVVVSTNIA 926
Cdd:pfam00271 1 EKLEALLELLKKER-GGKVLIFSQTKKTLE--AELLLEKEG---IKVARLHGDLSQEEREEILEDFrKGKIDVLVATDVA 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 398366185 927 ETSITIDDCVATIDtgraksmfYNPKDNTTKLIesfiskaevkQRRGRAGRV 978
Cdd:pfam00271 75 ERGLDLPDVDLVIN--------YDLPWNPASYI----------QRIGRAGRA 108
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
620-763 |
5.95e-12 |
|
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: 64.73 E-value: 5.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 620 NEVVLITGETGSGKSTQVVQFILD-FLQKEKgdfgktKIVCTQPRRISAIGLAERVSDERcvTCGEEVGYVIRGVNK--- 695
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLlLLKKGK------KVLVLVPTKALALQTAERLRELF--GPGIRVAVLVGGSSAeer 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398366185 696 ---TKASTRIKFMTTGVLVRLLQNARTMLEN--TIVVIDEVHERSIDTDliVTLMKNLLHRVRGMK---IVLMSAT 763
Cdd:cd00046 73 eknKLGDADIIIATPDMLLNLLLREDRLFLKdlKLIIVDEAHALLIDSR--GALILDLAVRKAGLKnaqVILLSAT 146
|
|
| RWD |
smart00591 |
domain in RING finger and WD repeat containing proteins and DEXDc-like helicases subfamily ... |
431-529 |
2.32e-11 |
|
domain in RING finger and WD repeat containing proteins and DEXDc-like helicases subfamily related to the UBCc domain;
Pssm-ID: 214735 Cd Length: 107 Bit Score: 61.99 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 431 ELESLESIYEGCVMDAKEDSH---YTLNLIEK--------LKIKLKVYRTKNYPASLPGIVVSTFdknYKLPDYIKKQIL 499
Cdd:smart00591 1 ELEALESIYPEDFEVIDEDARipeITIKLSPSsdegedqyVSLTLQVKLPENYPDEAPPISLLNS---EGLSDEQLAELL 77
|
90 100 110
....*....|....*....|....*....|
gi 398366185 500 TRLLHYLQEgnLIGDMLVYHIYEWLKENIS 529
Cdd:smart00591 78 KKLEEIAEE--NLGEVMIFELVEKLQEFLS 105
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
610-768 |
5.24e-11 |
|
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: 62.65 E-value: 5.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 610 QKVIIDIINKNEVVLITGETGSGKSTqvvQFILDFLQKEKGDFGKTKIVCTQPRRISAIGLAERVSdERCVTCGEEVGYV 689
Cdd:pfam00270 4 QAEAIPAILEGRDVLVQAPTGSGKTL---AFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELK-KLGKGLGLKVASL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 690 IRGVNKTK-----ASTRIKFMTTGVLVRLLQNARTMLENTIVVIDEVHeRSIDTDLIVTLmKNLLHRVRGM-KIVLMSAT 763
Cdd:pfam00270 80 LGGDSRKEqleklKGPDILVGTPGRLLDLLQERKLLKNLKLLVLDEAH-RLLDMGFGPDL-EEILRRLPKKrQILLLSAT 157
|
....*
gi 398366185 764 VNVDL 768
Cdd:pfam00270 158 LPRNL 162
|
|
| HA2 |
smart00847 |
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ... |
1050-1134 |
3.82e-08 |
|
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: 51.89 E-value: 3.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 1050 IGLVDESDKsLTQLGQFISLMPVmDSKHGKLLIYGILFGCTDISVLLVSILGIGVlpfIGGFENREKIKKLLCKYES-RG 1128
Cdd:smart00847 2 LGALDDDGR-LTPLGRKMAELPL-DPRLAKMLLAAAEFGCLDEILTIVAMLSVGD---PRPKEKREDADAARRRFADpES 76
|
....*.
gi 398366185 1129 DLFAVL 1134
Cdd:smart00847 77 DHLTLL 82
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
610-773 |
1.19e-06 |
|
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350679 [Multi-domain] Cd Length: 181 Bit Score: 50.34 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 610 QKVIID-IINKNEVVLITGETGSGKSTQVVQFILDFLQKEKGdfgktKIVCTQPRRisAIGlAERVSD--ERCVTCGEEV 686
Cdd:cd17921 6 QREALRaLYLSGDSVLVSAPTSSGKTLIAELAILRALATSGG-----KAVYIAPTR--ALV-NQKEADlrERFGPLGKNV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 687 GYVIRGV---NKTKASTRIKFMTTGVLVRLLQNARTML--ENTIVVIDEVH-----ERSIDTDLIVTLMKNllhRVRGMK 756
Cdd:cd17921 78 GLLTGDPsvnKLLLAEADILVATPEKLDLLLRNGGERLiqDVRLVVVDEAHligdgERGVVLELLLSRLLR---INKNAR 154
|
170
....*....|....*...
gi 398366185 757 IVLMSATV-NVDLFKKFF 773
Cdd:cd17921 155 FVGLSATLpNAEDLAEWL 172
|
|
| RWD-RWDD4 |
cd23817 |
RWD domain of RWD domain-containing protein 4 (RWDD4) and related proteins; RWDD4, also called ... |
431-528 |
6.84e-06 |
|
RWD domain of RWD domain-containing protein 4 (RWDD4) and related proteins; RWDD4, also called protein FAM28A, is a target of the tumor suppressor MicroRNA (MiR)-506 in bladder cancer cells. Downregulation of RWDD4 suppresses bladder cancer cell proliferation, migration and invasion. RWDD4 has also been identified as a modifier of metastasis in human prostate cancer.
Pssm-ID: 467653 Cd Length: 104 Bit Score: 46.35 E-value: 6.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 431 ELESLESIYEGcvmDA--KEDSHYTLN--LIEKLKIK---LKVYRTKNYPASLPGIVVSTFdKNYKLPDYIKKQILTRLL 503
Cdd:cd23817 3 ELEVLLSIYEG---DEnfKQISDTTFQykYGEDGDPKsflLEISWPENYPEEPPIINLDAF-YNKHISSSVKEKIVSKLN 78
|
90 100
....*....|....*....|....*
gi 398366185 504 HYLQEgnLIGDMLVYHIYEWLKENI 528
Cdd:cd23817 79 EEAEQ--NLGSAMTYTLFEWAKENA 101
|
|
| RWD_RWDD3 |
cd23819 |
RWD domain of RWD domain-containing protein 3 (RWDD3) and related proteins; RWDD3, also called ... |
431-528 |
7.90e-06 |
|
RWD domain of RWD domain-containing protein 3 (RWDD3) and related proteins; RWDD3, also called RWD domain-containing sumoylation enhancer (RSUME), acts as an enhancer of SUMO conjugation and has no effect on ubiquitination. It increases protein sumoylation (a dynamic ubiquitin-like post translational modification) of several proteins including HIF1alpha and I-kappa-B, through direct interaction with UBC9. Its RWD domain is required for the sumoylation enhancement activity.
Pssm-ID: 467655 Cd Length: 106 Bit Score: 46.16 E-value: 7.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 431 ELESLESIY----EGCVMDAKEDSH-YTL-------NLIEKLKIKLKVYRTKNYPASLPGIVVSTfdknyklpDYIKKQI 498
Cdd:cd23819 2 ELSVLQAIFcgpgEFEVLSSSETSDgVSFkiqisveGFDEDIVLKLTFHLSPNYPSSLPDISVSS--------EQLTRAQ 73
|
90 100 110
....*....|....*....|....*....|..
gi 398366185 499 LTRLLHYLQE--GNLIGDMLVYHIYEWLKENI 528
Cdd:cd23819 74 CNDLQDSLLEyaNSLLGEPMVLELVLWLQENL 105
|
|
| OB_NTP_bind |
pfam07717 |
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ... |
1205-1342 |
6.53e-05 |
|
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: 42.62 E-value: 6.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 1205 LRAILTGAFYPHIARvqlpdvkylstssgaveKDPEAKmikywirseeyqdkleEYKTKISQEtqkvdledlplpatRAF 1284
Cdd:pfam07717 1 LRAALAAGLYPNVAR-----------------RDPKGK----------------GYTTLSDNQ--------------RVF 33
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 398366185 1285 IHPSSVLFStnsvnledakllsevdgpisrqskiPTVVKYPFVLFTTSQVTNKLYLRD 1342
Cdd:pfam07717 34 IHPSSVLFN-------------------------EKTFPPEWVVYQELVETTKVYIRT 66
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
721-940 |
8.90e-05 |
|
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 440816 [Multi-domain] Cd Length: 535 Bit Score: 47.00 E-value: 8.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 721 LENTIVVIDEVHerSIDTDLIvTLMKNLLHRVR--GMKIVLMSATvnvdlfkkfFPglatchiegrtfpitdyfleDILS 798
Cdd:COG1203 267 LANSVIILDEVQ--AYPPYML-ALLLRLLEWLKnlGGSVILMTAT---------LP--------------------PLLR 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 799 DLDFKIKREKalsyDDDSVDERNNDDQYLKPRADskfFTSGQINYDLLCQVVeyvhkrLKAANDNGSIIVflpgvgeink 878
Cdd:COG1203 315 EELLEAYELI----PDEPEELPEYFRAFVRKRVE---LKEGPLSDEELAELI------LEALHKGKSVLV---------- 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 879 CCN----------LLANKSNEADFMVlpLHSALTPEDQKRVFKK-----YHGKRKVVVSTNIAETSITID-DCV----AT 938
Cdd:COG1203 372 IVNtvkdaqelyeALKEKLPDEEVYL--LHSRFCPADRSEIEKEikerlERGKPCILVSTQVVEAGVDIDfDVVirdlAP 449
|
..
gi 398366185 939 ID 940
Cdd:COG1203 450 LD 451
|
|
| RWD_RWDD2 |
cd23829 |
RWD domain of RWD domain-containing protein 2A (RWDD2A), 2B (RWDD2B) and related proteins; ... |
430-532 |
3.37e-04 |
|
RWD domain of RWD domain-containing protein 2A (RWDD2A), 2B (RWDD2B) and related proteins; This subfamily includes RWDD2A, previously known as RWD domain-containing 2 (RWDD2) and RWDD2B, previously known in humans as chromosome 21 open reading frame (C21orf6). C21orf6 appears to be involved in monosomy 21 phenotype. The RWD domain may mediate protein-protein interactions.
Pssm-ID: 467663 Cd Length: 129 Bit Score: 42.18 E-value: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 430 QELESLESIY----------EGCVMDAKE----DSH--------YTLNL-IEKLKIKLKVYRT--KNYPASLPGIVV--S 482
Cdd:cd23829 7 SEIEMLQSMFpnegelklddPSAVADLKRflegDTDsplpsrleFTINLkIEEPKVKVELSVTlpHEYPSVPPEIFVrsD 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 398366185 483 TFDKNYKlpdyikKQILTRLLHYLQEgNLIGDMLVYHIYEWLKENISKII 532
Cdd:cd23829 87 SLSRSQQ------RQLNEDLSEYISS-LERGELCILQIVQWLQDNASSYI 129
|
|
| UBA |
smart00165 |
Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 ... |
369-403 |
5.43e-04 |
|
Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 is known to bind ubiquitin.
Pssm-ID: 197551 [Multi-domain] Cd Length: 37 Bit Score: 38.62 E-value: 5.43e-04
10 20 30
....*....|....*....|....*....|....*
gi 398366185 369 RMIVERLTEIGVSSDEALLALQQNDMNENEAAGFL 403
Cdd:smart00165 2 EEKIDQLLEMGFSREEALKALRAANGNVERAAEYL 36
|
|
| RWD_DRWD_ELF-like |
cd11605 |
RWD, DRWD, and ELF domain family; The family includes the RWD, double-RWD (DRWD), and ELF ... |
434-524 |
6.49e-04 |
|
RWD, DRWD, and ELF domain family; The family includes the RWD, double-RWD (DRWD), and ELF domains. They belong to the ubiquitin-conjugating (UBC) superfamily that represents a structural domain with an alpha-beta(4)-alpha(3) core fold. The RWD domain (named after three major RWD-containing proteins: RING finger, WD-repeat-containing proteins and DEXD-like helicases) mediates protein-protein interactions in a variety of pathways in eukaryotes. The DRWD domain is responsible for substrate binding. It is involved in interactions with other kinetochore proteins. The ELF (N-terminal E2-like fold) domain is found in all Fanconi anemia group L protein (FANCL) homologs. It is required to promote efficient DNA damage-induced FANCD2 (Fanconi anemia group D2 protein) monoubiquitination in vertebrate cells.
Pssm-ID: 467641 Cd Length: 94 Bit Score: 40.24 E-value: 6.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 434 SLESIYEGC--VMDAKEDSHYTLNL-----IEKLKIKLKVYRTKNY-PASLPGIVVSTFdknyKLPDYIKKQILTRLLHy 505
Cdd:cd11605 1 ALESIYGDEleVLSDDSPLRFSIRLspeeeEDDPPLELEFTLPPGYpPEEPPLITLRSP----KLSSAERLSLLKLELE- 75
|
90
....*....|....*....
gi 398366185 506 LQEGNLIGDMLVYHIYEWL 524
Cdd:cd11605 76 EAAEENLGEPMLFDLVEAL 94
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
721-763 |
1.74e-03 |
|
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase responsible for degradation of dsDNA. The two enzymatic units of Cas3, a histidine-aspartate (HD) nuclease and a Superfamily 2 (SF2) helicase, may be expressed from separate genes as Cas3' (SF2 helicase) and Cas3'' (HD nuclease) or may be fused as a single HD-SF2 polypeptide. The nucleolytic activity of most Cas3 enzymes is transition metal ion-dependent. Cas3 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: 350688 [Multi-domain] Cd Length: 186 Bit Score: 41.12 E-value: 1.74e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 398366185 721 LENTIVVIDEVHerSIDTDLIVTLMKNLLHRVRGM--KIVLMSAT 763
Cdd:cd17930 129 LANSVVVLDEVQ--AYDPEYMALLLKALLELLGELggPVVLMTAT 171
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
629-1057 |
1.81e-03 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 42.70 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 629 TGSGKSTqvvqFILDFLQKEKGDfGKTKIVCtqPRRISAIGLAERVSDERcvtcgeevGYVIRGVNKTKASTRIKFMTTG 708
Cdd:COG1061 109 TGTGKTV----LALALAAELLRG-KRVLVLV--PRRELLEQWAEELRRFL--------GDPLAGGGKKDSDAPITVATYQ 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 709 VLVRLLQNARTMLENTIVVIDEVHERSIDTdlivtlMKNLLHRVRGMKIVLMSATV----NVDLFKKFFPGLATchiegr 784
Cdd:COG1061 174 SLARRAHLDELGDRFGLVIIDEAHHAGAPS------YRRILEAFPAAYRLGLTATPfrsdGREILLFLFDGIVY------ 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 785 TFPITDYFLEDILSDLDFKIkrekalsYDDDSVDERNNDDQyLKPRADSKFFTSGQINYDLLCQVVEYVHKRLKaandng 864
Cdd:COG1061 242 EYSLKEAIEDGYLAPPEYYG-------IRVDLTDERAEYDA-LSERLREALAADAERKDKILRELLREHPDDRK------ 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 865 sIIVFLPGVGEinkcCNLLANKSNEADFMVLPLHSALTPEDQKRVFKKY-HGKRKVVVSTNIAETSITIDDC-VATIDTG 942
Cdd:COG1061 308 -TLVFCSSVDH----AEALAELLNEAGIRAAVVTGDTPKKEREEILEAFrDGELRILVTVDVLNEGVDVPRLdVAILLRP 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 943 raksmfynpkdntTKliesfiSKAEVKQRRGRAGRVREGLSYKLFsknlYenDMISMPIPEIKRIPLESLYLSVKAMGIK 1022
Cdd:COG1061 383 -------------TG------SPREFIQRLGRGLRPAPGKEDALV----Y--DFVGNDVPVLEELAKDLRDLAGYRVEFL 437
|
410 420 430
....*....|....*....|....*....|....*
gi 398366185 1023 DVKAFLSTALDAPPLPALQKAERILTTIGLVDESD 1057
Cdd:COG1061 438 DEEESEELALLIAVKPALEVKGELEEELLEELELL 472
|
|
| RWD_GCN2 |
cd23823 |
RWD domain of eIF-2-alpha kinase GCN2 and related proteins; GCN2 (EC 2.7.11.1), also called ... |
430-527 |
3.25e-03 |
|
RWD domain of eIF-2-alpha kinase GCN2 and related proteins; GCN2 (EC 2.7.11.1), also called eukaryotic translation initiation factor 2-alpha kinase 4 (EIF2AK4), acts as a metabolic-stress sensing protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (EIF2S1/eIF-2-alpha) in response to low amino acid availability. It also plays a role in modulating the adaptive immune response to yellow fever virus infection and promotes dendritic cells to initiate autophagy and antigene presentation to both CD4(+) and CD8(+) T-cells under amino acid starvation.
Pssm-ID: 467659 Cd Length: 117 Bit Score: 38.74 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 430 QELESLESIYEGCVMD------AKEDSHYTLNL--------IEKLKIKLKVYRTKNYPASLPGIVVstfdKNYK-LPDYI 494
Cdd:cd23823 6 EELEALQSIYGDDFEDlsskkaVWSPPEFRIRLrpqegeseENHVSVDLHVKFPPTYPDVPPEIEL----ENVKgLSDEQ 81
|
90 100 110
....*....|....*....|....*....|....*..
gi 398366185 495 KKQILTRLLHYLQEgnLIGDMLVY----HIYEWLKEN 527
Cdd:cd23823 82 LEELLKELEELAKE--LLGEEMIFelaeAVQEFLEEH 116
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
608-650 |
3.98e-03 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 39.67 E-value: 3.98e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 398366185 608 KKQKVIIDI---INKNEVVLITGETGSGKSTqVVQFILDFLQKEKG 650
Cdd:cd03228 13 RPKPVLKDVsltIKPGEKVAIVGPSGSGKST-LLKLLLRLYDPTSG 57
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
611-772 |
4.27e-03 |
|
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350781 [Multi-domain] Cd Length: 206 Bit Score: 40.03 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 611 KVIIDIINKNEVVLITGETGSGKSTQVVQFILDFLQK-EKGDFGKTKIVCTQPrrISAIgLAERVSDER------CVTCG 683
Cdd:cd18023 8 EVFPDLLYSDKNFVVSAPTGSGKTVLFELAILRLLKErNPLPWGNRKVVYIAP--IKAL-CSEKYDDWKekfgplGLSCA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 684 EEVG-------YVIRGVN-------KTKASTRiKFMTTGVLVRLLQnartmlentIVVIDEVH----ERSIDTDLIVTLM 745
Cdd:cd18023 85 ELTGdtemddtFEIQDADiilttpeKWDSMTR-RWRDNGNLVQLVA---------LVLIDEVHiikeNRGATLEVVVSRM 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 398366185 746 KnLLHR--------VRGMKIVLMSATV-NVDLFKKF 772
Cdd:cd18023 155 K-TLSSsselrgstVRPMRFVAVSATIpNIEDLAEW 189
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
918-977 |
5.10e-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: 37.30 E-value: 5.10e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 918 KVVVSTNIAETSITIDDCVATIDTGRaksmfynpkdnttkliesFISKAEVKQRRGRAGR 977
Cdd:cd18785 24 EILVATNVLGEGIDVPSLDTVIFFDP------------------PSSAASYIQRVGRAGR 65
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
619-755 |
7.53e-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: 38.51 E-value: 7.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366185 619 KNEVVLITGETGSGKSTqVVQFILDFLQKEKGDFgktkivctqpRRISAIGLAERVSDERCVTCGEEVGYVIRGVNK-TK 697
Cdd:smart00382 1 PGEVILIVGPPGSGKTT-LARALARELGPPGGGV----------IYIDGEDILEEVLDQLLLIIVGGKKASGSGELRlRL 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398366185 698 ASTRIKFMTTGVLV-----RLLQNARTMLENTIVVIDEVHERSIDTDLIVTLMKNLLHRVRGM 755
Cdd:smart00382 70 ALALARKLKPDVLIldeitSLLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPA 132
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
608-635 |
8.83e-03 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 39.37 E-value: 8.83e-03
10 20 30
....*....|....*....|....*....|.
gi 398366185 608 KKQKVIIDI---INKNEVVLITGETGSGKST 635
Cdd:cd03225 12 GARPALDDIsltIKKGEFVLIVGPNGSGKST 42
|
|
| |
