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Conserved domains on  [gi|2462581889|ref|XP_054180151|]
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3'-5' exoribonuclease HELZ2 isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEXXc_HELZ2-C cd18040
C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ...
2180-2454 1.41e-150

C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known as PPAR-alpha-interacting complex protein 285 or PRIC285 and PPAR-gamma DBD-interacting protein 1 or PDIP1) acts as a transcriptional coactivator for a number of nuclear receptors including PPARA, PPARG, THRA, THRB and RXRA. It 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: 350798 [Multi-domain]  Cd Length: 271  Bit Score: 468.16  E-value: 1.41e-150
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2180 KLNPSQNVAVREALEKPFTVIQGPPGTGKTIVGLHIVFWFHKSNQEQVQPGGpprgeKRLGGPCILYCGPSNKSVDVLAG 2259
Cdd:cd18040      1 KLNPSQNHAVRTALTKPFTLIQGPPGTGKTVTGVHIAYWFAKQNREIQSVSG-----EGDGGPCVLYCGPSNKSVDVVAE 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2260 LLLRRMELKPLRVYSEQAEASEFPVPRVGSRKLlRKSPREGRPNQSLRSITLHHRIRQAPNPYSSEIKAFDTRLQR-GEL 2338
Cdd:cd18040     76 LLLKVPGLKILRVYSEQIETTEYPIPNEPRHPN-KKSERESKPNSELSSITLHHRIRQPSNPHSQQIKAFEARFERtQEK 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2339 FSREDLVWYKKVLWEARKFELDRHEVILCTCSCAASASLK-ILDVRQILVDEAGMATEPETLIPLVQFPQAEKVVLLGDH 2417
Cdd:cd18040    155 ITEEDIKTYKILIWEARFEELETVDVILCTCSEAASQKMRtHANVKQCIVDECGMCTEPESLIPIVSAPRAEQVVLIGDH 234
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 2462581889 2418 KQLRPVVKNERLQNLGLDRSLFERYHEDAHMLDTQYR 2454
Cdd:cd18040    235 KQLRPVVQNKEAQKLGLGRSLFERYAEKACMLDTQYR 271
DEXXQc_HELZ2-N cd18076
N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ...
514-744 5.19e-149

N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known as PPAR-alpha-interacting complex protein 285 or PRIC285 and PPAR-gamma DBD-interacting protein 1 or PDIP1) acts as a transcriptional coactivator for a number of nuclear receptors including PPARA, PPARG, THRA, THRB, and RXRA. It 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: 350834 [Multi-domain]  Cd Length: 230  Bit Score: 461.67  E-value: 5.19e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  514 RGNRKQELAVALIAGWGPGdGRRVPPLLIYGPFGTGKTYTLAMASLEVIRRPETKVLICTHTNSAADIYIREYFHSHVSG 593
Cdd:cd18076      1 AGNNKQQLAFNFIAGKPSE-ARFVPPLLIYGPFGTGKTFTLAMAALEVIREPGTKVLICTHTNSAADIYIREYFHPYVDK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  594 GHPEATPLRVMYTDRPLSQTDPVTLQYCCLTDDRQAFRPPTRAELARHRVVVTTTSQARELRVPVGFFSHILIDEAAQML 673
Cdd:cd18076     80 GHPEARPLRIKATDRPNAITDPDTITYCCLTKDRQCFRLPTRDELDFHNIVITTTAMAFNLHVLSGFFTHIFIDEAAQML 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462581889  674 ECEALTPLAYASHGTRLVLAGDHMQVTPRLFSVARARAAEHTLLHRLFLCYQQETHEVARQSRLVFHENYR 744
Cdd:cd18076    160 ECEALIPLSYAGPKTRVVLAGDHMQMTPKLFSVADYNRANHTLLNRLFHYYQGEKHEVAVKSRVIFSENYR 230
AAA_12 pfam13087
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
2434-2639 1.41e-61

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.


:

Pssm-ID: 463780 [Multi-domain]  Cd Length: 196  Bit Score: 209.71  E-value: 1.41e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2434 LDRSLFER----YHEDAHMLDTQYRMHEGICAFPSVAFYKSKLKTWQGLR-RPPSVLGHAGKESCPVIFGHVQGHErsll 2508
Cdd:pfam13087    1 LDRSLFERlqelGPSAVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAeRPLPDDFHLPDPLGPLVFIDVDGSE---- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2509 vSTDEGNENSKANLEEVAEVVRITKQLTLGRTVEPQDIAVLTPYNAQASEISKALRRE--GIAGVAVSSITKSQGSEWRY 2586
Cdd:pfam13087   77 -EEESDGGTSYSNEAEAELVVQLVEKLIKSGPEEPSDIGVITPYRAQVRLIRKLLKRKlgGKLEIEVNTVDGFQGREKDV 155
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462581889 2587 VLVSTVRTCAKSDldqrptkswlkkfLGFVVDPNQVNVAVTRAQEGLCLIGDH 2639
Cdd:pfam13087  156 IIFSCVRSNEKGG-------------IGFLSDPRRLNVALTRAKRGLIIVGNA 195
RNB smart00955
This domain is the catalytic domain of ribonuclease II;
1334-1693 1.64e-60

This domain is the catalytic domain of ribonuclease II;


:

Pssm-ID: 214935 [Multi-domain]  Cd Length: 286  Bit Score: 210.20  E-value: 1.64e-60
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  1334 REDCRAFLTFTVDPQGACNLDDALSVRDLGP-RCEVAVHITDVASFVPRDGVLDVEARRQGAAFYAPGRePVPMLPASLC 1412
Cdd:smart00955    1 RVDLRDLPLFTIDPEDAKDIDDAVSVEKLDNgGYRLGVHIADVSHYVKPGSALDREARKRGTSVYLPDR-VIPMLPEELS 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  1413 QDVLSLLPGRDRLAISLFLTMEKASGQLKSLRFAPSVVQSDRQLSYEEAEEVIRQHpgagrelparldsvdacvvaacyf 1492
Cdd:smart00955   80 NGLCSLNPGEDRLALSVEMTLDADGGEILDYEFYRSVIRSKARLTYEEVDAILEKI------------------------ 135
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  1493 srllrrhrlrsdcfyeQPDEDGTLG------FRAAHIMVKEYMIQFNRLVAEFLVGSECTrtvTPLRWQPAPR----SQQ 1562
Cdd:smart00955  136 ----------------VLDEEGKIEdivpreRNDAHSLVEEFMILANEAVARFLAKNGIP---GLYRVHEGPDpeklAEL 196
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  1563 LKALCEKHGDRVPLSlhlghhlhggggsppDTRLHLLASLWKqvqfaARTQDYEQMVDLVttddmhpflapagrdLRKAL 1642
Cdd:smart00955  197 LKEFLALLGLLLLGG---------------DGPKALAKLLEK-----IRDSPEERLLELL---------------LLRSM 241
                           330       340       350       360       370
                    ....*....|....*....|....*....|....*....|....*....|.
gi 2462581889  1643 ERSAFGRcarghqQQGGHYSLQVDWYTWATSPIRRYLDVVLQRQILLALGH 1693
Cdd:smart00955  242 PHAEYSV------DNSGHFGLALDAYTHFTSPIRRYPDLIVHRQLKAALRG 286
AAA_12 super family cl38387
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
715-915 1.02e-36

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.


The actual alignment was detected with superfamily member pfam13087:

Pssm-ID: 463780 [Multi-domain]  Cd Length: 196  Bit Score: 138.45  E-value: 1.02e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  715 TLLHRLFLCYQQethevarqSRLVFHENYRCTDAIVSFISRHFYVAK-GNPIHARGKVPPHPRH-----YPLMFCHVAGN 788
Cdd:pfam13087    4 SLFERLQELGPS--------AVVMLDTQYRMHPEIMEFPSKLFYGGKlKDGPSVAERPLPDDFHlpdplGPLVFIDVDGS 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  789 PDRDM-SMASWLNLAEIAQVVEKVQEAYNTWPSCWggreqRCICVVS-HGAQVSALRQELRRRDLG--QVSVGSFEILPG 864
Cdd:pfam13087   76 EEEESdGGTSYSNEAEAELVVQLVEKLIKSGPEEP-----SDIGVITpYRAQVRLIRKLLKRKLGGklEIEVNTVDGFQG 150
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462581889  865 RQFRVVVLSTVHTCQSllspGALApeFFTDARVLNTVLTRAQSQLVVVGDA 915
Cdd:pfam13087  151 REKDVIIFSCVRSNEK----GGIG--FLSDPRRLNVALTRAKRGLIIVGNA 195
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
106-915 5.88e-33

Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];


:

Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 139.88  E-value: 5.88e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  106 AHSAQELQEWVRRTQAVELRGQAAWQDGLVPYQERLLAEYQRSSSEVLVLAETLDGVRVTCNQPLMYQAQERKTQYSWTF 185
Cdd:COG1112      3 ALLLDAARALLALLALALLALLLALALLLDLLLLLLLAAALLLLALALALLLLALRALELLDLLAALALLLLLLLLDAEL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  186 AVHSEEPLLHVALLKQEPGADFSLVAPGLPPGRLYARGERFRVPSSTADFQVGVRVQAASFGTFEQWVVFDFGRRPVLLQ 265
Cdd:COG1112     83 LLLALRALLLLLAAELLLLLLLLLLLAALLLALAALLLALALLLLALALLALLALLLAELLDLLAALAALAALLAALLLL 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  266 KLGLQLGQGRRPGPCRNLALGHPEEMERWHTGNRHVVPGV-ERTAEQTALMAKYKGPALALEFNRSSVASGPISPTNYRQ 344
Cdd:COG1112    163 LLLLAALLLLDLRLLALLELLLAAALALALLALLALALEDeLALLLLLLLLALLLLLALLLLLDALLLLLAALALLALAL 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  345 RMHQFLYEEEAAQQQLVAKLTLRGQVFLKTALQTPALNMLFAPPGALYAEVPVPSSLMPDTDQGFLLGRAVSTALVAPVP 424
Cdd:COG1112    243 LLALLLLLLALLLLAALALLRAALRLDLLAALELLAALSLALLALLAALALALLLLAALALLLALALAALLALLALLALL 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  425 APDNTVFEVRLERRASSEQALWLLLPARCCLALGLQPEARLVLEVQFQIDPMTFRLWHQAVDTLPEEQLVVPDLPTCALP 504
Cdd:COG1112    323 AARLAAALAALLLLLLLEELALLAALLLLLELALLRLLAALLLALALLLLLALEELLLLALLRLLAEGLALLLLLLLAAL 402
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  505 RPWSVPPLRRGNRKQELAVALIAGWGPGDGRRVPPLLIYGPFGTGKTYTLAMASLEVIRRPETKVLIcTHTNSAADIYIR 584
Cdd:COG1112    403 LRLARALLLLALLLAAAAAALAALLLLALALLAALLALLLLLAAALAALLALLLLLLLALAALLLLL-AAAAALLALALL 481
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  585 EYFHSHVSGGHPEATPLRVMYTDRPLSQTDPVTLQyccLTDDRQAFRPPTRAELARHRVVVTTTSQ-ARELRVPVGFFSH 663
Cdd:COG1112    482 ESLLEELIEEHPEELEKLIAELREAARLRRALRRE---LKKRRELRKLLWDALLELAPVVGMTPASvARLLPLGEGSFDL 558
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  664 ILIDEAAQMLECEALTPLAYAShgtRLVLAGDHMQVTPRLFSVARARAAEH----TLLHRLFLCYQQethevaRQSRLVF 739
Cdd:COG1112    559 VIIDEASQATLAEALGALARAK---RVVLVGDPKQLPPVVFGEEAEEVAEEgldeSLLDRLLARLPE------RGVMLRE 629
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  740 HenYRCTDAIVSFISRHFYvakGNPIHARGKVPPHPR---HYPLMFCHVAGNPDRDMSmaSWLNLAEIAQVVEKVQEAYN 816
Cdd:COG1112    630 H--YRMHPEIIAFSNRLFY---DGKLVPLPSPKARRLadpDSPLVFIDVDGVYERRGG--SRTNPEEAEAVVELVRELLE 702
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  817 TWPscwggrEQRCICVVS-HGAQVSALRQELRRRDLG---QVSVGSFEILPGRQFRVVVLSTVhtcqslLSPGALAPEFF 892
Cdd:COG1112    703 DGP------DGESIGVITpYRAQVALIRELLREALGDglePVFVGTVDRFQGDERDVIIFSLV------YSNDEDVPRNF 770
                          810       820
                   ....*....|....*....|....*..
gi 2462581889  893 ----TDARVLNTVLTRAQSQLVVVGDA 915
Cdd:COG1112    771 gflnGGPRRLNVAVSRARRKLIVVGSR 797
zf-C2H2_jaz pfam12171
Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, ...
39-64 4.64e-03

Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, and is approximately 30 amino acids in length. The mammalian members of this group occur multiple times along the protein, joined by flexible linkers, and are referred to as JAZ - dsRNA-binding ZF protein - zinc-fingers. The JAZ proteins are expressed in all tissues tested and localize in the nucleus, particularly the nucleolus. JAZ preferentially binds to double-stranded (ds) RNA or RNA/DNA hybrids rather than DNA. In addition to binding double-stranded RNA, these zinc-fingers are required for nucleolar localization.


:

Pssm-ID: 432381 [Multi-domain]  Cd Length: 27  Bit Score: 36.76  E-value: 4.64e-03
                           10        20
                   ....*....|....*....|....*.
gi 2462581889   39 QLYCPACLVTCHSQEAFENHCASSEH 64
Cdd:pfam12171    1 QFYCVLCDKYFKSENALQNHLKSKKH 26
 
Name Accession Description Interval E-value
DEXXc_HELZ2-C cd18040
C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ...
2180-2454 1.41e-150

C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known as PPAR-alpha-interacting complex protein 285 or PRIC285 and PPAR-gamma DBD-interacting protein 1 or PDIP1) acts as a transcriptional coactivator for a number of nuclear receptors including PPARA, PPARG, THRA, THRB and RXRA. It 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: 350798 [Multi-domain]  Cd Length: 271  Bit Score: 468.16  E-value: 1.41e-150
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2180 KLNPSQNVAVREALEKPFTVIQGPPGTGKTIVGLHIVFWFHKSNQEQVQPGGpprgeKRLGGPCILYCGPSNKSVDVLAG 2259
Cdd:cd18040      1 KLNPSQNHAVRTALTKPFTLIQGPPGTGKTVTGVHIAYWFAKQNREIQSVSG-----EGDGGPCVLYCGPSNKSVDVVAE 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2260 LLLRRMELKPLRVYSEQAEASEFPVPRVGSRKLlRKSPREGRPNQSLRSITLHHRIRQAPNPYSSEIKAFDTRLQR-GEL 2338
Cdd:cd18040     76 LLLKVPGLKILRVYSEQIETTEYPIPNEPRHPN-KKSERESKPNSELSSITLHHRIRQPSNPHSQQIKAFEARFERtQEK 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2339 FSREDLVWYKKVLWEARKFELDRHEVILCTCSCAASASLK-ILDVRQILVDEAGMATEPETLIPLVQFPQAEKVVLLGDH 2417
Cdd:cd18040    155 ITEEDIKTYKILIWEARFEELETVDVILCTCSEAASQKMRtHANVKQCIVDECGMCTEPESLIPIVSAPRAEQVVLIGDH 234
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 2462581889 2418 KQLRPVVKNERLQNLGLDRSLFERYHEDAHMLDTQYR 2454
Cdd:cd18040    235 KQLRPVVQNKEAQKLGLGRSLFERYAEKACMLDTQYR 271
DEXXQc_HELZ2-N cd18076
N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ...
514-744 5.19e-149

N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known as PPAR-alpha-interacting complex protein 285 or PRIC285 and PPAR-gamma DBD-interacting protein 1 or PDIP1) acts as a transcriptional coactivator for a number of nuclear receptors including PPARA, PPARG, THRA, THRB, and RXRA. It 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: 350834 [Multi-domain]  Cd Length: 230  Bit Score: 461.67  E-value: 5.19e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  514 RGNRKQELAVALIAGWGPGdGRRVPPLLIYGPFGTGKTYTLAMASLEVIRRPETKVLICTHTNSAADIYIREYFHSHVSG 593
Cdd:cd18076      1 AGNNKQQLAFNFIAGKPSE-ARFVPPLLIYGPFGTGKTFTLAMAALEVIREPGTKVLICTHTNSAADIYIREYFHPYVDK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  594 GHPEATPLRVMYTDRPLSQTDPVTLQYCCLTDDRQAFRPPTRAELARHRVVVTTTSQARELRVPVGFFSHILIDEAAQML 673
Cdd:cd18076     80 GHPEARPLRIKATDRPNAITDPDTITYCCLTKDRQCFRLPTRDELDFHNIVITTTAMAFNLHVLSGFFTHIFIDEAAQML 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462581889  674 ECEALTPLAYASHGTRLVLAGDHMQVTPRLFSVARARAAEHTLLHRLFLCYQQETHEVARQSRLVFHENYR 744
Cdd:cd18076    160 ECEALIPLSYAGPKTRVVLAGDHMQMTPKLFSVADYNRANHTLLNRLFHYYQGEKHEVAVKSRVIFSENYR 230
AAA_12 pfam13087
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
2434-2639 1.41e-61

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.


Pssm-ID: 463780 [Multi-domain]  Cd Length: 196  Bit Score: 209.71  E-value: 1.41e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2434 LDRSLFER----YHEDAHMLDTQYRMHEGICAFPSVAFYKSKLKTWQGLR-RPPSVLGHAGKESCPVIFGHVQGHErsll 2508
Cdd:pfam13087    1 LDRSLFERlqelGPSAVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAeRPLPDDFHLPDPLGPLVFIDVDGSE---- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2509 vSTDEGNENSKANLEEVAEVVRITKQLTLGRTVEPQDIAVLTPYNAQASEISKALRRE--GIAGVAVSSITKSQGSEWRY 2586
Cdd:pfam13087   77 -EEESDGGTSYSNEAEAELVVQLVEKLIKSGPEEPSDIGVITPYRAQVRLIRKLLKRKlgGKLEIEVNTVDGFQGREKDV 155
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462581889 2587 VLVSTVRTCAKSDldqrptkswlkkfLGFVVDPNQVNVAVTRAQEGLCLIGDH 2639
Cdd:pfam13087  156 IIFSCVRSNEKGG-------------IGFLSDPRRLNVALTRAKRGLIIVGNA 195
RNB smart00955
This domain is the catalytic domain of ribonuclease II;
1334-1693 1.64e-60

This domain is the catalytic domain of ribonuclease II;


Pssm-ID: 214935 [Multi-domain]  Cd Length: 286  Bit Score: 210.20  E-value: 1.64e-60
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  1334 REDCRAFLTFTVDPQGACNLDDALSVRDLGP-RCEVAVHITDVASFVPRDGVLDVEARRQGAAFYAPGRePVPMLPASLC 1412
Cdd:smart00955    1 RVDLRDLPLFTIDPEDAKDIDDAVSVEKLDNgGYRLGVHIADVSHYVKPGSALDREARKRGTSVYLPDR-VIPMLPEELS 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  1413 QDVLSLLPGRDRLAISLFLTMEKASGQLKSLRFAPSVVQSDRQLSYEEAEEVIRQHpgagrelparldsvdacvvaacyf 1492
Cdd:smart00955   80 NGLCSLNPGEDRLALSVEMTLDADGGEILDYEFYRSVIRSKARLTYEEVDAILEKI------------------------ 135
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  1493 srllrrhrlrsdcfyeQPDEDGTLG------FRAAHIMVKEYMIQFNRLVAEFLVGSECTrtvTPLRWQPAPR----SQQ 1562
Cdd:smart00955  136 ----------------VLDEEGKIEdivpreRNDAHSLVEEFMILANEAVARFLAKNGIP---GLYRVHEGPDpeklAEL 196
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  1563 LKALCEKHGDRVPLSlhlghhlhggggsppDTRLHLLASLWKqvqfaARTQDYEQMVDLVttddmhpflapagrdLRKAL 1642
Cdd:smart00955  197 LKEFLALLGLLLLGG---------------DGPKALAKLLEK-----IRDSPEERLLELL---------------LLRSM 241
                           330       340       350       360       370
                    ....*....|....*....|....*....|....*....|....*....|.
gi 2462581889  1643 ERSAFGRcarghqQQGGHYSLQVDWYTWATSPIRRYLDVVLQRQILLALGH 1693
Cdd:smart00955  242 PHAEYSV------DNSGHFGLALDAYTHFTSPIRRYPDLIVHRQLKAALRG 286
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
2254-2658 7.68e-52

Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 198.81  E-value: 7.68e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2254 VDVLAGLLLRRMELKPLRVYSEQAEASEFPVPRVGSRKLLRKSPREGRPNQSLRSITLHHRIRQAPNPYSSEIKAFDTRL 2333
Cdd:COG1112    428 LLALALLAALLALLLLLAAALAALLALLLLLLLALAALLLLLAAAAALLALALLESLLEELIEEHPEELEKLIAELREAA 507
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2334 QRGELFSREdLVWYKKVLWEARKFELDRHEVILCTC-SCAASASLKILDVRQILVDEAGMATEPETLIPLVQfpqAEKVV 2412
Cdd:COG1112    508 RLRRALRRE-LKKRRELRKLLWDALLELAPVVGMTPaSVARLLPLGEGSFDLVIIDEASQATLAEALGALAR---AKRVV 583
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2413 LLGDHKQLRPVVKNER---LQNLGLDRSLFER----YHEDAHMLDTQYRMHEGICAFPSVAFYKSKLKTwqgLRRPPSVl 2485
Cdd:COG1112    584 LVGDPKQLPPVVFGEEaeeVAEEGLDESLLDRllarLPERGVMLREHYRMHPEIIAFSNRLFYDGKLVP---LPSPKAR- 659
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2486 gHAGKESCPVIFGHVQGhersllvsTDEGNENSKANLEEVAEVVRITKQLtLGRTVEPQDIAVLTPYNAQASEISKALRR 2565
Cdd:COG1112    660 -RLADPDSPLVFIDVDG--------VYERRGGSRTNPEEAEAVVELVREL-LEDGPDGESIGVITPYRAQVALIRELLRE 729
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2566 E---GIAGVAVSSITKSQGSEWRYVLVSTVRTcakSDLDQRPTKSWLKKflgfvvDPNQVNVAVTRAQEGLCLIGDHLLL 2642
Cdd:COG1112    730 AlgdGLEPVFVGTVDRFQGDERDVIIFSLVYS---NDEDVPRNFGFLNG------GPRRLNVAVSRARRKLIVVGSRELL 800
                          410
                   ....*....|....*....
gi 2462581889 2643 RCCP---LWRSLLDFCEAQ 2658
Cdd:COG1112    801 DSDPstpALKRLLEYLERA 819
TIGR00376 TIGR00376
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
2181-2665 1.55e-51

DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of this family have been characterized as binding certain single-stranded G-rich DNA sequences (GGGGT and GGGCT). A number of related proteins are characterized as helicases. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273041 [Multi-domain]  Cd Length: 636  Bit Score: 194.65  E-value: 1.55e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2181 LNPSQNVAVREAL-EKPFTVIQGPPGTGKTIVGLHIVfwfhksnQEQVQpggppRGEKrlggpcILYCGPSNKSVDVlag 2259
Cdd:TIGR00376  158 LNESQKEAVLFALsSKDLFLIHGPPGTGKTRTVVELI-------RQLVK-----RGLR------VLVTAPSNIAVDN--- 216
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2260 lLLRRMELKPLRVYseqaeasefpvpRVGSRKLLRKSPREgrpnQSLRSITLHHRIRQAPNPYSSEIKAF---------- 2329
Cdd:TIGR00376  217 -LLERLALCDQKIV------------RLGHPARLLKSNKQ----HSLDYLIENHPKYQIVADIREKIDELieernkktkp 279
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2330 ---------DTRLQRGELFSRE-----DLVWYKKVLWEARKFELDR----------------HEVILCTCSCAASASLKI 2379
Cdd:TIGR00376  280 spqkrrglsDIKILRKALKKREargieSLKIASMAEWIETNKSIDRllkllpeseerimneiLAESDATNSMAGSEILNG 359
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2380 LDVRQILVDEAGMATEPETLIPLVqfpQAEKVVLLGDHKQLRPVVKNErlQNLGLDRSLFER----YHEDAHMLDTQYRM 2455
Cdd:TIGR00376  360 QYFDVAVIDEASQAMEPSCLIPLL---KARKLILAGDHKQLPPTILSH--DAEELSLTLFERlikeYPERSRTLNVQYRM 434
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2456 HEGICAFPSVAFYKSKLK-----TWQGLRRPPSVlgHAGKESC------PVIFGHVQGHERSLLvstDEGNENSKANLEE 2524
Cdd:TIGR00376  435 NQKIMEFPSREFYNGKLTahesvANILLRDLPKV--EATESEDdletgiPLLFIDTSGCELFEL---KEADSTSKYNPGE 509
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2525 VAEVVRITKQLtLGRTVEPQDIAVLTPYNAQASEISKALRREGIaGVAVSSITKSQGSEWRYVLVSTVRTCAKSDldqrp 2604
Cdd:TIGR00376  510 AELVSEIIQAL-VKMGVPANDIGVITPYDAQVDLLRQLLEHRHI-DIEVSSVDGFQGREKEVIIISFVRSNRKGE----- 582
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462581889 2605 tkswlkkfLGFVVDPNQVNVAVTRAQEGLCLIGDHLLLRCCPLWRSLLDFCEAQQTLVPAG 2665
Cdd:TIGR00376  583 --------VGFLKDLRRLNVALTRARRKLIVIGDSRTLSNHKFYKRLIEWCKQHGEVREAF 635
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
2455-2656 5.03e-50

C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family includes UPF1, HELZ, Mov10L1, Aquarius, IGHMBP2 (SMUBP2), and similar proteins. They are DEAD-like helicases belonging to superfamily (SF)1, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF2 helicases, SF1 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: 350195 [Multi-domain]  Cd Length: 184  Bit Score: 176.27  E-value: 5.03e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2455 MHEGICAFPSVAFYKSKLKTWQGLRRPPSVLgHAGKESCPVIFGHVQGHERSllvstdEGNENSKANLEEVAEVVRITKQ 2534
Cdd:cd18808      1 MHPEISEFPSKLFYEGKLKAGVSVAARLNPP-PLPGPSKPLVFVDVSGGEER------EESGTSKSNEAEAELVVELVKY 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2535 LtLGRTVEPQDIAVLTPYNAQASEISKALRREGIA--GVAVSSITKSQGSEWRYVLVSTVRTCAKsdldqrptkswlKKF 2612
Cdd:cd18808     74 L-LKSGVKPSSIGVITPYRAQVALIRELLRKRGGLleDVEVGTVDNFQGREKDVIILSLVRSNES------------GGS 140
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 2462581889 2613 LGFVVDPNQVNVAVTRAQEGLCLIGDHLLLRCCPLWRSLLDFCE 2656
Cdd:cd18808    141 IGFLSDPRRLNVALTRAKRGLIIVGNPDTLSKDPLWKKLLEYLE 184
AAA_11 pfam13086
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
2184-2427 4.21e-49

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.


Pssm-ID: 404072 [Multi-domain]  Cd Length: 248  Bit Score: 176.00  E-value: 4.21e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2184 SQNVAVREALEKP-FTVIQGPPGTGKTivgLHIVFWFHKSNQeqvqpggpPRGEKRLGGPCILYCGPSNKSVDVLAGLLL 2262
Cdd:pfam13086    1 SQREAIRSALSSShFTLIQGPPGTGKT---TTIVELIRQLLS--------YPATSAAAGPRILVCAPSNAAVDNILERLL 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2263 RRME---LKPLRVYSEQAEASEfpvprvgSRKLLRKSPREGRPNQSlRSITLHHRIRQAPNPYSSEIKAF-----DTRLQ 2334
Cdd:pfam13086   70 RKGQkygPKIVRIGHPAAISEA-------VLPVSLDYLVESKLNNE-EDAQIVKDISKELEKLAKALRAFekeiiVEKLL 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2335 RGELFSREDLVWYKKVLWEARK---------------FELDRHEVILCTCSCAASASLKILD-VRQILVDEAGMATEPET 2398
Cdd:pfam13086  142 KSRNKDKSKLEQERRKLRSERKelrkelrrreqslerEILDEAQIVCSTLSGAGSRLLSSLAnFDVVIIDEAAQALEPST 221
                          250       260
                   ....*....|....*....|....*....
gi 2462581889 2399 LIPLVQfpQAEKVVLLGDHKQLRPVVKNE 2427
Cdd:pfam13086  222 LIPLLR--GPKKVVLVGDPKQLPPTVISK 248
RNB pfam00773
RNB domain; This domain is the catalytic domain of ribonuclease II.
1334-1691 6.84e-49

RNB domain; This domain is the catalytic domain of ribonuclease II.


Pssm-ID: 459934 [Multi-domain]  Cd Length: 314  Bit Score: 177.86  E-value: 6.84e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 1334 REDCRAFLTFTVDPQGACNLDDALSVRDLGP-RCEVAVHITDVASFVPRDGVLDVEARRQGAAFYAPGREpVPMLPASLC 1412
Cdd:pfam00773    1 RKDLRDLPFITIDPADAKDLDDAISVEKLPNgGYRLGVHIADVSHYVPPGSPLDREARKRGTSVYLPDRV-IPMLPEKLS 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 1413 QDVLSLLPGRDRLAISLFLTMEKaSGQLKSLRFAPSVVQSDRQLSYEEAEEVIRQHPGAGRELP--ARLDSVDACV---- 1486
Cdd:pfam00773   80 NDLCSLNPGEDRLALSVEITIDA-DGEVTSYEIYPSVIRSKARLTYEEVDDLLEGKDAEKDKPDlaEDLRLLYELAkilr 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 1487 ---VAACYFSRLLRRHRLRSDcfYEQPDEDGTLGFRAAHIMVKEYMIQFNRLVAEFLvgsECTRTVTPLRWQPAPRSQQL 1563
Cdd:pfam00773  159 akrLQRGALDLDTPENKLILD--EEGVIDILIQERTDAHSLIEEFMLLANEAVARHL---QELGIPALYRVHPEPDLEKL 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 1564 kalcekhgdrvplslhlghhlhggggsppdtrlhllASLWKQVQFAARTQDYEQmvDLVTTDDMHPFLAPAgrdLRKALE 1643
Cdd:pfam00773  234 ------------------------------------NSLIKLLQLLPDDKGLSK--SLEKIKDDERLLSIL---LLRTMP 272
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 2462581889 1644 RSAFGrcarghQQQGGHYSLQVDWYTWATSPIRRYLDVVLQRQILLAL 1691
Cdd:pfam00773  273 RAEYS------PEPLGHFGLGLDIYTHFTSPIRRYPDLIVHRQLKALL 314
VacB COG0557
Exoribonuclease R [Transcription];
1166-1708 9.85e-40

Exoribonuclease R [Transcription];


Pssm-ID: 440323 [Multi-domain]  Cd Length: 711  Bit Score: 159.89  E-value: 9.85e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 1166 AFAGDEVLVQLLSGDKapEGRLRGRVLGVLKRKRHElaFVCRMDTWDPR-IMVPINGSVTK-IFVAELKdpsqvpiyslr 1243
Cdd:COG0557    103 ALHGDRVLVRVTKEDR--RGRPEGRVVEILERANTR--VVGRFEKEKGFgFVVPDDKRLLQdIFIPPDD----------- 167
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 1244 kgrlqrvglerlTAEARHSRLFWVQIVLWRQGFYYPLGIVREVLPEAStwEQGLRILGL--EYSLRL--PPS--DQA-TI 1316
Cdd:COG0557    168 ------------LNGAKDGDLVVVEITRYPERRGPPEGRVVEVLGSPG--DPGAEILIAirKHGLPHefPEEvlAEAeAL 233
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 1317 TKVLQKyhTELGRvagrREDCRAFLTFTVDPQGACNLDDALSVRDLGPRC-EVAVHITDVASFVPRDGVLDVEARRQGAA 1395
Cdd:COG0557    234 PDEVPE--ADLKG----RRDLRDLPLVTIDGEDAKDFDDAVSAEKLDNGGwRLGVHIADVSHYVRPGSALDREARKRGTS 307
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 1396 FYAPGRePVPMLPASLCQDVLSLLPGRDRLAISLFLTMEkASGQLKSLRFAPSVVQSDRQLSYEEAEEVIRQHPGAGREL 1475
Cdd:COG0557    308 VYLPDR-VIPMLPERLSNGLCSLNPGEDRLAMSCEMEID-AKGEVVSYEFYRSVIRSDARLTYEEVQAILDGKDEELREE 385
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 1476 P-------------------AR-------LDSVDACVVaacyFsrllrrhrlrsdcfyeqpDEDGTLG---FRA---AHI 1523
Cdd:COG0557    386 YadlvpmleelyelakilrkARekrgaidFDLPETKII----L------------------DEEGKPEdivPRErndAHK 443
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 1524 MVKEYMIQFNRLVAEFLVGSECTrtvTPLRWQPAP---RSQQLKALCEKHGdrvplslhlghhlhggggsppdtrLHLla 1600
Cdd:COG0557    444 LIEEFMLLANEAVAEFLEKLKLP---FLYRVHEEPdpeKLEALREFLANLG------------------------LKL-- 494
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 1601 SLWKQVQfaarTQDYEQMVDLVttddmhpflapAGRD----LRKALERSafgrcarghQQQ-------GGHYSLQVDWYT 1669
Cdd:COG0557    495 KGGDEPT----PKDLQKLLEQV-----------KGRPeeelLNTLLLRS---------MKQavyspenIGHFGLALEAYT 550
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|...
gi 2462581889 1670 WATSPIRRYLDVVLQRQILLALGHGGSA----YSARDIDGLCQ 1708
Cdd:COG0557    551 HFTSPIRRYPDLLVHRALKAYLEGKRSPglqeYLEEELEEIAE 593
AAA_12 pfam13087
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
715-915 1.02e-36

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.


Pssm-ID: 463780 [Multi-domain]  Cd Length: 196  Bit Score: 138.45  E-value: 1.02e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  715 TLLHRLFLCYQQethevarqSRLVFHENYRCTDAIVSFISRHFYVAK-GNPIHARGKVPPHPRH-----YPLMFCHVAGN 788
Cdd:pfam13087    4 SLFERLQELGPS--------AVVMLDTQYRMHPEIMEFPSKLFYGGKlKDGPSVAERPLPDDFHlpdplGPLVFIDVDGS 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  789 PDRDM-SMASWLNLAEIAQVVEKVQEAYNTWPSCWggreqRCICVVS-HGAQVSALRQELRRRDLG--QVSVGSFEILPG 864
Cdd:pfam13087   76 EEEESdGGTSYSNEAEAELVVQLVEKLIKSGPEEP-----SDIGVITpYRAQVRLIRKLLKRKLGGklEIEVNTVDGFQG 150
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462581889  865 RQFRVVVLSTVHTCQSllspGALApeFFTDARVLNTVLTRAQSQLVVVGDA 915
Cdd:pfam13087  151 REKDVIIFSCVRSNEK----GGIG--FLSDPRRLNVALTRAKRGLIIVGNA 195
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
748-932 1.95e-35

C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family includes UPF1, HELZ, Mov10L1, Aquarius, IGHMBP2 (SMUBP2), and similar proteins. They are DEAD-like helicases belonging to superfamily (SF)1, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF2 helicases, SF1 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: 350195 [Multi-domain]  Cd Length: 184  Bit Score: 134.28  E-value: 1.95e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  748 AIVSFISRHFY----VAKGNPIHARGKVPPHPRHYPLMFCHVAGNPDRDMSMASWLNLAEIAQVVEKVQEAYNTwpscwg 823
Cdd:cd18808      4 EISEFPSKLFYegklKAGVSVAARLNPPPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYLLKS------ 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  824 GREQRCICVVSH-GAQVSALRQELRRR--DLGQVSVGSFEILPGRQFRVVVLSTVHTCQSLLSPGalapeFFTDARVLNT 900
Cdd:cd18808     78 GVKPSSIGVITPyRAQVALIRELLRKRggLLEDVEVGTVDNFQGREKDVIILSLVRSNESGGSIG-----FLSDPRRLNV 152
                          170       180       190
                   ....*....|....*....|....*....|..
gi 2462581889  901 VLTRAQSQLVVVGDAVALCSFGACGKLWESFI 932
Cdd:cd18808    153 ALTRAKRGLIIVGNPDTLSKDPLWKKLLEYLE 184
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
106-915 5.88e-33

Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 139.88  E-value: 5.88e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  106 AHSAQELQEWVRRTQAVELRGQAAWQDGLVPYQERLLAEYQRSSSEVLVLAETLDGVRVTCNQPLMYQAQERKTQYSWTF 185
Cdd:COG1112      3 ALLLDAARALLALLALALLALLLALALLLDLLLLLLLAAALLLLALALALLLLALRALELLDLLAALALLLLLLLLDAEL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  186 AVHSEEPLLHVALLKQEPGADFSLVAPGLPPGRLYARGERFRVPSSTADFQVGVRVQAASFGTFEQWVVFDFGRRPVLLQ 265
Cdd:COG1112     83 LLLALRALLLLLAAELLLLLLLLLLLAALLLALAALLLALALLLLALALLALLALLLAELLDLLAALAALAALLAALLLL 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  266 KLGLQLGQGRRPGPCRNLALGHPEEMERWHTGNRHVVPGV-ERTAEQTALMAKYKGPALALEFNRSSVASGPISPTNYRQ 344
Cdd:COG1112    163 LLLLAALLLLDLRLLALLELLLAAALALALLALLALALEDeLALLLLLLLLALLLLLALLLLLDALLLLLAALALLALAL 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  345 RMHQFLYEEEAAQQQLVAKLTLRGQVFLKTALQTPALNMLFAPPGALYAEVPVPSSLMPDTDQGFLLGRAVSTALVAPVP 424
Cdd:COG1112    243 LLALLLLLLALLLLAALALLRAALRLDLLAALELLAALSLALLALLAALALALLLLAALALLLALALAALLALLALLALL 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  425 APDNTVFEVRLERRASSEQALWLLLPARCCLALGLQPEARLVLEVQFQIDPMTFRLWHQAVDTLPEEQLVVPDLPTCALP 504
Cdd:COG1112    323 AARLAAALAALLLLLLLEELALLAALLLLLELALLRLLAALLLALALLLLLALEELLLLALLRLLAEGLALLLLLLLAAL 402
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  505 RPWSVPPLRRGNRKQELAVALIAGWGPGDGRRVPPLLIYGPFGTGKTYTLAMASLEVIRRPETKVLIcTHTNSAADIYIR 584
Cdd:COG1112    403 LRLARALLLLALLLAAAAAALAALLLLALALLAALLALLLLLAAALAALLALLLLLLLALAALLLLL-AAAAALLALALL 481
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  585 EYFHSHVSGGHPEATPLRVMYTDRPLSQTDPVTLQyccLTDDRQAFRPPTRAELARHRVVVTTTSQ-ARELRVPVGFFSH 663
Cdd:COG1112    482 ESLLEELIEEHPEELEKLIAELREAARLRRALRRE---LKKRRELRKLLWDALLELAPVVGMTPASvARLLPLGEGSFDL 558
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  664 ILIDEAAQMLECEALTPLAYAShgtRLVLAGDHMQVTPRLFSVARARAAEH----TLLHRLFLCYQQethevaRQSRLVF 739
Cdd:COG1112    559 VIIDEASQATLAEALGALARAK---RVVLVGDPKQLPPVVFGEEAEEVAEEgldeSLLDRLLARLPE------RGVMLRE 629
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  740 HenYRCTDAIVSFISRHFYvakGNPIHARGKVPPHPR---HYPLMFCHVAGNPDRDMSmaSWLNLAEIAQVVEKVQEAYN 816
Cdd:COG1112    630 H--YRMHPEIIAFSNRLFY---DGKLVPLPSPKARRLadpDSPLVFIDVDGVYERRGG--SRTNPEEAEAVVELVRELLE 702
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  817 TWPscwggrEQRCICVVS-HGAQVSALRQELRRRDLG---QVSVGSFEILPGRQFRVVVLSTVhtcqslLSPGALAPEFF 892
Cdd:COG1112    703 DGP------DGESIGVITpYRAQVALIRELLREALGDglePVFVGTVDRFQGDERDVIIFSLV------YSNDEDVPRNF 770
                          810       820
                   ....*....|....*....|....*..
gi 2462581889  893 ----TDARVLNTVLTRAQSQLVVVGDA 915
Cdd:COG1112    771 gflnGGPRRLNVAVSRARRKLIVVGSR 797
3_prime_RNase TIGR00358
VacB and RNase II family 3'-5' exoribonucleases; This model is defined to identify a pair of ...
1334-1725 1.88e-22

VacB and RNase II family 3'-5' exoribonucleases; This model is defined to identify a pair of paralogous 3-prime exoribonucleases in E. coli, plus the set of proteins apparently orthologous to one or the other in other eubacteria. VacB was characterized originally as required for the expression of virulence genes, but is now recognized as the exoribonuclease RNase R (Rnr). Its paralog in E. coli and H. influenzae is designated exoribonuclease II (Rnb). Both are involved in the degradation of mRNA, and consequently have strong pleiotropic effects that may be difficult to disentangle. Both these proteins share domain-level similarity (RNB, S1) with a considerable number of other proteins, and full-length similarity scoring below the trusted cutoff to proteins associated with various phenotypes but uncertain biochemistry; it may be that these latter proteins are also 3-prime exoribonucleases. [Transcription, Degradation of RNA]


Pssm-ID: 273033 [Multi-domain]  Cd Length: 654  Bit Score: 105.18  E-value: 1.88e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 1334 REDCRAFLTFTVDPQGACNLDDALSVRDLGPR-CEVAVHITDVASFVPRDGVLDVEARRQGAAFYAPGREpVPMLPASLC 1412
Cdd:TIGR00358  194 REDLTDLAFVTIDGADAKDLDDAVYVKKLPDGgWKLYVAIADVSYYVAENSPLDKEAKHRGFSVYLPGFV-IPMLPEELS 272
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 1413 QDVLSLLPGRDRLAISLFLTMEkASGQLKSLRFAPSVVQSDRQLSYEEAEEVIRQHPGAGRELPARLDSVDAcvvAACYF 1492
Cdd:TIGR00358  273 NGLCSLNPNEDRLVLVCEMTIS-AQGRITDNEFYPATIESKARLTYDKVNDWLENDDELQPEYETLVEQLKA---LHQLS 348
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 1493 SRLLRRHRLRSDCFYEQP------DEDG------TLGFRAAHIMVKEYMIQFNRLVAEFLvgsECTRTVTPLRWQPAPRS 1560
Cdd:TIGR00358  349 QALGEWRHKRGLIDFEHPetkfivDEEGrvidivAEVRRIAEKIIEEAMIVANICAARFL---HNHKVPGIYRVHPGPSK 425
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 1561 QQLKALCE---KHGDRVPLSLHLGHHLHGgggsppdtrlhlLASLWKQVqfaARTQDYEQMVDLvttddmhpflapagrd 1637
Cdd:TIGR00358  426 KKLQSLLEflaELGLTLPGGNAENVTTLD------------GACWLREV---KDRPEYEILVTR---------------- 474
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 1638 LRKALERSAFgrcargHQQQGGHYSLQVDWYTWATSPIRRYLDVVLQRQILLALGHG----GSAYSARDIDGLCQAFSlq 1713
Cdd:TIGR00358  475 LLRSLSQAEY------SPEPLGHFGLGLEHYAHFTSPIRRYPDLTNHRLIKAVLAKEqtdtERYQPQDELLQIAEHCS-- 546
                          410
                   ....*....|..
gi 2462581889 1714 halaqSYQRRAR 1725
Cdd:TIGR00358  547 -----DTERRAR 553
TIGR00376 TIGR00376
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
541-914 1.88e-18

DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of this family have been characterized as binding certain single-stranded G-rich DNA sequences (GGGGT and GGGCT). A number of related proteins are characterized as helicases. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273041 [Multi-domain]  Cd Length: 636  Bit Score: 92.19  E-value: 1.88e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  541 LIYGPFGTGKTYTLamasLEVIRRP---ETKVLICTHTNSAADiYIREYF----------------------HS--HVSG 593
Cdd:TIGR00376  177 LIHGPPGTGKTRTV----VELIRQLvkrGLRVLVTAPSNIAVD-NLLERLalcdqkivrlghparllksnkqHSldYLIE 251
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  594 GHPEATPLRVMY--TDRPLSQTDPVTLQYCCLT---DDRQAFRPPTR--------AELARHRVVVTTTSQA--------- 651
Cdd:TIGR00376  252 NHPKYQIVADIRekIDELIEERNKKTKPSPQKRrglSDIKILRKALKkreargieSLKIASMAEWIETNKSidrllkllp 331
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  652 -----------RELRVPVG----------FFSHILIDEAAQMLECEALTPLAYAShgtRLVLAGDHMQVTPRLFSvARAR 710
Cdd:TIGR00376  332 eseerimneilAESDATNSmagseilngqYFDVAVIDEASQAMEPSCLIPLLKAR---KLILAGDHKQLPPTILS-HDAE 407
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  711 AAEHTLLHRLFLCYQQETHEVARQsrlvfhenYRCTDAIVSFISRHFYvakGNPIHARGKVPPH---------------- 774
Cdd:TIGR00376  408 ELSLTLFERLIKEYPERSRTLNVQ--------YRMNQKIMEFPSREFY---NGKLTAHESVANIllrdlpkveatesedd 476
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  775 -PRHYPLMFCHVAG---NPDRDMSMASWLNLAEIAQVVEKVQEAYNTwpscwgGREQRCICVVS-HGAQVSALRQ--ELR 847
Cdd:TIGR00376  477 lETGIPLLFIDTSGcelFELKEADSTSKYNPGEAELVSEIIQALVKM------GVPANDIGVITpYDAQVDLLRQllEHR 550
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462581889  848 RRDLGQVSVGSFEilpGRQFRVVVLSTVHTCQSllspGALApeFFTDARVLNTVLTRAQSQLVVVGD 914
Cdd:TIGR00376  551 HIDIEVSSVDGFQ---GREKEVIIISFVRSNRK----GEVG--FLKDLRRLNVALTRARRKLIVIGD 608
AAA_11 pfam13086
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
541-705 1.51e-10

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.


Pssm-ID: 404072 [Multi-domain]  Cd Length: 248  Bit Score: 63.90  E-value: 1.51e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  541 LIYGPFGTGKTYTLamasLEVIRR----------PETKVLICTHTNSAADIyIREYFHSHvsGGHPEATPLRVMYTDRPL 610
Cdd:pfam13086   17 LIQGPPGTGKTTTI----VELIRQllsypatsaaAGPRILVCAPSNAAVDN-ILERLLRK--GQKYGPKIVRIGHPAAIS 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  611 SQTDPVTLQY--------------------------------------------------------CCLTDDRQAFRPP- 633
Cdd:pfam13086   90 EAVLPVSLDYlvesklnneedaqivkdiskeleklakalrafekeiivekllksrnkdkskleqerRKLRSERKELRKEl 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  634 -------TRAELARHRVVVTT--TSQARELRVPVGFFShILIDEAAQMLECEALTPLAYASHgtRLVLAGDHMQVTPRLF 704
Cdd:pfam13086  170 rrreqslEREILDEAQIVCSTlsGAGSRLLSSLANFDV-VIIDEAAQALEPSTLIPLLRGPK--KVVLVGDPKQLPPTVI 246

                   .
gi 2462581889  705 S 705
Cdd:pfam13086  247 S 247
PRK11642 PRK11642
ribonuclease R;
1334-1468 5.70e-09

ribonuclease R;


Pssm-ID: 236944 [Multi-domain]  Cd Length: 813  Bit Score: 61.68  E-value: 5.70e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 1334 REDCRAFLTFTVDPQGACNLDDALSV---RDLGPRCEVAvhITDVASFVPRDGVLDVEARRQGAAFYAPGrEPVPMLPAS 1410
Cdd:PRK11642   260 RVDLRDLPLVTIDGEDARDFDDAVYCekkRGGGWRLWVA--IADVSYYVRPPTPLDREARNRGTSVYFPS-QVVPMLPEV 336
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462581889 1411 LCQDVLSLLPGRDRLAISLFLTMEkASGQLKSLRFAPSVVQSDRQLSYE------EAEEVIRQH 1468
Cdd:PRK11642   337 LSNGLCSLNPQVDRLCMVCEMTIS-SKGRLTGYKFYEAVMSSHARLTYTkvwhilQGDQDLREQ 399
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
2175-2585 2.74e-05

ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];


Pssm-ID: 440273 [Multi-domain]  Cd Length: 514  Bit Score: 49.59  E-value: 2.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2175 PGGRHKLNPSQNVAVREALEK-PFTVIQGPPGTGKTIVGLHIVFWFHKSNQEqvqpggpprgekrlggpcILYCGPSNKS 2253
Cdd:COG0507    119 PRAGITLSDEQREAVALALTTrRVSVLTGGAGTGKTTTLRALLAALEALGLR------------------VALAAPTGKA 180
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2254 VDVLaglllrrmelkplrvyseqAEASEFPvprvgsrkllrkspregrpnqslrSITLHHRIRQAPNpysseikafdtrl 2333
Cdd:COG0507    181 AKRL-------------------SESTGIE------------------------ARTIHRLLGLRPD------------- 204
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2334 qrgelfsredlvwykkvlweARKFELDRHEVilctcscaasasLKILDVrqILVDEAGMATEP--ETLIPLVQFPQAeKV 2411
Cdd:COG0507    205 --------------------SGRFRHNRDNP------------LTPADL--LVVDEASMVDTRlmAALLEALPRAGA-RL 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2412 VLLGDHKQLRPVVKNERLqnlgldRSLFERYHEDAHMLDTQYRMHEGIcAFPSVAfyksklktwQGLR--RPPSVLGHAG 2489
Cdd:COG0507    250 ILVGDPDQLPSVGAGAVL------RDLIESGTVPVVELTEVYRQADDS-RIIELA---------HAIRegDAPEALNARY 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2490 KEscpVIFGHVQGHERSllvstdegnenskanLEEVAEVVRitkqltlGRTVEPQDIAVLTPYNAQASEISKALRRE-GI 2568
Cdd:COG0507    314 AD---VVFVEAEDAEEA---------------AEAIVELYA-------DRPAGGEDIQVLAPTNAGVDALNQAIREAlNP 368
                          410
                   ....*....|....*..
gi 2462581889 2569 AGVAVSSITKSQGSEWR 2585
Cdd:COG0507    369 AGELERELAEDGELELY 385
zf-C2H2_jaz pfam12171
Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, ...
39-64 4.64e-03

Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, and is approximately 30 amino acids in length. The mammalian members of this group occur multiple times along the protein, joined by flexible linkers, and are referred to as JAZ - dsRNA-binding ZF protein - zinc-fingers. The JAZ proteins are expressed in all tissues tested and localize in the nucleus, particularly the nucleolus. JAZ preferentially binds to double-stranded (ds) RNA or RNA/DNA hybrids rather than DNA. In addition to binding double-stranded RNA, these zinc-fingers are required for nucleolar localization.


Pssm-ID: 432381 [Multi-domain]  Cd Length: 27  Bit Score: 36.76  E-value: 4.64e-03
                           10        20
                   ....*....|....*....|....*.
gi 2462581889   39 QLYCPACLVTCHSQEAFENHCASSEH 64
Cdd:pfam12171    1 QFYCVLCDKYFKSENALQNHLKSKKH 26
ZnF_U1 smart00451
U1-like zinc finger; Family of C2H2-type zinc fingers, present in matrin, U1 small nuclear ...
39-69 5.83e-03

U1-like zinc finger; Family of C2H2-type zinc fingers, present in matrin, U1 small nuclear ribonucleoprotein C and other RNA-binding proteins.


Pssm-ID: 197732 [Multi-domain]  Cd Length: 35  Bit Score: 36.46  E-value: 5.83e-03
                            10        20        30
                    ....*....|....*....|....*....|.
gi 2462581889    39 QLYCPACLVTCHSQEAFENHCASSEHAQMVA 69
Cdd:smart00451    3 GFYCKLCNVTFTDEISVEAHLKGKKHKKNVK 33
 
Name Accession Description Interval E-value
DEXXc_HELZ2-C cd18040
C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ...
2180-2454 1.41e-150

C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known as PPAR-alpha-interacting complex protein 285 or PRIC285 and PPAR-gamma DBD-interacting protein 1 or PDIP1) acts as a transcriptional coactivator for a number of nuclear receptors including PPARA, PPARG, THRA, THRB and RXRA. It 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: 350798 [Multi-domain]  Cd Length: 271  Bit Score: 468.16  E-value: 1.41e-150
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2180 KLNPSQNVAVREALEKPFTVIQGPPGTGKTIVGLHIVFWFHKSNQEQVQPGGpprgeKRLGGPCILYCGPSNKSVDVLAG 2259
Cdd:cd18040      1 KLNPSQNHAVRTALTKPFTLIQGPPGTGKTVTGVHIAYWFAKQNREIQSVSG-----EGDGGPCVLYCGPSNKSVDVVAE 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2260 LLLRRMELKPLRVYSEQAEASEFPVPRVGSRKLlRKSPREGRPNQSLRSITLHHRIRQAPNPYSSEIKAFDTRLQR-GEL 2338
Cdd:cd18040     76 LLLKVPGLKILRVYSEQIETTEYPIPNEPRHPN-KKSERESKPNSELSSITLHHRIRQPSNPHSQQIKAFEARFERtQEK 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2339 FSREDLVWYKKVLWEARKFELDRHEVILCTCSCAASASLK-ILDVRQILVDEAGMATEPETLIPLVQFPQAEKVVLLGDH 2417
Cdd:cd18040    155 ITEEDIKTYKILIWEARFEELETVDVILCTCSEAASQKMRtHANVKQCIVDECGMCTEPESLIPIVSAPRAEQVVLIGDH 234
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 2462581889 2418 KQLRPVVKNERLQNLGLDRSLFERYHEDAHMLDTQYR 2454
Cdd:cd18040    235 KQLRPVVQNKEAQKLGLGRSLFERYAEKACMLDTQYR 271
DEXXQc_HELZ2-N cd18076
N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ...
514-744 5.19e-149

N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known as PPAR-alpha-interacting complex protein 285 or PRIC285 and PPAR-gamma DBD-interacting protein 1 or PDIP1) acts as a transcriptional coactivator for a number of nuclear receptors including PPARA, PPARG, THRA, THRB, and RXRA. It 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: 350834 [Multi-domain]  Cd Length: 230  Bit Score: 461.67  E-value: 5.19e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  514 RGNRKQELAVALIAGWGPGdGRRVPPLLIYGPFGTGKTYTLAMASLEVIRRPETKVLICTHTNSAADIYIREYFHSHVSG 593
Cdd:cd18076      1 AGNNKQQLAFNFIAGKPSE-ARFVPPLLIYGPFGTGKTFTLAMAALEVIREPGTKVLICTHTNSAADIYIREYFHPYVDK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  594 GHPEATPLRVMYTDRPLSQTDPVTLQYCCLTDDRQAFRPPTRAELARHRVVVTTTSQARELRVPVGFFSHILIDEAAQML 673
Cdd:cd18076     80 GHPEARPLRIKATDRPNAITDPDTITYCCLTKDRQCFRLPTRDELDFHNIVITTTAMAFNLHVLSGFFTHIFIDEAAQML 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462581889  674 ECEALTPLAYASHGTRLVLAGDHMQVTPRLFSVARARAAEHTLLHRLFLCYQQETHEVARQSRLVFHENYR 744
Cdd:cd18076    160 ECEALIPLSYAGPKTRVVLAGDHMQMTPKLFSVADYNRANHTLLNRLFHYYQGEKHEVAVKSRVIFSENYR 230
DEXXQc_HELZ cd18077
DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that ...
514-744 6.87e-73

DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that plays a role in RNA metabolism during development. HELZ is a member of the family I class of RNA helicases 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: 350835 [Multi-domain]  Cd Length: 226  Bit Score: 243.55  E-value: 6.87e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  514 RGNRKQELAVALIAGwgpGDGRRVPPLLIYGPFGTGKTYTLAMASLEVIRRPETKVLICTHTNSAADIYIREYFHSHVSG 593
Cdd:cd18077      1 RLNAKQKEAVLAITT---PLSIQLPPVLLIGPFGTGKTFTLAQAVKHILQQPETRILICTHSNSAADLYIKEYLHPYVET 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  594 GHPEATPLRVMYTDRPLSQTDPVTLQYcCLTDDRQAFRPPTRAELARHRVVVTTTSQAREL---RVPVGFFSHILIDEAA 670
Cdd:cd18077     78 GNPRARPLRVYYRNRWVKTVHPVVQKY-CLIDEHGTFRMPTREDVMRHRVVVVTLSTSQYLcqlDLEPGFFTHILLDEAA 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462581889  671 QMLECEALTPLAYASHGTRLVLAGDHMQVTPRLFSV-ARARAAEHTLLHRLFLCYQQEthevaRQSRLVFHENYR 744
Cdd:cd18077    157 QAMECEAIMPLALATKSTRIVLAGDHMQLSPEVYSEfARERNLHISLLERLYEHYPSE-----HPCRILLCENYR 226
DEXXQc_Helz-like cd18038
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ...
514-744 2.00e-66

DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and similar proteins. Helicase with zinc finger (HELZ) acts as a helicase that plays a role in RNA metabolism during development. Moloney leukemia virus 10-like protein 1 (Mov10L1) binds Piwi-interacting RNA (piRNA) precursors to initiate piRNA processing. All are members 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: 350796 [Multi-domain]  Cd Length: 229  Bit Score: 224.81  E-value: 2.00e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  514 RGNRKQELAVALIAGwGPgdgRRVPPLLIYGPFGTGKTYTLAMASLEVIR-RPETKVLICTHTNSAADIYIREYFHShvs 592
Cdd:cd18038      1 ELNDEQKLAVRNIVT-GT---SRPPPYIIFGPPGTGKTVTLVEAILQVLRqPPEARILVCAPSNSAADLLAERLLNA--- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  593 gGHPEATPLRVMYTDRPLSQTDPVTLQYCCLTDDRqAFRPPTRAELARHRVVVTTTSQA---RELRVPVGFFSHILIDEA 669
Cdd:cd18038     74 -LVTKREILRLNAPSRDRASVPPELLPYCNSKAEG-TFRLPSLEELKKYRIVVCTLMTAgrlVQAGVPNGHFTHIFIDEA 151
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462581889  670 AQMLECEALTPLAY-ASHGTRLVLAGDHMQVTPRLFS-VARARAAEHTLLHRLFLCYQ-QETHEVARQSRLVFHENYR 744
Cdd:cd18038    152 GQATEPEALIPLSElASKNTQIVLAGDPKQLGPVVRSpLARKYGLGKSLLERLMERPLyYKDGEYNPSYITKLLKNYR 229
AAA_12 pfam13087
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
2434-2639 1.41e-61

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.


Pssm-ID: 463780 [Multi-domain]  Cd Length: 196  Bit Score: 209.71  E-value: 1.41e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2434 LDRSLFER----YHEDAHMLDTQYRMHEGICAFPSVAFYKSKLKTWQGLR-RPPSVLGHAGKESCPVIFGHVQGHErsll 2508
Cdd:pfam13087    1 LDRSLFERlqelGPSAVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAeRPLPDDFHLPDPLGPLVFIDVDGSE---- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2509 vSTDEGNENSKANLEEVAEVVRITKQLTLGRTVEPQDIAVLTPYNAQASEISKALRRE--GIAGVAVSSITKSQGSEWRY 2586
Cdd:pfam13087   77 -EEESDGGTSYSNEAEAELVVQLVEKLIKSGPEEPSDIGVITPYRAQVRLIRKLLKRKlgGKLEIEVNTVDGFQGREKDV 155
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462581889 2587 VLVSTVRTCAKSDldqrptkswlkkfLGFVVDPNQVNVAVTRAQEGLCLIGDH 2639
Cdd:pfam13087  156 IIFSCVRSNEKGG-------------IGFLSDPRRLNVALTRAKRGLIIVGNA 195
RNB smart00955
This domain is the catalytic domain of ribonuclease II;
1334-1693 1.64e-60

This domain is the catalytic domain of ribonuclease II;


Pssm-ID: 214935 [Multi-domain]  Cd Length: 286  Bit Score: 210.20  E-value: 1.64e-60
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  1334 REDCRAFLTFTVDPQGACNLDDALSVRDLGP-RCEVAVHITDVASFVPRDGVLDVEARRQGAAFYAPGRePVPMLPASLC 1412
Cdd:smart00955    1 RVDLRDLPLFTIDPEDAKDIDDAVSVEKLDNgGYRLGVHIADVSHYVKPGSALDREARKRGTSVYLPDR-VIPMLPEELS 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  1413 QDVLSLLPGRDRLAISLFLTMEKASGQLKSLRFAPSVVQSDRQLSYEEAEEVIRQHpgagrelparldsvdacvvaacyf 1492
Cdd:smart00955   80 NGLCSLNPGEDRLALSVEMTLDADGGEILDYEFYRSVIRSKARLTYEEVDAILEKI------------------------ 135
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  1493 srllrrhrlrsdcfyeQPDEDGTLG------FRAAHIMVKEYMIQFNRLVAEFLVGSECTrtvTPLRWQPAPR----SQQ 1562
Cdd:smart00955  136 ----------------VLDEEGKIEdivpreRNDAHSLVEEFMILANEAVARFLAKNGIP---GLYRVHEGPDpeklAEL 196
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  1563 LKALCEKHGDRVPLSlhlghhlhggggsppDTRLHLLASLWKqvqfaARTQDYEQMVDLVttddmhpflapagrdLRKAL 1642
Cdd:smart00955  197 LKEFLALLGLLLLGG---------------DGPKALAKLLEK-----IRDSPEERLLELL---------------LLRSM 241
                           330       340       350       360       370
                    ....*....|....*....|....*....|....*....|....*....|.
gi 2462581889  1643 ERSAFGRcarghqQQGGHYSLQVDWYTWATSPIRRYLDVVLQRQILLALGH 1693
Cdd:smart00955  242 PHAEYSV------DNSGHFGLALDAYTHFTSPIRRYPDLIVHRQLKAALRG 286
DEXXQc_UPF1 cd18039
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ...
2180-2454 9.39e-53

DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of Nonsense Transcripts, or ATP-Dependent Helicase RENT1) is an RNA-dependent helicase and ATPase required for nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. It is recruited to mRNAs upon translation termination and undergoes a cycle of phosphorylation and dephosphorylation; its phosphorylation appears to be a key step in NMD. It is recruited by release factors to stalled ribosomes together with the SMG1C protein kinase complex to form the transient SURF (SMG1-UPF1-eRF1-eRF3) complex. In EJC-dependent NMD, the SURF complex associates with the exon junction complex (EJC) located downstream from the termination codon through UPF2 and allows the formation of an UPF1-UPF2-UPF3 surveillance complex which is believed to activate NMD. Diseases associated with UPF1 include juvenile amyotrophic lateral sclerosis and epidermolysis bullosa, junctional, non-Herlitz type. UPF1 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: 350797 [Multi-domain]  Cd Length: 234  Bit Score: 185.91  E-value: 9.39e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2180 KLNPSQNVAVREALEKPFTVIQGPPGTGKTIVGLHIVFWFHKSNQEQVqpggpprgekrlggpciLYCGPSNKSVDVLAg 2259
Cdd:cd18039      1 ELNHSQVDAVKTALQRPLSLIQGPPGTGKTVTSATIVYHLVKQGNGPV-----------------LVCAPSNVAVDQLT- 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2260 LLLRRMELKPLRVYSEQAEASEFPVPrvgsrkllrkspregrpnqslrSITLHHRIRQAPNPYSSEIKAFdTRLQRGELf 2339
Cdd:cd18039     63 EKIHQTGLKVVRLCAKSREAVESPVS----------------------FLALHNQVRNLDSAEKLELLKL-LKLETGEL- 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2340 SREDLVWYKKVLWEARKFELDRHEVILCTCSCAASASLKILDVRQILVDEAGMATEPETLIPLVQfpQAEKVVLLGDHKQ 2419
Cdd:cd18039    119 SSADEKRYRKLKRKAERELLRNADVICCTCVGAGDPRLSKMKFRTVLIDEATQATEPECLIPLVH--GAKQVILVGDHCQ 196
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 2462581889 2420 LRPVVKNERLQNLGLDRSLFERYHEDAH---MLDTQYR 2454
Cdd:cd18039    197 LGPVVMCKKAAKAGLSQSLFERLVQLGIrpiRLQVQYR 234
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
2254-2658 7.68e-52

Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 198.81  E-value: 7.68e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2254 VDVLAGLLLRRMELKPLRVYSEQAEASEFPVPRVGSRKLLRKSPREGRPNQSLRSITLHHRIRQAPNPYSSEIKAFDTRL 2333
Cdd:COG1112    428 LLALALLAALLALLLLLAAALAALLALLLLLLLALAALLLLLAAAAALLALALLESLLEELIEEHPEELEKLIAELREAA 507
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2334 QRGELFSREdLVWYKKVLWEARKFELDRHEVILCTC-SCAASASLKILDVRQILVDEAGMATEPETLIPLVQfpqAEKVV 2412
Cdd:COG1112    508 RLRRALRRE-LKKRRELRKLLWDALLELAPVVGMTPaSVARLLPLGEGSFDLVIIDEASQATLAEALGALAR---AKRVV 583
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2413 LLGDHKQLRPVVKNER---LQNLGLDRSLFER----YHEDAHMLDTQYRMHEGICAFPSVAFYKSKLKTwqgLRRPPSVl 2485
Cdd:COG1112    584 LVGDPKQLPPVVFGEEaeeVAEEGLDESLLDRllarLPERGVMLREHYRMHPEIIAFSNRLFYDGKLVP---LPSPKAR- 659
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2486 gHAGKESCPVIFGHVQGhersllvsTDEGNENSKANLEEVAEVVRITKQLtLGRTVEPQDIAVLTPYNAQASEISKALRR 2565
Cdd:COG1112    660 -RLADPDSPLVFIDVDG--------VYERRGGSRTNPEEAEAVVELVREL-LEDGPDGESIGVITPYRAQVALIRELLRE 729
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2566 E---GIAGVAVSSITKSQGSEWRYVLVSTVRTcakSDLDQRPTKSWLKKflgfvvDPNQVNVAVTRAQEGLCLIGDHLLL 2642
Cdd:COG1112    730 AlgdGLEPVFVGTVDRFQGDERDVIIFSLVYS---NDEDVPRNFGFLNG------GPRRLNVAVSRARRKLIVVGSRELL 800
                          410
                   ....*....|....*....
gi 2462581889 2643 RCCP---LWRSLLDFCEAQ 2658
Cdd:COG1112    801 DSDPstpALKRLLEYLERA 819
TIGR00376 TIGR00376
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
2181-2665 1.55e-51

DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of this family have been characterized as binding certain single-stranded G-rich DNA sequences (GGGGT and GGGCT). A number of related proteins are characterized as helicases. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273041 [Multi-domain]  Cd Length: 636  Bit Score: 194.65  E-value: 1.55e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2181 LNPSQNVAVREAL-EKPFTVIQGPPGTGKTIVGLHIVfwfhksnQEQVQpggppRGEKrlggpcILYCGPSNKSVDVlag 2259
Cdd:TIGR00376  158 LNESQKEAVLFALsSKDLFLIHGPPGTGKTRTVVELI-------RQLVK-----RGLR------VLVTAPSNIAVDN--- 216
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2260 lLLRRMELKPLRVYseqaeasefpvpRVGSRKLLRKSPREgrpnQSLRSITLHHRIRQAPNPYSSEIKAF---------- 2329
Cdd:TIGR00376  217 -LLERLALCDQKIV------------RLGHPARLLKSNKQ----HSLDYLIENHPKYQIVADIREKIDELieernkktkp 279
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2330 ---------DTRLQRGELFSRE-----DLVWYKKVLWEARKFELDR----------------HEVILCTCSCAASASLKI 2379
Cdd:TIGR00376  280 spqkrrglsDIKILRKALKKREargieSLKIASMAEWIETNKSIDRllkllpeseerimneiLAESDATNSMAGSEILNG 359
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2380 LDVRQILVDEAGMATEPETLIPLVqfpQAEKVVLLGDHKQLRPVVKNErlQNLGLDRSLFER----YHEDAHMLDTQYRM 2455
Cdd:TIGR00376  360 QYFDVAVIDEASQAMEPSCLIPLL---KARKLILAGDHKQLPPTILSH--DAEELSLTLFERlikeYPERSRTLNVQYRM 434
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2456 HEGICAFPSVAFYKSKLK-----TWQGLRRPPSVlgHAGKESC------PVIFGHVQGHERSLLvstDEGNENSKANLEE 2524
Cdd:TIGR00376  435 NQKIMEFPSREFYNGKLTahesvANILLRDLPKV--EATESEDdletgiPLLFIDTSGCELFEL---KEADSTSKYNPGE 509
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2525 VAEVVRITKQLtLGRTVEPQDIAVLTPYNAQASEISKALRREGIaGVAVSSITKSQGSEWRYVLVSTVRTCAKSDldqrp 2604
Cdd:TIGR00376  510 AELVSEIIQAL-VKMGVPANDIGVITPYDAQVDLLRQLLEHRHI-DIEVSSVDGFQGREKEVIIISFVRSNRKGE----- 582
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462581889 2605 tkswlkkfLGFVVDPNQVNVAVTRAQEGLCLIGDHLLLRCCPLWRSLLDFCEAQQTLVPAG 2665
Cdd:TIGR00376  583 --------VGFLKDLRRLNVALTRARRKLIVIGDSRTLSNHKFYKRLIEWCKQHGEVREAF 635
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
2455-2656 5.03e-50

C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family includes UPF1, HELZ, Mov10L1, Aquarius, IGHMBP2 (SMUBP2), and similar proteins. They are DEAD-like helicases belonging to superfamily (SF)1, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF2 helicases, SF1 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: 350195 [Multi-domain]  Cd Length: 184  Bit Score: 176.27  E-value: 5.03e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2455 MHEGICAFPSVAFYKSKLKTWQGLRRPPSVLgHAGKESCPVIFGHVQGHERSllvstdEGNENSKANLEEVAEVVRITKQ 2534
Cdd:cd18808      1 MHPEISEFPSKLFYEGKLKAGVSVAARLNPP-PLPGPSKPLVFVDVSGGEER------EESGTSKSNEAEAELVVELVKY 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2535 LtLGRTVEPQDIAVLTPYNAQASEISKALRREGIA--GVAVSSITKSQGSEWRYVLVSTVRTCAKsdldqrptkswlKKF 2612
Cdd:cd18808     74 L-LKSGVKPSSIGVITPYRAQVALIRELLRKRGGLleDVEVGTVDNFQGREKDVIILSLVRSNES------------GGS 140
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 2462581889 2613 LGFVVDPNQVNVAVTRAQEGLCLIGDHLLLRCCPLWRSLLDFCE 2656
Cdd:cd18808    141 IGFLSDPRRLNVALTRAKRGLIIVGNPDTLSKDPLWKKLLEYLE 184
AAA_11 pfam13086
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
2184-2427 4.21e-49

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.


Pssm-ID: 404072 [Multi-domain]  Cd Length: 248  Bit Score: 176.00  E-value: 4.21e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2184 SQNVAVREALEKP-FTVIQGPPGTGKTivgLHIVFWFHKSNQeqvqpggpPRGEKRLGGPCILYCGPSNKSVDVLAGLLL 2262
Cdd:pfam13086    1 SQREAIRSALSSShFTLIQGPPGTGKT---TTIVELIRQLLS--------YPATSAAAGPRILVCAPSNAAVDNILERLL 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2263 RRME---LKPLRVYSEQAEASEfpvprvgSRKLLRKSPREGRPNQSlRSITLHHRIRQAPNPYSSEIKAF-----DTRLQ 2334
Cdd:pfam13086   70 RKGQkygPKIVRIGHPAAISEA-------VLPVSLDYLVESKLNNE-EDAQIVKDISKELEKLAKALRAFekeiiVEKLL 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2335 RGELFSREDLVWYKKVLWEARK---------------FELDRHEVILCTCSCAASASLKILD-VRQILVDEAGMATEPET 2398
Cdd:pfam13086  142 KSRNKDKSKLEQERRKLRSERKelrkelrrreqslerEILDEAQIVCSTLSGAGSRLLSSLAnFDVVIIDEAAQALEPST 221
                          250       260
                   ....*....|....*....|....*....
gi 2462581889 2399 LIPLVQfpQAEKVVLLGDHKQLRPVVKNE 2427
Cdd:pfam13086  222 LIPLLR--GPKKVVLVGDPKQLPPTVISK 248
RNB pfam00773
RNB domain; This domain is the catalytic domain of ribonuclease II.
1334-1691 6.84e-49

RNB domain; This domain is the catalytic domain of ribonuclease II.


Pssm-ID: 459934 [Multi-domain]  Cd Length: 314  Bit Score: 177.86  E-value: 6.84e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 1334 REDCRAFLTFTVDPQGACNLDDALSVRDLGP-RCEVAVHITDVASFVPRDGVLDVEARRQGAAFYAPGREpVPMLPASLC 1412
Cdd:pfam00773    1 RKDLRDLPFITIDPADAKDLDDAISVEKLPNgGYRLGVHIADVSHYVPPGSPLDREARKRGTSVYLPDRV-IPMLPEKLS 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 1413 QDVLSLLPGRDRLAISLFLTMEKaSGQLKSLRFAPSVVQSDRQLSYEEAEEVIRQHPGAGRELP--ARLDSVDACV---- 1486
Cdd:pfam00773   80 NDLCSLNPGEDRLALSVEITIDA-DGEVTSYEIYPSVIRSKARLTYEEVDDLLEGKDAEKDKPDlaEDLRLLYELAkilr 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 1487 ---VAACYFSRLLRRHRLRSDcfYEQPDEDGTLGFRAAHIMVKEYMIQFNRLVAEFLvgsECTRTVTPLRWQPAPRSQQL 1563
Cdd:pfam00773  159 akrLQRGALDLDTPENKLILD--EEGVIDILIQERTDAHSLIEEFMLLANEAVARHL---QELGIPALYRVHPEPDLEKL 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 1564 kalcekhgdrvplslhlghhlhggggsppdtrlhllASLWKQVQFAARTQDYEQmvDLVTTDDMHPFLAPAgrdLRKALE 1643
Cdd:pfam00773  234 ------------------------------------NSLIKLLQLLPDDKGLSK--SLEKIKDDERLLSIL---LLRTMP 272
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 2462581889 1644 RSAFGrcarghQQQGGHYSLQVDWYTWATSPIRRYLDVVLQRQILLAL 1691
Cdd:pfam00773  273 RAEYS------PEPLGHFGLGLDIYTHFTSPIRRYPDLIVHRQLKALL 314
VacB COG0557
Exoribonuclease R [Transcription];
1166-1708 9.85e-40

Exoribonuclease R [Transcription];


Pssm-ID: 440323 [Multi-domain]  Cd Length: 711  Bit Score: 159.89  E-value: 9.85e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 1166 AFAGDEVLVQLLSGDKapEGRLRGRVLGVLKRKRHElaFVCRMDTWDPR-IMVPINGSVTK-IFVAELKdpsqvpiyslr 1243
Cdd:COG0557    103 ALHGDRVLVRVTKEDR--RGRPEGRVVEILERANTR--VVGRFEKEKGFgFVVPDDKRLLQdIFIPPDD----------- 167
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 1244 kgrlqrvglerlTAEARHSRLFWVQIVLWRQGFYYPLGIVREVLPEAStwEQGLRILGL--EYSLRL--PPS--DQA-TI 1316
Cdd:COG0557    168 ------------LNGAKDGDLVVVEITRYPERRGPPEGRVVEVLGSPG--DPGAEILIAirKHGLPHefPEEvlAEAeAL 233
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 1317 TKVLQKyhTELGRvagrREDCRAFLTFTVDPQGACNLDDALSVRDLGPRC-EVAVHITDVASFVPRDGVLDVEARRQGAA 1395
Cdd:COG0557    234 PDEVPE--ADLKG----RRDLRDLPLVTIDGEDAKDFDDAVSAEKLDNGGwRLGVHIADVSHYVRPGSALDREARKRGTS 307
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 1396 FYAPGRePVPMLPASLCQDVLSLLPGRDRLAISLFLTMEkASGQLKSLRFAPSVVQSDRQLSYEEAEEVIRQHPGAGREL 1475
Cdd:COG0557    308 VYLPDR-VIPMLPERLSNGLCSLNPGEDRLAMSCEMEID-AKGEVVSYEFYRSVIRSDARLTYEEVQAILDGKDEELREE 385
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 1476 P-------------------AR-------LDSVDACVVaacyFsrllrrhrlrsdcfyeqpDEDGTLG---FRA---AHI 1523
Cdd:COG0557    386 YadlvpmleelyelakilrkARekrgaidFDLPETKII----L------------------DEEGKPEdivPRErndAHK 443
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 1524 MVKEYMIQFNRLVAEFLVGSECTrtvTPLRWQPAP---RSQQLKALCEKHGdrvplslhlghhlhggggsppdtrLHLla 1600
Cdd:COG0557    444 LIEEFMLLANEAVAEFLEKLKLP---FLYRVHEEPdpeKLEALREFLANLG------------------------LKL-- 494
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 1601 SLWKQVQfaarTQDYEQMVDLVttddmhpflapAGRD----LRKALERSafgrcarghQQQ-------GGHYSLQVDWYT 1669
Cdd:COG0557    495 KGGDEPT----PKDLQKLLEQV-----------KGRPeeelLNTLLLRS---------MKQavyspenIGHFGLALEAYT 550
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|...
gi 2462581889 1670 WATSPIRRYLDVVLQRQILLALGHGGSA----YSARDIDGLCQ 1708
Cdd:COG0557    551 HFTSPIRRYPDLLVHRALKAYLEGKRSPglqeYLEEELEEIAE 593
AAA_12 pfam13087
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
715-915 1.02e-36

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.


Pssm-ID: 463780 [Multi-domain]  Cd Length: 196  Bit Score: 138.45  E-value: 1.02e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  715 TLLHRLFLCYQQethevarqSRLVFHENYRCTDAIVSFISRHFYVAK-GNPIHARGKVPPHPRH-----YPLMFCHVAGN 788
Cdd:pfam13087    4 SLFERLQELGPS--------AVVMLDTQYRMHPEIMEFPSKLFYGGKlKDGPSVAERPLPDDFHlpdplGPLVFIDVDGS 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  789 PDRDM-SMASWLNLAEIAQVVEKVQEAYNTWPSCWggreqRCICVVS-HGAQVSALRQELRRRDLG--QVSVGSFEILPG 864
Cdd:pfam13087   76 EEEESdGGTSYSNEAEAELVVQLVEKLIKSGPEEP-----SDIGVITpYRAQVRLIRKLLKRKLGGklEIEVNTVDGFQG 150
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462581889  865 RQFRVVVLSTVHTCQSllspGALApeFFTDARVLNTVLTRAQSQLVVVGDA 915
Cdd:pfam13087  151 REKDVIIFSCVRSNEK----GGIG--FLSDPRRLNVALTRAKRGLIIVGNA 195
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
748-932 1.95e-35

C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family includes UPF1, HELZ, Mov10L1, Aquarius, IGHMBP2 (SMUBP2), and similar proteins. They are DEAD-like helicases belonging to superfamily (SF)1, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF2 helicases, SF1 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: 350195 [Multi-domain]  Cd Length: 184  Bit Score: 134.28  E-value: 1.95e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  748 AIVSFISRHFY----VAKGNPIHARGKVPPHPRHYPLMFCHVAGNPDRDMSMASWLNLAEIAQVVEKVQEAYNTwpscwg 823
Cdd:cd18808      4 EISEFPSKLFYegklKAGVSVAARLNPPPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYLLKS------ 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  824 GREQRCICVVSH-GAQVSALRQELRRR--DLGQVSVGSFEILPGRQFRVVVLSTVHTCQSLLSPGalapeFFTDARVLNT 900
Cdd:cd18808     78 GVKPSSIGVITPyRAQVALIRELLRKRggLLEDVEVGTVDNFQGREKDVIILSLVRSNESGGSIG-----FLSDPRRLNV 152
                          170       180       190
                   ....*....|....*....|....*....|..
gi 2462581889  901 VLTRAQSQLVVVGDAVALCSFGACGKLWESFI 932
Cdd:cd18808    153 ALTRAKRGLIIVGNPDTLSKDPLWKKLLEYLE 184
DEXXQc_SETX cd18042
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in ...
2181-2454 1.23e-34

DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in transcription, neurogenesis, and antiviral response. SEXT is an R-loop-associated protein that is thought to function as an RNA/DNA helicase. R-loops consist of RNA/DNA hybrids, formed during transcription when nascent RNA hybridizes to the DNA template strand, displacing the non-template DNA strand. Mutations in SETX are linked to two neurodegenerative disorders: ataxia with oculomotor apraxia type 2 (AOA2) and amyotrophic lateral sclerosis type 4 (ALS4). S. cerevisiae homolog splicing endonuclease 1 (Sen1) is an exclusively nuclear protein, important for nucleolar organization. S. cerevisiae Sen1 and its ortholog, the Schizosaccharomyces pombe Sen1, share conserved domains and belong to the family I class of helicases. Both proteins translocate 5' to 3' and unwind both DNA and RNA duplexes and also RNA/DNA hybrids in vitro. SETX 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: 438712 [Multi-domain]  Cd Length: 218  Bit Score: 133.11  E-value: 1.23e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2181 LNPSQNVAVREAL--EKPFTVIQGPPGTGKT--IVGL--HIVFWFHKSNQEQVQPGGPPRGEK---RLGGPCILYCGPSN 2251
Cdd:cd18042      1 LNESQLEAIASALqnSPGITLIQGPPGTGKTktIVGIlsVLLAGKYRKYYEKVKKKLRKLQRNlnnKKKKNRILVCAPSN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2252 KSVDvlaGLLLRrmeLKPLRVYSEQAEASEFPVPRVGSRKLlRKSpregrpnqslrsitlhhrirqapnpysseikafdt 2331
Cdd:cd18042     81 AAVD---EIVLR---LLSEGFLDGDGRSYKPNVVRVGRQEL-RAS----------------------------------- 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2332 rlqrgelfsredlvwykkVLWEArkfeldrhEVILCTCSCAASASLKILDVR--QILVDEAGMATEPETLIPLvQFpQAE 2409
Cdd:cd18042    119 ------------------ILNEA--------DIVCTTLSSSGSDLLESLPRGfdTVIIDEAAQAVELSTLIPL-RL-GCK 170
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 2462581889 2410 KVVLLGDHKQLRPVVKNERLQNLGLDRSLFERYHE---DAHMLDTQYR 2454
Cdd:cd18042    171 RLILVGDPKQLPATVFSKVAQKLGYDRSLFERLQLagyPVLMLTTQYR 218
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
106-915 5.88e-33

Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 139.88  E-value: 5.88e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  106 AHSAQELQEWVRRTQAVELRGQAAWQDGLVPYQERLLAEYQRSSSEVLVLAETLDGVRVTCNQPLMYQAQERKTQYSWTF 185
Cdd:COG1112      3 ALLLDAARALLALLALALLALLLALALLLDLLLLLLLAAALLLLALALALLLLALRALELLDLLAALALLLLLLLLDAEL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  186 AVHSEEPLLHVALLKQEPGADFSLVAPGLPPGRLYARGERFRVPSSTADFQVGVRVQAASFGTFEQWVVFDFGRRPVLLQ 265
Cdd:COG1112     83 LLLALRALLLLLAAELLLLLLLLLLLAALLLALAALLLALALLLLALALLALLALLLAELLDLLAALAALAALLAALLLL 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  266 KLGLQLGQGRRPGPCRNLALGHPEEMERWHTGNRHVVPGV-ERTAEQTALMAKYKGPALALEFNRSSVASGPISPTNYRQ 344
Cdd:COG1112    163 LLLLAALLLLDLRLLALLELLLAAALALALLALLALALEDeLALLLLLLLLALLLLLALLLLLDALLLLLAALALLALAL 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  345 RMHQFLYEEEAAQQQLVAKLTLRGQVFLKTALQTPALNMLFAPPGALYAEVPVPSSLMPDTDQGFLLGRAVSTALVAPVP 424
Cdd:COG1112    243 LLALLLLLLALLLLAALALLRAALRLDLLAALELLAALSLALLALLAALALALLLLAALALLLALALAALLALLALLALL 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  425 APDNTVFEVRLERRASSEQALWLLLPARCCLALGLQPEARLVLEVQFQIDPMTFRLWHQAVDTLPEEQLVVPDLPTCALP 504
Cdd:COG1112    323 AARLAAALAALLLLLLLEELALLAALLLLLELALLRLLAALLLALALLLLLALEELLLLALLRLLAEGLALLLLLLLAAL 402
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  505 RPWSVPPLRRGNRKQELAVALIAGWGPGDGRRVPPLLIYGPFGTGKTYTLAMASLEVIRRPETKVLIcTHTNSAADIYIR 584
Cdd:COG1112    403 LRLARALLLLALLLAAAAAALAALLLLALALLAALLALLLLLAAALAALLALLLLLLLALAALLLLL-AAAAALLALALL 481
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  585 EYFHSHVSGGHPEATPLRVMYTDRPLSQTDPVTLQyccLTDDRQAFRPPTRAELARHRVVVTTTSQ-ARELRVPVGFFSH 663
Cdd:COG1112    482 ESLLEELIEEHPEELEKLIAELREAARLRRALRRE---LKKRRELRKLLWDALLELAPVVGMTPASvARLLPLGEGSFDL 558
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  664 ILIDEAAQMLECEALTPLAYAShgtRLVLAGDHMQVTPRLFSVARARAAEH----TLLHRLFLCYQQethevaRQSRLVF 739
Cdd:COG1112    559 VIIDEASQATLAEALGALARAK---RVVLVGDPKQLPPVVFGEEAEEVAEEgldeSLLDRLLARLPE------RGVMLRE 629
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  740 HenYRCTDAIVSFISRHFYvakGNPIHARGKVPPHPR---HYPLMFCHVAGNPDRDMSmaSWLNLAEIAQVVEKVQEAYN 816
Cdd:COG1112    630 H--YRMHPEIIAFSNRLFY---DGKLVPLPSPKARRLadpDSPLVFIDVDGVYERRGG--SRTNPEEAEAVVELVRELLE 702
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  817 TWPscwggrEQRCICVVS-HGAQVSALRQELRRRDLG---QVSVGSFEILPGRQFRVVVLSTVhtcqslLSPGALAPEFF 892
Cdd:COG1112    703 DGP------DGESIGVITpYRAQVALIRELLREALGDglePVFVGTVDRFQGDERDVIIFSLV------YSNDEDVPRNF 770
                          810       820
                   ....*....|....*....|....*..
gi 2462581889  893 ----TDARVLNTVLTRAQSQLVVVGDA 915
Cdd:COG1112    771 gflnGGPRRLNVAVSRARRKLIVVGSR 797
DEXXQc_Helz-like cd18038
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ...
2181-2441 2.58e-29

DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and similar proteins. Helicase with zinc finger (HELZ) acts as a helicase that plays a role in RNA metabolism during development. Moloney leukemia virus 10-like protein 1 (Mov10L1) binds Piwi-interacting RNA (piRNA) precursors to initiate piRNA processing. All are members 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: 350796 [Multi-domain]  Cd Length: 229  Bit Score: 118.49  E-value: 2.58e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2181 LNPSQNVAVREALEKPFT----VIQGPPGTGKTIVglhIVfwfhksnqE---QVqpggpprgEKRLGGPCILYCGPSNKS 2253
Cdd:cd18038      2 LNDEQKLAVRNIVTGTSRpppyIIFGPPGTGKTVT---LV--------EailQV--------LRQPPEARILVCAPSNSA 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2254 VDVLAGLLLRRMELK--PLRVYSEQAEASEFPVPrvgsrkllrkspregrpnqslrsitlhhrirqaPNPYSSEIKAFDT 2331
Cdd:cd18038     63 ADLLAERLLNALVTKreILRLNAPSRDRASVPPE---------------------------------LLPYCNSKAEGTF 109
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2332 RLqrgelFSREdlvwykkvlwearkfELDRHEVILCTCSCAASasLKILDVRQ-----ILVDEAGMATEPETLIPLVQFP 2406
Cdd:cd18038    110 RL-----PSLE---------------ELKKYRIVVCTLMTAGR--LVQAGVPNghfthIFIDEAGQATEPEALIPLSELA 167
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 2462581889 2407 QAE-KVVLLGDHKQLRPVVKNERLQNLGLDRSLFER 2441
Cdd:cd18038    168 SKNtQIVLAGDPKQLGPVVRSPLARKYGLGKSLLER 203
DEXXQc_Mov10L1 cd18078
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds ...
516-744 1.27e-27

DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds Piwi-interacting RNA (piRNA) precursors to initiate piRNA processing. Mov10L1 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: 350836 [Multi-domain]  Cd Length: 230  Bit Score: 113.62  E-value: 1.27e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  516 NRKQELAVALIAGwgpGDGRRVPpLLIYGPFGTGKTYTLAMASLEVIRR-PETKVLICTHTNSAADIYIREYfhsHVSGG 594
Cdd:cd18078      3 NELQKEAVKRILG---GECRPLP-YILFGPPGTGKTVTIIEAILQVVYNlPRSRILVCAPSNSAADLVTSRL---HESKV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  595 HPEATPLRVMYTDRPLSQTDPVTLQYCCLTDDRQAfrpptraeLARHRVVVTTTSQA---RELRVPVGFFSHILIDEAAQ 671
Cdd:cd18078     76 LKPGDMVRLNAVNRFESTVIDARKLYCRLGEDLSK--------ASRHRIVISTCSTAgllYQMGLPVGHFTHVFVDEAGQ 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  672 MLECEALTPLAYASHGT-RLVLAGDHMQVTPRLFS-VARARAAEHTLLHRLFL--CYQQET----HEVARQSRLVFH--E 741
Cdd:cd18078    148 ATEPESLIPLGLISSRDgQIILAGDPMQLGPVIKSrLASAYGLGVSFLERLMNrpLYLRDPnrfgESGGYNPLLVTKlvD 227

                   ...
gi 2462581889  742 NYR 744
Cdd:cd18078    228 NYR 230
DEXXQc_SMUBP2 cd18044
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ...
2180-2454 4.49e-25

DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, or IGHMBP2) is a 5' to 3' helicase that unwinds RNA and DNA duplexes in an ATP-dependent reaction. It is a DNA-binding protein specific to 5'-phosphorylated single-stranded guanine-rich sequence (5'-GGGCT-3') related to the immunoglobulin mu chain switch region. The IGHMBP2 gene is responsible for Charcot-Marie-Tooth disease (CMT) type 2S and spinal muscular atrophy with respiratory distress type 1 (SMARD1). It is also thought to play a role in frontotemporal dementia (FTD) with amyotrophic lateral sclerosis (ALS) and major depressive disorder (MDD). SMUBP2 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: 350802 [Multi-domain]  Cd Length: 191  Bit Score: 105.00  E-value: 4.49e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2180 KLNPSQNVAVREALE-KPFTVIQGPPGTGKTIVGLHIVfwfhksnQEQVQpggppRGEKrlggpcILYCGPSNKSVDVLA 2258
Cdd:cd18044      1 NLNDSQKEAVKFALSqKDVALIHGPPGTGKTTTVVEII-------LQAVK-----RGEK------VLACAPSNIAVDNLV 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2259 GLLLRRMeLKPLRVyseqaeasefpvprvgsrkllrkspreGRPNQSLRSITLHhrirqapnpysseikAFDTRLQrgel 2338
Cdd:cd18044     63 ERLVALK-VKVVRI---------------------------GHPARLLESVLDH---------------SLDALVA---- 95
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2339 fsredlvwykkvlweARkfeldrheVILCTCSCAASASLKIL---DVrqILVDEAGMATEPETLIPLVQFPqaeKVVLLG 2415
Cdd:cd18044     96 ---------------AQ--------VVLATNTGAGSRQLLPNelfDV--VVIDEAAQALEASCWIPLLKAR---RCILAG 147
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 2462581889 2416 DHKQLRPVVKNERLQNLGLDRSLFER----YHEDAH-MLDTQYR 2454
Cdd:cd18044    148 DHKQLPPTILSDKAARGGLGVTLFERlvnlYGESVVrMLTVQYR 191
3_prime_RNase TIGR00358
VacB and RNase II family 3'-5' exoribonucleases; This model is defined to identify a pair of ...
1334-1725 1.88e-22

VacB and RNase II family 3'-5' exoribonucleases; This model is defined to identify a pair of paralogous 3-prime exoribonucleases in E. coli, plus the set of proteins apparently orthologous to one or the other in other eubacteria. VacB was characterized originally as required for the expression of virulence genes, but is now recognized as the exoribonuclease RNase R (Rnr). Its paralog in E. coli and H. influenzae is designated exoribonuclease II (Rnb). Both are involved in the degradation of mRNA, and consequently have strong pleiotropic effects that may be difficult to disentangle. Both these proteins share domain-level similarity (RNB, S1) with a considerable number of other proteins, and full-length similarity scoring below the trusted cutoff to proteins associated with various phenotypes but uncertain biochemistry; it may be that these latter proteins are also 3-prime exoribonucleases. [Transcription, Degradation of RNA]


Pssm-ID: 273033 [Multi-domain]  Cd Length: 654  Bit Score: 105.18  E-value: 1.88e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 1334 REDCRAFLTFTVDPQGACNLDDALSVRDLGPR-CEVAVHITDVASFVPRDGVLDVEARRQGAAFYAPGREpVPMLPASLC 1412
Cdd:TIGR00358  194 REDLTDLAFVTIDGADAKDLDDAVYVKKLPDGgWKLYVAIADVSYYVAENSPLDKEAKHRGFSVYLPGFV-IPMLPEELS 272
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 1413 QDVLSLLPGRDRLAISLFLTMEkASGQLKSLRFAPSVVQSDRQLSYEEAEEVIRQHPGAGRELPARLDSVDAcvvAACYF 1492
Cdd:TIGR00358  273 NGLCSLNPNEDRLVLVCEMTIS-AQGRITDNEFYPATIESKARLTYDKVNDWLENDDELQPEYETLVEQLKA---LHQLS 348
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 1493 SRLLRRHRLRSDCFYEQP------DEDG------TLGFRAAHIMVKEYMIQFNRLVAEFLvgsECTRTVTPLRWQPAPRS 1560
Cdd:TIGR00358  349 QALGEWRHKRGLIDFEHPetkfivDEEGrvidivAEVRRIAEKIIEEAMIVANICAARFL---HNHKVPGIYRVHPGPSK 425
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 1561 QQLKALCE---KHGDRVPLSLHLGHHLHGgggsppdtrlhlLASLWKQVqfaARTQDYEQMVDLvttddmhpflapagrd 1637
Cdd:TIGR00358  426 KKLQSLLEflaELGLTLPGGNAENVTTLD------------GACWLREV---KDRPEYEILVTR---------------- 474
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 1638 LRKALERSAFgrcargHQQQGGHYSLQVDWYTWATSPIRRYLDVVLQRQILLALGHG----GSAYSARDIDGLCQAFSlq 1713
Cdd:TIGR00358  475 LLRSLSQAEY------SPEPLGHFGLGLEHYAHFTSPIRRYPDLTNHRLIKAVLAKEqtdtERYQPQDELLQIAEHCS-- 546
                          410
                   ....*....|..
gi 2462581889 1714 halaqSYQRRAR 1725
Cdd:TIGR00358  547 -----DTERRAR 553
DEXXQc_DNA2 cd18041
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ...
2180-2454 2.88e-20

DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses different enzymatic activities, such as single-stranded DNA (ssDNA)-dependent ATPase, 5-3 helicase, and endonuclease activities, and is involved in DNA replication and DNA repair in the nucleus and mitochondrion. It is involved in Okazaki fragment processing by cleaving long flaps that escape FEN1: flaps that are longer than 27 nucleotides are coated by replication protein A complex (RPA), leading to recruit DNA2 which cleaves the flap until it is too short to bind RPA and becomes a substrate for FEN1. It is also involved in 5-end resection of DNA during double-strand break (DSB) repair; it is recruited by BLM and mediates the cleavage of 5-ssDNA, while the 3-ssDNA cleavage is prevented by the presence of RPA. DNA2 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: 350799 [Multi-domain]  Cd Length: 203  Bit Score: 91.53  E-value: 2.88e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2180 KLNPSQNVAVREALE-KPFTVIQGPPGTGKTIVGLHIVFWFHKSNQeqvqpggpprgekrlggpCILYCGPSNKSVDvla 2258
Cdd:cd18041      1 GLNKDQRQAIKKVLNaKDYALILGMPGTGKTTTIAALVRILVALGK------------------SVLLTSYTHSAVD--- 59
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2259 GLLLRrmeLKPLRVyseqaeasefPVPRVGsrkllrkspregrpnqslRSITLHHRIRQapnpysseikafdtrlqrgel 2338
Cdd:cd18041     60 NILLK---LKKFGV----------NFLRLG------------------RLKKIHPDVQE--------------------- 87
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2339 FSREDLVWYKKVLWEARKFeLDRHEVILCTCSCAASASL--KILDVrqILVDEAGMATEPETLIPLVQfpqAEKVVLLGD 2416
Cdd:cd18041     88 FTLEAILKSCKSVEELESK-YESVSVVATTCLGINHPIFrrRTFDY--CIVDEASQITLPICLGPLRL---AKKFVLVGD 161
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 2462581889 2417 HKQLRPVVKNERLQNLGLDRSLFERY---HEDAH-MLDTQYR 2454
Cdd:cd18041    162 HYQLPPLVKSREARELGMDESLFKRLseaHPDAVvQLTIQYR 203
DEXXQc_Upf1-like cd17934
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ...
2197-2454 1.34e-18

DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, HELZ, Mov10L1, Aquarius, IGHMBP2 (SMUBP2), coronavirus Nsp13, and similar proteins. They belong 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: 438708 [Multi-domain]  Cd Length: 121  Bit Score: 83.82  E-value: 1.34e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2197 FTVIQGPPGTGKTIVGLHIVFWFHKsnqeqvqpggpprgekRLGGPCILYCGPSNKSVDVlaglllrrmelkplrvyseq 2276
Cdd:cd17934      1 ISLIQGPPGTGKTTTIAAIVLQLLK----------------GLRGKRVLVTAQSNVAVDN-------------------- 44
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2277 aeasefpvprvgsrkllrkspregrpnqslrsitlhhrirqapnpysseikafdtrlqrgelfsredlvwykkvlweark 2356
Cdd:cd17934        --------------------------------------------------------------------------------
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2357 feldrhevilctcscaasaslkildVRQILVDEAGMATEPETLIPLvqfPQAEKVVLLGDHKQLRPVVKNERLQNLG--- 2433
Cdd:cd17934     45 -------------------------VDVVIIDEASQITEPELLIAL---IRAKKVVLVGDPKQLPPVVQEDHAALLGlsf 96
                          250       260
                   ....*....|....*....|....*
gi 2462581889 2434 ----LDRSLFERYHEDAHMLDTQYR 2454
Cdd:cd17934     97 ilslLLLFRLLLPGSPKVMLDTQYR 121
TIGR00376 TIGR00376
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
541-914 1.88e-18

DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of this family have been characterized as binding certain single-stranded G-rich DNA sequences (GGGGT and GGGCT). A number of related proteins are characterized as helicases. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273041 [Multi-domain]  Cd Length: 636  Bit Score: 92.19  E-value: 1.88e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  541 LIYGPFGTGKTYTLamasLEVIRRP---ETKVLICTHTNSAADiYIREYF----------------------HS--HVSG 593
Cdd:TIGR00376  177 LIHGPPGTGKTRTV----VELIRQLvkrGLRVLVTAPSNIAVD-NLLERLalcdqkivrlghparllksnkqHSldYLIE 251
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  594 GHPEATPLRVMY--TDRPLSQTDPVTLQYCCLT---DDRQAFRPPTR--------AELARHRVVVTTTSQA--------- 651
Cdd:TIGR00376  252 NHPKYQIVADIRekIDELIEERNKKTKPSPQKRrglSDIKILRKALKkreargieSLKIASMAEWIETNKSidrllkllp 331
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  652 -----------RELRVPVG----------FFSHILIDEAAQMLECEALTPLAYAShgtRLVLAGDHMQVTPRLFSvARAR 710
Cdd:TIGR00376  332 eseerimneilAESDATNSmagseilngqYFDVAVIDEASQAMEPSCLIPLLKAR---KLILAGDHKQLPPTILS-HDAE 407
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  711 AAEHTLLHRLFLCYQQETHEVARQsrlvfhenYRCTDAIVSFISRHFYvakGNPIHARGKVPPH---------------- 774
Cdd:TIGR00376  408 ELSLTLFERLIKEYPERSRTLNVQ--------YRMNQKIMEFPSREFY---NGKLTAHESVANIllrdlpkveatesedd 476
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  775 -PRHYPLMFCHVAG---NPDRDMSMASWLNLAEIAQVVEKVQEAYNTwpscwgGREQRCICVVS-HGAQVSALRQ--ELR 847
Cdd:TIGR00376  477 lETGIPLLFIDTSGcelFELKEADSTSKYNPGEAELVSEIIQALVKM------GVPANDIGVITpYDAQVDLLRQllEHR 550
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462581889  848 RRDLGQVSVGSFEilpGRQFRVVVLSTVHTCQSllspGALApeFFTDARVLNTVLTRAQSQLVVVGD 914
Cdd:TIGR00376  551 HIDIEVSSVDGFQ---GREKEVIIISFVRSNRK----GEVG--FLKDLRRLNVALTRARRKLIVIGD 608
DEXXQc_Mov10L1 cd18078
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds ...
2180-2441 4.11e-17

DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds Piwi-interacting RNA (piRNA) precursors to initiate piRNA processing. Mov10L1 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: 350836 [Multi-domain]  Cd Length: 230  Bit Score: 82.80  E-value: 4.11e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2180 KLNPSQNVAVREALEK-----PFtVIQGPPGTGKTIVGLHIVFwfhksnqeQVQpggpprgeKRLGGPCILYCGPSNKSV 2254
Cdd:cd18078      1 DLNELQKEAVKRILGGecrplPY-ILFGPPGTGKTVTIIEAIL--------QVV--------YNLPRSRILVCAPSNSAA 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2255 DVLAgllLRRMELKPLRvyseqaeasefpvprvgsrkllrkspregrPNQSLRSITLHHRIRQapnpYSSEIKAFDTRLQ 2334
Cdd:cd18078     64 DLVT---SRLHESKVLK------------------------------PGDMVRLNAVNRFEST----VIDARKLYCRLGE 106
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2335 RgelfsredlvwykkvLWEArkfelDRHEVILCTCScaASASLKILDVR-----QILVDEAGMATEPETLIPLVQFPQAE 2409
Cdd:cd18078    107 D---------------LSKA-----SRHRIVISTCS--TAGLLYQMGLPvghftHVFVDEAGQATEPESLIPLGLISSRD 164
                          250       260       270
                   ....*....|....*....|....*....|...
gi 2462581889 2410 -KVVLLGDHKQLRPVVKNERLQNLGLDRSLFER 2441
Cdd:cd18078    165 gQIILAGDPMQLGPVIKSRLASAYGLGVSFLER 197
EEXXEc_NFX1 cd17936
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ...
2181-2441 7.15e-17

EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that represses class II MHC (major histocompatibility complex) gene expression. NFX1 binds a conserved cis-acting element, termed the X-box, in promoters of human class II MHC genes. The Cys-rich region contains several NFX1-type zinc finger domains. Frequently, a R3H domain is present in the C-terminus, and a RING finger domain and a PAM2 motif are present in the N-terminus. The lack of R3H and PAM2 motifs in the plant proteins indicates functional differences. Plant NFX1-like proteins are proposed to modulate growth and survival by coordinating reactive oxygen species, salicylic acid, further biotic stress and abscisic acid responses. A common feature of all members may be E3 ubiquitin ligase, due to the presence of a RING finger domain, as well as DNA binding. NFX1 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: 350694 [Multi-domain]  Cd Length: 178  Bit Score: 80.67  E-value: 7.15e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2181 LNPSQNVAVREALEKPFTVIQGPPGTGKTIVGLHIVF-WFHKSNQEQVQPggpprgekrlggpcILYCGPSNKSVDVLAG 2259
Cdd:cd17936      2 LDPSQLEALKHALTSELALIQGPPGTGKTFLGVKLVRaLLQNQDLSITGP--------------ILVVCYTNHALDQFLE 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2260 LLLRRMELKplrvyseqaeasefpVPRVGsrkllrkspregrpnqslrsitlhhrirqapnpysseikafdtrlqrgelf 2339
Cdd:cd17936     68 GLLDFGPTK---------------IVRLG--------------------------------------------------- 81
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2340 sredlvwykkvlwearkfeldrHEVILCTCSCAASAS--LKILDVRQILVDEAGMATEPETLIPLvqFPQAEKVVLLGDH 2417
Cdd:cd17936     82 ----------------------ARVIGMTTTGAAKYRelLQALGPKVVIVEEAAEVLEAHILAAL--TPSTEHLILIGDH 137
                          250       260
                   ....*....|....*....|....*.
gi 2462581889 2418 KQLRPVVKNERLQNLG--LDRSLFER 2441
Cdd:cd17936    138 KQLRPKVNVYELTAKKynLDVSLFER 163
DEXXQc_UPF1 cd18039
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ...
541-725 2.40e-14

DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of Nonsense Transcripts, or ATP-Dependent Helicase RENT1) is an RNA-dependent helicase and ATPase required for nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. It is recruited to mRNAs upon translation termination and undergoes a cycle of phosphorylation and dephosphorylation; its phosphorylation appears to be a key step in NMD. It is recruited by release factors to stalled ribosomes together with the SMG1C protein kinase complex to form the transient SURF (SMG1-UPF1-eRF1-eRF3) complex. In EJC-dependent NMD, the SURF complex associates with the exon junction complex (EJC) located downstream from the termination codon through UPF2 and allows the formation of an UPF1-UPF2-UPF3 surveillance complex which is believed to activate NMD. Diseases associated with UPF1 include juvenile amyotrophic lateral sclerosis and epidermolysis bullosa, junctional, non-Herlitz type. UPF1 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: 350797 [Multi-domain]  Cd Length: 234  Bit Score: 74.98  E-value: 2.40e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  541 LIYGPFGTGKTYTLAMASLEVIRRPETKVLICTHTNSAAD-------------IYI----REYFHSHVS----------- 592
Cdd:cd18039     20 LIQGPPGTGKTVTSATIVYHLVKQGNGPVLVCAPSNVAVDqltekihqtglkvVRLcaksREAVESPVSflalhnqvrnl 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  593 GGHPEATPLRVMYTD-RPLSQTDPVTlqyccltdDRQAFRPPTRAELARHRVVVTTTSQARELRVPVGFFSHILIDEAAQ 671
Cdd:cd18039    100 DSAEKLELLKLLKLEtGELSSADEKR--------YRKLKRKAERELLRNADVICCTCVGAGDPRLSKMKFRTVLIDEATQ 171
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462581889  672 MLECEALTPLAYASHgtRLVLAGDHMQVTPRLFS--VARARAAeHTLLHRL--------FLCYQ 725
Cdd:cd18039    172 ATEPECLIPLVHGAK--QVILVGDHCQLGPVVMCkkAAKAGLS-QSLFERLvqlgirpiRLQVQ 232
DEXXQc_SMUBP2 cd18044
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ...
541-720 3.10e-14

DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, or IGHMBP2) is a 5' to 3' helicase that unwinds RNA and DNA duplexes in an ATP-dependent reaction. It is a DNA-binding protein specific to 5'-phosphorylated single-stranded guanine-rich sequence (5'-GGGCT-3') related to the immunoglobulin mu chain switch region. The IGHMBP2 gene is responsible for Charcot-Marie-Tooth disease (CMT) type 2S and spinal muscular atrophy with respiratory distress type 1 (SMARD1). It is also thought to play a role in frontotemporal dementia (FTD) with amyotrophic lateral sclerosis (ALS) and major depressive disorder (MDD). SMUBP2 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: 350802 [Multi-domain]  Cd Length: 191  Bit Score: 73.41  E-value: 3.10e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  541 LIYGPFGTGKTYTLAmaslEVIRR---PETKVLICTHTNSAADiYIREYFHSH----VSGGHPEatplRVMYTdrplsqt 613
Cdd:cd18044     21 LIHGPPGTGKTTTVV----EIILQavkRGEKVLACAPSNIAVD-NLVERLVALkvkvVRIGHPA----RLLES------- 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  614 dpvtLQYCCLTddrqafrpptraELARHRVVVTTTSQA--RELRVPVgFFSHILIDEAAQMLECEALTPLAYAShgtRLV 691
Cdd:cd18044     85 ----VLDHSLD------------ALVAAQVVLATNTGAgsRQLLPNE-LFDVVVIDEAAQALEASCWIPLLKAR---RCI 144
                          170       180       190
                   ....*....|....*....|....*....|
gi 2462581889  692 LAGDHMQVTPRLFSVARARAA-EHTLLHRL 720
Cdd:cd18044    145 LAGDHKQLPPTILSDKAARGGlGVTLFERL 174
EEXXQc_AQR cd17935
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds ...
2364-2461 1.79e-12

EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds precursor-mRNA introns at a defined position and is part of a pentameric intron-binding complex (IBC). It 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: 350693 [Multi-domain]  Cd Length: 207  Bit Score: 68.99  E-value: 1.79e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2364 VILCTCSCAAS--ASLKILDVR--QILVDEAGMATEPETLIPL-VQFPQAE-----KVVLLGDHKQLRPVVKNERLQNLG 2433
Cdd:cd17935     89 IIAMTCTHAALkrGELVELGFKydNILMEEAAQILEIETFIPLlLQNPEDGpnrlkRLIMIGDHHQLPPVIKNMAFQKYS 168
                           90       100       110
                   ....*....|....*....|....*....|..
gi 2462581889 2434 -LDRSLFERYHE---DAHMLDTQYRMHEGICA 2461
Cdd:cd17935    169 nMEQSLFTRLVRlgvPTVDLDAQGRARASISS 200
DExxQc_SF1-N cd17914
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ...
2348-2441 6.79e-12

DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members include UvrD/Rep, Pif1-like, and Upf-1-like proteins. Like SF2, they do not form toroidal, predominantly hexameric structures like SF3-6. 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. SF1 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: 438706 [Multi-domain]  Cd Length: 121  Bit Score: 64.81  E-value: 6.79e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2348 KKVLWEARKFELDRHEVILCTCSCAASASLkildvRQILVDEAGMATEPETLIPLVQFPQAEKVVLLGDHKQLRPVVKNE 2427
Cdd:cd17914     18 KIVAALMQNKNGEPGRILLVTPTNKAAAQL-----DNILVDEAAQILEPETSRLIDLALDQGRVILVGDHDQLGPVWRGA 92
                           90
                   ....*....|....
gi 2462581889 2428 RLQNLGLDRSLFER 2441
Cdd:cd17914     93 VLAKICNEQSLFTR 106
AAA_11 pfam13086
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
541-705 1.51e-10

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.


Pssm-ID: 404072 [Multi-domain]  Cd Length: 248  Bit Score: 63.90  E-value: 1.51e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  541 LIYGPFGTGKTYTLamasLEVIRR----------PETKVLICTHTNSAADIyIREYFHSHvsGGHPEATPLRVMYTDRPL 610
Cdd:pfam13086   17 LIQGPPGTGKTTTI----VELIRQllsypatsaaAGPRILVCAPSNAAVDN-ILERLLRK--GQKYGPKIVRIGHPAAIS 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  611 SQTDPVTLQY--------------------------------------------------------CCLTDDRQAFRPP- 633
Cdd:pfam13086   90 EAVLPVSLDYlvesklnneedaqivkdiskeleklakalrafekeiivekllksrnkdkskleqerRKLRSERKELRKEl 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  634 -------TRAELARHRVVVTT--TSQARELRVPVGFFShILIDEAAQMLECEALTPLAYASHgtRLVLAGDHMQVTPRLF 704
Cdd:pfam13086  170 rrreqslEREILDEAQIVCSTlsGAGSRLLSSLANFDV-VIIDEAAQALEPSTLIPLLRGPK--KVVLVGDPKQLPPTVI 246

                   .
gi 2462581889  705 S 705
Cdd:pfam13086  247 S 247
DEXXQc_Upf1-like cd17934
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ...
540-744 1.84e-10

DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, HELZ, Mov10L1, Aquarius, IGHMBP2 (SMUBP2), coronavirus Nsp13, and similar proteins. They belong 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: 438708 [Multi-domain]  Cd Length: 121  Bit Score: 60.71  E-value: 1.84e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  540 LLIYGPFGTGKTYTLAMASLEVIRRPETK-VLICTHTNSAADiyireyfhshvsgghpeatplrvmytdrplsqtdpvtl 618
Cdd:cd17934      2 SLIQGPPGTGKTTTIAAIVLQLLKGLRGKrVLVTAQSNVAVD-------------------------------------- 43
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  619 qyccltddrqafrpptraelarhrvvvtttsqarelRVPVgffshILIDEAAQMLECEAltpLAYASHGTRLVLAGDHMQ 698
Cdd:cd17934     44 ------------------------------------NVDV-----VIIDEASQITEPEL---LIALIRAKKVVLVGDPKQ 79
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2462581889  699 VTPRLFSVARARAAEHTLLHRLFLCyqQETHEVARQSRLVfhENYR 744
Cdd:cd17934     80 LPPVVQEDHAALLGLSFILSLLLLF--RLLLPGSPKVMLD--TQYR 121
DEXXQc_SETX cd18042
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in ...
541-723 1.13e-09

DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in transcription, neurogenesis, and antiviral response. SEXT is an R-loop-associated protein that is thought to function as an RNA/DNA helicase. R-loops consist of RNA/DNA hybrids, formed during transcription when nascent RNA hybridizes to the DNA template strand, displacing the non-template DNA strand. Mutations in SETX are linked to two neurodegenerative disorders: ataxia with oculomotor apraxia type 2 (AOA2) and amyotrophic lateral sclerosis type 4 (ALS4). S. cerevisiae homolog splicing endonuclease 1 (Sen1) is an exclusively nuclear protein, important for nucleolar organization. S. cerevisiae Sen1 and its ortholog, the Schizosaccharomyces pombe Sen1, share conserved domains and belong to the family I class of helicases. Both proteins translocate 5' to 3' and unwind both DNA and RNA duplexes and also RNA/DNA hybrids in vitro. SETX 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: 438712 [Multi-domain]  Cd Length: 218  Bit Score: 60.69  E-value: 1.13e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  541 LIYGPFGTGKTYTLaMASLEVI-------------------------RRPETKVLICTHTNSAADiyireyfhshvsggh 595
Cdd:cd18042     21 LIQGPPGTGKTKTI-VGILSVLlagkyrkyyekvkkklrklqrnlnnKKKKNRILVCAPSNAAVD--------------- 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  596 pEATpLRVMyTDRPLsQTDPVTLQYCCLTDDRQAFRpptRAELARHRVVVTTTSQA--RELRVPVGFFSHILIDEAAQML 673
Cdd:cd18042     85 -EIV-LRLL-SEGFL-DGDGRSYKPNVVRVGRQELR---ASILNEADIVCTTLSSSgsDLLESLPRGFDTVIIDEAAQAV 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462581889  674 ECEALTPLAYASHgtRLVLAGDHMQVTPRLFS-VARARAAEHTLLHRLFLC 723
Cdd:cd18042    158 ELSTLIPLRLGCK--RLILVGDPKQLPATVFSkVAQKLGYDRSLFERLQLA 206
PRK11642 PRK11642
ribonuclease R;
1334-1468 5.70e-09

ribonuclease R;


Pssm-ID: 236944 [Multi-domain]  Cd Length: 813  Bit Score: 61.68  E-value: 5.70e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 1334 REDCRAFLTFTVDPQGACNLDDALSV---RDLGPRCEVAvhITDVASFVPRDGVLDVEARRQGAAFYAPGrEPVPMLPAS 1410
Cdd:PRK11642   260 RVDLRDLPLVTIDGEDARDFDDAVYCekkRGGGWRLWVA--IADVSYYVRPPTPLDREARNRGTSVYFPS-QVVPMLPEV 336
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462581889 1411 LCQDVLSLLPGRDRLAISLFLTMEkASGQLKSLRFAPSVVQSDRQLSYE------EAEEVIRQH 1468
Cdd:PRK11642   337 LSNGLCSLNPQVDRLCMVCEMTIS-SKGRLTGYKFYEAVMSSHARLTYTkvwhilQGDQDLREQ 399
SF1_C cd18786
C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family ...
2545-2633 9.86e-09

C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family members include UvrD/Rep, Pif1-like, and Upf-1-like proteins. Similar to SF2 helicases, they do not form toroidal, predominantly hexameric structures like SF3-6. SF1 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: 350173 [Multi-domain]  Cd Length: 89  Bit Score: 54.75  E-value: 9.86e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2545 DIAVLTPYNAQASEISKALRREGI-----AGVAVSSITKSQGSEWRYVLVSTVRtcAKSDldqrptkswlkkflgfvvDP 2619
Cdd:cd18786     12 KGVVLTPYHRDRAYLNQYLQGLSLdefdlQLVGAITIDSSQGLTFDVVTLYLPT--ANSL------------------TP 71
                           90
                   ....*....|....
gi 2462581889 2620 NQVNVAVTRAQEGL 2633
Cdd:cd18786     72 RRLYVALTRARKRL 85
DEXXQc_HELZ cd18077
DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that ...
2358-2444 3.24e-08

DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that plays a role in RNA metabolism during development. HELZ is a member of the family I class of RNA helicases 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: 350835 [Multi-domain]  Cd Length: 226  Bit Score: 56.72  E-value: 3.24e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2358 ELDRHEVI---LCTCSCAASASLKILDVRQILVDEAGMATEPETLIPLVQFPQAEKVVLLGDHKQLRPVVKNERLQNLGL 2434
Cdd:cd18077    120 DVMRHRVVvvtLSTSQYLCQLDLEPGFFTHILLDEAAQAMECEAIMPLALATKSTRIVLAGDHMQLSPEVYSEFARERNL 199
                           90
                   ....*....|
gi 2462581889 2435 DRSLFERYHE 2444
Cdd:cd18077    200 HISLLERLYE 209
EEXXEc_NFX1 cd17936
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ...
541-703 7.84e-08

EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that represses class II MHC (major histocompatibility complex) gene expression. NFX1 binds a conserved cis-acting element, termed the X-box, in promoters of human class II MHC genes. The Cys-rich region contains several NFX1-type zinc finger domains. Frequently, a R3H domain is present in the C-terminus, and a RING finger domain and a PAM2 motif are present in the N-terminus. The lack of R3H and PAM2 motifs in the plant proteins indicates functional differences. Plant NFX1-like proteins are proposed to modulate growth and survival by coordinating reactive oxygen species, salicylic acid, further biotic stress and abscisic acid responses. A common feature of all members may be E3 ubiquitin ligase, due to the presence of a RING finger domain, as well as DNA binding. NFX1 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: 350694 [Multi-domain]  Cd Length: 178  Bit Score: 54.47  E-value: 7.84e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  541 LIYGPFGTGKTYT---LAMASLEVIRRPETK-VLICTHTNSAADiyireYFHSHVsgghpeatplrvmytdrplsqtdpv 616
Cdd:cd17936     20 LIQGPPGTGKTFLgvkLVRALLQNQDLSITGpILVVCYTNHALD-----QFLEGL------------------------- 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  617 tLQYCcltddrqafrpptRAELARH--RVV-VTTTSQAR------ELRVPVgffshILIDEAAQMLECEALTPLayASHG 687
Cdd:cd17936     70 -LDFG-------------PTKIVRLgaRVIgMTTTGAAKyrellqALGPKV-----VIVEEAAEVLEAHILAAL--TPST 128
                          170
                   ....*....|....*.
gi 2462581889  688 TRLVLAGDHMQVTPRL 703
Cdd:cd17936    129 EHLILIGDHKQLRPKV 144
EEXXQc_AQR cd17935
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds ...
524-720 2.07e-07

EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds precursor-mRNA introns at a defined position and is part of a pentameric intron-binding complex (IBC). It 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: 350693 [Multi-domain]  Cd Length: 207  Bit Score: 53.97  E-value: 2.07e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  524 ALIAGWGPGdgrrvpPLLIYGPFGTGKTyTLAMASLEVIRR--PETKVLICTHTNSAADIYIREYFHSHVSGGHPeatpL 601
Cdd:cd17935     13 AIRSGMQPG------LTMVVGPPGTGKT-DVAVQIISNLYHnfPNQRTLIVTHSNQALNQLFEKIMALDIDERHL----L 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  602 RVMYTDRPLSQTdpvtlqycCltddrqafrppTRAELARHRVVvtttsqarELrvpvGF-FSHILIDEAAQMLECEALTP 680
Cdd:cd17935     82 RLGHGAKIIAMT--------C-----------THAALKRGELV--------EL----GFkYDNILMEEAAQILEIETFIP 130
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2462581889  681 LAYASHGT------RLVLAGDHMQVTPRLFSVARARAA--EHTLLHRL 720
Cdd:cd17935    131 LLLQNPEDgpnrlkRLIMIGDHHQLPPVIKNMAFQKYSnmEQSLFTRL 178
DEXXQc_HELZ2-N cd18076
N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ...
2356-2455 3.38e-06

N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known as PPAR-alpha-interacting complex protein 285 or PRIC285 and PPAR-gamma DBD-interacting protein 1 or PDIP1) acts as a transcriptional coactivator for a number of nuclear receptors including PPARA, PPARG, THRA, THRB, and RXRA. It 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: 350834 [Multi-domain]  Cd Length: 230  Bit Score: 50.66  E-value: 3.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2356 KFELDRHEVILCTCSCAASASLKILDVRQILVDEAGMATEPETLIPLVQFPQAEKVVLLGDHKQLRP---VVKNERLQNL 2432
Cdd:cd18076    121 RDELDFHNIVITTTAMAFNLHVLSGFFTHIFIDEAAQMLECEALIPLSYAGPKTRVVLAGDHMQMTPklfSVADYNRANH 200
                           90       100
                   ....*....|....*....|...
gi 2462581889 2433 GLDRSLFERYHEDAHMLDTQYRM 2455
Cdd:cd18076    201 TLLNRLFHYYQGEKHEVAVKSRV 223
DEXXQc_SF1 cd18043
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are ...
2182-2213 6.60e-06

DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are nucleic acid motor proteins that couple ATP hydrolysis to translocation along with the concomitant unwinding of DNA or RNA. This is central to many aspects of cellular DNA and RNA metabolism and accordingly, they are implicated in a wide range of nucleic acid processing events including DNA replication, recombination, and repair as well as many aspects of RNA metabolism. Superfamily 1 helicases are members 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: 350801 [Multi-domain]  Cd Length: 127  Bit Score: 47.58  E-value: 6.60e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2462581889 2182 NPSQNVAVREALEKPFTVIQGPPGTGK--TIVGL 2213
Cdd:cd18043      1 DSSQEAAIISARNGKNVVIQGPPGTGKsqTIANI 34
DEXXc_HELZ2-C cd18040
C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ...
538-736 1.65e-05

C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known as PPAR-alpha-interacting complex protein 285 or PRIC285 and PPAR-gamma DBD-interacting protein 1 or PDIP1) acts as a transcriptional coactivator for a number of nuclear receptors including PPARA, PPARG, THRA, THRB and RXRA. It 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: 350798 [Multi-domain]  Cd Length: 271  Bit Score: 49.06  E-value: 1.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  538 PPLLIYGPFGTGKTYT------------LAMASLEVIRRPETKVLICTHTNSAADIY------------IREY------- 586
Cdd:cd18040     17 PFTLIQGPPGTGKTVTgvhiaywfakqnREIQSVSGEGDGGPCVLYCGPSNKSVDVVaelllkvpglkiLRVYseqiett 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  587 -FHSHVSGGHPEATPLRvmyTDRPLSQTDPVTLQYCCltddRQAFRPPTRA----------------------------- 636
Cdd:cd18040     97 eYPIPNEPRHPNKKSER---ESKPNSELSSITLHHRI----RQPSNPHSQQikafearfertqekiteediktykiliwe 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889  637 ----ELARHRVVVTTTSQA--RELRVPVGFfSHILIDEAAQMLECEALTPLAYASHGTRLVLAGDHMQVTPrlfSVARAR 710
Cdd:cd18040    170 arfeELETVDVILCTCSEAasQKMRTHANV-KQCIVDECGMCTEPESLIPIVSAPRAEQVVLIGDHKQLRP---VVQNKE 245
                          250       260
                   ....*....|....*....|....*.
gi 2462581889  711 AAEHTLLHRLFLCYQQETHEVARQSR 736
Cdd:cd18040    246 AQKLGLGRSLFERYAEKACMLDTQYR 271
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
2175-2585 2.74e-05

ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];


Pssm-ID: 440273 [Multi-domain]  Cd Length: 514  Bit Score: 49.59  E-value: 2.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2175 PGGRHKLNPSQNVAVREALEK-PFTVIQGPPGTGKTIVGLHIVFWFHKSNQEqvqpggpprgekrlggpcILYCGPSNKS 2253
Cdd:COG0507    119 PRAGITLSDEQREAVALALTTrRVSVLTGGAGTGKTTTLRALLAALEALGLR------------------VALAAPTGKA 180
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2254 VDVLaglllrrmelkplrvyseqAEASEFPvprvgsrkllrkspregrpnqslrSITLHHRIRQAPNpysseikafdtrl 2333
Cdd:COG0507    181 AKRL-------------------SESTGIE------------------------ARTIHRLLGLRPD------------- 204
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2334 qrgelfsredlvwykkvlweARKFELDRHEVilctcscaasasLKILDVrqILVDEAGMATEP--ETLIPLVQFPQAeKV 2411
Cdd:COG0507    205 --------------------SGRFRHNRDNP------------LTPADL--LVVDEASMVDTRlmAALLEALPRAGA-RL 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2412 VLLGDHKQLRPVVKNERLqnlgldRSLFERYHEDAHMLDTQYRMHEGIcAFPSVAfyksklktwQGLR--RPPSVLGHAG 2489
Cdd:COG0507    250 ILVGDPDQLPSVGAGAVL------RDLIESGTVPVVELTEVYRQADDS-RIIELA---------HAIRegDAPEALNARY 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2490 KEscpVIFGHVQGHERSllvstdegnenskanLEEVAEVVRitkqltlGRTVEPQDIAVLTPYNAQASEISKALRRE-GI 2568
Cdd:COG0507    314 AD---VVFVEAEDAEEA---------------AEAIVELYA-------DRPAGGEDIQVLAPTNAGVDALNQAIREAlNP 368
                          410
                   ....*....|....*..
gi 2462581889 2569 AGVAVSSITKSQGSEWR 2585
Cdd:COG0507    369 AGELERELAEDGELELY 385
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
2185-2209 1.28e-04

DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD 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: 350691 [Multi-domain]  Cd Length: 155  Bit Score: 44.85  E-value: 1.28e-04
                           10        20
                   ....*....|....*....|....*
gi 2462581889 2185 QNVAVREALEKPFTVIQGPPGTGKT 2209
Cdd:cd17933      2 QKAAVRLVLRNRVSVLTGGAGTGKT 26
SF1_C_UvrD cd18807
C-terminal helicase domain of UvrD family helicases; UvrD is a highly conserved helicase ...
2496-2587 1.72e-04

C-terminal helicase domain of UvrD family helicases; UvrD is a highly conserved helicase involved in mismatch repair, nucleotide excision repair, and recombinational repair. It plays a critical role in maintaining genomic stability and facilitating DNA lesion repair in many prokaryotic species including Helicobacter pylori and Escherichia coli. This family also includes ATP-dependent helicase/nuclease AddA and helicase/nuclease RecBCD subunit RecB, among others. UvrD family helicases are DEAD-like helicases belonging to superfamily (SF)1, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF2 helicases, SF1 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: 350194 [Multi-domain]  Cd Length: 150  Bit Score: 44.14  E-value: 1.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2496 IFGHVQGHERSLLVStdeGNENSKA-----NLEEVAEVVRIT---KQLTLGRTVEPQDIAVLTPYNAQASEISKALRreg 2567
Cdd:cd18807     12 LIKQNKNRPKKPLKA---GNKSGGPvelllAKDEADEAKAIAdeiKRLIESGPVQYSDIAILVRTNRQARVIEEALR--- 85
                           90       100
                   ....*....|....*....|
gi 2462581889 2568 iagVAVSSITKSQGSEWRYV 2587
Cdd:cd18807     86 ---VTLMTIHASKGLEFPVV 102
CoV_Nsp13-helicase cd21718
helicase domain of coronavirus non-structural protein 13; This model represents the helicase ...
2385-2636 4.35e-04

helicase domain of coronavirus non-structural protein 13; This model represents the helicase domain of non-structural protein 13 (Nsp13) from alpha-, beta-, gamma-, and deltacoronavirus, including pathogenic human viruses such as Severe acute respiratory syndrome coronavirus (SARS-CoV), SARS-CoV2 (also called 2019 novel CoV or 2019-nCoV), and Middle East respiratory syndrome-related (MERS) CoV. Helicases catalyze NTP-dependent unwinding of nucleic acid duplexes into single strands and are classified based on the arrangement of conserved motifs into six superfamilies. CoV Nsp13 is a member of the helicase superfamily 1 (SF1); SF1 and SF2 helicases do not form toroidal structures, while SF3-6 helicases do. Nsp13 is a component of the viral RNA synthesis replication and transcription complex (RTC). It is a multidomain protein containing a Cys/His rich zinc-binding domain (CH/ZBD), a stalk domain, a 1B domain involved in nucleic acid substrate binding, and a SF1 helicase core.


Pssm-ID: 409652 [Multi-domain]  Cd Length: 341  Bit Score: 45.21  E-value: 4.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2385 ILVDEAGMATEPEtLIPLVQFPQAEKVVLLGDHKQL---RPVVKNERLQNLGLDRSLFERYHEDAH-MLDTQYRMHEGIC 2460
Cdd:cd21718    121 VVVDEVSMCTNYD-LSVVNARLKYKHIVYVGDPAQLpapRTLLTEGSLEPKDYNVVTRLMVGSGPDvFLSKCYRCPKEIV 199
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2461 AFPSVAFYKSKLKTwqglrrppsvlGHAGKESCPVIFGhvqghersllvSTDEGNENSKANLEEVAEVVRitkqLTLGRT 2540
Cdd:cd21718    200 DTVSKLVYDNKLKA-----------IKPKSRQCFKTFG-----------KGDVRHDNGSAINRPQLEFVK----RFLDRN 253
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2541 VEPQDIAVLTPYNAQASEISKalrregIAGVAVSSITKSQGSEWRYVLVstvrtCAKSDLDQrptkswlkkflgfVVDPN 2620
Cdd:cd21718    254 PRWRKAVFISPYNAMNNRASR------LLGLSTQTVDSSQGSEYDYVIF-----CQTTDTAH-------------ALNIN 309
                          250
                   ....*....|....*.
gi 2462581889 2621 QVNVAVTRAQEGLCLI 2636
Cdd:cd21718    310 RFNVAITRAKHGILVI 325
betaCoV_Nsp13-helicase cd21722
helicase domain of betacoronavirus non-structural protein 13; This model represents the ...
2549-2641 8.34e-04

helicase domain of betacoronavirus non-structural protein 13; This model represents the helicase domain of non-structural protein 13 (Nsp13) from betacoronavirus, including pathogenic human viruses such as Severe acute respiratory syndrome coronavirus (SARS-CoV), SARS-CoV2 (also called 2019 novel CoV or 2019-nCoV), and Middle East respiratory syndrome-related (MERS) CoV. Helicases catalyze NTP-dependent unwinding of nucleic acid duplexes into single strands and are classified based on the arrangement of conserved motifs into six superfamilies. CoV Nsp13 is a member of the helicase superfamily 1 (SF1); SF1 and SF2 helicases do not form toroidal structures, while SF3-6 helicases do. Nsp13 is a component of the viral RNA synthesis replication and transcription complex (RTC). It is a multidomain protein containing a Cys/His rich zinc-binding domain (CH/ZBD), a stalk domain, a 1B domain involved in nucleic acid substrate binding, and a SF1 helicase core.


Pssm-ID: 409655 [Multi-domain]  Cd Length: 340  Bit Score: 44.41  E-value: 8.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581889 2549 LTPYNAQASEISKALrregiaGVAVSSITKSQGSEWRYVLVSTVRTCAKSdldqrptkswlkkflgfvVDPNQVNVAVTR 2628
Cdd:cd21722    262 ISPYNSQNAVARRVL------GLQTQTVDSSQGSEYDYVIYCQTAETAHS------------------VNVNRFNVAITR 317
                           90
                   ....*....|....
gi 2462581889 2629 AQEG-LCLIGDHLL 2641
Cdd:cd21722    318 AKKGiLCVMSSMQL 331
DExxQc_SF1-N cd17914
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ...
539-586 1.31e-03

DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members include UvrD/Rep, Pif1-like, and Upf-1-like proteins. Like SF2, they do not form toroidal, predominantly hexameric structures like SF3-6. 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. SF1 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: 438706 [Multi-domain]  Cd Length: 121  Bit Score: 40.93  E-value: 1.31e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462581889  539 PLLIYGPFGTGKTYTLA---MASLEVIRRPETKVLICTHTNSAAD----IYIREY 586
Cdd:cd17914      1 LSLIQGPPGTGKTRVLVkivAALMQNKNGEPGRILLVTPTNKAAAqldnILVDEA 55
HelD COG3973
DNA helicase IV [Replication, recombination and repair];
2185-2214 1.89e-03

DNA helicase IV [Replication, recombination and repair];


Pssm-ID: 443173 [Multi-domain]  Cd Length: 699  Bit Score: 43.70  E-value: 1.89e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 2462581889 2185 QNVAVREALEKPfTVIQGPPGTGKTIVGLH 2214
Cdd:COG3973    196 QDRIIRADLRGV-LVVQGGAGSGKTAVALH 224
zf-C2H2_jaz pfam12171
Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, ...
39-64 4.64e-03

Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, and is approximately 30 amino acids in length. The mammalian members of this group occur multiple times along the protein, joined by flexible linkers, and are referred to as JAZ - dsRNA-binding ZF protein - zinc-fingers. The JAZ proteins are expressed in all tissues tested and localize in the nucleus, particularly the nucleolus. JAZ preferentially binds to double-stranded (ds) RNA or RNA/DNA hybrids rather than DNA. In addition to binding double-stranded RNA, these zinc-fingers are required for nucleolar localization.


Pssm-ID: 432381 [Multi-domain]  Cd Length: 27  Bit Score: 36.76  E-value: 4.64e-03
                           10        20
                   ....*....|....*....|....*.
gi 2462581889   39 QLYCPACLVTCHSQEAFENHCASSEH 64
Cdd:pfam12171    1 QFYCVLCDKYFKSENALQNHLKSKKH 26
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
519-590 5.73e-03

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 39.82  E-value: 5.73e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462581889  519 QELAVALIAGWGPGdgRRVPPLLIYGPFGTGKTyTLAMASLEVIRRPETKVLICTHTNSAADIYIREYFHSH 590
Cdd:cd00009      3 QEEAIEALREALEL--PPPKNLLLYGPPGTGKT-TLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHF 71
ZnF_U1 smart00451
U1-like zinc finger; Family of C2H2-type zinc fingers, present in matrin, U1 small nuclear ...
39-69 5.83e-03

U1-like zinc finger; Family of C2H2-type zinc fingers, present in matrin, U1 small nuclear ribonucleoprotein C and other RNA-binding proteins.


Pssm-ID: 197732 [Multi-domain]  Cd Length: 35  Bit Score: 36.46  E-value: 5.83e-03
                            10        20        30
                    ....*....|....*....|....*....|.
gi 2462581889    39 QLYCPACLVTCHSQEAFENHCASSEHAQMVA 69
Cdd:smart00451    3 GFYCKLCNVTFTDEISVEAHLKGKKHKKNVK 33
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
2378-2423 7.90e-03

DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD 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: 350691 [Multi-domain]  Cd Length: 155  Bit Score: 39.46  E-value: 7.90e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2462581889 2378 KILDVRQILVDEAGMATEP--ETLIPLVqfPQAEKVVLLGDHKQLRPV 2423
Cdd:cd17933     86 NPLDADLLIVDEASMVDTRlmAALLSAI--PAGARLILVGDPDQLPSV 131
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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