|
Name |
Accession |
Description |
Interval |
E-value |
| DNA2 |
COG1112 |
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair]; |
448-1272 |
3.38e-60 |
|
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
Pssm-ID: 440729 [Multi-domain] Cd Length: 819 Bit Score: 223.08 E-value: 3.38e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 448 LATALGGLRAIAENESATYRIDDVDLSPADVGAWLREHAAHGGIPDPIAPTDRPPLSADEFATLLSLAARITHADRTAAL 527
Cdd:COG1112 3 ALLLDAARALLALLALALLALLLALALLLDLLLLLLLAAALLLLALALALLLLALRALELLDLLAALALLLLLLLLDAEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 528 RPLPDVAALPDARTAKQARADRDAAADRVSRLELAGVDTDSVRAHGPNPVAALREGLTDAIAWLHRREGTWTDRLGRLLA 607
Cdd:COG1112 83 LLLALRALLLLLAAELLLLLLLLLLLAALLLALAALLLALALLLLALALLALLALLLAELLDLLAALAALAALLAALLLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 608 DPHWATVWTDHVTATEDLQRALADLARLLGGHRVTVANALAAEPKRLLAGLGELRERFAAGKGVNRLLQAGLWRIAEEVR 687
Cdd:COG1112 163 LLLLAALLLLDLRLLALLELLLAAALALALLALLALALEDELALLLLLLLLALLLLLALLLLLDALLLLLAALALLALAL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 688 VDGEPLRTVEDVDLAAAWVRRGQAQRRLGEHWAEWIQRLGIPARQGDPEVWAGTLLAEAAQSLGWDAREWPELSARLRVL 767
Cdd:COG1112 243 LLALLLLLLALLLLAALALLRAALRLDLLAALELLAALSLALLALLAALALALLLLAALALLLALALAALLALLALLALL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 768 VPQEELDLDAARLAEVAALLDDSPVVFDLDELDARDRAVADSLVPWPELAAAWFDPELAEWDGLVAEARRLTAIRPEAAR 847
Cdd:COG1112 323 AARLAAALAALLLLLLLEELALLAALLLLLELALLRLLAALLLALALLLLLALEELLLLALLRLLAEGLALLLLLLLAAL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 848 YVELLDRLGELAPEWAGQIDAGQVPAVPGTACLHAWQWRQAQTWFDLVVGSVDPAVLNRRVELGRDKIRRLTGDLVVA-S 926
Cdd:COG1112 403 LRLARALLLLALLLAAAAAALAALLLLALALLAALLALLLLLAAALAALLALLLLLLLALAALLLLLAAAAALLALALlE 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 927 AWLEVARSLDDRRRAALADWTTALRKIGKGTGRTAAAWQAHAQRAMESAVEAVPVWVMSVDRAIEQF-AGGAHFDVVIVD 1005
Cdd:COG1112 483 SLLEELIEEHPEELEKLIAELREAARLRRALRRELKKRRELRKLLWDALLELAPVVGMTPASVARLLpLGEGSFDLVIID 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 1006 EASQADL-FALPVLSLAERAVVVGDDQQIGPQlgfvgsvsglihSHLDDVPSAEHFDPESSLYDHAVRRSPER-ILLTEH 1083
Cdd:COG1112 563 EASQATLaEALGALARAKRVVLVGDPKQLPPV------------VFGEEAEEVAEEGLDESLLDRLLARLPERgVMLREH 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 1084 FRCVPQIIEFSSRHYYDGKIQPLR--ADRPLSTPVRPV-FIA-DGVRQPlPPYGDVNVAEADALVAQVAAIVADpDYRGK 1159
Cdd:COG1112 631 YRMHPEIIAFSNRLFYDGKLVPLPspKARRLADPDSPLvFIDvDGVYER-RGGSRTNPEEAEAVVELVRELLED-GPDGE 708
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 1160 TLGVISLLSTsgQANYLLQALREAIGedeMEARRLRVGDAYTFQGDERDVVLVSMVVSDNDGRLAAFTK-REYHRRVNVA 1238
Cdd:COG1112 709 SIGVITPYRA--QVALIRELLREALG---DGLEPVFVGTVDRFQGDERDVIIFSLVYSNDEDVPRNFGFlNGGPRRLNVA 783
|
810 820 830
....*....|....*....|....*....|....*
gi 556602761 1239 ASRARDQLWIFHSVRPQSLLADD-ARALLLNYAQN 1272
Cdd:COG1112 784 VSRARRKLIVVGSRELLDSDPSTpALKRLLEYLER 818
|
|
| MTES_1575 |
pfam18741 |
REase_MTES_1575; Vsr REase Fold. Fused to HEPN (SWT1/Abi2 family), along with Transglutaminase ... |
1290-1384 |
1.33e-34 |
|
REase_MTES_1575; Vsr REase Fold. Fused to HEPN (SWT1/Abi2 family), along with Transglutaminase and wHTH.
Pssm-ID: 465853 Cd Length: 96 Bit Score: 127.59 E-value: 1.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 1290 FERDVLRRLVKRGYRPTPQFRIGGYRIDFVLNAPDGR-RLAIECDGDAYHG-PEQWESDMRRQAVLERVGnCVFVRIRGS 1367
Cdd:pfam18741 1 FEEEVAEALRERGYRVVPQVGVGGYRIDLVVVDPPGRyRLGIECDGATYHSsKSARDRDRLRQRVLERLG-WKFHRIWST 79
|
90
....*....|....*..
gi 556602761 1368 IFAREPEAALRPLWQRI 1384
Cdd:pfam18741 80 DWYRDPEAELERLWEAL 96
|
|
| SF1_C_Upf1 |
cd18808 |
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ... |
1086-1271 |
1.45e-32 |
|
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: 125.42 E-value: 1.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 1086 CVPQIIEFSSRHYYDGKIQPLRADR------PLSTPVRPVF---IADGVRQPLPPYGDVNVAEADALVAQVAAIVADPdY 1156
Cdd:cd18808 1 MHPEISEFPSKLFYEGKLKAGVSVAarlnppPLPGPSKPLVfvdVSGGEEREESGTSKSNEAEAELVVELVKYLLKSG-V 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 1157 RGKTLGVISLLStsGQANYLLQALREAIGEDEmearRLRVGDAYTFQGDERDVVLVSMVVSDNDGRLAAFTKREyhRRVN 1236
Cdd:cd18808 80 KPSSIGVITPYR--AQVALIRELLRKRGGLLE----DVEVGTVDNFQGREKDVIILSLVRSNESGGSIGFLSDP--RRLN 151
|
170 180 190
....*....|....*....|....*....|....*
gi 556602761 1237 VAASRARDQLWIFHSvrPQSLLADDARALLLNYAQ 1271
Cdd:cd18808 152 VALTRAKRGLIIVGN--PDTLSKDPLWKKLLEYLE 184
|
|
| DEXXQc_SF1 |
cd18043 |
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are ... |
328-386 |
2.39e-23 |
|
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: 96.88 E-value: 2.39e-23
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 556602761 328 NEAQESIARRLAQHRNVAVQGPPGTGKTHTIRNLICHLMANGKRVLVVAQKEDPLRVLR 386
Cdd:cd18043 1 DSSQEAAIISARNGKNVVIQGPPGTGKSQTIANIIANALARGKRVLFVSEKKAALDVVR 59
|
|
| AAA_12 |
pfam13087 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1065-1248 |
1.29e-22 |
|
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: 96.85 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 1065 SLYDHAVRRSPER-ILLTEHFRCVPQIIEFSSRHYYDGKIQ--------PLRADRPLSTPVRP-VFI-ADGVRQPLPPYG 1133
Cdd:pfam13087 4 SLFERLQELGPSAvVMLDTQYRMHPEIMEFPSKLFYGGKLKdgpsvaerPLPDDFHLPDPLGPlVFIdVDGSEEEESDGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 1134 D--VNVAEADALVAQVAAIVAD-PDYRGKtLGVISLlstsgqanYLLQ--ALREAIGEDEMEARRLRVG--DAytFQGDE 1206
Cdd:pfam13087 84 TsySNEAEAELVVQLVEKLIKSgPEEPSD-IGVITP--------YRAQvrLIRKLLKRKLGGKLEIEVNtvDG--FQGRE 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 556602761 1207 RDVVLVSMVVSDNDGRLaAFTKREyhRRVNVAASRARDQLWI 1248
Cdd:pfam13087 153 KDVIIFSCVRSNEKGGI-GFLSDP--RRLNVALTRAKRGLII 191
|
|
| YcjD |
COG2852 |
Very-short-patch-repair endonuclease [Replication, recombination and repair]; |
1286-1387 |
6.70e-21 |
|
Very-short-patch-repair endonuclease [Replication, recombination and repair];
Pssm-ID: 442100 Cd Length: 104 Bit Score: 88.77 E-value: 6.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 1286 CESGFERDV---LRRLVKRGYRPTPQFRIGGYRIDFVLNapdGRRLAIECDGDAYHGPEQWESDMRRQAVLERVGNCVfV 1362
Cdd:COG2852 4 NDTPAERRLwqrLRNRQLRGLKFRRQVPIGGYIVDFYCP---EARLAIEVDGGYHGSPEQRERDRRRDAYLERLGWRV-L 79
|
90 100
....*....|....*....|....*
gi 556602761 1363 RIRGSIFAREPEAALRPLWQRIEEL 1387
Cdd:COG2852 80 RFWNEDVLRNPEGVLEEILAALEER 104
|
|
| Endonuclease_DUF559 |
cd01038 |
Putative endonuclease; Domain of unknown function 559 (DUF559) is a putative endonuclease of ... |
1295-1384 |
5.06e-09 |
|
Putative endonuclease; Domain of unknown function 559 (DUF559) is a putative endonuclease of unknown function, belongs to a superfamily of nucleases including very short patch repair (Vsr) endonucleases, archaeal Holliday junction resolvases, MutH methyl-directed DNA mismatch-repair endonucleases, and catalytic domains of many restriction endonucleases, such as EcoRI, BamHI, and FokI.
Pssm-ID: 411708 Cd Length: 97 Bit Score: 54.90 E-value: 5.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 1295 LRRLVKRGYRPTPQFRIGGYRIDFVLNApdgRRLAIECDGDAYHGPEQWESDMRRQAVLERVGNCVfVRIRGSIFAREPE 1374
Cdd:cd01038 12 LRNRQFLGLKFRRQKPIGFYIVDFYCAE---KKLVIEIDGGQHHEKKAEEYDARRDKYLESLGYTV-LRFWNEEVLNNIE 87
|
90
....*....|
gi 556602761 1375 AALRPLWQRI 1384
Cdd:cd01038 88 GVLEKIEKFL 97
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
50-644 |
2.47e-06 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 52.57 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 50 VEVGPALDGTSWLRVGLPDLPPPVAVPAeLRRrlnqvsatdepkvgdEDDEFETWRD---EVWR-----PWSLLSQEAEK 121
Cdd:COG3321 795 LEVGPGPVLTGLVRQCLAAAGDAVVLPS-LRR---------------GEDELAQLLTalaQLWVagvpvDWSALYPGRGR 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 122 T----------RTLHRQLFDLMHQVDMTAATTELVWGHGLLETTIGEQRVRYPLVATPVIIEYEPDRSLITVSPQGPSRL 191
Cdd:COG3321 859 RrvplptypfqREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAA 938
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 192 QTDALAGLDERYLSQLLGLAGPAGTLEVDLWDVLERQELFERALGRLGYDRRVIKPGESAVGPHLVDTGVLFARPKQRLL 271
Cdd:COG3321 939 AAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAA 1018
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 272 RGFLESLRDRLLAGDTSSIGALAAIVAHEPSKLRMPDDQPENWHRVGERLLMPLPTNEAQESIARRLAQHRNVAVQGPPG 351
Cdd:COG3321 1019 AALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALA 1098
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 352 TGKTHTIRNLICHLMANGKRVLVVAQKEDPLRVLRDGLPEEVQALCLAVLGRTTDQLVQLQLAARELSDRAATLDKTAEA 431
Cdd:COG3321 1099 LAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALA 1178
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 432 GRVERLTKRLEDAERDLATALGGLRAIAENESATyriddVDLSPADVGAWLREHAAHGGIPDPIAPTDRPPLSADEFATL 511
Cdd:COG3321 1179 LALAAALAAALAGLAALLLAALLAALLAALLALA-----LAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAA 1253
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 512 LSLAARITHADRTAALRPLPDVAALPDARTAKQARADRDAAADRVSRLELAGVDTDSVRAHGPNPVAALREGLTDAIAWL 591
Cdd:COG3321 1254 ALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAAL 1333
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 556602761 592 HRREGTWTDRLGRLLADPHWATVWTDHVTATEDLQRALADLARLLGGHRVTVA 644
Cdd:COG3321 1334 AAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAAVA 1386
|
|
| RecD |
COG0507 |
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
297-376 |
1.45e-04 |
|
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: 46.12 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 297 VAHEPSKLRMPDDQPENWHRVGERLLMPLPT--NEAQESIARRLA-QHRNVAVQGPPGTGKTHTIRNLICHLMANGKRVL 373
Cdd:COG0507 93 LARRLRRLARPALDEADVEAALAALEPRAGItlSDEQREAVALALtTRRVSVLTGGAGTGKTTTLRALLAALEALGLRVA 172
|
...
gi 556602761 374 VVA 376
Cdd:COG0507 173 LAA 175
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
340-420 |
2.06e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 43.13 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 340 QHRNVAVQGPPGTGKTHTIRNLICHLMANGKRVLVVAqKEDPLRVLRDGLPEEVQALCLAVLGRTTDQLVQLQLAARELS 419
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYID-GEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKP 79
|
.
gi 556602761 420 D 420
Cdd:smart00382 80 D 80
|
|
| AAA_19 |
pfam13245 |
AAA domain; |
331-376 |
2.19e-04 |
|
AAA domain;
Pssm-ID: 433059 [Multi-domain] Cd Length: 136 Bit Score: 42.59 E-value: 2.19e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 556602761 331 QESIARRLAQHRNVAVQGPPGTGKTHTIRNLICHLMANG---KRVLVVA 376
Cdd:pfam13245 1 QREAVRTALPSKVVLLTGGPGTGKTTTIRHIVALLVALGgvsFPILLAA 49
|
|
| TIGR00376 |
TIGR00376 |
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ... |
328-376 |
2.31e-03 |
|
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: 42.49 E-value: 2.31e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 556602761 328 NEAQ-ESIARRLAQHRNVAVQGPPGTGKTHTIRNLICHLMANGKRVLVVA 376
Cdd:TIGR00376 159 NESQkEAVLFALSSKDLFLIHGPPGTGKTRTVVELIRQLVKRGLRVLVTA 208
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DNA2 |
COG1112 |
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair]; |
448-1272 |
3.38e-60 |
|
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
Pssm-ID: 440729 [Multi-domain] Cd Length: 819 Bit Score: 223.08 E-value: 3.38e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 448 LATALGGLRAIAENESATYRIDDVDLSPADVGAWLREHAAHGGIPDPIAPTDRPPLSADEFATLLSLAARITHADRTAAL 527
Cdd:COG1112 3 ALLLDAARALLALLALALLALLLALALLLDLLLLLLLAAALLLLALALALLLLALRALELLDLLAALALLLLLLLLDAEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 528 RPLPDVAALPDARTAKQARADRDAAADRVSRLELAGVDTDSVRAHGPNPVAALREGLTDAIAWLHRREGTWTDRLGRLLA 607
Cdd:COG1112 83 LLLALRALLLLLAAELLLLLLLLLLLAALLLALAALLLALALLLLALALLALLALLLAELLDLLAALAALAALLAALLLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 608 DPHWATVWTDHVTATEDLQRALADLARLLGGHRVTVANALAAEPKRLLAGLGELRERFAAGKGVNRLLQAGLWRIAEEVR 687
Cdd:COG1112 163 LLLLAALLLLDLRLLALLELLLAAALALALLALLALALEDELALLLLLLLLALLLLLALLLLLDALLLLLAALALLALAL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 688 VDGEPLRTVEDVDLAAAWVRRGQAQRRLGEHWAEWIQRLGIPARQGDPEVWAGTLLAEAAQSLGWDAREWPELSARLRVL 767
Cdd:COG1112 243 LLALLLLLLALLLLAALALLRAALRLDLLAALELLAALSLALLALLAALALALLLLAALALLLALALAALLALLALLALL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 768 VPQEELDLDAARLAEVAALLDDSPVVFDLDELDARDRAVADSLVPWPELAAAWFDPELAEWDGLVAEARRLTAIRPEAAR 847
Cdd:COG1112 323 AARLAAALAALLLLLLLEELALLAALLLLLELALLRLLAALLLALALLLLLALEELLLLALLRLLAEGLALLLLLLLAAL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 848 YVELLDRLGELAPEWAGQIDAGQVPAVPGTACLHAWQWRQAQTWFDLVVGSVDPAVLNRRVELGRDKIRRLTGDLVVA-S 926
Cdd:COG1112 403 LRLARALLLLALLLAAAAAALAALLLLALALLAALLALLLLLAAALAALLALLLLLLLALAALLLLLAAAAALLALALlE 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 927 AWLEVARSLDDRRRAALADWTTALRKIGKGTGRTAAAWQAHAQRAMESAVEAVPVWVMSVDRAIEQF-AGGAHFDVVIVD 1005
Cdd:COG1112 483 SLLEELIEEHPEELEKLIAELREAARLRRALRRELKKRRELRKLLWDALLELAPVVGMTPASVARLLpLGEGSFDLVIID 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 1006 EASQADL-FALPVLSLAERAVVVGDDQQIGPQlgfvgsvsglihSHLDDVPSAEHFDPESSLYDHAVRRSPER-ILLTEH 1083
Cdd:COG1112 563 EASQATLaEALGALARAKRVVLVGDPKQLPPV------------VFGEEAEEVAEEGLDESLLDRLLARLPERgVMLREH 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 1084 FRCVPQIIEFSSRHYYDGKIQPLR--ADRPLSTPVRPV-FIA-DGVRQPlPPYGDVNVAEADALVAQVAAIVADpDYRGK 1159
Cdd:COG1112 631 YRMHPEIIAFSNRLFYDGKLVPLPspKARRLADPDSPLvFIDvDGVYER-RGGSRTNPEEAEAVVELVRELLED-GPDGE 708
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 1160 TLGVISLLSTsgQANYLLQALREAIGedeMEARRLRVGDAYTFQGDERDVVLVSMVVSDNDGRLAAFTK-REYHRRVNVA 1238
Cdd:COG1112 709 SIGVITPYRA--QVALIRELLREALG---DGLEPVFVGTVDRFQGDERDVIIFSLVYSNDEDVPRNFGFlNGGPRRLNVA 783
|
810 820 830
....*....|....*....|....*....|....*
gi 556602761 1239 ASRARDQLWIFHSVRPQSLLADD-ARALLLNYAQN 1272
Cdd:COG1112 784 VSRARRKLIVVGSRELLDSDPSTpALKRLLEYLER 818
|
|
| MTES_1575 |
pfam18741 |
REase_MTES_1575; Vsr REase Fold. Fused to HEPN (SWT1/Abi2 family), along with Transglutaminase ... |
1290-1384 |
1.33e-34 |
|
REase_MTES_1575; Vsr REase Fold. Fused to HEPN (SWT1/Abi2 family), along with Transglutaminase and wHTH.
Pssm-ID: 465853 Cd Length: 96 Bit Score: 127.59 E-value: 1.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 1290 FERDVLRRLVKRGYRPTPQFRIGGYRIDFVLNAPDGR-RLAIECDGDAYHG-PEQWESDMRRQAVLERVGnCVFVRIRGS 1367
Cdd:pfam18741 1 FEEEVAEALRERGYRVVPQVGVGGYRIDLVVVDPPGRyRLGIECDGATYHSsKSARDRDRLRQRVLERLG-WKFHRIWST 79
|
90
....*....|....*..
gi 556602761 1368 IFAREPEAALRPLWQRI 1384
Cdd:pfam18741 80 DWYRDPEAELERLWEAL 96
|
|
| SF1_C_Upf1 |
cd18808 |
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ... |
1086-1271 |
1.45e-32 |
|
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: 125.42 E-value: 1.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 1086 CVPQIIEFSSRHYYDGKIQPLRADR------PLSTPVRPVF---IADGVRQPLPPYGDVNVAEADALVAQVAAIVADPdY 1156
Cdd:cd18808 1 MHPEISEFPSKLFYEGKLKAGVSVAarlnppPLPGPSKPLVfvdVSGGEEREESGTSKSNEAEAELVVELVKYLLKSG-V 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 1157 RGKTLGVISLLStsGQANYLLQALREAIGEDEmearRLRVGDAYTFQGDERDVVLVSMVVSDNDGRLAAFTKREyhRRVN 1236
Cdd:cd18808 80 KPSSIGVITPYR--AQVALIRELLRKRGGLLE----DVEVGTVDNFQGREKDVIILSLVRSNESGGSIGFLSDP--RRLN 151
|
170 180 190
....*....|....*....|....*....|....*
gi 556602761 1237 VAASRARDQLWIFHSvrPQSLLADDARALLLNYAQ 1271
Cdd:cd18808 152 VALTRAKRGLIIVGN--PDTLSKDPLWKKLLEYLE 184
|
|
| DEXXQc_SF1 |
cd18043 |
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are ... |
328-386 |
2.39e-23 |
|
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: 96.88 E-value: 2.39e-23
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 556602761 328 NEAQESIARRLAQHRNVAVQGPPGTGKTHTIRNLICHLMANGKRVLVVAQKEDPLRVLR 386
Cdd:cd18043 1 DSSQEAAIISARNGKNVVIQGPPGTGKSQTIANIIANALARGKRVLFVSEKKAALDVVR 59
|
|
| AAA_12 |
pfam13087 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1065-1248 |
1.29e-22 |
|
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: 96.85 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 1065 SLYDHAVRRSPER-ILLTEHFRCVPQIIEFSSRHYYDGKIQ--------PLRADRPLSTPVRP-VFI-ADGVRQPLPPYG 1133
Cdd:pfam13087 4 SLFERLQELGPSAvVMLDTQYRMHPEIMEFPSKLFYGGKLKdgpsvaerPLPDDFHLPDPLGPlVFIdVDGSEEEESDGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 1134 D--VNVAEADALVAQVAAIVAD-PDYRGKtLGVISLlstsgqanYLLQ--ALREAIGEDEMEARRLRVG--DAytFQGDE 1206
Cdd:pfam13087 84 TsySNEAEAELVVQLVEKLIKSgPEEPSD-IGVITP--------YRAQvrLIRKLLKRKLGGKLEIEVNtvDG--FQGRE 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 556602761 1207 RDVVLVSMVVSDNDGRLaAFTKREyhRRVNVAASRARDQLWI 1248
Cdd:pfam13087 153 KDVIIFSCVRSNEKGGI-GFLSDP--RRLNVALTRAKRGLII 191
|
|
| YcjD |
COG2852 |
Very-short-patch-repair endonuclease [Replication, recombination and repair]; |
1286-1387 |
6.70e-21 |
|
Very-short-patch-repair endonuclease [Replication, recombination and repair];
Pssm-ID: 442100 Cd Length: 104 Bit Score: 88.77 E-value: 6.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 1286 CESGFERDV---LRRLVKRGYRPTPQFRIGGYRIDFVLNapdGRRLAIECDGDAYHGPEQWESDMRRQAVLERVGNCVfV 1362
Cdd:COG2852 4 NDTPAERRLwqrLRNRQLRGLKFRRQVPIGGYIVDFYCP---EARLAIEVDGGYHGSPEQRERDRRRDAYLERLGWRV-L 79
|
90 100
....*....|....*....|....*
gi 556602761 1363 RIRGSIFAREPEAALRPLWQRIEEL 1387
Cdd:COG2852 80 RFWNEDVLRNPEGVLEEILAALEER 104
|
|
| DEXXQc_SF1 |
cd18043 |
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are ... |
976-1037 |
4.93e-17 |
|
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: 78.78 E-value: 4.93e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556602761 976 VEAVPVWVMSVDRAIEQF-AGGAHFDVVIVDEASQADL-FALPVLSLAERAVVVGDDQQIGPQL 1037
Cdd:cd18043 57 VVRFPCWIMSPLSVSQYLpLNRNLFDLVIFDEASQIPIeEALPALFRGKQVVVVGDDKQLPPSI 120
|
|
| DEXXQc_Upf1-like |
cd17934 |
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ... |
956-1085 |
1.10e-11 |
|
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: 63.41 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 956 GTGRTAAAwqAHAQRAMESAVEAVPVWVMS-----VDRAieqfaggahfDVVIVDEASQADLF-ALPVLSLAERAVVVGD 1029
Cdd:cd17934 9 GTGKTTTI--AAIVLQLLKGLRGKRVLVTAqsnvaVDNV----------DVVIIDEASQITEPeLLIALIRAKKVVLVGD 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 556602761 1030 DQQIGPqlgfvgsvsgLIHSHLDDvPSAEHFDPESSLYDHAVRRSPERILLTEHFR 1085
Cdd:cd17934 77 PKQLPP----------VVQEDHAA-LLGLSFILSLLLLFRLLLPGSPKVMLDTQYR 121
|
|
| DEXXQc_Upf1-like |
cd17934 |
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ... |
346-377 |
1.43e-09 |
|
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: 57.24 E-value: 1.43e-09
10 20 30
....*....|....*....|....*....|....
gi 556602761 346 VQGPPGTGKTHTIRNLICHLMA--NGKRVLVVAQ 377
Cdd:cd17934 4 IQGPPGTGKTTTIAAIVLQLLKglRGKRVLVTAQ 37
|
|
| Endonuclease_DUF559 |
cd01038 |
Putative endonuclease; Domain of unknown function 559 (DUF559) is a putative endonuclease of ... |
1295-1384 |
5.06e-09 |
|
Putative endonuclease; Domain of unknown function 559 (DUF559) is a putative endonuclease of unknown function, belongs to a superfamily of nucleases including very short patch repair (Vsr) endonucleases, archaeal Holliday junction resolvases, MutH methyl-directed DNA mismatch-repair endonucleases, and catalytic domains of many restriction endonucleases, such as EcoRI, BamHI, and FokI.
Pssm-ID: 411708 Cd Length: 97 Bit Score: 54.90 E-value: 5.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 1295 LRRLVKRGYRPTPQFRIGGYRIDFVLNApdgRRLAIECDGDAYHGPEQWESDMRRQAVLERVGNCVfVRIRGSIFAREPE 1374
Cdd:cd01038 12 LRNRQFLGLKFRRQKPIGFYIVDFYCAE---KKLVIEIDGGQHHEKKAEEYDARRDKYLESLGYTV-LRFWNEEVLNNIE 87
|
90
....*....|
gi 556602761 1375 AALRPLWQRI 1384
Cdd:cd01038 88 GVLEKIEKFL 97
|
|
| DEXXQc_SMUBP2 |
cd18044 |
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ... |
328-412 |
5.00e-07 |
|
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: 51.46 E-value: 5.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 328 NEAQ-ESIARRLAQhRNVA-VQGPPGTGKTHTIRNLICHLMANGKRVLVVAQKE---D---------PLRVLRDGLPEEV 393
Cdd:cd18044 3 NDSQkEAVKFALSQ-KDVAlIHGPPGTGKTTTVVEIILQAVKRGEKVLACAPSNiavDnlverlvalKVKVVRIGHPARL 81
|
90
....*....|....*....
gi 556602761 394 QAlclAVLGRTTDQLVQLQ 412
Cdd:cd18044 82 LE---SVLDHSLDALVAAQ 97
|
|
| AAA_11 |
pfam13086 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
332-460 |
7.44e-07 |
|
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: 51.96 E-value: 7.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 332 ESIARRLAQHRNVAVQGPPGTGKTHTIRNLICHL-------MANGKRVLVVAQ----------------KEDPLRVLRDG 388
Cdd:pfam13086 4 EAIRSALSSSHFTLIQGPPGTGKTTTIVELIRQLlsypatsAAAGPRILVCAPsnaavdnilerllrkgQKYGPKIVRIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 389 LPEEVQAlclAVLGRTTDQLVQLQLAA-----------RELSDRAATLDKTAEAGRVERLTKRLEDAERDLATALGGLRA 457
Cdd:pfam13086 84 HPAAISE---AVLPVSLDYLVESKLNNeedaqivkdisKELEKLAKALRAFEKEIIVEKLLKSRNKDKSKLEQERRKLRS 160
|
...
gi 556602761 458 IAE 460
Cdd:pfam13086 161 ERK 163
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
50-644 |
2.47e-06 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 52.57 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 50 VEVGPALDGTSWLRVGLPDLPPPVAVPAeLRRrlnqvsatdepkvgdEDDEFETWRD---EVWR-----PWSLLSQEAEK 121
Cdd:COG3321 795 LEVGPGPVLTGLVRQCLAAAGDAVVLPS-LRR---------------GEDELAQLLTalaQLWVagvpvDWSALYPGRGR 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 122 T----------RTLHRQLFDLMHQVDMTAATTELVWGHGLLETTIGEQRVRYPLVATPVIIEYEPDRSLITVSPQGPSRL 191
Cdd:COG3321 859 RrvplptypfqREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAA 938
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 192 QTDALAGLDERYLSQLLGLAGPAGTLEVDLWDVLERQELFERALGRLGYDRRVIKPGESAVGPHLVDTGVLFARPKQRLL 271
Cdd:COG3321 939 AAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAA 1018
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 272 RGFLESLRDRLLAGDTSSIGALAAIVAHEPSKLRMPDDQPENWHRVGERLLMPLPTNEAQESIARRLAQHRNVAVQGPPG 351
Cdd:COG3321 1019 AALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALA 1098
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 352 TGKTHTIRNLICHLMANGKRVLVVAQKEDPLRVLRDGLPEEVQALCLAVLGRTTDQLVQLQLAARELSDRAATLDKTAEA 431
Cdd:COG3321 1099 LAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALA 1178
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 432 GRVERLTKRLEDAERDLATALGGLRAIAENESATyriddVDLSPADVGAWLREHAAHGGIPDPIAPTDRPPLSADEFATL 511
Cdd:COG3321 1179 LALAAALAAALAGLAALLLAALLAALLAALLALA-----LAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAA 1253
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 512 LSLAARITHADRTAALRPLPDVAALPDARTAKQARADRDAAADRVSRLELAGVDTDSVRAHGPNPVAALREGLTDAIAWL 591
Cdd:COG3321 1254 ALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAAL 1333
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 556602761 592 HRREGTWTDRLGRLLADPHWATVWTDHVTATEDLQRALADLARLLGGHRVTVA 644
Cdd:COG3321 1334 AAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAAVA 1386
|
|
| DEXSc_RecD-like |
cd17933 |
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ... |
330-376 |
5.15e-06 |
|
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: 47.93 E-value: 5.15e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 556602761 330 AQESIARRLAQHRNVAVQGPPGTGKTHTIRNLICHLMANGKRVLVVA 376
Cdd:cd17933 1 EQKAAVRLVLRNRVSVLTGGAGTGKTTTLKALLAALEAEGKRVVLAA 47
|
|
| DEXXQc_UPF1 |
cd18039 |
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ... |
328-377 |
3.67e-05 |
|
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: 46.86 E-value: 3.67e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 556602761 328 NEAQESIARRLAQHRNVAVQGPPGTGKTHTIRNLICHLM-ANGKRVLVVAQ 377
Cdd:cd18039 3 NHSQVDAVKTALQRPLSLIQGPPGTGKTVTSATIVYHLVkQGNGPVLVCAP 53
|
|
| DEXXQc_DNA2 |
cd18041 |
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ... |
999-1035 |
3.69e-05 |
|
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: 46.46 E-value: 3.69e-05
10 20 30
....*....|....*....|....*....|....*...
gi 556602761 999 FDVVIVDEASQADL-FALPVLSLAERAVVVGDDQQIGP 1035
Cdd:cd18041 130 FDYCIVDEASQITLpICLGPLRLAKKFVLVGDHYQLPP 167
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
575-968 |
3.92e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 48.48 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 575 NPVAALREGLTDAIAWLHRREGTWTDRLGRLLADPHWATVWTDHVTATEDLQRALADLARLLGGHRVTVANALAAEPKRL 654
Cdd:COG3903 540 DAELALRLAAALAPFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAA 619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 655 LAGLGELRERFAAGKGVNRLLQAGLWRIAEEVRVDGEPLRTVEDVDLAAAWVRRGQAQRRLGEHWAEWIQRLGIPARQGD 734
Cdd:COG3903 620 AAALLLLAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAA 699
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 735 PEVWAGTLLAEAAQSLGWDAREWPELSARLRVLVPQEELDLDAARLAEVAALLDDSPVVFDLDELDARDRAVADSLVPWP 814
Cdd:COG3903 700 AAALAAAAAAALAAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLAL 779
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 815 ELAAAWFDPELAEWDGLVAEARRLTAIRPEAARYVELLDRLGELAPEWAGQIDAGQVPAVPGTACLHAWQWRQAQTWFDL 894
Cdd:COG3903 780 AAAAAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALA 859
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556602761 895 VVGSVDPAVLNRRVELGRDKIRRLTGDLVVASAWLEVARSLDDRRRAALADWTTALRKIGKGTGRTAAAWQAHA 968
Cdd:COG3903 860 AAAAAAAAAALAAAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAAAA 933
|
|
| NACHT |
COG5635 |
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
587-1032 |
4.99e-05 |
|
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 47.88 E-value: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 587 AIAWLHRREGTWTDRLGRLLADPHWATVWTDHVTATEDLQRALADLARLLGGHRVTVANALAAEPKRLLAGLGELRERFA 666
Cdd:COG5635 483 ARALVEELDEELLELLAEHLEDPRWREVLLLLAGLLDDVKQIKELIDALLARDDAAALALAAALLLALLLALALLALLAL 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 667 AGKGVNRLLQAGLWRIAEEVRVDGEPLRTVEDVDLAAAWVRRGQAQRRLGEHWAEWIQRLGIPARQGDPEVWAGTLLAEA 746
Cdd:COG5635 563 LLLLRLLLALLALLLLALLLLLLLALLLALLALDLGLAALLLLLLLLLLLLLLLALALLLALLLLLLLLLLAELLLLALL 642
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 747 AQSLGWDAREWPELSARLRVLVPQEELDLDAARLAEVAALLDDSPVVFDLDELDARDRAVADSLVPWPELAAAWFDPELA 826
Cdd:COG5635 643 ALVLLSLLLASRLLLITLLLLAAASAALLLLLLLLLAELLLALLALASLLLLLLLALALALALLLLAVLLAAALDLLLLL 722
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 827 EWDGLVAEARRLTAIRPEAARYVELLDRLGELAPEWAGQIDAGQVPAVPGTACLHAWQWRQAQTWFDLVVGSVDPAVLNR 906
Cdd:COG5635 723 VLLLALLLVLALALSLLLLALALLLAGALLLESSALLAVLLASLLLALLLLSLLLLLVLLLALALLASLLLALLLLILLL 802
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 907 RVELGRDKIRRLTGDLVVASAWLEVARSLDDRRRAALADWTTALRKIGKGTGRTAAAWQAHAQRAMESAVEAVPVWVMSV 986
Cdd:COG5635 803 VLLGSLLLLRLLDDLALLLLLALAAARLLLSSLALVALELARASLGASLVLLALLLATLLLLLLLLLALALALLSLLSLS 882
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 556602761 987 DRAIEQFAGGAHFDVVIVDEASQADLFALPVLSLAERAVVVGDDQQ 1032
Cdd:COG5635 883 SLALLSLLGLLLALSLLALLLLSLSLALAALLLAAREALTLDRLLS 928
|
|
| DEXXQc_SETX |
cd18042 |
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in ... |
328-367 |
1.29e-04 |
|
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: 44.90 E-value: 1.29e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 556602761 328 NEAQ-ESIARRLAQHRNVA-VQGPPGTGKTHTIRNLICHLMA 367
Cdd:cd18042 2 NESQlEAIASALQNSPGITlIQGPPGTGKTKTIVGILSVLLA 43
|
|
| RecD |
COG0507 |
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
297-376 |
1.45e-04 |
|
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: 46.12 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 297 VAHEPSKLRMPDDQPENWHRVGERLLMPLPT--NEAQESIARRLA-QHRNVAVQGPPGTGKTHTIRNLICHLMANGKRVL 373
Cdd:COG0507 93 LARRLRRLARPALDEADVEAALAALEPRAGItlSDEQREAVALALtTRRVSVLTGGAGTGKTTTLRALLAALEALGLRVA 172
|
...
gi 556602761 374 VVA 376
Cdd:COG0507 173 LAA 175
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
524-907 |
2.04e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 46.16 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 524 TAALRPLPDVAALPDARTAKQARADRDAAADRVSRLELAGVDTDSVRAHGPNPVAALREGLTDAIAWLHRREGTWTDRLG 603
Cdd:COG3903 548 AAALAPFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLA 627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 604 RLLADPHWATVWTDHVTATEDLQRALADLARLLGGHRVTVANALAAEPKRLLAGLGELRERFAAGKGVNRLLQAGLWRIA 683
Cdd:COG3903 628 ALAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAA 707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 684 EEVRVDGEPLRTVEDVDLAAAWVRRGQAQRRLGEHWAEWIQRLGIPARQGDPEVWAGTLLAEAAQSLGWDAREWPELSAR 763
Cdd:COG3903 708 AAALAAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALA 787
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 764 LRVLVPQEELDLDAARLAEVAALLDDSPVVFDLDELDARDRAVADSLVPWPELAAAWFDPELAEWDGLVAEARRLTAIRP 843
Cdd:COG3903 788 AAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAA 867
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556602761 844 EAARYVELLDRLGELAPEWAGQIDAGQVPAVPGTACLHAWQWRQAQTWFDLVVGSVDPAVLNRR 907
Cdd:COG3903 868 AALAAAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAA 931
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
340-420 |
2.06e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 43.13 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 340 QHRNVAVQGPPGTGKTHTIRNLICHLMANGKRVLVVAqKEDPLRVLRDGLPEEVQALCLAVLGRTTDQLVQLQLAARELS 419
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYID-GEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKP 79
|
.
gi 556602761 420 D 420
Cdd:smart00382 80 D 80
|
|
| AAA_19 |
pfam13245 |
AAA domain; |
331-376 |
2.19e-04 |
|
AAA domain;
Pssm-ID: 433059 [Multi-domain] Cd Length: 136 Bit Score: 42.59 E-value: 2.19e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 556602761 331 QESIARRLAQHRNVAVQGPPGTGKTHTIRNLICHLMANG---KRVLVVA 376
Cdd:pfam13245 1 QREAVRTALPSKVVLLTGGPGTGKTTTIRHIVALLVALGgvsFPILLAA 49
|
|
| EEXXEc_NFX1 |
cd17936 |
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ... |
328-378 |
2.62e-04 |
|
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: 43.30 E-value: 2.62e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 556602761 328 NEAQESiARRLAQHRNVA-VQGPPGTGKTHT----IRNLICHL-MANGKRVLVVAQK 378
Cdd:cd17936 3 DPSQLE-ALKHALTSELAlIQGPPGTGKTFLgvklVRALLQNQdLSITGPILVVCYT 58
|
|
| DEXXQc_DNA2 |
cd18041 |
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ... |
346-412 |
2.70e-04 |
|
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: 43.76 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 346 VQGPPGTGKTHTIRNLICHLMANGKRVLVVAQ------------KEDPLRVLRDGLP----EEVQALCLAVLGRTTDQLV 409
Cdd:cd18041 22 ILGMPGTGKTTTIAALVRILVALGKSVLLTSYthsavdnillklKKFGVNFLRLGRLkkihPDVQEFTLEAILKSCKSVE 101
|
...
gi 556602761 410 QLQ 412
Cdd:cd18041 102 ELE 104
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
559-1024 |
1.01e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 43.69 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 559 LELAGVDTDSVRAHGPNPVAALREGLTDAIAWLHRREGTWTDRLGRLLADPHWATVWTDHVTA--------TEDLQRALA 630
Cdd:COG3899 772 LAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFGELALALAERLGDRRLEARALFnlgfilhwLGPLREALE 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 631 DLARLLGGHRVTVANALAAEPKRLLAGLGELRERFAAGKGVNRLLQAGLWRIAEEVRVDGEPLRTVEDVDLAAAWVRRGQ 710
Cdd:COG3899 852 LLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAAL 931
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 711 AQRRLGEHWAEWIQRLGIPARQGDPEVWAGTLLAEAAQSLGWDAREWPELSARLRVLVPQEELDLDAARLAEVAALLDDS 790
Cdd:COG3899 932 ALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAA 1011
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 791 PVVFDLDELDARDRAVADSLVPWPELAAAWFDPELAEWDGLVAEARRLTAIRPEAARYVELLDRLGELAPEWAGQIDAGQ 870
Cdd:COG3899 1012 AAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAA 1091
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 871 VPAVPGTACLHAWQWRQAQTWFDLVVGSVDPAVLNRRVELGRdkIRRLTGDLVVASAWLEVARSLDDRRRAALADWTTAL 950
Cdd:COG3899 1092 LAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAA--ALLLLAAALALALAALLLLAALLLALALLLLALAAL 1169
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556602761 951 RKIGKGTGRTAAAWQAHAQRAMESAVEAVPVWVMSVDRAIEQFAGGAHFDVVIVDEASQADLFALPVLSLAERA 1024
Cdd:COG3899 1170 ALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLALEAAALLLLLLLAALALAAALLALRLL 1243
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
330-375 |
1.07e-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: 40.98 E-value: 1.07e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 556602761 330 AQESIARRLAQHRNVAVQGPPGTGKTHTIRNLICHLMANGKRVLVV 375
Cdd:cd00009 8 EALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYL 53
|
|
| AAA_11 |
pfam13086 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
999-1032 |
1.70e-03 |
|
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: 41.95 E-value: 1.70e-03
10 20 30
....*....|....*....|....*....|....*.
gi 556602761 999 FDVVIVDEASQA-DLFAL-PVLSLAERAVVVGDDQQ 1032
Cdd:pfam13086 205 FDVVIIDEAAQAlEPSTLiPLLRGPKKVVLVGDPKQ 240
|
|
| DEXXQc_Helz-like |
cd18038 |
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ... |
327-397 |
1.94e-03 |
|
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: 41.45 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 327 TNEAQESIARRLAQ--HRNVA--VQGPPGTGKTHTIRNLICHLMAN--GKRVLVVA------------------QKEDPL 382
Cdd:cd18038 2 LNDEQKLAVRNIVTgtSRPPPyiIFGPPGTGKTVTLVEAILQVLRQppEARILVCApsnsaadllaerllnalvTKREIL 81
|
90 100
....*....|....*....|
gi 556602761 383 RV-----LRDGLPEEVQALC 397
Cdd:cd18038 82 RLnapsrDRASVPPELLPYC 101
|
|
| DExxQc_SF1-N |
cd17914 |
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ... |
346-394 |
2.28e-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: 39.39 E-value: 2.28e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 556602761 346 VQGPPGTGKTHTIRNLICHLMANGK----RVLVVAQKEDPLRVLRDGLPEEVQ 394
Cdd:cd17914 4 IQGPPGTGKTRVLVKIVAALMQNKNgepgRILLVTPTNKAAAQLDNILVDEAA 56
|
|
| TIGR00376 |
TIGR00376 |
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ... |
328-376 |
2.31e-03 |
|
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: 42.49 E-value: 2.31e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 556602761 328 NEAQ-ESIARRLAQHRNVAVQGPPGTGKTHTIRNLICHLMANGKRVLVVA 376
Cdd:TIGR00376 159 NESQkEAVLFALSSKDLFLIHGPPGTGKTRTVVELIRQLVKRGLRVLVTA 208
|
|
| DEXXQc_UPF1 |
cd18039 |
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ... |
998-1035 |
2.35e-03 |
|
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: 41.08 E-value: 2.35e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 556602761 998 HFDVVIVDEASQAD--LFALPVLSLAERAVVVGDDQQIGP 1035
Cdd:cd18039 160 KFRTVLIDEATQATepECLIPLVHGAKQVILVGDHCQLGP 199
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
319-397 |
2.48e-03 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 40.94 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 319 ERLLMPLPTNEAQESIARRLAQHRNVAVQGPPGTGKTHTIRNLICHLMANG--KRVLVVAqkedPLRVLRDGLPEEVQAL 396
Cdd:smart00487 2 EKFGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGkgGRVLVLV----PTRELAEQWAEELKKL 77
|
.
gi 556602761 397 C 397
Cdd:smart00487 78 G 78
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
629-1024 |
2.53e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 42.31 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 629 LADLARLLGGHRVTVANALAAEPKRLLAGLGELRERFAAGKGVNRLLQAGLWRIAEEVRVDGEPLRTVEDVDLAAAWVRR 708
Cdd:COG3903 529 RAALRWALAHGDAELALRLAAALAPFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAA 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 709 GQAQRRLGEHWAEWIQRLGIPARQGDPEVWAGTLLAEAAQSLGWDAREWPELSARLRVLVPQEELDLDAARLAEVAALLD 788
Cdd:COG3903 609 AAAAAAAAAAAAAALLLLAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALA 688
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 789 DSPVVFDLDELDARDRAVADSLVPWPELAAAWFDPELAEWDGLVAEARRLTAIRPEAARYVELLDRLGELAPEWAGQIDA 868
Cdd:COG3903 689 AAAAALAAAAAAAALAAAAAAALAAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAA 768
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 869 GQVPAVPGTACLHAWQWRQAQTWFDLVVGSVDPAVLNRRVELGRDKIRRLTGDLVVASAWLEVARSLDDRRRAALADWTT 948
Cdd:COG3903 769 AAALAALLLALAAAAAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAA 848
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556602761 949 ALRKIGKGTGRTAAAWQAHAQRAMESAVEAVPVWVMSVDRAIEQFAGGAHFDVVIVDEASQADLFALPVLSLAERA 1024
Cdd:COG3903 849 AAAAALAAALAAAAAAAAAAALAAAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAA 924
|
|
| DEXXQc_SETX |
cd18042 |
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in ... |
998-1032 |
4.36e-03 |
|
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: 40.27 E-value: 4.36e-03
10 20 30
....*....|....*....|....*....|....*..
gi 556602761 998 HFDVVIVDEASQA-DLFALPVLSL-AERAVVVGDDQQ 1032
Cdd:cd18042 144 GFDTVIIDEAAQAvELSTLIPLRLgCKRLILVGDPKQ 180
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
395-784 |
5.28e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 41.54 E-value: 5.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 395 ALCLAVLGRTTDQLVQLQLAARELSDRAATLDKTAEAGRVERLTKRLEDAERDLATALGGLRAIAENESATYRIDDVDLS 474
Cdd:COG3903 544 ALRLAAALAPFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAAL 623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 475 PADVGAWLREHAAHGGIPDPIAPTDRPPLSADEFATLLSLAARITHADRTAALRPLPDVAALPDARTAKQARADRDAAAD 554
Cdd:COG3903 624 LLLAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAAL 703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 555 RVSRLELAGVDTDSVRAHGPNPVAALREGLTDAIAWLHRREGTWTDRLGRLLADPHWATVWTDHVTATEDLQRALADLAR 634
Cdd:COG3903 704 AAAAAAALAAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAA 783
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 635 LLGGHRVTVANALAAEPKRLLAGLGELRERFAAGKGVNRLLQAGLWRIAEEVRVDGEPLRTVEDVDLAAAWVRRGQAQRR 714
Cdd:COG3903 784 AALAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAA 863
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 715 LGEHWAEWIQRLGIPARQGDPEVWAGTLLAEAAQSLGWDAREWPELSARLRVLVPQEELDLDAARLAEVA 784
Cdd:COG3903 864 AAAAAALAAAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAAAA 933
|
|
| SPS1 |
COG0515 |
Serine/threonine protein kinase [Signal transduction mechanisms]; |
620-878 |
6.35e-03 |
|
Serine/threonine protein kinase [Signal transduction mechanisms];
Pssm-ID: 440281 [Multi-domain] Cd Length: 482 Bit Score: 40.77 E-value: 6.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 620 TATEDLQRALADLARLLGGHRVTVANALAAEPKRLLAGlgELRERFAAGKGVNRLLQAGLWRIAEEVRVDGEPLRTVEDV 699
Cdd:COG0515 212 SPAELLRAHLREPPPPPSELRPDLPPALDAIVLRALAK--DPEERYQSAAELAAALRAVLRSLAAAAAAAAAAAAAAAAA 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 700 DLAAAWVRRGQAQRRLGEHWAEWIQRLGIPARQGDPeVWAGTLLAEAAQSLGWDAREWPELSARLRVLVPQEELDLDAAR 779
Cdd:COG0515 290 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAPAA-AAAAAAAAAALAAAAAAAAAAAAAALLAAAAALAAAAAAAAAA 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 780 LAEVAALLDDSPVVFDLDELDARDRAVADSLVPWPELAAAWFDPELAEWDGLVAEARRLTAIRPEAARYVELLDRLGELA 859
Cdd:COG0515 369 AAAAAAAAAAAAAAAALAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAAAARLLAAA 448
|
250
....*....|....*....
gi 556602761 860 PEWAGQIDAGQVPAVPGTA 878
Cdd:COG0515 449 AAAAAAAAAAPLLAALLAA 467
|
|
| DUF559 |
pfam04480 |
Protein of unknown function (DUF559); |
1291-1385 |
6.53e-03 |
|
Protein of unknown function (DUF559);
Pssm-ID: 398268 Cd Length: 95 Bit Score: 37.35 E-value: 6.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556602761 1291 ERDVLRRLVKR---GYRPTPQFRIGGYRIDFVLNAPdgrRLAIECDGDAYHGPEQWesDMRRQAVLERVGNCVfVRIRGS 1367
Cdd:pfam04480 4 ERKLWQLLRNRrlgGFKFRRQKPIGSYIVDFVCEKA---KLIVELDGSQHDEQEEY--DARRTAFLESQGFTV-LRFWND 77
|
90
....*....|....*...
gi 556602761 1368 IFAREPEAALRPLWQRIE 1385
Cdd:pfam04480 78 EVLKNPEGVLEEILLELE 95
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
328-385 |
9.67e-03 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 38.38 E-value: 9.67e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556602761 328 NEAQESIARRLAQHRNVAVQGPPGTGKTHT-IRNLICHL--MANGKRVLVVAqkedPLRVL 385
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAfLLPALEALdkLDNGPQALVLA----PTREL 57
|
|
| |
