|
Name |
Accession |
Description |
Interval |
E-value |
| DEXXQc_SETX |
cd18042 |
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in ... |
1140-1419 |
1.96e-91 |
|
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: 295.66 E-value: 1.96e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1140 YNDSQVQAILGCLGEDSRV-IIQGPPGTGKTKTILGLLSALLDGAGLSTLQKAKGTARIRvgaslqnartsAVSKTVAET 1218
Cdd:cd18042 1 LNESQLEAIASALQNSPGItLIQGPPGTGKTKTIVGILSVLLAGKYRKYYEKVKKKLRKL-----------QRNLNNKKK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1219 SIRILVAAPSNAAVDELVLRVLSEGLYDGeKGESYRPRIVRVGRpesqqlsslaaareaseskknrkkmrkyareveevl 1298
Cdd:cd18042 70 KNRILVCAPSNAAVDEIVLRLLSEGFLDG-DGRSYKPNVVRVGR------------------------------------ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1299 leslvtkhrstfptvKQARQAIIKNAQIVFCTLSGAGSVAMCEFAQDFDALIIDEAAQAVEASTLIPFKFRPHRVVLVGD 1378
Cdd:cd18042 113 ---------------QELRASILNEADIVCTTLSSSGSDLLESLPRGFDTVIIDEAAQAVELSTLIPLRLGCKRLILVGD 177
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 568023250 1379 HRQLPATVISKNLVSMGYDRSLQQRLVENGSPVLLLNQQYR 1419
Cdd:cd18042 178 PKQLPATVFSKVAQKLGYDRSLFERLQLAGYPVLMLTTQYR 218
|
|
| AAA_12 |
pfam13087 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1396-1608 |
5.19e-78 |
|
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: 256.32 E-value: 5.19e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1396 YDRSLQQRLVENG-SPVLLLNQQYRMHPEISEFPSKFFYEGKLVQDDNMREWTA-QDYHRDRAFKPLLFLDVQGA-QSQV 1472
Cdd:pfam13087 1 LDRSLFERLQELGpSAVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAERPLpDDFHLPDPLGPLVFIDVDGSeEEES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1473 SGSTSLRNMSEVEAVIQLVRRLLTKSPRIewKKRIGVIAPYKQQIYEVRGAigkLEAEFDRHLGIEVNTVDGFQGREKEI 1552
Cdd:pfam13087 81 DGGTSYSNEAEAELVVQLVEKLIKSGPEE--PSDIGVITPYRAQVRLIRKL---LKRKLGGKLEIEVNTVDGFQGREKDV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568023250 1553 IIYSCVRTsyggrrkqkkrsrgNDEEDVldAFWADERRMNVAITRAKSSLWIVGNS 1608
Cdd:pfam13087 156 IIFSCVRS--------------NEKGGI--GFLSDPRRLNVALTRAKRGLIIVGNA 195
|
|
| DNA2 |
COG1112 |
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair]; |
1173-1627 |
1.44e-66 |
|
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
Pssm-ID: 440729 [Multi-domain] Cd Length: 819 Bit Score: 242.73 E-value: 1.44e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1173 LGLLSALLDGAGLSTLQKAKGTARIRVGASLQNARTSAVSKTVAETSIRILVAAPSNAAVDELVLRVLSEGLYDGEKGES 1252
Cdd:COG1112 379 LLLALLRLLAEGLALLLLLLLAALLRLARALLLLALLLAAAAAALAALLLLALALLAALLALLLLLAAALAALLALLLLL 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1253 YRPRIVRVGRPESQQLSSLAAAREASESKKNRKKMRKYAREVEEvlLESLVTKHRSTFPTVKQAR-------QAIIKNAQ 1325
Cdd:COG1112 459 LLALAALLLLLAAAAALLALALLESLLEELIEEHPEELEKLIAE--LREAARLRRALRRELKKRRelrkllwDALLELAP 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1326 IVFCTLSGAGSVAMCEfAQDFDALIIDEAAQAVEASTLIPFkFRPHRVVLVGDHRQLPATVIS---KNLVSMGYDRSLQQ 1402
Cdd:COG1112 537 VVGMTPASVARLLPLG-EGSFDLVIIDEASQATLAEALGAL-ARAKRVVLVGDPKQLPPVVFGeeaEEVAEEGLDESLLD 614
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1403 RLVEN-GSPVLLLNQQYRMHPEISEFPSKFFYEGKLVqddNMREWTAQdyHRDRAFKPLLFLDVQGAQSQVSGSTSlrNM 1481
Cdd:COG1112 615 RLLARlPERGVMLREHYRMHPEIIAFSNRLFYDGKLV---PLPSPKAR--RLADPDSPLVFIDVDGVYERRGGSRT--NP 687
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1482 SEVEAVIQLVRRLLTKSPRiewKKRIGVIAPYKQQIYEVRGAIgkLEAEFDRHLGIEVNTVDGFQGREKEIIIYSCVRts 1561
Cdd:COG1112 688 EEAEAVVELVRELLEDGPD---GESIGVITPYRAQVALIRELL--REALGDGLEPVFVGTVDRFQGDERDVIIFSLVY-- 760
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568023250 1562 yggrrkqkkrSRGNDEEDVLDAFWADERRMNVAITRAKSSLWIVGNSTLLKQSR---AWRALIQHTKDH 1627
Cdd:COG1112 761 ----------SNDEDVPRNFGFLNGGPRRLNVAVSRARRKLIVVGSRELLDSDPstpALKRLLEYLERA 819
|
|
| TIGR00376 |
TIGR00376 |
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ... |
1133-1631 |
3.05e-65 |
|
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: 234.71 E-value: 3.05e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1133 LKYLQKHYNDSQVQAILGCLGEDSRVIIQGPPGTGKTKTILGLLSALLdgaglstlqkakgtarirvgasLQNArtsavs 1212
Cdd:TIGR00376 151 FQFFDPNLNESQKEAVLFALSSKDLFLIHGPPGTGKTRTVVELIRQLV----------------------KRGL------ 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1213 ktvaetsiRILVAAPSNAAVDELVLRVLSEGLydgekgesyrpRIVRVGRP----ESQQLSSLAAAREASES-------- 1280
Cdd:TIGR00376 203 --------RVLVTAPSNIAVDNLLERLALCDQ-----------KIVRLGHParllKSNKQHSLDYLIENHPKyqivadir 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1281 --------KKNRKK---------------MRKYAREVEEVLLESLVTKHRSTFPTVKQARQAIIKNAQ-----IVFCTLS 1332
Cdd:TIGR00376 264 ekidelieERNKKTkpspqkrrglsdikiLRKALKKREARGIESLKIASMAEWIETNKSIDRLLKLLPeseerIMNEILA 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1333 GAGSV---AMCEF--AQDFDALIIDEAAQAVEASTLIPFkFRPHRVVLVGDHRQLPATVISKNlvSMGYDRSLQQRLVEN 1407
Cdd:TIGR00376 344 ESDATnsmAGSEIlnGQYFDVAVIDEASQAMEPSCLIPL-LKARKLILAGDHKQLPPTILSHD--AEELSLTLFERLIKE 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1408 -GSPVLLLNQQYRMHPEISEFPSKFFYEGKLVQDDNMREWTAQDYHRDRAFK---------PLLFLDVQG---AQSQVSG 1474
Cdd:TIGR00376 421 yPERSRTLNVQYRMNQKIMEFPSREFYNGKLTAHESVANILLRDLPKVEATEseddletgiPLLFIDTSGcelFELKEAD 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1475 STSLRNMSEVEAVIQLVRRLLT-KSPriewKKRIGVIAPYKQQIYEVRGAIGkleaefDRHLGIEVNTVDGFQGREKEII 1553
Cdd:TIGR00376 501 STSKYNPGEAELVSEIIQALVKmGVP----ANDIGVITPYDAQVDLLRQLLE------HRHIDIEVSSVDGFQGREKEVI 570
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568023250 1554 IYSCVRTSyggrrkqKKRSRGndeedvldaFWADERRMNVAITRAKSSLWIVGNSTLLKQSRAWRALIQHTKDHKRYV 1631
Cdd:TIGR00376 571 IISFVRSN-------RKGEVG---------FLKDLRRLNVALTRARRKLIVIGDSRTLSNHKFYKRLIEWCKQHGEVR 632
|
|
| SF1_C_Upf1 |
cd18808 |
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ... |
1420-1625 |
4.35e-63 |
|
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: 212.86 E-value: 4.35e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1420 MHPEISEFPSKFFYEGKLVQDDNMREwTAQDYHRDRAFKPLLFLDVQGAQSQVSGSTSLRNMSEVEAVIQLVRRLLTKSP 1499
Cdd:cd18808 1 MHPEISEFPSKLFYEGKLKAGVSVAA-RLNPPPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYLLKSGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1500 rieWKKRIGVIAPYKQQIYEVRGaigKLEAEFDRHLGIEVNTVDGFQGREKEIIIYSCVRTSyggrrkqkkrsrgndEED 1579
Cdd:cd18808 80 ---KPSSIGVITPYRAQVALIRE---LLRKRGGLLEDVEVGTVDNFQGREKDVIILSLVRSN---------------ESG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568023250 1580 VLDAFWADERRMNVAITRAKSSLWIVGNSTLLKQSRAWRALIQHTK 1625
Cdd:cd18808 139 GSIGFLSDPRRLNVALTRAKRGLIIVGNPDTLSKDPLWKKLLEYLE 184
|
|
| AAA_11 |
pfam13086 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1143-1389 |
1.10e-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: 404072 [Multi-domain] Cd Length: 248 Bit Score: 211.43 E-value: 1.10e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1143 SQVQAILGCLGEDSRVIIQGPPGTGKTKTILGLLSALLdgaglstlqkakgtarirvgaslqnartsAVSKTVAETSIRI 1222
Cdd:pfam13086 1 SQREAIRSALSSSHFTLIQGPPGTGKTTTIVELIRQLL-----------------------------SYPATSAAAGPRI 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1223 LVAAPSNAAVDELVLRVLSeglydgeKGESYRPRIVRVGRPES------------QQLSSLAAAREASESKKNRKKMRKY 1290
Cdd:pfam13086 52 LVCAPSNAAVDNILERLLR-------KGQKYGPKIVRIGHPAAiseavlpvsldyLVESKLNNEEDAQIVKDISKELEKL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1291 AR-------------------------EVEEVLLESLVTKHRSTFPTVKQARQA-IIKNAQIVFCTLSGAGSVAMCEFAQ 1344
Cdd:pfam13086 125 AKalrafekeiivekllksrnkdksklEQERRKLRSERKELRKELRRREQSLEReILDEAQIVCSTLSGAGSRLLSSLAN 204
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 568023250 1345 dFDALIIDEAAQAVEASTLIPFKFRPHRVVLVGDHRQLPATVISK 1389
Cdd:pfam13086 205 -FDVVIIDEAAQALEPSTLIPLLRGPKKVVLVGDPKQLPPTVISK 248
|
|
| DEXXQc_SMUBP2 |
cd18044 |
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ... |
1139-1419 |
3.67e-37 |
|
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: 138.90 E-value: 3.67e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1139 HYNDSQVQAILGCLGEDSRVIIQGPPGTGKTKTILGLLsalldgagLSTLQKAKgtarirvgaslqnartsavsktvaet 1218
Cdd:cd18044 1 NLNDSQKEAVKFALSQKDVALIHGPPGTGKTTTVVEII--------LQAVKRGE-------------------------- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1219 siRILVAAPSNAAVDELVLRVLSEGLydgekgesyrpRIVRVGRPesqqlsslaaareaseskknrkkmrkyAREVEEVL 1298
Cdd:cd18044 47 --KVLACAPSNIAVDNLVERLVALKV-----------KVVRIGHP---------------------------ARLLESVL 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1299 ---LESLVtkhrstfptvkqarqaiikNAQIVFCTLSGAGSvAMCEFAQDFDALIIDEAAQAVEASTLIPFkFRPHRVVL 1375
Cdd:cd18044 87 dhsLDALV-------------------AAQVVLATNTGAGS-RQLLPNELFDVVVIDEAAQALEASCWIPL-LKARRCIL 145
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 568023250 1376 VGDHRQLPATVISKNLVSMGYDRSLQQRLVE--NGSPVLLLNQQYR 1419
Cdd:cd18044 146 AGDHKQLPPTILSDKAARGGLGVTLFERLVNlyGESVVRMLTVQYR 191
|
|
| DEXXQc_UPF1 |
cd18039 |
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ... |
1141-1419 |
9.18e-37 |
|
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: 139.30 E-value: 9.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1141 NDSQVQAILGCLGedSRV-IIQGPPGTGKTKTIlgllSALLdgagLSTLQKAKGtarirvgaslqnartsavsktvaets 1219
Cdd:cd18039 3 NHSQVDAVKTALQ--RPLsLIQGPPGTGKTVTS----ATIV----YHLVKQGNG-------------------------- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1220 iRILVAAPSNAAVDELVLRVLSEGLydgekgesyrpRIVRVgrpesqqlssLAAAREASES--------------KKNRK 1285
Cdd:cd18039 47 -PVLVCAPSNVAVDQLTEKIHQTGL-----------KVVRL----------CAKSREAVESpvsflalhnqvrnlDSAEK 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1286 KMRKYAREVEEVLLESLVTKHRSTFptVKQARQAIIKNAQIVFCTLSGAGSVAMCEFAqdFDALIIDEAAQAVEASTLIP 1365
Cdd:cd18039 105 LELLKLLKLETGELSSADEKRYRKL--KRKAERELLRNADVICCTCVGAGDPRLSKMK--FRTVLIDEATQATEPECLIP 180
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 568023250 1366 FKFRPHRVVLVGDHRQLPATVISKNLVSMGYDRSLQQRLVENGSPVLLLNQQYR 1419
Cdd:cd18039 181 LVHGAKQVILVGDHCQLGPVVMCKKAAKAGLSQSLFERLVQLGIRPIRLQVQYR 234
|
|
| DEXXQc_Helz-like |
cd18038 |
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ... |
1141-1419 |
3.35e-30 |
|
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: 120.42 E-value: 3.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1141 NDSQVQAILGCLGEDSRV---IIQGPPGTGKTKTIlgllsalldgaglstlqkakgtarirVGASLQnartsaVSKTVAE 1217
Cdd:cd18038 3 NDEQKLAVRNIVTGTSRPppyIIFGPPGTGKTVTL--------------------------VEAILQ------VLRQPPE 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1218 TsiRILVAAPSNAAVDELVLRVLSEglydgekgESYRPRIVRVgrpesqqlssLAAAREASESKKnrkkmrkyarevEEV 1297
Cdd:cd18038 51 A--RILVCAPSNSAADLLAERLLNA--------LVTKREILRL----------NAPSRDRASVPP------------ELL 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1298 LLESLVTKHRSTFPTVKQarqaiIKNAQIVFCTLSGAGSVAMCEFAQD-FDALIIDEAAQAVEASTLIPFK----FRPhR 1372
Cdd:cd18038 99 PYCNSKAEGTFRLPSLEE-----LKKYRIVVCTLMTAGRLVQAGVPNGhFTHIFIDEAGQATEPEALIPLSelasKNT-Q 172
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 568023250 1373 VVLVGDHRQLPATVISKNLVSMGYDRSLQQRLVE----------NGSPVLLLNQQYR 1419
Cdd:cd18038 173 IVLAGDPKQLGPVVRSPLARKYGLGKSLLERLMErplyykdgeyNPSYITKLLKNYR 229
|
|
| DEXXQc_DNA2 |
cd18041 |
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ... |
1141-1419 |
2.95e-23 |
|
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: 99.23 E-value: 2.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1141 NDSQVQAILGCLGEDSRVIIQGPPGTGKTKTILGLLSALLdgaglstlqkAKGtarirvgaslqnartsavsKTVaetsi 1220
Cdd:cd18041 3 NKDQRQAIKKVLNAKDYALILGMPGTGKTTTIAALVRILV----------ALG-------------------KSV----- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1221 riLVAAPSNAAVDELVLRVLSEGLydgekgesyrpRIVRVGRPesqqlsslaaareasesKKNRKKMRKYAREveevlle 1300
Cdd:cd18041 49 --LLTSYTHSAVDNILLKLKKFGV-----------NFLRLGRL-----------------KKIHPDVQEFTLE------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1301 slvtKHRSTFPTVKQArQAIIKNAQIVFCTLSGAGSVAmceFAQ-DFDALIIDEAAQAVEASTLIPFkFRPHRVVLVGDH 1379
Cdd:cd18041 92 ----AILKSCKSVEEL-ESKYESVSVVATTCLGINHPI---FRRrTFDYCIVDEASQITLPICLGPL-RLAKKFVLVGDH 162
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 568023250 1380 RQLPATVISKNLVSMGYDRSLQQRLVENG-SPVLLLNQQYR 1419
Cdd:cd18041 163 YQLPPLVKSREARELGMDESLFKRLSEAHpDAVVQLTIQYR 203
|
|
| DEXXc_HELZ2-C |
cd18040 |
C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ... |
1141-1419 |
5.55e-21 |
|
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: 94.90 E-value: 5.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1141 NDSQVQAILGCLgEDSRVIIQGPPGTGKTKTILGLLSALLDgaglstlqkakgtarirvgaslQNARTSAVSKTvAETSI 1220
Cdd:cd18040 3 NPSQNHAVRTAL-TKPFTLIQGPPGTGKTVTGVHIAYWFAK----------------------QNREIQSVSGE-GDGGP 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1221 RILVAAPSNAAVDEL-----------VLRVLSEGL----YDGEKGESYRPRIVRVGRPESQQLSSLA---AAREASE--S 1280
Cdd:cd18040 59 CVLYCGPSNKSVDVVaelllkvpglkILRVYSEQIetteYPIPNEPRHPNKKSERESKPNSELSSITlhhRIRQPSNphS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1281 KKNRKKMRKYAREVEEVLLESLVT-KHrstfpTVKQARQAIIKNAQIVFCTLSGAGSVAMcEFAQDFDALIIDEAAQAVE 1359
Cdd:cd18040 139 QQIKAFEARFERTQEKITEEDIKTyKI-----LIWEARFEELETVDVILCTCSEAASQKM-RTHANVKQCIVDECGMCTE 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568023250 1360 ASTLIPF--KFRPHRVVLVGDHRQLPATVISKNLVSMGYDRSLQQRLVENGSpvlLLNQQYR 1419
Cdd:cd18040 213 PESLIPIvsAPRAEQVVLIGDHKQLRPVVQNKEAQKLGLGRSLFERYAEKAC---MLDTQYR 271
|
|
| DEXXQc_Upf1-like |
cd17934 |
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ... |
1158-1419 |
1.96e-15 |
|
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: 74.19 E-value: 1.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1158 VIIQGPPGTGKTKTILGLLSALLDGAGLStlqkakgtarirvgaslqnartsavsktvaetsiRILVAAPSNAAVDELvl 1237
Cdd:cd17934 2 SLIQGPPGTGKTTTIAAIVLQLLKGLRGK----------------------------------RVLVTAQSNVAVDNV-- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1238 rvlseglydgekgesyrprivrvgrpesqqlsslaaareaseskknrkkmrkyareveevlleslvtkhrstfptvkqar 1317
Cdd:cd17934 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1318 qaiiknaqivfctlsgagsvamcefaqdfDALIIDEAAQAVEASTLIPFkFRPHRVVLVGDHRQLPATV----ISKNLVS 1393
Cdd:cd17934 46 -----------------------------DVVIIDEASQITEPELLIAL-IRAKKVVLVGDPKQLPPVVqedhAALLGLS 95
|
250 260
....*....|....*....|....*.
gi 568023250 1394 MGYDRSLQQRLVENGSPVLLLNQQYR 1419
Cdd:cd17934 96 FILSLLLLFRLLLPGSPKVMLDTQYR 121
|
|
| DEXXQc_Mov10L1 |
cd18078 |
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds ... |
1133-1407 |
5.72e-15 |
|
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: 76.25 E-value: 5.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1133 LKYLQKhyndSQVQAILGCLGEDSRVIIQGPPGTGKTKTIlgllsalldgaglstlqkakgtarirVGASLQnartsaVS 1212
Cdd:cd18078 2 LNELQK----EAVKRILGGECRPLPYILFGPPGTGKTVTI--------------------------IEAILQ------VV 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1213 KTVAETsiRILVAAPSNAAVDELVLRVLseglydgekgesyrprivrvgrpESQQLSSLAAAReaseskknrkkMRKYAR 1292
Cdd:cd18078 46 YNLPRS--RILVCAPSNSAADLVTSRLH-----------------------ESKVLKPGDMVR-----------LNAVNR 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1293 eveevlLESLVTKHRSTFPTVKQARQAIIKnAQIVFCTLSGAGSVAMCEFAQD-FDALIIDEAAQAVEASTLIPFKF--- 1368
Cdd:cd18078 90 ------FESTVIDARKLYCRLGEDLSKASR-HRIVISTCSTAGLLYQMGLPVGhFTHVFVDEAGQATEPESLIPLGLiss 162
|
250 260 270
....*....|....*....|....*....|....*....
gi 568023250 1369 RPHRVVLVGDHRQLPATVISKNLVSMGYDRSLQQRLVEN 1407
Cdd:cd18078 163 RDGQIILAGDPMQLGPVIKSRLASAYGLGVSFLERLMNR 201
|
|
| EEXXEc_NFX1 |
cd17936 |
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ... |
1139-1418 |
2.28e-13 |
|
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: 69.88 E-value: 2.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1139 HYNDSQVQAILGCLGedSRV-IIQGPPGTGKTKTILGLLSALLdgaglstlqkakgtarirvgaslQNARTSAVSktvae 1217
Cdd:cd17936 1 TLDPSQLEALKHALT--SELaLIQGPPGTGKTFLGVKLVRALL-----------------------QNQDLSITG----- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1218 tsiRILVAAPSNAAVDELVLRVLSEGlydgekgesyRPRIVRVGrpesqqlsslaaareaseskknrkkmrkyareveev 1297
Cdd:cd17936 51 ---PILVVCYTNHALDQFLEGLLDFG----------PTKIVRLG------------------------------------ 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1298 lleslvtkhrstfptvkqarqaiiknAQIVFCTLSGAGSVAMCEFAQDFDALIIDEAAQAVEASTL--IPFKFRpHrVVL 1375
Cdd:cd17936 82 --------------------------ARVIGMTTTGAAKYRELLQALGPKVVIVEEAAEVLEAHILaaLTPSTE-H-LIL 133
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 568023250 1376 VGDHRQLPATVISKNLVSMGY--DRSLQQRLVENGSPVLLLNQQY 1418
Cdd:cd17936 134 IGDHKQLRPKVNVYELTAKKYnlDVSLFERLVKNGLPFVTLNVQR 178
|
|
| CoV_Nsp13-helicase |
cd21718 |
helicase domain of coronavirus non-structural protein 13; This model represents the helicase ... |
1323-1608 |
2.70e-13 |
|
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: 73.33 E-value: 2.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1323 NAQIVFCTLSgagsvAMCEFAQDFdaLIIDEAAQAVEAS-TLIPFKFRPHRVVLVGDHRQLPA--TVISKNLVSMGYDRS 1399
Cdd:cd21718 102 NAQYIFSTIN-----ALPECSADI--VVVDEVSMCTNYDlSVVNARLKYKHIVYVGDPAQLPAprTLLTEGSLEPKDYNV 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1400 LQQRLVENGsPVLLLNQQYRMHPEISEFPSKFFYEGKLVqddnmrewtAQDYHRDRAFKPLLFLDVQgaqsqVSGSTSLr 1479
Cdd:cd21718 175 VTRLMVGSG-PDVFLSKCYRCPKEIVDTVSKLVYDNKLK---------AIKPKSRQCFKTFGKGDVR-----HDNGSAI- 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1480 NMSEVEaviqLVRRLLTKSPRieWKKRIgVIAPYKQQIYEVRgaigkleaefdRHLGIEVNTVDGFQGREKEIIIYsCVR 1559
Cdd:cd21718 239 NRPQLE----FVKRFLDRNPR--WRKAV-FISPYNAMNNRAS-----------RLLGLSTQTVDSSQGSEYDYVIF-CQT 299
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 568023250 1560 TsyggrrkqkkrsrgnDEEDVLDAfwadeRRMNVAITRAKSSLWIVGNS 1608
Cdd:cd21718 300 T---------------DTAHALNI-----NRFNVAITRAKHGILVIMRD 328
|
|
| EEXXQc_AQR |
cd17935 |
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds ... |
1324-1426 |
3.47e-13 |
|
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: 70.15 E-value: 3.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1324 AQIVFCTLSGAgSVAMCEFAQ---DFDALIIDEAAQAVEASTLIPFKF--------RPHRVVLVGDHRQLPATVisKNLV 1392
Cdd:cd17935 87 AKIIAMTCTHA-ALKRGELVElgfKYDNILMEEAAQILEIETFIPLLLqnpedgpnRLKRLIMIGDHHQLPPVI--KNMA 163
|
90 100 110
....*....|....*....|....*....|....*..
gi 568023250 1393 SMGY---DRSLQQRLVENGSPVLLLNQQYRMHPEISE 1426
Cdd:cd17935 164 FQKYsnmEQSLFTRLVRLGVPTVDLDAQGRARASISS 200
|
|
| alphaCoV_Nsp13-helicase |
cd21723 |
helicase domain of alphacoronavirus non-structural protein 13; This model represents the ... |
1323-1605 |
4.17e-11 |
|
helicase domain of alphacoronavirus non-structural protein 13; This model represents the helicase domain of non-structural protein 13 (Nsp13) from alphacoronavirus, including Porcine epidemic diarrhea virus and Human coronavirus (CoV) NL63. 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: 409656 [Multi-domain] Cd Length: 340 Bit Score: 66.30 E-value: 4.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1323 NAQIVFCTLSGAGSVAMcefaqdfDALIIDEAAQAVEAS-TLIPFKFRPHRVVLVGDHRQLPA--TVISKNLVSMGYDRS 1399
Cdd:cd21723 102 SAQYIFSTVNALPECNA-------DIVVVDEVSMCTNYDlSVINQRVSYKHIVYVGDPQQLPAprTMITRGVLEPKDYNV 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1400 LQQRLVENGsPVLLLNQQYRMHPEISEFPSKFFYEGKlvqddnmrewtaqdyhrdraFKPLLFLDVQGAQSQVSGSTSLR 1479
Cdd:cd21723 175 VTQRMCALG-PDVFLHKCYRCPAEIVNTVSELVYENK--------------------FKPVHPESKQCFKIFCKGNVQVD 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1480 NMSEV-EAVIQLVRRLLTKSPRieWKKRIgVIAPYKQQIYEVRgaigkleaefdRHLGIEVNTVDGFQGREKEIIIYScv 1558
Cdd:cd21723 234 NGSSInRRQLDVVKMFLAKNPK--WSKAV-FISPYNSQNYVAS-----------RVLGLQIQTVDSSQGSEYDYVIYT-- 297
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 568023250 1559 RTSyggrrkqkkrsrgndeeDVLDAfwADERRMNVAITRAKSSLWIV 1605
Cdd:cd21723 298 QTS-----------------DTAHA--CNVNRFNVAITRAKKGILCV 325
|
|
| betaCoV_Nsp13-helicase |
cd21722 |
helicase domain of betacoronavirus non-structural protein 13; This model represents the ... |
1323-1614 |
1.90e-10 |
|
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: 64.44 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1323 NAQIVFCTLSgagsvAMCEFAQDFdaLIIDEAAQAVEAS-TLIPFKFRPHRVVLVGDHRQLPA--TVISKNLVSMGYDRS 1399
Cdd:cd21722 102 SRQYVFSTIN-----ALPETVTDI--LVVDEVSMCTNYDlSVINARVRAKHIVYIGDPAQLPAprTLLTKGTLEPEYFNS 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1400 LQqRLVENGSPVLLLNQQYRMHPEISEFPSKFFYEGKLVqddnmrewtAQDYHRDRAFKPLLfldvqgaQSQVS-GSTSL 1478
Cdd:cd21722 175 VT-RLMCCLGPDIFLGTCYRCPKEIVDTVSALVYDNKLK---------AKKDNSGQCFKVYY-------KGSVThDSSSA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1479 RNMSEveavIQLVRRLLTKSPRieWKKRIgVIAPYKQQIYEVRgaigkleaefdRHLGIEVNTVDGFQGREKEIIIYScv 1558
Cdd:cd21722 238 INRPQ----IYLVKKFLKANPA--WSKAV-FISPYNSQNAVAR-----------RVLGLQTQTVDSSQGSEYDYVIYC-- 297
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 568023250 1559 rtsyggrrkQKKRSrgndeedvldAFWADERRMNVAITRAKSSLWIVGNSTLLKQS 1614
Cdd:cd21722 298 ---------QTAET----------AHSVNVNRFNVAITRAKKGILCVMSSMQLFES 334
|
|
| DEXXQc_HELZ |
cd18077 |
DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that ... |
1141-1419 |
2.98e-09 |
|
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: 59.04 E-value: 2.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1141 NDSQVQAILGCLGEDSR----VIIQGPPGTGKTKTIlgllsalldgaglstlqkakgtarirvgaslqnarTSAVSKTVA 1216
Cdd:cd18077 3 NAKQKEAVLAITTPLSIqlppVLLIGPFGTGKTFTL-----------------------------------AQAVKHILQ 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1217 ETSIRILVAAPSNAAVDELVLRVLSEGLYDGEKgesyRPRIVRVgrpesqqlsslaaareaseSKKNRKkmrkyAREVEE 1296
Cdd:cd18077 48 QPETRILICTHSNSAADLYIKEYLHPYVETGNP----RARPLRV-------------------YYRNRW-----VKTVHP 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1297 VLLESLVTKHRSTF--PTVKQarqaiIKNAQIVFCTLSGagSVAMCEFAQD---FDALIIDEAAQAVEASTLIPFKF--R 1369
Cdd:cd18077 100 VVQKYCLIDEHGTFrmPTRED-----VMRHRVVVVTLST--SQYLCQLDLEpgfFTHILLDEAAQAMECEAIMPLALatK 172
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 568023250 1370 PHRVVLVGDHRQLPATVISKNLVSMGYDRSLQQRLVENGSP----VLLLNQQYR 1419
Cdd:cd18077 173 STRIVLAGDHMQLSPEVYSEFARERNLHISLLERLYEHYPSehpcRILLCENYR 226
|
|
| DExxQc_SF1-N |
cd17914 |
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ... |
1343-1418 |
6.06e-08 |
|
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: 52.87 E-value: 6.06e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568023250 1343 AQDFDALIIDEAAQAVEASTLIPFKF--RPHRVVLVGDHRQLPATVISKNLVSMGYDRSLQQRLVENGSPVLLLNQQY 1418
Cdd:cd17914 44 AAQLDNILVDEAAQILEPETSRLIDLalDQGRVILVGDHDQLGPVWRGAVLAKICNEQSLFTRLVRLGVSLIRLQVQY 121
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
90-359 |
1.11e-07 |
|
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
Pssm-ID: 465521 [Multi-domain] Cd Length: 506 Bit Score: 56.51 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 90 VTTRKTAPRTTTQKATAAekkmTVKKTPVkrTTRSSSKMTLAEVKAQLErEQKDRVEYRIqtlrrdtkPTAVPASSVSVG 169
Cdd:pfam17823 62 AATAAPAPVTLTKGTSAA----HLNSTEV--TAEHTPHGTDLSEPATRE-GAADGAASRA--------LAAAASSSPSSA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 170 ASAVTTApgLAAPvdeaPSLAPVAPALAVPVALPVQIQAAAVVSAQHPMEVTS----AAPATVMPSLTLPATIENHTQST 245
Cdd:pfam17823 127 AQSLPAA--IAAL----PSEAFSAPRAAACRANASAAPRAAIAAASAPHAASPaprtAASSTTAASSTTAASSAPTTAAS 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 246 QAYTSTTPAPPTANLSV-----NLAPVSTAVPPSNPVKNEFIADDVEEDL----MFAMALEEVERKLATPQKQPPSSKAV 316
Cdd:pfam17823 201 SAPATLTPARGISTAATatghpAAGTALAAVGNSSPAAGTVTAAVGTVTPaalaTLAAAAGTVASAAGTINMGDPHARRL 280
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 568023250 317 VATNSLPS-VSHQAPAVPAKPTPVEQKVEVQPTQTLNASQPQPT 359
Cdd:pfam17823 281 SPAKHMPSdTMARNPAAPMGAQAQGPIIQVSTDQPVHNTAGEPT 324
|
|
| gammaCoV_Nsp13-helicase |
cd21720 |
helicase domain of gammacoronavirus non-structural protein 13; This model represents the ... |
1347-1605 |
1.93e-07 |
|
helicase domain of gammacoronavirus non-structural protein 13; This model represents the helicase domain of non-structural protein 13 (Nsp13) from gammacoronavirus, including Avian infectious bronchitis virus. 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. Coronavirus (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: 409653 [Multi-domain] Cd Length: 343 Bit Score: 54.92 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1347 DALIIDEAAQAVEAS-TLIPFKFRPHRVVLVGDHRQLPA--TVISKNLVSMGYDrsLQQRLVENGSPVLLLNQQYRMHPE 1423
Cdd:cd21720 119 DILLVDEVSMLTNYElSFINGKINYQYVVYVGDPAQLPAprTLLNGSLSPKDYN--VVTNLMVCVKPDIFLAKCYRCPKE 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1424 ISEFPSKFFYEGKLVqddnmrewtAQDYHRDRAFKPLlfldVQGAQSQVSG-STSLRNMSEVEaviqLVRRLLTKSPriE 1502
Cdd:cd21720 197 IVDTVSTLVYDGKFI---------ANNPESRQCFKVI----VNNGNSDVGHeSGSAYNTTQLE----FVKDFVCRNK--E 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1503 WKKRIgVIAPYK---QQIYevrgaigkleaefdRHLGIEVNTVDGFQGREKEIIIYsCVRTsyggrrkqkkrsrgnDEED 1579
Cdd:cd21720 258 WREAT-FISPYNamnQRAY--------------RMLGLNVQTVDSSQGSEYDYVIF-CVTA---------------DSQH 306
|
250 260
....*....|....*....|....*.
gi 568023250 1580 VLDAfwadeRRMNVAITRAKSSLWIV 1605
Cdd:cd21720 307 ALNI-----NRFNVALTRAKRGILVV 327
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
159-361 |
2.02e-07 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 56.49 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 159 TAVPASSVSVGASAVTTAPGLAAPvDEAPSLAPvAPALAVPVALPVQIQAAAVVSAQHPMEVTSA--APATVMPSLTLPA 236
Cdd:PHA03247 2748 PATPGGPARPARPPTTAGPPAPAP-PAAPAAGP-PRRLTRPAVASLSESRESLPSPWDPADPPAAvlAPAAALPPAASPA 2825
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 237 TIE-NHTQSTQAYTSTTPAPPTANLsvnlaPVSTAVPPSNPVKNEfiaddveedlmfamaleeverklaTPQKQPPsskA 315
Cdd:PHA03247 2826 GPLpPPTSAQPTAPPPPPGPPPPSL-----PLGGSVAPGGDVRRR------------------------PPSRSPA---A 2873
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 568023250 316 VVATNSLPSVSHQA-PAVPAKPTPVEQKVEVQPTQTLNASQPQPTET 361
Cdd:PHA03247 2874 KPAAPARPPVRRLArPAVSRSTESFALPPDQPERPPQPQAPPPPQPQ 2920
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
158-358 |
2.62e-07 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 56.10 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 158 PTAVPASSVSVGASAVTTAPGL-AAPVDEAPSLAPVA---PALAVPVALPVQIQAAAVVSAQHPMEVTSA--APATVMPS 231
Cdd:PHA03247 2741 PPAVPAGPATPGGPARPARPPTtAGPPAPAPPAAPAAgppRRLTRPAVASLSESRESLPSPWDPADPPAAvlAPAAALPP 2820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 232 LTLPATIE-NHTQSTQAYTSTTPAPPTANLSVNLA-----PVSTAVPPSNPVKNEFIADDVEEDLMFAMALEEVERKLAT 305
Cdd:PHA03247 2821 AASPAGPLpPPTSAQPTAPPPPPGPPPPSLPLGGSvapggDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFAL 2900
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568023250 306 PQKQP-PSSKAVVATNSLPSVSHQAPAVPAKPTPVEQKVEVQP---TQTLNASQPQP 358
Cdd:PHA03247 2901 PPDQPeRPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLaptTDPAGAGEPSG 2957
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
160-340 |
2.78e-07 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 55.65 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 160 AVPASSVSVGASAVTTAPGLAAPVDEAPSLAPVAPALAVPVALPVQIQAAAVVSAQHPMEVTSAA-------------PA 226
Cdd:PRK12323 372 AGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAArqasargpggapaPA 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 227 TVMPSLTLPATIENHTQSTQAYTSTTPAPPTANLSVNLAPVSTAVPPSNPVKNEFIADDVEE-DLMFAMALEEVERKLAT 305
Cdd:PRK12323 452 PAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQpDAAPAGWVAESIPDPAT 531
|
170 180 190
....*....|....*....|....*....|....*
gi 568023250 306 PQKQPPSSKAVVATNSLPsvshqAPAVPAKPTPVE 340
Cdd:PRK12323 532 ADPDDAFETLAPAPAAAP-----APRAAAATEPVV 561
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
160-338 |
3.75e-07 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 55.24 E-value: 3.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 160 AVPASSVSVGASAVTTAPGLAAPvdeAPSLAPVAPALAVPVALPVqiqAAAVVSAQHPMEVTSAAPATVM--PSLTLPAT 237
Cdd:PRK07003 361 AVTGGGAPGGGVPARVAGAVPAP---GARAAAAVGASAVPAVTAV---TGAAGAALAPKAAAAAAATRAEapPAAPAPPA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 238 IENHTQSTQAYTSTTPAPPTANLSVNLAPVS-TAVPPSNPVKNEFIADDVEEDLMFAMALEEVERKLATPQK-QPPSSKA 315
Cdd:PRK07003 435 TADRGDDAADGDAPVPAKANARASADSRCDErDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAvPDARAPA 514
|
170 180
....*....|....*....|...
gi 568023250 316 VVATNSlpsvshqAPAVPAKPTP 338
Cdd:PRK07003 515 AASRED-------APAAAAPPAP 530
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
77-358 |
5.24e-07 |
|
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
Pssm-ID: 465521 [Multi-domain] Cd Length: 506 Bit Score: 54.20 E-value: 5.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 77 TRTRAKPKTEVKKvTTRKTAPRTTTQKATAAEKKMTVKKTPVKRTTRSSSKMTLAEVKAQLEREQKdrveyriQTLRRDT 156
Cdd:pfam17823 131 PAAIAALPSEAFS-APRAAACRANASAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAP-------TTAASSA 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 157 KPTAVPASSVSVGASAvTTAPGLAAPVDEAPSLAPVAPAlaVPVALPVQIQAAAVVSAQHPMEVTSAAPATVM--PSLTL 234
Cdd:pfam17823 203 PATLTPARGISTAATA-TGHPAAGTALAAVGNSSPAAGT--VTAAVGTVTPAALATLAAAAGTVASAAGTINMgdPHARR 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 235 PATIENHTQSTqayTSTTPAPP--------TANLSVNLAPVSTAVPPSNPVKNEFIADDveedlmfamaleeverklaTP 306
Cdd:pfam17823 280 LSPAKHMPSDT---MARNPAAPmgaqaqgpIIQVSTDQPVHNTAGEPTPSPSNTTLEPN-------------------TP 337
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 568023250 307 QKQPPSSKAVVATNSLPSVSHQAPAVPAKPTPVEQKVE-VQPTqtlnaSQPQP 358
Cdd:pfam17823 338 KSVASTNLAVVTTTKAQAKEPSASPVPVLHTSMIPEVEaTSPT-----TQPSP 385
|
|
| SF1_C |
cd18786 |
C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family ... |
1506-1606 |
7.18e-07 |
|
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: 48.59 E-value: 7.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1506 RIGVIAPYKQQIYEVRGAIGKL-EAEFDRHLGIEVnTVDGFQGREKEIIIYSCVRTsyggrrkqkkrsrgNDEedvldaf 1584
Cdd:cd18786 12 KGVVLTPYHRDRAYLNQYLQGLsLDEFDLQLVGAI-TIDSSQGLTFDVVTLYLPTA--------------NSL------- 69
|
90 100
....*....|....*....|..
gi 568023250 1585 waDERRMNVAITRAKSSLWIVG 1606
Cdd:cd18786 70 --TPRRLYVALTRARKRLVIYD 89
|
|
| DEXXQc_SF1 |
cd18043 |
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are ... |
1141-1199 |
1.45e-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: 49.12 E-value: 1.45e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 568023250 1141 NDSQVQAILGCLGEDSrVIIQGPPGTGKTKTILGLLSALLdGAGLSTLQKAKGTARIRV 1199
Cdd:cd18043 1 DSSQEAAIISARNGKN-VVIQGPPGTGKSQTIANIIANAL-ARGKRVLFVSEKKAALDV 57
|
|
| PRK12727 |
PRK12727 |
flagellar biosynthesis protein FlhF; |
172-428 |
1.12e-05 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 237182 [Multi-domain] Cd Length: 559 Bit Score: 49.99 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 172 AVTTAPGLAAPVDEAPSLAPVAPAL-AVPVALPVQIQAAAVVSAQHpmEVTSAAPATVMP-SLTLPATIENHTQSTQAYT 249
Cdd:PRK12727 54 ALETARSDTPATAAAPAPAPQAPTKpAAPVHAPLKLSANANMSQRQ--RVASAAEDMIAAmALRQPVSVPRQAPAAAPVR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 250 STTPAPPTANLSVNLAPVSTAVPPsnpvknEFIADDVEEDLmFAMALEE--VERKLATPQKQPPSSKAVVATNSLPSVSH 327
Cdd:PRK12727 132 AASIPSPAAQALAHAAAVRTAPRQ------EHALSAVPEQL-FADFLTTapVPRAPVQAPVVAAPAPVPAIAAALAAHAA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 328 QAPAVPAKPTPVEQKVEVQPTQTLnasQPQPTETLM------DIKQAELAVVLAPDVLEEMERLRRENELLRRSNELLQA 401
Cdd:PRK12727 205 YAQDDDEQLDDDGFDLDDALPQIL---PPAALPPIVvapaapAALAAVAAAAPAPQNDEELKQLRGELALMRQMIEREMN 281
|
250 260
....*....|....*....|....*..
gi 568023250 402 AVTppahpetrvDEQPRRSPDRSTAHD 428
Cdd:PRK12727 282 RLT---------DERLRGSPVRAQALE 299
|
|
| DEXXQc_SF1 |
cd18043 |
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are ... |
1346-1383 |
1.35e-05 |
|
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: 46.04 E-value: 1.35e-05
10 20 30
....*....|....*....|....*....|....*....
gi 568023250 1346 FDALIIDEAAQA-VEAstLIPFKFRPHRVVLVGDHRQLP 1383
Cdd:cd18043 81 FDLVIFDEASQIpIEE--ALPALFRGKQVVVVGDDKQLP 117
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
166-413 |
1.38e-05 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 50.08 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 166 VSVGASAVTTAPGLAAPVDEAPSLAPVaPALAVPVALPvQIQAAAVVSAQHPMEVTSAAPATVMPSLTLPATIENHTQST 245
Cdd:PRK10263 320 VAVAAAATTATQSWAAPVEPVTQTPPV-ASVDVPPAQP-TVAWQPVPGPQTGEPVIAPAPEGYPQQSQYAQPAVQYNEPL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 246 QaytstTPAPPTanlsvnlaPVSTAVPPSNPVKNEFIADDVEEDLMFAMALEEVERKLATPQKQPPSSKAVVATNSL--P 323
Cdd:PRK10263 398 Q-----QPVQPQ--------QPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQSTyqT 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 324 SVSHQAPAVPA----KPTPVEQKVEVQPTQTLNASQP--------QPTETLMDIKQAELAVVLAPdVLEEMerlrRENEL 391
Cdd:PRK10263 465 EQTYQQPAAQEplyqQPQPVEQQPVVEPEPVVEETKParpplyyfEEVEEKRAREREQLAAWYQP-IPEPV----KEPEP 539
|
250 260
....*....|....*....|..
gi 568023250 392 LRRSNELLQAAVTPPAHPETRV 413
Cdd:PRK10263 540 IKSSLKAPSVAAVPPVEAAAAV 561
|
|
| PRK12727 |
PRK12727 |
flagellar biosynthesis protein FlhF; |
148-331 |
1.98e-05 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 237182 [Multi-domain] Cd Length: 559 Bit Score: 49.22 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 148 RIQTLRRDTKPTAVPA-SSVSVGASAVTTAPGLAAPVD---EAPSLAPVAPALAVPVALPVQIQAAAVVSAQHPMEVTSA 223
Cdd:PRK12727 82 PVHAPLKLSANANMSQrQRVASAAEDMIAAMALRQPVSvprQAPAAAPVRAASIPSPAAQALAHAAAVRTAPRQEHALSA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 224 APATVMPSLTLPATIENHTQSTQAYTSTTPAPPTAnlsvnlAPVSTAVPPSNPVKNEFIADDVEEDLMFAMALEeverkl 303
Cdd:PRK12727 162 VPEQLFADFLTTAPVPRAPVQAPVVAAPAPVPAIA------AALAAHAAYAQDDDEQLDDDGFDLDDALPQILP------ 229
|
170 180
....*....|....*....|....*...
gi 568023250 304 atPQKQPPSSKAVVATNSLPSVSHQAPA 331
Cdd:PRK12727 230 --PAALPPIVVAPAAPAALAAVAAAAPA 255
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
155-425 |
2.78e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 49.17 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 155 DTKPTAVPASSVSVGASAVTTAPGLAAPVDEAPSLAPVAPALAVPVALPVQIQAAAVVSA-QHPMEvtSAAPATVMPSLT 233
Cdd:PHA03247 2620 DTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPpQRPRR--RAARPTVGSLTS 2697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 234 L---PATIENHTQSTQAYTSTTPAPPTANLSVNLAPVSTAVPPSNPVKNEFIADDVEEDLMFAMALEEVER------KLA 304
Cdd:PHA03247 2698 LadpPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPApappaaPAA 2777
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 305 TPQKQ---PPSSKAVVATNSLPS----------VSHQAPAVPAKPTPVeqKVEVQPTQTLNASQPQPTETLMDIKQAELA 371
Cdd:PHA03247 2778 GPPRRltrPAVASLSESRESLPSpwdpadppaaVLAPAAALPPAASPA--GPLPPPTSAQPTAPPPPPGPPPPSLPLGGS 2855
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 568023250 372 VVLAPDVleemerlrrenellRRSNELLQAAVTPPAHPETRVDEQPRRSPDRST 425
Cdd:PHA03247 2856 VAPGGDV--------------RRRPPSRSPAAKPAAPARPPVRRLARPAVSRST 2895
|
|
| PRK13914 |
PRK13914 |
invasion associated endopeptidase; |
71-275 |
2.78e-05 |
|
invasion associated endopeptidase;
Pssm-ID: 237555 [Multi-domain] Cd Length: 481 Bit Score: 48.64 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 71 TQDVKK--TRTRAKPKTEVKkvttrkTAPRTTTQKATAAEKKMTVKKTPVKRTTRSSSKMTLAEVKAQLEreqkdrVEYR 148
Cdd:PRK13914 151 TQEVKKetTTQQAAPAAETK------TEVKQTTQATTPAPKVAETKETPVVDQNATTHAVKSGDTIWALS------VKYG 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 149 IqTLRRDTKPTAVPASSVSVGAS-AVTTAPGLAAPVDEAPSLAPVAPALAVPV---------ALPVQIQAAA--VVSAQH 216
Cdd:PRK13914 219 V-SVQDIMSWNNLSSSSIYVGQKlAIKQTANTATPKAEVKTEAPAAEKQAAPVvkentntntATTEKKETTTqqQTAPKA 297
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568023250 217 PMEVTSAAPAtvmPSLTLPATIENHTQSTQAYTSTTPApPTANLSVNLAPVSTAVPPSN 275
Cdd:PRK13914 298 PTEAAKPAPA---PSTNTNANKTNTNTNTNTNNTNTST-PSKNTNTNTNSNTNTNSNTN 352
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
157-359 |
4.52e-05 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 48.31 E-value: 4.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 157 KPTAVPASSVSVGASAVTTAPGLAAPVDEAPSLAPVAPALAVPVALPVQIQAAAVVSAQHPMEVTSAAPATVMPSLT--- 233
Cdd:PRK07003 386 RAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSRcde 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 234 LPATIENHTQSTQAYTSTTPAPPTANLSVNLAPVSTAVPPSNPVkNEFIADDVEEDLMFAMALEEVERKLATPQKQPPSS 313
Cdd:PRK07003 466 RDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPD-ARAPAAASREDAPAAAAPPAPEARPPTPAAAAPAA 544
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568023250 314 KAVVATNSL------------------PSVSHQAPAVPAKPTPVEQKVEVQ-PTQTLNASQPQPT 359
Cdd:PRK07003 545 RAGGAAAALdvlrnagmrvssdrgaraAAAAKPAAAPAAAPKPAAPRVAVQvPTPRARAATGDAP 609
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
143-258 |
1.54e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 46.52 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 143 DRVEYRIQTLRRDTKPTAVPASSVSVGASAVTTAPGLAAPVDEAPSLAPVAPALAVPVALPVQiQAAAVVSAQHPMEVTS 222
Cdd:PRK07764 379 ERLERRLGVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAP-PSPAGNAPAGGAPSPP 457
|
90 100 110
....*....|....*....|....*....|....*.
gi 568023250 223 AAPATVMPSLTLPATIENHTQSTQAYTSTTPAPPTA 258
Cdd:PRK07764 458 PAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAA 493
|
|
| DUF6465 |
pfam20069 |
Family of unknown function (DUF6465); This family of proteins is functionally uncharacterized. ... |
74-127 |
2.98e-04 |
|
Family of unknown function (DUF6465); This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 117 and 173 amino acids in length. These proteins have a highly charged N-terminus.
Pssm-ID: 466279 [Multi-domain] Cd Length: 130 Bit Score: 42.21 E-value: 2.98e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 568023250 74 VKKTRTRAKPKTEVKKVTTRKTAPRTTTQKATAAEKKMTVKKTPVKRTTRSSSK 127
Cdd:pfam20069 12 AKAAKKAAKKAAKKKAAKKAKAAKAAKAAAKKAAAKKAAAKKTAAKKAKKAEVK 65
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
177-430 |
2.98e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 45.48 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 177 PGLAAP-VDEAPSLAPVAPALAVPVALPVQIQAAAVVSAQHPMEVTSAAPATVMPSLTLPAtienhtqSTQAYTSTTPAP 255
Cdd:PRK14951 366 PAAAAEaAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPV-------AAPAAAAPAAAP 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 256 PTANLSVNLAPVSTAVPPSNPVKnefiaddveedlmfamaleevERKLATPQKQPPSSKAVVATnslpsvshQAPAVPAK 335
Cdd:PRK14951 439 AAAPAAVALAPAPPAQAAPETVA---------------------IPVRVAPEPAVASAAPAPAA--------APAAARLT 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 336 PTPvEQKVEVQPTQTLNASQPQPTETLMDIKQAELavvLAPDvlEEMERLRRENELLRRSN--ELLQAAVTPPAHPETRV 413
Cdd:PRK14951 490 PTE-EGDVWHATVQQLAAAEAITALARELALQSEL---VARD--GDQWLLRVERESLNQPGarERLRAALEAALGHAVRL 563
|
250 260
....*....|....*....|
gi 568023250 414 D-EQPR--RSPDRSTAHDRK 430
Cdd:PRK14951 564 EvEVGAvtDSPARRNAAARA 583
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
152-338 |
3.51e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 45.25 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 152 LRRDTKPTAVPASSVSVGASAVTTAPGLAAPVDEAPSLAPVAPALAVPVALPVQIQAAAVVSAQHPMEVTSAAPATVMPS 231
Cdd:PRK12323 389 AAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAG 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 232 LTLPATIENHTQSTQAYTSTTPAPPTANLSVNLAPVSTAVPPSNPVKNEFIADDVEEDLMFAMALEEVERKLATPQKqPP 311
Cdd:PRK12323 469 PRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAP-AA 547
|
170 180
....*....|....*....|....*..
gi 568023250 312 SSKAVVATNSLPSVSHQAPAVPAKPTP 338
Cdd:PRK12323 548 APAPRAAAATEPVVAPRPPRASASGLP 574
|
|
| FimV |
COG3170 |
Type IV pilus assembly protein FimV [Cell motility, Extracellular structures]; |
131-571 |
5.60e-04 |
|
Type IV pilus assembly protein FimV [Cell motility, Extracellular structures];
Pssm-ID: 442403 [Multi-domain] Cd Length: 508 Bit Score: 44.40 E-value: 5.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 131 AEVKAQLEREQKDRVEYRIQTLRRDTKPTAVPASSVSVGASAVTTAPGLAA--PVDEAPSLAPVAPALAVPVAlPVQIQA 208
Cdd:COG3170 54 AGLRFAVERRADGRPVLRVTSSRPVNEPFLDFLVEVNWPSGRLVREYTLLLdpPAYAAAAAAPAAAPAPAPAA-PAAAAA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 209 AAVVSAQHPMEVTSAAPATVMPSLTLPATIENHTQSTQAYT---------STTP-APPTANLSVNLAPVSTAVPPSNPVK 278
Cdd:COG3170 133 AADQPAAEAAPAASGEYYPVRPGDTLWSIAARPVRPSSGVSldqmmvalyRANPdAFIDGNINRLKAGAVLRVPAAEEVA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 279 NEFIADDVEEDLMFAMALEEVERKLATPQKQPPSSKAVVATNSLPSVSHQAPA-VPAKPTPVEQKVEVQPTQTLNASQPQ 357
Cdd:COG3170 213 ALSPAEARQEVQAQSADWAAYRARLAAAVEPAPAAAAPAAPPAAAAAAGPVPAaAEDTLSPEVTAAAAAEEADALPEAAA 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 358 PTETLMDIKQAELAvvlapdvleemeRLRRENELLRRSNELLQAAVTPPAHPETRVDEQPRRSPDRSTAHDRKIESTVSL 437
Cdd:COG3170 293 ELAERLAALEAQLA------------ELQRLLALKNPAPAAAVSAPAAAAAAATVEAAAPAAAAQPAAAAPAPALDNPLL 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 438 EDTSARSIAQ-------------YLDLARCDSDQNMKQTAYAKIPDRTidmnSPEKRSGNAEPNGEDNSENITNEEKKIH 504
Cdd:COG3170 361 LAGLLRRRKAeadevdpvaeadvYLAYGRDDQAEEILKEALASEPERL----DLRLKLLEIYAARGDRAAFEALAAELYA 436
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568023250 505 EGEHKPAEDTEAVAEHQIHTENVSQLSTAVTSQAESQSTPLPDHSTPSEKDDHSPTRQIAIEQEADG 571
Cdd:COG3170 437 LTGGGRALDPDNPLYAPGAAAAAEDAPAAEAEDDSPAEEPAASAAAAAELGDEEGARELLEEVLAEG 503
|
|
| PRK07994 |
PRK07994 |
DNA polymerase III subunits gamma and tau; Validated |
222-384 |
6.04e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236138 [Multi-domain] Cd Length: 647 Bit Score: 44.47 E-value: 6.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 222 SAAPATVMPSLTLPAtienhtQSTQAYTSTTPAPPTANLSVNLAPVSTAVPPSNPVKNEFIAddvEEDLMFAMALEEVER 301
Cdd:PRK07994 363 APLPEPEVPPQSAAP------AASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPET---TSQLLAARQQLQRAQ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 302 KLATPQKQPPSskAVVATNSLPSVSHQAPAVPAKPTPVEQKVEVQPTQTLNASQPQPTETLMDIKQAELAVVLAPD---- 377
Cdd:PRK07994 434 GATKAKKSEPA--AASRARPVNSALERLASVRPAPSALEKAPAKKEAYRWKATNPVEVKKEPVATPKALKKALEHEktpe 511
|
170
....*....|..
gi 568023250 378 -----VLEEMER 384
Cdd:PRK07994 512 laaklAAEAIER 523
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
92-276 |
6.30e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 44.48 E-value: 6.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 92 TRKTAPRTTTQKATAAEKKMTVKKTPVKRTTRSSSKMTLA--EVKAQLEREQKDRVEYRIQTLRRDTKPTAVPASSVSVG 169
Cdd:PRK12323 376 TAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAarAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPA 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 170 ASAVTTAPGLAAPVDEAPSLAPVAPALAVPVALPVQIQAAAVVSAQHPMEVTSAAPATVMPS----LTLPATIENHTQST 245
Cdd:PRK12323 456 AAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAApagwVAESIPDPATADPD 535
|
170 180 190
....*....|....*....|....*....|.
gi 568023250 246 QAYTSTTPAPPTANLSVNLAPVSTAVPPSNP 276
Cdd:PRK12323 536 DAFETLAPAPAAAPAPRAAAATEPVVAPRPP 566
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
159-361 |
6.91e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 44.46 E-value: 6.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 159 TAVPASSVSVGASAVTTAPGLAAPVDEAPSLAPVAPALAVPVALPVQiQAAAVVSAQHPMEVTSAAPATVMPSLTLPATI 238
Cdd:PRK07003 430 PAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGS-ASAPASDAPPDAAFEPAPRAAAPSAATPAAVP 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 239 ENHTqSTQAYTSTTPAPPTANLSVNLAPVSTAVPPSNPVKNEFIADDVeedLMFAMALEEVERKLATPQKQPPSSKAVVA 318
Cdd:PRK07003 509 DARA-PAAASREDAPAAAAPPAPEARPPTPAAAAPAARAGGAAAALDV---LRNAGMRVSSDRGARAAAAAKPAAAPAAA 584
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 568023250 319 TNSLPSvshqAPAVPAkPTPVEQKVEVQPTQTLNASQPQPTET 361
Cdd:PRK07003 585 PKPAAP----RVAVQV-PTPRARAATGDAPPNGAARAEQAAES 622
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
157-274 |
6.92e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 44.32 E-value: 6.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 157 KPTAVPASSVSVGASAVTTaPGLAAPVDEAPSLAPVAPALAVPVALPVQIQAAAVVSAQ----------HPMEVTSAAPA 226
Cdd:PRK14951 365 KPAAAAEAAAPAEKKTPAR-PEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPpapvaapaaaAPAAAPAAAPA 443
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 568023250 227 TVMPSLTLPATIENHTQSTQAYTSTTPAPPTANLSVNLAPVSTAVPPS 274
Cdd:PRK14951 444 AVALAPAPPAQAAPETVAIPVRVAPEPAVASAAPAPAAAPAAARLTPT 491
|
|
| RecD |
COG0507 |
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
1131-1179 |
7.07e-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: 44.20 E-value: 7.07e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 568023250 1131 RLLKYLQKHYNDSQVQAILGCLGEDSRVIIQGPPGTGKTKTILGLLSAL 1179
Cdd:COG0507 116 ALEPRAGITLSDEQREAVALALTTRRVSVLTGGAGTGKTTTLRALLAAL 164
|
|
| DEXXQc_HELZ2-N |
cd18076 |
N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ... |
1346-1382 |
2.17e-03 |
|
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: 41.41 E-value: 2.17e-03
10 20 30
....*....|....*....|....*....|....*....
gi 568023250 1346 FDALIIDEAAQAVEASTLIPFKFRPH--RVVLVGDHRQL 1382
Cdd:cd18076 147 FTHIFIDEAAQMLECEALIPLSYAGPktRVVLAGDHMQM 185
|
|
| PRK10856 |
PRK10856 |
cytoskeleton protein RodZ; |
184-284 |
2.80e-03 |
|
cytoskeleton protein RodZ;
Pssm-ID: 236776 [Multi-domain] Cd Length: 331 Bit Score: 41.94 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 184 DEAPSLAPVAPALAVPVALPVQIQAAAVVSAQHPmEVTSAAPATVMPSLTLPATIENHTQSTQAYTSTTPAPPTANlsvn 263
Cdd:PRK10856 167 STTTDPATTPAPAAPVDTTPTNSQTPAVATAPAP-AVDPQQNAVVAPSQANVDTAATPAPAAPATPDGAAPLPTDQ---- 241
|
90 100
....*....|....*....|.
gi 568023250 264 lAPVSTAVPPSNPVKNEFIAD 284
Cdd:PRK10856 242 -AGVSTPAADPNALVMNFTAD 261
|
|
| AAA_30 |
pfam13604 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1139-1235 |
3.40e-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. There is a Walker A and Walker B.
Pssm-ID: 433343 [Multi-domain] Cd Length: 191 Bit Score: 40.63 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 1139 HYNDSQVQAILGCLGEDSRV-IIQGPPGTGKTkTILGLLSALLDGAGlstlqkakgtarirvgaslqnartsavsktvae 1217
Cdd:pfam13604 1 TLNAEQAAAVRALLTSGDRVaVLVGPAGTGKT-TALKALREAWEAAG--------------------------------- 46
|
90
....*....|....*...
gi 568023250 1218 tsIRILVAAPSNAAVDEL 1235
Cdd:pfam13604 47 --YRVIGLAPTGRAAKVL 62
|
|
| PRK07994 |
PRK07994 |
DNA polymerase III subunits gamma and tau; Validated |
176-349 |
6.37e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236138 [Multi-domain] Cd Length: 647 Bit Score: 41.39 E-value: 6.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 176 APGLAAPVDEAPSLAPVAPALAVPVALPVQIQAAAVVSAQHPMEVTSAAPATVMPSLTLPAT-IENHTQSTQAYTSTTPA 254
Cdd:PRK07994 362 AAPLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQLLaARQQLQRAQGATKAKKS 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 255 PPTAnlSVNLAPVSTAVPPSNPVKNEFIADDVEEdlmfamALEEVERklATPQKQPPSSKAVVATnslPSVSHQAPAVPA 334
Cdd:PRK07994 442 EPAA--ASRARPVNSALERLASVRPAPSALEKAP------AKKEAYR--WKATNPVEVKKEPVAT---PKALKKALEHEK 508
|
170
....*....|....*
gi 568023250 335 KPTPVEQKVEVQPTQ 349
Cdd:PRK07994 509 TPELAAKLAAEAIER 523
|
|
| PRK07994 |
PRK07994 |
DNA polymerase III subunits gamma and tau; Validated |
162-318 |
8.80e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236138 [Multi-domain] Cd Length: 647 Bit Score: 40.62 E-value: 8.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 162 PASSVSVGASAVTTAPGLAAPVDEAPSLAPVAPALAVPVALPVQiQAAAVVSAQHPMEVTSAAPATVMPsltLPATIENH 241
Cdd:PRK07994 361 PAAPLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPA-SAPQQAPAVPLPETTSQLLAARQQ---LQRAQGAT 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568023250 242 TQSTQAYTSTTPAPPTANLSVNLAPVSTA--VPPSNPVKNEFI---ADDVEEDLMFAMALEEVERKLATPQKQPPSSKAV 316
Cdd:PRK07994 437 KAKKSEPAAASRARPVNSALERLASVRPApsALEKAPAKKEAYrwkATNPVEVKKEPVATPKALKKALEHEKTPELAAKL 516
|
..
gi 568023250 317 VA 318
Cdd:PRK07994 517 AA 518
|
|
| DEXSc_RecD-like |
cd17933 |
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ... |
1144-1179 |
9.14e-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: 38.69 E-value: 9.14e-03
10 20 30
....*....|....*....|....*....|....*.
gi 568023250 1144 QVQAILGCLGEDSrVIIQGPPGTGKTKTILGLLSAL 1179
Cdd:cd17933 2 QKAAVRLVLRNRV-SVLTGGAGTGKTTTLKALLAAL 36
|
|
| |
