|
Name |
Accession |
Description |
Interval |
E-value |
| DEXSc_Pif1_like |
cd18037 |
DEAD-box helicase domain of Pif1; Pif1 and other members of this family are RecD-like ... |
3-178 |
1.05e-81 |
|
DEAD-box helicase domain of Pif1; Pif1 and other members of this family are RecD-like helicases involved in maintaining genome stability through unwinding double-stranded DNAs (dsDNAs), DNA/RNA hybrids, and G quadruplex (G4) structures. The members of Pif1 helicase subfamily studied so far all appear to contribute to telomere maintenance. Pif1 is a member of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350795 [Multi-domain] Cd Length: 183 Bit Score: 253.71 E-value: 1.05e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 3 QETALKLLKAGENVFLTGSAGAGKTYTLNQYIQYLKARKVPVAITASTGIAATHMNGMTIHTWAGIGIKDQLTDDDLKRM 82
Cdd:cd18037 2 QRRVLDLVLDGKNVFFTGSAGTGKSYLLRRIIRALPSRPKRVAVTASTGIAACNIGGTTLHSFAGIGLGSEPAEDLLERV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 83 KERKYLKEHLENAQVLVIDEISMLHAKQLNLVNQVLKYFKESDEAFGGIQVIVAGDFFQLPPVGRNSEANRDKF------ 156
Cdd:cd18037 82 KRSPYLVQRWRKCDVLIIDEISMLDADLFDKLDRVAREVRGSDKPFGGIQLILCGDFLQLPPVTKNSERQAFFFrgdqqf 161
|
170 180
....*....|....*....|..
gi 490929748 157 CFMSDAWVEAKFRVCYLTEQHR 178
Cdd:cd18037 162 CFEAKSWERCIFLTVELTKVFR 183
|
|
| RecD |
COG0507 |
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
3-388 |
1.02e-55 |
|
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: 195.97 E-value: 1.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 3 QETALKLLKAGENVF-LTGSAGAGKTYTLNQYIQYLKARKVPVAITASTGIAATHMN------GMTIHTWAGIGIKDQlt 75
Cdd:COG0507 129 QREAVALALTTRRVSvLTGGAGTGKTTTLRALLAALEALGLRVALAAPTGKAAKRLSestgieARTIHRLLGLRPDSG-- 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 76 dddlkrmKERKYLKEHLENAQVLVIDEISMLHAKQLnlvNQVLKYFKEsdeafGGIQVIVAGDFFQLPPVGRNSeanrdk 155
Cdd:COG0507 207 -------RFRHNRDNPLTPADLLVVDEASMVDTRLM---AALLEALPR-----AGARLILVGDPDQLPSVGAGA------ 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 156 fcFMSDAWVEAKFRVCYLTEQHRQDDE--ILnQILNAIRAQN--------------IQSDHLQALRQ------SRSHDIG 213
Cdd:COG0507 266 --VLRDLIESGTVPVVELTEVYRQADDsrII-ELAHAIREGDapealnaryadvvfVEAEDAEEAAEaivelyADRPAGG 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 214 ETFTRLYTHNMDVDNINYQHLNEIDNEGhqfnavldgneklveTLKSSVRAPEELTLKKHAKVMFVKNNFDMGYINGSLG 293
Cdd:COG0507 343 EDIQVLAPTNAGVDALNQAIREALNPAG---------------ELERELAEDGELELYVGDRVMFTRNDYDLGVFNGDIG 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 294 EVIGFEEDDENgllPKVKLTDGTTLLVAPETWSveneagkviasfqqiPLRLAWAITIHKSQGMTLEAAEINLTN----T 369
Cdd:COG0507 408 TVLSIDEDEGR---LTVRFDGREIVTYDPSELD---------------QLELAYAITVHKSQGSTFDRVILVLPSehspL 469
|
410
....*....|....*....
gi 490929748 370 FEKGQGYVALSRLKSLTGL 388
Cdd:COG0507 470 LSRELLYTALTRARELLTL 488
|
|
| PIF1 |
pfam05970 |
PIF1-like helicase; This family includes homologs of the PIF1 helicase, which inhibits ... |
3-298 |
3.50e-42 |
|
PIF1-like helicase; This family includes homologs of the PIF1 helicase, which inhibits telomerase activity and is cell cycle regulated. This family includes a large number of largely uncharacterized plant proteins. This family includes a P-loop motif that is involved in nucleotide binding.
Pssm-ID: 428699 [Multi-domain] Cd Length: 361 Bit Score: 155.23 E-value: 3.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 3 QETALKLL------KAGENVFLTGSAGAGKTYTLNQYIQYLKARKVPVAITASTGIAATHM-NGMTIHTWAGIGIkdQLT 75
Cdd:pfam05970 5 QKKVFDAIiesvinNKGGVFFVYGYGGTGKTFLWKAIITSLRSEGKIVLAVASSGVAALLLpGGRTAHSRFGIPL--DID 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 76 DDDLKRMKERKYLKEHLENAQVLVIDEISMLHAKQLNLVNQVLKYFKES--DEAFGGIQVIVAGDFFQLPPVGRNseANR 153
Cdd:pfam05970 83 ELSTCKIKRGSKLAELLEKTSLIVWDEAPMTHRHCFEALDRTLRDILSEtdDKPFGGKTVVLGGDFRQILPVIPK--GSR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 154 -DKFCFM---SDAWveAKFRVCYLTEQHRQDDEILNQI-----------LNAIRAQNIQS-------------------- 198
Cdd:pfam05970 161 pEIVNASitnSYLW--KHVKVLELTKNMRLLADSLDQTeakelqdfsdwLLAIGDGKINDenereqlidipidillntgg 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 199 DHLQALRQSRSHDIGETFT---------RLYTHNMDVDNINYQHLNEIDNEGHQFNAVlDG--------------NEKLV 255
Cdd:pfam05970 239 DPIEAIVSEVYPDILQNSTdpnyleeraILCPTNEDVDEINNYRLSQLPGEEKEYLSS-DSisksdndseidalyPTEFL 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 490929748 256 ETLKSSVRAPEELTLKKHAKVMFVKN-NFDMGYINGSLGEVIGF 298
Cdd:pfam05970 318 NSLNANGLPNHVLKLKVGAPVMLLRNlDQSRGLCNGTRLIVTQL 361
|
|
| HTH_40 |
pfam14493 |
Helix-turn-helix domain; This presumed domain is found at the C-terminus of a large number of ... |
466-566 |
2.44e-16 |
|
Helix-turn-helix domain; This presumed domain is found at the C-terminus of a large number of helicase proteins.
Pssm-ID: 464189 Cd Length: 89 Bit Score: 74.08 E-value: 2.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 466 TLDETRALFEEGYEIEDIAHERGLTPATIINHLARLHKEQKLDISVAHPGEEVVEEIRKIYKKLkkrqnpdhfsddGSIK 545
Cdd:pfam14493 1 SAEITLELYKEGLSIEEIAEERGLKESTIEGHLAELIEAGEPVDIERLVSEEEQKEILDAIEKL------------GSES 68
|
90 100
....*....|....*....|.
gi 490929748 546 LRPIVEATSPRMGYDQVRLAL 566
Cdd:pfam14493 69 LKPIKEALPEEISYFEIRLVL 89
|
|
| TraA_Ti |
TIGR02768 |
Ti-type conjugative transfer relaxase TraA; This protein contains domains distinctive of a ... |
20-381 |
1.39e-12 |
|
Ti-type conjugative transfer relaxase TraA; This protein contains domains distinctive of a single strand exonuclease (N-terminus, MobA/MobL, pfam03389) as well as a helicase domain (central region, homologous to the corresponding region of the F-type relaxase TraI, TIGR02760). This protein likely fills the same role as TraI(F), nicking (at the oriT site) and unwinding the coiled plasmid prior to conjugative transfer.
Pssm-ID: 274289 [Multi-domain] Cd Length: 744 Bit Score: 70.61 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 20 GSAGAGKTYTLNQYIQYLKARKVPVAITASTGIAATHMNgmtihtwAGIGIKDQlTDDDLKRMKERKylKEHLENAQVLV 99
Cdd:TIGR02768 375 GRAGTGKSTMLKAAREAWEAAGYRVIGAALSGKAAEGLQ-------AESGIESR-TLASLEYAWANG--RDLLSDKDVLV 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 100 IDEISMLHAKQLNLVnqvlkyFKESDEAfgGIQVIVAGDFFQLPPVGRN---------------SEANRDKFCFMSDAWV 164
Cdd:TIGR02768 445 IDEAGMVGSRQMARV------LKEAEEA--GAKVVLVGDPEQLQPIEAGaafraiaerigyaelETIRRQREAWARQASL 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 165 E-AKFRVCYLTEQHRQDDEI-LNQILNAIRAQnIQSDHLQALRQSRSHDigeTFTRLYTHNMDVdninyQHLNEIDNEGH 242
Cdd:TIGR02768 517 ElARGDVEKALAAYRDHGHItIHDTREEAIEQ-VVADWKQDLREANPAG---SQIMLAHTRKDV-----RALNEAAREAL 587
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 243 QFNAVLdGNEKLVETLKSSVR-APEEltlkkhaKVMFVKNNFDMGYINGSLGEVigfeEDDENGLLpKVKLtDGTTLLVA 321
Cdd:TIGR02768 588 IERGEL-GESILFQTARGERKfAAGD-------RIVFLENNRDLGVKNGMLGTV----EEIEDGRL-VVQL-DSGELVII 653
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 322 PEtwsveneagkviASFQQipLRLAWAITIHKSQGMTLEAAEINLTNTFEKGQGYVALSR 381
Cdd:TIGR02768 654 PQ------------AEYDA--LDHGYATTIHKSQGVTVDRAFVLASKSMDRHLAYVAMTR 699
|
|
| SF1_C_RecD |
cd18809 |
C-terminal helicase domain of RecD family helicases; RecD is a member of the RecBCD (EC 3.1.11. ... |
345-388 |
1.93e-12 |
|
C-terminal helicase domain of RecD family helicases; 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 family helicases are DEAD-like helicases belonging to superfamily (SF)1, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF2 helicases, SF1 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350196 [Multi-domain] Cd Length: 80 Bit Score: 62.96 E-value: 1.93e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 490929748 345 LAWAITIHKSQGMTLEAAEINLTNT---FEKGQGYVALSRLKSLTGL 388
Cdd:cd18809 32 QAYAMTIHKSQGSEFDRVIVVLPTShpmLSRGLLYTALTRARKLLTL 78
|
|
| YpbB |
COG4955 |
Uncharacterized conserved protein YpbB, contains C-terminal HTH domain [Function unknown]; |
459-566 |
7.75e-07 |
|
Uncharacterized conserved protein YpbB, contains C-terminal HTH domain [Function unknown];
Pssm-ID: 443982 [Multi-domain] Cd Length: 346 Bit Score: 51.17 E-value: 7.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 459 KQNYATATLDETRALFEEGYEIEDIAHERGLTPATIINHLARLH-KEQKLDISVAHPGEEvVEEIRKIYKKLkkrqnpdh 537
Cdd:COG4955 244 KESLLTQSAQKTYQLLQQGLSLEEIAQIRRLKLSTIEDHLVEIAiKDPDFPIEPFVNKED-QQEIIQAIEKL-------- 314
|
90 100
....*....|....*....|....*....
gi 490929748 538 fsddGSIKLRPIVEAtSPRMGYDQVRLAL 566
Cdd:COG4955 315 ----GTWKLKEIKEQ-LPDLSYFQIRLVL 338
|
|
| PRK13889 |
PRK13889 |
conjugal transfer relaxase TraA; Provisional |
19-381 |
4.32e-06 |
|
conjugal transfer relaxase TraA; Provisional
Pssm-ID: 237546 [Multi-domain] Cd Length: 988 Bit Score: 49.69 E-value: 4.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 19 TGSAGAGKTYTLNQYIQYLKARKVPVAITASTGIAATHMNG------MTI----HTWAGiGiKDQLTDDDlkrmkerkyl 88
Cdd:PRK13889 368 VGYAGTGKSAMLGVAREAWEAAGYEVRGAALSGIAAENLEGgsgiasRTIasleHGWGQ-G-RDLLTSRD---------- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 89 kehlenaqVLVIDEISMLHAKQLNlvnQVLkyfkeSDEAFGGIQVIVAGDFFQLPPVgrnsEANrdkfcfmsdawveAKF 168
Cdd:PRK13889 436 --------VLVIDEAGMVGTRQLE---RVL-----SHAADAGAKVVLVGDPQQLQAI----EAG-------------AAF 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 169 RVcyLTEQH-----------RQD-------DEILNQILNAIRAQNIQSD-HLQALRQSRSHDIGETFTRLYTHNMDVDNI 229
Cdd:PRK13889 483 RS--IHERHggaeigevrrqREDwqrdatrDLATGRTGEALDAYEAHGMvHAAATREQARADLIDRWDRDRQAAPDRSRI 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 230 NYQHLNEidnEGHQFNAVLDGNEKLVETLKSSVRAPEELTLKKHA---KVMFVKNNFDMGYINGSLGEVIGfeeddengl 306
Cdd:PRK13889 561 ILTHTND---EVRALNEAARERMRAAGDLGDDVRVTVERGERSFAsgdRVMFLQNERGLGVKNGTLGTIEQ--------- 628
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490929748 307 lpkvkltdgttllVAPETWSVENEAGKVIA----SFQQIPLrlAWAITIHKSQGMTLEAAEINLTNTFEKGQGYVALSR 381
Cdd:PRK13889 629 -------------VSAQSMSVRLDDGRSVAfdlkDYDRIDH--GYAATIHKAQGMTVDRTHVLATPGMDAHSSYVALSR 692
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
13-136 |
3.43e-05 |
|
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: 44.29 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 13 GENVFLTGSAGAGKTYTLNQYIQYLKARKVPVAITASTGIAATHMNGMtihtWAGIGIKDQLTDDDLKRMKERKYLKEHl 92
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQL----LLIIVGGKKASGSGELRLRLALALARK- 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 490929748 93 ENAQVLVIDEISMLHAKQLN--LVNQVLKYFKESDEAFGGIQVIVA 136
Cdd:smart00382 77 LKPDVLILDEITSLLDAEQEalLLLLEELRLLLLLKSEKNLTVILT 122
|
|
| DNA2 |
COG1112 |
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair]; |
97-183 |
3.07e-03 |
|
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
Pssm-ID: 440729 [Multi-domain] Cd Length: 819 Bit Score: 40.50 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 97 VLVIDEISmlhakQLNLVnqvlkyfkesdEAFGGI----QVIVAGDFFQLPPVGRNSEANRDKFCFMSD-----AWVEAK 167
Cdd:COG1112 558 LVIIDEAS-----QATLA-----------EALGALarakRVVLVGDPKQLPPVVFGEEAEEVAEEGLDEslldrLLARLP 621
|
90
....*....|....*.
gi 490929748 168 FRVCYLTEQHRQDDEI 183
Cdd:COG1112 622 ERGVMLREHYRMHPEI 637
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DEXSc_Pif1_like |
cd18037 |
DEAD-box helicase domain of Pif1; Pif1 and other members of this family are RecD-like ... |
3-178 |
1.05e-81 |
|
DEAD-box helicase domain of Pif1; Pif1 and other members of this family are RecD-like helicases involved in maintaining genome stability through unwinding double-stranded DNAs (dsDNAs), DNA/RNA hybrids, and G quadruplex (G4) structures. The members of Pif1 helicase subfamily studied so far all appear to contribute to telomere maintenance. Pif1 is a member of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350795 [Multi-domain] Cd Length: 183 Bit Score: 253.71 E-value: 1.05e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 3 QETALKLLKAGENVFLTGSAGAGKTYTLNQYIQYLKARKVPVAITASTGIAATHMNGMTIHTWAGIGIKDQLTDDDLKRM 82
Cdd:cd18037 2 QRRVLDLVLDGKNVFFTGSAGTGKSYLLRRIIRALPSRPKRVAVTASTGIAACNIGGTTLHSFAGIGLGSEPAEDLLERV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 83 KERKYLKEHLENAQVLVIDEISMLHAKQLNLVNQVLKYFKESDEAFGGIQVIVAGDFFQLPPVGRNSEANRDKF------ 156
Cdd:cd18037 82 KRSPYLVQRWRKCDVLIIDEISMLDADLFDKLDRVAREVRGSDKPFGGIQLILCGDFLQLPPVTKNSERQAFFFrgdqqf 161
|
170 180
....*....|....*....|..
gi 490929748 157 CFMSDAWVEAKFRVCYLTEQHR 178
Cdd:cd18037 162 CFEAKSWERCIFLTVELTKVFR 183
|
|
| RecD |
COG0507 |
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
3-388 |
1.02e-55 |
|
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: 195.97 E-value: 1.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 3 QETALKLLKAGENVF-LTGSAGAGKTYTLNQYIQYLKARKVPVAITASTGIAATHMN------GMTIHTWAGIGIKDQlt 75
Cdd:COG0507 129 QREAVALALTTRRVSvLTGGAGTGKTTTLRALLAALEALGLRVALAAPTGKAAKRLSestgieARTIHRLLGLRPDSG-- 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 76 dddlkrmKERKYLKEHLENAQVLVIDEISMLHAKQLnlvNQVLKYFKEsdeafGGIQVIVAGDFFQLPPVGRNSeanrdk 155
Cdd:COG0507 207 -------RFRHNRDNPLTPADLLVVDEASMVDTRLM---AALLEALPR-----AGARLILVGDPDQLPSVGAGA------ 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 156 fcFMSDAWVEAKFRVCYLTEQHRQDDE--ILnQILNAIRAQN--------------IQSDHLQALRQ------SRSHDIG 213
Cdd:COG0507 266 --VLRDLIESGTVPVVELTEVYRQADDsrII-ELAHAIREGDapealnaryadvvfVEAEDAEEAAEaivelyADRPAGG 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 214 ETFTRLYTHNMDVDNINYQHLNEIDNEGhqfnavldgneklveTLKSSVRAPEELTLKKHAKVMFVKNNFDMGYINGSLG 293
Cdd:COG0507 343 EDIQVLAPTNAGVDALNQAIREALNPAG---------------ELERELAEDGELELYVGDRVMFTRNDYDLGVFNGDIG 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 294 EVIGFEEDDENgllPKVKLTDGTTLLVAPETWSveneagkviasfqqiPLRLAWAITIHKSQGMTLEAAEINLTN----T 369
Cdd:COG0507 408 TVLSIDEDEGR---LTVRFDGREIVTYDPSELD---------------QLELAYAITVHKSQGSTFDRVILVLPSehspL 469
|
410
....*....|....*....
gi 490929748 370 FEKGQGYVALSRLKSLTGL 388
Cdd:COG0507 470 LSRELLYTALTRARELLTL 488
|
|
| PIF1 |
pfam05970 |
PIF1-like helicase; This family includes homologs of the PIF1 helicase, which inhibits ... |
3-298 |
3.50e-42 |
|
PIF1-like helicase; This family includes homologs of the PIF1 helicase, which inhibits telomerase activity and is cell cycle regulated. This family includes a large number of largely uncharacterized plant proteins. This family includes a P-loop motif that is involved in nucleotide binding.
Pssm-ID: 428699 [Multi-domain] Cd Length: 361 Bit Score: 155.23 E-value: 3.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 3 QETALKLL------KAGENVFLTGSAGAGKTYTLNQYIQYLKARKVPVAITASTGIAATHM-NGMTIHTWAGIGIkdQLT 75
Cdd:pfam05970 5 QKKVFDAIiesvinNKGGVFFVYGYGGTGKTFLWKAIITSLRSEGKIVLAVASSGVAALLLpGGRTAHSRFGIPL--DID 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 76 DDDLKRMKERKYLKEHLENAQVLVIDEISMLHAKQLNLVNQVLKYFKES--DEAFGGIQVIVAGDFFQLPPVGRNseANR 153
Cdd:pfam05970 83 ELSTCKIKRGSKLAELLEKTSLIVWDEAPMTHRHCFEALDRTLRDILSEtdDKPFGGKTVVLGGDFRQILPVIPK--GSR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 154 -DKFCFM---SDAWveAKFRVCYLTEQHRQDDEILNQI-----------LNAIRAQNIQS-------------------- 198
Cdd:pfam05970 161 pEIVNASitnSYLW--KHVKVLELTKNMRLLADSLDQTeakelqdfsdwLLAIGDGKINDenereqlidipidillntgg 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 199 DHLQALRQSRSHDIGETFT---------RLYTHNMDVDNINYQHLNEIDNEGHQFNAVlDG--------------NEKLV 255
Cdd:pfam05970 239 DPIEAIVSEVYPDILQNSTdpnyleeraILCPTNEDVDEINNYRLSQLPGEEKEYLSS-DSisksdndseidalyPTEFL 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 490929748 256 ETLKSSVRAPEELTLKKHAKVMFVKN-NFDMGYINGSLGEVIGF 298
Cdd:pfam05970 318 NSLNANGLPNHVLKLKVGAPVMLLRNlDQSRGLCNGTRLIVTQL 361
|
|
| DEXSc_RecD-like |
cd17933 |
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ... |
2-177 |
9.09e-22 |
|
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: 91.85 E-value: 9.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 2 KQETALKLLKAGENVFLTGSAGAGKTYTLNQYIQYLKARKVPVAITASTGIAATHMN------GMTIHTWAGIGikdqlt 75
Cdd:cd17933 1 EQKAAVRLVLRNRVSVLTGGAGTGKTTTLKALLAALEAEGKRVVLAAPTGKAAKRLSestgieASTIHRLLGIN------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 76 dddlKRMKERKYLKEHLENAQVLVIDEISMLHAKQLnlvNQVLKyfkesdEAFGGIQVIVAGDFFQLPPVGRNSeanrdk 155
Cdd:cd17933 75 ----PGGGGFYYNEENPLDADLLIVDEASMVDTRLM---AALLS------AIPAGARLILVGDPDQLPSVGAGN------ 135
|
170 180
....*....|....*....|..
gi 490929748 156 fcFMSDAWVEAKFRVCYLTEQH 177
Cdd:cd17933 136 --VLRDLIASKGVPTVELTEVF 155
|
|
| HTH_40 |
pfam14493 |
Helix-turn-helix domain; This presumed domain is found at the C-terminus of a large number of ... |
466-566 |
2.44e-16 |
|
Helix-turn-helix domain; This presumed domain is found at the C-terminus of a large number of helicase proteins.
Pssm-ID: 464189 Cd Length: 89 Bit Score: 74.08 E-value: 2.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 466 TLDETRALFEEGYEIEDIAHERGLTPATIINHLARLHKEQKLDISVAHPGEEVVEEIRKIYKKLkkrqnpdhfsddGSIK 545
Cdd:pfam14493 1 SAEITLELYKEGLSIEEIAEERGLKESTIEGHLAELIEAGEPVDIERLVSEEEQKEILDAIEKL------------GSES 68
|
90 100
....*....|....*....|.
gi 490929748 546 LRPIVEATSPRMGYDQVRLAL 566
Cdd:pfam14493 69 LKPIKEALPEEISYFEIRLVL 89
|
|
| AAA_30 |
pfam13604 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
3-224 |
3.28e-15 |
|
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: 74.14 E-value: 3.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 3 QETALKLLKAGEN--VFLTGSAGAGKTYTLNQYIQYLKARKVPVAITASTGIAA------THMNGMTIHTWagigikdql 74
Cdd:pfam13604 6 QAAAVRALLTSGDrvAVLVGPAGTGKTTALKALREAWEAAGYRVIGLAPTGRAAkvlgeeLGIPADTIAKL--------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 75 tdddLKRMKERkylkEHLENAQVLVIDEISMLHAKQLNlvnQVLKYFKESdeafgGIQVIVAGDFFQLPPVGRNSeanrd 154
Cdd:pfam13604 77 ----LHRLGGR----AGLDPGTLLIVDEAGMVGTRQMA---RLLKLAEDA-----GARVILVGDPRQLPSVEAGG----- 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 155 kfcfMSDAWVEAKFRVCYLTEQHRQDDEilnqilnAIRaqniqsdhlQALRQSRSHDIGETFTRLYTHNM 224
Cdd:pfam13604 136 ----AFRDLLAAGIGTAELTEIVRQRDP-------WQR---------AASLALRDGDPAEALDALADRGR 185
|
|
| AAA_19 |
pfam13245 |
AAA domain; |
3-147 |
2.16e-13 |
|
AAA domain;
Pssm-ID: 433059 [Multi-domain] Cd Length: 136 Bit Score: 67.24 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 3 QETALKLLKAGENVFLTGSAGAGKTYTLNQYIQYLKARKV---PVAITASTGIAATHMN------GMTIHtwagigikdQ 73
Cdd:pfam13245 1 QREAVRTALPSKVVLLTGGPGTGKTTTIRHIVALLVALGGvsfPILLAAPTGRAAKRLSertglpASTIH---------R 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490929748 74 LTDDDLKRMKERKYLKEHLENAQVLVIDEISMLhakQLNLVNQVLKYFKESDeafggiQVIVAGDFFQLPPVGR 147
Cdd:pfam13245 72 LLGFDDLEAGGFLRDEEEPLDGDLLIVDEFSMV---DLPLAYRLLKALPDGA------QLLLVGDPDQLPSVGP 136
|
|
| TraA_Ti |
TIGR02768 |
Ti-type conjugative transfer relaxase TraA; This protein contains domains distinctive of a ... |
20-381 |
1.39e-12 |
|
Ti-type conjugative transfer relaxase TraA; This protein contains domains distinctive of a single strand exonuclease (N-terminus, MobA/MobL, pfam03389) as well as a helicase domain (central region, homologous to the corresponding region of the F-type relaxase TraI, TIGR02760). This protein likely fills the same role as TraI(F), nicking (at the oriT site) and unwinding the coiled plasmid prior to conjugative transfer.
Pssm-ID: 274289 [Multi-domain] Cd Length: 744 Bit Score: 70.61 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 20 GSAGAGKTYTLNQYIQYLKARKVPVAITASTGIAATHMNgmtihtwAGIGIKDQlTDDDLKRMKERKylKEHLENAQVLV 99
Cdd:TIGR02768 375 GRAGTGKSTMLKAAREAWEAAGYRVIGAALSGKAAEGLQ-------AESGIESR-TLASLEYAWANG--RDLLSDKDVLV 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 100 IDEISMLHAKQLNLVnqvlkyFKESDEAfgGIQVIVAGDFFQLPPVGRN---------------SEANRDKFCFMSDAWV 164
Cdd:TIGR02768 445 IDEAGMVGSRQMARV------LKEAEEA--GAKVVLVGDPEQLQPIEAGaafraiaerigyaelETIRRQREAWARQASL 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 165 E-AKFRVCYLTEQHRQDDEI-LNQILNAIRAQnIQSDHLQALRQSRSHDigeTFTRLYTHNMDVdninyQHLNEIDNEGH 242
Cdd:TIGR02768 517 ElARGDVEKALAAYRDHGHItIHDTREEAIEQ-VVADWKQDLREANPAG---SQIMLAHTRKDV-----RALNEAAREAL 587
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 243 QFNAVLdGNEKLVETLKSSVR-APEEltlkkhaKVMFVKNNFDMGYINGSLGEVigfeEDDENGLLpKVKLtDGTTLLVA 321
Cdd:TIGR02768 588 IERGEL-GESILFQTARGERKfAAGD-------RIVFLENNRDLGVKNGMLGTV----EEIEDGRL-VVQL-DSGELVII 653
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 322 PEtwsveneagkviASFQQipLRLAWAITIHKSQGMTLEAAEINLTNTFEKGQGYVALSR 381
Cdd:TIGR02768 654 PQ------------AEYDA--LDHGYATTIHKSQGVTVDRAFVLASKSMDRHLAYVAMTR 699
|
|
| SF1_C_RecD |
cd18809 |
C-terminal helicase domain of RecD family helicases; RecD is a member of the RecBCD (EC 3.1.11. ... |
345-388 |
1.93e-12 |
|
C-terminal helicase domain of RecD family helicases; 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 family helicases are DEAD-like helicases belonging to superfamily (SF)1, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF2 helicases, SF1 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350196 [Multi-domain] Cd Length: 80 Bit Score: 62.96 E-value: 1.93e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 490929748 345 LAWAITIHKSQGMTLEAAEINLTNT---FEKGQGYVALSRLKSLTGL 388
Cdd:cd18809 32 QAYAMTIHKSQGSEFDRVIVVLPTShpmLSRGLLYTALTRARKLLTL 78
|
|
| YpbB |
COG4955 |
Uncharacterized conserved protein YpbB, contains C-terminal HTH domain [Function unknown]; |
459-566 |
7.75e-07 |
|
Uncharacterized conserved protein YpbB, contains C-terminal HTH domain [Function unknown];
Pssm-ID: 443982 [Multi-domain] Cd Length: 346 Bit Score: 51.17 E-value: 7.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 459 KQNYATATLDETRALFEEGYEIEDIAHERGLTPATIINHLARLH-KEQKLDISVAHPGEEvVEEIRKIYKKLkkrqnpdh 537
Cdd:COG4955 244 KESLLTQSAQKTYQLLQQGLSLEEIAQIRRLKLSTIEDHLVEIAiKDPDFPIEPFVNKED-QQEIIQAIEKL-------- 314
|
90 100
....*....|....*....|....*....
gi 490929748 538 fsddGSIKLRPIVEAtSPRMGYDQVRLAL 566
Cdd:COG4955 315 ----GTWKLKEIKEQ-LPDLSYFQIRLVL 338
|
|
| PRK13889 |
PRK13889 |
conjugal transfer relaxase TraA; Provisional |
19-381 |
4.32e-06 |
|
conjugal transfer relaxase TraA; Provisional
Pssm-ID: 237546 [Multi-domain] Cd Length: 988 Bit Score: 49.69 E-value: 4.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 19 TGSAGAGKTYTLNQYIQYLKARKVPVAITASTGIAATHMNG------MTI----HTWAGiGiKDQLTDDDlkrmkerkyl 88
Cdd:PRK13889 368 VGYAGTGKSAMLGVAREAWEAAGYEVRGAALSGIAAENLEGgsgiasRTIasleHGWGQ-G-RDLLTSRD---------- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 89 kehlenaqVLVIDEISMLHAKQLNlvnQVLkyfkeSDEAFGGIQVIVAGDFFQLPPVgrnsEANrdkfcfmsdawveAKF 168
Cdd:PRK13889 436 --------VLVIDEAGMVGTRQLE---RVL-----SHAADAGAKVVLVGDPQQLQAI----EAG-------------AAF 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 169 RVcyLTEQH-----------RQD-------DEILNQILNAIRAQNIQSD-HLQALRQSRSHDIGETFTRLYTHNMDVDNI 229
Cdd:PRK13889 483 RS--IHERHggaeigevrrqREDwqrdatrDLATGRTGEALDAYEAHGMvHAAATREQARADLIDRWDRDRQAAPDRSRI 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 230 NYQHLNEidnEGHQFNAVLDGNEKLVETLKSSVRAPEELTLKKHA---KVMFVKNNFDMGYINGSLGEVIGfeeddengl 306
Cdd:PRK13889 561 ILTHTND---EVRALNEAARERMRAAGDLGDDVRVTVERGERSFAsgdRVMFLQNERGLGVKNGTLGTIEQ--------- 628
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490929748 307 lpkvkltdgttllVAPETWSVENEAGKVIA----SFQQIPLrlAWAITIHKSQGMTLEAAEINLTNTFEKGQGYVALSR 381
Cdd:PRK13889 629 -------------VSAQSMSVRLDDGRSVAfdlkDYDRIDH--GYAATIHKAQGMTVDRTHVLATPGMDAHSSYVALSR 692
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
7-136 |
1.02e-05 |
|
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: 45.60 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 7 LKLLKAGENVFLTGSAGAGKTYTLNQYIQYLKARKVPVAITASTGIAATHMNGMTIHTWAgigikdqltdddLKRMKERK 86
Cdd:cd00009 13 ALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHFL------------VRLLFELA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 490929748 87 YLKEHlenaQVLVIDEISMLHAKQLNLVNQVLKYFKESDEAFGGIQVIVA 136
Cdd:cd00009 81 EKAKP----GVLFIDEIDSLSRGAQNALLRVLETLNDLRIDRENVRVIGA 126
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
16-137 |
1.89e-05 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 44.25 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 16 VFLTGSAGAGKTYTLNQYIQYLKARKVPVA-ITASTGiaathMNGMTIHTWAGIGIKDQLTD-DDLKRMKERkyLKEHLE 93
Cdd:pfam13401 8 LVLTGESGTGKTTLLRRLLEQLPEVRDSVVfVDLPSG-----TSPKDLLRALLRALGLPLSGrLSKEELLAA--LQQLLL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 490929748 94 N---AQVLVIDEISMLHAKQLNLvnqvLKYFkeSDEAFGGIQVIVAG 137
Cdd:pfam13401 81 AlavAVVLIIDEAQHLSLEALEE----LRDL--LNLSSKLLQLILVG 121
|
|
| SF1_C |
cd18786 |
C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family ... |
337-381 |
3.05e-05 |
|
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: 42.81 E-value: 3.05e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 490929748 337 SFQQIPLRLAWAITIHKSQGMTLEAAEINL--TNTFEKGQGYVALSR 381
Cdd:cd18786 34 SLDEFDLQLVGAITIDSSQGLTFDVVTLYLptANSLTPRRLYVALTR 80
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
13-136 |
3.43e-05 |
|
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: 44.29 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 13 GENVFLTGSAGAGKTYTLNQYIQYLKARKVPVAITASTGIAATHMNGMtihtWAGIGIKDQLTDDDLKRMKERKYLKEHl 92
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQL----LLIIVGGKKASGSGELRLRLALALARK- 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 490929748 93 ENAQVLVIDEISMLHAKQLN--LVNQVLKYFKESDEAFGGIQVIVA 136
Cdd:smart00382 77 LKPDVLILDEITSLLDAEQEalLLLLEELRLLLLLKSEKNLTVILT 122
|
|
| DNA2 |
COG1112 |
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair]; |
97-183 |
3.07e-03 |
|
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
Pssm-ID: 440729 [Multi-domain] Cd Length: 819 Bit Score: 40.50 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 97 VLVIDEISmlhakQLNLVnqvlkyfkesdEAFGGI----QVIVAGDFFQLPPVGRNSEANRDKFCFMSD-----AWVEAK 167
Cdd:COG1112 558 LVIIDEAS-----QATLA-----------EALGALarakRVVLVGDPKQLPPVVFGEEAEEVAEEGLDEslldrLLARLP 621
|
90
....*....|....*.
gi 490929748 168 FRVCYLTEQHRQDDEI 183
Cdd:COG1112 622 ERGVMLREHYRMHPEI 637
|
|
| recD |
PRK10875 |
exodeoxyribonuclease V subunit alpha; |
276-370 |
4.44e-03 |
|
exodeoxyribonuclease V subunit alpha;
Pssm-ID: 236783 [Multi-domain] Cd Length: 615 Bit Score: 39.92 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929748 276 VMFVKNNFDMGYINGSlgevIGFEEDDENGLLpKV--KLTDGTtllvapetwsveneagkvIASFQqiPLRL-----AWA 348
Cdd:PRK10875 487 VMIARNDSALGLFNGD----IGIALDRGQGEL-RVwfQLPDGN------------------IKSVQ--PSRLpehetAWA 541
|
90 100
....*....|....*....|..
gi 490929748 349 ITIHKSQGMTLEAAEINLTNTF 370
Cdd:PRK10875 542 MTVHKSQGSEFDHTALVLPNQF 563
|
|
| |
