|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10308 |
PRK10308 |
3-methyl-adenine DNA glycosylase II; Provisional |
209-496 |
3.07e-118 |
|
3-methyl-adenine DNA glycosylase II; Provisional
Pssm-ID: 236671 [Multi-domain] Cd Length: 283 Bit Score: 348.67 E-value: 3.07e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362590 209 FHLGYRPPYDWARMLNFLQARAVQGVERVEGRRYLRSIAVSqggtEHRGWFSVQPEEARNRVRVEIAPTLSLVTTEVLRR 288
Cdd:PRK10308 2 YTLNWQPPYDWSWMLGFLAARAVSGVETVAEGYYARSLAVG----EHRGVVTVIPDIARHTLHINLSAGLEPVAAECLAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362590 289 VRLLFDLDAAPDRINEALGSLAADAPGLRLPGCVNSFEQATRAVLGQLVSVKMAATFAGRMAERWGEALATPHEGIthVF 368
Cdd:PRK10308 78 MSRLFDLQCNPQIVNGALGKLGAARPGLRLPGSVDAFEQGVRAILGQLVSVAMAAKLTAKVAQLYGERLDDFPEYV--CF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362590 369 PTAERVAQLQPEELRPLGVQVKRAAALIEIARALGEGRLQLDNVLDIEQGIKALTALPGIGSWTASYIAMRAWSWPDVFL 448
Cdd:PRK10308 156 PTPERLAAADPQALKALGMPLKRAEALIHLANAALEGTLPLTIPGDVEQAMKTLQTFPGIGRWTANYFALRGWQAKDVFL 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 644362590 449 AGDYLIKQRFPGMTPRQIERYAERWRPWRSYATLHLWHNGGWAPEGES 496
Cdd:PRK10308 236 PDDYLIKQRFPGMTPAQIRRYAERWKPWRSYALLHIWYTEGWQPDEDS 283
|
|
| AdaA |
COG2169 |
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ... |
11-339 |
3.83e-86 |
|
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), contains Zn-binding and two AraC-type DNA-binding domains [Replication, recombination and repair];
Pssm-ID: 441772 [Multi-domain] Cd Length: 358 Bit Score: 269.23 E-value: 3.83e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362590 11 MNTQQQALYDALRARDRKFDGRFFVGVSSTGIYCRPVCSARTPKRENCTFYPSAAAAELAGFRPCLKCRPELAPGLALID 90
Cdd:COG2169 4 DLLDDDERWQAVLARDARFDGRFFYGVKTTGIYCRPSCPARKPKRENVRFFATAAAAEAAGFRPCKRCRPDLAPGSPPRA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362590 91 lgnRYAQVAVQLIEQGYLSEHSCEALAARLGISDRHLRRIFAEQFGASPIDYAQSHRLLQAKRLLaDTDLPLSEVAFAAG 170
Cdd:COG2169 84 ---DLVARACRLIEAGAEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQLL-QTGLSVTDAAYAAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362590 171 FGSLRRFNELFKARYRLIPSALRSGGARGERaaasglvfhlgYRPPYDWARMLNFLQARAVQGVERVEGRRYLRSIAVSQ 250
Cdd:COG2169 160 FGSLSRFYEAFKKLLGMTPSAYRRGGAGAAI-----------RFAPTPCSLGLLLVAASARGVCAILLGDDPEALLRDLQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362590 251 GGTehrGWFSVQPEEARNRVRVEIAPTLSLVTTEVLRRVRLLFDLDAAPDRINEAL----GSLAADAPGLRLPGCVNSFE 326
Cdd:COG2169 229 DRF---PAAELIGGDAAFEQLVAEVVGFVEGPLLGLDLPLDLRGTAFQQRVWQALRaipaGETASYAEIAARIGAPKAVR 305
|
330
....*....|...
gi 644362590 327 QATRAVLGQLVSV 339
Cdd:COG2169 306 AVAAACAANQLAV 318
|
|
| AlkA |
COG0122 |
3-methyladenine DNA glycosylase/8-oxoguanine DNA glycosylase [Replication, recombination and ... |
216-486 |
1.74e-62 |
|
3-methyladenine DNA glycosylase/8-oxoguanine DNA glycosylase [Replication, recombination and repair];
Pssm-ID: 439892 [Multi-domain] Cd Length: 255 Bit Score: 204.35 E-value: 1.74e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362590 216 PYDWARMLnflqaravqgvervEGRRYLRSiavsqggTEHRGWFSVQPEEARNRVRVEiaptlslvttEVLRRVRLLFDL 295
Cdd:COG0122 1 PFDLDATL--------------DDGTWRRL-------PDGPGVVRMRPGGDALEVELA----------EAVARLRRLLDL 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362590 296 DAAPDRINE------ALGSLAADAPGLRLPGCVNSFEQATRAVLGQLVSVKMAATFAGRMAERWGEALATPHEGiTHVFP 369
Cdd:COG0122 50 DDDLEAIAAlaardpVLAPLIERYPGLRLPRRPDPFEALVRAILGQQVSVAAARTIWRRLVALFGEPIEGPGGG-LYAFP 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362590 370 TAERVAQLQPEELRPLGVQVKRAAALIEIARALGEGRLQLDNV--LDIEQGIKALTALPGIGSWTASYIAMRAWSWPDVF 447
Cdd:COG0122 129 TPEALAAASEEELRACGLSRRKARYLRALARAVADGELDLEALagLDDEEAIARLTALPGIGPWTAEMVLLFALGRPDAF 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 644362590 448 LAGDY----LIKQRFPG---MTPRQIERYAERWRPWRSYATLHLWH 486
Cdd:COG0122 209 PAGDLglrrALGRLYGLgerPTPKELRELAEPWRPYRSYAARYLWR 254
|
|
| AlkA_N |
smart01009 |
AlkA N-terminal domain; This domain is found at the N terminus of bacterial AlkA . AlkA ... |
213-323 |
1.53e-34 |
|
AlkA N-terminal domain; This domain is found at the N terminus of bacterial AlkA . AlkA (3-methyladenine-DNA glycosylase II) is a base excision repair glycosylase from Escherichia coli. It removes a variety of alkylated bases from DNA, primarily by removing alkylation damage from duplex and single stranded DNA. AlkA flips a 1-azaribose abasic nucleotide out of DNA. This produces a 66 degrees bend in the DNA and a marked widening of the minor groove.
Pssm-ID: 214972 [Multi-domain] Cd Length: 113 Bit Score: 125.38 E-value: 1.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362590 213 YRPPYDWARMLNFLQARAVQGVERVEGRRYLRSIAVSqggtEHRGWFSVQPEEARNRVRVEIAPTLSLVTTEVLRRVRLL 292
Cdd:smart01009 1 YRPPYDWAALLAFLAARAVPGVERVDDGSYRRTLRLG----GGAGWVTVRHDPDRHQLRVTLSLSDLRDLPALIARVRRL 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 644362590 293 FDLDAAPDRINE------ALGSLAADAPGLRLPGCVN 323
Cdd:smart01009 77 LDLDADPEAIDAhlaadpLLGPLVAARPGLRVPGAVD 113
|
|
| AlkA_N |
pfam06029 |
AlkA N-terminal domain; |
208-323 |
3.15e-33 |
|
AlkA N-terminal domain;
Pssm-ID: 428728 [Multi-domain] Cd Length: 118 Bit Score: 121.93 E-value: 3.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362590 208 VFHLGYRPPYDWARMLNFLQARAVQGVERVEGRRYLRSIAVSqggtEHRGWFSVQPEEARNRVRVEIAPTLSLVTTEVLR 287
Cdd:pfam06029 1 TLRLPYRPPYDWAALLAFLAARAIPGVEWVDDGAYRRTLRLG----GGTGWVEVRHDPDRHALRVRLSLSLLRALPPLIA 76
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 644362590 288 RVRLLFDLDAAPDRINEALGS------LAADAPGLRLPGCVN 323
Cdd:pfam06029 77 RVRRLFDLDADPAAIAAHLAAdpllapLVAARPGLRVPGAWD 118
|
|
| Ada_Zn_binding |
pfam02805 |
Metal binding domain of Ada; The Escherichia coli Ada protein repairs O6-methylguanine ... |
17-78 |
6.20e-33 |
|
Metal binding domain of Ada; The Escherichia coli Ada protein repairs O6-methylguanine residues and methyl phosphotriesters in DNA by direct transfer of the methyl group to a cysteine residue. This domain contains four conserved cysteines that form a zinc binding site. One of these cysteines is a methyl group acceptor. The methylated domain can then specifically bind to the ada box on a DNA duplex.
Pssm-ID: 460701 [Multi-domain] Cd Length: 62 Bit Score: 119.47 E-value: 6.20e-33
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 644362590 17 ALYDALRARDRKFDGRFFVGVSSTGIYCRPVCSARTPKRENCTFYPSAAAAELAGFRPCLKC 78
Cdd:pfam02805 1 ARWQAVLARDPRADGSFFYAVKTTGIYCRPSCPARLPKRENVRFFDTAAEAEAAGFRPCKRC 62
|
|
| ENDO3c |
cd00056 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
325-488 |
1.04e-23 |
|
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), alkylbase DNA glycosidases (Alka-family) and other DNA glycosidases
Pssm-ID: 238013 [Multi-domain] Cd Length: 158 Bit Score: 97.31 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362590 325 FEQATRAVLGQLVSVKMAATFAGRMAERWGealatphegithvfPTAERVAQLQPEELRPLGVQV---KRAAALIEIARA 401
Cdd:cd00056 1 FEVLVSEILSQQTTDKAVNKAYERLFERYG--------------PTPEALAAADEEELRELIRSLgyrRKAKYLKELARA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362590 402 LGEGrlQLDNVLDIEQGIKALTALPGIGSWTASYIAMRAWSwPDVFLAgDYLIKQRF-------PGMTPRQIERYAERWR 474
Cdd:cd00056 67 IVEG--FGGLVLDDPDAREELLALPGVGRKTANVVLLFALG-PDAFPV-DTHVRRVLkrlglipKKKTPEELEELLEELL 142
|
170
....*....|....*.
gi 644362590 475 P--WRSYATLHLWHNG 488
Cdd:cd00056 143 PkpYWGEANQALMDLG 158
|
|
| HTH_ARAC |
smart00342 |
helix_turn_helix, arabinose operon control protein; |
110-193 |
2.27e-22 |
|
helix_turn_helix, arabinose operon control protein;
Pssm-ID: 197666 [Multi-domain] Cd Length: 84 Bit Score: 91.08 E-value: 2.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362590 110 EHSCEALAARLGISDRHLRRIFAEQFGASPIDYAQSHRLLQAKRLLADTDLPLSEVAFAAGFGSLRRFNELFKARYRLIP 189
Cdd:smart00342 1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80
|
....
gi 644362590 190 SALR 193
Cdd:smart00342 81 SEYR 84
|
|
| PRK15435 |
PRK15435 |
bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada; |
19-171 |
5.10e-21 |
|
bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;
Pssm-ID: 185333 [Multi-domain] Cd Length: 353 Bit Score: 94.09 E-value: 5.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362590 19 YDALRARDRKFDGRFFVGVSSTGIYCRPVCSARTPKRENCTFYPSAAAAELAGFRPCLKCRPELAPGLAlidlgNRYAQV 98
Cdd:PRK15435 13 WQSVLARDPNADGEFVFAVRTTGIFCRPSCRARHALRENVRFYANASEALAAGFRPCKRCQPDKANPQQ-----HRLDKI 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 644362590 99 --AVQLIEQGylSEHSCEALAARLGISDRHLRRIFAEQFGASPIDYAQSHRLLQAKRLLADTDlPLSEVAFAAGF 171
Cdd:PRK15435 88 thACRLLEQE--TPVTLEALADQVAMSPFHLHRLFKATTGMTPKAWQQAWRARRLREALAKGE-SVTTSILNAGF 159
|
|
| ogg |
TIGR00588 |
8-oxoguanine DNA-glycosylase (ogg); All proteins in this family for which functions are known ... |
258-447 |
9.93e-04 |
|
8-oxoguanine DNA-glycosylase (ogg); All proteins in this family for which functions are known are 8-oxo-guanaine DNA glycosylases that function in base excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). This family is distantly realted to the Nth-MutY superfamily. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 211589 [Multi-domain] Cd Length: 310 Bit Score: 41.05 E-value: 9.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362590 258 WFSVQPEEARNRVRVEI-APTLSLVTTEVLRRVRLLFDLDAAPDR---INEALGSLAADAPGLRLpgcvnsFEQ-ATRAV 332
Cdd:TIGR00588 50 WTLTQTEEQLLCTVYRGdKPTQDELETKLEKYFQLDVSLAQLYTHwgsVDKHFQYVAQKFQGVRL------LRQdPFECL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362590 333 LGQLVSVKMAATFAGRMAER----WGEALATPHEGITHVFPTAERVAQLQPE-ELRPLGVQVkRAAALIEIARALGE--- 404
Cdd:TIGR00588 124 ISFICSSNNNIARITRMVERlcqaFGPRLITLDGVTYHGFPSLHALTGPEAEaHLRKLGLGY-RARYIRETARALLEeqg 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 644362590 405 --GRLQLDNVLDIEQGIKALTALPGIGSWTASYIAMRAWSWPDVF 447
Cdd:TIGR00588 203 grAWLQQIRGASYEDAREALCELPGVGPKVADCICLMGLDKPQAV 247
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10308 |
PRK10308 |
3-methyl-adenine DNA glycosylase II; Provisional |
209-496 |
3.07e-118 |
|
3-methyl-adenine DNA glycosylase II; Provisional
Pssm-ID: 236671 [Multi-domain] Cd Length: 283 Bit Score: 348.67 E-value: 3.07e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362590 209 FHLGYRPPYDWARMLNFLQARAVQGVERVEGRRYLRSIAVSqggtEHRGWFSVQPEEARNRVRVEIAPTLSLVTTEVLRR 288
Cdd:PRK10308 2 YTLNWQPPYDWSWMLGFLAARAVSGVETVAEGYYARSLAVG----EHRGVVTVIPDIARHTLHINLSAGLEPVAAECLAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362590 289 VRLLFDLDAAPDRINEALGSLAADAPGLRLPGCVNSFEQATRAVLGQLVSVKMAATFAGRMAERWGEALATPHEGIthVF 368
Cdd:PRK10308 78 MSRLFDLQCNPQIVNGALGKLGAARPGLRLPGSVDAFEQGVRAILGQLVSVAMAAKLTAKVAQLYGERLDDFPEYV--CF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362590 369 PTAERVAQLQPEELRPLGVQVKRAAALIEIARALGEGRLQLDNVLDIEQGIKALTALPGIGSWTASYIAMRAWSWPDVFL 448
Cdd:PRK10308 156 PTPERLAAADPQALKALGMPLKRAEALIHLANAALEGTLPLTIPGDVEQAMKTLQTFPGIGRWTANYFALRGWQAKDVFL 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 644362590 449 AGDYLIKQRFPGMTPRQIERYAERWRPWRSYATLHLWHNGGWAPEGES 496
Cdd:PRK10308 236 PDDYLIKQRFPGMTPAQIRRYAERWKPWRSYALLHIWYTEGWQPDEDS 283
|
|
| AdaA |
COG2169 |
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ... |
11-339 |
3.83e-86 |
|
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), contains Zn-binding and two AraC-type DNA-binding domains [Replication, recombination and repair];
Pssm-ID: 441772 [Multi-domain] Cd Length: 358 Bit Score: 269.23 E-value: 3.83e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362590 11 MNTQQQALYDALRARDRKFDGRFFVGVSSTGIYCRPVCSARTPKRENCTFYPSAAAAELAGFRPCLKCRPELAPGLALID 90
Cdd:COG2169 4 DLLDDDERWQAVLARDARFDGRFFYGVKTTGIYCRPSCPARKPKRENVRFFATAAAAEAAGFRPCKRCRPDLAPGSPPRA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362590 91 lgnRYAQVAVQLIEQGYLSEHSCEALAARLGISDRHLRRIFAEQFGASPIDYAQSHRLLQAKRLLaDTDLPLSEVAFAAG 170
Cdd:COG2169 84 ---DLVARACRLIEAGAEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQLL-QTGLSVTDAAYAAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362590 171 FGSLRRFNELFKARYRLIPSALRSGGARGERaaasglvfhlgYRPPYDWARMLNFLQARAVQGVERVEGRRYLRSIAVSQ 250
Cdd:COG2169 160 FGSLSRFYEAFKKLLGMTPSAYRRGGAGAAI-----------RFAPTPCSLGLLLVAASARGVCAILLGDDPEALLRDLQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362590 251 GGTehrGWFSVQPEEARNRVRVEIAPTLSLVTTEVLRRVRLLFDLDAAPDRINEAL----GSLAADAPGLRLPGCVNSFE 326
Cdd:COG2169 229 DRF---PAAELIGGDAAFEQLVAEVVGFVEGPLLGLDLPLDLRGTAFQQRVWQALRaipaGETASYAEIAARIGAPKAVR 305
|
330
....*....|...
gi 644362590 327 QATRAVLGQLVSV 339
Cdd:COG2169 306 AVAAACAANQLAV 318
|
|
| AlkA |
COG0122 |
3-methyladenine DNA glycosylase/8-oxoguanine DNA glycosylase [Replication, recombination and ... |
216-486 |
1.74e-62 |
|
3-methyladenine DNA glycosylase/8-oxoguanine DNA glycosylase [Replication, recombination and repair];
Pssm-ID: 439892 [Multi-domain] Cd Length: 255 Bit Score: 204.35 E-value: 1.74e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362590 216 PYDWARMLnflqaravqgvervEGRRYLRSiavsqggTEHRGWFSVQPEEARNRVRVEiaptlslvttEVLRRVRLLFDL 295
Cdd:COG0122 1 PFDLDATL--------------DDGTWRRL-------PDGPGVVRMRPGGDALEVELA----------EAVARLRRLLDL 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362590 296 DAAPDRINE------ALGSLAADAPGLRLPGCVNSFEQATRAVLGQLVSVKMAATFAGRMAERWGEALATPHEGiTHVFP 369
Cdd:COG0122 50 DDDLEAIAAlaardpVLAPLIERYPGLRLPRRPDPFEALVRAILGQQVSVAAARTIWRRLVALFGEPIEGPGGG-LYAFP 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362590 370 TAERVAQLQPEELRPLGVQVKRAAALIEIARALGEGRLQLDNV--LDIEQGIKALTALPGIGSWTASYIAMRAWSWPDVF 447
Cdd:COG0122 129 TPEALAAASEEELRACGLSRRKARYLRALARAVADGELDLEALagLDDEEAIARLTALPGIGPWTAEMVLLFALGRPDAF 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 644362590 448 LAGDY----LIKQRFPG---MTPRQIERYAERWRPWRSYATLHLWH 486
Cdd:COG0122 209 PAGDLglrrALGRLYGLgerPTPKELRELAEPWRPYRSYAARYLWR 254
|
|
| AlkA_N |
smart01009 |
AlkA N-terminal domain; This domain is found at the N terminus of bacterial AlkA . AlkA ... |
213-323 |
1.53e-34 |
|
AlkA N-terminal domain; This domain is found at the N terminus of bacterial AlkA . AlkA (3-methyladenine-DNA glycosylase II) is a base excision repair glycosylase from Escherichia coli. It removes a variety of alkylated bases from DNA, primarily by removing alkylation damage from duplex and single stranded DNA. AlkA flips a 1-azaribose abasic nucleotide out of DNA. This produces a 66 degrees bend in the DNA and a marked widening of the minor groove.
Pssm-ID: 214972 [Multi-domain] Cd Length: 113 Bit Score: 125.38 E-value: 1.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362590 213 YRPPYDWARMLNFLQARAVQGVERVEGRRYLRSIAVSqggtEHRGWFSVQPEEARNRVRVEIAPTLSLVTTEVLRRVRLL 292
Cdd:smart01009 1 YRPPYDWAALLAFLAARAVPGVERVDDGSYRRTLRLG----GGAGWVTVRHDPDRHQLRVTLSLSDLRDLPALIARVRRL 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 644362590 293 FDLDAAPDRINE------ALGSLAADAPGLRLPGCVN 323
Cdd:smart01009 77 LDLDADPEAIDAhlaadpLLGPLVAARPGLRVPGAVD 113
|
|
| AlkA_N |
pfam06029 |
AlkA N-terminal domain; |
208-323 |
3.15e-33 |
|
AlkA N-terminal domain;
Pssm-ID: 428728 [Multi-domain] Cd Length: 118 Bit Score: 121.93 E-value: 3.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362590 208 VFHLGYRPPYDWARMLNFLQARAVQGVERVEGRRYLRSIAVSqggtEHRGWFSVQPEEARNRVRVEIAPTLSLVTTEVLR 287
Cdd:pfam06029 1 TLRLPYRPPYDWAALLAFLAARAIPGVEWVDDGAYRRTLRLG----GGTGWVEVRHDPDRHALRVRLSLSLLRALPPLIA 76
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 644362590 288 RVRLLFDLDAAPDRINEALGS------LAADAPGLRLPGCVN 323
Cdd:pfam06029 77 RVRRLFDLDADPAAIAAHLAAdpllapLVAARPGLRVPGAWD 118
|
|
| Ada_Zn_binding |
pfam02805 |
Metal binding domain of Ada; The Escherichia coli Ada protein repairs O6-methylguanine ... |
17-78 |
6.20e-33 |
|
Metal binding domain of Ada; The Escherichia coli Ada protein repairs O6-methylguanine residues and methyl phosphotriesters in DNA by direct transfer of the methyl group to a cysteine residue. This domain contains four conserved cysteines that form a zinc binding site. One of these cysteines is a methyl group acceptor. The methylated domain can then specifically bind to the ada box on a DNA duplex.
Pssm-ID: 460701 [Multi-domain] Cd Length: 62 Bit Score: 119.47 E-value: 6.20e-33
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 644362590 17 ALYDALRARDRKFDGRFFVGVSSTGIYCRPVCSARTPKRENCTFYPSAAAAELAGFRPCLKC 78
Cdd:pfam02805 1 ARWQAVLARDPRADGSFFYAVKTTGIYCRPSCPARLPKRENVRFFDTAAEAEAAGFRPCKRC 62
|
|
| ENDO3c |
cd00056 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
325-488 |
1.04e-23 |
|
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), alkylbase DNA glycosidases (Alka-family) and other DNA glycosidases
Pssm-ID: 238013 [Multi-domain] Cd Length: 158 Bit Score: 97.31 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362590 325 FEQATRAVLGQLVSVKMAATFAGRMAERWGealatphegithvfPTAERVAQLQPEELRPLGVQV---KRAAALIEIARA 401
Cdd:cd00056 1 FEVLVSEILSQQTTDKAVNKAYERLFERYG--------------PTPEALAAADEEELRELIRSLgyrRKAKYLKELARA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362590 402 LGEGrlQLDNVLDIEQGIKALTALPGIGSWTASYIAMRAWSwPDVFLAgDYLIKQRF-------PGMTPRQIERYAERWR 474
Cdd:cd00056 67 IVEG--FGGLVLDDPDAREELLALPGVGRKTANVVLLFALG-PDAFPV-DTHVRRVLkrlglipKKKTPEELEELLEELL 142
|
170
....*....|....*.
gi 644362590 475 P--WRSYATLHLWHNG 488
Cdd:cd00056 143 PkpYWGEANQALMDLG 158
|
|
| HTH_18 |
pfam12833 |
Helix-turn-helix domain; |
116-193 |
1.18e-22 |
|
Helix-turn-helix domain;
Pssm-ID: 432818 [Multi-domain] Cd Length: 81 Bit Score: 91.50 E-value: 1.18e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 644362590 116 LAARLGISDRHLRRIFAEQFGASPIDYAQSHRLLQAKRLLAD-TDLPLSEVAFAAGFGSLRRFNELFKARYRLIPSALR 193
Cdd:pfam12833 1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLEdTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYR 79
|
|
| HTH_ARAC |
smart00342 |
helix_turn_helix, arabinose operon control protein; |
110-193 |
2.27e-22 |
|
helix_turn_helix, arabinose operon control protein;
Pssm-ID: 197666 [Multi-domain] Cd Length: 84 Bit Score: 91.08 E-value: 2.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362590 110 EHSCEALAARLGISDRHLRRIFAEQFGASPIDYAQSHRLLQAKRLLADTDLPLSEVAFAAGFGSLRRFNELFKARYRLIP 189
Cdd:smart00342 1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80
|
....
gi 644362590 190 SALR 193
Cdd:smart00342 81 SEYR 84
|
|
| GlxA |
COG4977 |
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ... |
99-202 |
4.76e-21 |
|
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH domain [Transcription];
Pssm-ID: 444002 [Multi-domain] Cd Length: 318 Bit Score: 93.68 E-value: 4.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362590 99 AVQLIEQGYLSEHSCEALAARLGISDRHLRRIFAEQFGASPIDYAQSHRLLQAKRLLADTDLPLSEVAFAAGFGSLRRFN 178
Cdd:COG4977 215 AQAWMEANLEEPLSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFGSASHFR 294
|
90 100
....*....|....*....|....
gi 644362590 179 ELFKARYRLIPSALRSGGARGERA 202
Cdd:COG4977 295 RAFRRRFGVSPSAYRRRFRARAAA 318
|
|
| PRK15435 |
PRK15435 |
bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada; |
19-171 |
5.10e-21 |
|
bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;
Pssm-ID: 185333 [Multi-domain] Cd Length: 353 Bit Score: 94.09 E-value: 5.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362590 19 YDALRARDRKFDGRFFVGVSSTGIYCRPVCSARTPKRENCTFYPSAAAAELAGFRPCLKCRPELAPGLAlidlgNRYAQV 98
Cdd:PRK15435 13 WQSVLARDPNADGEFVFAVRTTGIFCRPSCRARHALRENVRFYANASEALAAGFRPCKRCQPDKANPQQ-----HRLDKI 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 644362590 99 --AVQLIEQGylSEHSCEALAARLGISDRHLRRIFAEQFGASPIDYAQSHRLLQAKRLLADTDlPLSEVAFAAGF 171
Cdd:PRK15435 88 thACRLLEQE--TPVTLEALADQVAMSPFHLHRLFKATTGMTPKAWQQAWRARRLREALAKGE-SVTTSILNAGF 159
|
|
| AraC |
COG2207 |
AraC-type DNA-binding domain and AraC-containing proteins [Transcription]; |
64-198 |
1.07e-19 |
|
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
Pssm-ID: 441809 [Multi-domain] Cd Length: 258 Bit Score: 88.68 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362590 64 AAAAELAGFRPCLKCRPELAPGLALIDLGNRYAQVAVQLIEQGYLSEHSCEALAARLGISDRHLRRIFAEQFGASPIDYA 143
Cdd:COG2207 122 LLLLLLLALLRALELLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLTLEELARELGLSPRTLSRLFKEETGTSPKQYL 201
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 644362590 144 QSHRLLQAKRLLADTDLPLSEVAFAAGFGSLRRFNELFKARYRLIPSALRSGGAR 198
Cdd:COG2207 202 RELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPSEYRKRLRA 256
|
|
| ENDO3c |
smart00478 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
345-486 |
6.47e-17 |
|
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), alkylbase DNA glycosidases (Alka-family) and other DNA glycosidases
Pssm-ID: 214684 [Multi-domain] Cd Length: 149 Bit Score: 77.69 E-value: 6.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362590 345 FAGRMAERWGEAlatphegithvFPTAERVAQLQPEEL----RPLGVQVKRAAALIEIARALGEGRLQldnvlDIEQGIK 420
Cdd:smart00478 9 RVNKATERLFEK-----------FPTPEDLAAADEEELeeliRGLGFYRRKARYLIELARILVEEYGG-----EVPDDRE 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 644362590 421 ALTALPGIGSWTASYIAMRAWSwpDVFLAGD---YLIKQRFPGM----TPRQIERYAERWRP---WRSYATLHLWH 486
Cdd:smart00478 73 ELLKLPGVGRKTANAVLSFALG--KPFIPVDthvLRIAKRLGLVdkksTPEEVEKLLEKLLPeedWRELNLLLIDF 146
|
|
| HhH-GPD |
pfam00730 |
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ... |
330-473 |
3.91e-12 |
|
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of structurally related DNA repair proteins. The superfamily is called the HhH-GPD family after its hallmark Helix-hairpin-helix and Gly/Pro rich loop followed by a conserved aspartate. This includes endonuclease III, EC:4.2.99.18 and MutY an A/G-specific adenine glycosylase, both have a C terminal 4Fe-4S cluster. The family also includes 8-oxoguanine DNA glycosylases. The methyl-CPG binding protein MBD4 also contains a related domain that is a thymine DNA glycosylase. The family also includes DNA-3-methyladenine glycosylase II EC:3.2.2.21 and other members of the AlkA family.
Pssm-ID: 425841 [Multi-domain] Cd Length: 141 Bit Score: 63.84 E-value: 3.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362590 330 RAVLGQLVSVKmaatFAGRMAERWGEAlatphegithVFPTAERVAQLQPEELR----PLGVQVKRAAALIEIARALGEG 405
Cdd:pfam00730 2 SAILSQQTSDK----AVNKITERLFEK----------FFPTPEDLADADEEELRelirGLGFYRRKAKYLKELARILVEG 67
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 644362590 406 RLQldnvlDIEQGIKAL-TALPGIGSWTASYIAMRAWSWPDVFLAGDYLIK---QRFPGM----TPRQIERYAERW 473
Cdd:pfam00730 68 YGG-----EVPLDEEELeALLKGVGRWTAEAVLIFALGRPDPLPVVDTHVRrvlKRLGLIkekpTPKEVERELEEL 138
|
|
| ftrA |
PRK09393 |
transcriptional activator FtrA; Provisional |
110-193 |
4.37e-10 |
|
transcriptional activator FtrA; Provisional
Pssm-ID: 181818 [Multi-domain] Cd Length: 322 Bit Score: 61.13 E-value: 4.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362590 110 EHSCEALAARLGISDRHLRRIFAEQFGASPIDYAQSHRLLQAKRLLADTDLPLSEVAFAAGFGSLRRFNELFKARYRLIP 189
Cdd:PRK09393 234 PHTVASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLARARDLLESSALSIDQIAERAGFGSEESLRHHFRRRAATSP 313
|
....
gi 644362590 190 SALR 193
Cdd:PRK09393 314 AAYR 317
|
|
| PRK13503 |
PRK13503 |
HTH-type transcriptional activator RhaS; |
101-195 |
5.66e-10 |
|
HTH-type transcriptional activator RhaS;
Pssm-ID: 184094 [Multi-domain] Cd Length: 278 Bit Score: 60.08 E-value: 5.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362590 101 QLIeqGYLSEHSCE-----ALAARLGISDRHLRRIFAEQFGASPIDYAQSHRLLQAKRLLADTDLPLSEVAFAAGFGSLR 175
Cdd:PRK13503 175 QLL--AWLEDHFAEevnweALADQFSLSLRTLHRQLKQQTGLTPQRYLNRLRLLKARHLLRHSDASVTDIAYRCGFGDSN 252
|
90 100
....*....|....*....|
gi 644362590 176 RFNELFKARYRLIPSALRSG 195
Cdd:PRK13503 253 HFSTLFRREFSWSPRDIRQG 272
|
|
| PRK09685 |
PRK09685 |
DNA-binding transcriptional activator FeaR; Provisional |
97-195 |
3.33e-07 |
|
DNA-binding transcriptional activator FeaR; Provisional
Pssm-ID: 236612 [Multi-domain] Cd Length: 302 Bit Score: 51.96 E-value: 3.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362590 97 QVAVQLIEQGYLSEH-SCEALAARLGISDRHLRRIFAEQfGASPIDYAQSHRL-LQAKRLLADT-DLPLSEVAFAAGFGS 173
Cdd:PRK09685 200 QKVVALIDQSIQEEIlRPEWIAGELGISVRSLYRLFAEQ-GLVVAQYIRNRRLdRCADDLRPAAdDEKITSIAYKWGFSD 278
|
90 100
....*....|....*....|..
gi 644362590 174 LRRFNELFKARYRLIPSALRSG 195
Cdd:PRK09685 279 SSHFSTAFKQRFGVSPGEYRRK 300
|
|
| PRK11511 |
PRK11511 |
MDR efflux pump AcrAB transcriptional activator MarA; |
103-200 |
3.14e-06 |
|
MDR efflux pump AcrAB transcriptional activator MarA;
Pssm-ID: 236920 [Multi-domain] Cd Length: 127 Bit Score: 46.63 E-value: 3.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362590 103 IEQGYLSEHSCEALAARLGISDRHLRRIFAEQFGASPIDYAQSHRLLQAKRLLADTDLPLSEVAFAAGFGSLRRFNELFK 182
Cdd:PRK11511 18 IEDNLESPLSLEKVSERSGYSKWHLQRMFKKETGHSLGQYIRSRKMTEIAQKLKESNEPILYLAERYGFESQQTLTRTFK 97
|
90
....*....|....*...
gi 644362590 183 ARYRLIPSALRSGGARGE 200
Cdd:PRK11511 98 NYFDVPPHKYRMTNMQGE 115
|
|
| PRK13501 |
PRK13501 |
HTH-type transcriptional activator RhaR; |
122-193 |
3.24e-05 |
|
HTH-type transcriptional activator RhaR;
Pssm-ID: 184092 [Multi-domain] Cd Length: 290 Bit Score: 45.67 E-value: 3.24e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 644362590 122 ISDRHLRRIFAEQFGASPIDYAQSHRLLQAKRLLADTDLPLSEVAFAAGFGSLRRFNELFKARYRLIPSALR 193
Cdd:PRK13501 204 LVERSLKQLFRQQTGMSISHYLRQIRLCHAKCLLRGSEHRISDIAARCGFEDSNYFSAVFTREAGMTPRDYR 275
|
|
| PRK10371 |
PRK10371 |
transcriptional regulator MelR; |
69-206 |
6.34e-05 |
|
transcriptional regulator MelR;
Pssm-ID: 182416 [Multi-domain] Cd Length: 302 Bit Score: 44.81 E-value: 6.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362590 69 LAGFRPCLKCRPELAPGLALidlgNRYAQVAVQLIeQGYLSEHSCEAL-----AARLGISDRHLRRIFAEQFGASPIDYA 143
Cdd:PRK10371 166 LSGWEPILVNKTSRTHKNSV----SRHAQFYVSQM-LGFIAENYDQALtindvAEHVKLNANYAMGIFQRVMQLTMKQYI 240
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 644362590 144 QSHRLLQAKRLLADTDLPLSEVAFAAGFGSLRRFNELFKARYRLIPSALRSgGARGERAAASG 206
Cdd:PRK10371 241 TAMRINHVRALLSDTDKSILDIALTAGFRSSSRFYSTFGKYVGMSPQQYRK-LSQQRRQTFPG 302
|
|
| ogg |
TIGR00588 |
8-oxoguanine DNA-glycosylase (ogg); All proteins in this family for which functions are known ... |
258-447 |
9.93e-04 |
|
8-oxoguanine DNA-glycosylase (ogg); All proteins in this family for which functions are known are 8-oxo-guanaine DNA glycosylases that function in base excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). This family is distantly realted to the Nth-MutY superfamily. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 211589 [Multi-domain] Cd Length: 310 Bit Score: 41.05 E-value: 9.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362590 258 WFSVQPEEARNRVRVEI-APTLSLVTTEVLRRVRLLFDLDAAPDR---INEALGSLAADAPGLRLpgcvnsFEQ-ATRAV 332
Cdd:TIGR00588 50 WTLTQTEEQLLCTVYRGdKPTQDELETKLEKYFQLDVSLAQLYTHwgsVDKHFQYVAQKFQGVRL------LRQdPFECL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362590 333 LGQLVSVKMAATFAGRMAER----WGEALATPHEGITHVFPTAERVAQLQPE-ELRPLGVQVkRAAALIEIARALGE--- 404
Cdd:TIGR00588 124 ISFICSSNNNIARITRMVERlcqaFGPRLITLDGVTYHGFPSLHALTGPEAEaHLRKLGLGY-RARYIRETARALLEeqg 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 644362590 405 --GRLQLDNVLDIEQGIKALTALPGIGSWTASYIAMRAWSWPDVF 447
Cdd:TIGR00588 203 grAWLQQIRGASYEDAREALCELPGVGPKVADCICLMGLDKPQAV 247
|
|
| Nth |
COG0177 |
Endonuclease III [Replication, recombination and repair]; |
367-444 |
1.11e-03 |
|
Endonuclease III [Replication, recombination and repair];
Pssm-ID: 439947 [Multi-domain] Cd Length: 198 Bit Score: 40.08 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362590 367 VFPTAERVAQLQPEEL----RPLGVQVKRAAALIEIARAL-----GEgrlqldnvldIEQGIKALTALPGIGSWTASYIA 437
Cdd:COG0177 48 RYPTPEALAAADLEELeeliRPIGLYRNKAKNIIALARILvekygGE----------VPETREELESLPGVGRKTANVVL 117
|
....*..
gi 644362590 438 MRAWSWP 444
Cdd:COG0177 118 NFAFGKP 124
|
|
| PRK13502 |
PRK13502 |
HTH-type transcriptional activator RhaR; |
114-193 |
8.41e-03 |
|
HTH-type transcriptional activator RhaR;
Pssm-ID: 184093 [Multi-domain] Cd Length: 282 Bit Score: 38.11 E-value: 8.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644362590 114 EALAARLGISDRHLRRIFAEQFGASPIDYAQSHRLLQAKRLLADTDLPLSEVAFAAGFGSLRRFNELFKARYRLIPSALR 193
Cdd:PRK13502 196 DAFCQQEQCSERVLRQQFRAQTGMTINQYLRQVRICHAQYLLQHSPLMISEISMQCGFEDSNYFSVVFTRETGMTPSQWR 275
|
|
| |
