|
Name |
Accession |
Description |
Interval |
E-value |
| MurI |
COG0796 |
Glutamate racemase [Cell wall/membrane/envelope biogenesis]; Glutamate racemase is part of the ... |
3-266 |
2.05e-133 |
|
Glutamate racemase [Cell wall/membrane/envelope biogenesis]; Glutamate racemase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440559 Cd Length: 261 Bit Score: 385.98 E-value: 2.05e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 3 KQPIGFIDSGVGGLTVVKEALHQLPAENTIYLGDQARLPYGPRPAEQVQAFTWQMVNFLLTKHIKMLVIACNTATAAALP 82
Cdd:COG0796 1 NAPIGVFDSGVGGLTVLREIRKLLPNEDIIYFGDTARFPYGEKSEEEIRERTLEIVEFLLEQGVKLIVIACNTASAAALD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 83 LIKARLKIPVIGVIkPGSRAALKATQTGHIGIIATEGTVKSGAYPKALRAKAPDIRLTSLAAPKFVSLVESNEAHSPIAK 162
Cdd:COG0796 81 ALRERYDIPVVGVI-PAIKPAAAATRNGRIGVLATPATVKSGAYQRLIARFAPDVEVISQACPGLVPLVEEGLLDGPETR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 163 RVVADTLQPLLHQDIDTLVLGCTHYPILRPIIQNVMGEDVTLIDSGAETVNDVSMLLDYFDLANDGSEVPTHTYYTTGAP 242
Cdd:COG0796 160 ALVREYLAPLLAAGIDTLVLGCTHYPLLKPLIQEVLGPGVTLIDSAEAVARRVKRLLEEHGLLNPEGAPGTVRFYTTGDP 239
|
250 260
....*....|....*....|....
gi 491946784 243 SMFDELGESWLELkkPMHAQHVDI 266
Cdd:COG0796 240 EAFARLARRFLGE--PISVEKLDL 261
|
|
| PRK00865 |
PRK00865 |
glutamate racemase; Provisional |
1-260 |
1.70e-129 |
|
glutamate racemase; Provisional
Pssm-ID: 234851 Cd Length: 261 Bit Score: 375.98 E-value: 1.70e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 1 MNKQPIGFIDSGVGGLTVVKEALHQLPAENTIYLGDQARLPYGPRPAEQVQAFTWQMVNFLLTKHIKMLVIACNTATAAA 80
Cdd:PRK00865 3 MMNAPIGVFDSGVGGLTVLREIRRLLPDEHIIYVGDTARFPYGEKSEEEIRERTLEIVEFLLEYGVKMLVIACNTASAVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 81 LPLIKARLKIPVIGvIKPGSRAALKATQTGHIGIIATEGTVKSGAYPKALRAKAPDIRLTSLAAPKFVSLVESNEAHSPI 160
Cdd:PRK00865 83 LPDLRERYDIPVVG-IVPAIKPAAALTRNGRIGVLATPGTVKSAAYRDLIARFAPDCQVESLACPELVPLVEAGILGGPV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 161 AKRVVADTLQPLLHQDIDTLVLGCTHYPILRPIIQNVMGEDVTLIDSGAETVNDVSMLLDYFDLANDGSEVPTHTYYTTG 240
Cdd:PRK00865 162 TLEVLREYLAPLLAAGIDTLVLGCTHYPLLKPEIQQVLGEGVTLIDSGEAIARRVARLLEELNLLASSDENPAHRFFTTG 241
|
250 260
....*....|....*....|
gi 491946784 241 APSMFDELGESWLELKKPMH 260
Cdd:PRK00865 242 DPEAFKRLAQRWLGLLEKVE 261
|
|
| PRK14822 |
PRK14822 |
XTP/dITP diphosphatase; |
283-482 |
6.23e-98 |
|
XTP/dITP diphosphatase;
Pssm-ID: 184835 [Multi-domain] Cd Length: 200 Bit Score: 293.33 E-value: 6.23e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 283 KTIVIASKNPGKIKEFKAMFEPAGVTVKSLADFPTVPTVDETGTTFEANARQKADQYAQDLNLPVLADDSGLMVDALDGQ 362
Cdd:PRK14822 2 KEIVIATKNKGKVREFKEIFEKFDIEVKSLADFPPIPEVEETGTTFEENAILKAEAAAKALNKPVIADDSGLEVDALNGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 363 PGIRSARYAGDGHNDAANNAKLLAALADVPEEARTATFHTTLVLAKPNHPeaDLVVHGDLSGRITAIPRGTDGFGYDPFF 442
Cdd:PRK14822 82 PGVYSARYAGEAKDDAANNEKLLKELGGVPFEKRTARFHCVIAVAFPGGE--TKTVEGTCEGEILEEPRGENGFGYDPLF 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 491946784 443 LVPALDKTLAELTADEKNEISHRGNAMRALEKVWQAWLEE 482
Cdd:PRK14822 160 YVPEKGKTMAELSSEEKNAISHRGKALKKLEAELPEWLKV 199
|
|
| RdgB |
COG0127 |
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide ... |
284-482 |
6.07e-86 |
|
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide transport and metabolism];
Pssm-ID: 439897 [Multi-domain] Cd Length: 191 Bit Score: 261.92 E-value: 6.07e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 284 TIVIASKNPGKIKEFKAMFEPAGVTVKSLADFPtVPTVDETGTTFEANARQKADQYAQDLNLPVLADDSGLMVDALDGQP 363
Cdd:COG0127 1 KLVFATGNAGKLREIRALLAPLGIEVVSLSDLG-LPEPEETGDTFEENALIKARAAAKATGLPALADDSGLEVDALGGAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 364 GIRSARYAGDGHNDAANNAKLLAALADVPEEaRTATFHTTLVLAKPNHPEadLVVHGDLSGRITAIPRGTDGFGYDPFFL 443
Cdd:COG0127 80 GVYSARYAGEGADDEANNEKLLKLLEGVDED-RRARFVCVLALADPDGEP--LVFEGEVEGEIAEEPRGEGGFGYDPIFI 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 491946784 444 VPALDKTLAELTADEKNEISHRGNAMRALekvwQAWLEE 482
Cdd:COG0127 157 PDGYGKTFAELSPEEKNAISHRGRALRKL----AEWLKE 191
|
|
| glut_race |
TIGR00067 |
glutamate racemase; This family consists of glutamate racemase, a protein required for making ... |
6-255 |
1.81e-83 |
|
glutamate racemase; This family consists of glutamate racemase, a protein required for making the UDP-N-acetylmuramoyl-pentapeptide used as a precursor in bacterial peptidoglycan biosynthesis. The most closely related proteins differing in function are aspartate racemases. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 272885 Cd Length: 251 Bit Score: 258.11 E-value: 1.81e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 6 IGFIDSGVGGLTVVKEALHQLPAENTIYLGDQARLPYGPRPAEQVQAFTWQMVNFLLTKH-IKMLVIACNTATAAALPLI 84
Cdd:TIGR00067 1 IGVFDSGVGGLSVLKEIRKQLPKEHYIYVGDTKRFPYGEKSPEFILEYVLELLTFLKERHnIKLLVVACNTASALALEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 85 KARLKIPVIGVIKPGSRAALKATQTGHIGIIATEGTVKSGAYPKALRAKAPDIRLTSLAAPKFVSLVESNEAHSPIAKRV 164
Cdd:TIGR00067 81 QRNFDFPVVGVIEPAIKAAIRLTANGRVLVIATNATIKSNAYHEALKEIANDLLVEMLACPELVPLAEAGLLGEDYALEC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 165 VADTLQPLLHQDIDTLVLGCTHYPILRPIIQNVMGEDVTLIDSGAETVNDVSMLLDYFDLANDGSEVPTHTYYTTGAPSM 244
Cdd:TIGR00067 161 LKRYLRPLLDTLPDTVVLGCTHFPLLKEEIEQYLPEHVRLVDSGVHTARRTAWLLEHKGPLAKSADAPDIEFCMSGTPIQ 240
|
250
....*....|.
gi 491946784 245 FDELGESWLEL 255
Cdd:TIGR00067 241 FQELAKKWLGL 251
|
|
| Ham1p_like |
pfam01725 |
Ham1 family; This family consists of the HAM1 protein and hypothetical archaeal bacterial and ... |
285-472 |
5.25e-80 |
|
Ham1 family; This family consists of the HAM1 protein and hypothetical archaeal bacterial and C. elegans proteins. HAM1 controls 6-N-hydroxylaminopurine (HAP) sensitivity and mutagenesis in S. cerevisiae. The HAM1 protein protects the cell from HAP, either on the level of deoxynucleoside triphosphate or the DNA level by a yet unidentified set of reactions.
Pssm-ID: 460306 [Multi-domain] Cd Length: 186 Bit Score: 246.59 E-value: 5.25e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 285 IVIASKNPGKIKEFKAMFEPaGVTVKSLADFPTVPTVDETGTTFEANARQKAdQYAQDLNLPVLADDSGLMVDALDGQPG 364
Cdd:pfam01725 1 IVFATGNAGKLRELKAILAD-GIEVLSLKDLGELPEIEETGGTFEENALIKA-RAAAKTGLPVLADDSGLEVDALNGFPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 365 IRSARYAGDGHNDAANNAKLLAALaDVPEEARTATFHTTLVLAKPNHPEadLVVHGDLSGRITAIPRGTDGFGYDPFFLV 444
Cdd:pfam01725 79 VYSARFAGEGGDDEANNAKLLEEL-EVPDEDRSARFVCVIALADPGGPE--LVFEGEVEGEIVEEPRGEGGFGYDPIFIP 155
|
170 180
....*....|....*....|....*...
gi 491946784 445 PALDKTLAELTADEKNEISHRGNAMRAL 472
Cdd:pfam01725 156 PEGGKTFAELSPEEKNAISHRGKALRKL 183
|
|
| HAM1 |
cd00515 |
NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ ... |
285-472 |
3.21e-70 |
|
NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ inosine triphosphatase. HAM1 protects the cell against mutagenesis by the base analog 6-N-hydroxylaminopurine (HAP) in E. Coli and S. cerevisiae. A Ham1-related protein from Methanococcus jannaschii is a novel NTPase that has been shown to hydrolyze nonstandard nucleotides such as XTP to XMP and ITP to IMP, but not the standard nucleotides, in the presence of Mg or Mn ions. The enzyme exists as a homodimer. The HAM1 protein may be acting as an NTPase by hydrolyzing the HAP triphosphate.
Pssm-ID: 238285 [Multi-domain] Cd Length: 183 Bit Score: 221.24 E-value: 3.21e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 285 IVIASKNPGKIKEFKAMFEPAGVTVKSLADFPTVPtvdETGTTFEANARQKADQYAQDLNLPVLADDSGLMVDALDGQPG 364
Cdd:cd00515 1 IVFATGNKGKLKEFKEILAPFGIEVVSLKDIIDIE---ETGSTFEENALLKARAAAEALGLPVLADDSGLCVDALNGFPG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 365 IRSARYAGDgHNDAANNAKLLAALADvpEEARTATFHTTLVLAKPNHPEadLVVHGDLSGRITAIPRGTDGFGYDPFFLV 444
Cdd:cd00515 78 VYSARFAGE-HDDAENNEKLLELLEG--DEDRSAYFVCVIALVDPDGEP--LVFEGEVEGKIVTEPRGTGGFGYDPIFIP 152
|
170 180
....*....|....*....|....*...
gi 491946784 445 PALDKTLAELTADEKNEISHRGNAMRAL 472
Cdd:cd00515 153 EGYGKTFAEMSPEEKNAISHRGKALRKL 180
|
|
| TIGR00042 |
TIGR00042 |
non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 ... |
284-476 |
6.82e-55 |
|
non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 protects against the mutagenic effects of the base analog 6-N-hydroxylaminopurine, which can be a natural product of monooxygenase activity on adenine. Methanococcus jannaschii MJ0226 and E. coli RdgB are also characterized as pyrophosphatases active against non-standard purines NTPs. E. coli RdgB appears to act by intercepting non-canonical deoxyribonucleotide triphosphates from replication precursor pools. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 272870 [Multi-domain] Cd Length: 184 Bit Score: 181.80 E-value: 6.82e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 284 TIVIASKNPGKIKEFKAMFEPAGVTVKSLADFPTVptvDETGTTFEANARQKADQYAQDLNLPVLADDSGLMVDALDGQP 363
Cdd:TIGR00042 1 KIVFATGNPGKLKEVQSILSDLGDNEIEQLDLGYP---EETGLTFEENALLKAKHAAKILNKPVIAEDSGLFVDALNGFP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 364 GIRSARYAGDGHNDAANNAKLLAaladvPEEARTATFHTTLVLAKPNhpEADLVVHGDLSGRITAIPRGTDGFGYDPFFL 443
Cdd:TIGR00042 78 GIYSARYQGTDIGNLEKILKLLE-----GVENRQAYFVCVIGYCDPN--GEPLVFEGIVKGKITREPRGTYGFGYDPIFI 150
|
170 180 190
....*....|....*....|....*....|...
gi 491946784 444 VPALDKTLAELTADEKNEISHRGNAMRALEKVW 476
Cdd:TIGR00042 151 PPEEGKTFAELTTEEKNKISHRGKAFKKFKKFL 183
|
|
| Asp_Glu_race |
pfam01177 |
Asp/Glu/Hydantoin racemase; This family contains aspartate racemase, maleate isomerases EC:5.2. ... |
6-213 |
7.20e-24 |
|
Asp/Glu/Hydantoin racemase; This family contains aspartate racemase, maleate isomerases EC:5.2.1.1, glutamate racemase, hydantoin racemase and arylmalonate decarboxylase EC:4.1.1.76.
Pssm-ID: 426101 Cd Length: 210 Bit Score: 99.26 E-value: 7.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 6 IGFIDSGvGGLTVVKEALHQLPAEN----TIYLGDQARLPYGPRPAEQVQAFTWQMVNFLLT---KHIKMLVIACNTATA 78
Cdd:pfam01177 1 IGGINPN-STASMTRKIVEAARAVLpphvPVILVTSPDGPDRIESPEDGALAAPALLEALRRleaAGADAIVIACFTDHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 79 AaLPLIKARLKIPVIGVIKPGSRAALKatQTGHIGIIATEGTvKSGAYPKALRAKAPDIRLTSLAAPKFVSLVESNEAHS 158
Cdd:pfam01177 80 G-LDALRELTDIPVLGIAEAAALAALA--LGGRFGVLTTLGT-SSPVYERALRAYGLEVRCPGVRAQEGLPVLIVKGGDT 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491946784 159 PIAKRVVADTLQPLLHQDIDTLVLGCTHYPILRPIIQNVMGedVTLIDSGAETVN 213
Cdd:pfam01177 156 EEARALLLEAAKALVEDGADAIILGCTGLPGLAEELEAELG--VPVIDPVDAAVR 208
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MurI |
COG0796 |
Glutamate racemase [Cell wall/membrane/envelope biogenesis]; Glutamate racemase is part of the ... |
3-266 |
2.05e-133 |
|
Glutamate racemase [Cell wall/membrane/envelope biogenesis]; Glutamate racemase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440559 Cd Length: 261 Bit Score: 385.98 E-value: 2.05e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 3 KQPIGFIDSGVGGLTVVKEALHQLPAENTIYLGDQARLPYGPRPAEQVQAFTWQMVNFLLTKHIKMLVIACNTATAAALP 82
Cdd:COG0796 1 NAPIGVFDSGVGGLTVLREIRKLLPNEDIIYFGDTARFPYGEKSEEEIRERTLEIVEFLLEQGVKLIVIACNTASAAALD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 83 LIKARLKIPVIGVIkPGSRAALKATQTGHIGIIATEGTVKSGAYPKALRAKAPDIRLTSLAAPKFVSLVESNEAHSPIAK 162
Cdd:COG0796 81 ALRERYDIPVVGVI-PAIKPAAAATRNGRIGVLATPATVKSGAYQRLIARFAPDVEVISQACPGLVPLVEEGLLDGPETR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 163 RVVADTLQPLLHQDIDTLVLGCTHYPILRPIIQNVMGEDVTLIDSGAETVNDVSMLLDYFDLANDGSEVPTHTYYTTGAP 242
Cdd:COG0796 160 ALVREYLAPLLAAGIDTLVLGCTHYPLLKPLIQEVLGPGVTLIDSAEAVARRVKRLLEEHGLLNPEGAPGTVRFYTTGDP 239
|
250 260
....*....|....*....|....
gi 491946784 243 SMFDELGESWLELkkPMHAQHVDI 266
Cdd:COG0796 240 EAFARLARRFLGE--PISVEKLDL 261
|
|
| PRK00865 |
PRK00865 |
glutamate racemase; Provisional |
1-260 |
1.70e-129 |
|
glutamate racemase; Provisional
Pssm-ID: 234851 Cd Length: 261 Bit Score: 375.98 E-value: 1.70e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 1 MNKQPIGFIDSGVGGLTVVKEALHQLPAENTIYLGDQARLPYGPRPAEQVQAFTWQMVNFLLTKHIKMLVIACNTATAAA 80
Cdd:PRK00865 3 MMNAPIGVFDSGVGGLTVLREIRRLLPDEHIIYVGDTARFPYGEKSEEEIRERTLEIVEFLLEYGVKMLVIACNTASAVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 81 LPLIKARLKIPVIGvIKPGSRAALKATQTGHIGIIATEGTVKSGAYPKALRAKAPDIRLTSLAAPKFVSLVESNEAHSPI 160
Cdd:PRK00865 83 LPDLRERYDIPVVG-IVPAIKPAAALTRNGRIGVLATPGTVKSAAYRDLIARFAPDCQVESLACPELVPLVEAGILGGPV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 161 AKRVVADTLQPLLHQDIDTLVLGCTHYPILRPIIQNVMGEDVTLIDSGAETVNDVSMLLDYFDLANDGSEVPTHTYYTTG 240
Cdd:PRK00865 162 TLEVLREYLAPLLAAGIDTLVLGCTHYPLLKPEIQQVLGEGVTLIDSGEAIARRVARLLEELNLLASSDENPAHRFFTTG 241
|
250 260
....*....|....*....|
gi 491946784 241 APSMFDELGESWLELKKPMH 260
Cdd:PRK00865 242 DPEAFKRLAQRWLGLLEKVE 261
|
|
| PRK14822 |
PRK14822 |
XTP/dITP diphosphatase; |
283-482 |
6.23e-98 |
|
XTP/dITP diphosphatase;
Pssm-ID: 184835 [Multi-domain] Cd Length: 200 Bit Score: 293.33 E-value: 6.23e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 283 KTIVIASKNPGKIKEFKAMFEPAGVTVKSLADFPTVPTVDETGTTFEANARQKADQYAQDLNLPVLADDSGLMVDALDGQ 362
Cdd:PRK14822 2 KEIVIATKNKGKVREFKEIFEKFDIEVKSLADFPPIPEVEETGTTFEENAILKAEAAAKALNKPVIADDSGLEVDALNGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 363 PGIRSARYAGDGHNDAANNAKLLAALADVPEEARTATFHTTLVLAKPNHPeaDLVVHGDLSGRITAIPRGTDGFGYDPFF 442
Cdd:PRK14822 82 PGVYSARYAGEAKDDAANNEKLLKELGGVPFEKRTARFHCVIAVAFPGGE--TKTVEGTCEGEILEEPRGENGFGYDPLF 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 491946784 443 LVPALDKTLAELTADEKNEISHRGNAMRALEKVWQAWLEE 482
Cdd:PRK14822 160 YVPEKGKTMAELSSEEKNAISHRGKALKKLEAELPEWLKV 199
|
|
| RdgB |
COG0127 |
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide ... |
284-482 |
6.07e-86 |
|
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide transport and metabolism];
Pssm-ID: 439897 [Multi-domain] Cd Length: 191 Bit Score: 261.92 E-value: 6.07e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 284 TIVIASKNPGKIKEFKAMFEPAGVTVKSLADFPtVPTVDETGTTFEANARQKADQYAQDLNLPVLADDSGLMVDALDGQP 363
Cdd:COG0127 1 KLVFATGNAGKLREIRALLAPLGIEVVSLSDLG-LPEPEETGDTFEENALIKARAAAKATGLPALADDSGLEVDALGGAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 364 GIRSARYAGDGHNDAANNAKLLAALADVPEEaRTATFHTTLVLAKPNHPEadLVVHGDLSGRITAIPRGTDGFGYDPFFL 443
Cdd:COG0127 80 GVYSARYAGEGADDEANNEKLLKLLEGVDED-RRARFVCVLALADPDGEP--LVFEGEVEGEIAEEPRGEGGFGYDPIFI 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 491946784 444 VPALDKTLAELTADEKNEISHRGNAMRALekvwQAWLEE 482
Cdd:COG0127 157 PDGYGKTFAELSPEEKNAISHRGRALRKL----AEWLKE 191
|
|
| glut_race |
TIGR00067 |
glutamate racemase; This family consists of glutamate racemase, a protein required for making ... |
6-255 |
1.81e-83 |
|
glutamate racemase; This family consists of glutamate racemase, a protein required for making the UDP-N-acetylmuramoyl-pentapeptide used as a precursor in bacterial peptidoglycan biosynthesis. The most closely related proteins differing in function are aspartate racemases. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 272885 Cd Length: 251 Bit Score: 258.11 E-value: 1.81e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 6 IGFIDSGVGGLTVVKEALHQLPAENTIYLGDQARLPYGPRPAEQVQAFTWQMVNFLLTKH-IKMLVIACNTATAAALPLI 84
Cdd:TIGR00067 1 IGVFDSGVGGLSVLKEIRKQLPKEHYIYVGDTKRFPYGEKSPEFILEYVLELLTFLKERHnIKLLVVACNTASALALEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 85 KARLKIPVIGVIKPGSRAALKATQTGHIGIIATEGTVKSGAYPKALRAKAPDIRLTSLAAPKFVSLVESNEAHSPIAKRV 164
Cdd:TIGR00067 81 QRNFDFPVVGVIEPAIKAAIRLTANGRVLVIATNATIKSNAYHEALKEIANDLLVEMLACPELVPLAEAGLLGEDYALEC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 165 VADTLQPLLHQDIDTLVLGCTHYPILRPIIQNVMGEDVTLIDSGAETVNDVSMLLDYFDLANDGSEVPTHTYYTTGAPSM 244
Cdd:TIGR00067 161 LKRYLRPLLDTLPDTVVLGCTHFPLLKEEIEQYLPEHVRLVDSGVHTARRTAWLLEHKGPLAKSADAPDIEFCMSGTPIQ 240
|
250
....*....|.
gi 491946784 245 FDELGESWLEL 255
Cdd:TIGR00067 241 FQELAKKWLGL 251
|
|
| PRK00120 |
PRK00120 |
dITP/XTP pyrophosphatase; Reviewed |
283-481 |
1.08e-82 |
|
dITP/XTP pyrophosphatase; Reviewed
Pssm-ID: 234648 [Multi-domain] Cd Length: 196 Bit Score: 253.85 E-value: 1.08e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 283 KTIVIASKNPGKIKEFKAMFEPAGVTVKSLADFPtVPTVDETGTTFEANARQKADQYAQDLNLPVLADDSGLMVDALDGQ 362
Cdd:PRK00120 1 MKIVLASHNAGKLRELKALLAPFGIEVVSQGELG-VPEPEETGTTFVENALIKARHAAKATGLPALADDSGLCVDALGGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 363 PGIRSARYAGDGHNDAANNAKLLAALADVPEEARTATFHTTLVLAKPN-HPeadLVVHGDLSGRITAIPRGTDGFGYDPF 441
Cdd:PRK00120 80 PGVYSARYAGEGASDAANNEKLLEELKGVPDEDRRARFVCVLVLVRPDpTP---LVAEGRWEGEILWEPRGENGFGYDPI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 491946784 442 FLVPALDKTLAELTADEKNEISHRGNAMRALEKVWQAWLE 481
Cdd:PRK00120 157 FFPPGYGKTFAELTPEEKNAISHRGKALKLLLEALRELLA 196
|
|
| Ham1p_like |
pfam01725 |
Ham1 family; This family consists of the HAM1 protein and hypothetical archaeal bacterial and ... |
285-472 |
5.25e-80 |
|
Ham1 family; This family consists of the HAM1 protein and hypothetical archaeal bacterial and C. elegans proteins. HAM1 controls 6-N-hydroxylaminopurine (HAP) sensitivity and mutagenesis in S. cerevisiae. The HAM1 protein protects the cell from HAP, either on the level of deoxynucleoside triphosphate or the DNA level by a yet unidentified set of reactions.
Pssm-ID: 460306 [Multi-domain] Cd Length: 186 Bit Score: 246.59 E-value: 5.25e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 285 IVIASKNPGKIKEFKAMFEPaGVTVKSLADFPTVPTVDETGTTFEANARQKAdQYAQDLNLPVLADDSGLMVDALDGQPG 364
Cdd:pfam01725 1 IVFATGNAGKLRELKAILAD-GIEVLSLKDLGELPEIEETGGTFEENALIKA-RAAAKTGLPVLADDSGLEVDALNGFPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 365 IRSARYAGDGHNDAANNAKLLAALaDVPEEARTATFHTTLVLAKPNHPEadLVVHGDLSGRITAIPRGTDGFGYDPFFLV 444
Cdd:pfam01725 79 VYSARFAGEGGDDEANNAKLLEEL-EVPDEDRSARFVCVIALADPGGPE--LVFEGEVEGEIVEEPRGEGGFGYDPIFIP 155
|
170 180
....*....|....*....|....*...
gi 491946784 445 PALDKTLAELTADEKNEISHRGNAMRAL 472
Cdd:pfam01725 156 PEGGKTFAELSPEEKNAISHRGKALRKL 183
|
|
| HAM1 |
cd00515 |
NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ ... |
285-472 |
3.21e-70 |
|
NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ inosine triphosphatase. HAM1 protects the cell against mutagenesis by the base analog 6-N-hydroxylaminopurine (HAP) in E. Coli and S. cerevisiae. A Ham1-related protein from Methanococcus jannaschii is a novel NTPase that has been shown to hydrolyze nonstandard nucleotides such as XTP to XMP and ITP to IMP, but not the standard nucleotides, in the presence of Mg or Mn ions. The enzyme exists as a homodimer. The HAM1 protein may be acting as an NTPase by hydrolyzing the HAP triphosphate.
Pssm-ID: 238285 [Multi-domain] Cd Length: 183 Bit Score: 221.24 E-value: 3.21e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 285 IVIASKNPGKIKEFKAMFEPAGVTVKSLADFPTVPtvdETGTTFEANARQKADQYAQDLNLPVLADDSGLMVDALDGQPG 364
Cdd:cd00515 1 IVFATGNKGKLKEFKEILAPFGIEVVSLKDIIDIE---ETGSTFEENALLKARAAAEALGLPVLADDSGLCVDALNGFPG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 365 IRSARYAGDgHNDAANNAKLLAALADvpEEARTATFHTTLVLAKPNHPEadLVVHGDLSGRITAIPRGTDGFGYDPFFLV 444
Cdd:cd00515 78 VYSARFAGE-HDDAENNEKLLELLEG--DEDRSAYFVCVIALVDPDGEP--LVFEGEVEGKIVTEPRGTGGFGYDPIFIP 152
|
170 180
....*....|....*....|....*...
gi 491946784 445 PALDKTLAELTADEKNEISHRGNAMRAL 472
Cdd:cd00515 153 EGYGKTFAEMSPEEKNAISHRGKALRKL 180
|
|
| PRK02491 |
PRK02491 |
putative deoxyribonucleotide triphosphate pyrophosphatase/unknown domain fusion protein; ... |
271-483 |
4.59e-62 |
|
putative deoxyribonucleotide triphosphate pyrophosphatase/unknown domain fusion protein; Reviewed
Pssm-ID: 179431 [Multi-domain] Cd Length: 328 Bit Score: 205.43 E-value: 4.59e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 271 THFVEPTSEATDKTIVIASKNPGKIKEFKAMFEPAGVTVKSLADFPTVPTVDETGTTFEANARQKADQYAQDLNLPVLAD 350
Cdd:PRK02491 116 ADFFGTSKQGFGDTILIATRNEGKTKEFRKLFGKLGYKVENLNDYPDLPEVAETGMTFEENARLKAETISRLTGKMVLAD 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 351 DSGLMVDALDGQPGIRSARYAGDGHNDAANNAKLLAALADVPE-EARTATFHTTLVLAKPNhpEADLVVHGDLSGRITAI 429
Cdd:PRK02491 196 DSGLKVDALGGLPGVWSARFSGPDATDAENNAKLLHELAMVFDlKDRSAQFHTTLVVAAPN--KDSLVVEADWPGYIATE 273
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491946784 430 PRGTDGFGYDPFFLVPALDKTLAELTADEKNEISHRGNAMRALEKVWQAWLEEN 483
Cdd:PRK02491 274 PKGENGFGYDPLFLVGETGRHAAELTAEEKNQLSHRGQAVKKLMEVFPAWQAKQ 327
|
|
| TIGR00042 |
TIGR00042 |
non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 ... |
284-476 |
6.82e-55 |
|
non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 protects against the mutagenic effects of the base analog 6-N-hydroxylaminopurine, which can be a natural product of monooxygenase activity on adenine. Methanococcus jannaschii MJ0226 and E. coli RdgB are also characterized as pyrophosphatases active against non-standard purines NTPs. E. coli RdgB appears to act by intercepting non-canonical deoxyribonucleotide triphosphates from replication precursor pools. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 272870 [Multi-domain] Cd Length: 184 Bit Score: 181.80 E-value: 6.82e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 284 TIVIASKNPGKIKEFKAMFEPAGVTVKSLADFPTVptvDETGTTFEANARQKADQYAQDLNLPVLADDSGLMVDALDGQP 363
Cdd:TIGR00042 1 KIVFATGNPGKLKEVQSILSDLGDNEIEQLDLGYP---EETGLTFEENALLKAKHAAKILNKPVIAEDSGLFVDALNGFP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 364 GIRSARYAGDGHNDAANNAKLLAaladvPEEARTATFHTTLVLAKPNhpEADLVVHGDLSGRITAIPRGTDGFGYDPFFL 443
Cdd:TIGR00042 78 GIYSARYQGTDIGNLEKILKLLE-----GVENRQAYFVCVIGYCDPN--GEPLVFEGIVKGKITREPRGTYGFGYDPIFI 150
|
170 180 190
....*....|....*....|....*....|...
gi 491946784 444 VPALDKTLAELTADEKNEISHRGNAMRALEKVW 476
Cdd:TIGR00042 151 PPEEGKTFAELTTEEKNKISHRGKAFKKFKKFL 183
|
|
| PRK14823 |
PRK14823 |
putative deoxyribonucleoside-triphosphatase; Provisional |
285-472 |
9.99e-43 |
|
putative deoxyribonucleoside-triphosphatase; Provisional
Pssm-ID: 237823 [Multi-domain] Cd Length: 191 Bit Score: 149.83 E-value: 9.99e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 285 IVIASKNPGKIKEFKAMFePAGVTVKSLADFPTVPTVDETGTTFEANARQKADQYAQDLNLPVLADDSGLMVDALDGQPG 364
Cdd:PRK14823 3 LVFATNNKHKLEEIRSIL-PEKIELLSLSDIGCHEDIPETADTLEGNALLKAEYVYKKYGYDCFADDTGLEVEALNGAPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 365 IRSARYAGDGHNDAANNAKLLAALADVPEeaRTATFHTTLVLakpNHPEADLVVHGDLSGRITAIPRGTDGFGYDPFFLV 444
Cdd:PRK14823 82 VYSARYAGGEHNAEANMRKLLEELEGKDN--RKAQFRTVIAL---ILDGKEHLFEGIIKGEIIKEKRGDSGFGYDPIFVP 156
|
170 180
....*....|....*....|....*...
gi 491946784 445 PALDKTLAELTADEKNEISHRGNAMRAL 472
Cdd:PRK14823 157 EGYDKTFAELGLEIKNQISHRAKAVQKL 184
|
|
| PRK14826 |
PRK14826 |
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional |
276-471 |
5.21e-42 |
|
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
Pssm-ID: 173287 Cd Length: 222 Bit Score: 149.05 E-value: 5.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 276 PTSEATDKTIVIASKNPGKIKEFKAMFEP--AGVTVKSLADFPTVPTVDETGTTFEANARQKADQYAQDL-----NLPVL 348
Cdd:PRK14826 2 PQIATETITIVLATGNRDKVRELRPLLEHisPLFSVRSLADLGVEVDIEETEETLEGNALLKADAIFELLsdrfpFLIAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 349 ADDSGLMVDALDGQPGIRSARYA--GDGHNDAANNAKLLAALADVPEEARTATFHTTLVLaKPNHPEAD------LVVHG 420
Cdd:PRK14826 82 ADDTGLEVDALGGAPGVYSARFApvPEGEKPTYEDNVRHLLSEMEGKTERSARFRTVIAL-KGRLPGKNgafefeETAEG 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491946784 421 DLSGRITAIPRGTDGFGYDPFFLVPALDKTLAELTADEKNEISHRGNAMRA 471
Cdd:PRK14826 161 VVEGSITTEKKGDGGFGYDPIFRVEATGKTFAEMSTEEKNTISHRALAVQK 211
|
|
| PRK14824 |
PRK14824 |
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional |
285-472 |
2.03e-41 |
|
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
Pssm-ID: 237824 [Multi-domain] Cd Length: 201 Bit Score: 146.83 E-value: 2.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 285 IVIASKNPGKIKEFKAMFEPAGVTVKSLadfPTVPTVDETGTTFEANARQKADQYAQDLNLPVLADDSGLMVDALDGQPG 364
Cdd:PRK14824 3 ILLATTNEGKVREIKRLLSDLGIEVLSP---DKKIEVEEDGETFLENAYLKARAYAEFYKIPVLADDSGLEVPALEGYPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 365 IRSAR-----YAGDGHNDAANNAKLLAALADVPE--EARTATFHTTLVLAkpnHPEADLVVHGDLSGRITAIPRGTDGFG 437
Cdd:PRK14824 80 VYSSRfyqieFGGKEEVVESKDEANIRKLLRLLEgkQNRKARFVAFVVLY---FGDWGIWTEGECRGKIAEEPRGSGGFG 156
|
170 180 190
....*....|....*....|....*....|....*
gi 491946784 438 YDPFFLVPALDKTLAELTADEKNEISHRGNAMRAL 472
Cdd:PRK14824 157 YDPVFIPEGYNKTMAELSPEEKNKISHRGKAVRKL 191
|
|
| PRK14821 |
PRK14821 |
XTP/dITP diphosphatase; |
285-484 |
2.64e-29 |
|
XTP/dITP diphosphatase;
Pssm-ID: 184834 [Multi-domain] Cd Length: 184 Bit Score: 113.51 E-value: 2.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 285 IVIASKNPGKIKEFKAMFEPAGVTVKSLADfpTVPTVDETgtTFEANARQKADQYAQDLNLPVLADDSGLMVDALDGQPG 364
Cdd:PRK14821 3 IYFATGNKGKVEEAKIILKPLGIEVEQIKI--EYPEIQAD--TLEEVAAFGAKWVYNKLNRPVIVEDSGLFIEALNGFPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 365 IRSA---RYAGdghNDAANNAKLLaaladvpEEARTATFHTTLVLAKPNHPEadlVVHGDLSGRITAIPRGTDGFGYDPF 441
Cdd:PRK14821 79 PYSAfvyKTLG---NEGILKLLEG-------EENRRAYFKSVIGYCDPGGEK---LFTGIVEGKIANEIRGKGGFGYDPI 145
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 491946784 442 FLVPALDKTLAELTADEKNEISHRGNAMRALEKvwqaWLEENV 484
Cdd:PRK14821 146 FIPEGEEKTFAEMTTEEKNKISHRKRAFDEFKE----WLKENL 184
|
|
| Asp_Glu_race |
pfam01177 |
Asp/Glu/Hydantoin racemase; This family contains aspartate racemase, maleate isomerases EC:5.2. ... |
6-213 |
7.20e-24 |
|
Asp/Glu/Hydantoin racemase; This family contains aspartate racemase, maleate isomerases EC:5.2.1.1, glutamate racemase, hydantoin racemase and arylmalonate decarboxylase EC:4.1.1.76.
Pssm-ID: 426101 Cd Length: 210 Bit Score: 99.26 E-value: 7.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 6 IGFIDSGvGGLTVVKEALHQLPAEN----TIYLGDQARLPYGPRPAEQVQAFTWQMVNFLLT---KHIKMLVIACNTATA 78
Cdd:pfam01177 1 IGGINPN-STASMTRKIVEAARAVLpphvPVILVTSPDGPDRIESPEDGALAAPALLEALRRleaAGADAIVIACFTDHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 79 AaLPLIKARLKIPVIGVIKPGSRAALKatQTGHIGIIATEGTvKSGAYPKALRAKAPDIRLTSLAAPKFVSLVESNEAHS 158
Cdd:pfam01177 80 G-LDALRELTDIPVLGIAEAAALAALA--LGGRFGVLTTLGT-SSPVYERALRAYGLEVRCPGVRAQEGLPVLIVKGGDT 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491946784 159 PIAKRVVADTLQPLLHQDIDTLVLGCTHYPILRPIIQNVMGedVTLIDSGAETVN 213
Cdd:pfam01177 156 EEARALLLEAAKALVEDGADAIILGCTGLPGLAEELEAELG--VPVIDPVDAAVR 208
|
|
| Maf_Ham1 |
cd00985 |
Maf_Ham1. Maf, a nucleotide binding protein, has been implicated in inhibition of septum ... |
285-426 |
1.28e-20 |
|
Maf_Ham1. Maf, a nucleotide binding protein, has been implicated in inhibition of septum formation in eukaryotes, bacteria and archaea. A Ham1-related protein from Methanococcus jannaschii is a novel NTPase that has been shown to hydrolyze nonstandard nucleotides, such as hypoxanthine/xanthine NTP, but not standard nucleotides.
Pssm-ID: 238485 Cd Length: 131 Bit Score: 87.56 E-value: 1.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 285 IVIASKNPGKIKEFKAMFepaGVTVKSL-ADFPTVPTVDETGTTFEANARQKADQYAQDLN-LPVLADDSGLmvdALDGQ 362
Cdd:cd00985 1 LILASGSPRRLEELKQIG---GIEFEVLpSDIDETGLKGEPEDTVEELALLKARAVAERLPdAPVIADDTGL---VVDGR 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491946784 363 PGIRSARYAGdghndaannakllAALADVPEEARTATFHTTLVLAKPNHPEadLVVHGDLSGRI 426
Cdd:cd00985 75 PGGKPARFAE-------------ALEMLRGLSGRTAEFVTAVALVDPDGKI--ITFEGETEGKI 123
|
|
| PRK14825 |
PRK14825 |
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional |
283-474 |
2.31e-20 |
|
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
Pssm-ID: 173286 Cd Length: 199 Bit Score: 88.84 E-value: 2.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 283 KTIVIASKNPGKIKEFKAMFEPAGVTVKSLADFptvpTVDETGTTFEANARQKADQYAQDLN--LPVLADDSGLMVDALD 360
Cdd:PRK14825 2 KTLFFATTNINKINEVKQILDIPNIKIEIPQNF----DIKETGKTFKENSLLKAKALFEILNnkQPVFSEDSGLCIEALN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 361 GQPGIRSARYAGDGHNDAANNAKLLAALADV--PEEARTATFHTtlvlakpnhpeadLVVHGDLSGRIT---AIPRGT-- 433
Cdd:PRK14825 78 LEPGIYSKRYDQYKLGKKLSTNEKNHLIIDLmkNEKNRTAYFIC-------------NISYISKDGTILnfeGIIKGTia 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491946784 434 --------DGFGYDPFFLVpALDKTLAELTADEKNEISHRGNAMRALEK 474
Cdd:PRK14825 145 lsiddykkNGFGYDPIFLT-KNNKRLSELTLEEKNKISHRGIAFDKFKK 192
|
|
| RacX |
COG1794 |
Amino acid racemase YgeA [Cell wall/membrane/envelope biogenesis]; |
69-207 |
8.80e-10 |
|
Amino acid racemase YgeA [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441399 Cd Length: 228 Bit Score: 58.60 E-value: 8.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946784 69 LVIACNTATAAAlPLIKARLKIPVIGVIKPgSRAALKATQTGHIGIIATEGTVKSGAYPKALRAKAPDIRLTSLAAPKFV 148
Cdd:COG1794 80 IVIPCNTAHYVA-DEIQAAVSIPLLHIADA-TAEAIRARGIKRVGLLGTRGTMESGFYQDRLEAAGIEVIVPDEEDQELV 157
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491946784 149 S------LVESNEahSPIAKRVVADTLQPLLHQDIDTLVLGCTHYPILRPIIQNvmgeDVTLIDS 207
Cdd:COG1794 158 HriiydeLKAGII--TEESRAALLEIIERLAARGAEAVILGCTELPLLLDQEDS----PVPLIDT 216
|
|
| |
