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Conserved domains on  [gi|1308963989|gb|PKO73957|]
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hypothetical protein CVU23_00025 [Betaproteobacteria bacterium HGW-Betaproteobacteria-17]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK08223 super family cl30837
hypothetical protein; Validated
 2-282 9.81e-127

hypothetical protein; Validated


The actual alignment was detected with superfamily member PRK08223:

Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 362.08  E-value: 9.81e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308963989   2 FDYDEAFSRNLGWLTPQEQQRLRGARVAVAGMGGVGGVHVQGLARLGVGALNLTDFDSFEVANFNRQAGAAMSTLGQPKV 81
Cdd:PRK08223    4 FDYDEAFCRNLGWITPTEQQRLRNSRVAIAGLGGVGGIHLLTLARLGIGKFTIADFDVFELRNFNRQAGAMMSTLGRPKA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308963989  82 EVMRGFALDVNPETDVRVFPNGLDEANLSDYLDGVDLLIDAIDFFANSLRPALYRAARERGIPVVCAAPLGAGASLICFK 161
Cdd:PRK08223   84 EVLAEMVRDINPELEIRAFPEGIGKENADAFLDGVDVYVDGLDFFEFDARRLVFAACQQRGIPALTAAPLGMGTALLVFD 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308963989 162 PDGMRFDDYFGFA-GCDDLTMAVRFMVGMSPRLPQRHYLAYPEIVDFVKRRVPSLGMACQFAAGMVVTASMKLLLQRGGV 240
Cdd:PRK08223  164 PGGMSFDDYFDLSdGMNEVEKAVRFLAGLAPSMLHRGYLADPSRVDLENRTGPSTGLACQLCAGVVATEVLKILLGRGRV 243

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1308963989 241 KAAPHTEQYDAYLGRHYRSWRPGGYRNPLQRLAEGIVVSRLK 282
Cdd:PRK08223  244 YAAPWFHQFDAYRSRYVRTWRPGGNRHPLQRLKRRLLRRRLN 285
 
Name Accession Description Interval E-value
PRK08223 PRK08223
hypothetical protein; Validated
 2-282 9.81e-127

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 362.08  E-value: 9.81e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308963989   2 FDYDEAFSRNLGWLTPQEQQRLRGARVAVAGMGGVGGVHVQGLARLGVGALNLTDFDSFEVANFNRQAGAAMSTLGQPKV 81
Cdd:PRK08223    4 FDYDEAFCRNLGWITPTEQQRLRNSRVAIAGLGGVGGIHLLTLARLGIGKFTIADFDVFELRNFNRQAGAMMSTLGRPKA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308963989  82 EVMRGFALDVNPETDVRVFPNGLDEANLSDYLDGVDLLIDAIDFFANSLRPALYRAARERGIPVVCAAPLGAGASLICFK 161
Cdd:PRK08223   84 EVLAEMVRDINPELEIRAFPEGIGKENADAFLDGVDVYVDGLDFFEFDARRLVFAACQQRGIPALTAAPLGMGTALLVFD 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308963989 162 PDGMRFDDYFGFA-GCDDLTMAVRFMVGMSPRLPQRHYLAYPEIVDFVKRRVPSLGMACQFAAGMVVTASMKLLLQRGGV 240
Cdd:PRK08223  164 PGGMSFDDYFDLSdGMNEVEKAVRFLAGLAPSMLHRGYLADPSRVDLENRTGPSTGLACQLCAGVVATEVLKILLGRGRV 243

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1308963989 241 KAAPHTEQYDAYLGRHYRSWRPGGYRNPLQRLAEGIVVSRLK 282
Cdd:PRK08223  244 YAAPWFHQFDAYRSRYVRTWRPGGNRHPLQRLKRRLLRRRLN 285
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 3-154 3.96e-33

tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and biogenesis]; tRNA A37 threonylcarbamoyladenosine dehydratase is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440792  Cd Length: 247  Bit Score: 121.34  E-value: 3.96e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308963989   3 DYDEAFSRNLGWLTPQEQQRLRGARVAVAgmggvggvhvqG-----------LARLGVGALNLTDFDSFEVANFNRQAGA 71
Cdd:COG1179     2 DMERRFSRTERLYGEEGLERLANAHVAVV-----------GlggvgswaaeaLARSGVGRLTLVDLDDVCESNINRQLHA 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308963989  72 AMSTLGQPKVEVMRGFALDVNPETDVRVFPNGLDEANLSDYLD-GVDLLIDAIDffanSLRP--ALYRAARERGIPVVCA 148
Cdd:COG1179    71 LDSTVGRPKVEVMAERIRDINPDCEVTAIDEFVTPENADELLSeDYDYVIDAID----SVSAkaALIAWCRRRGIPIISS 146


                  ....*.
gi 1308963989 149 apLGAG 154
Cdd:COG1179   147 --MGAG 150
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 33-168 9.81e-27

Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes classical ubiquitin-activating enzymes E1, ubiquitin-like (ubl) activating enzymes and other mechanistic homologes, like MoeB, Thif1 and others. The common reaction mechanism catalyzed by MoeB, ThiF and the E1 enzymes begins with a nucleophilic attack of the C-terminal carboxylate of MoaD, ThiS and ubiquitin, respectively, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of MoaD and ThiS.


Pssm-ID: 238760 [Multi-domain]  Cd Length: 143  Bit Score: 101.58  E-value: 9.81e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308963989  33 MGGVGGVHVQGLARLGVGALNLTDFDSFEVANFNRQAGAAMSTLGQPKVEVMRGFALDVNPETDVRVFPNGLDEANLSDY 112
Cdd:cd01483     7 LGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPEGISEDNLDDF 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1308963989 113 LDGVDLLIDAIDFFAnsLRPALYRAARERGIPVVCAAPLGagaslicFKPDGMRFD 168
Cdd:cd01483    87 LDGVDLVIDAIDNIA--VRRALNRACKELGIPVIDAGGLG-------LGGDIQVID 133
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 20-255 4.35e-24

ThiF family; This domain is found in ubiquitin activating E1 family and members of the bacterial ThiF/MoeB/HesA family. It is repeated in Ubiquitin-activating enzyme E1.


Pssm-ID: 459987 [Multi-domain]  Cd Length: 238  Bit Score: 97.33  E-value: 4.35e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308963989  20 QQRLRGARVAVAGMGGVGGVHVQGLARLGVGALNLTDFDSFEVANFNRQAGAAMSTLGQPKVEVMRGFALDVNPETDVRV 99
Cdd:pfam00899  15 QEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAAERLREINPDVEVEA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308963989 100 FPNGLDEANLSDYLDGVDLLIDAIDFFAnsLRPALYRAARERGIPVVCAAPLGA-GASLICFKPDGMRFDDYFGfagcdd 178
Cdd:pfam00899  95 YTERLTPENAEELIKSFDIVVDATDNFA--ARYLVNDACVKLGKPLIEAGVLGFkGQVTVVIPGKTPCYRCLFP------ 166

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1308963989 179 ltmavrfmVGMSPRLPQRhylaypeivdFVKRRVpsLGMACQFAAGMVVTASMKLLLQRGGVKAAPHTEQYDAYLGR 255
Cdd:pfam00899 167 --------EDPPPKLVPS----------CTVAGV--LGPTTAVVAGLQALEALKLLLGKGEPNLAGRLLQFDALTMT 223
adenyl_thiF TIGR02356
thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily; Members of the HesA/MoeB ...
 20-164 9.22e-17

thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily; Members of the HesA/MoeB/ThiF family of proteins (pfam00899) include a number of members encoded in the midst of thiamine biosynthetic operons. This mix of known and putative ThiF proteins shows a deep split in phylogenetic trees, with the Escherichia. coli ThiF and the E. coli MoeB proteins seemingly more closely related than E. coli ThiF and Campylobacter (for example) ThiF. This model represents the more widely distributed clade of ThiF proteins such found in E. coli. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 274094  Cd Length: 202  Bit Score: 76.63  E-value: 9.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308963989  20 QQRLRGARVAVAGMGGVGGVHVQGLARLGVGALNLTDFDSFEVANFNRQAGAAMSTLGQPKVEVMRGFALDVNPETDVRV 99
Cdd:TIGR02356  16 QQRLLNSHVLIIGAGGLGSPAALYLAGAGVGTIVIVDDDHVDLSNLQRQILFTEEDVGRPKVEVAAQRLRELNSDIQVTA 95

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1308963989 100 FPNGLDEANLSDYLDGVDLLIDAIDFFAnsLRPALYRAARERGIPVVCAAPLGAGASLICFKPDG 164
Cdd:TIGR02356  96 LKERVTAENLELLINNVDLVLDCTDNFA--TRYLINDACVALGTPLISAAVVGFGGQLMVFDPGG 158
 
Name Accession Description Interval E-value
PRK08223 PRK08223
hypothetical protein; Validated
 2-282 9.81e-127

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 362.08  E-value: 9.81e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308963989   2 FDYDEAFSRNLGWLTPQEQQRLRGARVAVAGMGGVGGVHVQGLARLGVGALNLTDFDSFEVANFNRQAGAAMSTLGQPKV 81
Cdd:PRK08223    4 FDYDEAFCRNLGWITPTEQQRLRNSRVAIAGLGGVGGIHLLTLARLGIGKFTIADFDVFELRNFNRQAGAMMSTLGRPKA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308963989  82 EVMRGFALDVNPETDVRVFPNGLDEANLSDYLDGVDLLIDAIDFFANSLRPALYRAARERGIPVVCAAPLGAGASLICFK 161
Cdd:PRK08223   84 EVLAEMVRDINPELEIRAFPEGIGKENADAFLDGVDVYVDGLDFFEFDARRLVFAACQQRGIPALTAAPLGMGTALLVFD 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308963989 162 PDGMRFDDYFGFA-GCDDLTMAVRFMVGMSPRLPQRHYLAYPEIVDFVKRRVPSLGMACQFAAGMVVTASMKLLLQRGGV 240
Cdd:PRK08223  164 PGGMSFDDYFDLSdGMNEVEKAVRFLAGLAPSMLHRGYLADPSRVDLENRTGPSTGLACQLCAGVVATEVLKILLGRGRV 243

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1308963989 241 KAAPHTEQYDAYLGRHYRSWRPGGYRNPLQRLAEGIVVSRLK 282
Cdd:PRK08223  244 YAAPWFHQFDAYRSRYVRTWRPGGNRHPLQRLKRRLLRRRLN 285
PRK14851 PRK14851
hypothetical protein; Provisional
 4-272 4.28e-67

hypothetical protein; Provisional


Pssm-ID: 184853 [Multi-domain]  Cd Length: 679  Bit Score: 220.89  E-value: 4.28e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308963989   4 YDEAFSRNLGWLTPQEQQRLRGARVAVAGMGGVGGVHVQGLARLGVGALNLTDFDSFEVANFNRQAGAAMSTLGQPKVEV 83
Cdd:PRK14851   22 REAAFSRNIGLFTPGEQERLAEAKVAIPGMGGVGGVHLITMVRTGIGRFHIADFDQFEPVNVNRQFGARVPSFGRPKLAV 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308963989  84 MRGFALDVNPETDVRVFPNGLDEANLSDYLDGVDLLIDAIDFFANSLRPALYRAARERGIPVVCAAPLGAGASLICFKPD 163
Cdd:PRK14851  102 MKEQALSINPFLEITPFPAGINADNMDAFLDGVDVVLDGLDFFQFEIRRTLFNMAREKGIPVITAGPLGYSSAMLVFTPQ 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308963989 164 GMRFDDYFGFAG-CDDLTMAVRFMVGMSPRLPQRHYLAYPEiVDFVKRRVPSLGMACQFAAGMVVTASMKLLLQRGGVKA 242
Cdd:PRK14851  182 GMGFDDYFNIGGkMPEEQKYLRFAMGLAPRPTHIKYMDLSK-VDLKGGKGPSLNIACQLCSGMAGTEAVRIILGKGGLRP 260

                         250       260       270
                  ....*....|....*....|....*....|
gi 1308963989 243 APHTEQYDAYLGRHYRSWRPGGYRNPLQRL 272
Cdd:PRK14851  261 VPCYLQFDPFLQKLRKGRLSRGNKTPSQRA 290
PRK14852 PRK14852
hypothetical protein; Provisional
 5-276 2.17e-58

hypothetical protein; Provisional


Pssm-ID: 184854 [Multi-domain]  Cd Length: 989  Bit Score: 200.69  E-value: 2.17e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308963989   5 DEAFSRNLGWLTPQEQQRLRGARVAVAGMGGVGGVHVQGLARLGVGALNLTDFDSFEVANFNRQAGAAMSTLGQPKVEVM 84
Cdd:PRK14852  312 DIAFSRNLGLVDYAGQRRLLRSRVAIAGLGGVGGIHLMTLARTGIGNFNLADFDAYSPVNLNRQYGASIASFGRGKLDVM 391

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308963989  85 RGFALDVNPETDVRVFPNGLDEANLSDYLDGVDLLIDAIDFFANSLRPALYRAARERGIPVVCAAPLGAGASLICFKPDG 164
Cdd:PRK14852  392 TERALSVNPFLDIRSFPEGVAAETIDAFLKDVDLLVDGIDFFALDIRRRLFNRALELGIPVITAGPLGYSCALLVFMPGG 471

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308963989 165 MRFDDYFGFagcDDLTMA----VRFMVGMSPRLPQRHYLAYpEIVDFVKRRVPSLGMACQFAAGMVVTASMKLLLQRGGV 240
Cdd:PRK14852  472 MNFDSYFGI---DDDTPPmegyLRFGMGLAPRPAHLGYMDR-RFVSLHDRRGPSLDIACHLCAGMAATEAVRILLHRRGI 547

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1308963989 241 KAAPHTEQYDAYLGRHYRSWRPGGYRNPLQRLAEGI 276
Cdd:PRK14852  548 RPVPYFRQFDPLTGRHVRGRLRKGLRSPLQRLKLAI 583
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 3-154 3.96e-33

tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and biogenesis]; tRNA A37 threonylcarbamoyladenosine dehydratase is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440792  Cd Length: 247  Bit Score: 121.34  E-value: 3.96e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308963989   3 DYDEAFSRNLGWLTPQEQQRLRGARVAVAgmggvggvhvqG-----------LARLGVGALNLTDFDSFEVANFNRQAGA 71
Cdd:COG1179     2 DMERRFSRTERLYGEEGLERLANAHVAVV-----------GlggvgswaaeaLARSGVGRLTLVDLDDVCESNINRQLHA 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308963989  72 AMSTLGQPKVEVMRGFALDVNPETDVRVFPNGLDEANLSDYLD-GVDLLIDAIDffanSLRP--ALYRAARERGIPVVCA 148
Cdd:COG1179    71 LDSTVGRPKVEVMAERIRDINPDCEVTAIDEFVTPENADELLSeDYDYVIDAID----SVSAkaALIAWCRRRGIPIISS 146


                  ....*.
gi 1308963989 149 apLGAG 154
Cdd:COG1179   147 --MGAG 150
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 6-238 1.99e-29

Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; Molybdopterin or thiamine biosynthesis adenylyltransferase is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440244 [Multi-domain]  Cd Length: 244  Bit Score: 111.76  E-value: 1.99e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308963989   6 EAFSRNLG--WLTPQEQQRLRGARVAVAGMggvggvhvqG---------LARLGVGALNLTDFDSFEVANFNRQAGAAMS 74
Cdd:COG0476     6 ERYSRQILlpEIGEEGQEKLKAARVLVVGA---------GglgspvalyLAAAGVGTLTLVDDDVVELSNLQRQILYTEA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308963989  75 TLGQPKVEVMRGFALDVNPETDVRVFPNGLDEANLSDYLDGVDLLIDAIDFFAnsLRPALYRAARERGIPVVCAAPLGAG 154
Cdd:COG0476    77 DVGRPKVEAAAERLRALNPDVEVEAIPERLTEENALELLAGADLVLDCTDNFA--TRYLLNDACVKLGIPLVSGAVIGFE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308963989 155 ASLICFKP-DGMRFDDYFgfagcddltmavrfmvgmsPRLPQRhylaypeivDFVKRRVPSLGMACQFAAGMVVTASMKL 233
Cdd:COG0476   155 GQVTVFIPgDTPCYRCLF-------------------PEPPEP---------GPSCAEAGVLGPLVGVIGSLQATEAIKL 206


                  ....*
gi 1308963989 234 LLQRG 238
Cdd:COG0476   207 LTGIG 211
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 33-168 9.81e-27

Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes classical ubiquitin-activating enzymes E1, ubiquitin-like (ubl) activating enzymes and other mechanistic homologes, like MoeB, Thif1 and others. The common reaction mechanism catalyzed by MoeB, ThiF and the E1 enzymes begins with a nucleophilic attack of the C-terminal carboxylate of MoaD, ThiS and ubiquitin, respectively, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of MoaD and ThiS.


Pssm-ID: 238760 [Multi-domain]  Cd Length: 143  Bit Score: 101.58  E-value: 9.81e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308963989  33 MGGVGGVHVQGLARLGVGALNLTDFDSFEVANFNRQAGAAMSTLGQPKVEVMRGFALDVNPETDVRVFPNGLDEANLSDY 112
Cdd:cd01483     7 LGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPEGISEDNLDDF 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1308963989 113 LDGVDLLIDAIDFFAnsLRPALYRAARERGIPVVCAAPLGagaslicFKPDGMRFD 168
Cdd:cd01483    87 LDGVDLVIDAIDNIA--VRRALNRACKELGIPVIDAGGLG-------LGGDIQVID 133
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 20-255 4.35e-24

ThiF family; This domain is found in ubiquitin activating E1 family and members of the bacterial ThiF/MoeB/HesA family. It is repeated in Ubiquitin-activating enzyme E1.


Pssm-ID: 459987 [Multi-domain]  Cd Length: 238  Bit Score: 97.33  E-value: 4.35e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308963989  20 QQRLRGARVAVAGMGGVGGVHVQGLARLGVGALNLTDFDSFEVANFNRQAGAAMSTLGQPKVEVMRGFALDVNPETDVRV 99
Cdd:pfam00899  15 QEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAAERLREINPDVEVEA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308963989 100 FPNGLDEANLSDYLDGVDLLIDAIDFFAnsLRPALYRAARERGIPVVCAAPLGA-GASLICFKPDGMRFDDYFGfagcdd 178
Cdd:pfam00899  95 YTERLTPENAEELIKSFDIVVDATDNFA--ARYLVNDACVKLGKPLIEAGVLGFkGQVTVVIPGKTPCYRCLFP------ 166

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1308963989 179 ltmavrfmVGMSPRLPQRhylaypeivdFVKRRVpsLGMACQFAAGMVVTASMKLLLQRGGVKAAPHTEQYDAYLGR 255
Cdd:pfam00899 167 --------EDPPPKLVPS----------CTVAGV--LGPTTAVVAGLQALEALKLLLGKGEPNLAGRLLQFDALTMT 223
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 21-157 1.04e-20

Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli hypothetical protein ygdL. The common reaction mechanism catalyzed by E1-like enzymes begins with a nucleophilic attack of the C-terminal carboxylate of the ubiquitin-like substrate, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of the substrate. The exact function of this family is unknown.


Pssm-ID: 238384 [Multi-domain]  Cd Length: 231  Bit Score: 88.05  E-value: 1.04e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308963989  21 QRLRGARVAVAGMGGVGGVHVQGLARLGVGALNLTDFDSFEVANFNRQAGAAMSTLGQPKVEVMRGFALDVNPETDVRVF 100
Cdd:cd00755     7 EKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAERIRDINPECEVDAV 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308963989 101 PNGLDEANLSDYLDG-VDLLIDAIDffanSLRP--ALYRAARERGIPVVCAapLGAGASL 157
Cdd:cd00755    87 EEFLTPDNSEDLLGGdPDFVVDAID----SIRAkvALIAYCRKRKIPVISS--MGAGGKL 140
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 8-152 1.50e-19

ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis family. The common reaction mechanism catalyzed by MoeB and ThiF, like other E1 enzymes, begins with a nucleophilic attack of the C-terminal carboxylate of MoaD and ThiS, respectively, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of MoaD and ThiS. MoeB, as the MPT synthase (MoaE/MoaD complex) sulfurase, is involved in the biosynthesis of the molybdenum cofactor, a derivative of the tricyclic pterin, molybdopterin (MPT). ThiF catalyzes the adenylation of ThiS, as part of the biosynthesis pathway of thiamin pyrophosphate (vitamin B1).


Pssm-ID: 238386 [Multi-domain]  Cd Length: 228  Bit Score: 84.84  E-value: 1.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308963989   8 FSRN--LGWLTPQEQQRLRGARVAVAGMGGVGGVHVQGLARLGVGALNLTDFDSFEVANFNRQAGAAMSTLGQPKVEVMR 85
Cdd:cd00757     2 YSRQilLPEIGEEGQEKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADVGQPKAEAAA 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1308963989  86 GFALDVNPETDVRVFPNGLDEANLSDYLDGVDLLIDAIDFFAnsLRPALYRAARERGIPVVCAAPLG 152
Cdd:cd00757    82 ERLRAINPDVEIEAYNERLDAENAEELIAGYDLVLDCTDNFA--TRYLINDACVKLGKPLVSGAVLG 146
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 42-157 3.87e-17

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 79.08  E-value: 3.87e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308963989  42 QGLARLGVGALNLTDFDSFEVANFNRQAGAAMSTLGQPKVEVMRGFALDVNPETDVRVFPNGLDEANLSDYLD-GVDLLI 120
Cdd:PRK15116   47 EALARTGIGAITLIDMDDVCVTNTNRQIHALRDNVGLAKAEVMAERIRQINPECRVTVVDDFITPDNVAEYMSaGFSYVI 126

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1308963989 121 DAIDffanSLRP--ALYRAARERGIPVVCAAplGAGASL 157
Cdd:PRK15116  127 DAID----SVRPkaALIAYCRRNKIPLVTTG--GAGGQI 159
adenyl_thiF TIGR02356
thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily; Members of the HesA/MoeB ...
 20-164 9.22e-17

thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily; Members of the HesA/MoeB/ThiF family of proteins (pfam00899) include a number of members encoded in the midst of thiamine biosynthetic operons. This mix of known and putative ThiF proteins shows a deep split in phylogenetic trees, with the Escherichia. coli ThiF and the E. coli MoeB proteins seemingly more closely related than E. coli ThiF and Campylobacter (for example) ThiF. This model represents the more widely distributed clade of ThiF proteins such found in E. coli. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 274094  Cd Length: 202  Bit Score: 76.63  E-value: 9.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308963989  20 QQRLRGARVAVAGMGGVGGVHVQGLARLGVGALNLTDFDSFEVANFNRQAGAAMSTLGQPKVEVMRGFALDVNPETDVRV 99
Cdd:TIGR02356  16 QQRLLNSHVLIIGAGGLGSPAALYLAGAGVGTIVIVDDDHVDLSNLQRQILFTEEDVGRPKVEVAAQRLRELNSDIQVTA 95

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1308963989 100 FPNGLDEANLSDYLDGVDLLIDAIDFFAnsLRPALYRAARERGIPVVCAAPLGAGASLICFKPDG 164
Cdd:TIGR02356  96 LKERVTAENLELLINNVDLVLDCTDNFA--TRYLINDACVALGTPLISAAVVGFGGQLMVFDPGG 158
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 12-171 1.83e-15

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 75.29  E-value: 1.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308963989  12 LGWLTPQEQQRLRGARVAVAGMGGVGGVHVQGLARLGVGALNLTDFDSFEVANFNRQAGAAMSTLGQPKVEVMRGFALDV 91
Cdd:PRK05597   15 LGEIGQQGQQSLFDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHSTAGVGQPKAESAREAMLAL 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308963989  92 NPETDVRVFPNGLDEANLSDYLDGVDLLIDAIDFFANslRPALYRAARERGIPVVCAAPLGAGASLICFKPD-GMRFDDY 170
Cdd:PRK05597   95 NPDVKVTVSVRRLTWSNALDELRDADVILDGSDNFDT--RHLASWAAARLGIPHVWASILGFDAQLSVFHAGhGPIYEDL 172


                  .
gi 1308963989 171 F 171
Cdd:PRK05597  173 F 173
PRK07877 PRK07877
Rv1355c family protein;
9-148 5.04e-15

Rv1355c family protein;


Pssm-ID: 236122 [Multi-domain]  Cd Length: 722  Bit Score: 75.03  E-value: 5.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308963989   9 SRNLGWLTPQEQQRLRGARVavagmggvggvhvqGLARLGVG--------------ALNLTDFDSFEVANFNRqAGAAMS 74
Cdd:PRK07877   91 DRNRNKITAEEQERLGRLRI--------------GVVGLSVGhaiahtlaaeglcgELRLADFDTLELSNLNR-VPAGVF 155

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1308963989  75 TLGQPKVEVMRGFALDVNPETDVRVFPNGLDEANLSDYLDGVDLLIDAIDFFAnsLRPALYRAARERGIPVVCA 148
Cdd:PRK07877  156 DLGVNKAVVAARRIAELDPYLPVEVFTDGLTEDNVDAFLDGLDVVVEECDSLD--VKVLLREAARARRIPVLMA 227
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 44-192 3.88e-14

E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. The common reaction mechanism catalyzed by E1-like enzymes begins with a nucleophilic attack of the C-terminal carboxylate of the ubiquitin-like substrate, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of the substrate. The exact function of this family is unknown.


Pssm-ID: 238764 [Multi-domain]  Cd Length: 174  Bit Score: 68.95  E-value: 3.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308963989  44 LARLGVGALNLTDFDSFEVANFNRQAgAAMSTLGQPKVEVMRGFALDVNPETDVRVFPNGLDEANLSDYLDGVDLLIDAI 123
Cdd:cd01487    18 LARSGVGNLKLVDFDVVEPSNLNRQQ-YFLSQIGEPKVEALKENLREINPFVKIEAINIKIDENNLEGLFGDCDIVVEAF 96

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1308963989 124 D------FFANSLRpalyraaRERGIPVVCAAPLGAGAS--LICFKPDGMRfddyfgFAGCDDLTMAVRFMVG-MSPR 192
Cdd:cd01487    97 DnaetkaMLAESLL-------GNKNKPVVCASGMAGFGDsnNIKTKKISDN------FYICGDLVNEAKEGLGlMAPR 161
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 42-149 8.74e-13

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 66.41  E-value: 8.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308963989  42 QGLARLGVGALNLTDFDSFEVANFNRQAGAAMSTLGQPKVEVMRGFALDVNPETDVRVFPNGLDEANLSDYLDGVDLLID 121
Cdd:PRK05690   49 QYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDATIGQPKVESARAALARINPHIAIETINARLDDDELAALIAGHDLVLD 128

                          90       100
                  ....*....|....*....|....*...
gi 1308963989 122 AIDFFAnsLRPALYRAARERGIPVVCAA 149
Cdd:PRK05690  129 CTDNVA--TRNQLNRACFAAKKPLVSGA 154
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
44-192 1.50e-12

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 65.26  E-value: 1.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308963989  44 LARLGVGALNLTDFDSFEVANFNRQAgAAMSTLGQPKVEVMRGFALDVNPETDVRVFPNGLDEANLSDYLDGVDLLIDAI 123
Cdd:PRK08644   47 LARSGVGNLKLVDFDVVEPSNLNRQQ-YFISQIGMPKVEALKENLLEINPFVEIEAHNEKIDEDNIEELFKDCDIVVEAF 125

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1308963989 124 DffanslRPA----LYRAARER-GIPVVCAAPL-GAGAS-LICFKPDGMRFddYFgfagCDDLTMAVRFMVG-MSPR 192
Cdd:PRK08644  126 D------NAEtkamLVETVLEHpGKKLVAASGMaGYGDSnSIKTRRIGKNF--YI----VGDFVTEAKPGNPlMAPR 190
thiF_fam2 TIGR02354
thiamine biosynthesis protein ThiF, family 2; Members of the HesA/MoeB/ThiF family of proteins ...
 16-124 3.13e-12

thiamine biosynthesis protein ThiF, family 2; Members of the HesA/MoeB/ThiF family of proteins (pfam00899) include a number of members encoded in the midst of thiamine biosynthetic operons. This mix of known and putative ThiF proteins shows a deep split in phylogenetic trees, with one the E. coli ThiF and the E. coli MoeB proteins seemingly more closely related than E. coli ThiF and Campylobacter (for example) ThiF. This model represents the divergent clade of putative ThiF proteins such found in Campylobacter. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 162819  Cd Length: 200  Bit Score: 64.12  E-value: 3.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308963989  16 TPQEQQRLRGARVAVAGMGGVGGVHVQGLARLGVGALNLTDFDSFEVANFNRQAGAAmSTLGQPKVEVMRGFALDVNPET 95
Cdd:TIGR02354  12 TPKIVQKLEQATVAICGLGGLGSNVAINLARAGIGKLILVDFDVVEPSNLNRQQYKA-SQVGEPKTEALKENISEINPYT 90

                          90       100
                  ....*....|....*....|....*....
gi 1308963989  96 DVRVFPNGLDEANLSDYLDGVDLLIDAID 124
Cdd:TIGR02354  91 EIEAYDEKITEENIDKFFKDADIVCEAFD 119
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
44-166 1.11e-11

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 64.26  E-value: 1.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308963989  44 LARLGVGALNLTDFDSFEVANFNRQAGAAMSTLGQPKVEVMRGFALDVNPETDVRVFPNGLDEANLSDYLDGVDLLIDAI 123
Cdd:PRK08762  154 LAAAGVGTLGIVDHDVVDRSNLQRQILHTEDRVGQPKVDSAAQRLAALNPDVQVEAVQERVTSDNVEALLQDVDVVVDGA 233

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1308963989 124 DFFAnsLRPALYRAARERGIPVVCAAPLGAGASLICFKPDGMR 166
Cdd:PRK08762  234 DNFP--TRYLLNDACVKLGKPLVYGAVFRFEGQVSVFDAGRQR 274
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 17-151 1.54e-10

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 61.05  E-value: 1.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308963989  17 PQEQQRLRGARVAVAGMGGVGGVHVQGLARLGVGALNLTDFDSFEVANFNRQAGAAMSTLGQPKVEVMRGFALDVNPETD 96
Cdd:PRK05600   33 IEQQERLHNARVLVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRQILFGASDVGRPKVEVAAERLKEIQPDIR 112

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1308963989  97 VRVFPNGLDEANLSDYLDGVDLLIDAIDFFANSLRPAlyRAARERGIPVVCAAPL 151
Cdd:PRK05600  113 VNALRERLTAENAVELLNGVDLVLDGSDSFATKFLVA--DAAEITGTPLVWGTVL 165
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 44-127 3.00e-09

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 57.03  E-value: 3.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308963989  44 LARLGVGALNLTDFDSFEVANFNRQAGAAMSTLGQPKVEVMRGFALDVNPETDVRVFPNGLDEANLSDYLDGVDLLIDAI 123
Cdd:PRK07878   61 LAAAGVGTLGIVEFDVVDESNLQRQVIHGQSDVGRSKAQSARDSIVEINPLVNVRLHEFRLDPSNAVELFSQYDLILDGT 140


                  ....
gi 1308963989 124 DFFA 127
Cdd:PRK07878  141 DNFA 144
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
44-126 1.30e-08

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 55.13  E-value: 1.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308963989  44 LARLGVGALNLTDFDSFEVANFNRQAGAAMSTLGQPKVEVMRGFALDVNPETDVRVFPNGLDEANLSDYLDGVDLLIDAI 123
Cdd:PRK07411   57 LAAAGIGRIGIVDFDVVDSSNLQRQVIHGTSWVGKPKIESAKNRILEINPYCQVDLYETRLSSENALDILAPYDVVVDGT 136


                  ...
gi 1308963989 124 DFF 126
Cdd:PRK07411  137 DNF 139
PRK08328 PRK08328
hypothetical protein; Provisional
 6-149 1.35e-06

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 48.25  E-value: 1.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308963989   6 EAFSRNLGWLTPQEQQRLRGARVAVAGMGGVGGVHVQGLARLGVGALNLTDFDSFEVANFNRQAGAAMSTLGQ-PKVEVM 84
Cdd:PRK08328    8 ERYDRQIMIFGVEGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRQILHWEEDLGKnPKPLSA 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1308963989  85 RGFALDVNPETDVRVFPNGLDEANLSDYLDGVDLLIDAIDFFANslRPALYRAARERGIPVVCAA 149
Cdd:PRK08328   88 KWKLERFNSDIKIETFVGRLSEENIDEVLKGVDVIVDCLDNFET--RYLLDDYAHKKGIPLVHGA 150
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 44-124 8.10e-05

Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present universally in eukaryotic cells, is part of cascade to attach ubiquitin (Ub) covalently to substrate proteins. This cascade consists of activating (E1), conjugating (E2), and/or ligating (E3) enzymes and then targets them for degradation by the 26S proteasome. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and ubiquitin's C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. A set of novel molecules with a structural similarity to Ub, called Ub-like proteins (Ubls), have similar conjugation cascades. In contrast to ubiquitin-E1, which is a single-chain protein with a weakly conserved two-fold repeat, many of the Ubls-E1are a heterodimer where each subunit corresponds to one half of a single-chain E1. This CD represents the family homologous to the second repeat of Ub-E1.


Pssm-ID: 238761 [Multi-domain]  Cd Length: 234  Bit Score: 42.95  E-value: 8.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308963989  44 LARLGVGALNLTDFDSFEVANFNRQAGAAMSTLGQPKVEVMRGFALDVNPETD-VRVFPNGLDEANLSD-YLDGVDLLID 121
Cdd:cd01484    18 LALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNPNCKvVPYQNKVGPEQDFNDtFFEQFHIIVN 97


                  ...
gi 1308963989 122 AID 124
Cdd:cd01484    98 ALD 100
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 17-158 1.02e-04

thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 43.06  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308963989  17 PQEQQRLRGARVAVAGMGGVGGVHVQGLARLGVGALNLTDFDSFEVANFNRQ--------------AGAAMSTLGQPKVE 82
Cdd:PRK07688   16 EEGQQKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQqlytesdvknnlpkAVAAKKRLEEINSD 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308963989  83 V-MRGFALDVNPEtdvrvfpngldeaNLSDYLDGVDLLIDAIDFFanSLRPALYRAARERGIPVV---CAAPLGAGASLI 158
Cdd:PRK07688   96 VrVEAIVQDVTAE-------------ELEELVTGVDLIIDATDNF--ETRFIVNDAAQKYGIPWIygaCVGSYGLSYTII 160
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 42-126 2.71e-04

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 42.02  E-value: 2.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308963989  42 QGLARLGVGALNLTDFDSFEVANFNRQ--------------AGAAMSTLGQPKVEV-MRGFALDVNPEtdvrvfpnglde 106
Cdd:PRK12475   41 EALVRAGIGKLTIADRDYVEWSNLQRQqlyteedakqkkpkAIAAKEHLRKINSEVeIVPVVTDVTVE------------ 108

                          90       100
                  ....*....|....*....|
gi 1308963989 107 aNLSDYLDGVDLLIDAIDFF 126
Cdd:PRK12475  109 -ELEELVKEVDLIIDATDNF 127
NAD_binding_7 pfam13241
Putative NAD(P)-binding; This domain is found in fungi, plants, archaea and bacteria.
 104-145 6.07e-03

Putative NAD(P)-binding; This domain is found in fungi, plants, archaea and bacteria.


Pssm-ID: 433055 [Multi-domain]  Cd Length: 104  Bit Score: 35.53  E-value: 6.07e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1308963989 104 LDEANLSDYLDGVDLLIDAIDffANSLRPALYRAARERGIPV 145
Cdd:pfam13241  50 LIRREFEGDLDGADLVIAATD--DPELNERIAALARARGILV 89
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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