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Conserved domains on  [gi|515741997|ref|WP_017174597|]
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MULTISPECIES: FADH(2)-oxidizing methylenetetrahydrofolate--tRNA-(uracil(54)-C(5))-methyltransferase TrmFO [Staphylococcus]

Protein Classification

methylenetetrahydrofolate--tRNA-(uracil(54)-C(5))-methyltransferase (FADH(2)-oxidizing) TrmFO( domain architecture ID 10787361)

methylenetetrahydrofolate--tRNA-(uracil(54)-C(5))-methyltransferase (FADH(2)-oxidizing) TrmFO modifies tRNA containing uridine at position 54 to form a 5-methyluridine (ribothymidine)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TrmFO COG1206
Folate-dependent tRNA-U54 methylase TrmFO/GidA [Translation, ribosomal structure and ...
 2-435 0e+00

Folate-dependent tRNA-U54 methylase TrmFO/GidA [Translation, ribosomal structure and biogenesis]; Folate-dependent tRNA-U54 methylase TrmFO/GidA is part of the Pathway/BioSystem: tRNA modification


:

Pssm-ID: 440819  Cd Length: 436  Bit Score: 881.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997   2 SQTVNVIGAGLAGSEAAYQLAERGIKVNLIEMRPVKQTPAHHTDKFAELVCSNSLRGNALTNGVGVLKEEMRRLDSLIIA 81
Cdd:COG1206    1 MKPVTVIGGGLAGSEAAWQLAERGVPVRLYEMRPVKMTPAHKTDGFAELVCSNSLRSDDLTNAVGLLKEEMRRLGSLIMA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997  82 AADKARVPAGGALAVDRHDFAGYITDTLKNHPNVTVLNKEIHSIPE-GHTIIATGPLTTEHLAKEIVEITGKDQLYFYDA 160
Cdd:COG1206   81 AADAHRVPAGGALAVDREGFSAAVTEKLENHPNITVVREEVTEIPEdGPVIIATGPLTSDALAEAIQELTGEEYLYFYDA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997 161 AAPIIEKDSIDMDKVYLKSRYDKGEAAYLNCPMTEEEFNRFYDAVLEAEVAPVNEFEKEKYFEGCMPFEVMAGRGHKTLL 240
Cdd:COG1206  161 IAPIVDADSIDMDKAFRASRYDKGEADYLNCPMTKEEYEAFYEALLAAEKVELKDFEKEKYFEGCLPIEVMARRGRDTLR 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997 241 FGPMKPVGLEDPKTGKRPYAVVQLRQDDAAGTLYNIVGFQTHLKWGAQKEVIQLIPGLENVDIVRYGVMHRNTFINSPDV 320
Cdd:COG1206  241 FGPMKPVGLTDPRTGKRPYAVVQLRQENAEGTLYNLVGFQTKLKWGEQKRVFRMIPGLENAEFVRYGVMHRNTFINSPKL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997 321 LNEKYELINNDRIQFAGQMTGVEGYVESAASGLVAGINLAHKLLGKGEVIFPRETMIGSMAYYISHAkNEKNFQPMNANF 400
Cdd:COG1206  321 LDPTLQLKARPNLFFAGQITGVEGYVESAASGLLAGINAARLLLGKEPVPPPPTTALGALLNYITGA-DPKDFQPMNVNF 399

                        410       420       430
                 ....*....|....*....|....*....|....*
gi 515741997 401 GLLPSLDRRIKDKKERYEAQAYRALDYLENFKKTL 435
Cdd:COG1206  400 GLLPPLEKRIRDKKERKEAYAERALEDLEAWLAEL 434
 
Name Accession Description Interval E-value
TrmFO COG1206
Folate-dependent tRNA-U54 methylase TrmFO/GidA [Translation, ribosomal structure and ...
 2-435 0e+00

Folate-dependent tRNA-U54 methylase TrmFO/GidA [Translation, ribosomal structure and biogenesis]; Folate-dependent tRNA-U54 methylase TrmFO/GidA is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440819  Cd Length: 436  Bit Score: 881.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997   2 SQTVNVIGAGLAGSEAAYQLAERGIKVNLIEMRPVKQTPAHHTDKFAELVCSNSLRGNALTNGVGVLKEEMRRLDSLIIA 81
Cdd:COG1206    1 MKPVTVIGGGLAGSEAAWQLAERGVPVRLYEMRPVKMTPAHKTDGFAELVCSNSLRSDDLTNAVGLLKEEMRRLGSLIMA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997  82 AADKARVPAGGALAVDRHDFAGYITDTLKNHPNVTVLNKEIHSIPE-GHTIIATGPLTTEHLAKEIVEITGKDQLYFYDA 160
Cdd:COG1206   81 AADAHRVPAGGALAVDREGFSAAVTEKLENHPNITVVREEVTEIPEdGPVIIATGPLTSDALAEAIQELTGEEYLYFYDA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997 161 AAPIIEKDSIDMDKVYLKSRYDKGEAAYLNCPMTEEEFNRFYDAVLEAEVAPVNEFEKEKYFEGCMPFEVMAGRGHKTLL 240
Cdd:COG1206  161 IAPIVDADSIDMDKAFRASRYDKGEADYLNCPMTKEEYEAFYEALLAAEKVELKDFEKEKYFEGCLPIEVMARRGRDTLR 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997 241 FGPMKPVGLEDPKTGKRPYAVVQLRQDDAAGTLYNIVGFQTHLKWGAQKEVIQLIPGLENVDIVRYGVMHRNTFINSPDV 320
Cdd:COG1206  241 FGPMKPVGLTDPRTGKRPYAVVQLRQENAEGTLYNLVGFQTKLKWGEQKRVFRMIPGLENAEFVRYGVMHRNTFINSPKL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997 321 LNEKYELINNDRIQFAGQMTGVEGYVESAASGLVAGINLAHKLLGKGEVIFPRETMIGSMAYYISHAkNEKNFQPMNANF 400
Cdd:COG1206  321 LDPTLQLKARPNLFFAGQITGVEGYVESAASGLLAGINAARLLLGKEPVPPPPTTALGALLNYITGA-DPKDFQPMNVNF 399

                        410       420       430
                 ....*....|....*....|....*....|....*
gi 515741997 401 GLLPSLDRRIKDKKERYEAQAYRALDYLENFKKTL 435
Cdd:COG1206  400 GLLPPLEKRIRDKKERKEAYAERALEDLEAWLAEL 434
PRK05335 PRK05335
tRNA (uracil-5-)-methyltransferase Gid; Reviewed
 1-435 0e+00

tRNA (uracil-5-)-methyltransferase Gid; Reviewed


Pssm-ID: 235416  Cd Length: 436  Bit Score: 877.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997   1 MSQTVNVIGAGLAGSEAAYQLAERGIKVNLIEMRPVKQTPAHHTDKFAELVCSNSLRGNALTNGVGVLKEEMRRLDSLII 80
Cdd:PRK05335   1 MMKPVNVIGAGLAGSEAAWQLAKRGVPVELYEMRPVKKTPAHHTDGFAELVCSNSFRSDSLTNAVGLLKEEMRRLGSLIM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997  81 AAADKARVPAGGALAVDRHDFAGYITDTLKNHPNVTVLNKEIHSIPEGHTIIATGPLTTEHLAKEIVEITGKDQLYFYDA 160
Cdd:PRK05335  81 EAADAHRVPAGGALAVDREGFSEYVTEALENHPLITVIREEVTEIPEDITIIATGPLTSDALAEAIKALTGEDYLYFFDA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997 161 AAPIIEKDSIDMDKVYLKSRYDKGEAAYLNCPMTEEEFNRFYDAVLEAEVAPVNEFEKEKYFEGCMPFEVMAGRGHKTLL 240
Cdd:PRK05335 161 AAPIVDKDSIDMDKVYLASRYDKGEADYLNCPMTKEEYEAFYEALIAAEKAELKDFEKEKYFEGCMPIEVMAERGRETLR 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997 241 FGPMKPVGLEDPKTGKRPYAVVQLRQDDAAGTLYNIVGFQTHLKWGAQKEVIQLIPGLENVDIVRYGVMHRNTFINSPDV 320
Cdd:PRK05335 241 FGPMKPVGLTDPRTGKRPYAVVQLRQDNAAGTLYNIVGFQTKLKWGEQKRVFRMIPGLENAEFVRYGVMHRNTFINSPKL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997 321 LNEKYELINNDRIQFAGQMTGVEGYVESAASGLVAGINLAHKLLGKGEVIFPRETMIGSMAYYISHAkNEKNFQPMNANF 400
Cdd:PRK05335 321 LDPTLQLKKRPNLFFAGQITGVEGYVESAASGLLAGINAARLALGKEPVIPPPTTALGALLNYITGA-NPKHFQPMNANF 399

                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 515741997 401 GLLPSLDRRIK--DKKERYEAQAYRALDYLENFKKTL 435
Cdd:PRK05335 400 GLFPPLGKRIRgeDKKERKEAYAERALADLKEWLKEL 436
gid_trmFO TIGR00137
tRNA:m(5)U-54 methyltransferase; This model represents an orthologous set of proteins present ...
 3-435 0e+00

tRNA:m(5)U-54 methyltransferase; This model represents an orthologous set of proteins present in relatively few bacteria but very tightly conserved where it occurs. It is closely related to gidA (glucose-inhibited division protein A), which appears to be present in all complete eubacterial genomes so far and in Saccharomyces cerevisiae. It was designated gid but is now recognized as a tRNA:m(5)U-54 methyltransferase and is now designated trmFO. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 129243  Cd Length: 433  Bit Score: 684.71  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997    3 QTVNVIGAGLAGSEAAYQLAERGIKVNLIEMRPVKQTPAHHTDKFAELVCSNSLRGNALTNGVGVLKEEMRRLDSLIIAA 82
Cdd:TIGR00137   1 TPVHVIGGGLAGSEAAWQLAQAGVPVILYEMRPEKLTPAHHTEDLAELVCSNSLGAKALDRAAGLLKTEMRQLSSLIITA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997   83 ADKARVPAGGALAVDRHDFAGYITDTLKNHPNVTVLNKEIHSIPEGH-TIIATGPLTTEHLAKEIVEITGKDQLYFYDAA 161
Cdd:TIGR00137  81 ADRHAVPAGGALAVDRGIFSRSLTEQVASHPNVTLIREEVTEIPEEGiTVIATGPLTSPALSEDLKELTGMDYLYFYDAA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997  162 APIIEKDSIDMDKVYLKSRYDKGEAAYLNCPMTEEEFNRFYDAVLEAEVAPVNEFEKEKYFEGCMPFEVMAGRGHKTLLF 241
Cdd:TIGR00137 161 APIVEGDSIDKEKAFFASRYDKGEAAYLNCPFTEEEYFNFWEALCEAEQVPLKDFEKAKFFEGCLPIEEMAQRGEKTMLF 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997  242 GPMKPVGLEDPKTGKRPYAVVQLRQDDAAGTLYNIVGFQTHLKWGAQKEVIQLIPGLENVDIVRYGVMHRNTFINSPDVL 321
Cdd:TIGR00137 241 GPMKPVGLFDPRTGKKPYAVVQLRQEDKAGTLWNMVGFQTNLRWGEQKRVFRLIPGLENAEFVRMGVMHRNTFINSPQLL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997  322 NEKYELINNDRIQFAGQMTGVEGYVESAASGLVAGINLAHKLLGKGEVIFPRETMIGSMAYYIShAKNEKNFQPMNANFG 401
Cdd:TIGR00137 321 TASLHFKDRQTLFFAGQLTGVEGYVASTAGGWLAGINAARLALGEPLLTLPAETMMGALFNYIS-TASPKHFQPMNPNFG 399

                         410       420       430
                  ....*....|....*....|....*....|....
gi 515741997  402 LLPSLDRRIKDKKERYEAQAYRALDYLENFKKTL 435
Cdd:TIGR00137 400 LLPELPQKIRNKKERYEQYADRALETLTTWQKSI 433
GIDA pfam01134
Glucose inhibited division protein A;
4-366 3.15e-140

Glucose inhibited division protein A;


Pssm-ID: 250388 [Multi-domain]  Cd Length: 391  Bit Score: 406.55  E-value: 3.15e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997    4 TVNVIGAGLAGSEAAYQLAERGIKVNLIemrpvkqtpAHHTDKFAELVCSNSLRGNAltngVGVLKEEMRRLDSLIIAAA 83
Cdd:pfam01134   1 DVIVIGGGHAGCEAALAAARMGAKVLLI---------THNTDTIAELSCNPSIGGIA----KGHLVREIDALGGLMGKAA 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997   84 DKARV----------PAGGAL--AVDRHDFAGYITDTLKNHPNVTVLNKEIHSI------------------PEGHTIIA 133
Cdd:pfam01134  68 DKTGIqfrmlntskgPAVRALraQVDRDLYSKEMTETLENHPNLTLIQGEVTDLipengkvkgvvtedgeeyKAKAVVLA 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997  134 TGP--------------------LTTEHLAKEIVEiTGKDQLYFYDAAAPIIEKDSIDMDKVYLKSRYDKG-EAAYLNCP 192
Cdd:pfam01134 148 TGTflngkihiglkcypagrlgeLTSEGLSESLKE-LGFELGRFKTGTPPRIDKDSIDFSKLEEQPGDKPGpPFSYLNCP 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997  193 MTEEEFNRFYDAVLEAEVAPVNEFEKEK-YFEGCMpfEVMAGRGHKTLLFgpmKPVGLEDpktgkRPYAVVQLRQDDAAG 271
Cdd:pfam01134 227 MNKEQYPCFLTYTNEATHEIIRDNLHRSpMFEGCI--EGIGPRYCPSIED---KPVRFAD-----KPYHQVFLEPEGLDT 296

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997  272 TLYNIVGFQTHLKWGAQKEVIQLIPGLENVDIVRYGVMHRNTFINSPDVLNeKYELINNDRIQFAGQMTGVEGYVESAAS 351
Cdd:pfam01134 297 DEYYLVGFSTSLPEDVQKRVLRTIPGLENAEIVRPGYAIEYDYIDPPQLLP-TLETKKIPGLFFAGQINGTEGYEEAAAQ 375

                         410
                  ....*....|....*
gi 515741997  352 GLVAGINLAHKLLGK 366
Cdd:pfam01134 376 GLLAGINAARKALGK 390
nuc_hydro cd00455
nuc_hydro: Nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in ...
 51-139 9.12e-04

nuc_hydro: Nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in nucleosides generating ribose and the respective base. These enzymes vary in their substrate specificity. This group contains eukaryotic, bacterial and archeal proteins similar to the inosine-uridine preferring nucleoside hydrolase from Crithidia fasciculata, the xanthosine-inosine-uridine-adenosine-preferring nucleoside hydrolase RihC from Salmonella enterica serovar Typhimurium, the purine-specific inosine-adenosine-guanosine-preferring nucleoside hydrolase from Trypanosoma vivax and, pyrimidine-specific uridine-cytidine preferring nucleoside hydrolases such as URH1 from Saccharomyces cerevisiae, RihA and RihB from Escherichia coli. Nucleoside hydrolases are of interest as a target for antiprotozoan drugs as, no nucleoside hydrolase activity or genes encoding these enzymes have been detected in humans and, parasitic protozoans lack de novo purine synthesis relying on nucleoside hydrolase to scavenge purine and/or pyrimidines from the environment.


Pssm-ID: 238257 [Multi-domain]  Cd Length: 295  Bit Score: 41.16  E-value: 9.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997  51 VCSNSLRGNALTNgVGVLKEEMRRLDSLIIAAADKARVPaGGALAVDRHDFAGYITDTLK------NHPNVTVLNKEIHS 124
Cdd:cd00455   32 TYGNVTLEQATQN-AAYLLELLGRLDIPVYAGATRPLTG-EIPAAYPEIHGEGGLGLPIPpiieadDPEAVQLLIDLIRK 109

                         90
                 ....*....|....*
gi 515741997 125 IPEGHTIIATGPLTT 139
Cdd:cd00455  110 YPDEITIVALGPLTN 124
 
Name Accession Description Interval E-value
TrmFO COG1206
Folate-dependent tRNA-U54 methylase TrmFO/GidA [Translation, ribosomal structure and ...
 2-435 0e+00

Folate-dependent tRNA-U54 methylase TrmFO/GidA [Translation, ribosomal structure and biogenesis]; Folate-dependent tRNA-U54 methylase TrmFO/GidA is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440819  Cd Length: 436  Bit Score: 881.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997   2 SQTVNVIGAGLAGSEAAYQLAERGIKVNLIEMRPVKQTPAHHTDKFAELVCSNSLRGNALTNGVGVLKEEMRRLDSLIIA 81
Cdd:COG1206    1 MKPVTVIGGGLAGSEAAWQLAERGVPVRLYEMRPVKMTPAHKTDGFAELVCSNSLRSDDLTNAVGLLKEEMRRLGSLIMA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997  82 AADKARVPAGGALAVDRHDFAGYITDTLKNHPNVTVLNKEIHSIPE-GHTIIATGPLTTEHLAKEIVEITGKDQLYFYDA 160
Cdd:COG1206   81 AADAHRVPAGGALAVDREGFSAAVTEKLENHPNITVVREEVTEIPEdGPVIIATGPLTSDALAEAIQELTGEEYLYFYDA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997 161 AAPIIEKDSIDMDKVYLKSRYDKGEAAYLNCPMTEEEFNRFYDAVLEAEVAPVNEFEKEKYFEGCMPFEVMAGRGHKTLL 240
Cdd:COG1206  161 IAPIVDADSIDMDKAFRASRYDKGEADYLNCPMTKEEYEAFYEALLAAEKVELKDFEKEKYFEGCLPIEVMARRGRDTLR 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997 241 FGPMKPVGLEDPKTGKRPYAVVQLRQDDAAGTLYNIVGFQTHLKWGAQKEVIQLIPGLENVDIVRYGVMHRNTFINSPDV 320
Cdd:COG1206  241 FGPMKPVGLTDPRTGKRPYAVVQLRQENAEGTLYNLVGFQTKLKWGEQKRVFRMIPGLENAEFVRYGVMHRNTFINSPKL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997 321 LNEKYELINNDRIQFAGQMTGVEGYVESAASGLVAGINLAHKLLGKGEVIFPRETMIGSMAYYISHAkNEKNFQPMNANF 400
Cdd:COG1206  321 LDPTLQLKARPNLFFAGQITGVEGYVESAASGLLAGINAARLLLGKEPVPPPPTTALGALLNYITGA-DPKDFQPMNVNF 399

                        410       420       430
                 ....*....|....*....|....*....|....*
gi 515741997 401 GLLPSLDRRIKDKKERYEAQAYRALDYLENFKKTL 435
Cdd:COG1206  400 GLLPPLEKRIRDKKERKEAYAERALEDLEAWLAEL 434
PRK05335 PRK05335
tRNA (uracil-5-)-methyltransferase Gid; Reviewed
 1-435 0e+00

tRNA (uracil-5-)-methyltransferase Gid; Reviewed


Pssm-ID: 235416  Cd Length: 436  Bit Score: 877.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997   1 MSQTVNVIGAGLAGSEAAYQLAERGIKVNLIEMRPVKQTPAHHTDKFAELVCSNSLRGNALTNGVGVLKEEMRRLDSLII 80
Cdd:PRK05335   1 MMKPVNVIGAGLAGSEAAWQLAKRGVPVELYEMRPVKKTPAHHTDGFAELVCSNSFRSDSLTNAVGLLKEEMRRLGSLIM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997  81 AAADKARVPAGGALAVDRHDFAGYITDTLKNHPNVTVLNKEIHSIPEGHTIIATGPLTTEHLAKEIVEITGKDQLYFYDA 160
Cdd:PRK05335  81 EAADAHRVPAGGALAVDREGFSEYVTEALENHPLITVIREEVTEIPEDITIIATGPLTSDALAEAIKALTGEDYLYFFDA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997 161 AAPIIEKDSIDMDKVYLKSRYDKGEAAYLNCPMTEEEFNRFYDAVLEAEVAPVNEFEKEKYFEGCMPFEVMAGRGHKTLL 240
Cdd:PRK05335 161 AAPIVDKDSIDMDKVYLASRYDKGEADYLNCPMTKEEYEAFYEALIAAEKAELKDFEKEKYFEGCMPIEVMAERGRETLR 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997 241 FGPMKPVGLEDPKTGKRPYAVVQLRQDDAAGTLYNIVGFQTHLKWGAQKEVIQLIPGLENVDIVRYGVMHRNTFINSPDV 320
Cdd:PRK05335 241 FGPMKPVGLTDPRTGKRPYAVVQLRQDNAAGTLYNIVGFQTKLKWGEQKRVFRMIPGLENAEFVRYGVMHRNTFINSPKL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997 321 LNEKYELINNDRIQFAGQMTGVEGYVESAASGLVAGINLAHKLLGKGEVIFPRETMIGSMAYYISHAkNEKNFQPMNANF 400
Cdd:PRK05335 321 LDPTLQLKKRPNLFFAGQITGVEGYVESAASGLLAGINAARLALGKEPVIPPPTTALGALLNYITGA-NPKHFQPMNANF 399

                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 515741997 401 GLLPSLDRRIK--DKKERYEAQAYRALDYLENFKKTL 435
Cdd:PRK05335 400 GLFPPLGKRIRgeDKKERKEAYAERALADLKEWLKEL 436
gid_trmFO TIGR00137
tRNA:m(5)U-54 methyltransferase; This model represents an orthologous set of proteins present ...
 3-435 0e+00

tRNA:m(5)U-54 methyltransferase; This model represents an orthologous set of proteins present in relatively few bacteria but very tightly conserved where it occurs. It is closely related to gidA (glucose-inhibited division protein A), which appears to be present in all complete eubacterial genomes so far and in Saccharomyces cerevisiae. It was designated gid but is now recognized as a tRNA:m(5)U-54 methyltransferase and is now designated trmFO. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 129243  Cd Length: 433  Bit Score: 684.71  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997    3 QTVNVIGAGLAGSEAAYQLAERGIKVNLIEMRPVKQTPAHHTDKFAELVCSNSLRGNALTNGVGVLKEEMRRLDSLIIAA 82
Cdd:TIGR00137   1 TPVHVIGGGLAGSEAAWQLAQAGVPVILYEMRPEKLTPAHHTEDLAELVCSNSLGAKALDRAAGLLKTEMRQLSSLIITA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997   83 ADKARVPAGGALAVDRHDFAGYITDTLKNHPNVTVLNKEIHSIPEGH-TIIATGPLTTEHLAKEIVEITGKDQLYFYDAA 161
Cdd:TIGR00137  81 ADRHAVPAGGALAVDRGIFSRSLTEQVASHPNVTLIREEVTEIPEEGiTVIATGPLTSPALSEDLKELTGMDYLYFYDAA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997  162 APIIEKDSIDMDKVYLKSRYDKGEAAYLNCPMTEEEFNRFYDAVLEAEVAPVNEFEKEKYFEGCMPFEVMAGRGHKTLLF 241
Cdd:TIGR00137 161 APIVEGDSIDKEKAFFASRYDKGEAAYLNCPFTEEEYFNFWEALCEAEQVPLKDFEKAKFFEGCLPIEEMAQRGEKTMLF 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997  242 GPMKPVGLEDPKTGKRPYAVVQLRQDDAAGTLYNIVGFQTHLKWGAQKEVIQLIPGLENVDIVRYGVMHRNTFINSPDVL 321
Cdd:TIGR00137 241 GPMKPVGLFDPRTGKKPYAVVQLRQEDKAGTLWNMVGFQTNLRWGEQKRVFRLIPGLENAEFVRMGVMHRNTFINSPQLL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997  322 NEKYELINNDRIQFAGQMTGVEGYVESAASGLVAGINLAHKLLGKGEVIFPRETMIGSMAYYIShAKNEKNFQPMNANFG 401
Cdd:TIGR00137 321 TASLHFKDRQTLFFAGQLTGVEGYVASTAGGWLAGINAARLALGEPLLTLPAETMMGALFNYIS-TASPKHFQPMNPNFG 399

                         410       420       430
                  ....*....|....*....|....*....|....
gi 515741997  402 LLPSLDRRIKDKKERYEAQAYRALDYLENFKKTL 435
Cdd:TIGR00137 400 LLPELPQKIRNKKERYEQYADRALETLTTWQKSI 433
GIDA pfam01134
Glucose inhibited division protein A;
4-366 3.15e-140

Glucose inhibited division protein A;


Pssm-ID: 250388 [Multi-domain]  Cd Length: 391  Bit Score: 406.55  E-value: 3.15e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997    4 TVNVIGAGLAGSEAAYQLAERGIKVNLIemrpvkqtpAHHTDKFAELVCSNSLRGNAltngVGVLKEEMRRLDSLIIAAA 83
Cdd:pfam01134   1 DVIVIGGGHAGCEAALAAARMGAKVLLI---------THNTDTIAELSCNPSIGGIA----KGHLVREIDALGGLMGKAA 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997   84 DKARV----------PAGGAL--AVDRHDFAGYITDTLKNHPNVTVLNKEIHSI------------------PEGHTIIA 133
Cdd:pfam01134  68 DKTGIqfrmlntskgPAVRALraQVDRDLYSKEMTETLENHPNLTLIQGEVTDLipengkvkgvvtedgeeyKAKAVVLA 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997  134 TGP--------------------LTTEHLAKEIVEiTGKDQLYFYDAAAPIIEKDSIDMDKVYLKSRYDKG-EAAYLNCP 192
Cdd:pfam01134 148 TGTflngkihiglkcypagrlgeLTSEGLSESLKE-LGFELGRFKTGTPPRIDKDSIDFSKLEEQPGDKPGpPFSYLNCP 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997  193 MTEEEFNRFYDAVLEAEVAPVNEFEKEK-YFEGCMpfEVMAGRGHKTLLFgpmKPVGLEDpktgkRPYAVVQLRQDDAAG 271
Cdd:pfam01134 227 MNKEQYPCFLTYTNEATHEIIRDNLHRSpMFEGCI--EGIGPRYCPSIED---KPVRFAD-----KPYHQVFLEPEGLDT 296

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997  272 TLYNIVGFQTHLKWGAQKEVIQLIPGLENVDIVRYGVMHRNTFINSPDVLNeKYELINNDRIQFAGQMTGVEGYVESAAS 351
Cdd:pfam01134 297 DEYYLVGFSTSLPEDVQKRVLRTIPGLENAEIVRPGYAIEYDYIDPPQLLP-TLETKKIPGLFFAGQINGTEGYEEAAAQ 375

                         410
                  ....*....|....*
gi 515741997  352 GLVAGINLAHKLLGK 366
Cdd:pfam01134 376 GLLAGINAARKALGK 390
MnmG COG0445
tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal ...
 278-380 2.57e-11

tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal structure and biogenesis]; tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440214 [Multi-domain]  Cd Length: 626  Bit Score: 65.41  E-value: 2.57e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997 278 GFQTHLKWGAQKEVIQLIPGLENVDIVRYGvmhrntFINsPDVLNEKYELinnDRIQ---FAGQMTGVEGYVESAASGLV 354
Cdd:COG0445  310 GISTSLPEDVQLAMLRSIPGLENAEILRPGyaieydYVD-PTQLKPTLET---KKIEglfFAGQINGTTGYEEAAAQGLM 385

                         90       100
                 ....*....|....*....|....*..
gi 515741997 355 AGINLAHKLLGKGEVIFPR-ETMIGSM 380
Cdd:COG0445  386 AGINAALKAQGKEPFILDRsEAYIGVL 412
COG3349 COG3349
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ...
 1-35 1.33e-06

Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function prediction only];


Pssm-ID: 442577 [Multi-domain]  Cd Length: 445  Bit Score: 50.24  E-value: 1.33e-06
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 515741997   1 MSQTVNVIGAGLAGSEAAYQLAERGIKVNLIEMRP 35
Cdd:COG3349    2 MPPRVVVVGGGLAGLAAAVELAEAGFRVTLLEARP 36
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
7-35 6.57e-06

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 43.67  E-value: 6.57e-06
                          10        20
                  ....*....|....*....|....*....
gi 515741997    7 VIGAGLAGSEAAYQLAERGIKVNLIEMRP 35
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLEKRD 29
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
1-32 6.19e-05

Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 45.24  E-value: 6.19e-05
                         10        20        30
                 ....*....|....*....|....*....|..
gi 515741997   1 MSQTVNVIGAGLAGSEAAYQLAERGIKVNLIE 32
Cdd:COG1148  139 VNKRALVIGGGIAGMTAALELAEQGYEVYLVE 170
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
7-44 8.70e-05

Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 44.51  E-value: 8.70e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 515741997   7 VIGAGLAGSEAAYQLAERGIKVNLIEmrpvKQTPAHHT 44
Cdd:COG0665    7 VIGGGIAGLSTAYHLARRGLDVTVLE----RGRPGSGA 40
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 7-44 1.66e-04

FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.


Pssm-ID: 426168 [Multi-domain]  Cd Length: 339  Bit Score: 43.54  E-value: 1.66e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 515741997    7 VIGAGLAGSEAAYQLAERGIKVNLIEMRPVkqtPAHHT 44
Cdd:pfam01266   4 VIGGGIVGLSTAYELARRGLSVTLLERGDD---PGSGA 38
PRK07208 PRK07208
hypothetical protein; Provisional
 1-36 1.75e-04

hypothetical protein; Provisional


Pssm-ID: 235967 [Multi-domain]  Cd Length: 479  Bit Score: 43.72  E-value: 1.75e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 515741997   1 MSQTVNVIGAGLAGSEAAYQLAERGIKVNLIEMRPV 36
Cdd:PRK07208   3 NKKSVVIIGAGPAGLTAAYELLKRGYPVTVLEADPV 38
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 3-143 2.01e-04

NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];


Pssm-ID: 440215 [Multi-domain]  Cd Length: 322  Bit Score: 43.26  E-value: 2.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997   3 QTVNVIGAGLAGSEAAYQLAERGIKVNLIEMRPV---KQTP-------AHHTDKFAELVCSNSLRGNALTNGVGVLKEEM 72
Cdd:COG0446  125 KRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRllgVLDPemaalleEELREHGVELRLGETVVAIDGDDKVAVTLTDG 204

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997  73 RRLDS-LIIAA---------ADKARVPAG--GALAVDRHdfagyitdtLK-NHPNV----------TVLNKEIHSIPEGH 129
Cdd:COG0446  205 EEIPAdLVVVApgvrpntelAKDAGLALGerGWIKVDET---------LQtSDPDVyaagdcaevpHPVTGKTVYIPLAS 275

                        170
                 ....*....|....
gi 515741997 130 TIIATGPLTTEHLA 143
Cdd:COG0446  276 AANKQGRVAAENIL 289
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
7-35 2.82e-04

NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 42.82  E-value: 2.82e-04
                         10        20
                 ....*....|....*....|....*....
gi 515741997   7 VIGAGLAGSEAAYQLAERGIKVNLIEMRP 35
Cdd:COG1251  147 VIGGGLIGLEAAAALRKRGLEVTVVERAP 175
sdhA PRK08641
succinate dehydrogenase flavoprotein subunit; Reviewed
 1-37 4.04e-04

succinate dehydrogenase flavoprotein subunit; Reviewed


Pssm-ID: 236319 [Multi-domain]  Cd Length: 589  Bit Score: 42.65  E-value: 4.04e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 515741997   1 MSQTVNVIGAGLAGSEAAYQLAERGIKVNLIEMRPVK 37
Cdd:PRK08641   2 AKGKVIVVGGGLAGLMATIKAAEAGVHVDLFSLVPVK 38
PRK07233 PRK07233
hypothetical protein; Provisional
 4-36 7.56e-04

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 41.80  E-value: 7.56e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 515741997   4 TVNVIGAGLAGSEAAYQLAERGIKVNLIEMRPV 36
Cdd:PRK07233   1 KIAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQ 33
GG-red-SF TIGR02032
geranylgeranyl reductase family; This model represents a subfamily which includes ...
 5-212 8.48e-04

geranylgeranyl reductase family; This model represents a subfamily which includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 273936 [Multi-domain]  Cd Length: 295  Bit Score: 41.15  E-value: 8.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997    5 VNVIGAGLAGSEAAYQLAERGIKVNLIEMRpvkqtpahhtDKFAELVCsnslrGNALTNGVGVLKEEMRRLDSLIIAAAD 84
Cdd:TIGR02032   3 VVVVGAGPAGASAAYRLADKGLRVLLLEKK----------SFPRYKPC-----GGALSPRALEELDLPGELIVNLVRGAR 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997   85 ---------KARVPAGGALAVDRHDFAGYITDTLKNHPNVTVLNKEIHSIPEGHTIIATGPLTTEH--LAKEIVEITGkd 153
Cdd:TIGR02032  68 ffspngdsvEIPIETELAYVIDRDAFDEQLAERAQEAGAELRLGTRVLDVEIHDDRVVVIVRGSEGtvTAKIVIGADG-- 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997  154 qlyfydAAAPIieKDSIDMDkvylKSRYDKGEAAYLNCPMTEEEFNR-FYDAVLEAEVAP 212
Cdd:TIGR02032 146 ------SRSIV--AKKLGLK----KEPREYGVAARAEVEMPDEEVDEdFVEVYIDRGIVP 193
nuc_hydro cd00455
nuc_hydro: Nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in ...
 51-139 9.12e-04

nuc_hydro: Nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in nucleosides generating ribose and the respective base. These enzymes vary in their substrate specificity. This group contains eukaryotic, bacterial and archeal proteins similar to the inosine-uridine preferring nucleoside hydrolase from Crithidia fasciculata, the xanthosine-inosine-uridine-adenosine-preferring nucleoside hydrolase RihC from Salmonella enterica serovar Typhimurium, the purine-specific inosine-adenosine-guanosine-preferring nucleoside hydrolase from Trypanosoma vivax and, pyrimidine-specific uridine-cytidine preferring nucleoside hydrolases such as URH1 from Saccharomyces cerevisiae, RihA and RihB from Escherichia coli. Nucleoside hydrolases are of interest as a target for antiprotozoan drugs as, no nucleoside hydrolase activity or genes encoding these enzymes have been detected in humans and, parasitic protozoans lack de novo purine synthesis relying on nucleoside hydrolase to scavenge purine and/or pyrimidines from the environment.


Pssm-ID: 238257 [Multi-domain]  Cd Length: 295  Bit Score: 41.16  E-value: 9.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997  51 VCSNSLRGNALTNgVGVLKEEMRRLDSLIIAAADKARVPaGGALAVDRHDFAGYITDTLK------NHPNVTVLNKEIHS 124
Cdd:cd00455   32 TYGNVTLEQATQN-AAYLLELLGRLDIPVYAGATRPLTG-EIPAAYPEIHGEGGLGLPIPpiieadDPEAVQLLIDLIRK 109

                         90
                 ....*....|....*
gi 515741997 125 IPEGHTIIATGPLTT 139
Cdd:cd00455  110 YPDEITIVALGPLTN 124
mnmC PRK01747
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ...
 7-32 1.01e-03

bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent 5-carboxymethylaminomethyl-2-thiouridine(34) oxidoreductase MnmC;


Pssm-ID: 234978 [Multi-domain]  Cd Length: 662  Bit Score: 41.37  E-value: 1.01e-03
                         10        20
                 ....*....|....*....|....*.
gi 515741997   7 VIGAGLAGSEAAYQLAERGIKVNLIE 32
Cdd:PRK01747 265 IIGGGIAGAALALALARRGWQVTLYE 290
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
7-34 1.20e-03

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 41.06  E-value: 1.20e-03
                         10        20
                 ....*....|....*....|....*...
gi 515741997   7 VIGAGLAGSEAAYQLAERGIKVNLIEMR 34
Cdd:COG1231   12 IVGAGLAGLAAARELRKAGLDVTVLEAR 39
PRK06847 PRK06847
hypothetical protein; Provisional
 3-35 2.53e-03

hypothetical protein; Provisional


Pssm-ID: 235874 [Multi-domain]  Cd Length: 375  Bit Score: 39.86  E-value: 2.53e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 515741997   3 QTVNVIGAGLAGSEAAYQLAERGIKVNLIEMRP 35
Cdd:PRK06847   5 KKVLIVGGGIGGLSAAIALRRAGIAVDLVEIDP 37
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
10-107 3.01e-03

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 39.18  E-value: 3.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741997  10 AGLAGSEAAYQLAERGIKVNLIEMRPVkqtPAHHtdkfaelVCsnslrgnaltnGVGVLKEEMRRLDSLIIAAA------ 83
Cdd:COG0644    1 AGPAGSAAARRLARAGLSVLLLEKGSF---PGDK-------IC-----------GGGLLPRALEELEPLGLDEPlerpvr 59

                         90       100
                 ....*....|....*....|....*
gi 515741997  84 -DKARVPAGGALAVDRHDFAGYITD 107
Cdd:COG0644   60 gARFYSPGGKSVELPPGRGGGYVVD 84
PRK12834 PRK12834
putative FAD-binding dehydrogenase; Reviewed
 1-35 3.06e-03

putative FAD-binding dehydrogenase; Reviewed


Pssm-ID: 183782 [Multi-domain]  Cd Length: 549  Bit Score: 39.88  E-value: 3.06e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 515741997   1 MSQTVNVIGAGLAGSEAAYQLAERGIKVNLIEMRP 35
Cdd:PRK12834   3 MDADVIVVGAGLAGLVAAAELADAGKRVLLLDQEN 37
FAD_binding_2 pfam00890
FAD binding domain; This family includes members that bind FAD. This family includes the ...
 7-32 4.29e-03

FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.


Pssm-ID: 395718 [Multi-domain]  Cd Length: 398  Bit Score: 39.19  E-value: 4.29e-03
                          10        20
                  ....*....|....*....|....*.
gi 515741997    7 VIGAGLAGSEAAYQLAERGIKVNLIE 32
Cdd:pfam00890   4 VIGGGLAGLAAALAAAEAGLKVAVVE 29
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 7-35 4.34e-03

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 425450 [Multi-domain]  Cd Length: 80  Bit Score: 36.03  E-value: 4.34e-03
                          10        20
                  ....*....|....*....|....*....
gi 515741997    7 VIGAGLAGSEAAYQLAERGIKVNLIEMRP 35
Cdd:pfam00070   4 VVGGGYIGLELAGALARLGSKVTVVERRD 32
solA PRK11259
N-methyl-L-tryptophan oxidase;
5-42 4.59e-03

N-methyl-L-tryptophan oxidase;


Pssm-ID: 236887 [Multi-domain]  Cd Length: 376  Bit Score: 39.05  E-value: 4.59e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 515741997   5 VNVIGAGLAGSEAAYQLAERGIKVNLIEmrpvKQTPAH 42
Cdd:PRK11259   6 VIVIGLGSMGSAAGYYLARRGLRVLGLD----RFMPPH 39
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 1-35 6.01e-03

2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 440419 [Multi-domain]  Cd Length: 326  Bit Score: 38.38  E-value: 6.01e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 515741997   1 MSQTVNVIGAGLAGSEAAYQLAERGIKVNLIEMRP 35
Cdd:COG0654    2 MRTDVLIVGGGPAGLALALALARAGIRVTVVERAP 36
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 5-35 6.01e-03

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 39.09  E-value: 6.01e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 515741997   5 VNVIGAGLAGSEAAYQLAERGIKVNLIEMRP 35
Cdd:PRK12771 140 VAVIGGGPAGLSAAYHLRRMGHAVTIFEAGP 170
soxA_mon TIGR01377
sarcosine oxidase, monomeric form; Sarcosine oxidase catalyzes the oxidative demethylation of ...
 5-32 7.10e-03

sarcosine oxidase, monomeric form; Sarcosine oxidase catalyzes the oxidative demethylation of sarcosine to glycine. The reaction converts tetrahydrofolate to 5,10-methylene-tetrahydrofolate. The enzyme is known in monomeric and heterotetrameric (alpha,beta,gamma,delta) forms [Energy metabolism, Amino acids and amines]


Pssm-ID: 130444 [Multi-domain]  Cd Length: 380  Bit Score: 38.27  E-value: 7.10e-03
                          10        20
                  ....*....|....*....|....*...
gi 515741997    5 VNVIGAGLAGSEAAYQLAERGIKVNLIE 32
Cdd:TIGR01377   3 VIVVGAGIMGCFAAYHLAKHGKKTLLLE 30
 
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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