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Conserved domains on  [gi|515929286|ref|WP_017359869|]
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MULTISPECIES: tRNA uridine-5-carboxymethylaminomethyl(34) synthesis enzyme MnmG [Bacillus]

Protein Classification

tRNA uridine-5-carboxymethylaminomethyl modification enzyme MnmG/GidA( domain architecture ID 11418560)

tRNA uridine-5-carboxymethylaminomethyl modification enzyme MnmG/GidA such as tRNA uridine-5-carboxymethylaminomethyl(34) synthesis enzyme MnmG, which is involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MnmG COG0445
tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal ...
3-627 0e+00

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: 1251.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286   3 YEAGQYDVIVVGAGHAGVEAALASARQGAKTLVLTINLDMVAFMPCNPSVGGPAKGIVVREIDALGGEMARNIDKTHIQM 82
Cdd:COG0445    2 YYPKEYDVIVVGGGHAGCEAALAAARMGAKTLLLTHNLDTIGQMSCNPAIGGIAKGHLVREIDALGGEMGRAADKTGIQF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286  83 RMLNTGKGPAVRALRAQADKFQYQHEMKKTMENEPNLTMLQGMVDHLIVEDDECKGVVTQTGANYRAKSVVLTTGTFLKG 162
Cdd:COG0445   82 RMLNTSKGPAVRAPRAQADRKLYRAAMRETLENQPNLDLIQGEVEDLIVEDGRVTGVVTADGIEFRAKAVVLTTGTFLNG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 163 RIILGDLSYSSGPNNQQPSIKLSDHLAELGFDLVRFKTGTPPRVNSHSIDYSKTEIQPGDDVPRAFSYETVEYITDQLPC 242
Cdd:COG0445  162 LIHIGEKSYPGGRAGEPPSVGLSESLRELGFELGRLKTGTPPRIDGRSIDFSKLEEQPGDEPPPPFSFLTEKIHPPQIPC 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 243 WLTYTSLETHQIIDENLHRSPMYSGMIKGTGPRYCPSIEDKVVRFNDKPRHQIFLEPEGRNTQEVYVQGLSTSLPEDVQQ 322
Cdd:COG0445  242 WITYTNEETHEIIRENLHRSPMYSGVIEGVGPRYCPSIEDKIVRFADKDRHQIFLEPEGLDTNEVYPNGISTSLPEDVQL 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 323 RMLSTIPGLENVQMMRAGYAIEYDAIVPTQLWPTLETKKISGLYTAGQINGTSGYEEAAGQGIMAGINAGRKALGKEEVI 402
Cdd:COG0445  322 AMLRSIPGLENAEILRPGYAIEYDYVDPTQLKPTLETKKIEGLFFAGQINGTTGYEEAAAQGLMAGINAALKAQGKEPFI 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 403 LSRSDAYIGVLIDDLVTKGTNEPYRLLTSRAEYRLLLRHDNADLRLTELGYNIGLISEERFQAFTQKKEAIEAEKKRLYS 482
Cdd:COG0445  402 LDRSEAYIGVLIDDLVTKGTDEPYRMFTSRAEYRLLLRQDNADLRLTEKGYELGLVSDERYERFEEKKEAIEEEIERLKS 481
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 483 VIIKPTAETQEYIRSLGGSELKDGIRASDLMKRPEMNYESVVKLAPADTQLPADVCEQVEIQIKYEGYIEKSLQQVEKLK 562
Cdd:COG0445  482 TRVTPNEEVNEGLEELGSSPLKRGVSLFDLLRRPEITYEDLAELDPELPDLDPEVAEQVEIEIKYEGYIERQEEEIEKLK 561
                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515929286 563 KMENKKIPDRIDYDAIKGIATEAKQKLKEVRPLSVAQASRISGVNPADISILLVYLEQGRIAKIA 627
Cdd:COG0445  562 RLENLKIPEDFDYDAIPGLSNEAREKLKKIRPETLGQASRISGVTPADISLLLVYLKRRRRRKKA 626
 
Name Accession Description Interval E-value
MnmG COG0445
tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal ...
3-627 0e+00

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: 1251.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286   3 YEAGQYDVIVVGAGHAGVEAALASARQGAKTLVLTINLDMVAFMPCNPSVGGPAKGIVVREIDALGGEMARNIDKTHIQM 82
Cdd:COG0445    2 YYPKEYDVIVVGGGHAGCEAALAAARMGAKTLLLTHNLDTIGQMSCNPAIGGIAKGHLVREIDALGGEMGRAADKTGIQF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286  83 RMLNTGKGPAVRALRAQADKFQYQHEMKKTMENEPNLTMLQGMVDHLIVEDDECKGVVTQTGANYRAKSVVLTTGTFLKG 162
Cdd:COG0445   82 RMLNTSKGPAVRAPRAQADRKLYRAAMRETLENQPNLDLIQGEVEDLIVEDGRVTGVVTADGIEFRAKAVVLTTGTFLNG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 163 RIILGDLSYSSGPNNQQPSIKLSDHLAELGFDLVRFKTGTPPRVNSHSIDYSKTEIQPGDDVPRAFSYETVEYITDQLPC 242
Cdd:COG0445  162 LIHIGEKSYPGGRAGEPPSVGLSESLRELGFELGRLKTGTPPRIDGRSIDFSKLEEQPGDEPPPPFSFLTEKIHPPQIPC 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 243 WLTYTSLETHQIIDENLHRSPMYSGMIKGTGPRYCPSIEDKVVRFNDKPRHQIFLEPEGRNTQEVYVQGLSTSLPEDVQQ 322
Cdd:COG0445  242 WITYTNEETHEIIRENLHRSPMYSGVIEGVGPRYCPSIEDKIVRFADKDRHQIFLEPEGLDTNEVYPNGISTSLPEDVQL 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 323 RMLSTIPGLENVQMMRAGYAIEYDAIVPTQLWPTLETKKISGLYTAGQINGTSGYEEAAGQGIMAGINAGRKALGKEEVI 402
Cdd:COG0445  322 AMLRSIPGLENAEILRPGYAIEYDYVDPTQLKPTLETKKIEGLFFAGQINGTTGYEEAAAQGLMAGINAALKAQGKEPFI 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 403 LSRSDAYIGVLIDDLVTKGTNEPYRLLTSRAEYRLLLRHDNADLRLTELGYNIGLISEERFQAFTQKKEAIEAEKKRLYS 482
Cdd:COG0445  402 LDRSEAYIGVLIDDLVTKGTDEPYRMFTSRAEYRLLLRQDNADLRLTEKGYELGLVSDERYERFEEKKEAIEEEIERLKS 481
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 483 VIIKPTAETQEYIRSLGGSELKDGIRASDLMKRPEMNYESVVKLAPADTQLPADVCEQVEIQIKYEGYIEKSLQQVEKLK 562
Cdd:COG0445  482 TRVTPNEEVNEGLEELGSSPLKRGVSLFDLLRRPEITYEDLAELDPELPDLDPEVAEQVEIEIKYEGYIERQEEEIEKLK 561
                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515929286 563 KMENKKIPDRIDYDAIKGIATEAKQKLKEVRPLSVAQASRISGVNPADISILLVYLEQGRIAKIA 627
Cdd:COG0445  562 RLENLKIPEDFDYDAIPGLSNEAREKLKKIRPETLGQASRISGVTPADISLLLVYLKRRRRRKKA 626
gidA TIGR00136
glucose-inhibited division protein A; GidA, the longer of two forms of GidA-related proteins, ...
8-622 0e+00

glucose-inhibited division protein A; GidA, the longer of two forms of GidA-related proteins, appears to be present in all complete eubacterial genomes so far, as well as Saccharomyces cerevisiae. A subset of these organisms have a closely related protein. GidA is absent in the Archaea. It appears to act with MnmE, in an alpha2/beta2 heterotetramer, in the 5-carboxymethylaminomethyl modification of uridine 34 in certain tRNAs. The shorter, related protein, previously called gid or gidA(S), is now called TrmFO (see model TIGR00137). [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 272927 [Multi-domain]  Cd Length: 616  Bit Score: 1091.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286    8 YDVIVVGAGHAGVEAALASARQGAKTLVLTINLDMVAFMPCNPSVGGPAKGIVVREIDALGGEMARNIDKTHIQMRMLNT 87
Cdd:TIGR00136   1 FDVIVIGGGHAGCEAALAAARLGAKTLLLTLNLDTIGKCSCNPAIGGPAKGILVKEIDALGGEMGKAADKTGLQFRVLNS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286   88 GKGPAVRALRAQADKFQYQHEMKKTMENEPNLTMLQGMVDHLIVED-DECKGVVTQTGANYRAKSVVLTTGTFLKGRIIL 166
Cdd:TIGR00136  81 SKGPAVRATRAQIDKILYQKWMRNQLENQPNLSLFQGEVEDLILEDnDEIKGVVTKDGNEFRAKAVIITTGTFLRGKIHI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286  167 GDLSYSSGPNNQQPSIKLSDHLAELGFDLVRFKTGTPPRVNSHSIDYSKTEIQPGDDVPRAFSYETVEYITDQLPCWLTY 246
Cdd:TIGR00136 161 GDKSYEAGRAGEQASYGLSTTLRELGFKTGRLKTGTPPRIDKRSIDFSKLEVQFGDTQPPAFSFTNKNFLPQQLPCYLTH 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286  247 TSLETHQIIDENLHRSPMYSGMIKGTGPRYCPSIEDKVVRFNDKPRHQIFLEPEGRNTQEVYVQGLSTSLPEDVQQRMLS 326
Cdd:TIGR00136 241 TNPKTHQIIRDNLHRSPMYSGSIEGNGPRYCPSIEDKVVRFADKERHQIFLEPEGLNSDEIYLNGLSTSLPEDVQLKIIR 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286  327 TIPGLENVQMMRAGYAIEYDAIVPTQLWPTLETKKISGLYTAGQINGTSGYEEAAGQGIMAGINAGRKALGKEEVILSRS 406
Cdd:TIGR00136 321 SIPGLENAEILRPGYAIEYDYFDPTQLKPTLETKLIKGLFFAGQINGTTGYEEAAAQGLMAGINAALKLQNKEPFILKRN 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286  407 DAYIGVLIDDLVTKGTNEPYRLLTSRAEYRLLLRHDNADLRLTELGYNIGLISEERFQAFTQKKEAIEAEKKRLYSVIIK 486
Cdd:TIGR00136 401 EAYIGVLIDDLVTKGTKEPYRMFTSRAEYRLLLREDNADFRLTEIGRELGLIDEDRYARFLKKKQNIEEEIERLKSTRLS 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286  487 PTAETQEYIRSLGGSELKDGIRASDLMKRPEMNYESVVKLAPADTQLPADVCEQVEIQIKYEGYIEKSLQQVEKLKKMEN 566
Cdd:TIGR00136 481 PSKEVKEELKNLAQSPLKDEVSGYDLLKRPEMNLDKLTKLLPFLPPLDEEVLEQVEIEIKYEGYIKKQQQYIKKLDRLEN 560
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 515929286  567 KKIPDRIDYDAIKGIATEAKQKLKEVRPLSVAQASRISGVNPADISILLVYLEQGR 622
Cdd:TIGR00136 561 VKIPADFDYRKIPGLSTEAREKLSKFRPLSLGQASRISGINPADISALLVYLKKQK 616
GIDA pfam01134
Glucose inhibited division protein A;
9-399 0e+00

Glucose inhibited division protein A;


Pssm-ID: 250388 [Multi-domain]  Cd Length: 391  Bit Score: 689.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286    9 DVIVVGAGHAGVEAALASARQGAKTLVLTINLDMVAFMPCNPSVGGPAKGIVVREIDALGGEMARNIDKTHIQMRMLNTG 88
Cdd:pfam01134   1 DVIVIGGGHAGCEAALAAARMGAKVLLITHNTDTIAELSCNPSIGGIAKGHLVREIDALGGLMGKAADKTGIQFRMLNTS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286   89 KGPAVRALRAQADKFQYQHEMKKTMENEPNLTMLQGMVDHLIVEDDECKGVVTQTGANYRAKSVVLTTGTFLKGRIILGD 168
Cdd:pfam01134  81 KGPAVRALRAQVDRDLYSKEMTETLENHPNLTLIQGEVTDLIPENGKVKGVVTEDGEEYKAKAVVLATGTFLNGKIHIGL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286  169 LSYSSGPNNQQPSIKLSDHLAELGFDLVRFKTGTPPRVNSHSIDYSKTEIQPGDDVPRAFSYETVEYITDQLPCWLTYTS 248
Cdd:pfam01134 161 KCYPAGRLGELTSEGLSESLKELGFELGRFKTGTPPRIDKDSIDFSKLEEQPGDKPGPPFSYLNCPMNKEQYPCFLTYTN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286  249 LETHQIIDENLHRSPMYSGMIKGTGPRYCPSIEDKVVRFNDKPRHQIFLEPEGRNTQEVYVQGLSTSLPEDVQQRMLSTI 328
Cdd:pfam01134 241 EATHEIIRDNLHRSPMFEGCIEGIGPRYCPSIEDKPVRFADKPYHQVFLEPEGLDTDEYYLVGFSTSLPEDVQKRVLRTI 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515929286  329 PGLENVQMMRAGYAIEYDAIVPTQLWPTLETKKISGLYTAGQINGTSGYEEAAGQGIMAGINAGRKALGKE 399
Cdd:pfam01134 321 PGLENAEIVRPGYAIEYDYIDPPQLLPTLETKKIPGLFFAGQINGTEGYEEAAAQGLLAGINAARKALGKE 391
PRK05335 PRK05335
tRNA (uracil-5-)-methyltransferase Gid; Reviewed
311-414 6.35e-18

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


Pssm-ID: 235416  Cd Length: 436  Bit Score: 86.74  E-value: 6.35e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 311 GLSTSL--PEdvQQRMLSTIPGLENVQMMRAGyaieydaiV---------PTQLWPTLETKKISGLYTAGQINGTSGYEE 379
Cdd:PRK05335 278 GFQTKLkwGE--QKRVFRMIPGLENAEFVRYG--------VmhrntfinsPKLLDPTLQLKKRPNLFFAGQITGVEGYVE 347
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 515929286 380 AAGQGIMAGINAGRKALGKEEVILSRSDAyIGVLI 414
Cdd:PRK05335 348 SAASGLLAGINAARLALGKEPVIPPPTTA-LGALL 381
 
Name Accession Description Interval E-value
MnmG COG0445
tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal ...
3-627 0e+00

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: 1251.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286   3 YEAGQYDVIVVGAGHAGVEAALASARQGAKTLVLTINLDMVAFMPCNPSVGGPAKGIVVREIDALGGEMARNIDKTHIQM 82
Cdd:COG0445    2 YYPKEYDVIVVGGGHAGCEAALAAARMGAKTLLLTHNLDTIGQMSCNPAIGGIAKGHLVREIDALGGEMGRAADKTGIQF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286  83 RMLNTGKGPAVRALRAQADKFQYQHEMKKTMENEPNLTMLQGMVDHLIVEDDECKGVVTQTGANYRAKSVVLTTGTFLKG 162
Cdd:COG0445   82 RMLNTSKGPAVRAPRAQADRKLYRAAMRETLENQPNLDLIQGEVEDLIVEDGRVTGVVTADGIEFRAKAVVLTTGTFLNG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 163 RIILGDLSYSSGPNNQQPSIKLSDHLAELGFDLVRFKTGTPPRVNSHSIDYSKTEIQPGDDVPRAFSYETVEYITDQLPC 242
Cdd:COG0445  162 LIHIGEKSYPGGRAGEPPSVGLSESLRELGFELGRLKTGTPPRIDGRSIDFSKLEEQPGDEPPPPFSFLTEKIHPPQIPC 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 243 WLTYTSLETHQIIDENLHRSPMYSGMIKGTGPRYCPSIEDKVVRFNDKPRHQIFLEPEGRNTQEVYVQGLSTSLPEDVQQ 322
Cdd:COG0445  242 WITYTNEETHEIIRENLHRSPMYSGVIEGVGPRYCPSIEDKIVRFADKDRHQIFLEPEGLDTNEVYPNGISTSLPEDVQL 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 323 RMLSTIPGLENVQMMRAGYAIEYDAIVPTQLWPTLETKKISGLYTAGQINGTSGYEEAAGQGIMAGINAGRKALGKEEVI 402
Cdd:COG0445  322 AMLRSIPGLENAEILRPGYAIEYDYVDPTQLKPTLETKKIEGLFFAGQINGTTGYEEAAAQGLMAGINAALKAQGKEPFI 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 403 LSRSDAYIGVLIDDLVTKGTNEPYRLLTSRAEYRLLLRHDNADLRLTELGYNIGLISEERFQAFTQKKEAIEAEKKRLYS 482
Cdd:COG0445  402 LDRSEAYIGVLIDDLVTKGTDEPYRMFTSRAEYRLLLRQDNADLRLTEKGYELGLVSDERYERFEEKKEAIEEEIERLKS 481
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 483 VIIKPTAETQEYIRSLGGSELKDGIRASDLMKRPEMNYESVVKLAPADTQLPADVCEQVEIQIKYEGYIEKSLQQVEKLK 562
Cdd:COG0445  482 TRVTPNEEVNEGLEELGSSPLKRGVSLFDLLRRPEITYEDLAELDPELPDLDPEVAEQVEIEIKYEGYIERQEEEIEKLK 561
                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515929286 563 KMENKKIPDRIDYDAIKGIATEAKQKLKEVRPLSVAQASRISGVNPADISILLVYLEQGRIAKIA 627
Cdd:COG0445  562 RLENLKIPEDFDYDAIPGLSNEAREKLKKIRPETLGQASRISGVTPADISLLLVYLKRRRRRKKA 626
gidA TIGR00136
glucose-inhibited division protein A; GidA, the longer of two forms of GidA-related proteins, ...
8-622 0e+00

glucose-inhibited division protein A; GidA, the longer of two forms of GidA-related proteins, appears to be present in all complete eubacterial genomes so far, as well as Saccharomyces cerevisiae. A subset of these organisms have a closely related protein. GidA is absent in the Archaea. It appears to act with MnmE, in an alpha2/beta2 heterotetramer, in the 5-carboxymethylaminomethyl modification of uridine 34 in certain tRNAs. The shorter, related protein, previously called gid or gidA(S), is now called TrmFO (see model TIGR00137). [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 272927 [Multi-domain]  Cd Length: 616  Bit Score: 1091.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286    8 YDVIVVGAGHAGVEAALASARQGAKTLVLTINLDMVAFMPCNPSVGGPAKGIVVREIDALGGEMARNIDKTHIQMRMLNT 87
Cdd:TIGR00136   1 FDVIVIGGGHAGCEAALAAARLGAKTLLLTLNLDTIGKCSCNPAIGGPAKGILVKEIDALGGEMGKAADKTGLQFRVLNS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286   88 GKGPAVRALRAQADKFQYQHEMKKTMENEPNLTMLQGMVDHLIVED-DECKGVVTQTGANYRAKSVVLTTGTFLKGRIIL 166
Cdd:TIGR00136  81 SKGPAVRATRAQIDKILYQKWMRNQLENQPNLSLFQGEVEDLILEDnDEIKGVVTKDGNEFRAKAVIITTGTFLRGKIHI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286  167 GDLSYSSGPNNQQPSIKLSDHLAELGFDLVRFKTGTPPRVNSHSIDYSKTEIQPGDDVPRAFSYETVEYITDQLPCWLTY 246
Cdd:TIGR00136 161 GDKSYEAGRAGEQASYGLSTTLRELGFKTGRLKTGTPPRIDKRSIDFSKLEVQFGDTQPPAFSFTNKNFLPQQLPCYLTH 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286  247 TSLETHQIIDENLHRSPMYSGMIKGTGPRYCPSIEDKVVRFNDKPRHQIFLEPEGRNTQEVYVQGLSTSLPEDVQQRMLS 326
Cdd:TIGR00136 241 TNPKTHQIIRDNLHRSPMYSGSIEGNGPRYCPSIEDKVVRFADKERHQIFLEPEGLNSDEIYLNGLSTSLPEDVQLKIIR 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286  327 TIPGLENVQMMRAGYAIEYDAIVPTQLWPTLETKKISGLYTAGQINGTSGYEEAAGQGIMAGINAGRKALGKEEVILSRS 406
Cdd:TIGR00136 321 SIPGLENAEILRPGYAIEYDYFDPTQLKPTLETKLIKGLFFAGQINGTTGYEEAAAQGLMAGINAALKLQNKEPFILKRN 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286  407 DAYIGVLIDDLVTKGTNEPYRLLTSRAEYRLLLRHDNADLRLTELGYNIGLISEERFQAFTQKKEAIEAEKKRLYSVIIK 486
Cdd:TIGR00136 401 EAYIGVLIDDLVTKGTKEPYRMFTSRAEYRLLLREDNADFRLTEIGRELGLIDEDRYARFLKKKQNIEEEIERLKSTRLS 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286  487 PTAETQEYIRSLGGSELKDGIRASDLMKRPEMNYESVVKLAPADTQLPADVCEQVEIQIKYEGYIEKSLQQVEKLKKMEN 566
Cdd:TIGR00136 481 PSKEVKEELKNLAQSPLKDEVSGYDLLKRPEMNLDKLTKLLPFLPPLDEEVLEQVEIEIKYEGYIKKQQQYIKKLDRLEN 560
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 515929286  567 KKIPDRIDYDAIKGIATEAKQKLKEVRPLSVAQASRISGVNPADISILLVYLEQGR 622
Cdd:TIGR00136 561 VKIPADFDYRKIPGLSTEAREKLSKFRPLSLGQASRISGINPADISALLVYLKKQK 616
GIDA pfam01134
Glucose inhibited division protein A;
9-399 0e+00

Glucose inhibited division protein A;


Pssm-ID: 250388 [Multi-domain]  Cd Length: 391  Bit Score: 689.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286    9 DVIVVGAGHAGVEAALASARQGAKTLVLTINLDMVAFMPCNPSVGGPAKGIVVREIDALGGEMARNIDKTHIQMRMLNTG 88
Cdd:pfam01134   1 DVIVIGGGHAGCEAALAAARMGAKVLLITHNTDTIAELSCNPSIGGIAKGHLVREIDALGGLMGKAADKTGIQFRMLNTS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286   89 KGPAVRALRAQADKFQYQHEMKKTMENEPNLTMLQGMVDHLIVEDDECKGVVTQTGANYRAKSVVLTTGTFLKGRIILGD 168
Cdd:pfam01134  81 KGPAVRALRAQVDRDLYSKEMTETLENHPNLTLIQGEVTDLIPENGKVKGVVTEDGEEYKAKAVVLATGTFLNGKIHIGL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286  169 LSYSSGPNNQQPSIKLSDHLAELGFDLVRFKTGTPPRVNSHSIDYSKTEIQPGDDVPRAFSYETVEYITDQLPCWLTYTS 248
Cdd:pfam01134 161 KCYPAGRLGELTSEGLSESLKELGFELGRFKTGTPPRIDKDSIDFSKLEEQPGDKPGPPFSYLNCPMNKEQYPCFLTYTN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286  249 LETHQIIDENLHRSPMYSGMIKGTGPRYCPSIEDKVVRFNDKPRHQIFLEPEGRNTQEVYVQGLSTSLPEDVQQRMLSTI 328
Cdd:pfam01134 241 EATHEIIRDNLHRSPMFEGCIEGIGPRYCPSIEDKPVRFADKPYHQVFLEPEGLDTDEYYLVGFSTSLPEDVQKRVLRTI 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515929286  329 PGLENVQMMRAGYAIEYDAIVPTQLWPTLETKKISGLYTAGQINGTSGYEEAAGQGIMAGINAGRKALGKE 399
Cdd:pfam01134 321 PGLENAEIVRPGYAIEYDYIDPPQLLPTLETKKIPGLFFAGQINGTEGYEEAAAQGLLAGINAARKALGKE 391
GIDA_C pfam13932
tRNA modifying enzyme MnmG/GidA C-terminal domain; The GidA associated domain is a domain that ...
401-615 3.69e-128

tRNA modifying enzyme MnmG/GidA C-terminal domain; The GidA associated domain is a domain that has been identified at the C-terminus of protein GidA. It consists of several helices, the last three being rather short and forming small bundle. GidA is an tRNA modification enzyme found in bacteria and mitochondrial. Based on mutational analysis this domain has been suggested to be implicated in binding of the D-stem of tRNA and to be responsible for the interaction with protein MnmE. Structures of GidA in complex with either tRNA or MnmE are missing. Reported to bind to Pfam family MnmE, pfam12631.


Pssm-ID: 464049 [Multi-domain]  Cd Length: 214  Bit Score: 375.95  E-value: 3.69e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286  401 VILSRSDAYIGVLIDDLVTKGTNEPYRLLTSRAEYRLLLRHDNADLRLTELGYNIGLISEERFQAFTQKKEAIEAEKKRL 480
Cdd:pfam13932   1 LILSRSEAYIGVLIDDLVTKGTSEPYRMFTSRAEYRLLLRQDNADLRLTEKGRELGLVSDERYERFEEKKEAIEEEIERL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286  481 YSVIIKPTAETQEYIrSLGGSELKDGIRASDLMKRPEMNYESVVKLAPADTQLPADVCEQVEIQIKYEGYIEKSLQQVEK 560
Cdd:pfam13932  81 KSTRLSPSEWNNALL-ELGSAPLGTGRSAFDLLRRPEVTYEDLAALIPELAPLDPEVLEQVEIEAKYEGYIERQEAEIEK 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 515929286  561 LKKMENKKIPDRIDYDAIKGIATEAKQKLKEVRPLSVAQASRISGVNPADISILL 615
Cdd:pfam13932 160 FKRLENLKIPEDLDYDAIPGLSNEAREKLNKIRPETIGQASRISGVTPADISVLL 214
PRK05335 PRK05335
tRNA (uracil-5-)-methyltransferase Gid; Reviewed
311-414 6.35e-18

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


Pssm-ID: 235416  Cd Length: 436  Bit Score: 86.74  E-value: 6.35e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 311 GLSTSL--PEdvQQRMLSTIPGLENVQMMRAGyaieydaiV---------PTQLWPTLETKKISGLYTAGQINGTSGYEE 379
Cdd:PRK05335 278 GFQTKLkwGE--QKRVFRMIPGLENAEFVRYG--------VmhrntfinsPKLLDPTLQLKKRPNLFFAGQITGVEGYVE 347
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 515929286 380 AAGQGIMAGINAGRKALGKEEVILSRSDAyIGVLI 414
Cdd:PRK05335 348 SAASGLLAGINAARLALGKEPVIPPPTTA-LGALL 381
TrmFO COG1206
Folate-dependent tRNA-U54 methylase TrmFO/GidA [Translation, ribosomal structure and ...
321-414 3.58e-17

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: 84.34  E-value: 3.58e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 321 QQRMLSTIPGLENVQMMRAGyaieydaiV---------PTQLWPTLETKKISGLYTAGQINGTSGYEEAAGQGIMAGINA 391
Cdd:COG1206  288 QKRVFRMIPGLENAEFVRYG--------VmhrntfinsPKLLDPTLQLKARPNLFFAGQITGVEGYVESAASGLLAGINA 359
                         90       100
                 ....*....|....*....|...
gi 515929286 392 GRKALGKEEVILSRSDAyIGVLI 414
Cdd:COG1206  360 ARLLLGKEPVPPPPTTA-LGALL 381
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
8-157 3.69e-10

Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 61.29  E-value: 3.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286   8 YDVIVVGAGHAGVEAALASARQGAKTLVLtinldmvafmpcnpsvggpakgivvrEIDALGGEMAR-----NI--DKTHI 80
Cdd:COG0492    1 YDVVIIGAGPAGLTAAIYAARAGLKTLVI--------------------------EGGEPGGQLATtkeieNYpgFPEGI 54
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515929286  81 QmrmlntgkGPA-VRALRAQADKFqyqhemkktmenepNLTMLQGMVDHlIVEDDECKGVVTQTGANYRAKSVVLTTG 157
Cdd:COG0492   55 S--------GPElAERLREQAERF--------------GAEILLEEVTS-VDKDDGPFRVTTDDGTEYEAKAVIIATG 109
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
7-157 6.55e-09

Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 440673 [Multi-domain]  Cd Length: 443  Bit Score: 58.31  E-value: 6.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286   7 QYDVIVVGAGHAGVEAALASARQGAKTLVLT---------------INL-------------------DMVAFM--PCNP 50
Cdd:COG1053    3 EYDVVVVGSGGAGLRAALEAAEAGLKVLVLEkvpprgghtaaaqggINAagtnvqkaagedspeehfyDTVKGGdgLADQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286  51 SV------GGPAkgiVVREIDALGGEMARNIDKTHIQM------RMLNTGK--GPA-VRALRAQADK----FQYQHEMKK 111
Cdd:COG1053   83 DLvealaeEAPE---AIDWLEAQGVPFSRTPDGRLPQFgghsvgRTCYAGDgtGHAlLATLYQAALRlgveIFTETEVLD 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 515929286 112 tmenepnltmlqgmvdhLIVEDDECKGVV--TQTGA--NYRAKSVVLTTG 157
Cdd:COG1053  160 -----------------LIVDDGRVVGVVarDRTGEivRIRAKAVVLATG 192
FAD_oxidored pfam12831
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ...
9-174 2.43e-08

FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.


Pssm-ID: 432816 [Multi-domain]  Cd Length: 420  Bit Score: 56.46  E-value: 2.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286    9 DVIVVGAGHAGVEAALASARQGAKTLV----------LT---INLDMVAFMPCNPSVGGpakgiVVREIdalggeMARNI 75
Cdd:pfam12831   1 DVVVVGGGPAGVAAAIAAARAGAKVLLverrgflggmLTsglVGPDMGFYLNKEQVVGG-----IAREF------RQRLR 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286   76 DKTHIQMRMLNTGKGPAvralraqadkfqYQHE-MKKTMEN---EPNLTMLQG-MVDHLIVEDDECKGVVTQT---GANY 147
Cdd:pfam12831  70 ARGGLPGPYGLRGGWVP------------FDPEvAKAVLDEmlaEAGVTVLLHtRVVGVVKEGGRITGVTVETkggRITI 137
                         170       180
                  ....*....|....*....|....*..
gi 515929286  148 RAKSVVLTTGtflkgriiLGDLSYSSG 174
Cdd:pfam12831 138 RAKVFIDATG--------DGDLAALAG 156
PRK07843 PRK07843
3-oxosteroid 1-dehydrogenase;
1-36 5.80e-06

3-oxosteroid 1-dehydrogenase;


Pssm-ID: 236111 [Multi-domain]  Cd Length: 557  Bit Score: 49.26  E-value: 5.80e-06
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 515929286   1 MGYEAGQYDVIVVGAGHAGVEAALASARQGAKTLVL 36
Cdd:PRK07843   1 MAMTVQEYDVVVVGSGAAGMVAALTAAHRGLSTVVV 36
FAD_binding_2 pfam00890
FAD binding domain; This family includes members that bind FAD. This family includes the ...
9-159 6.99e-06

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: 48.82  E-value: 6.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286    9 DVIVVGAGHAGVEAALASARQGAKTLVLT------INLDM---VAFMPCNPSVGGPAKGIVVRE--------------ID 65
Cdd:pfam00890   1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEkgqpfgGATAWssgGIDALGNPPQGGIDSPELHPTdtlkgldeladhpyVE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286   66 AL---GGEMARNIDKTHiqMRMLNTGKGP-AVRALRAQADKFQYQHEMKKTMENEPN-----LTMLQG------------ 124
Cdd:pfam00890  81 AFveaAPEAVDWLEALG--VPFSRTEDGHlDLRPLGGLSATWRTPHDAADRRRGLGTghallARLLEGlrkagvdfqprt 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 515929286  125 MVDHLIVEDDECKGVVTQTGAN-----YRAKS-VVLTTGTF 159
Cdd:pfam00890 159 AADDLIVEDGRVTGAVVENRRNgrevrIRAIAaVLLATGGF 199
sdhA PRK07803
succinate dehydrogenase flavoprotein subunit; Reviewed
1-40 2.39e-05

succinate dehydrogenase flavoprotein subunit; Reviewed


Pssm-ID: 236101 [Multi-domain]  Cd Length: 626  Bit Score: 47.34  E-value: 2.39e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 515929286   1 MGYEAGQYDVIVVGAGHAGVEAALASARQGAKTLVLTINL 40
Cdd:PRK07803   2 TEVERHSYDVVVIGAGGAGLRAAIEARERGLRVAVVCKSL 41
PRK05329 PRK05329
glycerol-3-phosphate dehydrogenase subunit GlpB;
8-37 1.07e-04

glycerol-3-phosphate dehydrogenase subunit GlpB;


Pssm-ID: 235412  Cd Length: 422  Bit Score: 44.84  E-value: 1.07e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 515929286   8 YDVIVVGAGHAGVEAALASARQGAKTLVLT 37
Cdd:PRK05329   3 FDVLVIGGGLAGLTAALAAAEAGKRVALVA 32
PRK08274 PRK08274
FAD-dependent tricarballylate dehydrogenase TcuA;
8-36 1.26e-04

FAD-dependent tricarballylate dehydrogenase TcuA;


Pssm-ID: 236214 [Multi-domain]  Cd Length: 466  Bit Score: 44.87  E-value: 1.26e-04
                         10        20
                 ....*....|....*....|....*....
gi 515929286   8 YDVIVVGAGHAGVEAALASARQGAKTLVL 36
Cdd:PRK08274   5 VDVLVIGGGNAALCAALAAREAGASVLLL 33
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
7-36 1.65e-04

Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 44.46  E-value: 1.65e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 515929286   7 QYDVIVVGAGHAGVEAALASARQGAKTLVL 36
Cdd:COG1233    3 MYDVVVIGAGIGGLAAAALLARAGYRVTVL 32
PRK07121 PRK07121
FAD-binding protein;
8-36 2.17e-04

FAD-binding protein;


Pssm-ID: 180854 [Multi-domain]  Cd Length: 492  Bit Score: 44.11  E-value: 2.17e-04
                         10        20
                 ....*....|....*....|....*....
gi 515929286   8 YDVIVVGAGHAGVEAALASARQGAKTLVL 36
Cdd:PRK07121  21 ADVVVVGFGAAGACAAIEAAAAGARVLVL 49
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
8-39 2.23e-04

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: 400379 [Multi-domain]  Cd Length: 301  Bit Score: 43.46  E-value: 2.23e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 515929286    8 YDVIVVGAGHAGVEAALASARQGAKTLVLTIN 39
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDE 32
GG-red-SF TIGR02032
geranylgeranyl reductase family; This model represents a subfamily which includes ...
8-80 2.90e-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: 43.08  E-value: 2.90e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515929286    8 YDVIVVGAGHAGVEAALASARQGAKTLVLTINlDMVAFMPCnpsvGGPAKGIVVREIDALGGEMARNIDKTHI 80
Cdd:TIGR02032   1 YDVVVVGAGPAGASAAYRLADKGLRVLLLEKK-SFPRYKPC----GGALSPRALEELDLPGELIVNLVRGARF 68
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
7-35 3.11e-04

Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation


Pssm-ID: 440861 [Multi-domain]  Cd Length: 456  Bit Score: 43.54  E-value: 3.11e-04
                         10        20
                 ....*....|....*....|....*....
gi 515929286   7 QYDVIVVGAGHAGVEAALASARQGAKTLV 35
Cdd:COG1249    3 DYDLVVIGAGPGGYVAAIRAAQLGLKVAL 31
PRK07791 PRK07791
short chain dehydrogenase; Provisional
10-76 6.75e-04

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 41.97  E-value: 6.75e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515929286  10 VIVVGAGHA-GVEAALASARQGAKTLVltiNlDMVAFMPCNPSVGGPAKGiVVREIDALGGEMARNID 76
Cdd:PRK07791   9 VIVTGAGGGiGRAHALAFAAEGARVVV---N-DIGVGLDGSASGGSAAQA-VVDEIVAAGGEAVANGD 71
PRK07804 PRK07804
L-aspartate oxidase; Provisional
9-37 2.09e-03

L-aspartate oxidase; Provisional


Pssm-ID: 236102 [Multi-domain]  Cd Length: 541  Bit Score: 41.11  E-value: 2.09e-03
                         10        20
                 ....*....|....*....|....*....
gi 515929286   9 DVIVVGAGHAGVEAALASARQGAKTLVLT 37
Cdd:PRK07804  18 DVVVVGSGVAGLTAALAARRAGRRVLVVT 46
PRK12839 PRK12839
FAD-dependent oxidoreductase;
7-36 2.31e-03

FAD-dependent oxidoreductase;


Pssm-ID: 237223 [Multi-domain]  Cd Length: 572  Bit Score: 40.97  E-value: 2.31e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 515929286   7 QYDVIVVGAGHAGVEAALASARQGAKTLVL 36
Cdd:PRK12839   8 TYDVVVVGSGAGGLSAAVAAAYGGAKVLVV 37
HI0933_like pfam03486
HI0933-like protein;
8-36 2.61e-03

HI0933-like protein;


Pssm-ID: 427330 [Multi-domain]  Cd Length: 406  Bit Score: 40.64  E-value: 2.61e-03
                          10        20
                  ....*....|....*....|....*....
gi 515929286    8 YDVIVVGAGHAGVEAALASARQGAKTLVL 36
Cdd:pfam03486   1 FDVIVIGGGAAGLMAAISAAKRGRRVLLI 29
PRK12843 PRK12843
FAD-dependent oxidoreductase;
4-36 2.86e-03

FAD-dependent oxidoreductase;


Pssm-ID: 237225 [Multi-domain]  Cd Length: 578  Bit Score: 40.49  E-value: 2.86e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 515929286   4 EAGQYDVIVVGAGHAGVEAALASARQGAKTLVL 36
Cdd:PRK12843  13 WDAEFDVIVIGAGAAGMSAALFAAIAGLKVLLV 45
PRK15317 PRK15317
alkyl hydroperoxide reductase subunit F; Provisional
4-33 3.88e-03

alkyl hydroperoxide reductase subunit F; Provisional


Pssm-ID: 237942 [Multi-domain]  Cd Length: 517  Bit Score: 40.14  E-value: 3.88e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 515929286   4 EAGQYDVIVVGAGHAGVEAALASARQGAKT 33
Cdd:PRK15317 208 AKDPYDVLVVGGGPAGAAAAIYAARKGIRT 237
 
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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