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Conserved domains on  [gi|1051353490|gb|AOA56896|]
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tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG [Bacillus subtilis]

Protein Classification

tRNA uridine-5-carboxymethylaminomethyl(34) synthesis enzyme MnmG( domain architecture ID 11418560)

tRNA uridine-5-carboxymethylaminomethyl(34) synthesis enzyme MnmG 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

CATH:  1.10.10.1800
Gene Ontology:  GO:0030488|GO:0002098|GO:0050660
PubMed:  18565343
SCOP:  4006485

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: 1249.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490   3 YEAGQYDVIVIGAGHAGVEAALASARQGAKTLVLTINLDMVAFMPCNPSVGGPAKGIVVREIDALGGEMGRNIDKTHIQM 82
Cdd:COG0445     2 YYPKEYDVIVVGGGHAGCEAALAAARMGAKTLLLTHNLDTIGQMSCNPAIGGIAKGHLVREIDALGGEMGRAADKTGIQF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490  83 RMLNTGKGPAVRALRAQADKFQYQHEMKNTLEKEPNLTLLQGIVERLIVEDGECRGVITQTGAHYRAKAVVMTTGTYLRG 162
Cdd:COG0445    82 RMLNTSKGPAVRAPRAQADRKLYRAAMRETLENQPNLDLIQGEVEDLIVEDGRVTGVVTADGIEFRAKAVVLTTGTFLNG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490 163 RIILGDLSYSSGPNNQQPSIKLSEHLEELGFDLVRFKTGTPPRVKSDTIDYSKTEIQPGDDVPRAFSYETVEYITDQLPC 242
Cdd:COG0445   162 LIHIGEKSYPGGRAGEPPSVGLSESLRELGFELGRLKTGTPPRIDGRSIDFSKLEEQPGDEPPPPFSFLTEKIHPPQIPC 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490 243 WLTYTSPETHEIIDSNLHRSPMYSGMIKGTGPRYCPSIEDKVVRFNDKPRHQIFLEPEGRNTQEVYVQGLSTSLPEDVQQ 322
Cdd:COG0445   242 WITYTNEETHEIIRENLHRSPMYSGVIEGVGPRYCPSIEDKIVRFADKDRHQIFLEPEGLDTNEVYPNGISTSLPEDVQL 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490 323 RMLATIPGLENVQMMRAGYAIEYDAIVPTQLWPTLETKKITNLYTAGQINGTSGYEEAAGQGIMAGINAGRKALGKEEVI 402
Cdd:COG0445   322 AMLRSIPGLENAEILRPGYAIEYDYVDPTQLKPTLETKKIEGLFFAGQINGTTGYEEAAAQGLMAGINAALKAQGKEPFI 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490 403 LSRSDAYIGVLIDDLVTKGTNEPYRLLTSRAEYRLLLRHDNADLRLTEIGHRIGLISDERYAAFEKKKAAIEAEKKRLHS 482
Cdd:COG0445   402 LDRSEAYIGVLIDDLVTKGTDEPYRMFTSRAEYRLLLRQDNADLRLTEKGYELGLVSDERYERFEEKKEAIEEEIERLKS 481

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490 483 VIIKPSPENQEYIRSLGGSELKDGVRGTDLMKRPEMNYETVTKLAPPEVPVPQDVAEQVEIQVKYEGYIEKSLQQVEKLK 562
Cdd:COG0445   482 TRVTPNEEVNEGLEELGSSPLKRGVSLFDLLRRPEITYEDLAELDPELPDLDPEVAEQVEIEIKYEGYIERQEEEIEKLK 561

                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1051353490 563 KMENKKIPDRIDYDAIKGIATEARQKLKNVRPLSVAQASRISGVNPADISILLVYLEQGRIAKIA 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: 1249.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490   3 YEAGQYDVIVIGAGHAGVEAALASARQGAKTLVLTINLDMVAFMPCNPSVGGPAKGIVVREIDALGGEMGRNIDKTHIQM 82
Cdd:COG0445     2 YYPKEYDVIVVGGGHAGCEAALAAARMGAKTLLLTHNLDTIGQMSCNPAIGGIAKGHLVREIDALGGEMGRAADKTGIQF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490  83 RMLNTGKGPAVRALRAQADKFQYQHEMKNTLEKEPNLTLLQGIVERLIVEDGECRGVITQTGAHYRAKAVVMTTGTYLRG 162
Cdd:COG0445    82 RMLNTSKGPAVRAPRAQADRKLYRAAMRETLENQPNLDLIQGEVEDLIVEDGRVTGVVTADGIEFRAKAVVLTTGTFLNG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490 163 RIILGDLSYSSGPNNQQPSIKLSEHLEELGFDLVRFKTGTPPRVKSDTIDYSKTEIQPGDDVPRAFSYETVEYITDQLPC 242
Cdd:COG0445   162 LIHIGEKSYPGGRAGEPPSVGLSESLRELGFELGRLKTGTPPRIDGRSIDFSKLEEQPGDEPPPPFSFLTEKIHPPQIPC 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490 243 WLTYTSPETHEIIDSNLHRSPMYSGMIKGTGPRYCPSIEDKVVRFNDKPRHQIFLEPEGRNTQEVYVQGLSTSLPEDVQQ 322
Cdd:COG0445   242 WITYTNEETHEIIRENLHRSPMYSGVIEGVGPRYCPSIEDKIVRFADKDRHQIFLEPEGLDTNEVYPNGISTSLPEDVQL 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490 323 RMLATIPGLENVQMMRAGYAIEYDAIVPTQLWPTLETKKITNLYTAGQINGTSGYEEAAGQGIMAGINAGRKALGKEEVI 402
Cdd:COG0445   322 AMLRSIPGLENAEILRPGYAIEYDYVDPTQLKPTLETKKIEGLFFAGQINGTTGYEEAAAQGLMAGINAALKAQGKEPFI 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490 403 LSRSDAYIGVLIDDLVTKGTNEPYRLLTSRAEYRLLLRHDNADLRLTEIGHRIGLISDERYAAFEKKKAAIEAEKKRLHS 482
Cdd:COG0445   402 LDRSEAYIGVLIDDLVTKGTDEPYRMFTSRAEYRLLLRQDNADLRLTEKGYELGLVSDERYERFEEKKEAIEEEIERLKS 481

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490 483 VIIKPSPENQEYIRSLGGSELKDGVRGTDLMKRPEMNYETVTKLAPPEVPVPQDVAEQVEIQVKYEGYIEKSLQQVEKLK 562
Cdd:COG0445   482 TRVTPNEEVNEGLEELGSSPLKRGVSLFDLLRRPEITYEDLAELDPELPDLDPEVAEQVEIEIKYEGYIERQEEEIEKLK 561

                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1051353490 563 KMENKKIPDRIDYDAIKGIATEARQKLKNVRPLSVAQASRISGVNPADISILLVYLEQGRIAKIA 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: 1130.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490   8 YDVIVIGAGHAGVEAALASARQGAKTLVLTINLDMVAFMPCNPSVGGPAKGIVVREIDALGGEMGRNIDKTHIQMRMLNT 87
Cdd:TIGR00136   1 FDVIVIGGGHAGCEAALAAARLGAKTLLLTLNLDTIGKCSCNPAIGGPAKGILVKEIDALGGEMGKAADKTGLQFRVLNS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490  88 GKGPAVRALRAQADKFQYQHEMKNTLEKEPNLTLLQGIVERLIVED-GECRGVITQTGAHYRAKAVVMTTGTYLRGRIIL 166
Cdd:TIGR00136  81 SKGPAVRATRAQIDKILYQKWMRNQLENQPNLSLFQGEVEDLILEDnDEIKGVVTKDGNEFRAKAVIITTGTFLRGKIHI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490 167 GDLSYSSGPNNQQPSIKLSEHLEELGFDLVRFKTGTPPRVKSDTIDYSKTEIQPGDDVPRAFSYETVEYITDQLPCWLTY 246
Cdd:TIGR00136 161 GDKSYEAGRAGEQASYGLSTTLRELGFKTGRLKTGTPPRIDKRSIDFSKLEVQFGDTQPPAFSFTNKNFLPQQLPCYLTH 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490 247 TSPETHEIIDSNLHRSPMYSGMIKGTGPRYCPSIEDKVVRFNDKPRHQIFLEPEGRNTQEVYVQGLSTSLPEDVQQRMLA 326
Cdd:TIGR00136 241 TNPKTHQIIRDNLHRSPMYSGSIEGNGPRYCPSIEDKVVRFADKERHQIFLEPEGLNSDEIYLNGLSTSLPEDVQLKIIR 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490 327 TIPGLENVQMMRAGYAIEYDAIVPTQLWPTLETKKITNLYTAGQINGTSGYEEAAGQGIMAGINAGRKALGKEEVILSRS 406
Cdd:TIGR00136 321 SIPGLENAEILRPGYAIEYDYFDPTQLKPTLETKLIKGLFFAGQINGTTGYEEAAAQGLMAGINAALKLQNKEPFILKRN 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490 407 DAYIGVLIDDLVTKGTNEPYRLLTSRAEYRLLLRHDNADLRLTEIGHRIGLISDERYAAFEKKKAAIEAEKKRLHSVIIK 486
Cdd:TIGR00136 401 EAYIGVLIDDLVTKGTKEPYRMFTSRAEYRLLLREDNADFRLTEIGRELGLIDEDRYARFLKKKQNIEEEIERLKSTRLS 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490 487 PSPENQEYIRSLGGSELKDGVRGTDLMKRPEMNYETVTKLAPPEVPVPQDVAEQVEIQVKYEGYIEKSLQQVEKLKKMEN 566
Cdd:TIGR00136 481 PSKEVKEELKNLAQSPLKDEVSGYDLLKRPEMNLDKLTKLLPFLPPLDEEVLEQVEIEIKYEGYIKKQQQYIKKLDRLEN 560

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1051353490 567 KKIPDRIDYDAIKGIATEARQKLKNVRPLSVAQASRISGVNPADISILLVYLEQGR 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: 688.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490   9 DVIVIGAGHAGVEAALASARQGAKTLVLTINLDMVAFMPCNPSVGGPAKGIVVREIDALGGEMGRNIDKTHIQMRMLNTG 88
Cdd:pfam01134   1 DVIVIGGGHAGCEAALAAARMGAKVLLITHNTDTIAELSCNPSIGGIAKGHLVREIDALGGLMGKAADKTGIQFRMLNTS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490  89 KGPAVRALRAQADKFQYQHEMKNTLEKEPNLTLLQGIVERLIVEDGECRGVITQTGAHYRAKAVVMTTGTYLRGRIILGD 168
Cdd:pfam01134  81 KGPAVRALRAQVDRDLYSKEMTETLENHPNLTLIQGEVTDLIPENGKVKGVVTEDGEEYKAKAVVLATGTFLNGKIHIGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490 169 LSYSSGPNNQQPSIKLSEHLEELGFDLVRFKTGTPPRVKSDTIDYSKTEIQPGDDVPRAFSYETVEYITDQLPCWLTYTS 248
Cdd:pfam01134 161 KCYPAGRLGELTSEGLSESLKELGFELGRFKTGTPPRIDKDSIDFSKLEEQPGDKPGPPFSYLNCPMNKEQYPCFLTYTN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490 249 PETHEIIDSNLHRSPMYSGMIKGTGPRYCPSIEDKVVRFNDKPRHQIFLEPEGRNTQEVYVQGLSTSLPEDVQQRMLATI 328
Cdd:pfam01134 241 EATHEIIRDNLHRSPMFEGCIEGIGPRYCPSIEDKPVRFADKPYHQVFLEPEGLDTDEYYLVGFSTSLPEDVQKRVLRTI 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1051353490 329 PGLENVQMMRAGYAIEYDAIVPTQLWPTLETKKITNLYTAGQINGTSGYEEAAGQGIMAGINAGRKALGKE 399
Cdd:pfam01134 321 PGLENAEIVRPGYAIEYDYIDPPQLLPTLETKKIPGLFFAGQINGTEGYEEAAAQGLLAGINAARKALGKE 391
PRK05335 PRK05335
tRNA (uracil-5-)-methyltransferase Gid; Reviewed
 311-414 8.17e-18

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


Pssm-ID: 235416  Cd Length: 436  Bit Score: 86.35  E-value: 8.17e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490 311 GLSTSL--PEdvQQRMLATIPGLENVQMMRAGyaieydaiV---------PTQLWPTLETKKITNLYTAGQINGTSGYEE 379
Cdd:PRK05335  278 GFQTKLkwGE--QKRVFRMIPGLENAEFVRYG--------VmhrntfinsPKLLDPTLQLKKRPNLFFAGQITGVEGYVE 347

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1051353490 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: 1249.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490   3 YEAGQYDVIVIGAGHAGVEAALASARQGAKTLVLTINLDMVAFMPCNPSVGGPAKGIVVREIDALGGEMGRNIDKTHIQM 82
Cdd:COG0445     2 YYPKEYDVIVVGGGHAGCEAALAAARMGAKTLLLTHNLDTIGQMSCNPAIGGIAKGHLVREIDALGGEMGRAADKTGIQF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490  83 RMLNTGKGPAVRALRAQADKFQYQHEMKNTLEKEPNLTLLQGIVERLIVEDGECRGVITQTGAHYRAKAVVMTTGTYLRG 162
Cdd:COG0445    82 RMLNTSKGPAVRAPRAQADRKLYRAAMRETLENQPNLDLIQGEVEDLIVEDGRVTGVVTADGIEFRAKAVVLTTGTFLNG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490 163 RIILGDLSYSSGPNNQQPSIKLSEHLEELGFDLVRFKTGTPPRVKSDTIDYSKTEIQPGDDVPRAFSYETVEYITDQLPC 242
Cdd:COG0445   162 LIHIGEKSYPGGRAGEPPSVGLSESLRELGFELGRLKTGTPPRIDGRSIDFSKLEEQPGDEPPPPFSFLTEKIHPPQIPC 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490 243 WLTYTSPETHEIIDSNLHRSPMYSGMIKGTGPRYCPSIEDKVVRFNDKPRHQIFLEPEGRNTQEVYVQGLSTSLPEDVQQ 322
Cdd:COG0445   242 WITYTNEETHEIIRENLHRSPMYSGVIEGVGPRYCPSIEDKIVRFADKDRHQIFLEPEGLDTNEVYPNGISTSLPEDVQL 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490 323 RMLATIPGLENVQMMRAGYAIEYDAIVPTQLWPTLETKKITNLYTAGQINGTSGYEEAAGQGIMAGINAGRKALGKEEVI 402
Cdd:COG0445   322 AMLRSIPGLENAEILRPGYAIEYDYVDPTQLKPTLETKKIEGLFFAGQINGTTGYEEAAAQGLMAGINAALKAQGKEPFI 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490 403 LSRSDAYIGVLIDDLVTKGTNEPYRLLTSRAEYRLLLRHDNADLRLTEIGHRIGLISDERYAAFEKKKAAIEAEKKRLHS 482
Cdd:COG0445   402 LDRSEAYIGVLIDDLVTKGTDEPYRMFTSRAEYRLLLRQDNADLRLTEKGYELGLVSDERYERFEEKKEAIEEEIERLKS 481

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490 483 VIIKPSPENQEYIRSLGGSELKDGVRGTDLMKRPEMNYETVTKLAPPEVPVPQDVAEQVEIQVKYEGYIEKSLQQVEKLK 562
Cdd:COG0445   482 TRVTPNEEVNEGLEELGSSPLKRGVSLFDLLRRPEITYEDLAELDPELPDLDPEVAEQVEIEIKYEGYIERQEEEIEKLK 561

                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1051353490 563 KMENKKIPDRIDYDAIKGIATEARQKLKNVRPLSVAQASRISGVNPADISILLVYLEQGRIAKIA 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: 1130.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490   8 YDVIVIGAGHAGVEAALASARQGAKTLVLTINLDMVAFMPCNPSVGGPAKGIVVREIDALGGEMGRNIDKTHIQMRMLNT 87
Cdd:TIGR00136   1 FDVIVIGGGHAGCEAALAAARLGAKTLLLTLNLDTIGKCSCNPAIGGPAKGILVKEIDALGGEMGKAADKTGLQFRVLNS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490  88 GKGPAVRALRAQADKFQYQHEMKNTLEKEPNLTLLQGIVERLIVED-GECRGVITQTGAHYRAKAVVMTTGTYLRGRIIL 166
Cdd:TIGR00136  81 SKGPAVRATRAQIDKILYQKWMRNQLENQPNLSLFQGEVEDLILEDnDEIKGVVTKDGNEFRAKAVIITTGTFLRGKIHI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490 167 GDLSYSSGPNNQQPSIKLSEHLEELGFDLVRFKTGTPPRVKSDTIDYSKTEIQPGDDVPRAFSYETVEYITDQLPCWLTY 246
Cdd:TIGR00136 161 GDKSYEAGRAGEQASYGLSTTLRELGFKTGRLKTGTPPRIDKRSIDFSKLEVQFGDTQPPAFSFTNKNFLPQQLPCYLTH 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490 247 TSPETHEIIDSNLHRSPMYSGMIKGTGPRYCPSIEDKVVRFNDKPRHQIFLEPEGRNTQEVYVQGLSTSLPEDVQQRMLA 326
Cdd:TIGR00136 241 TNPKTHQIIRDNLHRSPMYSGSIEGNGPRYCPSIEDKVVRFADKERHQIFLEPEGLNSDEIYLNGLSTSLPEDVQLKIIR 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490 327 TIPGLENVQMMRAGYAIEYDAIVPTQLWPTLETKKITNLYTAGQINGTSGYEEAAGQGIMAGINAGRKALGKEEVILSRS 406
Cdd:TIGR00136 321 SIPGLENAEILRPGYAIEYDYFDPTQLKPTLETKLIKGLFFAGQINGTTGYEEAAAQGLMAGINAALKLQNKEPFILKRN 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490 407 DAYIGVLIDDLVTKGTNEPYRLLTSRAEYRLLLRHDNADLRLTEIGHRIGLISDERYAAFEKKKAAIEAEKKRLHSVIIK 486
Cdd:TIGR00136 401 EAYIGVLIDDLVTKGTKEPYRMFTSRAEYRLLLREDNADFRLTEIGRELGLIDEDRYARFLKKKQNIEEEIERLKSTRLS 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490 487 PSPENQEYIRSLGGSELKDGVRGTDLMKRPEMNYETVTKLAPPEVPVPQDVAEQVEIQVKYEGYIEKSLQQVEKLKKMEN 566
Cdd:TIGR00136 481 PSKEVKEELKNLAQSPLKDEVSGYDLLKRPEMNLDKLTKLLPFLPPLDEEVLEQVEIEIKYEGYIKKQQQYIKKLDRLEN 560

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1051353490 567 KKIPDRIDYDAIKGIATEARQKLKNVRPLSVAQASRISGVNPADISILLVYLEQGR 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: 688.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490   9 DVIVIGAGHAGVEAALASARQGAKTLVLTINLDMVAFMPCNPSVGGPAKGIVVREIDALGGEMGRNIDKTHIQMRMLNTG 88
Cdd:pfam01134   1 DVIVIGGGHAGCEAALAAARMGAKVLLITHNTDTIAELSCNPSIGGIAKGHLVREIDALGGLMGKAADKTGIQFRMLNTS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490  89 KGPAVRALRAQADKFQYQHEMKNTLEKEPNLTLLQGIVERLIVEDGECRGVITQTGAHYRAKAVVMTTGTYLRGRIILGD 168
Cdd:pfam01134  81 KGPAVRALRAQVDRDLYSKEMTETLENHPNLTLIQGEVTDLIPENGKVKGVVTEDGEEYKAKAVVLATGTFLNGKIHIGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490 169 LSYSSGPNNQQPSIKLSEHLEELGFDLVRFKTGTPPRVKSDTIDYSKTEIQPGDDVPRAFSYETVEYITDQLPCWLTYTS 248
Cdd:pfam01134 161 KCYPAGRLGELTSEGLSESLKELGFELGRFKTGTPPRIDKDSIDFSKLEEQPGDKPGPPFSYLNCPMNKEQYPCFLTYTN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490 249 PETHEIIDSNLHRSPMYSGMIKGTGPRYCPSIEDKVVRFNDKPRHQIFLEPEGRNTQEVYVQGLSTSLPEDVQQRMLATI 328
Cdd:pfam01134 241 EATHEIIRDNLHRSPMFEGCIEGIGPRYCPSIEDKPVRFADKPYHQVFLEPEGLDTDEYYLVGFSTSLPEDVQKRVLRTI 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1051353490 329 PGLENVQMMRAGYAIEYDAIVPTQLWPTLETKKITNLYTAGQINGTSGYEEAAGQGIMAGINAGRKALGKE 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 1.14e-129

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: 379.80  E-value: 1.14e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490 401 VILSRSDAYIGVLIDDLVTKGTNEPYRLLTSRAEYRLLLRHDNADLRLTEIGHRIGLISDERYAAFEKKKAAIEAEKKRL 480
Cdd:pfam13932   1 LILSRSEAYIGVLIDDLVTKGTSEPYRMFTSRAEYRLLLRQDNADLRLTEKGRELGLVSDERYERFEEKKEAIEEEIERL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490 481 HSVIIKPSPENQEYIrSLGGSELKDGVRGTDLMKRPEMNYETVTKLAPPEVPVPQDVAEQVEIQVKYEGYIEKSLQQVEK 560
Cdd:pfam13932  81 KSTRLSPSEWNNALL-ELGSAPLGTGRSAFDLLRRPEVTYEDLAALIPELAPLDPEVLEQVEIEAKYEGYIERQEAEIEK 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1051353490 561 LKKMENKKIPDRIDYDAIKGIATEARQKLKNVRPLSVAQASRISGVNPADISILL 615
Cdd:pfam13932 160 FKRLENLKIPEDLDYDAIPGLSNEAREKLNKIRPETIGQASRISGVTPADISVLL 214
PRK05335 PRK05335
tRNA (uracil-5-)-methyltransferase Gid; Reviewed
 311-414 8.17e-18

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


Pssm-ID: 235416  Cd Length: 436  Bit Score: 86.35  E-value: 8.17e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490 311 GLSTSL--PEdvQQRMLATIPGLENVQMMRAGyaieydaiV---------PTQLWPTLETKKITNLYTAGQINGTSGYEE 379
Cdd:PRK05335  278 GFQTKLkwGE--QKRVFRMIPGLENAEFVRYG--------VmhrntfinsPKLLDPTLQLKKRPNLFFAGQITGVEGYVE 347

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1051353490 380 AAGQGIMAGINAGRKALGKEEVILSRSDAyIGVLI 414
Cdd:PRK05335  348 SAASGLLAGINAARLALGKEPVIPPPTTA-LGALL 381
TrmFO COG1206
Folate-dependent tRNA-U54 methylase TrmFO/GidA [Translation, ribosomal structure and ...
 321-414 9.03e-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: 83.19  E-value: 9.03e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490 321 QQRMLATIPGLENVQMMRAGyaieydaiV---------PTQLWPTLETKKITNLYTAGQINGTSGYEEAAGQGIMAGINA 391
Cdd:COG1206   288 QKRVFRMIPGLENAEFVRYG--------VmhrntfinsPKLLDPTLQLKARPNLFFAGQITGVEGYVESAASGLLAGINA 359

                          90       100
                  ....*....|....*....|...
gi 1051353490 392 GRKALGKEEVILSRSDAyIGVLI 414
Cdd:COG1206   360 ARLLLGKEPVPPPPTTA-LGALL 381
FAD_oxidored pfam12831
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ...
 9-174 1.18e-09

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


Pssm-ID: 432816 [Multi-domain]  Cd Length: 420  Bit Score: 60.70  E-value: 1.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490   9 DVIVIGAGHAGVEAALASARQGAKTLVLtinldmvafMPcNPSVGGpakgivvreidALGGEMGRNIDKTHIQMRMLNTG 88
Cdd:pfam12831   1 DVVVVGGGPAGVAAAIAAARAGAKVLLV---------ER-RGFLGG-----------MLTSGLVGPDMGFYLNKEQVVGG 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490  89 -----------KGPAVRALRAQADKFQYQHE-MKNTLE---KEPNLTLLQG-IVERLIVEDGECRGVITQTGAH---YRA 149
Cdd:pfam12831  60 iarefrqrlraRGGLPGPYGLRGGWVPFDPEvAKAVLDemlAEAGVTVLLHtRVVGVVKEGGRITGVTVETKGGritIRA 139

                         170       180
                  ....*....|....*....|....*
gi 1051353490 150 KAVVMTTGtylrgriiLGDLSYSSG 174
Cdd:pfam12831 140 KVFIDATG--------DGDLAALAG 156
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
 7-157 2.85e-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: 59.46  E-value: 2.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490   7 QYDVIVIGAGHAGVEAALASARQGAKTLVLT---------------INL-------------------DMVAFM--PCNP 50
Cdd:COG1053     3 EYDVVVVGSGGAGLRAALEAAEAGLKVLVLEkvpprgghtaaaqggINAagtnvqkaagedspeehfyDTVKGGdgLADQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490  51 SV------GGPAkgiVVREIDALGGEMGRNIDKTHIQM------RMLNTGK--GPA-VRALRAQADK----FQYQHEmkn 111
Cdd:COG1053    83 DLvealaeEAPE---AIDWLEAQGVPFSRTPDGRLPQFgghsvgRTCYAGDgtGHAlLATLYQAALRlgveIFTETE--- 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1051353490 112 tlekepnltllqgiVERLIVEDGECRGVI--TQTGA--HYRAKAVVMTTG 157
Cdd:COG1053   157 --------------VLDLIVDDGRVVGVVarDRTGEivRIRAKAVVLATG 192
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
8-157 1.01e-08

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 57.05  E-value: 1.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490   8 YDVIVIGAGHAGVEAALASARQGAKTLVLtinldmvafmpcnpsvggpakgivvrEIDALGGEMGR-----NI--DKTHI 80
Cdd:COG0492     1 YDVVIIGAGPAGLTAAIYAARAGLKTLVI--------------------------EGGEPGGQLATtkeieNYpgFPEGI 54

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1051353490  81 QmrmlntgkGPA-VRALRAQADKFqyqhemkntlekepNLTLLQGIVERLIVEDGECRgVITQTGAHYRAKAVVMTTG 157
Cdd:COG0492    55 S--------GPElAERLREQAERF--------------GAEILLEEVTSVDKDDGPFR-VTTDDGTEYEAKAVIIATG 109
sdhA PRK07803
succinate dehydrogenase flavoprotein subunit; Reviewed
 1-40 1.12e-05

succinate dehydrogenase flavoprotein subunit; Reviewed


Pssm-ID: 236101 [Multi-domain]  Cd Length: 626  Bit Score: 48.49  E-value: 1.12e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1051353490   1 MGYEAGQYDVIVIGAGHAGVEAALASARQGAKTLVLTINL 40
Cdd:PRK07803    2 TEVERHSYDVVVIGAGGAGLRAAIEARERGLRVAVVCKSL 41
PRK07843 PRK07843
3-oxosteroid 1-dehydrogenase;
1-36 2.25e-05

3-oxosteroid 1-dehydrogenase;


Pssm-ID: 236111 [Multi-domain]  Cd Length: 557  Bit Score: 47.34  E-value: 2.25e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1051353490   1 MGYEAGQYDVIVIGAGHAGVEAALASARQGAKTLVL 36
Cdd:PRK07843    1 MAMTVQEYDVVVVGSGAAGMVAALTAAHRGLSTVVV 36
PRK05329 PRK05329
glycerol-3-phosphate dehydrogenase subunit GlpB;
8-37 2.94e-05

glycerol-3-phosphate dehydrogenase subunit GlpB;


Pssm-ID: 235412  Cd Length: 422  Bit Score: 46.77  E-value: 2.94e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 1051353490   8 YDVIVIGAGHAGVEAALASARQGAKTLVLT 37
Cdd:PRK05329    3 FDVLVIGGGLAGLTAALAAAEAGKRVALVA 32
FAD_binding_2 pfam00890
FAD binding domain; This family includes members that bind FAD. This family includes the ...
 9-159 3.01e-05

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: 46.90  E-value: 3.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490   9 DVIVIGAGHAGVEAALASARQGAKTLVLT---------------INL--------------------------------- 40
Cdd:pfam00890   1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEkgqpfggatawssggIDAlgnppqggidspelhptdtlkgldeladhpyve 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490  41 -------DMVA-----FMPCNPSVGGPakgIVVREidaLGGEmgRNIDKTHIQM----RMLNTGKGPAVRAL-RAQADKF 103
Cdd:pfam00890  81 afveaapEAVDwlealGVPFSRTEDGH---LDLRP---LGGL--SATWRTPHDAadrrRGLGTGHALLARLLeGLRKAGV 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1051353490 104 QYQHEMkntlekepnltllqgIVERLIVEDGECRGVI-----TQTGAHYRAK-AVVMTTGTY 159
Cdd:pfam00890 153 DFQPRT---------------AADDLIVEDGRVTGAVvenrrNGREVRIRAIaAVLLATGGF 199
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 7-35 5.68e-05

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: 45.85  E-value: 5.68e-05
                          10        20
                  ....*....|....*....|....*....
gi 1051353490   7 QYDVIVIGAGHAGVEAALASARQGAKTLV 35
Cdd:COG1249     3 DYDLVVIGAGPGGYVAAIRAAQLGLKVAL 31
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 7-36 9.72e-05

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


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 45.23  E-value: 9.72e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 1051353490   7 QYDVIVIGAGHAGVEAALASARQGAKTLVL 36
Cdd:COG1233     3 MYDVVVIGAGIGGLAAAALLARAGYRVTVL 32
PRK08274 PRK08274
FAD-dependent tricarballylate dehydrogenase TcuA;
8-36 1.19e-04

FAD-dependent tricarballylate dehydrogenase TcuA;


Pssm-ID: 236214 [Multi-domain]  Cd Length: 466  Bit Score: 44.87  E-value: 1.19e-04
                          10        20
                  ....*....|....*....|....*....
gi 1051353490   8 YDVIVIGAGHAGVEAALASARQGAKTLVL 36
Cdd:PRK08274    5 VDVLVIGGGNAALCAALAAREAGASVLLL 33
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 8-39 1.46e-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: 44.23  E-value: 1.46e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1051353490   8 YDVIVIGAGHAGVEAALASARQGAKTLVLTIN 39
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDE 32
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
7-162 2.09e-04

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


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 44.13  E-value: 2.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490   7 QYDVIVIGAGHAGVEAALASARQGAKTLVltinLDmvAFMP-----------CNPSVGGPAKGIVVR-------EIDALG 68
Cdd:COG0665     2 TADVVVIGGGIAGLSTAYHLARRGLDVTV----LE--RGRPgsgasgrnagqLRPGLAALADRALVRlarealdLWRELA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490  69 GEMGRNIDktHIQMRMLNTGKGPA----VRALRAQADKFQYQHEM---KNTLEKEPNLT--------------------L 121
Cdd:COG0665    76 AELGIDCD--FRRTGVLYLARTEAelaaLRAEAEALRALGLPVELldaAELREREPGLGspdyagglydpddghvdpakL 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1051353490 122 LQGI----------------VERLIVEDGECRGVITQTGAhYRAKAVVMTTGTYLRG 162
Cdd:COG0665   154 VRALaraaraagvriregtpVTGLEREGGRVTGVRTERGT-VRADAVVLAAGAWSAR 209
GlpB COG3075
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism];
7-37 2.64e-04

Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism];


Pssm-ID: 442309  Cd Length: 415  Bit Score: 43.63  E-value: 2.64e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1051353490   7 QYDVIVIGAGHAGVEAALASARQGAKTLVLT 37
Cdd:COG3075     2 KFDVVVIGGGLAGLTAAIRAAEAGLRVAIVS 32
PRK07121 PRK07121
FAD-binding protein;
8-36 4.09e-04

FAD-binding protein;


Pssm-ID: 180854 [Multi-domain]  Cd Length: 492  Bit Score: 43.34  E-value: 4.09e-04
                          10        20
                  ....*....|....*....|....*....
gi 1051353490   8 YDVIVIGAGHAGVEAALASARQGAKTLVL 36
Cdd:PRK07121   21 ADVVVVGFGAAGACAAIEAAAAGARVLVL 49
HI0933_like pfam03486
HI0933-like protein;
8-36 6.85e-04

HI0933-like protein;


Pssm-ID: 427330 [Multi-domain]  Cd Length: 406  Bit Score: 42.57  E-value: 6.85e-04
                          10        20
                  ....*....|....*....|....*....
gi 1051353490   8 YDVIVIGAGHAGVEAALASARQGAKTLVL 36
Cdd:pfam03486   1 FDVIVIGGGAAGLMAAISAAKRGRRVLLI 29
PRK12843 PRK12843
FAD-dependent oxidoreductase;
4-36 1.24e-03

FAD-dependent oxidoreductase;


Pssm-ID: 237225 [Multi-domain]  Cd Length: 578  Bit Score: 41.65  E-value: 1.24e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1051353490   4 EAGQYDVIVIGAGHAGVEAALASARQGAKTLVL 36
Cdd:PRK12843   13 WDAEFDVIVIGAGAAGMSAALFAAIAGLKVLLV 45
GG-red-SF TIGR02032
geranylgeranyl reductase family; This model represents a subfamily which includes ...
 8-157 1.28e-03

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: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490   8 YDVIVIGAGHAGVEAALASARQGAKTLVLTINlDMVAFMPCnpsvGGPAKGIVVREIDALGGEMGRNIDKTHIQM---RM 84
Cdd:TIGR02032   1 YDVVVVGAGPAGASAAYRLADKGLRVLLLEKK-SFPRYKPC----GGALSPRALEELDLPGELIVNLVRGARFFSpngDS 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1051353490  85 LN----TGKGPAVRalRAQADKFQYQHEMKNTLEkepnlTLLQGIVERLIVEDGEcRGVITQTGAH-YRAKAVVMTTG 157
Cdd:TIGR02032  76 VEipieTELAYVID--RDAFDEQLAERAQEAGAE-----LRLGTRVLDVEIHDDR-VVVIVRGSEGtVTAKIVIGADG 145
PRK07791 PRK07791
short chain dehydrogenase; Provisional
 10-70 1.64e-03

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 40.81  E-value: 1.64e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1051353490  10 VIVIGAGHA-GVEAALASARQGAKTLVltiNlDMVAFMPCNPSVGGPAKGiVVREIDALGGE 70
Cdd:PRK07791    9 VIVTGAGGGiGRAHALAFAAEGARVVV---N-DIGVGLDGSASGGSAAQA-VVDEIVAAGGE 65
PRK06134 PRK06134
putative FAD-binding dehydrogenase; Reviewed
 4-88 2.11e-03

putative FAD-binding dehydrogenase; Reviewed


Pssm-ID: 180419 [Multi-domain]  Cd Length: 581  Bit Score: 41.24  E-value: 2.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051353490   4 EAGQYDVIVIGAGHAGVEAALASARQGAKTLVL---------TINLDMVAFMPCNPSVggpAKGIVVREIDA----LGGE 70
Cdd:PRK06134    9 PDLECDVLVIGSGAAGLSAAVTAAWHGLKVIVVekdpvfggtTAWSGGWMWIPRNPLA---RRAGIVEDIEQprtyLRHE 85

                          90
                  ....*....|....*...
gi 1051353490  71 MGRNIDKTHIQMrMLNTG 88
Cdd:PRK06134   86 LGARYDAARIDA-FLEAG 102
PRK12839 PRK12839
FAD-dependent oxidoreductase;
7-36 2.77e-03

FAD-dependent oxidoreductase;


Pssm-ID: 237223 [Multi-domain]  Cd Length: 572  Bit Score: 40.58  E-value: 2.77e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1051353490   7 QYDVIVIGAGHAGVEAALASARQGAKTLVL 36
Cdd:PRK12839    8 TYDVVVVGSGAGGLSAAVAAAYGGAKVLVV 37
PRK07804 PRK07804
L-aspartate oxidase; Provisional
 9-37 3.50e-03

L-aspartate oxidase; Provisional


Pssm-ID: 236102 [Multi-domain]  Cd Length: 541  Bit Score: 40.34  E-value: 3.50e-03
                          10        20
                  ....*....|....*....|....*....
gi 1051353490   9 DVIVIGAGHAGVEAALASARQGAKTLVLT 37
Cdd:PRK07804   18 DVVVVGSGVAGLTAALAARRAGRRVLVVT 46
PRK05249 PRK05249
Si-specific NAD(P)(+) transhydrogenase;
7-35 3.60e-03

Si-specific NAD(P)(+) transhydrogenase;


Pssm-ID: 235373 [Multi-domain]  Cd Length: 461  Bit Score: 40.14  E-value: 3.60e-03
                          10        20
                  ....*....|....*....|....*....
gi 1051353490   7 QYDVIVIGAGHAGVEAALASARQGAKTLV 35
Cdd:PRK05249    5 DYDLVVIGSGPAGEGAAMQAAKLGKRVAV 33
glycerol3P_GlpB TIGR03378
glycerol-3-phosphate dehydrogenase, anaerobic, B subunit; Members of this protein family are ...
 8-37 4.99e-03

glycerol-3-phosphate dehydrogenase, anaerobic, B subunit; Members of this protein family are the B subunit, product of the glpB gene, of a three-subunit, membrane-anchored, FAD-dependent anaerobic glycerol-3-phosphate dehydrogenase. [Energy metabolism, Anaerobic]


Pssm-ID: 213807  Cd Length: 419  Bit Score: 39.62  E-value: 4.99e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1051353490   8 YDVIVIGAGHAGVEAALASARQGAKTLVLT 37
Cdd:TIGR03378   1 FDVIIIGGGLAGLSCALRLAEAGKKCAIIA 30
PRK15317 PRK15317
alkyl hydroperoxide reductase subunit F; Provisional
 4-33 6.44e-03

alkyl hydroperoxide reductase subunit F; Provisional


Pssm-ID: 237942 [Multi-domain]  Cd Length: 517  Bit Score: 39.37  E-value: 6.44e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1051353490   4 EAGQYDVIVIGAGHAGVEAALASARQGAKT 33
Cdd:PRK15317  208 AKDPYDVLVVGGGPAGAAAAIYAARKGIRT 237
PRK07494 PRK07494
UbiH/UbiF family hydroxylase;
7-33 8.96e-03

UbiH/UbiF family hydroxylase;


Pssm-ID: 181001 [Multi-domain]  Cd Length: 388  Bit Score: 38.73  E-value: 8.96e-03
                          10        20
                  ....*....|....*....|....*..
gi 1051353490   7 QYDVIVIGAGHAGVEAALASARQGAKT 33
Cdd:PRK07494    7 HTDIAVIGGGPAGLAAAIALARAGASV 33
 
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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