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Conserved domains on  [gi|1411378793|emb|SQB88986|]
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tRNA uridine 5-carboxymethylaminomethyl modification protein GidA [Clostridium sporogenes]

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

CATH:  1.10.10.1800
EC:  2.1.1.-
Gene Ontology:  GO:0050660|GO:0002098|GO:0030488|GO:0008033
PubMed:  18565343|19801413|19767610|11544186
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 ...
 3-625 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: 1182.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793   3 YLAGDFDVVVIGAGHAGCEAALASARMGCKTLICTMNLDSIALMACNPNIGGTAKGHLVREIDALGGEMGINIDHTFIQS 82
Cdd:COG0445     2 YYPKEYDVIVVGGGHAGCEAALAAARMGAKTLLLTHNLDTIGQMSCNPAIGGIAKGHLVREIDALGGEMGRAADKTGIQF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793  83 RMLNTSKGPAVHSLRAQADKKRYSERMKHLLEKEENVTLRQLEVIEIDVEDNKVKGILTKNGAYFTTKAIILCTGTYLKG 162
Cdd:COG0445    82 RMLNTSKGPAVRAPRAQADRKLYRAAMRETLENQPNLDLIQGEVEDLIVEDGRVTGVVTADGIEFRAKAVVLTTGTFLNG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793 163 KIIIGDIIYSSGPSGLYPANDLSQSLLDLGINLRRFKTGTPARINKRSVDFSKMIEQPGDEKIVPFSFIHDKLDKDQISC 242
Cdd:COG0445   162 LIHIGEKSYPGGRAGEPPSVGLSESLRELGFELGRLKTGTPPRIDGRSIDFSKLEEQPGDEPPPPFSFLTEKIHPPQIPC 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793 243 YLTYTSEETHKIIHENIHRSPLYNGSIEGVGPRYCPSIEDKIVRFPDKDKHQIFIEPEGEDTEELYVGGMSSSLPEDVQI 322
Cdd:COG0445   242 WITYTNEETHEIIRENLHRSPMYSGVIEGVGPRYCPSIEDKIVRFADKDRHQIFLEPEGLDTNEVYPNGISTSLPEDVQL 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793 323 KMYRSVPGLENAEILRTAYAIEYDCIDPQQLDLTLEFKNINGLYGAGQFNGSSGYEEAAAQGLVAGINSVLKIKGEDPLI 402
Cdd:COG0445   322 AMLRSIPGLENAEILRPGYAIEYDYVDPTQLKPTLETKKIEGLFFAGQINGTTGYEEAAAQGLMAGINAALKAQGKEPFI 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793 403 LKRSDAYIGVLIDDLVTKGTNEPYRMMTSRAEYRLLLRQDNADLRLTELGYKMGLVKEDRYNKFINRKKNVENEVERLKN 482
Cdd:COG0445   402 LDRSEAYIGVLIDDLVTKGTDEPYRMFTSRAEYRLLLRQDNADLRLTEKGYELGLVSDERYERFEEKKEAIEEEIERLKS 481

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793 483 VQITGKREINEFLLEKGSTELKKPISLYELIKRPELDYFKVEPLDDKRPSLNDDEKEEINIIAKYEGYINKQLEQVEQFK 562
Cdd:COG0445   482 TRVTPNEEVNEGLEELGSSPLKRGVSLFDLLRRPEITYEDLAELDPELPDLDPEVAEQVEIEIKYEGYIERQEEEIEKLK 561

                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1411378793 563 KYEDRLIPKSINYPDIKGLRLEAIQKLEKIKPINIGQASRISGVSPADISVLLIYMERKNREN 625
Cdd:COG0445   562 RLENLKIPEDFDYDAIPGLSNEAREKLKKIRPETLGQASRISGVTPADISLLLVYLKRRRRRK 624
 
Name Accession Description Interval E-value
MnmG COG0445
tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal ...
 3-625 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: 1182.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793   3 YLAGDFDVVVIGAGHAGCEAALASARMGCKTLICTMNLDSIALMACNPNIGGTAKGHLVREIDALGGEMGINIDHTFIQS 82
Cdd:COG0445     2 YYPKEYDVIVVGGGHAGCEAALAAARMGAKTLLLTHNLDTIGQMSCNPAIGGIAKGHLVREIDALGGEMGRAADKTGIQF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793  83 RMLNTSKGPAVHSLRAQADKKRYSERMKHLLEKEENVTLRQLEVIEIDVEDNKVKGILTKNGAYFTTKAIILCTGTYLKG 162
Cdd:COG0445    82 RMLNTSKGPAVRAPRAQADRKLYRAAMRETLENQPNLDLIQGEVEDLIVEDGRVTGVVTADGIEFRAKAVVLTTGTFLNG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793 163 KIIIGDIIYSSGPSGLYPANDLSQSLLDLGINLRRFKTGTPARINKRSVDFSKMIEQPGDEKIVPFSFIHDKLDKDQISC 242
Cdd:COG0445   162 LIHIGEKSYPGGRAGEPPSVGLSESLRELGFELGRLKTGTPPRIDGRSIDFSKLEEQPGDEPPPPFSFLTEKIHPPQIPC 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793 243 YLTYTSEETHKIIHENIHRSPLYNGSIEGVGPRYCPSIEDKIVRFPDKDKHQIFIEPEGEDTEELYVGGMSSSLPEDVQI 322
Cdd:COG0445   242 WITYTNEETHEIIRENLHRSPMYSGVIEGVGPRYCPSIEDKIVRFADKDRHQIFLEPEGLDTNEVYPNGISTSLPEDVQL 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793 323 KMYRSVPGLENAEILRTAYAIEYDCIDPQQLDLTLEFKNINGLYGAGQFNGSSGYEEAAAQGLVAGINSVLKIKGEDPLI 402
Cdd:COG0445   322 AMLRSIPGLENAEILRPGYAIEYDYVDPTQLKPTLETKKIEGLFFAGQINGTTGYEEAAAQGLMAGINAALKAQGKEPFI 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793 403 LKRSDAYIGVLIDDLVTKGTNEPYRMMTSRAEYRLLLRQDNADLRLTELGYKMGLVKEDRYNKFINRKKNVENEVERLKN 482
Cdd:COG0445   402 LDRSEAYIGVLIDDLVTKGTDEPYRMFTSRAEYRLLLRQDNADLRLTEKGYELGLVSDERYERFEEKKEAIEEEIERLKS 481

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793 483 VQITGKREINEFLLEKGSTELKKPISLYELIKRPELDYFKVEPLDDKRPSLNDDEKEEINIIAKYEGYINKQLEQVEQFK 562
Cdd:COG0445   482 TRVTPNEEVNEGLEELGSSPLKRGVSLFDLLRRPEITYEDLAELDPELPDLDPEVAEQVEIEIKYEGYIERQEEEIEKLK 561

                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1411378793 563 KYEDRLIPKSINYPDIKGLRLEAIQKLEKIKPINIGQASRISGVSPADISVLLIYMERKNREN 625
Cdd:COG0445   562 RLENLKIPEDFDYDAIPGLSNEAREKLKKIRPETLGQASRISGVTPADISLLLVYLKRRRRRK 624
gidA TIGR00136
glucose-inhibited division protein A; GidA, the longer of two forms of GidA-related proteins, ...
 8-619 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: 888.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793   8 FDVVVIGAGHAGCEAALASARMGCKTLICTMNLDSIALMACNPNIGGTAKGHLVREIDALGGEMGINIDHTFIQSRMLNT 87
Cdd:TIGR00136   1 FDVIVIGGGHAGCEAALAAARLGAKTLLLTLNLDTIGKCSCNPAIGGPAKGILVKEIDALGGEMGKAADKTGLQFRVLNS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793  88 SKGPAVHSLRAQADKKRYSERMKHLLEKEENVTLRQLEVIEIDVEDN-KVKGILTKNGAYFTTKAIILCTGTYLKGKIII 166
Cdd:TIGR00136  81 SKGPAVRATRAQIDKILYQKWMRNQLENQPNLSLFQGEVEDLILEDNdEIKGVVTKDGNEFRAKAVIITTGTFLRGKIHI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793 167 GDIIYSSGPSGLYPANDLSQSLLDLGINLRRFKTGTPARINKRSVDFSKMIEQPGDEKIVPFSFIHDKLDKDQISCYLTY 246
Cdd:TIGR00136 161 GDKSYEAGRAGEQASYGLSTTLRELGFKTGRLKTGTPPRIDKRSIDFSKLEVQFGDTQPPAFSFTNKNFLPQQLPCYLTH 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793 247 TSEETHKIIHENIHRSPLYNGSIEGVGPRYCPSIEDKIVRFPDKDKHQIFIEPEGEDTEELYVGGMSSSLPEDVQIKMYR 326
Cdd:TIGR00136 241 TNPKTHQIIRDNLHRSPMYSGSIEGNGPRYCPSIEDKVVRFADKERHQIFLEPEGLNSDEIYLNGLSTSLPEDVQLKIIR 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793 327 SVPGLENAEILRTAYAIEYDCIDPQQLDLTLEFKNINGLYGAGQFNGSSGYEEAAAQGLVAGINSVLKIKGEDPLILKRS 406
Cdd:TIGR00136 321 SIPGLENAEILRPGYAIEYDYFDPTQLKPTLETKLIKGLFFAGQINGTTGYEEAAAQGLMAGINAALKLQNKEPFILKRN 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793 407 DAYIGVLIDDLVTKGTNEPYRMMTSRAEYRLLLRQDNADLRLTELGYKMGLVKEDRYNKFINRKKNVENEVERLKNVQIT 486
Cdd:TIGR00136 401 EAYIGVLIDDLVTKGTKEPYRMFTSRAEYRLLLREDNADFRLTEIGRELGLIDEDRYARFLKKKQNIEEEIERLKSTRLS 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793 487 GKREINEFLLEKGSTELKKPISLYELIKRPELDYFKVEPLDDKRPSLNDDEKEEINIIAKYEGYINKQLEQVEQFKKYED 566
Cdd:TIGR00136 481 PSKEVKEELKNLAQSPLKDEVSGYDLLKRPEMNLDKLTKLLPFLPPLDEEVLEQVEIEIKYEGYIKKQQQYIKKLDRLEN 560

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1411378793 567 RLIPKSINYPDIKGLRLEAIQKLEKIKPINIGQASRISGVSPADISVLLIYME 619
Cdd:TIGR00136 561 VKIPADFDYRKIPGLSTEAREKLSKFRPLSLGQASRISGINPADISALLVYLK 613
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: 641.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793   9 DVVVIGAGHAGCEAALASARMGCKTLICTMNLDSIALMACNPNIGGTAKGHLVREIDALGGEMGINIDHTFIQSRMLNTS 88
Cdd:pfam01134   1 DVIVIGGGHAGCEAALAAARMGAKVLLITHNTDTIAELSCNPSIGGIAKGHLVREIDALGGLMGKAADKTGIQFRMLNTS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793  89 KGPAVHSLRAQADKKRYSERMKHLLEKEENVTLRQLEVIEIDVEDNKVKGILTKNGAYFTTKAIILCTGTYLKGKIIIGD 168
Cdd:pfam01134  81 KGPAVRALRAQVDRDLYSKEMTETLENHPNLTLIQGEVTDLIPENGKVKGVVTEDGEEYKAKAVVLATGTFLNGKIHIGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793 169 IIYSSGPSGLYPANDLSQSLLDLGINLRRFKTGTPARINKRSVDFSKMIEQPGDEKIVPFSFIHDKLDKDQISCYLTYTS 248
Cdd:pfam01134 161 KCYPAGRLGELTSEGLSESLKELGFELGRFKTGTPPRIDKDSIDFSKLEEQPGDKPGPPFSYLNCPMNKEQYPCFLTYTN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793 249 EETHKIIHENIHRSPLYNGSIEGVGPRYCPSIEDKIVRFPDKDKHQIFIEPEGEDTEELYVGGMSSSLPEDVQIKMYRSV 328
Cdd:pfam01134 241 EATHEIIRDNLHRSPMFEGCIEGIGPRYCPSIEDKPVRFADKPYHQVFLEPEGLDTDEYYLVGFSTSLPEDVQKRVLRTI 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1411378793 329 PGLENAEILRTAYAIEYDCIDPQQLDLTLEFKNINGLYGAGQFNGSSGYEEAAAQGLVAGINSVLKIKGED 399
Cdd:pfam01134 321 PGLENAEIVRPGYAIEYDYIDPPQLLPTLETKKIPGLFFAGQINGTEGYEEAAAQGLLAGINAARKALGKE 391
PRK05335 PRK05335
tRNA (uracil-5-)-methyltransferase Gid; Reviewed
 10-414 2.95e-14

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


Pssm-ID: 235416  Cd Length: 436  Bit Score: 75.18  E-value: 2.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793  10 VVVIGAGHAGCEAALASARMGCKTLICTM---------NLDSIALMACNPNIGG----TAKGHLVREIDALGgemginid 76
Cdd:PRK05335    5 VNVIGAGLAGSEAAWQLAKRGVPVELYEMrpvkktpahHTDGFAELVCSNSFRSdsltNAVGLLKEEMRRLG-------- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793  77 htfiqSRMLNTSKGPAVHSLRAQA-DKKRYSERMKHLLEKEENVTLRQLEVIEIDvednkvKGIltkngayfttkaIILC 155
Cdd:PRK05335   77 -----SLIMEAADAHRVPAGGALAvDREGFSEYVTEALENHPLITVIREEVTEIP------EDI------------TIIA 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793 156 TGtylkgkiiigdiiyssgpsglyP--ANDLSQSLLDL-GI-NLRRFKTGTPArINKRSVDFSKmieqpgdekiVPFSFI 231
Cdd:PRK05335  134 TG----------------------PltSDALAEAIKALtGEdYLYFFDAAAPI-VDKDSIDMDK----------VYLASR 180

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793 232 HDKLDKDQISCYLTytsEETHKIIHENI-----------HRSPLYNGsiegvgpryCPSIE------DKIVRF-PDKdkh 293
Cdd:PRK05335  181 YDKGEADYLNCPMT---KEEYEAFYEALiaaekaelkdfEKEKYFEG---------CMPIEvmaergRETLRFgPMK--- 245

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793 294 qifiePEG------------------EDTEE-LY--VGgMSSSL--PEdvQIKMYRSVPGLENAEILRtayaieY----- 345
Cdd:PRK05335  246 -----PVGltdprtgkrpyavvqlrqDNAAGtLYniVG-FQTKLkwGE--QKRVFRMIPGLENAEFVR------Ygvmhr 311

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1411378793 346 -DCID-PQQLDLTLEFKNINGLYGAGQFNGSSGYEEAAAQGLVAGINSVLKIKGEDPLILKRSDAyIGVLI 414
Cdd:PRK05335  312 nTFINsPKLLDPTLQLKKRPNLFFAGQITGVEGYVESAASGLLAGINAARLALGKEPVIPPPTTA-LGALL 381
 
Name Accession Description Interval E-value
MnmG COG0445
tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal ...
 3-625 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: 1182.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793   3 YLAGDFDVVVIGAGHAGCEAALASARMGCKTLICTMNLDSIALMACNPNIGGTAKGHLVREIDALGGEMGINIDHTFIQS 82
Cdd:COG0445     2 YYPKEYDVIVVGGGHAGCEAALAAARMGAKTLLLTHNLDTIGQMSCNPAIGGIAKGHLVREIDALGGEMGRAADKTGIQF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793  83 RMLNTSKGPAVHSLRAQADKKRYSERMKHLLEKEENVTLRQLEVIEIDVEDNKVKGILTKNGAYFTTKAIILCTGTYLKG 162
Cdd:COG0445    82 RMLNTSKGPAVRAPRAQADRKLYRAAMRETLENQPNLDLIQGEVEDLIVEDGRVTGVVTADGIEFRAKAVVLTTGTFLNG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793 163 KIIIGDIIYSSGPSGLYPANDLSQSLLDLGINLRRFKTGTPARINKRSVDFSKMIEQPGDEKIVPFSFIHDKLDKDQISC 242
Cdd:COG0445   162 LIHIGEKSYPGGRAGEPPSVGLSESLRELGFELGRLKTGTPPRIDGRSIDFSKLEEQPGDEPPPPFSFLTEKIHPPQIPC 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793 243 YLTYTSEETHKIIHENIHRSPLYNGSIEGVGPRYCPSIEDKIVRFPDKDKHQIFIEPEGEDTEELYVGGMSSSLPEDVQI 322
Cdd:COG0445   242 WITYTNEETHEIIRENLHRSPMYSGVIEGVGPRYCPSIEDKIVRFADKDRHQIFLEPEGLDTNEVYPNGISTSLPEDVQL 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793 323 KMYRSVPGLENAEILRTAYAIEYDCIDPQQLDLTLEFKNINGLYGAGQFNGSSGYEEAAAQGLVAGINSVLKIKGEDPLI 402
Cdd:COG0445   322 AMLRSIPGLENAEILRPGYAIEYDYVDPTQLKPTLETKKIEGLFFAGQINGTTGYEEAAAQGLMAGINAALKAQGKEPFI 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793 403 LKRSDAYIGVLIDDLVTKGTNEPYRMMTSRAEYRLLLRQDNADLRLTELGYKMGLVKEDRYNKFINRKKNVENEVERLKN 482
Cdd:COG0445   402 LDRSEAYIGVLIDDLVTKGTDEPYRMFTSRAEYRLLLRQDNADLRLTEKGYELGLVSDERYERFEEKKEAIEEEIERLKS 481

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793 483 VQITGKREINEFLLEKGSTELKKPISLYELIKRPELDYFKVEPLDDKRPSLNDDEKEEINIIAKYEGYINKQLEQVEQFK 562
Cdd:COG0445   482 TRVTPNEEVNEGLEELGSSPLKRGVSLFDLLRRPEITYEDLAELDPELPDLDPEVAEQVEIEIKYEGYIERQEEEIEKLK 561

                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1411378793 563 KYEDRLIPKSINYPDIKGLRLEAIQKLEKIKPINIGQASRISGVSPADISVLLIYMERKNREN 625
Cdd:COG0445   562 RLENLKIPEDFDYDAIPGLSNEAREKLKKIRPETLGQASRISGVTPADISLLLVYLKRRRRRK 624
gidA TIGR00136
glucose-inhibited division protein A; GidA, the longer of two forms of GidA-related proteins, ...
 8-619 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: 888.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793   8 FDVVVIGAGHAGCEAALASARMGCKTLICTMNLDSIALMACNPNIGGTAKGHLVREIDALGGEMGINIDHTFIQSRMLNT 87
Cdd:TIGR00136   1 FDVIVIGGGHAGCEAALAAARLGAKTLLLTLNLDTIGKCSCNPAIGGPAKGILVKEIDALGGEMGKAADKTGLQFRVLNS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793  88 SKGPAVHSLRAQADKKRYSERMKHLLEKEENVTLRQLEVIEIDVEDN-KVKGILTKNGAYFTTKAIILCTGTYLKGKIII 166
Cdd:TIGR00136  81 SKGPAVRATRAQIDKILYQKWMRNQLENQPNLSLFQGEVEDLILEDNdEIKGVVTKDGNEFRAKAVIITTGTFLRGKIHI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793 167 GDIIYSSGPSGLYPANDLSQSLLDLGINLRRFKTGTPARINKRSVDFSKMIEQPGDEKIVPFSFIHDKLDKDQISCYLTY 246
Cdd:TIGR00136 161 GDKSYEAGRAGEQASYGLSTTLRELGFKTGRLKTGTPPRIDKRSIDFSKLEVQFGDTQPPAFSFTNKNFLPQQLPCYLTH 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793 247 TSEETHKIIHENIHRSPLYNGSIEGVGPRYCPSIEDKIVRFPDKDKHQIFIEPEGEDTEELYVGGMSSSLPEDVQIKMYR 326
Cdd:TIGR00136 241 TNPKTHQIIRDNLHRSPMYSGSIEGNGPRYCPSIEDKVVRFADKERHQIFLEPEGLNSDEIYLNGLSTSLPEDVQLKIIR 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793 327 SVPGLENAEILRTAYAIEYDCIDPQQLDLTLEFKNINGLYGAGQFNGSSGYEEAAAQGLVAGINSVLKIKGEDPLILKRS 406
Cdd:TIGR00136 321 SIPGLENAEILRPGYAIEYDYFDPTQLKPTLETKLIKGLFFAGQINGTTGYEEAAAQGLMAGINAALKLQNKEPFILKRN 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793 407 DAYIGVLIDDLVTKGTNEPYRMMTSRAEYRLLLRQDNADLRLTELGYKMGLVKEDRYNKFINRKKNVENEVERLKNVQIT 486
Cdd:TIGR00136 401 EAYIGVLIDDLVTKGTKEPYRMFTSRAEYRLLLREDNADFRLTEIGRELGLIDEDRYARFLKKKQNIEEEIERLKSTRLS 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793 487 GKREINEFLLEKGSTELKKPISLYELIKRPELDYFKVEPLDDKRPSLNDDEKEEINIIAKYEGYINKQLEQVEQFKKYED 566
Cdd:TIGR00136 481 PSKEVKEELKNLAQSPLKDEVSGYDLLKRPEMNLDKLTKLLPFLPPLDEEVLEQVEIEIKYEGYIKKQQQYIKKLDRLEN 560

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1411378793 567 RLIPKSINYPDIKGLRLEAIQKLEKIKPINIGQASRISGVSPADISVLLIYME 619
Cdd:TIGR00136 561 VKIPADFDYRKIPGLSTEAREKLSKFRPLSLGQASRISGINPADISALLVYLK 613
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: 641.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793   9 DVVVIGAGHAGCEAALASARMGCKTLICTMNLDSIALMACNPNIGGTAKGHLVREIDALGGEMGINIDHTFIQSRMLNTS 88
Cdd:pfam01134   1 DVIVIGGGHAGCEAALAAARMGAKVLLITHNTDTIAELSCNPSIGGIAKGHLVREIDALGGLMGKAADKTGIQFRMLNTS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793  89 KGPAVHSLRAQADKKRYSERMKHLLEKEENVTLRQLEVIEIDVEDNKVKGILTKNGAYFTTKAIILCTGTYLKGKIIIGD 168
Cdd:pfam01134  81 KGPAVRALRAQVDRDLYSKEMTETLENHPNLTLIQGEVTDLIPENGKVKGVVTEDGEEYKAKAVVLATGTFLNGKIHIGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793 169 IIYSSGPSGLYPANDLSQSLLDLGINLRRFKTGTPARINKRSVDFSKMIEQPGDEKIVPFSFIHDKLDKDQISCYLTYTS 248
Cdd:pfam01134 161 KCYPAGRLGELTSEGLSESLKELGFELGRFKTGTPPRIDKDSIDFSKLEEQPGDKPGPPFSYLNCPMNKEQYPCFLTYTN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793 249 EETHKIIHENIHRSPLYNGSIEGVGPRYCPSIEDKIVRFPDKDKHQIFIEPEGEDTEELYVGGMSSSLPEDVQIKMYRSV 328
Cdd:pfam01134 241 EATHEIIRDNLHRSPMFEGCIEGIGPRYCPSIEDKPVRFADKPYHQVFLEPEGLDTDEYYLVGFSTSLPEDVQKRVLRTI 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1411378793 329 PGLENAEILRTAYAIEYDCIDPQQLDLTLEFKNINGLYGAGQFNGSSGYEEAAAQGLVAGINSVLKIKGED 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 9.69e-123

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: 361.70  E-value: 9.69e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793 401 LILKRSDAYIGVLIDDLVTKGTNEPYRMMTSRAEYRLLLRQDNADLRLTELGYKMGLVKEDRYNKFINRKKNVENEVERL 480
Cdd:pfam13932   1 LILSRSEAYIGVLIDDLVTKGTSEPYRMFTSRAEYRLLLRQDNADLRLTEKGRELGLVSDERYERFEEKKEAIEEEIERL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793 481 KNVQITGKREINEfLLEKGSTELKKPISLYELIKRPELDYFKVEPLDDKRPSLNDDEKEEINIIAKYEGYINKQLEQVEQ 560
Cdd:pfam13932  81 KSTRLSPSEWNNA-LLELGSAPLGTGRSAFDLLRRPEVTYEDLAALIPELAPLDPEVLEQVEIEAKYEGYIERQEAEIEK 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1411378793 561 FKKYEDRLIPKSINYPDIKGLRLEAIQKLEKIKPINIGQASRISGVSPADISVLL 615
Cdd:pfam13932 160 FKRLENLKIPEDLDYDAIPGLSNEAREKLNKIRPETIGQASRISGVTPADISVLL 214
TrmFO COG1206
Folate-dependent tRNA-U54 methylase TrmFO/GidA [Translation, ribosomal structure and ...
 321-414 2.14e-14

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: 75.48  E-value: 2.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793 321 QIKMYRSVPGLENAEILR-------TayaieYdcID-PQQLDLTLEFKNINGLYGAGQFNGSSGYEEAAAQGLVAGINSV 392
Cdd:COG1206   288 QKRVFRMIPGLENAEFVRygvmhrnT-----F--INsPKLLDPTLQLKARPNLFFAGQITGVEGYVESAASGLLAGINAA 360

                          90       100
                  ....*....|....*....|..
gi 1411378793 393 LKIKGEDPLILKRSDAyIGVLI 414
Cdd:COG1206   361 RLLLGKEPVPPPPTTA-LGALL 381
PRK05335 PRK05335
tRNA (uracil-5-)-methyltransferase Gid; Reviewed
 10-414 2.95e-14

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


Pssm-ID: 235416  Cd Length: 436  Bit Score: 75.18  E-value: 2.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793  10 VVVIGAGHAGCEAALASARMGCKTLICTM---------NLDSIALMACNPNIGG----TAKGHLVREIDALGgemginid 76
Cdd:PRK05335    5 VNVIGAGLAGSEAAWQLAKRGVPVELYEMrpvkktpahHTDGFAELVCSNSFRSdsltNAVGLLKEEMRRLG-------- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793  77 htfiqSRMLNTSKGPAVHSLRAQA-DKKRYSERMKHLLEKEENVTLRQLEVIEIDvednkvKGIltkngayfttkaIILC 155
Cdd:PRK05335   77 -----SLIMEAADAHRVPAGGALAvDREGFSEYVTEALENHPLITVIREEVTEIP------EDI------------TIIA 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793 156 TGtylkgkiiigdiiyssgpsglyP--ANDLSQSLLDL-GI-NLRRFKTGTPArINKRSVDFSKmieqpgdekiVPFSFI 231
Cdd:PRK05335  134 TG----------------------PltSDALAEAIKALtGEdYLYFFDAAAPI-VDKDSIDMDK----------VYLASR 180

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793 232 HDKLDKDQISCYLTytsEETHKIIHENI-----------HRSPLYNGsiegvgpryCPSIE------DKIVRF-PDKdkh 293
Cdd:PRK05335  181 YDKGEADYLNCPMT---KEEYEAFYEALiaaekaelkdfEKEKYFEG---------CMPIEvmaergRETLRFgPMK--- 245

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793 294 qifiePEG------------------EDTEE-LY--VGgMSSSL--PEdvQIKMYRSVPGLENAEILRtayaieY----- 345
Cdd:PRK05335  246 -----PVGltdprtgkrpyavvqlrqDNAAGtLYniVG-FQTKLkwGE--QKRVFRMIPGLENAEFVR------Ygvmhr 311

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1411378793 346 -DCID-PQQLDLTLEFKNINGLYGAGQFNGSSGYEEAAAQGLVAGINSVLKIKGEDPLILKRSDAyIGVLI 414
Cdd:PRK05335  312 nTFINsPKLLDPTLQLKKRPNLFFAGQITGVEGYVESAASGLLAGINAARLALGKEPVIPPPTTA-LGALL 381
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
8-157 6.41e-08

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 54.74  E-value: 6.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793   8 FDVVVIGAGHAGCEAALASARMGCKTLIctmnLDSialmacnPNIGGTAkgHLVREIDALGG-EMGINidhtfiqsrmln 86
Cdd:COG0492     1 YDVVIIGAGPAGLTAAIYAARAGLKTLV----IEG-------GEPGGQL--ATTKEIENYPGfPEGIS------------ 55

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1411378793  87 tskGPA-VHSLRAQAdkKRYsermkhllekeeNVTLRQLEVIEIDVEDNkVKGILTKNGAYFTTKAIILCTG 157
Cdd:COG0492    56 ---GPElAERLREQA--ERF------------GAEILLEEVTSVDKDDG-PFRVTTDDGTEYEAKAVIIATG 109
FAD_oxidored pfam12831
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ...
 9-157 6.91e-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: 55.31  E-value: 6.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793   9 DVVVIGAGHAGCEAALASARMGCKTLIctmnLDSialmacNPNIGGTAKGHLVREIdalggeMGINIDHTFIQSRML--- 85
Cdd:pfam12831   1 DVVVVGGGPAGVAAAIAAARAGAKVLL----VER------RGFLGGMLTSGLVGPD------MGFYLNKEQVVGGIAref 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793  86 ---NTSKGPAVHSLRAQADKKRY-SERMKHLLE---KEENVT-LRQLEVIEIDVEDNKVKGI--LTKNGAY-FTTKAIIL 154
Cdd:pfam12831  65 rqrLRARGGLPGPYGLRGGWVPFdPEVAKAVLDemlAEAGVTvLLHTRVVGVVKEGGRITGVtvETKGGRItIRAKVFID 144


                  ...
gi 1411378793 155 CTG 157
Cdd:pfam12831 145 ATG 147
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
 7-157 1.20e-05

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: 47.91  E-value: 1.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793   7 DFDVVVIGAGHAGCEAALASARMGCKTLICT---------------MNL-----------DSIALMA----------CNP 50
Cdd:COG1053     3 EYDVVVVGSGGAGLRAALEAAEAGLKVLVLEkvpprgghtaaaqggINAagtnvqkaageDSPEEHFydtvkggdglADQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793  51 --------NIGGTakghlVREIDALG--------GEMGINIDHTFiqSRMLNTSK--GPA-VHSLRAQADKKrysermkh 111
Cdd:COG1053    83 dlvealaeEAPEA-----IDWLEAQGvpfsrtpdGRLPQFGGHSV--GRTCYAGDgtGHAlLATLYQAALRL-------- 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1411378793 112 llekeeNVTLR-QLEVIEIDVEDNKVKGILTKNGA----YFTTKAIILCTG 157
Cdd:COG1053   148 ------GVEIFtETEVLDLIVDDGRVVGVVARDRTgeivRIRAKAVVLATG 192
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 8-157 9.38e-05

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: 44.62  E-value: 9.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793   8 FDVVVIGAGHAGCEAALASARMGCKTLICtmnldsialmacnpNIGGTAKGHLVREIDALGGEMGInidhtfiqsrmlnt 87
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLI--------------EDEGTCPYGGCVLSKALLGAAEA-------------- 52

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1411378793  88 skGPAVHSLRAQADKKRysermKHLLEKEENVTLR-QLEVIEIDVEDNKVKGILTKNGAYFTTKA--IILCTG 157
Cdd:pfam07992  53 --PEIASLWADLYKRKE-----EVVKKLNNGIEVLlGTEVVSIDPGAKKVVLEELVDGDGETITYdrLVIATG 118
PRK05329 PRK05329
glycerol-3-phosphate dehydrogenase subunit GlpB;
7-35 1.50e-04

glycerol-3-phosphate dehydrogenase subunit GlpB;


Pssm-ID: 235412  Cd Length: 422  Bit Score: 44.46  E-value: 1.50e-04
                          10        20
                  ....*....|....*....|....*....
gi 1411378793   7 DFDVVVIGAGHAGCEAALASARMGCKTLI 35
Cdd:PRK05329    2 KFDVLVIGGGLAGLTAALAAAEAGKRVAL 30
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
 5-159 7.15e-04

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 42.44  E-value: 7.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793   5 AGDFDVVVIGAGHAGCEAALASARMGCKTLICTMNldsialmacnpNIGGT-------------AKGHLVREIDALgGEM 71
Cdd:PRK06416    2 AFEYDVIVIGAGPGGYVAAIRAAQLGLKVAIVEKE-----------KLGGTclnrgcipskallHAAERADEARHS-EDF 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411378793  72 GINIdhTFIQSRMlntskgPAVHSLRAQADKKRYSErMKHLLEKeenvtlRQLEVIEID---VEDNKVKGILTKNGAYFT 148
Cdd:PRK06416   70 GIKA--ENVGIDF------KKVQEWKNGVVNRLTGG-VEGLLKK------NKVDIIRGEaklVDPNTVRVMTEDGEQTYT 134

                         170
                  ....*....|.
gi 1411378793 149 TKAIILCTGTY 159
Cdd:PRK06416  135 AKNIILATGSR 145
PRK12843 PRK12843
FAD-dependent oxidoreductase;
6-36 1.02e-03

FAD-dependent oxidoreductase;


Pssm-ID: 237225 [Multi-domain]  Cd Length: 578  Bit Score: 42.03  E-value: 1.02e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1411378793   6 GDFDVVVIGAGHAGCEAALASARMGCKTLIC 36
Cdd:PRK12843   15 AEFDVIVIGAGAAGMSAALFAAIAGLKVLLV 45
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 7-35 1.57e-03

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: 41.23  E-value: 1.57e-03
                          10        20
                  ....*....|....*....|....*....
gi 1411378793   7 DFDVVVIGAGHAGCEAALASARMGCKTLI 35
Cdd:COG1249     3 DYDLVVIGAGPGGYVAAIRAAQLGLKVAL 31
GG-red-SF TIGR02032
geranylgeranyl reductase family; This model represents a subfamily which includes ...
 8-35 2.33e-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: 40.38  E-value: 2.33e-03
                          10        20
                  ....*....|....*....|....*...
gi 1411378793   8 FDVVVIGAGHAGCEAALASARMGCKTLI 35
Cdd:TIGR02032   1 YDVVVVGAGPAGASAAYRLADKGLRVLL 28
GlpB COG3075
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism];
7-35 3.67e-03

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


Pssm-ID: 442309  Cd Length: 415  Bit Score: 40.16  E-value: 3.67e-03
                          10        20
                  ....*....|....*....|....*....
gi 1411378793   7 DFDVVVIGAGHAGCEAALASARMGCKTLI 35
Cdd:COG3075     2 KFDVVVIGGGLAGLTAAIRAAEAGLRVAI 30
PRK07843 PRK07843
3-oxosteroid 1-dehydrogenase;
1-35 6.35e-03

3-oxosteroid 1-dehydrogenase;


Pssm-ID: 236111 [Multi-domain]  Cd Length: 557  Bit Score: 39.63  E-value: 6.35e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1411378793   1 MKYLAGDFDVVVIGAGHAGCEAALASARMGCKTLI 35
Cdd:PRK07843    1 MAMTVQEYDVVVVGSGAAGMVAALTAAHRGLSTVV 35
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 7-36 6.72e-03

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


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 39.45  E-value: 6.72e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1411378793   7 DFDVVVIGAGHAGCEAALASARMGCKTLIC 36
Cdd:COG1233     3 MYDVVVIGAGIGGLAAAALLARAGYRVTVL 32
FAD_binding_2 pfam00890
FAD binding domain; This family includes members that bind FAD. This family includes the ...
 9-35 7.45e-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: 7.45e-03
                          10        20
                  ....*....|....*....|....*..
gi 1411378793   9 DVVVIGAGHAGCEAALASARMGCKTLI 35
Cdd:pfam00890   1 DVLVIGGGLAGLAAALAAAEAGLKVAV 27
PRK06327 PRK06327
dihydrolipoamide dehydrogenase; Validated
 7-55 7.80e-03

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235779 [Multi-domain]  Cd Length: 475  Bit Score: 39.14  E-value: 7.80e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1411378793   7 DFDVVVIGAGHAGCEAALASARMGCKTLICtmnlDSIALMACNPNIGGT 55
Cdd:PRK06327    4 QFDVVVIGAGPGGYVAAIRAAQLGLKVACI----EAWKNPKGKPALGGT 48
 
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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