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Conserved domains on  [gi|2745857892|gb|XBX10595|]
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tRNA uridine-5-carboxymethylaminomethyl(34) synthesis enzyme MnmG [Enterocloster clostridioformis]

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 ...
 4-625 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 2745857892   4 YVEETYDVVIVGAGHAGCEAALASARLGMETIMFTVSVDSIALMPCNPNIGGSSKGHLVRELDALGGEMGKNIDRTFIQS 83
Cdd:COG0445     2 YYPKEYDVIVVGGGHAGCEAALAAARMGAKTLLLTHNLDTIGQMSCNPAIGGIAKGHLVREIDALGGEMGRAADKTGIQF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892  84 KMLNESKGPAVHSLRAQADKQDYSRHMRKTLENTEHLTIRQAEVSEIMVKDGKIRGVKTFSGAVYHAKAVVLCTGTYLKA 163
Cdd:COG0445    82 RMLNTSKGPAVRAPRAQADRKLYRAAMRETLENQPNLDLIQGEVEDLIVEDGRVTGVVTADGIEFRAKAVVLTTGTFLNG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892 164 RCIYGDVSNPTGPNGLQAANHLTDSLKENGIEMFRFKTGTPARVDKKSIDFSKMEEQFGDSRVVPFSFSTnpDEIQKEQV 243
Cdd:COG0445   162 LIHIGEKSYPGGRAGEPPSVGLSESLRELGFELGRLKTGTPPRIDGRSIDFSKLEEQPGDEPPPPFSFLT--EKIHPPQI 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892 244 SCWLTYTNEDTHRIIKDNLDRSPLFSGAIEGTGPRYCPSIEDKVVKFPDKNRHQVFVEPEGLYTNEMYLGGMSSSLPEDV 323
Cdd:COG0445   240 PCWITYTNEETHEIIRENLHRSPMYSGVIEGVGPRYCPSIEDKIVRFADKDRHQIFLEPEGLDTNEVYPNGISTSLPEDV 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892 324 QYAMYRTVPGLEKVKIVRNAYAIEYDCINALQLKPTLEFKKISGLFAGGQFNGSSGYEEAAVQGFMAGVNAAMKIQGREA 403
Cdd:COG0445   320 QLAMLRSIPGLENAEILRPGYAIEYDYVDPTQLKPTLETKKIEGLFFAGQINGTTGYEEAAAQGLMAGINAALKAQGKEP 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892 404 VVLDRSQAYIGVLIDDLVTKENHEPYRMMTSRAEYRLLLRQDNADIRLRKIGHDIGLVSDEEYEHLLKKVDDIQSEIKRL 483
Cdd:COG0445   400 FILDRSEAYIGVLIDDLVTKGTDEPYRMFTSRAEYRLLLRQDNADLRLTEKGYELGLVSDERYERFEEKKEAIEEEIERL 479

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892 484 EKTVIGVNGQAQTFLEKYGSTLLKSGITLAELVKRPELDYDKLEELDEDRPRLPDDVREQVNIEIKYEGYIKRQMQQVAS 563
Cdd:COG0445   480 KSTRVTPNEEVNEGLEELGSSPLKRGVSLFDLLRRPEITYEDLAELDPELPDLDPEVAEQVEIEIKYEGYIERQEEEIEK 559

                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2745857892 564 FRKLEDKKLPEDFDYSEVNSLRREAVQKLNKVQPATIGQASRISGVSPADISVLLVHFTRKQ 625
Cdd:COG0445   560 LKRLENLKIPEDFDYDAIPGLSNEAREKLKKIRPETLGQASRISGVTPADISLLLVYLKRRR 621
 
Name Accession Description Interval E-value
MnmG COG0445
tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal ...
 4-625 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 2745857892   4 YVEETYDVVIVGAGHAGCEAALASARLGMETIMFTVSVDSIALMPCNPNIGGSSKGHLVRELDALGGEMGKNIDRTFIQS 83
Cdd:COG0445     2 YYPKEYDVIVVGGGHAGCEAALAAARMGAKTLLLTHNLDTIGQMSCNPAIGGIAKGHLVREIDALGGEMGRAADKTGIQF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892  84 KMLNESKGPAVHSLRAQADKQDYSRHMRKTLENTEHLTIRQAEVSEIMVKDGKIRGVKTFSGAVYHAKAVVLCTGTYLKA 163
Cdd:COG0445    82 RMLNTSKGPAVRAPRAQADRKLYRAAMRETLENQPNLDLIQGEVEDLIVEDGRVTGVVTADGIEFRAKAVVLTTGTFLNG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892 164 RCIYGDVSNPTGPNGLQAANHLTDSLKENGIEMFRFKTGTPARVDKKSIDFSKMEEQFGDSRVVPFSFSTnpDEIQKEQV 243
Cdd:COG0445   162 LIHIGEKSYPGGRAGEPPSVGLSESLRELGFELGRLKTGTPPRIDGRSIDFSKLEEQPGDEPPPPFSFLT--EKIHPPQI 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892 244 SCWLTYTNEDTHRIIKDNLDRSPLFSGAIEGTGPRYCPSIEDKVVKFPDKNRHQVFVEPEGLYTNEMYLGGMSSSLPEDV 323
Cdd:COG0445   240 PCWITYTNEETHEIIRENLHRSPMYSGVIEGVGPRYCPSIEDKIVRFADKDRHQIFLEPEGLDTNEVYPNGISTSLPEDV 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892 324 QYAMYRTVPGLEKVKIVRNAYAIEYDCINALQLKPTLEFKKISGLFAGGQFNGSSGYEEAAVQGFMAGVNAAMKIQGREA 403
Cdd:COG0445   320 QLAMLRSIPGLENAEILRPGYAIEYDYVDPTQLKPTLETKKIEGLFFAGQINGTTGYEEAAAQGLMAGINAALKAQGKEP 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892 404 VVLDRSQAYIGVLIDDLVTKENHEPYRMMTSRAEYRLLLRQDNADIRLRKIGHDIGLVSDEEYEHLLKKVDDIQSEIKRL 483
Cdd:COG0445   400 FILDRSEAYIGVLIDDLVTKGTDEPYRMFTSRAEYRLLLRQDNADLRLTEKGYELGLVSDERYERFEEKKEAIEEEIERL 479

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892 484 EKTVIGVNGQAQTFLEKYGSTLLKSGITLAELVKRPELDYDKLEELDEDRPRLPDDVREQVNIEIKYEGYIKRQMQQVAS 563
Cdd:COG0445   480 KSTRVTPNEEVNEGLEELGSSPLKRGVSLFDLLRRPEITYEDLAELDPELPDLDPEVAEQVEIEIKYEGYIERQEEEIEK 559

                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2745857892 564 FRKLEDKKLPEDFDYSEVNSLRREAVQKLNKVQPATIGQASRISGVSPADISVLLVHFTRKQ 625
Cdd:COG0445   560 LKRLENLKIPEDFDYDAIPGLSNEAREKLKKIRPETLGQASRISGVTPADISLLLVYLKRRR 621
gidA TIGR00136
glucose-inhibited division protein A; GidA, the longer of two forms of GidA-related proteins, ...
 9-625 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: 897.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892   9 YDVVIVGAGHAGCEAALASARLGMETIMFTVSVDSIALMPCNPNIGGSSKGHLVRELDALGGEMGKNIDRTFIQSKMLNE 88
Cdd:TIGR00136   1 FDVIVIGGGHAGCEAALAAARLGAKTLLLTLNLDTIGKCSCNPAIGGPAKGILVKEIDALGGEMGKAADKTGLQFRVLNS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892  89 SKGPAVHSLRAQADKQDYSRHMRKTLENTEHLTIRQAEVSEIMVKD-GKIRGVKTFSGAVYHAKAVVLCTGTYLKARCIY 167
Cdd:TIGR00136  81 SKGPAVRATRAQIDKILYQKWMRNQLENQPNLSLFQGEVEDLILEDnDEIKGVVTKDGNEFRAKAVIITTGTFLRGKIHI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892 168 GDVSNPTGPNGLQAANHLTDSLKENGIEMFRFKTGTPARVDKKSIDFSKMEEQFGDSRVVPFSFSTNpdEIQKEQVSCWL 247
Cdd:TIGR00136 161 GDKSYEAGRAGEQASYGLSTTLRELGFKTGRLKTGTPPRIDKRSIDFSKLEVQFGDTQPPAFSFTNK--NFLPQQLPCYL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892 248 TYTNEDTHRIIKDNLDRSPLFSGAIEGTGPRYCPSIEDKVVKFPDKNRHQVFVEPEGLYTNEMYLGGMSSSLPEDVQYAM 327
Cdd:TIGR00136 239 THTNPKTHQIIRDNLHRSPMYSGSIEGNGPRYCPSIEDKVVRFADKERHQIFLEPEGLNSDEIYLNGLSTSLPEDVQLKI 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892 328 YRTVPGLEKVKIVRNAYAIEYDCINALQLKPTLEFKKISGLFAGGQFNGSSGYEEAAVQGFMAGVNAAMKIQGREAVVLD 407
Cdd:TIGR00136 319 IRSIPGLENAEILRPGYAIEYDYFDPTQLKPTLETKLIKGLFFAGQINGTTGYEEAAAQGLMAGINAALKLQNKEPFILK 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892 408 RSQAYIGVLIDDLVTKENHEPYRMMTSRAEYRLLLRQDNADIRLRKIGHDIGLVSDEEYEHLLKKVDDIQSEIKRLEKTV 487
Cdd:TIGR00136 399 RNEAYIGVLIDDLVTKGTKEPYRMFTSRAEYRLLLREDNADFRLTEIGRELGLIDEDRYARFLKKKQNIEEEIERLKSTR 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892 488 IGVNGQAQTFLEKYGSTLLKSGITLAELVKRPELDYDKLEELDEDRPRLPDDVREQVNIEIKYEGYIKRQMQQVASFRKL 567
Cdd:TIGR00136 479 LSPSKEVKEELKNLAQSPLKDEVSGYDLLKRPEMNLDKLTKLLPFLPPLDEEVLEQVEIEIKYEGYIKKQQQYIKKLDRL 558

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2745857892 568 EDKKLPEDFDYSEVNSLRREAVQKLNKVQPATIGQASRISGVSPADISVLLvHFTRKQ 625
Cdd:TIGR00136 559 ENVKIPADFDYRKIPGLSTEAREKLSKFRPLSLGQASRISGINPADISALL-VYLKKQ 615
GIDA pfam01134
Glucose inhibited division protein A;
10-402 0e+00

Glucose inhibited division protein A;


Pssm-ID: 250388 [Multi-domain]  Cd Length: 391  Bit Score: 642.68  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892  10 DVVIVGAGHAGCEAALASARLGMETIMFTVSVDSIALMPCNPNIGGSSKGHLVRELDALGGEMGKNIDRTFIQSKMLNES 89
Cdd:pfam01134   1 DVIVIGGGHAGCEAALAAARMGAKVLLITHNTDTIAELSCNPSIGGIAKGHLVREIDALGGLMGKAADKTGIQFRMLNTS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892  90 KGPAVHSLRAQADKQDYSRHMRKTLENTEHLTIRQAEVSEIMVKDGKIRGVKTFSGAVYHAKAVVLCTGTYLKARCIYGD 169
Cdd:pfam01134  81 KGPAVRALRAQVDRDLYSKEMTETLENHPNLTLIQGEVTDLIPENGKVKGVVTEDGEEYKAKAVVLATGTFLNGKIHIGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892 170 VSNPTGPNGLQAANHLTDSLKENGIEMFRFKTGTPARVDKKSIDFSKMEEQFGDSRVVPFSFSTNPdeIQKEQVSCWLTY 249
Cdd:pfam01134 161 KCYPAGRLGELTSEGLSESLKELGFELGRFKTGTPPRIDKDSIDFSKLEEQPGDKPGPPFSYLNCP--MNKEQYPCFLTY 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892 250 TNEDTHRIIKDNLDRSPLFSGAIEGTGPRYCPSIEDKVVKFPDKNRHQVFVEPEGLYTNEMYLGGMSSSLPEDVQYAMYR 329
Cdd:pfam01134 239 TNEATHEIIRDNLHRSPMFEGCIEGIGPRYCPSIEDKPVRFADKPYHQVFLEPEGLDTDEYYLVGFSTSLPEDVQKRVLR 318

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2745857892 330 TVPGLEKVKIVRNAYAIEYDCINALQLKPTLEFKKISGLFAGGQFNGSSGYEEAAVQGFMAGVNAAMKIQGRE 402
Cdd:pfam01134 319 TIPGLENAEIVRPGYAIEYDYIDPPQLLPTLETKKIPGLFFAGQINGTEGYEEAAAQGLLAGINAARKALGKE 391
PRK05335 PRK05335
tRNA (uracil-5-)-methyltransferase Gid; Reviewed
 329-417 6.23e-14

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


Pssm-ID: 235416  Cd Length: 436  Bit Score: 74.03  E-value: 6.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892 329 RTVPGLEKVKIVR------NAYaieydcINALQ-LKPTLEFKKISGLFAGGQFNGSSGYEEAAVQGFMAGVNAAMKIQGR 401
Cdd:PRK05335  293 RMIPGLENAEFVRygvmhrNTF------INSPKlLDPTLQLKKRPNLFFAGQITGVEGYVESAASGLLAGINAARLALGK 366

                          90
                  ....*....|....*.
gi 2745857892 402 EAVVLDRSQAyIGVLI 417
Cdd:PRK05335  367 EPVIPPPTTA-LGALL 381
 
Name Accession Description Interval E-value
MnmG COG0445
tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal ...
 4-625 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 2745857892   4 YVEETYDVVIVGAGHAGCEAALASARLGMETIMFTVSVDSIALMPCNPNIGGSSKGHLVRELDALGGEMGKNIDRTFIQS 83
Cdd:COG0445     2 YYPKEYDVIVVGGGHAGCEAALAAARMGAKTLLLTHNLDTIGQMSCNPAIGGIAKGHLVREIDALGGEMGRAADKTGIQF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892  84 KMLNESKGPAVHSLRAQADKQDYSRHMRKTLENTEHLTIRQAEVSEIMVKDGKIRGVKTFSGAVYHAKAVVLCTGTYLKA 163
Cdd:COG0445    82 RMLNTSKGPAVRAPRAQADRKLYRAAMRETLENQPNLDLIQGEVEDLIVEDGRVTGVVTADGIEFRAKAVVLTTGTFLNG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892 164 RCIYGDVSNPTGPNGLQAANHLTDSLKENGIEMFRFKTGTPARVDKKSIDFSKMEEQFGDSRVVPFSFSTnpDEIQKEQV 243
Cdd:COG0445   162 LIHIGEKSYPGGRAGEPPSVGLSESLRELGFELGRLKTGTPPRIDGRSIDFSKLEEQPGDEPPPPFSFLT--EKIHPPQI 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892 244 SCWLTYTNEDTHRIIKDNLDRSPLFSGAIEGTGPRYCPSIEDKVVKFPDKNRHQVFVEPEGLYTNEMYLGGMSSSLPEDV 323
Cdd:COG0445   240 PCWITYTNEETHEIIRENLHRSPMYSGVIEGVGPRYCPSIEDKIVRFADKDRHQIFLEPEGLDTNEVYPNGISTSLPEDV 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892 324 QYAMYRTVPGLEKVKIVRNAYAIEYDCINALQLKPTLEFKKISGLFAGGQFNGSSGYEEAAVQGFMAGVNAAMKIQGREA 403
Cdd:COG0445   320 QLAMLRSIPGLENAEILRPGYAIEYDYVDPTQLKPTLETKKIEGLFFAGQINGTTGYEEAAAQGLMAGINAALKAQGKEP 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892 404 VVLDRSQAYIGVLIDDLVTKENHEPYRMMTSRAEYRLLLRQDNADIRLRKIGHDIGLVSDEEYEHLLKKVDDIQSEIKRL 483
Cdd:COG0445   400 FILDRSEAYIGVLIDDLVTKGTDEPYRMFTSRAEYRLLLRQDNADLRLTEKGYELGLVSDERYERFEEKKEAIEEEIERL 479

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892 484 EKTVIGVNGQAQTFLEKYGSTLLKSGITLAELVKRPELDYDKLEELDEDRPRLPDDVREQVNIEIKYEGYIKRQMQQVAS 563
Cdd:COG0445   480 KSTRVTPNEEVNEGLEELGSSPLKRGVSLFDLLRRPEITYEDLAELDPELPDLDPEVAEQVEIEIKYEGYIERQEEEIEK 559

                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2745857892 564 FRKLEDKKLPEDFDYSEVNSLRREAVQKLNKVQPATIGQASRISGVSPADISVLLVHFTRKQ 625
Cdd:COG0445   560 LKRLENLKIPEDFDYDAIPGLSNEAREKLKKIRPETLGQASRISGVTPADISLLLVYLKRRR 621
gidA TIGR00136
glucose-inhibited division protein A; GidA, the longer of two forms of GidA-related proteins, ...
 9-625 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: 897.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892   9 YDVVIVGAGHAGCEAALASARLGMETIMFTVSVDSIALMPCNPNIGGSSKGHLVRELDALGGEMGKNIDRTFIQSKMLNE 88
Cdd:TIGR00136   1 FDVIVIGGGHAGCEAALAAARLGAKTLLLTLNLDTIGKCSCNPAIGGPAKGILVKEIDALGGEMGKAADKTGLQFRVLNS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892  89 SKGPAVHSLRAQADKQDYSRHMRKTLENTEHLTIRQAEVSEIMVKD-GKIRGVKTFSGAVYHAKAVVLCTGTYLKARCIY 167
Cdd:TIGR00136  81 SKGPAVRATRAQIDKILYQKWMRNQLENQPNLSLFQGEVEDLILEDnDEIKGVVTKDGNEFRAKAVIITTGTFLRGKIHI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892 168 GDVSNPTGPNGLQAANHLTDSLKENGIEMFRFKTGTPARVDKKSIDFSKMEEQFGDSRVVPFSFSTNpdEIQKEQVSCWL 247
Cdd:TIGR00136 161 GDKSYEAGRAGEQASYGLSTTLRELGFKTGRLKTGTPPRIDKRSIDFSKLEVQFGDTQPPAFSFTNK--NFLPQQLPCYL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892 248 TYTNEDTHRIIKDNLDRSPLFSGAIEGTGPRYCPSIEDKVVKFPDKNRHQVFVEPEGLYTNEMYLGGMSSSLPEDVQYAM 327
Cdd:TIGR00136 239 THTNPKTHQIIRDNLHRSPMYSGSIEGNGPRYCPSIEDKVVRFADKERHQIFLEPEGLNSDEIYLNGLSTSLPEDVQLKI 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892 328 YRTVPGLEKVKIVRNAYAIEYDCINALQLKPTLEFKKISGLFAGGQFNGSSGYEEAAVQGFMAGVNAAMKIQGREAVVLD 407
Cdd:TIGR00136 319 IRSIPGLENAEILRPGYAIEYDYFDPTQLKPTLETKLIKGLFFAGQINGTTGYEEAAAQGLMAGINAALKLQNKEPFILK 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892 408 RSQAYIGVLIDDLVTKENHEPYRMMTSRAEYRLLLRQDNADIRLRKIGHDIGLVSDEEYEHLLKKVDDIQSEIKRLEKTV 487
Cdd:TIGR00136 399 RNEAYIGVLIDDLVTKGTKEPYRMFTSRAEYRLLLREDNADFRLTEIGRELGLIDEDRYARFLKKKQNIEEEIERLKSTR 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892 488 IGVNGQAQTFLEKYGSTLLKSGITLAELVKRPELDYDKLEELDEDRPRLPDDVREQVNIEIKYEGYIKRQMQQVASFRKL 567
Cdd:TIGR00136 479 LSPSKEVKEELKNLAQSPLKDEVSGYDLLKRPEMNLDKLTKLLPFLPPLDEEVLEQVEIEIKYEGYIKKQQQYIKKLDRL 558

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2745857892 568 EDKKLPEDFDYSEVNSLRREAVQKLNKVQPATIGQASRISGVSPADISVLLvHFTRKQ 625
Cdd:TIGR00136 559 ENVKIPADFDYRKIPGLSTEAREKLSKFRPLSLGQASRISGINPADISALL-VYLKKQ 615
GIDA pfam01134
Glucose inhibited division protein A;
10-402 0e+00

Glucose inhibited division protein A;


Pssm-ID: 250388 [Multi-domain]  Cd Length: 391  Bit Score: 642.68  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892  10 DVVIVGAGHAGCEAALASARLGMETIMFTVSVDSIALMPCNPNIGGSSKGHLVRELDALGGEMGKNIDRTFIQSKMLNES 89
Cdd:pfam01134   1 DVIVIGGGHAGCEAALAAARMGAKVLLITHNTDTIAELSCNPSIGGIAKGHLVREIDALGGLMGKAADKTGIQFRMLNTS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892  90 KGPAVHSLRAQADKQDYSRHMRKTLENTEHLTIRQAEVSEIMVKDGKIRGVKTFSGAVYHAKAVVLCTGTYLKARCIYGD 169
Cdd:pfam01134  81 KGPAVRALRAQVDRDLYSKEMTETLENHPNLTLIQGEVTDLIPENGKVKGVVTEDGEEYKAKAVVLATGTFLNGKIHIGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892 170 VSNPTGPNGLQAANHLTDSLKENGIEMFRFKTGTPARVDKKSIDFSKMEEQFGDSRVVPFSFSTNPdeIQKEQVSCWLTY 249
Cdd:pfam01134 161 KCYPAGRLGELTSEGLSESLKELGFELGRFKTGTPPRIDKDSIDFSKLEEQPGDKPGPPFSYLNCP--MNKEQYPCFLTY 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892 250 TNEDTHRIIKDNLDRSPLFSGAIEGTGPRYCPSIEDKVVKFPDKNRHQVFVEPEGLYTNEMYLGGMSSSLPEDVQYAMYR 329
Cdd:pfam01134 239 TNEATHEIIRDNLHRSPMFEGCIEGIGPRYCPSIEDKPVRFADKPYHQVFLEPEGLDTDEYYLVGFSTSLPEDVQKRVLR 318

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2745857892 330 TVPGLEKVKIVRNAYAIEYDCINALQLKPTLEFKKISGLFAGGQFNGSSGYEEAAVQGFMAGVNAAMKIQGRE 402
Cdd:pfam01134 319 TIPGLENAEIVRPGYAIEYDYIDPPQLLPTLETKKIPGLFFAGQINGTEGYEEAAAQGLLAGINAARKALGKE 391
GIDA_C pfam13932
tRNA modifying enzyme MnmG/GidA C-terminal domain; The GidA associated domain is a domain that ...
 404-618 1.64e-125

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: 369.02  E-value: 1.64e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892 404 VVLDRSQAYIGVLIDDLVTKENHEPYRMMTSRAEYRLLLRQDNADIRLRKIGHDIGLVSDEEYEHLLKKVDDIQSEIKRL 483
Cdd:pfam13932   1 LILSRSEAYIGVLIDDLVTKGTSEPYRMFTSRAEYRLLLRQDNADLRLTEKGRELGLVSDERYERFEEKKEAIEEEIERL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892 484 EKTVIGVNGQAQTFLEKyGSTLLKSGITLAELVKRPELDYDKLEELDEDRPRLPDDVREQVNIEIKYEGYIKRQMQQVAS 563
Cdd:pfam13932  81 KSTRLSPSEWNNALLEL-GSAPLGTGRSAFDLLRRPEVTYEDLAALIPELAPLDPEVLEQVEIEAKYEGYIERQEAEIEK 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2745857892 564 FRKLEDKKLPEDFDYSEVNSLRREAVQKLNKVQPATIGQASRISGVSPADISVLL 618
Cdd:pfam13932 160 FKRLENLKIPEDLDYDAIPGLSNEAREKLNKIRPETIGQASRISGVTPADISVLL 214
TrmFO COG1206
Folate-dependent tRNA-U54 methylase TrmFO/GidA [Translation, ribosomal structure and ...
 329-417 4.63e-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: 74.71  E-value: 4.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892 329 RTVPGLEKVKIVR------NAYaieydcINA-LQLKPTLEFKKISGLFAGGQFNGSSGYEEAAVQGFMAGVNAAMKIQGR 401
Cdd:COG1206   293 RMIPGLENAEFVRygvmhrNTF------INSpKLLDPTLQLKARPNLFFAGQITGVEGYVESAASGLLAGINAARLLLGK 366

                          90
                  ....*....|....*.
gi 2745857892 402 EAVVLDRSQAyIGVLI 417
Cdd:COG1206   367 EPVPPPPTTA-LGALL 381
PRK05335 PRK05335
tRNA (uracil-5-)-methyltransferase Gid; Reviewed
 329-417 6.23e-14

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


Pssm-ID: 235416  Cd Length: 436  Bit Score: 74.03  E-value: 6.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892 329 RTVPGLEKVKIVR------NAYaieydcINALQ-LKPTLEFKKISGLFAGGQFNGSSGYEEAAVQGFMAGVNAAMKIQGR 401
Cdd:PRK05335  293 RMIPGLENAEFVRygvmhrNTF------INSPKlLDPTLQLKKRPNLFFAGQITGVEGYVESAASGLLAGINAARLALGK 366

                          90
                  ....*....|....*.
gi 2745857892 402 EAVVLDRSQAyIGVLI 417
Cdd:PRK05335  367 EPVIPPPTTA-LGALL 381
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
9-158 3.76e-10

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 61.29  E-value: 3.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892   9 YDVVIVGAGHAGCEAALASARLGMETIMFTVSVD--SIALMPCNPNIGGSSKGHlvreldaLGGEMGKNidrtfiqskml 86
Cdd:COG0492     1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEGGEPggQLATTKEIENYPGFPEGI-------SGPELAER----------- 62

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2745857892  87 neskgpavhsLRAQADKQDysrhmrktlentehLTIRQAEVSEIMvKDGKIRGVKTFSGAVYHAKAVVLCTG 158
Cdd:COG0492    63 ----------LREQAERFG--------------AEILLEEVTSVD-KDDGPFRVTTDDGTEYEAKAVIIATG 109
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
 6-158 3.17e-07

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: 53.30  E-value: 3.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892   6 EETYDVVIVGAGHAGCEAALASARLGMETIMftVSVDS--------------IALMPCNPNIGGSSKGHLVRELDALGGE 71
Cdd:COG1053     1 DHEYDVVVVGSGGAGLRAALEAAEAGLKVLV--LEKVPprgghtaaaqgginAAGTNVQKAAGEDSPEEHFYDTVKGGDG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892  72 MGkNID--RTFIQ--SKMLN--ESKG----PAVHSLRAQADKQDYSR-----------HMRKTLENTEHL--TIR-QAEV 127
Cdd:COG1053    79 LA-DQDlvEALAEeaPEAIDwlEAQGvpfsRTPDGRLPQFGGHSVGRtcyagdgtghaLLATLYQAALRLgvEIFtETEV 157

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2745857892 128 SEIMVKDGKIRGVKTF--SGA--VYHAKAVVLCTG 158
Cdd:COG1053   158 LDLIVDDGRVVGVVARdrTGEivRIRAKAVVLATG 192
FAD_oxidored pfam12831
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ...
 10-158 6.78e-06

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


Pssm-ID: 432816 [Multi-domain]  Cd Length: 420  Bit Score: 48.76  E-value: 6.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892  10 DVVIVGAGHAGCEAALASARLGMETI----------MFT---VSVDSIALMPCNPNIGGSSkGHLVRELDALGGEMGKNI 76
Cdd:pfam12831   1 DVVVVGGGPAGVAAAIAAARAGAKVLlverrgflggMLTsglVGPDMGFYLNKEQVVGGIA-REFRQRLRARGGLPGPYG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892  77 DRTfiQSKMLNESKGPAV-HSLRAQADkqdysrhmrktlentehLTI-RQAEVSEIMVKDGKIRGVKTFS---GAVYHAK 151
Cdd:pfam12831  80 LRG--GWVPFDPEVAKAVlDEMLAEAG-----------------VTVlLHTRVVGVVKEGGRITGVTVETkggRITIRAK 140


                  ....*..
gi 2745857892 152 AVVLCTG 158
Cdd:pfam12831 141 VFIDATG 147
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 9-39 5.51e-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: 45.39  E-value: 5.51e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2745857892   9 YDVVIVGAGHAGCEAALASARLGMETIMFTV 39
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIED 31
PRK07843 PRK07843
3-oxosteroid 1-dehydrogenase;
2-35 2.10e-04

3-oxosteroid 1-dehydrogenase;


Pssm-ID: 236111 [Multi-domain]  Cd Length: 557  Bit Score: 44.26  E-value: 2.10e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2745857892   2 MPYVEETYDVVIVGAGHAGCEAALASARLGMETI 35
Cdd:PRK07843    1 MAMTVQEYDVVVVGSGAAGMVAALTAAHRGLSTV 34
GG-red-SF TIGR02032
geranylgeranyl reductase family; This model represents a subfamily which includes ...
 9-37 3.12e-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: 39.99  E-value: 3.12e-03
                          10        20
                  ....*....|....*....|....*....
gi 2745857892   9 YDVVIVGAGHAGCEAALASARLGMETIMF 37
Cdd:TIGR02032   1 YDVVVVGAGPAGASAAYRLADKGLRVLLL 29
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 125-162 4.04e-03

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


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 40.22  E-value: 4.04e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2745857892 125 AEVSEIMVKDGKIRGVKTFSGAVYHAKAVVLCTG---TYLK 162
Cdd:COG1233   243 AEVERILVEGGRATGVRLADGEEIRADAVVSNADpahTYLR 283
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 6-36 4.07e-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: 40.07  E-value: 4.07e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2745857892   6 EETYDVVIVGAGHAGCEAALASARLGMETIM 36
Cdd:COG1249     1 MKDYDLVVIGAGPGGYVAAIRAAQLGLKVAL 31
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
16-158 5.08e-03

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 39.18  E-value: 5.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892  16 AGHAGCEAALASARLGMETIMftvsVDSiALMPCNPNIGGSSKGHLVRELDALGGE--MGKNIDRTFIQSKMLNESKGPA 93
Cdd:COG0644     1 AGPAGSAAARRLARAGLSVLL----LEK-GSFPGDKICGGGLLPRALEELEPLGLDepLERPVRGARFYSPGGKSVELPP 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2745857892  94 VHSLRAQADKQDYSRHMRKTLENTEHLTIRQAEVSEIMVKDGKIRgVKTFSGAVYHAKAVVLCTG 158
Cdd:COG0644    76 GRGGGYVVDRARFDRWLAEQAEEAGAEVRTGTRVTDVLRDDGRVV-VRTGDGEEIRADYVVDADG 139
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
122-163 5.30e-03

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


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 39.50  E-value: 5.30e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2745857892 122 IRQAEVSEIMVKDGKIRGVKTfSGAVYHAKAVVLCTGTYLKA 163
Cdd:COG0665   169 REGTPVTGLEREGGRVTGVRT-ERGTVRADAVVLAAGAWSAR 209
PRK12844 PRK12844
3-ketosteroid-delta-1-dehydrogenase; Reviewed
 6-36 5.81e-03

3-ketosteroid-delta-1-dehydrogenase; Reviewed


Pssm-ID: 183787 [Multi-domain]  Cd Length: 557  Bit Score: 39.74  E-value: 5.81e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2745857892   6 EETYDVVIVGAGHAGCEAALASARLGMETIM 36
Cdd:PRK12844    4 DETYDVVVVGSGGGGMCAALAAADSGLEPLI 34
FAD_binding_2 pfam00890
FAD binding domain; This family includes members that bind FAD. This family includes the ...
 10-197 6.83e-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: 6.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892  10 DVVIVGAGHAGCEAALASARLGMETIMFT------------------------VSVDSIALMP----------CNPNIG- 54
Cdd:pfam00890   1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEkgqpfggatawssggidalgnppqGGIDSPELHPtdtlkgldelADHPYVe 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892  55 -GSSKG-HLVRELDALGGEMGKNIDRTFIQSKMlneskGPAVHSLRAQADKQDYSRH----------MRKTLENTEHLTI 122
Cdd:pfam00890  81 aFVEAApEAVDWLEALGVPFSRTEDGHLDLRPL-----GGLSATWRTPHDAADRRRGlgtghallarLLEGLRKAGVDFQ 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745857892 123 RQAEVSEIMVKDGKIRG--VKTFSGAVYHA----KAVVLCTGTY------LKARCIYGDVSNP---TGpNGLQAAnhLTD 187
Cdd:pfam00890 156 PRTAADDLIVEDGRVTGavVENRRNGREVRiraiAAVLLATGGFgrlaelLLPAAGYADTTNPpanTG-DGLALA--LRA 232

                         250
                  ....*....|
gi 2745857892 188 SLKENGIEMF 197
Cdd:pfam00890 233 GAALTDDLME 242
 
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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