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Conserved domains on  [gi|1539782540|emb|VEE44361|]
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glucose inhibited division protein A [Pseudomonas putida]

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

 Zoom to residue level

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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 ...
 1-625 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: 1275.71  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540   1 MDFPSRFDVIVIGGGHAGTEAALASARMGVKTLLLTHNVETLGHMSCNPAIGGIGKSHLVKEIDALGGAMALATDKSGIQ 80
Cdd:COG0445     1 MYYPKEYDVIVVGGGHAGCEAALAAARMGAKTLLLTHNLDTIGQMSCNPAIGGIAKGHLVREIDALGGEMGRAADKTGIQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540  81 FRVLNNRKGPAVRATRAQADRAIYKAVVREILENQPNLWIFQQSCDDLIVEQDQVKGVVTQMGLRFFAESVVLTTGTFLG 160
Cdd:COG0445    81 FRMLNTSKGPAVRAPRAQADRKLYRAAMRETLENQPNLDLIQGEVEDLIVEDGRVTGVVTADGIEFRAKAVVLTTGTFLN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540 161 GLIHIGLQNHSGGRAGDPPSIALAHRMRELPLRVGRLKTGTPPRIDGRSVDFSVMTEQPGDTPIPVMSFMGNaEMHPRQV 240
Cdd:COG0445   161 GLIHIGEKSYPGGRAGEPPSVGLSESLRELGFELGRLKTGTPPRIDGRSIDFSKLEEQPGDEPPPPFSFLTE-KIHPPQI 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540 241 SCWITHTNARTHEIIASNLDRSPMYSGVIEGVGPRYCPSIEDKIHRFADKESHQVFIEPEGLNTHELYPNGISTSLPFDV 320
Cdd:COG0445   240 PCWITYTNEETHEIIRENLHRSPMYSGVIEGVGPRYCPSIEDKIVRFADKDRHQIFLEPEGLDTNEVYPNGISTSLPEDV 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540 321 QLELVRSIRGMENAHIVRPGYAIEYDYFDPRDLKYSLETKVIGGLFFAGQINGTTGYEEAGAQGLLAGTNAALRAQGRDS 400
Cdd:COG0445   320 QLAMLRSIPGLENAEILRPGYAIEYDYVDPTQLKPTLETKKIEGLFFAGQINGTTGYEEAAAQGLMAGINAALKAQGKEP 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540 401 WCPRRDEAYIGVLVDDLITLGTQEPYRMFTSRAEYRLILREDNADLRLTEKGRELGLIDDQRWAAFCAKRDGIEREEQRL 480
Cdd:COG0445   400 FILDRSEAYIGVLIDDLVTKGTDEPYRMFTSRAEYRLLLRQDNADLRLTEKGYELGLVSDERYERFEEKKEAIEEEIERL 479

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540 481 KSTWVRPNTEQGQAIVDKFGTPLSHEYSLLNLLARPEIDYAGLIEATG-GEAIDPQVAEQVEIRTKYAGYIDRQQDEIAR 559
Cdd:COG0445   480 KSTRVTPNEEVNEGLEELGSSPLKRGVSLFDLLRRPEITYEDLAELDPeLPDLDPEVAEQVEIEIKYEGYIERQEEEIEK 559

                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1539782540 560 LRASEDTRLPVDIDYTTISGLSKEIQGKLSQTRPQTLGQASRIPGVTPAAISLLLIHLKKRGAGRE 625
Cdd:COG0445   560 LKRLENLKIPEDFDYDAIPGLSNEAREKLKKIRPETLGQASRISGVTPADISLLLVYLKRRRRRKK 625
 
Name Accession Description Interval E-value
MnmG COG0445
tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal ...
 1-625 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: 1275.71  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540   1 MDFPSRFDVIVIGGGHAGTEAALASARMGVKTLLLTHNVETLGHMSCNPAIGGIGKSHLVKEIDALGGAMALATDKSGIQ 80
Cdd:COG0445     1 MYYPKEYDVIVVGGGHAGCEAALAAARMGAKTLLLTHNLDTIGQMSCNPAIGGIAKGHLVREIDALGGEMGRAADKTGIQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540  81 FRVLNNRKGPAVRATRAQADRAIYKAVVREILENQPNLWIFQQSCDDLIVEQDQVKGVVTQMGLRFFAESVVLTTGTFLG 160
Cdd:COG0445    81 FRMLNTSKGPAVRAPRAQADRKLYRAAMRETLENQPNLDLIQGEVEDLIVEDGRVTGVVTADGIEFRAKAVVLTTGTFLN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540 161 GLIHIGLQNHSGGRAGDPPSIALAHRMRELPLRVGRLKTGTPPRIDGRSVDFSVMTEQPGDTPIPVMSFMGNaEMHPRQV 240
Cdd:COG0445   161 GLIHIGEKSYPGGRAGEPPSVGLSESLRELGFELGRLKTGTPPRIDGRSIDFSKLEEQPGDEPPPPFSFLTE-KIHPPQI 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540 241 SCWITHTNARTHEIIASNLDRSPMYSGVIEGVGPRYCPSIEDKIHRFADKESHQVFIEPEGLNTHELYPNGISTSLPFDV 320
Cdd:COG0445   240 PCWITYTNEETHEIIRENLHRSPMYSGVIEGVGPRYCPSIEDKIVRFADKDRHQIFLEPEGLDTNEVYPNGISTSLPEDV 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540 321 QLELVRSIRGMENAHIVRPGYAIEYDYFDPRDLKYSLETKVIGGLFFAGQINGTTGYEEAGAQGLLAGTNAALRAQGRDS 400
Cdd:COG0445   320 QLAMLRSIPGLENAEILRPGYAIEYDYVDPTQLKPTLETKKIEGLFFAGQINGTTGYEEAAAQGLMAGINAALKAQGKEP 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540 401 WCPRRDEAYIGVLVDDLITLGTQEPYRMFTSRAEYRLILREDNADLRLTEKGRELGLIDDQRWAAFCAKRDGIEREEQRL 480
Cdd:COG0445   400 FILDRSEAYIGVLIDDLVTKGTDEPYRMFTSRAEYRLLLRQDNADLRLTEKGYELGLVSDERYERFEEKKEAIEEEIERL 479

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540 481 KSTWVRPNTEQGQAIVDKFGTPLSHEYSLLNLLARPEIDYAGLIEATG-GEAIDPQVAEQVEIRTKYAGYIDRQQDEIAR 559
Cdd:COG0445   480 KSTRVTPNEEVNEGLEELGSSPLKRGVSLFDLLRRPEITYEDLAELDPeLPDLDPEVAEQVEIEIKYEGYIERQEEEIEK 559

                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1539782540 560 LRASEDTRLPVDIDYTTISGLSKEIQGKLSQTRPQTLGQASRIPGVTPAAISLLLIHLKKRGAGRE 625
Cdd:COG0445   560 LKRLENLKIPEDFDYDAIPGLSNEAREKLKKIRPETLGQASRISGVTPADISLLLVYLKRRRRRKK 625
gidA TIGR00136
glucose-inhibited division protein A; GidA, the longer of two forms of GidA-related proteins, ...
 7-621 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: 1003.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540   7 FDVIVIGGGHAGTEAALASARMGVKTLLLTHNVETLGHMSCNPAIGGIGKSHLVKEIDALGGAMALATDKSGIQFRVLNN 86
Cdd:TIGR00136   1 FDVIVIGGGHAGCEAALAAARLGAKTLLLTLNLDTIGKCSCNPAIGGPAKGILVKEIDALGGEMGKAADKTGLQFRVLNS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540  87 RKGPAVRATRAQADRAIYKAVVREILENQPNLWIFQQSCDDLIVEQ-DQVKGVVTQMGLRFFAESVVLTTGTFLGGLIHI 165
Cdd:TIGR00136  81 SKGPAVRATRAQIDKILYQKWMRNQLENQPNLSLFQGEVEDLILEDnDEIKGVVTKDGNEFRAKAVIITTGTFLRGKIHI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540 166 GLQNHSGGRAGDPPSIALAHRMRELPLRVGRLKTGTPPRIDGRSVDFSVMTEQPGDTPIPVMSFMGNaEMHPRQVSCWIT 245
Cdd:TIGR00136 161 GDKSYEAGRAGEQASYGLSTTLRELGFKTGRLKTGTPPRIDKRSIDFSKLEVQFGDTQPPAFSFTNK-NFLPQQLPCYLT 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540 246 HTNARTHEIIASNLDRSPMYSGVIEGVGPRYCPSIEDKIHRFADKESHQVFIEPEGLNTHELYPNGISTSLPFDVQLELV 325
Cdd:TIGR00136 240 HTNPKTHQIIRDNLHRSPMYSGSIEGNGPRYCPSIEDKVVRFADKERHQIFLEPEGLNSDEIYLNGLSTSLPEDVQLKII 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540 326 RSIRGMENAHIVRPGYAIEYDYFDPRDLKYSLETKVIGGLFFAGQINGTTGYEEAGAQGLLAGTNAALRAQGRDSWCPRR 405
Cdd:TIGR00136 320 RSIPGLENAEILRPGYAIEYDYFDPTQLKPTLETKLIKGLFFAGQINGTTGYEEAAAQGLMAGINAALKLQNKEPFILKR 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540 406 DEAYIGVLVDDLITLGTQEPYRMFTSRAEYRLILREDNADLRLTEKGRELGLIDDQRWAAFCAKRDGIEREEQRLKSTWV 485
Cdd:TIGR00136 400 NEAYIGVLIDDLVTKGTKEPYRMFTSRAEYRLLLREDNADFRLTEIGRELGLIDEDRYARFLKKKQNIEEEIERLKSTRL 479

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540 486 RPNTEQGQAIVDKFGTPLSHEYSLLNLLARPEIDYAGLIEATGGEAI-DPQVAEQVEIRTKYAGYIDRQQDEIARLRASE 564
Cdd:TIGR00136 480 SPSKEVKEELKNLAQSPLKDEVSGYDLLKRPEMNLDKLTKLLPFLPPlDEEVLEQVEIEIKYEGYIKKQQQYIKKLDRLE 559

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1539782540 565 DTRLPVDIDYTTISGLSKEIQGKLSQTRPQTLGQASRIPGVTPAAISLLLIHLKKRG 621
Cdd:TIGR00136 560 NVKIPADFDYRKIPGLSTEAREKLSKFRPLSLGQASRISGINPADISALLVYLKKQK 616
GIDA pfam01134
Glucose inhibited division protein A;
8-399 0e+00

Glucose inhibited division protein A;


Pssm-ID: 250388 [Multi-domain]  Cd Length: 391  Bit Score: 693.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540   8 DVIVIGGGHAGTEAALASARMGVKTLLLTHNVETLGHMSCNPAIGGIGKSHLVKEIDALGGAMALATDKSGIQFRVLNNR 87
Cdd:pfam01134   1 DVIVIGGGHAGCEAALAAARMGAKVLLITHNTDTIAELSCNPSIGGIAKGHLVREIDALGGLMGKAADKTGIQFRMLNTS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540  88 KGPAVRATRAQADRAIYKAVVREILENQPNLWIFQQSCDDLIVEQDQVKGVVTQMGLRFFAESVVLTTGTFLGGLIHIGL 167
Cdd:pfam01134  81 KGPAVRALRAQVDRDLYSKEMTETLENHPNLTLIQGEVTDLIPENGKVKGVVTEDGEEYKAKAVVLATGTFLNGKIHIGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540 168 QNHSGGRAGDPPSIALAHRMRELPLRVGRLKTGTPPRIDGRSVDFSVMTEQPGDTPIPVMSFMgNAEMHPRQVSCWITHT 247
Cdd:pfam01134 161 KCYPAGRLGELTSEGLSESLKELGFELGRFKTGTPPRIDKDSIDFSKLEEQPGDKPGPPFSYL-NCPMNKEQYPCFLTYT 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540 248 NARTHEIIASNLDRSPMYSGVIEGVGPRYCPSIEDKIHRFADKESHQVFIEPEGLNTHELYPNGISTSLPFDVQLELVRS 327
Cdd:pfam01134 240 NEATHEIIRDNLHRSPMFEGCIEGIGPRYCPSIEDKPVRFADKPYHQVFLEPEGLDTDEYYLVGFSTSLPEDVQKRVLRT 319

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1539782540 328 IRGMENAHIVRPGYAIEYDYFDPRDLKYSLETKVIGGLFFAGQINGTTGYEEAGAQGLLAGTNAALRAQGRD 399
Cdd:pfam01134 320 IPGLENAEIVRPGYAIEYDYIDPPQLLPTLETKKIPGLFFAGQINGTEGYEEAAAQGLLAGINAARKALGKE 391
PRK05335 PRK05335
tRNA (uracil-5-)-methyltransferase Gid; Reviewed
 311-399 9.85e-14

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


Pssm-ID: 235416  Cd Length: 436  Bit Score: 73.64  E-value: 9.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540 311 GISTSLPFDVQLELVRSIRGMENAHIVRPGYAIEYDYFD-PRDLKYSLETKVIGGLFFAGQINGTTGYEEAGAQGLLAGT 389
Cdd:PRK05335  278 GFQTKLKWGEQKRVFRMIPGLENAEFVRYGVMHRNTFINsPKLLDPTLQLKKRPNLFFAGQITGVEGYVESAASGLLAGI 357

                          90
                  ....*....|
gi 1539782540 390 NAALRAQGRD 399
Cdd:PRK05335  358 NAARLALGKE 367
 
Name Accession Description Interval E-value
MnmG COG0445
tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal ...
 1-625 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: 1275.71  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540   1 MDFPSRFDVIVIGGGHAGTEAALASARMGVKTLLLTHNVETLGHMSCNPAIGGIGKSHLVKEIDALGGAMALATDKSGIQ 80
Cdd:COG0445     1 MYYPKEYDVIVVGGGHAGCEAALAAARMGAKTLLLTHNLDTIGQMSCNPAIGGIAKGHLVREIDALGGEMGRAADKTGIQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540  81 FRVLNNRKGPAVRATRAQADRAIYKAVVREILENQPNLWIFQQSCDDLIVEQDQVKGVVTQMGLRFFAESVVLTTGTFLG 160
Cdd:COG0445    81 FRMLNTSKGPAVRAPRAQADRKLYRAAMRETLENQPNLDLIQGEVEDLIVEDGRVTGVVTADGIEFRAKAVVLTTGTFLN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540 161 GLIHIGLQNHSGGRAGDPPSIALAHRMRELPLRVGRLKTGTPPRIDGRSVDFSVMTEQPGDTPIPVMSFMGNaEMHPRQV 240
Cdd:COG0445   161 GLIHIGEKSYPGGRAGEPPSVGLSESLRELGFELGRLKTGTPPRIDGRSIDFSKLEEQPGDEPPPPFSFLTE-KIHPPQI 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540 241 SCWITHTNARTHEIIASNLDRSPMYSGVIEGVGPRYCPSIEDKIHRFADKESHQVFIEPEGLNTHELYPNGISTSLPFDV 320
Cdd:COG0445   240 PCWITYTNEETHEIIRENLHRSPMYSGVIEGVGPRYCPSIEDKIVRFADKDRHQIFLEPEGLDTNEVYPNGISTSLPEDV 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540 321 QLELVRSIRGMENAHIVRPGYAIEYDYFDPRDLKYSLETKVIGGLFFAGQINGTTGYEEAGAQGLLAGTNAALRAQGRDS 400
Cdd:COG0445   320 QLAMLRSIPGLENAEILRPGYAIEYDYVDPTQLKPTLETKKIEGLFFAGQINGTTGYEEAAAQGLMAGINAALKAQGKEP 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540 401 WCPRRDEAYIGVLVDDLITLGTQEPYRMFTSRAEYRLILREDNADLRLTEKGRELGLIDDQRWAAFCAKRDGIEREEQRL 480
Cdd:COG0445   400 FILDRSEAYIGVLIDDLVTKGTDEPYRMFTSRAEYRLLLRQDNADLRLTEKGYELGLVSDERYERFEEKKEAIEEEIERL 479

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540 481 KSTWVRPNTEQGQAIVDKFGTPLSHEYSLLNLLARPEIDYAGLIEATG-GEAIDPQVAEQVEIRTKYAGYIDRQQDEIAR 559
Cdd:COG0445   480 KSTRVTPNEEVNEGLEELGSSPLKRGVSLFDLLRRPEITYEDLAELDPeLPDLDPEVAEQVEIEIKYEGYIERQEEEIEK 559

                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1539782540 560 LRASEDTRLPVDIDYTTISGLSKEIQGKLSQTRPQTLGQASRIPGVTPAAISLLLIHLKKRGAGRE 625
Cdd:COG0445   560 LKRLENLKIPEDFDYDAIPGLSNEAREKLKKIRPETLGQASRISGVTPADISLLLVYLKRRRRRKK 625
gidA TIGR00136
glucose-inhibited division protein A; GidA, the longer of two forms of GidA-related proteins, ...
 7-621 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: 1003.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540   7 FDVIVIGGGHAGTEAALASARMGVKTLLLTHNVETLGHMSCNPAIGGIGKSHLVKEIDALGGAMALATDKSGIQFRVLNN 86
Cdd:TIGR00136   1 FDVIVIGGGHAGCEAALAAARLGAKTLLLTLNLDTIGKCSCNPAIGGPAKGILVKEIDALGGEMGKAADKTGLQFRVLNS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540  87 RKGPAVRATRAQADRAIYKAVVREILENQPNLWIFQQSCDDLIVEQ-DQVKGVVTQMGLRFFAESVVLTTGTFLGGLIHI 165
Cdd:TIGR00136  81 SKGPAVRATRAQIDKILYQKWMRNQLENQPNLSLFQGEVEDLILEDnDEIKGVVTKDGNEFRAKAVIITTGTFLRGKIHI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540 166 GLQNHSGGRAGDPPSIALAHRMRELPLRVGRLKTGTPPRIDGRSVDFSVMTEQPGDTPIPVMSFMGNaEMHPRQVSCWIT 245
Cdd:TIGR00136 161 GDKSYEAGRAGEQASYGLSTTLRELGFKTGRLKTGTPPRIDKRSIDFSKLEVQFGDTQPPAFSFTNK-NFLPQQLPCYLT 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540 246 HTNARTHEIIASNLDRSPMYSGVIEGVGPRYCPSIEDKIHRFADKESHQVFIEPEGLNTHELYPNGISTSLPFDVQLELV 325
Cdd:TIGR00136 240 HTNPKTHQIIRDNLHRSPMYSGSIEGNGPRYCPSIEDKVVRFADKERHQIFLEPEGLNSDEIYLNGLSTSLPEDVQLKII 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540 326 RSIRGMENAHIVRPGYAIEYDYFDPRDLKYSLETKVIGGLFFAGQINGTTGYEEAGAQGLLAGTNAALRAQGRDSWCPRR 405
Cdd:TIGR00136 320 RSIPGLENAEILRPGYAIEYDYFDPTQLKPTLETKLIKGLFFAGQINGTTGYEEAAAQGLMAGINAALKLQNKEPFILKR 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540 406 DEAYIGVLVDDLITLGTQEPYRMFTSRAEYRLILREDNADLRLTEKGRELGLIDDQRWAAFCAKRDGIEREEQRLKSTWV 485
Cdd:TIGR00136 400 NEAYIGVLIDDLVTKGTKEPYRMFTSRAEYRLLLREDNADFRLTEIGRELGLIDEDRYARFLKKKQNIEEEIERLKSTRL 479

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540 486 RPNTEQGQAIVDKFGTPLSHEYSLLNLLARPEIDYAGLIEATGGEAI-DPQVAEQVEIRTKYAGYIDRQQDEIARLRASE 564
Cdd:TIGR00136 480 SPSKEVKEELKNLAQSPLKDEVSGYDLLKRPEMNLDKLTKLLPFLPPlDEEVLEQVEIEIKYEGYIKKQQQYIKKLDRLE 559

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1539782540 565 DTRLPVDIDYTTISGLSKEIQGKLSQTRPQTLGQASRIPGVTPAAISLLLIHLKKRG 621
Cdd:TIGR00136 560 NVKIPADFDYRKIPGLSTEAREKLSKFRPLSLGQASRISGINPADISALLVYLKKQK 616
GIDA pfam01134
Glucose inhibited division protein A;
8-399 0e+00

Glucose inhibited division protein A;


Pssm-ID: 250388 [Multi-domain]  Cd Length: 391  Bit Score: 693.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540   8 DVIVIGGGHAGTEAALASARMGVKTLLLTHNVETLGHMSCNPAIGGIGKSHLVKEIDALGGAMALATDKSGIQFRVLNNR 87
Cdd:pfam01134   1 DVIVIGGGHAGCEAALAAARMGAKVLLITHNTDTIAELSCNPSIGGIAKGHLVREIDALGGLMGKAADKTGIQFRMLNTS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540  88 KGPAVRATRAQADRAIYKAVVREILENQPNLWIFQQSCDDLIVEQDQVKGVVTQMGLRFFAESVVLTTGTFLGGLIHIGL 167
Cdd:pfam01134  81 KGPAVRALRAQVDRDLYSKEMTETLENHPNLTLIQGEVTDLIPENGKVKGVVTEDGEEYKAKAVVLATGTFLNGKIHIGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540 168 QNHSGGRAGDPPSIALAHRMRELPLRVGRLKTGTPPRIDGRSVDFSVMTEQPGDTPIPVMSFMgNAEMHPRQVSCWITHT 247
Cdd:pfam01134 161 KCYPAGRLGELTSEGLSESLKELGFELGRFKTGTPPRIDKDSIDFSKLEEQPGDKPGPPFSYL-NCPMNKEQYPCFLTYT 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540 248 NARTHEIIASNLDRSPMYSGVIEGVGPRYCPSIEDKIHRFADKESHQVFIEPEGLNTHELYPNGISTSLPFDVQLELVRS 327
Cdd:pfam01134 240 NEATHEIIRDNLHRSPMFEGCIEGIGPRYCPSIEDKPVRFADKPYHQVFLEPEGLDTDEYYLVGFSTSLPEDVQKRVLRT 319

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1539782540 328 IRGMENAHIVRPGYAIEYDYFDPRDLKYSLETKVIGGLFFAGQINGTTGYEEAGAQGLLAGTNAALRAQGRD 399
Cdd:pfam01134 320 IPGLENAEIVRPGYAIEYDYIDPPQLLPTLETKKIPGLFFAGQINGTEGYEEAAAQGLLAGINAARKALGKE 391
GIDA_C pfam13932
tRNA modifying enzyme MnmG/GidA C-terminal domain; The GidA associated domain is a domain that ...
 401-614 2.35e-122

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: 360.93  E-value: 2.35e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540 401 WCPRRDEAYIGVLVDDLITLGTQEPYRMFTSRAEYRLILREDNADLRLTEKGRELGLIDDQRWAAFCAKRDGIEREEQRL 480
Cdd:pfam13932   1 LILSRSEAYIGVLIDDLVTKGTSEPYRMFTSRAEYRLLLRQDNADLRLTEKGRELGLVSDERYERFEEKKEAIEEEIERL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540 481 KSTWVRPNTEQGQAIVdKFGTPLSHEYSLLNLLARPEIDYAGLIEATGGEA-IDPQVAEQVEIRTKYAGYIDRQQDEIAR 559
Cdd:pfam13932  81 KSTRLSPSEWNNALLE-LGSAPLGTGRSAFDLLRRPEVTYEDLAALIPELApLDPEVLEQVEIEAKYEGYIERQEAEIEK 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1539782540 560 LRASEDTRLPVDIDYTTISGLSKEIQGKLSQTRPQTLGQASRIPGVTPAAISLLL 614
Cdd:pfam13932 160 FKRLENLKIPEDLDYDAIPGLSNEAREKLNKIRPETIGQASRISGVTPADISVLL 214
PRK05335 PRK05335
tRNA (uracil-5-)-methyltransferase Gid; Reviewed
 311-399 9.85e-14

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


Pssm-ID: 235416  Cd Length: 436  Bit Score: 73.64  E-value: 9.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540 311 GISTSLPFDVQLELVRSIRGMENAHIVRPGYAIEYDYFD-PRDLKYSLETKVIGGLFFAGQINGTTGYEEAGAQGLLAGT 389
Cdd:PRK05335  278 GFQTKLKWGEQKRVFRMIPGLENAEFVRYGVMHRNTFINsPKLLDPTLQLKKRPNLFFAGQITGVEGYVESAASGLLAGI 357

                          90
                  ....*....|
gi 1539782540 390 NAALRAQGRD 399
Cdd:PRK05335  358 NAARLALGKE 367
TrmFO COG1206
Folate-dependent tRNA-U54 methylase TrmFO/GidA [Translation, ribosomal structure and ...
 314-399 9.09e-13

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: 70.47  E-value: 9.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540 314 TSLPFDVQLELVRSIRGMENAHIVRPGyAIEYDYF--DPRDLKYSLETKVIGGLFFAGQINGTTGYEEAGAQGLLAGTNA 391
Cdd:COG1206   281 TKLKWGEQKRVFRMIPGLENAEFVRYG-VMHRNTFinSPKLLDPTLQLKARPNLFFAGQITGVEGYVESAASGLLAGINA 359


                  ....*...
gi 1539782540 392 ALRAQGRD 399
Cdd:COG1206   360 ARLLLGKE 367
FAD_oxidored pfam12831
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ...
 8-156 2.92e-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: 59.54  E-value: 2.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540   8 DVIVIGGGHAGTEAALASARMGVKTLLlthnVETLGHmscnpaIGGIGKShlvkeidALGGAMALATDK-----SGI--Q 80
Cdd:pfam12831   1 DVVVVGGGPAGVAAAIAAARAGAKVLL----VERRGF------LGGMLTS-------GLVGPDMGFYLNkeqvvGGIarE 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540  81 FRV-LNNRKGPAVRATRAQA----DRAIYKAVVREILEnQPNL-WIFQQSCDDLIVEQDQVKGVVTQM---GLRFFAESV 151
Cdd:pfam12831  64 FRQrLRARGGLPGPYGLRGGwvpfDPEVAKAVLDEMLA-EAGVtVLLHTRVVGVVKEGGRITGVTVETkggRITIRAKVF 142


                  ....*
gi 1539782540 152 VLTTG 156
Cdd:pfam12831 143 IDATG 147
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
 7-156 4.49e-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: 46.36  E-value: 4.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540   7 FDVIVIGGGHAGTEAALASARMGVKTLLLTHNVETLGH---------MSCNPAIGGIGK----SH---LVKEIDALG--- 67
Cdd:COG1053     4 YDVVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGGHtaaaqgginAAGTNVQKAAGEdspeEHfydTVKGGDGLAdqd 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540  68 ---------GAMALATDKSGIQFRV-----LNNRKGPAVRATRAQADR-------AIYKAVVR---EILENQPnlwifqq 123
Cdd:COG1053    84 lvealaeeaPEAIDWLEAQGVPFSRtpdgrLPQFGGHSVGRTCYAGDGtghallaTLYQAALRlgvEIFTETE------- 156

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1539782540 124 sCDDLIVEQDQVKGVVTQMG----LRFFAESVVLTTG 156
Cdd:COG1053   157 -VLDLIVDDGRVVGVVARDRtgeiVRIRAKAVVLATG 192
PRK05329 PRK05329
glycerol-3-phosphate dehydrogenase subunit GlpB;
6-46 8.39e-05

glycerol-3-phosphate dehydrogenase subunit GlpB;


Pssm-ID: 235412  Cd Length: 422  Bit Score: 45.23  E-value: 8.39e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1539782540   6 RFDVIVIGGGHAGTEAALASARMGVKTLLLTHNVETLGHMS 46
Cdd:PRK05329    2 KFDVLVIGGGLAGLTAALAAAEAGKRVALVAKGQGALHFSS 42
GlpB COG3075
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism];
6-42 1.45e-04

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


Pssm-ID: 442309  Cd Length: 415  Bit Score: 44.40  E-value: 1.45e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1539782540   6 RFDVIVIGGGHAGTEAALASARMGVKTLLLTHNVETL 42
Cdd:COG3075     2 KFDVVVIGGGLAGLTAAIRAAEAGLRVAIVSAGQSAL 38
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
7-156 3.41e-04

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 43.18  E-value: 3.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540   7 FDVIVIGGGHAGTEAALASARMGVKTLLLthnvetlghmscnpaiggigkshlvkEIDALGGAMALATD-------KSGI 79
Cdd:COG0492     1 YDVVIIGAGPAGLTAAIYAARAGLKTLVI--------------------------EGGEPGGQLATTKEienypgfPEGI 54

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540  80 QfrvlnnrkGPA-VRATRAQADRaiYKAVVR--EILEnqpnlwifqqscddlIVEQDQVKGVVTQMGLRFFAESVVLTTG 156
Cdd:COG0492    55 S--------GPElAERLREQAER--FGAEILleEVTS---------------VDKDDGPFRVTTDDGTEYEAKAVIIATG 109
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 7-35 3.68e-04

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


Pssm-ID: 400379 [Multi-domain]  Cd Length: 301  Bit Score: 43.08  E-value: 3.68e-04
                          10        20
                  ....*....|....*....|....*....
gi 1539782540   7 FDVIVIGGGHAGTEAALASARMGVKTLLL 35
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLI 29
HI0933_like pfam03486
HI0933-like protein;
7-156 8.47e-04

HI0933-like protein;


Pssm-ID: 427330 [Multi-domain]  Cd Length: 406  Bit Score: 42.18  E-value: 8.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540   7 FDVIVIGGGHAGTEAALASARMGVKTLLLTHNVETL------GHMSCNPAIGGIGKSHLVKEIDALGGAM--ALAT---- 74
Cdd:pfam03486   1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLGrkilisGGGRCNVTNLSEEPDNFLSRYPGNPKFLksALSRftpw 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539782540  75 ------DKSGIQFRVLNN-RKGPAvratraqADRA--IYKAVVREILENQPNLwIFQQSCDDLIVEQDQVKGVVTQmGLR 145
Cdd:pfam03486  81 dfiaffESLGVPLKEEDHgRLFPD-------SDKAsdIVDALLNELKELGVKI-RLRTRVLSVEKDDDGRFRVKTG-GEE 151

                         170
                  ....*....|.
gi 1539782540 146 FFAESVVLTTG 156
Cdd:pfam03486 152 LEADSLVLATG 162
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 7-34 1.19e-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: 41.61  E-value: 1.19e-03
                          10        20
                  ....*....|....*....|....*...
gi 1539782540   7 FDVIVIGGGHAGTEAALASARMGVKTLL 34
Cdd:COG1249     4 YDLVVIGAGPGGYVAAIRAAQLGLKVAL 31
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
8-53 2.00e-03

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 41.00  E-value: 2.00e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1539782540   8 DVIVIGGGHAGTEAALASARMGVKTLLlthnVETlghmscNPAIGG 53
Cdd:COG1148   142 RALVIGGGIAGMTAALELAEQGYEVYL----VEK------EPELGG 177
PRK15317 PRK15317
alkyl hydroperoxide reductase subunit F; Provisional
 7-32 2.24e-03

alkyl hydroperoxide reductase subunit F; Provisional


Pssm-ID: 237942 [Multi-domain]  Cd Length: 517  Bit Score: 40.91  E-value: 2.24e-03
                          10        20
                  ....*....|....*....|....*.
gi 1539782540   7 FDVIVIGGGHAGTEAALASARMGVKT 32
Cdd:PRK15317  212 YDVLVVGGGPAGAAAAIYAARKGIRT 237
PRK08274 PRK08274
FAD-dependent tricarballylate dehydrogenase TcuA;
4-35 3.13e-03

FAD-dependent tricarballylate dehydrogenase TcuA;


Pssm-ID: 236214 [Multi-domain]  Cd Length: 466  Bit Score: 40.24  E-value: 3.13e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1539782540   4 PSRFDVIVIGGGHAGTEAALASARMGVKTLLL 35
Cdd:PRK08274    2 ASMVDVLVIGGGNAALCAALAAREAGASVLLL 33
glycerol3P_GlpB TIGR03378
glycerol-3-phosphate dehydrogenase, anaerobic, B subunit; Members of this protein family are ...
 7-36 3.28e-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: 40.39  E-value: 3.28e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1539782540   7 FDVIVIGGGHAGTEAALASARMGVKTLLLT 36
Cdd:TIGR03378   1 FDVIIIGGGLAGLSCALRLAEAGKKCAIIA 30
PRK13800 PRK13800
fumarate reductase/succinate dehydrogenase flavoprotein subunit;
8-35 5.75e-03

fumarate reductase/succinate dehydrogenase flavoprotein subunit;


Pssm-ID: 237512 [Multi-domain]  Cd Length: 897  Bit Score: 39.83  E-value: 5.75e-03
                          10        20
                  ....*....|....*....|....*...
gi 1539782540   8 DVIVIGGGHAGTEAALASARMGVKTLLL 35
Cdd:PRK13800   15 DVLVIGGGTAGTMAALTAAEHGANVLLL 42
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 5-35 7.27e-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: 7.27e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1539782540   5 SRFDVIVIGGGHAGTEAALASARMGVKTLLL 35
Cdd:COG1233     2 MMYDVVVIGAGIGGLAAAALLARAGYRVTVL 32
 
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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