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Conserved domains on  [gi|1780591731|emb|VYS56282|]
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unnamed protein product [Arabidopsis thaliana]

Protein Classification

diphthine--ammonia ligase family protein( domain architecture ID 10113413)

diphthine--ammonia ligase family protein belonging to the adenine nucleotide alpha hydrolase (AANH) superfamily, similar to diphthine--ammonia ligase, an amidase that catalyzes the conversion of diphthine to diphthamide using ammonium and ATP

CATH:  3.40.50.620
EC:  6.3.1.14
Gene Ontology:  GO:0005524|GO:0017178|GO:0017183
PubMed:  12012333
SCOP:  3001593

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AANH_PF0828-like cd01994
putative ATP pyrophosphatase PF0828 and similar proteins; This subfamily includes Pyrococcus ...
 2-217 1.79e-101

putative ATP pyrophosphatase PF0828 and similar proteins; This subfamily includes Pyrococcus furiosus putative ATP pyrophosphatase PF0828 and Pyrococcus horikoshii PH1257. They belong to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. This subfamily of proteins is predicted to bind ATP. This domain has a strongly conserved motif SGGKD at the N-terminus.


:

Pssm-ID: 467498  Cd Length: 211  Bit Score: 309.99  E-value: 1.79e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591731   2 KVVALVSGGKDSCYAMMKCIQYGHEIVALANLLPVDDsvdelDSYMYQTVGHQILVGYAECMNVPLFRRRIRGSSRHQKL 81
Cdd:cd01994     1 KVVALISGGKDSIYALLHAIRNGHEVVALANLRPEDK-----DSYMFQTVGHELLELQAEALGLPLIRREIRGKSVTQEL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591731  82 SYQMTPDDEVEDMFVLLSEVKRQiPSITAVSSGAIASDYQRLRVESICSRLGLVSLAFLWKQDQTLLLQDMIANGIKAIL 161
Cdd:cd01994    76 GYEGEEEDEVEDLYELLKKVKER-PEVEAVVSGAILSDYQRNRVERVCERLGLKSLAPLWQRDQEELLEELIDLGFEARI 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1780591731 162 VKVAAIGLDPsKHLGKDLAFMEP-YLLKLKEKYGSNVCGEGGEYETLTLDCPLFTNA 217
Cdd:cd01994   155 VKVAAMGLDE-EWLGRRLDEDQPeELLKLNEKYGVHVCGEGGEYETLVLDGPLFKKR 210
eu_AANH_C_2 cd06156
A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine ...
 431-551 1.55e-35

A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine nucleotide alpha hydrolase (AANH)-like domain located N-terminal to two distinctly different YjgF-YER057c-UK114-like domains. This CD contains the second of these domains. The YjgF-YER057c-UK114 protein family is a large family of proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site.


:

Pssm-ID: 100013  Cd Length: 118  Bit Score: 130.14  E-value: 1.55e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591731 431 YSQATLHQSVLHMAGQLGLDPPTMNLQTEGAIAELNQALTNSEAIAESFNCSISssaILFVVFCSARTKQSERNQLHEKF 510
Cdd:cd06156     1 YSQAIVVPKVAYISGQIGLIPATMTLLEGGITLQAVLSLQHLERVAKAMNVQWV---LAAVCYVTDESSVPIARSAWSKY 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1780591731 511 VTFLGLAKSSRRVQNVLDPMFLYILVPDLPKRALVEVKPIL 551
Cdd:cd06156    78 CSELDLEDESRNESDDVNPPLVIVVVPELPRGALVEWQGIA 118
eu_AANH_C_1 cd06155
A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine ...
 297-392 2.22e-24

A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine nucleotide alpha hydrolase (AANH)-like domain located N-terminal to two distinctly different YjgF-YER057c-UK114-like domains. This CD contains the first of these domains. The YjgF-YER057c-UK114 protein family is a large family of proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site.


:

Pssm-ID: 100012  Cd Length: 101  Bit Score: 97.71  E-value: 2.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591731 297 LHISRAEKHNTFSICCWledsSESSKGLKEDLETVLTELESQLLKHGYNWQHVLYIHLYISDMSEFAVANETYVKFITQe 376
Cdd:cd06155     1 LSQNRTGGLLWISNVTA----SESDETVEEQMESIFSKLREILQSNGLSLSDILYVTLYLRDMSDFAEVNSVYGTFFDK- 75

                          90
                  ....*....|....*.
gi 1780591731 377 kcpFGVPSRSTIELPL 392
Cdd:cd06155    76 ---PNPPSRVCVECGL 88
 
Name Accession Description Interval E-value
AANH_PF0828-like cd01994
putative ATP pyrophosphatase PF0828 and similar proteins; This subfamily includes Pyrococcus ...
 2-217 1.79e-101

putative ATP pyrophosphatase PF0828 and similar proteins; This subfamily includes Pyrococcus furiosus putative ATP pyrophosphatase PF0828 and Pyrococcus horikoshii PH1257. They belong to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. This subfamily of proteins is predicted to bind ATP. This domain has a strongly conserved motif SGGKD at the N-terminus.


Pssm-ID: 467498  Cd Length: 211  Bit Score: 309.99  E-value: 1.79e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591731   2 KVVALVSGGKDSCYAMMKCIQYGHEIVALANLLPVDDsvdelDSYMYQTVGHQILVGYAECMNVPLFRRRIRGSSRHQKL 81
Cdd:cd01994     1 KVVALISGGKDSIYALLHAIRNGHEVVALANLRPEDK-----DSYMFQTVGHELLELQAEALGLPLIRREIRGKSVTQEL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591731  82 SYQMTPDDEVEDMFVLLSEVKRQiPSITAVSSGAIASDYQRLRVESICSRLGLVSLAFLWKQDQTLLLQDMIANGIKAIL 161
Cdd:cd01994    76 GYEGEEEDEVEDLYELLKKVKER-PEVEAVVSGAILSDYQRNRVERVCERLGLKSLAPLWQRDQEELLEELIDLGFEARI 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1780591731 162 VKVAAIGLDPsKHLGKDLAFMEP-YLLKLKEKYGSNVCGEGGEYETLTLDCPLFTNA 217
Cdd:cd01994   155 VKVAAMGLDE-EWLGRRLDEDQPeELLKLNEKYGVHVCGEGGEYETLVLDGPLFKKR 210
MJ0570_dom TIGR00290
MJ0570-related uncharacterized domain; Proteins with this uncharacterized domain include two ...
 1-214 6.08e-57

MJ0570-related uncharacterized domain; Proteins with this uncharacterized domain include two apparent ortholog families in the Archaea, one of which is universal among the first four completed archaeal genomes, and YLR143W, a much longer protein from Saccharomyces cerevisiae. The domain comprises the full length of the archaeal proteins and the first third of the yeast protein.


Pssm-ID: 273000  Cd Length: 223  Bit Score: 193.07  E-value: 6.08e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591731   1 MKVVALVSGGKDSCYAMMKCIQyGHEIVALANLLPvddsvDELDSYMYQTVGHQILVGYAECMNVPLFrrrirgssrhqK 80
Cdd:TIGR00290   1 MKVAALISGGKDSCLALYHALK-EHEVISLVNIMP-----ENEESYMFHGVNAHLTDLQAESIGIPLI-----------K 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591731  81 LSYQMTPDDEVEDMFVLLSEVKrqipsITAVSSGAIASDYQRLRVESICSRLGLVSLAFLWKQDQTLLLQDMIANGIKAI 160
Cdd:TIGR00290  64 LYTEGTEEDEVEELKGILHTLD-----VEAVVFGAIYSEYQKTRIERVCRELGLKSFAPLWHRDPEKLMEEFVEEKFEAR 138

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1780591731 161 LVKVAAIGLDPSkHLGKDL-AFMEPYLLKLKEKYGSNVCGEGGEYETLTLDCPLF 214
Cdd:TIGR00290 139 IIAVAAEGLDES-WLGRRIdRKMIDELKKLNEKYGIHPAGEGGEFETLVLDAPIF 192
Dph6 COG2102
Diphthamide synthase (EF-2-diphthine--ammonia ligase) [Translation, ribosomal structure and ...
 3-229 2.31e-52

Diphthamide synthase (EF-2-diphthine--ammonia ligase) [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441705  Cd Length: 213  Bit Score: 180.32  E-value: 2.31e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591731   3 VVALVSGGKDSCYAMMKCIQYGHEIVALANLLPVDDsvdelDSYMYQTVGHQILVGYAECMNVPLFRRRIRGSsrhqkls 82
Cdd:COG2102     1 VVVSWSGGKDSALALYRALQEGYEVVGLLTTVPEDF-----DRVMFHGPNLELLEAQAEALGIPLIEIELSGS------- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591731  83 yqmtPDDEVEDMFVLLSEVKRQipSITAVSSGAIASDYQRLRVESICSRLGLVSLAFLWKQDQTLLLQDMIANGIKAILV 162
Cdd:COG2102    69 ----NEEYEEELEEALKELKAE--GIEGVVFGDIFLEDQRDYRERVCEELGLEAVFPLWGRDTEELLEEFIDAGFEAIIV 142

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1780591731 163 KVAAIGLDPSkHLGKDL--AFMEpyllKLKEkYGSNVCGEGGEYETLTLDCPLFtNASIVLDEYQVVLH 229
Cdd:COG2102   143 CVDAEGLDES-WLGRELdeELLE----ELPA-YGVDPCGEGGEFHTFVLDGPLF-KKPIEIEEGEIVWR 204
Diphthami_syn_2 pfam01902
Diphthamide synthase; Diphthamide_syn, diphthamide synthase, catalyzes the last amidation step ...
 1-214 9.01e-37

Diphthamide synthase; Diphthamide_syn, diphthamide synthase, catalyzes the last amidation step of diphthamide biosynthesis using ammonium and ATP. Diphthamide synthase is evolutionarily conserved in eukaryotes. Diphthamide is a post-translationally modified histidine residue found on archaeal and eukaryotic translation elongation factor 2 (eEF-2). In some members of this family, this domain is associated with pfam01042. The enzyme classification is EC:6.3.1.14.


Pssm-ID: 280139  Cd Length: 219  Bit Score: 137.24  E-value: 9.01e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591731   1 MKVVALVSGGKDSCYAMMKCIQyGHEIVALANLLPvddsvDELDSYMYQTVGHQILVGYAECMNVPLFRRRIRGSSrhqk 80
Cdd:pfam01902   1 MKVAALYSGGKDSCLALYRALK-EMEVDSLVCVMS-----ENKESYMFHGPNAHLTKLQAESVGIPLIKLYTTGEE---- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591731  81 lsyqmtpDDEVEDMFVLLSEVKrqipsITAVSSGAIASDYQRLRVESICSRLGLVSLAFLWKQDQTLLLQDMIANGIKAI 160
Cdd:pfam01902  71 -------EKEVEDLKGILHRLD-----VEAAVFGAIYSEYQKSRIERVCRELGLKSFAPLWHEDPEELAEEFVEEGFEAY 138

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1780591731 161 LVKVAAIGLDPSkHLGK--DLAFMEPyLLKLKEKYGSNVCGEGGEYETLTLDCPLF 214
Cdd:pfam01902 139 VVAVKAEGLDES-WLGRriDRKFIDE-LKKLNEKYGIHPAGEGGEFETLVLDGPIF 192
eu_AANH_C_2 cd06156
A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine ...
 431-551 1.55e-35

A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine nucleotide alpha hydrolase (AANH)-like domain located N-terminal to two distinctly different YjgF-YER057c-UK114-like domains. This CD contains the second of these domains. The YjgF-YER057c-UK114 protein family is a large family of proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site.


Pssm-ID: 100013  Cd Length: 118  Bit Score: 130.14  E-value: 1.55e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591731 431 YSQATLHQSVLHMAGQLGLDPPTMNLQTEGAIAELNQALTNSEAIAESFNCSISssaILFVVFCSARTKQSERNQLHEKF 510
Cdd:cd06156     1 YSQAIVVPKVAYISGQIGLIPATMTLLEGGITLQAVLSLQHLERVAKAMNVQWV---LAAVCYVTDESSVPIARSAWSKY 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1780591731 511 VTFLGLAKSSRRVQNVLDPMFLYILVPDLPKRALVEVKPIL 551
Cdd:cd06156    78 CSELDLEDESRNESDDVNPPLVIVVVPELPRGALVEWQGIA 118
eu_AANH_C_1 cd06155
A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine ...
 297-392 2.22e-24

A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine nucleotide alpha hydrolase (AANH)-like domain located N-terminal to two distinctly different YjgF-YER057c-UK114-like domains. This CD contains the first of these domains. The YjgF-YER057c-UK114 protein family is a large family of proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site.


Pssm-ID: 100012  Cd Length: 101  Bit Score: 97.71  E-value: 2.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591731 297 LHISRAEKHNTFSICCWledsSESSKGLKEDLETVLTELESQLLKHGYNWQHVLYIHLYISDMSEFAVANETYVKFITQe 376
Cdd:cd06155     1 LSQNRTGGLLWISNVTA----SESDETVEEQMESIFSKLREILQSNGLSLSDILYVTLYLRDMSDFAEVNSVYGTFFDK- 75

                          90
                  ....*....|....*.
gi 1780591731 377 kcpFGVPSRSTIELPL 392
Cdd:cd06155    76 ---PNPPSRVCVECGL 88
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
 418-553 1.14e-09

Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 family [Defense mechanisms]; Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 family is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 440021  Cd Length: 125  Bit Score: 56.73  E-value: 1.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591731 418 QSISCWAPSCIGPYSQATLHQSVLHMAGQLGLDPPTMNLqTEGAIAELNQALTNSEAIAESFNCSISSsaILFV-VFCSA 496
Cdd:COG0251     4 ELINPPAPAPIGPYSQAVRVGNLVFVSGQVPLDPDTGEL-GGDIEAQTRQVLENILAVLAAAGGSLDD--VVKVtVYLTD 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1780591731 497 RtkqSERNQLHEKFVTFLGLAKSSRRVqnvldpmflyILVPDLPKRALVEVKPILYV 553
Cdd:COG0251    81 M---ADFAAVNEVYAEYFGEGRPARTA----------VGVAALPKGALVEIEAIAAL 124
TIGR00004 TIGR00004
reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of ...
 424-553 1.24e-09

reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of protein synthesis intiation, then as an endoribonuclease active on single-stranded mRNA, endoribonuclease L-PSP. Members of this family, conserved in all domains of life and often with several members per bacterial genome, appear to catalyze a reaction that minimizes toxic by-products from reactions catalyzed by pyridoxal phosphate-dependent enzymes. [Cellular processes, Other]


Pssm-ID: 129116  Cd Length: 124  Bit Score: 56.53  E-value: 1.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591731 424 APSCIGPYSQATLHQSVLHMAGQLGLDPPTMNLQTEGAIAELNQALTNSEAIAESFNCSIsSSAILFVVFCSARTKQSER 503
Cdd:TIGR00004   9 APAAIGPYSQAVKVGNTVYVSGQIPLDPSTGELVGGDIAEQAEQVLENLKAILEAAGLSL-DDVVKTTVFLTDLNDFAEV 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1780591731 504 NQLHEKFVTFLGLAKSSrrVQnvldpmflyilVPDLPKRALVEVKPILYV 553
Cdd:TIGR00004  88 NEVYGQYFDEHYPARSA--VQ-----------VAALPKGVLVEIEAIAVK 124
Ribonuc_L-PSP pfam01042
Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein ...
 424-550 2.85e-09

Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein synthesis by cleavage of mRNA. Previously thought to inhibit protein synthesis initiation. This protein may also be involved in the regulation of purine biosynthesis. YjgF (renamed RidA) family members are enamine/imine deaminases. They hydrolyze reactive intermediates released by PLP-dependent enzymes, including threonine dehydratase. YjgF also prevents inhibition of transaminase B (IlvE) in Salmonella.


Pssm-ID: 426010  Cd Length: 117  Bit Score: 55.38  E-value: 2.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591731 424 APSCIGPYSQATLHQSVLHMAGQLGLDPPTMNLQTEGAIAELNQALTNSEAIAESFNCSISSsaILFV-VFCSARTKQSE 502
Cdd:pfam01042   2 APAAAGPYSQAVKAGNLVYVSGQIPLDPDTGKLVEGDVAEQTRQVLENIKAVLAAAGASLSD--VVKVtIFLADMNDFAE 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1780591731 503 RNQLHEKFVTFLGL-AKSSrrVQnvldpmflyilVPDLPKRALVEVKPI 550
Cdd:pfam01042  80 VNEVYAEYFDADKApARSA--VG-----------VAALPLGALVEIEAI 115
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
 313-407 3.73e-06

Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 family [Defense mechanisms]; Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 family is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 440021  Cd Length: 125  Bit Score: 46.71  E-value: 3.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591731 313 WLEDSSESSKGLKEDLETVLTELESQLLKHGYNWQHVLYIHLYISDMSEFAVANETYVKFITQekcpfGVPSRSTIElpl 392
Cdd:COG0251    35 LDPDTGELGGDIEAQTRQVLENILAVLAAAGGSLDDVVKVTVYLTDMADFAAVNEVYAEYFGE-----GRPARTAVG--- 106

                          90
                  ....*....|....*...
gi 1780591731 393 vQAGLGKAY---IEVLVA 407
Cdd:COG0251   107 -VAALPKGAlveIEAIAA 123
Ribonuc_L-PSP pfam01042
Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein ...
 321-407 1.97e-03

Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein synthesis by cleavage of mRNA. Previously thought to inhibit protein synthesis initiation. This protein may also be involved in the regulation of purine biosynthesis. YjgF (renamed RidA) family members are enamine/imine deaminases. They hydrolyze reactive intermediates released by PLP-dependent enzymes, including threonine dehydratase. YjgF also prevents inhibition of transaminase B (IlvE) in Salmonella.


Pssm-ID: 426010  Cd Length: 117  Bit Score: 38.43  E-value: 1.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591731 321 SKGLKEDLETVLTELESQLLKHGYNWQHVLYIHLYISDMSEFAVANETYVKFITQEKcpfgVPSRSTIELPLVQAGLgKA 400
Cdd:pfam01042  36 EGDVAEQTRQVLENIKAVLAAAGASLSDVVKVTIFLADMNDFAEVNEVYAEYFDADK----APARSAVGVAALPLGA-LV 110


                  ....*..
gi 1780591731 401 YIEVLVA 407
Cdd:pfam01042 111 EIEAIAV 117
 
Name Accession Description Interval E-value
AANH_PF0828-like cd01994
putative ATP pyrophosphatase PF0828 and similar proteins; This subfamily includes Pyrococcus ...
 2-217 1.79e-101

putative ATP pyrophosphatase PF0828 and similar proteins; This subfamily includes Pyrococcus furiosus putative ATP pyrophosphatase PF0828 and Pyrococcus horikoshii PH1257. They belong to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. This subfamily of proteins is predicted to bind ATP. This domain has a strongly conserved motif SGGKD at the N-terminus.


Pssm-ID: 467498  Cd Length: 211  Bit Score: 309.99  E-value: 1.79e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591731   2 KVVALVSGGKDSCYAMMKCIQYGHEIVALANLLPVDDsvdelDSYMYQTVGHQILVGYAECMNVPLFRRRIRGSSRHQKL 81
Cdd:cd01994     1 KVVALISGGKDSIYALLHAIRNGHEVVALANLRPEDK-----DSYMFQTVGHELLELQAEALGLPLIRREIRGKSVTQEL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591731  82 SYQMTPDDEVEDMFVLLSEVKRQiPSITAVSSGAIASDYQRLRVESICSRLGLVSLAFLWKQDQTLLLQDMIANGIKAIL 161
Cdd:cd01994    76 GYEGEEEDEVEDLYELLKKVKER-PEVEAVVSGAILSDYQRNRVERVCERLGLKSLAPLWQRDQEELLEELIDLGFEARI 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1780591731 162 VKVAAIGLDPsKHLGKDLAFMEP-YLLKLKEKYGSNVCGEGGEYETLTLDCPLFTNA 217
Cdd:cd01994   155 VKVAAMGLDE-EWLGRRLDEDQPeELLKLNEKYGVHVCGEGGEYETLVLDGPLFKKR 210
MJ0570_dom TIGR00290
MJ0570-related uncharacterized domain; Proteins with this uncharacterized domain include two ...
 1-214 6.08e-57

MJ0570-related uncharacterized domain; Proteins with this uncharacterized domain include two apparent ortholog families in the Archaea, one of which is universal among the first four completed archaeal genomes, and YLR143W, a much longer protein from Saccharomyces cerevisiae. The domain comprises the full length of the archaeal proteins and the first third of the yeast protein.


Pssm-ID: 273000  Cd Length: 223  Bit Score: 193.07  E-value: 6.08e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591731   1 MKVVALVSGGKDSCYAMMKCIQyGHEIVALANLLPvddsvDELDSYMYQTVGHQILVGYAECMNVPLFrrrirgssrhqK 80
Cdd:TIGR00290   1 MKVAALISGGKDSCLALYHALK-EHEVISLVNIMP-----ENEESYMFHGVNAHLTDLQAESIGIPLI-----------K 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591731  81 LSYQMTPDDEVEDMFVLLSEVKrqipsITAVSSGAIASDYQRLRVESICSRLGLVSLAFLWKQDQTLLLQDMIANGIKAI 160
Cdd:TIGR00290  64 LYTEGTEEDEVEELKGILHTLD-----VEAVVFGAIYSEYQKTRIERVCRELGLKSFAPLWHRDPEKLMEEFVEEKFEAR 138

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1780591731 161 LVKVAAIGLDPSkHLGKDL-AFMEPYLLKLKEKYGSNVCGEGGEYETLTLDCPLF 214
Cdd:TIGR00290 139 IIAVAAEGLDES-WLGRRIdRKMIDELKKLNEKYGIHPAGEGGEFETLVLDAPIF 192
arCOG00187 TIGR03679
arCOG00187 universal archaeal metal-binding-domain/4Fe-4S-binding-domain containing ABC ...
 4-229 1.40e-53

arCOG00187 universal archaeal metal-binding-domain/4Fe-4S-binding-domain containing ABC transporter, ATP-binding protein; This protein consists of an N-terminal possible metal-binding domain (pfam04068) followed by a 4Fe-4S cluster binding domain (pfam00037) followed by a C-terminal ABC transporter, ATP-binding domain (pfam00005). This combination of N-terminal domains is observed in the RNase L inhibitor, RLI. This model has the same scope as an archaeal COG (arCOG00187) and is found in all completely sequenced archaea and does not recognize any known non-archaeal genes.


Pssm-ID: 188368  Cd Length: 218  Bit Score: 184.00  E-value: 1.40e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591731   4 VALVSGGKDSCYAMMKCIQYGHEIVALANLLPvddsvDELDSYMYQTVGHQILVGYAECMNVPLFRRRIRGSSrhqklsy 83
Cdd:TIGR03679   1 AALYSGGKDSNYALYKALEEGHEVTCLITVVP-----ENEDSYMFHTPNIELTRLQAEALGIPLVEIETSGEK------- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591731  84 qmtpDDEVEDMFVLLSEVKRQipSITAVSSGAIASDYQRLRVESICSRLGLVSLAFLWKQDQTLLLQDMIANGIKAILVK 163
Cdd:TIGR03679  69 ----EKEVEDLKGALKELKEE--GVEGIVTGAIASEYQKSRIERICEELGLKVFAPLWGRDPEEYLRELVERGFRFIIVS 142

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1780591731 164 VAAIGLDPSkHLGK--DLAFMEpYLLKLKEKYGSNVCGEGGEYETLTLDCPLFTNaSIVLDEYQVVLH 229
Cdd:TIGR03679 143 VSAYGLDES-WLGReiDEKYIE-ELKALNKRYGINPAGEGGEYETLVLDAPLFKR-RIEIVEYEKKWS 207
Dph6 COG2102
Diphthamide synthase (EF-2-diphthine--ammonia ligase) [Translation, ribosomal structure and ...
 3-229 2.31e-52

Diphthamide synthase (EF-2-diphthine--ammonia ligase) [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441705  Cd Length: 213  Bit Score: 180.32  E-value: 2.31e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591731   3 VVALVSGGKDSCYAMMKCIQYGHEIVALANLLPVDDsvdelDSYMYQTVGHQILVGYAECMNVPLFRRRIRGSsrhqkls 82
Cdd:COG2102     1 VVVSWSGGKDSALALYRALQEGYEVVGLLTTVPEDF-----DRVMFHGPNLELLEAQAEALGIPLIEIELSGS------- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591731  83 yqmtPDDEVEDMFVLLSEVKRQipSITAVSSGAIASDYQRLRVESICSRLGLVSLAFLWKQDQTLLLQDMIANGIKAILV 162
Cdd:COG2102    69 ----NEEYEEELEEALKELKAE--GIEGVVFGDIFLEDQRDYRERVCEELGLEAVFPLWGRDTEELLEEFIDAGFEAIIV 142

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1780591731 163 KVAAIGLDPSkHLGKDL--AFMEpyllKLKEkYGSNVCGEGGEYETLTLDCPLFtNASIVLDEYQVVLH 229
Cdd:COG2102   143 CVDAEGLDES-WLGRELdeELLE----ELPA-YGVDPCGEGGEFHTFVLDGPLF-KKPIEIEEGEIVWR 204
Diphthami_syn_2 pfam01902
Diphthamide synthase; Diphthamide_syn, diphthamide synthase, catalyzes the last amidation step ...
 1-214 9.01e-37

Diphthamide synthase; Diphthamide_syn, diphthamide synthase, catalyzes the last amidation step of diphthamide biosynthesis using ammonium and ATP. Diphthamide synthase is evolutionarily conserved in eukaryotes. Diphthamide is a post-translationally modified histidine residue found on archaeal and eukaryotic translation elongation factor 2 (eEF-2). In some members of this family, this domain is associated with pfam01042. The enzyme classification is EC:6.3.1.14.


Pssm-ID: 280139  Cd Length: 219  Bit Score: 137.24  E-value: 9.01e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591731   1 MKVVALVSGGKDSCYAMMKCIQyGHEIVALANLLPvddsvDELDSYMYQTVGHQILVGYAECMNVPLFRRRIRGSSrhqk 80
Cdd:pfam01902   1 MKVAALYSGGKDSCLALYRALK-EMEVDSLVCVMS-----ENKESYMFHGPNAHLTKLQAESVGIPLIKLYTTGEE---- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591731  81 lsyqmtpDDEVEDMFVLLSEVKrqipsITAVSSGAIASDYQRLRVESICSRLGLVSLAFLWKQDQTLLLQDMIANGIKAI 160
Cdd:pfam01902  71 -------EKEVEDLKGILHRLD-----VEAAVFGAIYSEYQKSRIERVCRELGLKSFAPLWHEDPEELAEEFVEEGFEAY 138

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1780591731 161 LVKVAAIGLDPSkHLGK--DLAFMEPyLLKLKEKYGSNVCGEGGEYETLTLDCPLF 214
Cdd:pfam01902 139 VVAVKAEGLDES-WLGRriDRKFIDE-LKKLNEKYGIHPAGEGGEFETLVLDGPIF 192
eu_AANH_C_2 cd06156
A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine ...
 431-551 1.55e-35

A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine nucleotide alpha hydrolase (AANH)-like domain located N-terminal to two distinctly different YjgF-YER057c-UK114-like domains. This CD contains the second of these domains. The YjgF-YER057c-UK114 protein family is a large family of proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site.


Pssm-ID: 100013  Cd Length: 118  Bit Score: 130.14  E-value: 1.55e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591731 431 YSQATLHQSVLHMAGQLGLDPPTMNLQTEGAIAELNQALTNSEAIAESFNCSISssaILFVVFCSARTKQSERNQLHEKF 510
Cdd:cd06156     1 YSQAIVVPKVAYISGQIGLIPATMTLLEGGITLQAVLSLQHLERVAKAMNVQWV---LAAVCYVTDESSVPIARSAWSKY 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1780591731 511 VTFLGLAKSSRRVQNVLDPMFLYILVPDLPKRALVEVKPIL 551
Cdd:cd06156    78 CSELDLEDESRNESDDVNPPLVIVVVPELPRGALVEWQGIA 118
TIGR00289 TIGR00289
TIGR00289 family protein; Homologous proteins related to MJ0570 of Methanococcus jannaschii ...
 1-229 3.32e-35

TIGR00289 family protein; Homologous proteins related to MJ0570 of Methanococcus jannaschii include both the apparent orthologs found by this model above the trusted cutoff, the much longer protein YLR143W from Saccharomyces cerevisiae, and second homologous proteins from Archaeoglobus fulgidus and Pyrococcus horikoshii that appear to represent a second orthologous group. [Hypothetical proteins, Conserved]


Pssm-ID: 129390  Cd Length: 222  Bit Score: 133.07  E-value: 3.32e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591731   1 MKVVALVSGGKDSCYAMMKCIQyGHEIVALANLLPvddsvDELDSYMYQTVGHQILVGYAECMNVPLFRRRIRGSSrhqk 80
Cdd:TIGR00289   1 MKVAVLYSGGKDSILALYKALE-EHEVISLVGVFS-----ENEESYMFHSPNLHLTDLVAEAVGIPLIKLYTSGEE---- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591731  81 lsyqmtpDDEVEDMFVLLSEVKrqipsITAVSSGAIASDYQRLRVESICSRLGLVSLAFLWKQDQTLLLQDmIANGIKAI 160
Cdd:TIGR00289  71 -------EKEVEDLAGQLGELD-----VEALCIGAIESNYQKSRIDKVCRELGLKSIAPLWHADPEKLMYE-VAEKFEVI 137

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1780591731 161 LVKVAAIGLDPSkHLGK--DLAFMEPyLLKLKEKYGSNVCGEGGEYETLTLDCPLFtNASIVLDEYQVVLH 229
Cdd:TIGR00289 138 IVSVSAMGLDES-WLGRriDKECIDD-LKRLNEKYGIHLAFEGGEAETLVLDAPLF-KKRIEVDEIEKFWD 205
eu_AANH_C_1 cd06155
A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine ...
 297-392 2.22e-24

A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine nucleotide alpha hydrolase (AANH)-like domain located N-terminal to two distinctly different YjgF-YER057c-UK114-like domains. This CD contains the first of these domains. The YjgF-YER057c-UK114 protein family is a large family of proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site.


Pssm-ID: 100012  Cd Length: 101  Bit Score: 97.71  E-value: 2.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591731 297 LHISRAEKHNTFSICCWledsSESSKGLKEDLETVLTELESQLLKHGYNWQHVLYIHLYISDMSEFAVANETYVKFITQe 376
Cdd:cd06155     1 LSQNRTGGLLWISNVTA----SESDETVEEQMESIFSKLREILQSNGLSLSDILYVTLYLRDMSDFAEVNSVYGTFFDK- 75

                          90
                  ....*....|....*.
gi 1780591731 377 kcpFGVPSRSTIELPL 392
Cdd:cd06155    76 ---PNPPSRVCVECGL 88
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
 418-553 1.14e-09

Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 family [Defense mechanisms]; Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 family is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 440021  Cd Length: 125  Bit Score: 56.73  E-value: 1.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591731 418 QSISCWAPSCIGPYSQATLHQSVLHMAGQLGLDPPTMNLqTEGAIAELNQALTNSEAIAESFNCSISSsaILFV-VFCSA 496
Cdd:COG0251     4 ELINPPAPAPIGPYSQAVRVGNLVFVSGQVPLDPDTGEL-GGDIEAQTRQVLENILAVLAAAGGSLDD--VVKVtVYLTD 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1780591731 497 RtkqSERNQLHEKFVTFLGLAKSSRRVqnvldpmflyILVPDLPKRALVEVKPILYV 553
Cdd:COG0251    81 M---ADFAAVNEVYAEYFGEGRPARTA----------VGVAALPKGALVEIEAIAAL 124
TIGR00004 TIGR00004
reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of ...
 424-553 1.24e-09

reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of protein synthesis intiation, then as an endoribonuclease active on single-stranded mRNA, endoribonuclease L-PSP. Members of this family, conserved in all domains of life and often with several members per bacterial genome, appear to catalyze a reaction that minimizes toxic by-products from reactions catalyzed by pyridoxal phosphate-dependent enzymes. [Cellular processes, Other]


Pssm-ID: 129116  Cd Length: 124  Bit Score: 56.53  E-value: 1.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591731 424 APSCIGPYSQATLHQSVLHMAGQLGLDPPTMNLQTEGAIAELNQALTNSEAIAESFNCSIsSSAILFVVFCSARTKQSER 503
Cdd:TIGR00004   9 APAAIGPYSQAVKVGNTVYVSGQIPLDPSTGELVGGDIAEQAEQVLENLKAILEAAGLSL-DDVVKTTVFLTDLNDFAEV 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1780591731 504 NQLHEKFVTFLGLAKSSrrVQnvldpmflyilVPDLPKRALVEVKPILYV 553
Cdd:TIGR00004  88 NEVYGQYFDEHYPARSA--VQ-----------VAALPKGVLVEIEAIAVK 124
Ribonuc_L-PSP pfam01042
Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein ...
 424-550 2.85e-09

Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein synthesis by cleavage of mRNA. Previously thought to inhibit protein synthesis initiation. This protein may also be involved in the regulation of purine biosynthesis. YjgF (renamed RidA) family members are enamine/imine deaminases. They hydrolyze reactive intermediates released by PLP-dependent enzymes, including threonine dehydratase. YjgF also prevents inhibition of transaminase B (IlvE) in Salmonella.


Pssm-ID: 426010  Cd Length: 117  Bit Score: 55.38  E-value: 2.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591731 424 APSCIGPYSQATLHQSVLHMAGQLGLDPPTMNLQTEGAIAELNQALTNSEAIAESFNCSISSsaILFV-VFCSARTKQSE 502
Cdd:pfam01042   2 APAAAGPYSQAVKAGNLVYVSGQIPLDPDTGKLVEGDVAEQTRQVLENIKAVLAAAGASLSD--VVKVtIFLADMNDFAE 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1780591731 503 RNQLHEKFVTFLGL-AKSSrrVQnvldpmflyilVPDLPKRALVEVKPI 550
Cdd:pfam01042  80 VNEVYAEYFDADKApARSA--VG-----------VAALPLGALVEIEAI 115
YjgF_YER057c_UK114_family cd00448
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
 431-547 1.12e-08

YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site.


Pssm-ID: 100004 [Multi-domain]  Cd Length: 107  Bit Score: 53.33  E-value: 1.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591731 431 YSQATLHQSVLHMAGQLGLDPPTMnLQTEGAIAELNQALTNSEAIAESFNCSISSsaILFV-VFCSARTKQSERNQLHEK 509
Cdd:cd00448     1 YSQAVRVGNLVFVSGQIPLDPDGE-LVPGDIEAQTRQALENLEAVLEAAGGSLDD--VVKVtVYLTDMADFAAVNEVYDE 77

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1780591731 510 FVTFLGLakssrrvqnvldPMFLYILVPDLPKRALVEV 547
Cdd:cd00448    78 FFGEGPP------------PARTAVGVAALPPGALVEI 103
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
 313-407 3.73e-06

Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 family [Defense mechanisms]; Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 family is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 440021  Cd Length: 125  Bit Score: 46.71  E-value: 3.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591731 313 WLEDSSESSKGLKEDLETVLTELESQLLKHGYNWQHVLYIHLYISDMSEFAVANETYVKFITQekcpfGVPSRSTIElpl 392
Cdd:COG0251    35 LDPDTGELGGDIEAQTRQVLENILAVLAAAGGSLDDVVKVTVYLTDMADFAAVNEVYAEYFGE-----GRPARTAVG--- 106

                          90
                  ....*....|....*...
gi 1780591731 393 vQAGLGKAY---IEVLVA 407
Cdd:COG0251   107 -VAALPKGAlveIEAIAA 123
YjgF_YER057c_UK114_like_2 cd06150
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 331-406 7.26e-04

This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site.


Pssm-ID: 100007  Cd Length: 105  Bit Score: 39.44  E-value: 7.26e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1780591731 331 VLTELESQLLKHGYNWQHVLYIHLYISDMSEFAVANETYVKFItQEKCPfgvPSRSTIELPLVQAGLgkaYIEVLV 406
Cdd:cd06150    34 VLAKIDALLAEAGSDKSRILSATIWLADMADFAAMNAVWDAWV-PPGHA---PARACVEAKLADPGY---LVEIVV 102
Ribonuc_L-PSP pfam01042
Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein ...
 321-407 1.97e-03

Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein synthesis by cleavage of mRNA. Previously thought to inhibit protein synthesis initiation. This protein may also be involved in the regulation of purine biosynthesis. YjgF (renamed RidA) family members are enamine/imine deaminases. They hydrolyze reactive intermediates released by PLP-dependent enzymes, including threonine dehydratase. YjgF also prevents inhibition of transaminase B (IlvE) in Salmonella.


Pssm-ID: 426010  Cd Length: 117  Bit Score: 38.43  E-value: 1.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591731 321 SKGLKEDLETVLTELESQLLKHGYNWQHVLYIHLYISDMSEFAVANETYVKFITQEKcpfgVPSRSTIELPLVQAGLgKA 400
Cdd:pfam01042  36 EGDVAEQTRQVLENIKAVLAAAGASLSDVVKVTIFLADMNDFAEVNEVYAEYFDADK----APARSAVGVAALPLGA-LV 110


                  ....*..
gi 1780591731 401 YIEVLVA 407
Cdd:pfam01042 111 EIEAIAV 117
 
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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