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Conserved domains on  [gi|665390831|ref|NP_001285140|]
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uncharacterized protein Dmel_CG1578, isoform C [Drosophila melanogaster]

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 ...
 2-215 1.59e-105

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: 325.01  E-value: 1.59e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390831   2 RVVAMVSGGKDSCYNMMQCVAEGHEIVALANLHPKDRDeldSFMYQTVGHMGIEILASAMGLPLYRRETKGKSTQTGKQY 81
Cdd:cd01994    1 KVVALISGGKDSIYALLHAIRNGHEVVALANLRPEDKD---SYMFQTVGHELLELQAEALGLPLIRREIRGKSVTQELGY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390831  82 VPTDDDEVEDLYSLLETCKHELQVDAVAVGAILSDYQRVRVENVCSRLNLISLAYLWRRDQTELLQEMIDCQVHAIIIKV 161
Cdd:cd01994   78 EGEEEDEVEDLYELLKKVKERPEVEAVVSGAILSDYQRNRVERVCERLGLKSLAPLWQRDQEELLEELIDLGFEARIVKV 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 665390831 162 AALGLVPdRHLGKSLREMQP-HLLKMRDKYGLNVCGEGGEYETFTLDCPLFRQRI 215
Cdd:cd01994  158 AAMGLDE-EWLGRRLDEDQPeELLKLNEKYGVHVCGEGGEYETLVLDGPLFKKRI 211
eu_AANH_C_2 cd06156
A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine ...
 610-716 1.46e-38

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: 139.39  E-value: 1.46e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390831 610 YSQSTRIGDITYISGQIALVPGSMTIIEGGIRPQCKLTLRHISRIAKAMNAhgqlRDVVHGICFVTHPAFIGEARRQWER 689
Cdd:cd06156    1 YSQAIVVPKVAYISGQIGLIPATMTLLEGGITLQAVLSLQHLERVAKAMNV----QWVLAAVCYVTDESSVPIARSAWSK 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 665390831 690 ---------------RTTNAIMDYIVLPALPREALVEWQVWA 716
Cdd:cd06156   77 ycseldledesrnesDDVNPPLVIVVVPELPRGALVEWQGIA 118
eu_AANH_C_1 cd06155
A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine ...
 465-561 7.84e-37

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: 133.54  E-value: 7.84e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390831 465 INAKGWMWLAGIQGSG-TEGIEQGMQQALDTLRDLCQAKGYDLQDLCYVTLYVRSIGEYPLLNRVYHRAFDFHNPPTRVC 543
Cdd:cd06155    4 NRTGGLLWISNVTASEsDETVEEQMESIFSKLREILQSNGLSLSDILYVTLYLRDMSDFAEVNSVYGTFFDKPNPPSRVC 83

                         90
                 ....*....|....*...
gi 665390831 544 VECPLPDGCHVVMEAIAY 561
Cdd:cd06155   84 VECGLPEGCDVQLSCVAA 101
 
Name Accession Description Interval E-value
AANH_PF0828-like cd01994
putative ATP pyrophosphatase PF0828 and similar proteins; This subfamily includes Pyrococcus ...
 2-215 1.59e-105

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: 325.01  E-value: 1.59e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390831   2 RVVAMVSGGKDSCYNMMQCVAEGHEIVALANLHPKDRDeldSFMYQTVGHMGIEILASAMGLPLYRRETKGKSTQTGKQY 81
Cdd:cd01994    1 KVVALISGGKDSIYALLHAIRNGHEVVALANLRPEDKD---SYMFQTVGHELLELQAEALGLPLIRREIRGKSVTQELGY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390831  82 VPTDDDEVEDLYSLLETCKHELQVDAVAVGAILSDYQRVRVENVCSRLNLISLAYLWRRDQTELLQEMIDCQVHAIIIKV 161
Cdd:cd01994   78 EGEEEDEVEDLYELLKKVKERPEVEAVVSGAILSDYQRNRVERVCERLGLKSLAPLWQRDQEELLEELIDLGFEARIVKV 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 665390831 162 AALGLVPdRHLGKSLREMQP-HLLKMRDKYGLNVCGEGGEYETFTLDCPLFRQRI 215
Cdd:cd01994  158 AAMGLDE-EWLGRRLDEDQPeELLKLNEKYGVHVCGEGGEYETLVLDGPLFKKRI 211
MJ0570_dom TIGR00290
MJ0570-related uncharacterized domain; Proteins with this uncharacterized domain include two ...
 1-220 4.71e-64

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: 215.03  E-value: 4.71e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390831    1 MRVVAMVSGGKDSCYNMMQCVAEgHEIVALANLHPKDRDeldSFMYQTVGHMGIEILASAMGLPLYRRETKGkstqtgkq 80
Cdd:TIGR00290   1 MKVAALISGGKDSCLALYHALKE-HEVISLVNIMPENEE---SYMFHGVNAHLTDLQAESIGIPLIKLYTEG-------- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390831   81 yvpTDDDEVEDLYSLLetckHELQVDAVAVGAILSDYQRVRVENVCSRLNLISLAYLWRRDQTELLQEMIDCQVHAIIIK 160
Cdd:TIGR00290  69 ---TEEDEVEELKGIL----HTLDVEAVVFGAIYSEYQKTRIERVCRELGLKSFAPLWHRDPEKLMEEFVEEKFEARIIA 141

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665390831  161 VAALGLVPDrHLGKSL-REMQPHLLKMRDKYGLNVCGEGGEYETFTLDCPLFRQRIVVEDI 220
Cdd:TIGR00290 142 VAAEGLDES-WLGRRIdRKMIDELKKLNEKYGIHPAGEGGEFETLVLDAPIFKKRLEVKEI 201
Dph6 COG2102
Diphthamide synthase (EF-2-diphthine--ammonia ligase) [Translation, ribosomal structure and ...
 3-225 1.59e-52

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


Pssm-ID: 441705  Cd Length: 213  Bit Score: 182.63  E-value: 1.59e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390831   3 VVAMVSGGKDSCYNMMQCVAEGHEIVALANLHPKDRDeldSFMYQTVGhmgIEIL---ASAMGLPLYRRETKGkstqtgk 79
Cdd:COG2102    1 VVVSWSGGKDSALALYRALQEGYEVVGLLTTVPEDFD---RVMFHGPN---LELLeaqAEALGIPLIEIELSG------- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390831  80 qyvpTDDDEVEDLYSLLETCKhELQVDAVAVGAILSDYQRVRVENVCSRLNLISLAYLWRRDQTELLQEMIDCQVHAIII 159
Cdd:COG2102   68 ----SNEEYEEELEEALKELK-AEGIEGVVFGDIFLEDQRDYRERVCEELGLEAVFPLWGRDTEELLEEFIDAGFEAIIV 142

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665390831 160 KVAALGLvPDRHLGkslREMQPHLLKMRDKYGLNVCGEGGEYETFTLDCPLFRQRIVVEDIQTIIS 225
Cdd:COG2102  143 CVDAEGL-DESWLG---RELDEELLEELPAYGVDPCGEGGEFHTFVLDGPLFKKPIEIEEGEIVWR 204
Diphthami_syn_2 pfam01902
Diphthamide synthase; Diphthamide_syn, diphthamide synthase, catalyzes the last amidation step ...
 1-221 6.67e-44

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: 158.43  E-value: 6.67e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390831    1 MRVVAMVSGGKDSCYNMMQcVAEGHEIVALANLHPKDRDeldSFMYQTVGHMGIEILASAMGLPLYRRETKGKstqtgkq 80
Cdd:pfam01902   1 MKVAALYSGGKDSCLALYR-ALKEMEVDSLVCVMSENKE---SYMFHGPNAHLTKLQAESVGIPLIKLYTTGE------- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390831   81 yvptDDDEVEDLYSLLetckHELQVDAVAVGAILSDYQRVRVENVCSRLNLISLAYLWRRDQTELLQEMIDCQVHAIIIK 160
Cdd:pfam01902  70 ----EEKEVEDLKGIL----HRLDVEAAVFGAIYSEYQKSRIERVCRELGLKSFAPLWHEDPEELAEEFVEEGFEAYVVA 141

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665390831  161 VAALGLVPDrHLGKSL-REMQPHLLKMRDKYGLNVCGEGGEYETFTLDCPLFRQRIVVEDIQ 221
Cdd:pfam01902 142 VKAEGLDES-WLGRRIdRKFIDELKKLNEKYGIHPAGEGGEFETLVLDGPIFKKRLEVKELE 202
eu_AANH_C_2 cd06156
A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine ...
 610-716 1.46e-38

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: 139.39  E-value: 1.46e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390831 610 YSQSTRIGDITYISGQIALVPGSMTIIEGGIRPQCKLTLRHISRIAKAMNAhgqlRDVVHGICFVTHPAFIGEARRQWER 689
Cdd:cd06156    1 YSQAIVVPKVAYISGQIGLIPATMTLLEGGITLQAVLSLQHLERVAKAMNV----QWVLAAVCYVTDESSVPIARSAWSK 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 665390831 690 ---------------RTTNAIMDYIVLPALPREALVEWQVWA 716
Cdd:cd06156   77 ycseldledesrnesDDVNPPLVIVVVPELPRGALVEWQGIA 118
eu_AANH_C_1 cd06155
A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine ...
 465-561 7.84e-37

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: 133.54  E-value: 7.84e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390831 465 INAKGWMWLAGIQGSG-TEGIEQGMQQALDTLRDLCQAKGYDLQDLCYVTLYVRSIGEYPLLNRVYHRAFDFHNPPTRVC 543
Cdd:cd06155    4 NRTGGLLWISNVTASEsDETVEEQMESIFSKLREILQSNGLSLSDILYVTLYLRDMSDFAEVNSVYGTFFDKPNPPSRVC 83

                         90
                 ....*....|....*...
gi 665390831 544 VECPLPDGCHVVMEAIAY 561
Cdd:cd06155   84 VECGLPEGCDVQLSCVAA 101
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
 594-717 2.46e-21

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: 90.24  E-value: 2.46e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390831 594 MHVQGISHWAPANIGPYSQSTRIGDITYISGQIALVPGSMTiIEGGIRPQCKLTLRHISRIAKAmnAHGQLRDVVHGICF 673
Cdd:COG0251    1 MTRELINPPAPAPIGPYSQAVRVGNLVFVSGQVPLDPDTGE-LGGDIEAQTRQVLENILAVLAA--AGGSLDDVVKVTVY 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 665390831 674 VTHPAFIGEARRQWER--------RTTnaimdyIVLPALPREALVEWQVWAH 717
Cdd:COG0251   78 LTDMADFAAVNEVYAEyfgegrpaRTA------VGVAALPKGALVEIEAIAA 123
TIGR00004 TIGR00004
reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of ...
 603-711 2.76e-14

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: 70.02  E-value: 2.76e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390831  603 APANIGPYSQSTRIGDITYISGQIALVPGSMTIIEGGIRPQCKLTLRHISRIAKAmnAHGQLRDVVHGICFVTHPAFIGE 682
Cdd:TIGR00004   9 APAAIGPYSQAVKVGNTVYVSGQIPLDPSTGELVGGDIAEQAEQVLENLKAILEA--AGLSLDDVVKTTVFLTDLNDFAE 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 665390831  683 arrqwerrtTNAIM-DYI--VLPA--------LPREALVE 711
Cdd:TIGR00004  87 ---------VNEVYgQYFdeHYPArsavqvaaLPKGVLVE 117
Ribonuc_L-PSP pfam01042
Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein ...
 603-717 1.82e-13

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: 67.71  E-value: 1.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390831  603 APANIGPYSQSTRIGDITYISGQIALVPGSMTIIEGGIRPQCKLTLRHISRIAKAMNAhgQLRDVVHGICFVT-HPAF-- 679
Cdd:pfam01042   2 APAAAGPYSQAVKAGNLVYVSGQIPLDPDTGKLVEGDVAEQTRQVLENIKAVLAAAGA--SLSDVVKVTIFLAdMNDFae 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 665390831  680 IGEARRQWER------RTTnaimdyIVLPALPREALVEWQVWAH 717
Cdd:pfam01042  80 VNEVYAEYFDadkapaRSA------VGVAALPLGALVEIEAIAV 117
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
 464-562 9.10e-13

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: 65.97  E-value: 9.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390831 464 AINAKGWMWLAGI------QGSGTEGIEQGMQQALDTLRDLCQAKGYDLQDLCYVTLYVRSIGEYPLLNRVYHRAFDfHN 537
Cdd:COG0251   20 AVRVGNLVFVSGQvpldpdTGELGGDIEAQTRQVLENILAVLAAAGGSLDDVVKVTVYLTDMADFAAVNEVYAEYFG-EG 98

                         90       100
                 ....*....|....*....|....*.
gi 665390831 538 PPTRVCVECP-LPDGCHVVMEAIAYR 562
Cdd:COG0251   99 RPARTAVGVAaLPKGALVEIEAIAAL 124
Ribonuc_L-PSP pfam01042
Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein ...
 482-561 3.87e-10

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: 58.08  E-value: 3.87e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390831  482 EGIEQGMQQALDTLRDLCQAKGYDLQDLCYVTLYVRSIGEYPLLNRVYHRAFDFHNPPTRVCVECP-LPDGCHVVMEAIA 560
Cdd:pfam01042  37 GDVAEQTRQVLENIKAVLAAAGASLSDVVKVTIFLADMNDFAEVNEVYAEYFDADKAPARSAVGVAaLPLGALVEIEAIA 116


                  .
gi 665390831  561 Y 561
Cdd:pfam01042 117 V 117
PRK11401 PRK11401
enamine/imine deaminase;
478-562 1.58e-06

enamine/imine deaminase;


Pssm-ID: 105214  Cd Length: 129  Bit Score: 48.14  E-value: 1.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390831 478 GSGTEGIEQGMQQALDTLRDLCQAKGYDLQDLCYVTLYVRSIGEYPLLNRVYHRAFDFHNP--PTRVCVECP-LPDGCHV 554
Cdd:PRK11401  40 GEIPADVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFITDLNDFATINEVYKQFFDEHQAtyPTRSCVQVArLPKDVKL 119


                 ....*...
gi 665390831 555 VMEAIAYR 562
Cdd:PRK11401 120 EIEAIAVR 127
PRK11401 PRK11401
enamine/imine deaminase;
603-716 9.59e-05

enamine/imine deaminase;


Pssm-ID: 105214  Cd Length: 129  Bit Score: 43.13  E-value: 9.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390831 603 APANIGPYSQSTRIGDITYISGQIALVPGSMTIIEgGIRPQCKLTLRHISRIAKAmnAHGQLRDVVHGICFVTHP---AF 679
Cdd:PRK11401  10 APGAIGPYVQGVDLGSMVFTSGQIPVCPQTGEIPA-DVQDQARLSLENVKAIVVA--AGLSVGDIIKMTVFITDLndfAT 86

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 665390831 680 IGEARRQW--ERRTTNAIMDYIVLPALPREALVEWQVWA 716
Cdd:PRK11401  87 INEVYKQFfdEHQATYPTRSCVQVARLPKDVKLEIEAIA 125
 
Name Accession Description Interval E-value
AANH_PF0828-like cd01994
putative ATP pyrophosphatase PF0828 and similar proteins; This subfamily includes Pyrococcus ...
 2-215 1.59e-105

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: 325.01  E-value: 1.59e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390831   2 RVVAMVSGGKDSCYNMMQCVAEGHEIVALANLHPKDRDeldSFMYQTVGHMGIEILASAMGLPLYRRETKGKSTQTGKQY 81
Cdd:cd01994    1 KVVALISGGKDSIYALLHAIRNGHEVVALANLRPEDKD---SYMFQTVGHELLELQAEALGLPLIRREIRGKSVTQELGY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390831  82 VPTDDDEVEDLYSLLETCKHELQVDAVAVGAILSDYQRVRVENVCSRLNLISLAYLWRRDQTELLQEMIDCQVHAIIIKV 161
Cdd:cd01994   78 EGEEEDEVEDLYELLKKVKERPEVEAVVSGAILSDYQRNRVERVCERLGLKSLAPLWQRDQEELLEELIDLGFEARIVKV 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 665390831 162 AALGLVPdRHLGKSLREMQP-HLLKMRDKYGLNVCGEGGEYETFTLDCPLFRQRI 215
Cdd:cd01994  158 AAMGLDE-EWLGRRLDEDQPeELLKLNEKYGVHVCGEGGEYETLVLDGPLFKKRI 211
MJ0570_dom TIGR00290
MJ0570-related uncharacterized domain; Proteins with this uncharacterized domain include two ...
 1-220 4.71e-64

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: 215.03  E-value: 4.71e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390831    1 MRVVAMVSGGKDSCYNMMQCVAEgHEIVALANLHPKDRDeldSFMYQTVGHMGIEILASAMGLPLYRRETKGkstqtgkq 80
Cdd:TIGR00290   1 MKVAALISGGKDSCLALYHALKE-HEVISLVNIMPENEE---SYMFHGVNAHLTDLQAESIGIPLIKLYTEG-------- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390831   81 yvpTDDDEVEDLYSLLetckHELQVDAVAVGAILSDYQRVRVENVCSRLNLISLAYLWRRDQTELLQEMIDCQVHAIIIK 160
Cdd:TIGR00290  69 ---TEEDEVEELKGIL----HTLDVEAVVFGAIYSEYQKTRIERVCRELGLKSFAPLWHRDPEKLMEEFVEEKFEARIIA 141

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665390831  161 VAALGLVPDrHLGKSL-REMQPHLLKMRDKYGLNVCGEGGEYETFTLDCPLFRQRIVVEDI 220
Cdd:TIGR00290 142 VAAEGLDES-WLGRRIdRKMIDELKKLNEKYGIHPAGEGGEFETLVLDAPIFKKRLEVKEI 201
arCOG00187 TIGR03679
arCOG00187 universal archaeal metal-binding-domain/4Fe-4S-binding-domain containing ABC ...
 4-240 1.70e-57

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: 196.71  E-value: 1.70e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390831    4 VAMVSGGKDSCYNMMQCVAEGHEIVALANLHPKDRDeldSFMYQTVG-HMGiEILASAMGLPLYRRETKGkstqtgkqyv 82
Cdd:TIGR03679   1 AALYSGGKDSNYALYKALEEGHEVTCLITVVPENED---SYMFHTPNiELT-RLQAEALGIPLVEIETSG---------- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390831   83 pTDDDEVEDLYSLLETCKHElQVDAVAVGAILSDYQRVRVENVCSRLNLISLAYLWRRDQTELLQEMIDCQVHAIIIKVA 162
Cdd:TIGR03679  67 -EKEKEVEDLKGALKELKEE-GVEGIVTGAIASEYQKSRIERICEELGLKVFAPLWGRDPEEYLRELVERGFRFIIVSVS 144

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665390831  163 ALGLvPDRHLGKSL-REMQPHLLKMRDKYGLNVCGEGGEYETFTLDCPLFRQRIVVEDIQTIISSAdpicpVGYINFTK 240
Cdd:TIGR03679 145 AYGL-DESWLGREIdEKYIEELKALNKRYGINPAGEGGEYETLVLDAPLFKRRIEIVEYEKKWSGG-----GGYLIIER 217
Dph6 COG2102
Diphthamide synthase (EF-2-diphthine--ammonia ligase) [Translation, ribosomal structure and ...
 3-225 1.59e-52

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


Pssm-ID: 441705  Cd Length: 213  Bit Score: 182.63  E-value: 1.59e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390831   3 VVAMVSGGKDSCYNMMQCVAEGHEIVALANLHPKDRDeldSFMYQTVGhmgIEIL---ASAMGLPLYRRETKGkstqtgk 79
Cdd:COG2102    1 VVVSWSGGKDSALALYRALQEGYEVVGLLTTVPEDFD---RVMFHGPN---LELLeaqAEALGIPLIEIELSG------- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390831  80 qyvpTDDDEVEDLYSLLETCKhELQVDAVAVGAILSDYQRVRVENVCSRLNLISLAYLWRRDQTELLQEMIDCQVHAIII 159
Cdd:COG2102   68 ----SNEEYEEELEEALKELK-AEGIEGVVFGDIFLEDQRDYRERVCEELGLEAVFPLWGRDTEELLEEFIDAGFEAIIV 142

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665390831 160 KVAALGLvPDRHLGkslREMQPHLLKMRDKYGLNVCGEGGEYETFTLDCPLFRQRIVVEDIQTIIS 225
Cdd:COG2102  143 CVDAEGL-DESWLG---RELDEELLEELPAYGVDPCGEGGEFHTFVLDGPLFKKPIEIEEGEIVWR 204
Diphthami_syn_2 pfam01902
Diphthamide synthase; Diphthamide_syn, diphthamide synthase, catalyzes the last amidation step ...
 1-221 6.67e-44

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: 158.43  E-value: 6.67e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390831    1 MRVVAMVSGGKDSCYNMMQcVAEGHEIVALANLHPKDRDeldSFMYQTVGHMGIEILASAMGLPLYRRETKGKstqtgkq 80
Cdd:pfam01902   1 MKVAALYSGGKDSCLALYR-ALKEMEVDSLVCVMSENKE---SYMFHGPNAHLTKLQAESVGIPLIKLYTTGE------- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390831   81 yvptDDDEVEDLYSLLetckHELQVDAVAVGAILSDYQRVRVENVCSRLNLISLAYLWRRDQTELLQEMIDCQVHAIIIK 160
Cdd:pfam01902  70 ----EEKEVEDLKGIL----HRLDVEAAVFGAIYSEYQKSRIERVCRELGLKSFAPLWHEDPEELAEEFVEEGFEAYVVA 141

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665390831  161 VAALGLVPDrHLGKSL-REMQPHLLKMRDKYGLNVCGEGGEYETFTLDCPLFRQRIVVEDIQ 221
Cdd:pfam01902 142 VKAEGLDES-WLGRRIdRKFIDELKKLNEKYGIHPAGEGGEFETLVLDGPIFKKRLEVKELE 202
eu_AANH_C_2 cd06156
A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine ...
 610-716 1.46e-38

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: 139.39  E-value: 1.46e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390831 610 YSQSTRIGDITYISGQIALVPGSMTIIEGGIRPQCKLTLRHISRIAKAMNAhgqlRDVVHGICFVTHPAFIGEARRQWER 689
Cdd:cd06156    1 YSQAIVVPKVAYISGQIGLIPATMTLLEGGITLQAVLSLQHLERVAKAMNV----QWVLAAVCYVTDESSVPIARSAWSK 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 665390831 690 ---------------RTTNAIMDYIVLPALPREALVEWQVWA 716
Cdd:cd06156   77 ycseldledesrnesDDVNPPLVIVVVPELPRGALVEWQGIA 118
eu_AANH_C_1 cd06155
A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine ...
 465-561 7.84e-37

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: 133.54  E-value: 7.84e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390831 465 INAKGWMWLAGIQGSG-TEGIEQGMQQALDTLRDLCQAKGYDLQDLCYVTLYVRSIGEYPLLNRVYHRAFDFHNPPTRVC 543
Cdd:cd06155    4 NRTGGLLWISNVTASEsDETVEEQMESIFSKLREILQSNGLSLSDILYVTLYLRDMSDFAEVNSVYGTFFDKPNPPSRVC 83

                         90
                 ....*....|....*...
gi 665390831 544 VECPLPDGCHVVMEAIAY 561
Cdd:cd06155   84 VECGLPEGCDVQLSCVAA 101
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
 594-717 2.46e-21

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: 90.24  E-value: 2.46e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390831 594 MHVQGISHWAPANIGPYSQSTRIGDITYISGQIALVPGSMTiIEGGIRPQCKLTLRHISRIAKAmnAHGQLRDVVHGICF 673
Cdd:COG0251    1 MTRELINPPAPAPIGPYSQAVRVGNLVFVSGQVPLDPDTGE-LGGDIEAQTRQVLENILAVLAA--AGGSLDDVVKVTVY 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 665390831 674 VTHPAFIGEARRQWER--------RTTnaimdyIVLPALPREALVEWQVWAH 717
Cdd:COG0251   78 LTDMADFAAVNEVYAEyfgegrpaRTA------VGVAALPKGALVEIEAIAA 123
YjgF_YER057c_UK114_family cd00448
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
 610-716 2.65e-20

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: 86.84  E-value: 2.65e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390831 610 YSQSTRIGDITYISGQIALVPGSmTIIEGGIRPQCKLTLRHISRIAKAMNahGQLRDVVHGICFVTHPAFIGEARRQWER 689
Cdd:cd00448    1 YSQAVRVGNLVFVSGQIPLDPDG-ELVPGDIEAQTRQALENLEAVLEAAG--GSLDDVVKVTVYLTDMADFAAVNEVYDE 77

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 665390831 690 ---------RTTnaimdyIVLPALPREALVEWQVWA 716
Cdd:cd00448   78 ffgegpppaRTA------VGVAALPPGALVEIEAIA 107
YjgF_YER057c_UK114_family cd00448
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
 464-560 1.91e-18

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: 81.45  E-value: 1.91e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390831 464 AINAKGWMWLAGiQGS-------GTEGIEQGMQQALDTLRDLCQAKGYDLQDLCYVTLYVRSIGEYPLLNRVYHRAFDFH 536
Cdd:cd00448    4 AVRVGNLVFVSG-QIPldpdgelVPGDIEAQTRQALENLEAVLEAAGGSLDDVVKVTVYLTDMADFAAVNEVYDEFFGEG 82

                         90       100
                 ....*....|....*....|....*
gi 665390831 537 NPPTRVCVECP-LPDGCHVVMEAIA 560
Cdd:cd00448   83 PPPARTAVGVAaLPPGALVEIEAIA 107
TIGR00004 TIGR00004
reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of ...
 603-711 2.76e-14

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: 70.02  E-value: 2.76e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390831  603 APANIGPYSQSTRIGDITYISGQIALVPGSMTIIEGGIRPQCKLTLRHISRIAKAmnAHGQLRDVVHGICFVTHPAFIGE 682
Cdd:TIGR00004   9 APAAIGPYSQAVKVGNTVYVSGQIPLDPSTGELVGGDIAEQAEQVLENLKAILEA--AGLSLDDVVKTTVFLTDLNDFAE 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 665390831  683 arrqwerrtTNAIM-DYI--VLPA--------LPREALVE 711
Cdd:TIGR00004  87 ---------VNEVYgQYFdeHYPArsavqvaaLPKGVLVE 117
Ribonuc_L-PSP pfam01042
Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein ...
 603-717 1.82e-13

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: 67.71  E-value: 1.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390831  603 APANIGPYSQSTRIGDITYISGQIALVPGSMTIIEGGIRPQCKLTLRHISRIAKAMNAhgQLRDVVHGICFVT-HPAF-- 679
Cdd:pfam01042   2 APAAAGPYSQAVKAGNLVYVSGQIPLDPDTGKLVEGDVAEQTRQVLENIKAVLAAAGA--SLSDVVKVTIFLAdMNDFae 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 665390831  680 IGEARRQWER------RTTnaimdyIVLPALPREALVEWQVWAH 717
Cdd:pfam01042  80 VNEVYAEYFDadkapaRSA------VGVAALPLGALVEIEAIAV 117
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
 464-562 9.10e-13

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: 65.97  E-value: 9.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390831 464 AINAKGWMWLAGI------QGSGTEGIEQGMQQALDTLRDLCQAKGYDLQDLCYVTLYVRSIGEYPLLNRVYHRAFDfHN 537
Cdd:COG0251   20 AVRVGNLVFVSGQvpldpdTGELGGDIEAQTRQVLENILAVLAAAGGSLDDVVKVTVYLTDMADFAAVNEVYAEYFG-EG 98

                         90       100
                 ....*....|....*....|....*.
gi 665390831 538 PPTRVCVECP-LPDGCHVVMEAIAYR 562
Cdd:COG0251   99 RPARTAVGVAaLPKGALVEIEAIAAL 124
YjgF_YER057c_UK114_like_2 cd06150
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 472-560 1.11e-10

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: 59.09  E-value: 1.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390831 472 WLAGIQGSGTEG-IEQGMQQALDTLRDLCQAKGYDLQDLCYVTLYVRSIGEYPLLNRVYHRAFDFHNPPTRVCVECPLPD 550
Cdd:cd06150   14 YLAGQVADDTSAdITGQTRQVLAKIDALLAEAGSDKSRILSATIWLADMADFAAMNAVWDAWVPPGHAPARACVEAKLAD 93

                         90
                 ....*....|.
gi 665390831 551 -GCHVVMEAIA 560
Cdd:cd06150   94 pGYLVEIVVTA 104
Ribonuc_L-PSP pfam01042
Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein ...
 482-561 3.87e-10

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: 58.08  E-value: 3.87e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390831  482 EGIEQGMQQALDTLRDLCQAKGYDLQDLCYVTLYVRSIGEYPLLNRVYHRAFDFHNPPTRVCVECP-LPDGCHVVMEAIA 560
Cdd:pfam01042  37 GDVAEQTRQVLENIKAVLAAAGASLSDVVKVTIFLADMNDFAEVNEVYAEYFDADKAPARSAVGVAaLPLGALVEIEAIA 116


                  .
gi 665390831  561 Y 561
Cdd:pfam01042 117 V 117
PRK11401 PRK11401
enamine/imine deaminase;
478-562 1.58e-06

enamine/imine deaminase;


Pssm-ID: 105214  Cd Length: 129  Bit Score: 48.14  E-value: 1.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390831 478 GSGTEGIEQGMQQALDTLRDLCQAKGYDLQDLCYVTLYVRSIGEYPLLNRVYHRAFDFHNP--PTRVCVECP-LPDGCHV 554
Cdd:PRK11401  40 GEIPADVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFITDLNDFATINEVYKQFFDEHQAtyPTRSCVQVArLPKDVKL 119


                 ....*...
gi 665390831 555 VMEAIAYR 562
Cdd:PRK11401 120 EIEAIAVR 127
PRK11401 PRK11401
enamine/imine deaminase;
603-716 9.59e-05

enamine/imine deaminase;


Pssm-ID: 105214  Cd Length: 129  Bit Score: 43.13  E-value: 9.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665390831 603 APANIGPYSQSTRIGDITYISGQIALVPGSMTIIEgGIRPQCKLTLRHISRIAKAmnAHGQLRDVVHGICFVTHP---AF 679
Cdd:PRK11401  10 APGAIGPYVQGVDLGSMVFTSGQIPVCPQTGEIPA-DVQDQARLSLENVKAIVVA--AGLSVGDIIKMTVFITDLndfAT 86

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 665390831 680 IGEARRQW--ERRTTNAIMDYIVLPALPREALVEWQVWA 716
Cdd:PRK11401  87 INEVYKQFfdEHQATYPTRSCVQVARLPKDVKLEIEAIA 125
YjgF_YER057c_UK114_like_6 cd06154
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 610-685 8.89e-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: 100011  Cd Length: 119  Bit Score: 39.84  E-value: 8.89e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665390831 610 YSQSTRIGDITYISGQIALVPGSMTiIEGGIRPQCKLTLRhisRIAKAMN-AHGQLRDVVHGICFVTHPAFIGEARR 685
Cdd:cd06154   13 YSRAVRVGNWVFVSGTTGYDYDGMV-MPGDAYEQTRQCLE---IIEAALAeAGASLEDVVRTRMYVTDIADFEAVGR 85
 
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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