SirA, YedF, and YeeD. Two-layered alpha/beta sandwich domain. SirA (also known as UvrY, and YhhP) belongs to a family of bacterial two-component response regulators that controls secondary metabolism and virulence. The other member of this two-component system is a sensor kinase called BarA which phosphorylates SirA. A variety of microorganisms have similar proteins, all of which contain a common CPxP sequence motif in the N-terminal region. YhhP is suggested to be important for normal cell division and growth in rich nutrient medium. Moreover, despite a low primary sequence similarity, the YccP structure closely resembles the non-homologous C-terminal RNA-binding domain of E. coli translation initiation factor IF3. The signature CPxP motif serves to stabilize the N-terminal helix as part of the N-capping box and might be important in mRNA-binding.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1821496541 18 GLSCPMPVLRAKKALAKMTPGAVLAVWSTDPHSTPDLSDFCRQTGHGLLKQEEVDDDGRHW 78
Cdd:cd00291    6 GLPCPLPVLKTKKALEKLKSGEVLEVLLDDPGAVEDIPAWAKETGHEVLEVEEEGGVYRIL 66

sulfurtransferase TusA;

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821496541  1 MTNVHNEPQsvETLRLPGLSCPMPVLRAKKALAKMTPGAVLAVWSTDPHSTPDLSDFCRQTGHGLLKQEE 70
Cdd:PRK00299   1 MTDLFSSPD--HTLDALGLRCPEPVMMVRKTVRNMQPGETLLIIADDPATTRDIPSFCRFMDHELLAQET 68

SirA, YedF, and YeeD. Two-layered alpha/beta sandwich domain. SirA (also known as UvrY, and YhhP) belongs to a family of bacterial two-component response regulators that controls secondary metabolism and virulence. The other member of this two-component system is a sensor kinase called BarA which phosphorylates SirA. A variety of microorganisms have similar proteins, all of which contain a common CPxP sequence motif in the N-terminal region. YhhP is suggested to be important for normal cell division and growth in rich nutrient medium. Moreover, despite a low primary sequence similarity, the YccP structure closely resembles the non-homologous C-terminal RNA-binding domain of E. coli translation initiation factor IF3. The signature CPxP motif serves to stabilize the N-terminal helix as part of the N-capping box and might be important in mRNA-binding.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1821496541 18 GLSCPMPVLRAKKALAKMTPGAVLAVWSTDPHSTPDLSDFCRQTGHGLLKQEEVDDDGRHW 78
Cdd:cd00291    6 GLPCPLPVLKTKKALEKLKSGEVLEVLLDDPGAVEDIPAWAKETGHEVLEVEEEGGVYRIL 66

SirA (also known as UvrY, and YhhP) belongs to a family of two-component response regulators that controls secondary metabolism and virulence. The other member of this two-component system is a sensor kinase called BarA which phosphorylates SirA. A variety of microorganisms have similar proteins, all of which contain a common CPxP sequence motif in the N-terminal region. YhhP is thought to be important for normal cell division and growth in rich nutrient medium. Moreover, despite a low primary sequence similarity, the YccP structure closely resembles the non-homologous C-terminal RNA-binding domain of E. coli translation initiation factor IF3. The signature CPxP motif serves to stabilize the N-terminal helix as part of the N-capping box and might be important in mRNA-binding.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1821496541 13 TLRLPGLSCPMPVLRAKKALAKMTPGAVLAVWSTDPHSTPDLSDFCRQTGHGLLKQEEVDDDGRHW 78
Cdd:cd03423    1 ILDTRGLRCPEPVMMLHKKVRKMKPGDTLLVLATDPSTTRDIPKFCTFLGHELLAQETEDEPYRYL 66

SirA_RHOD_Pry_redox. SirA-like domain located within a multidomain protein of unknown function. Other domains include RHOD (rhodanese homology domain), and Pry_redox (pyridine nucleotide-disulphide oxidoreductase) as well as a C-terminal domain that corresponds to COG2210. This fold is referred to as a two-layered alpha/beta sandwich, structurally similar to that of translation initiation factor 3.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 1821496541 18 GLSCPMPVLRAKKALAKMTPGAVLAVWSTDPHSTPDLSDFCRQTGHGLLKQEEVD 72
Cdd:cd03420    6 GLQCPGPILKLKKEIDKLQDGEQLEVKASDPGFARDAQAWCKSTGNTLISLETEK 60

selenium metabolism protein YedF; Members of this protein family are about 200 amino acids in size, and include the uncharacterized YedF protein of Escherichia coli. This family shares an N-terminal domain, modeled by pfam01206, with the sulfurtransferase TusA (also called SirA). The C-terminal domain includes a typical redox-active disulfide motif, CGXC. This protein family found only among those genomes that also carry the selenium donor protein SelD, and its connection to selenium metabolism is indicated by the method of partial phylogenetic profiling vs. SelD. Its gene typically is found next to selD. Members of this family are found even when selenocysteine and selenouridine biosynthesis pathways are, except for SelD, completely absent, as in Enterococcus faecalis. Its role in selenium metabolism is unclear, but may include either detoxification or a role in labile selenoprotein biosynthesis.

                          10        20
                  ....*....|....*....|....*.
gi 1821496541  18 GLSCPMPVLRAKKALAKMTPGAVLAV 43
Cdd:TIGR03527   5 GLACPQPVILTKKALDELGEEGVLTV 30

YedF is a bacterial SirA-like protein of unknown function. SirA (also known as UvrY, and YhhP) belongs to a family of a two-component response regulators that controls secondary metabolism and virulence. The other member of this two-component system is a sensor kinase called BarA which phosphorylates SirA. A variety of microorganisms have similar proteins, all of which contain a common CPxP sequence motif in the N-terminal region. YhhP is suggested to be important for normal cell division and growth in rich nutrient medium. Moreover, despite a low primary sequence similarity, the YccP structure closely resembles the non-homologous C-terminal RNA-binding domain of E. coli translation initiation factor IF3. The signature CPxP motif serves to stabilize the N-terminal helix as part of the N-capping box and might be important in mRNA-binding.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1821496541 14 LRLPGLSCPMPVLRAKKALAKMTPGAVLAVWSTDPHSTPDLSDFCRQTGHGLLkqeEVDDDG 75
Cdd:cd03422    2 LDLRGEPCPYPAIATLEALPSLKPGEILEVISDCPQSINNIPIDARNHGYKVL---AIEQSG 60