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ouroboros / 100sample.json

Nanny7

Enhanced T2P interface: structured prompt builder, random example, direct input

5284eb7 about 1 month ago

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	[
	{
	"uniprot_id": "B9LSR7",
	"sequence": "MEALKADVTQGLSKGSLITCADNTGARELKVISVAGYSGTKNRHPKAGIGDKVTVSVTKGTPEMRRQVLEAVVVRQRKPIRRPNGTRVKFEDNAAVIIDDLDEPRGTEIKGPVAREVAERFGSIASTATMIV",
	"function": [
	"Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome."
	],
	"subunit": [
	"Part of the 50S ribosomal subunit. Forms a cluster with proteins L3 and L24e, part of which may contact the 16S rRNA in 2 intersubunit bridges."
	],
	"similarity": [
	"Belongs to the universal ribosomal protein uL14 family."
	],
	"prompt": "Belongs to the universal ribosomal protein uL14 family.Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome.Part of the 50S ribosomal subunit. Forms a cluster with proteins L3 and L24e, part of which may contact the 16S rRNA in 2 intersubunit bridges.",
	"func_sim": "Belongs to the universal ribosomal protein uL14 family.Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome."
	},
	{
	"uniprot_id": "A5IKJ0",
	"sequence": "MKIHFVGIGGIGMSAVALHEFLNGNDVYGSNIEETERTAYLRKLGIPIFVPHSADNWYDPDLVIKTPAVRDDNPEIVRARMERVPVENRLHYFRDILKREKKEEFAVTGTDGKTTTTAMVAHVLKHLKKSPTVFLGGIMDSLEHGNYEKGNGPVVYELDESEEFFSEFSPNYLIITNARGDHLENYGNSLSRYRSAFEKISRNTDLVVTFAEDELTSHLGDVTFGVKKGTYTLEMRSASRAEQKAVVEKNGKRYLELKLKVPGFHNVLNALAVIALFDSLGYDLAPVLEALEEFRGVHRRFSIAFHDPETNIYVIDDYAHTPDEIRNLLQTAKEVFENEKIVVIFQPHRYTRLEREDGNFAKALQLADEVVVTEVYDAFEERKNGISGKMIWDSLKSLGKEAYFVEKLPELEKVIPVSENTVFLFVGAGDIIHSSRRFVERYQSSKSSPSRVLGSNK",
	"function": [
	"Cell wall formation."
	],
	"catalytic activity": [
	"UDP-N-acetyl-alpha-D-muramate + L-alanine + ATP = UDP-N-acetyl-alpha-D-muramoyl-L-alanine + ADP + phosphate + H(+)"
	],
	"pathway": [
	"Cell wall biogenesis; peptidoglycan biosynthesis."
	],
	"similarity": [
	"Belongs to the MurCDEF family."
	],
	"prompt": "Belongs to the MurCDEF family.Cell wall formation.UDP-N-acetyl-alpha-D-muramate + L-alanine + ATP = UDP-N-acetyl-alpha-D-muramoyl-L-alanine + ADP + phosphate + H(+).Cell wall biogenesis; peptidoglycan biosynthesis.",
	"func_sim": "Belongs to the MurCDEF family.Cell wall formation."
	},
	{
	"uniprot_id": "B0BAV0",
	"sequence": "MAFETFSVALDKDKTLIFETGKIARQASGAVLVKMNETWVFSSACAASLSEAVGFLPFRVDYQEKFSSAGRTSGGFLKREGRPSEREILVSRLIDRSLRPSFPNRLMQDIQVLSYVWSYDGKTLPDPLAICGASAALAISEVPQNCIIAGVRVGLVGGKWVINPTRDELSASKLDLVMAGTASAVLMIEGHCDFLTEEQVLEAIAFGQTYIAKICDAIEAWQKAIGKQKNFSAVLDMPEDVQNVVSDFIREKFEKALSFRDKEALEQASKELEESVIANLVQEENSDFSLLNVKAAFKTAKSNQMRALIQDLGIRVDGRTTTEIRPISIETPLLPRTHGSCLFTRGETQSMAVCTLGGENMAQRFEDLNGDGAARFYLQYFFPPFSVGEVGRIGSPGRREIGHGKLAEKALSHVLPETSRFPYIIRLESNITESNGSSSMASVCGGCLALMDAGVPIKAPVAGIAMGLILDRDQAIILSDISGIEDHLGDMDFKVAGTAKGITAFQMDIKIEGITHKIMEQALAQAKQGRSHILNLMTQVLASPKGTVSKYAPRIETMQINTSKIATVIGPGGKQIRQIIERSGAQVDINDDGVINIAASTQESINKAKELIEGLTGEVEVGKVYNGRVTSIATFGVFVEVLPGKEGLCHISELSKQKVDNISDFVKEGDKLAVKLLSINEKGQLKLSHKATLED",
	"function": [
	"Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction."
	],
	"catalytic activity": [
	"RNA(n+1) + phosphate = RNA(n) + a ribonucleoside 5'-diphosphate"
	],
	"similarity": [
	"Belongs to the polyribonucleotide nucleotidyltransferase family."
	],
	"prompt": "Belongs to the polyribonucleotide nucleotidyltransferase family.Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.RNA(n+1) + phosphate = RNA(n) + a ribonucleoside 5'-diphosphate.",
	"func_sim": "Belongs to the polyribonucleotide nucleotidyltransferase family.Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction."
	},
	{
	"uniprot_id": "B9MCH3",
	"sequence": "MALNQLSLSLQFARDAEATAHRATLPRHAVARWIRHALAVDAEITVRIVGAEEGQRLNREFRHKDYATNVLTFDYQQEPVAVADLVLCAPVVEREAREQNKTLEEHYAHLLVHGTLHAQGWDHETSEQDAQEMEVYETAILQELGFADPYAA",
	"function": [
	"Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA."
	],
	"cofactor": [
	"Binds 1 zinc ion."
	],
	"similarity": [
	"Belongs to the endoribonuclease YbeY family."
	],
	"prompt": "Belongs to the endoribonuclease YbeY family.Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.Binds 1 zinc ion.",
	"func_sim": "Belongs to the endoribonuclease YbeY family.Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA."
	},
	{
	"uniprot_id": "B8I7Z1",
	"sequence": "MTRLKDKYLNEAAPALIEKFKYSSRMQVPKLEKVVLNMGVGEVKDNPKAMDSAVNDMTLITGQKPIVTKAKKSVAAFKLRQGMNIGCKVTLRGDRMYEFVDKLFNVAIPRVRDFRGLSSNSFDGRGNYSMGIKDQLIFPEIEYDKVDKLRGMDIVFVTTAKSDEEAKELLKLLGMPFSQN",
	"function": [
	"This is one of the proteins that bind and probably mediate the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs."
	],
	"subunit": [
	"Part of the 50S ribosomal subunit; part of the 5S rRNA/L5/L18/L25 subcomplex. Contacts the 5S rRNA and the P site tRNA. Forms a bridge to the 30S subunit in the 70S ribosome."
	],
	"similarity": [
	"Belongs to the universal ribosomal protein uL5 family."
	],
	"prompt": "Belongs to the universal ribosomal protein uL5 family.This is one of the proteins that bind and probably mediate the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.Part of the 50S ribosomal subunit; part of the 5S rRNA/L5/L18/L25 subcomplex. Contacts the 5S rRNA and the P site tRNA. Forms a bridge to the 30S subunit in the 70S ribosome.",
	"func_sim": "Belongs to the universal ribosomal protein uL5 family.This is one of the proteins that bind and probably mediate the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs."
	},
	{
	"uniprot_id": "Q3B3L6",
	"sequence": "MKLIIGLGNPESRYNNTRHNIGFDLVDSLAAAFGSSFSSGKGKYLAAKITHRQETLMLIKPTTYMNLSGHAVVAAMNFHKVQKNDILVVCDDLNLPSGTMRLRAKGSAGGQNGLKHIIESLGSDEFARLRIGIRLGEMPPGSFSSFVLGKFSAEERVVMDRTLESCREAVLDFAKNGIEHAMNHYNKSAE",
	"function": [
	"Hydrolyzes ribosome-free peptidyl-tRNAs (with 1 or more amino acids incorporated), which drop off the ribosome during protein synthesis, or as a result of ribosome stalling.",
	"Catalyzes the release of premature peptidyl moieties from peptidyl-tRNA molecules trapped in stalled 50S ribosomal subunits, and thus maintains levels of free tRNAs and 50S ribosomes."
	],
	"catalytic activity": [
	"an N-acyl-L-alpha-aminoacyl-tRNA + H2O = an N-acyl-L-amino acid + a tRNA + H(+)"
	],
	"subunit": [
	"Monomer."
	],
	"similarity": [
	"Belongs to the PTH family."
	],
	"prompt": "Belongs to the PTH family.Hydrolyzes ribosome-free peptidyl-tRNAs (with 1 or more amino acids incorporated), which drop off the ribosome during protein synthesis, or as a result of ribosome stalling.Catalyzes the release of premature peptidyl moieties from peptidyl-tRNA molecules trapped in stalled 50S ribosomal subunits, and thus maintains levels of free tRNAs and 50S ribosomes.Monomer.an N-acyl-L-alpha-aminoacyl-tRNA + H2O = an N-acyl-L-amino acid + a tRNA + H(+).",
	"func_sim": "Belongs to the PTH family.Hydrolyzes ribosome-free peptidyl-tRNAs (with 1 or more amino acids incorporated), which drop off the ribosome during protein synthesis, or as a result of ribosome stalling.Catalyzes the release of premature peptidyl moieties from peptidyl-tRNA molecules trapped in stalled 50S ribosomal subunits, and thus maintains levels of free tRNAs and 50S ribosomes."
	},
	{
	"uniprot_id": "A9MXA7",
	"sequence": "MAGAKEIRSKIASVQNTQKITKAMEMVAASKMRKSQDRMAASRPYAETMRKVIGHLANGNLEYKHPYLEERDVKRVGYLVVSTDRGLCGGLNINLFKKLLADMKAWSDKGVQCELAMIGSKGVSFFNSVGGNVVAQVTGMGDNPSLSELIGPVKVMLQAYDEGRLDKLYIVSNKFINTMSQVPTITQLLPLPASEDDDLKRKAWDYLYEPDPKALLDTLLRRYVESQVYQGVVENLASEQAARMVAMKAATDNGGSLIKELQLVYNKARQASITQELTEIVSGAAAV",
	"function": [
	"Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex."
	],
	"subunit": [
	"F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c."
	],
	"similarity": [
	"Belongs to the ATPase gamma chain family."
	],
	"prompt": "Belongs to the ATPase gamma chain family.Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c.",
	"func_sim": "Belongs to the ATPase gamma chain family.Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex."
	},
	{
	"uniprot_id": "Q3YRK8",
	"sequence": "MVTQKIYIELKAFDSCLLDRSARSIILTAKRSGARVNGPIFFPRKVMKFIVNRSTHVDKKSREQFEIRTHKRLISLPRANSTIIQALMSLQLPAGVDVKVKVIGGNNG",
	"function": [
	"Involved in the binding of tRNA to the ribosomes."
	],
	"subunit": [
	"Part of the 30S ribosomal subunit."
	],
	"similarity": [
	"Belongs to the universal ribosomal protein uS10 family."
	],
	"prompt": "Belongs to the universal ribosomal protein uS10 family.Involved in the binding of tRNA to the ribosomes.Part of the 30S ribosomal subunit.",
	"func_sim": "Belongs to the universal ribosomal protein uS10 family.Involved in the binding of tRNA to the ribosomes."
	},
	{
	"uniprot_id": "Q3ASI0",
	"sequence": "MIVIDGKKVSLELKNELRERVEALNAKCGKVPGLTVIIVGEDPASQVYVRNKAKSCKEIGMNSTVIELPADTTQEHLLKIINDLNNDDTVHGILVQQPMPKQIDEFTITLAIDPAKDVDGFHPENLGRLVMGHLDKCFVSCTPYGILELLGRYNIETKGKHCVVVGRSNIVGKPMANLMLQKLKESNCTVTICHSATPNITEFTKQADILIAAIGKANFITADMVKAGAVVIDVGINRVDDASAKNGYRLVGDVEYAGVSALASAITPVPGGVGPMTIAMLLKNTVQSFQRVNGL",
	"function": [
	"Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate."
	],
	"catalytic activity": [
	"(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = (6R)-5,10-methenyltetrahydrofolate + NADPH",
	"(6R)-5,10-methenyltetrahydrofolate + H2O = (6R)-10-formyltetrahydrofolate + H(+)"
	],
	"pathway": [
	"One-carbon metabolism; tetrahydrofolate interconversion."
	],
	"subunit": [
	"Homodimer."
	],
	"similarity": [
	"Belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family."
	],
	"prompt": "Belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family.Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.Homodimer.(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = (6R)-5,10-methenyltetrahydrofolate + NADPH.(6R)-5,10-methenyltetrahydrofolate + H2O = (6R)-10-formyltetrahydrofolate + H(+).One-carbon metabolism; tetrahydrofolate interconversion.",
	"func_sim": "Belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family.Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate."
	},
	{
	"uniprot_id": "B7LHN5",
	"sequence": "MSTLEQKLTEMITAPVEALGFELVGIEFIRGRTSTLRIYIDSEDGINVDDCADVSHQVSAVLDVEDPITVAYNLEVSSPGLDRPLFTAEHYARFVGEEVTLVLRMAVQNRRKWQGVIKAVDGEMITVTVEGKDEVFALSNIQKANLVPHF",
	"function": [
	"Required for maturation of 30S ribosomal subunits."
	],
	"similarity": [
	"Belongs to the RimP family."
	],
	"prompt": "Belongs to the RimP family.Required for maturation of 30S ribosomal subunits.",
	"func_sim": "Belongs to the RimP family.Required for maturation of 30S ribosomal subunits."
	},
	{
	"uniprot_id": "Q8L803",
	"sequence": "MASPSCASTLPWTAAAFSYPRRLQTRRAPSLVIVAQGRVKKYRQVILKDDIDEISGKKGDTMKVRAGFYRNFLLPKGKATLLTPDVLKEMQLEQERIEAEKKRVKEEAQQLARVFETIGAFKVPRKGGKGKQIFGSVTAQDLVDIIKSQLNRDVDKRLVEVPEIREVGEYVAEIKLHPDVTAKVRLTVYTK",
	"function": [
	"Binds to the 23S rRNA."
	],
	"subunit": [
	"Part of the 50S ribosomal subunit."
	],
	"similarity": [
	"Belongs to the bacterial ribosomal protein bL9 family."
	],
	"prompt": "Belongs to the bacterial ribosomal protein bL9 family.Binds to the 23S rRNA.Part of the 50S ribosomal subunit.",
	"func_sim": "Belongs to the bacterial ribosomal protein bL9 family.Binds to the 23S rRNA."
	},
	{
	"uniprot_id": "Q661M5",
	"sequence": "MAKKKAISWIKLQVPAAQAAPGAKIGQALGPHGVSGPQFVKEFNERTAKMDPGIVVPVIITVYSDKSFSFIVKTPPASILIKKTIGIESGSKKSNTDKVGTISKEKLMEIVKIKMPDLNAKSESAAFKIISGSARSMGVEVEK",
	"function": [
	"Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors."
	],
	"subunit": [
	"Part of the ribosomal stalk of the 50S ribosomal subunit. Interacts with L10 and the large rRNA to form the base of the stalk. L10 forms an elongated spine to which L12 dimers bind in a sequential fashion forming a multimeric L10(L12)X complex."
	],
	"PTM": [
	"One or more lysine residues are methylated."
	],
	"similarity": [
	"Belongs to the universal ribosomal protein uL11 family."
	],
	"prompt": "Belongs to the universal ribosomal protein uL11 family.Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.Part of the ribosomal stalk of the 50S ribosomal subunit. Interacts with L10 and the large rRNA to form the base of the stalk. L10 forms an elongated spine to which L12 dimers bind in a sequential fashion forming a multimeric L10(L12)X complex.One or more lysine residues are methylated.",
	"func_sim": "Belongs to the universal ribosomal protein uL11 family.Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors."
	},
	{
	"uniprot_id": "A6GYU1",
	"sequence": "MADLKQFAEQLVNLTVKEVNDLATILKDEYGIEPAAAAVVMQAGGGEAAEEAQTEFTVVLKEAGASKLAVVKAVKELTGLGLKEAKDLVDAAPSNVKEGVSKDEAEGLKKSLEEAGAVVELK",
	"function": [
	"Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation."
	],
	"subunit": [
	"Homodimer. Part of the ribosomal stalk of the 50S ribosomal subunit. Forms a multimeric L10(L12)X complex, where L10 forms an elongated spine to which 2 to 4 L12 dimers bind in a sequential fashion. Binds GTP-bound translation factors."
	],
	"similarity": [
	"Belongs to the bacterial ribosomal protein bL12 family."
	],
	"prompt": "Belongs to the bacterial ribosomal protein bL12 family.Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation.Homodimer. Part of the ribosomal stalk of the 50S ribosomal subunit. Forms a multimeric L10(L12)X complex, where L10 forms an elongated spine to which 2 to 4 L12 dimers bind in a sequential fashion. Binds GTP-bound translation factors.",
	"func_sim": "Belongs to the bacterial ribosomal protein bL12 family.Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation."
	},
	{
	"uniprot_id": "A4I4C5",
	"sequence": "MPHRSLVCFAAPADKKAFMELVKTLRYRTEAPISDCSAALKETDGDMDAAMQVLRKRGAARAMKKGDRVTEHGFVVSCVGSTPASGAAIVTICSETDFAARNEHFQKVCVQARDQLCKLMDATNGAVLANPEEAVKHLSDVMAEELRVAIAVLGENMRVRSIAPLVPAPHMSERLLIGSYTHGSLNVDNVGRIVGLVALSQVRENEVVPKDVLTSVGRHFVATSGAEGNYAHQNFFGSETETVGKWLKQRGLKFSSSLVQEFGKEPVVHTAPEPHR",
	"function": [
	"Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome."
	],
	"miscellaneous": [
	"This protein may be expected to contain an N-terminal transit peptide but none has been predicted."
	],
	"similarity": [
	"Belongs to the EF-Ts family."
	],
	"prompt": "Belongs to the EF-Ts family.Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.This protein may be expected to contain an N-terminal transit peptide but none has been predicted.",
	"func_sim": "Belongs to the EF-Ts family.Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome."
	},
	{
	"uniprot_id": "P47415",
	"sequence": "MELHQLKSVSKSRNHKSKVVGRGHGSGLGKTSSRGQKGQKARKSGLTRLGFEGGQTPLYRRLPKYGVANKGILKKRWVVLNLNKVAKLNLKTVTRATLIEKKVISKKNNLPLKLIGNTKLTTPIHFEVQKISKNALNAVQTSKGSVKIIT",
	"function": [
	"Binds to the 23S rRNA."
	],
	"subunit": [
	"Part of the 50S ribosomal subunit."
	],
	"similarity": [
	"Belongs to the universal ribosomal protein uL15 family."
	],
	"prompt": "Belongs to the universal ribosomal protein uL15 family.Binds to the 23S rRNA.Part of the 50S ribosomal subunit.",
	"func_sim": "Belongs to the universal ribosomal protein uL15 family.Binds to the 23S rRNA."
	},
	{
	"uniprot_id": "B5XKP8",
	"sequence": "MTKKEQALIEQYAKSLVEVASEHHSLDALQADVLAILETFVTTNLDQSLSSLAVPHAEKIKLLTLLKGNNSVYMNNFLNLILQNEREAYLYQMLQAVLNEIAIVSNQYDVTVTSSLPLTEEQKSRVRAVVAKKFAVTAGRLIEKVDPSLIGGFIISVNNKVIDTSIRRQLQAFKMNLK",
	"function": [
	"F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.",
	"This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction."
	],
	"subunit": [
	"F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains."
	],
	"similarity": [
	"Belongs to the ATPase delta chain family."
	],
	"prompt": "Belongs to the ATPase delta chain family.F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction.F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains.",
	"func_sim": "Belongs to the ATPase delta chain family.F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction."
	},
	{
	"uniprot_id": "Q6AF77",
	"sequence": "MRLVFAGTPAVAVPSLTALAARFEVAAVITREDAPLGRKRILTPSPVAIAAEELGLSVIRANRLREEAIERVRVLRPDVGVVVAYGGLVHEPLLSLPRRGWVNLHFSLLPRWRGAAPVQHALIAGDRETGAAVFQLVPELDAGDVFGELRRLIRPDETAGELLDDLARSGARLLADTVAALADGTAVATPQSGEPVAAPKLGIADAKLDLTRPADEVYARFRGVTPEPGAWALLDGERFKIHAVRPTAAGVLPPGAVVADGKRILAGTGSRPLELVTVQPAGKRVMAAADWWRGAGGEAVLS",
	"function": [
	"Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus."
	],
	"catalytic activity": [
	"L-methionyl-tRNA(fMet) + (6R)-10-formyltetrahydrofolate = N-formyl-L-methionyl-tRNA(fMet) + (6S)-5,6,7,8-tetrahydrofolate + H(+)"
	],
	"similarity": [
	"Belongs to the Fmt family."
	],
	"prompt": "Belongs to the Fmt family.Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.L-methionyl-tRNA(fMet) + (6R)-10-formyltetrahydrofolate = N-formyl-L-methionyl-tRNA(fMet) + (6S)-5,6,7,8-tetrahydrofolate + H(+).",
	"func_sim": "Belongs to the Fmt family.Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus."
	},
	{
	"uniprot_id": "Q97SY4",
	"sequence": "MYAYLKGIITKITAKYIVLETNGIGYILHVANPYAYSGQVNQEAQIYVHQVVREDAHLLYGFRSEDEKKLFLSLISVSGIGPVSALAIIAADDNAGLVQAIETKNITYLTKFPKIGKKTAQQMVLDLEGKVVVAGDDLPAKVAVQASAENQELEEAMEAMLALGYKATELKKIKKFFEGTTDTAENYIKSALKMLVK",
	"function": [
	"The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA."
	],
	"subunit": [
	"Homotetramer. Forms an RuvA(8)-RuvB(12)-Holliday junction (HJ) complex. HJ DNA is sandwiched between 2 RuvA tetramers; dsDNA enters through RuvA and exits via RuvB. An RuvB hexamer assembles on each DNA strand where it exits the tetramer. Each RuvB hexamer is contacted by two RuvA subunits (via domain III) on 2 adjacent RuvB subunits; this complex drives branch migration. In the full resolvosome a probable DNA-RuvA(4)-RuvB(12)-RuvC(2) complex forms which resolves the HJ."
	],
	"domain": [
	"Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB."
	],
	"similarity": [
	"Belongs to the RuvA family."
	],
	"prompt": "Belongs to the RuvA family.The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.Homotetramer. Forms an RuvA(8)-RuvB(12)-Holliday junction (HJ) complex. HJ DNA is sandwiched between 2 RuvA tetramers; dsDNA enters through RuvA and exits via RuvB. An RuvB hexamer assembles on each DNA strand where it exits the tetramer. Each RuvB hexamer is contacted by two RuvA subunits (via domain III) on 2 adjacent RuvB subunits; this complex drives branch migration. In the full resolvosome a probable DNA-RuvA(4)-RuvB(12)-RuvC(2) complex forms which resolves the HJ.Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.",
	"func_sim": "Belongs to the RuvA family.The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA."
	},
	{
	"uniprot_id": "B4S6X4",
	"sequence": "MKRTFQPHNRKRRNKHGFRARMATKNGRRILASRRAKGRHSLSVSSAMGTRKQ",
	"similarity": [
	"Belongs to the bacterial ribosomal protein bL34 family."
	],
	"prompt": "Belongs to the bacterial ribosomal protein bL34 family.",
	"func_sim": "Belongs to the bacterial ribosomal protein bL34 family."
	},
	{
	"uniprot_id": "B8H416",
	"sequence": "MPTINQLIRKPRSPKPVRNKVPALKGCPQRRGVCTRVYTTTPKKPNSALRKVAKVRLTTGIEAVCYIPGEGHNLQEHSVVLIRGGRVKDLPGVRYHILRGVLDTQGVKDRKQRRSLYGAKRPK",
	"function": [
	"With S4 and S5 plays an important role in translational accuracy.",
	"Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit."
	],
	"subunit": [
	"Part of the 30S ribosomal subunit. Contacts proteins S8 and S17. May interact with IF1 in the 30S initiation complex."
	],
	"similarity": [
	"Belongs to the universal ribosomal protein uS12 family."
	],
	"prompt": "Belongs to the universal ribosomal protein uS12 family.With S4 and S5 plays an important role in translational accuracy.Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit.Part of the 30S ribosomal subunit. Contacts proteins S8 and S17. May interact with IF1 in the 30S initiation complex.",
	"func_sim": "Belongs to the universal ribosomal protein uS12 family.With S4 and S5 plays an important role in translational accuracy.Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit."
	},
	{
	"uniprot_id": "Q48EV0",
	"sequence": "MSHIRNFSIIAHIDHGKSTLADRFIQMCGGLSEREMEAQVLDSMDLERERGITIKAHSVTLYYKAKDGITYQLNFIDTPGHVDFTYEVSRSLAACEGALLVVDAGQGVEAQSVANCYTAIEQGLEVMPVLNKMDLPQADPDRVKEEIEKIIGIDATDAVACSAKSGMGVDEVLERLVATIPAPTGNIEDPLQALIIDSWFDNYLGVVSLVRVRHGRVKKGDKILVKSTGKLHLVDSVGVFNPKHTATVDLKAGEVGFIIAGIKDIHGAPVGDTLTLSTTPDVDVLPGFKRIQPQVYAGLFPVSSDDFEDFREALQKLTLNDSSLQYLPESSDALGFGFRCGFLGMLHMEIIQERLEREYNLDLITTAPTVIFELLLKTGETIYVDNPSKLPDLSSIEDMREPIVRANILVPQEHLGNVITLCIEKRGVQHDMLFLGTQVQVSYDLPMNEVVLDFFDRLKSVSRGYASLDYHFDRYQSANLVKLDVLINAEKVDALALIVHRDNAHYKGRALTEKMKELIPRQMFDVAIQAAIGGQIVARTTVKALRKNVLAKCYGGDVSRKRKLLEKQKAGKKRMKQVGNVEIPQEAFLAVLRLE",
	"function": [
	"Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner."
	],
	"catalytic activity": [
	"GTP + H2O = GDP + phosphate + H(+)"
	],
	"similarity": [
	"Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. LepA subfamily."
	],
	"prompt": "Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. LepA subfamily.Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner.GTP + H2O = GDP + phosphate + H(+).",
	"func_sim": "Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. LepA subfamily.Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner."
	},
	{
	"uniprot_id": "Q1CJV7",
	"sequence": "MESIIQQINQLRTSLRHHEHQYHVLDAPEIPDAEYDRMMQQLRDLEAQHPELVTNDSPTQRVGAAPLDAFEQVKHEVPMLSLDNVFDEESYLAFDKRVHDRLKTAEPLTFCCELKLDGLAVSLLYENGELVRAATRGDGTTGENITANVRTIRAIPLRLHGDNVPRRVEVRGEVFMPQAGFEQLNEEARRKGGKVFANPRNAAAGSLRQLDPRITAKRPLTFFCYGVGLLDGGELPRSHIQCLMQFKAWGLPVSERVKLCTGSDQVIAFYRQIEQDRAGLGFDIDGVVIKVDDLALQEQLGFVARAPRWATAFKFPAQEQITQVREVEFQVGRTGAITPVARLEPVQVAGVIVSNATLHNADEIERLGLRIGDTVIVRRAGDVIPQVVGVVMEQRPDDTKEITFPSQCPVCGSDIERVEGEAVARCTGGLFCAAQRKEALKHFVSRRALDVDGMGDKIIEQLVEKQYVENPADLFQLTAGKLTGLDRMGPKSAQNLIAALEKAKQTTFARFLYALGIREVGEATAANLAAHFRTLDNLRAADIETLKSVPDVGEVVAKHVMNFLSEEHNQKVIEELEKVVSWPEPQQIVVEESDSPFAGKTVVLTGSLTILSRDEAKDRLTALGAKVSGSVSKKTHLVIAGEAAGSKLAKAQELGIKVIDEAEMIRLLGE",
	"function": [
	"DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA."
	],
	"catalytic activity": [
	"NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-nicotinamide D-nucleotide."
	],
	"similarity": [
	"Belongs to the NAD-dependent DNA ligase family. LigA subfamily."
	],
	"prompt": "Belongs to the NAD-dependent DNA ligase family. LigA subfamily.DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-nicotinamide D-nucleotide.",
	"func_sim": "Belongs to the NAD-dependent DNA ligase family. LigA subfamily.DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA."
	},
	{
	"uniprot_id": "Q04MN2",
	"sequence": "MGRSLKKGPFVDEHLMKKVEAQANDEKKKVIKTWSRRSTIFPSFIGYTIAVYDGRKHVPVYIQEDMVGHKLGEFAPTRTYKGHAADDKKTRRK",
	"function": [
	"Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA."
	],
	"similarity": [
	"Belongs to the universal ribosomal protein uS19 family."
	],
	"prompt": "Belongs to the universal ribosomal protein uS19 family.Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.",
	"func_sim": "Belongs to the universal ribosomal protein uS19 family.Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA."
	},
	{
	"uniprot_id": "Q9REQ9",
	"sequence": "MTSDSFLAPHIPVLLDEVIEALSPVEGGIYIDGTFGAGGYSRAILEKADTQVIAFDRDPDAIREGASLVEKYKGRLRLVNDCFSNIGHHLDALDIKTVDGMVFDIGVSSMQIDRPERGFSIQADGPLDMRMAQAGLSAEEFLNNAQEKDIADVLYLYGEERQSRRVARAIVAARPLTTTFQLAKVIRQSLGYRPFDKKDPAAHCFQAIRIHLNRELDELKDGLQTAERFLKTKGCLAVVTFHSLEDRIVKHFMREHAGQTGQVSRHQPVIPQQNPVFFSKPARPVRAGETELARNPRARSATLRAVYRTETPFSEDISRPDTHIPRSRRQSA",
	"function": [
	"Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA."
	],
	"catalytic activity": [
	"cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine + H(+)"
	],
	"similarity": [
	"Belongs to the methyltransferase superfamily. RsmH family."
	],
	"prompt": "Belongs to the methyltransferase superfamily. RsmH family.Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine + H(+).",
	"func_sim": "Belongs to the methyltransferase superfamily. RsmH family.Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA."
	},
	{
	"uniprot_id": "A0R8K7",
	"sequence": "MAYRKLGRTSAQRKAMLRDLATDLIINERIQTTETRAKELRSVVEKMITLGKRGDLHARRQAAAFIRNEVANAETGQDALQKLFADVAPRYAERQGGYTRIAKIGPRRGDAAPMVIIELV",
	"subunit": [
	"Part of the 50S ribosomal subunit. Contacts protein L32."
	],
	"similarity": [
	"Belongs to the bacterial ribosomal protein bL17 family."
	],
	"prompt": "Belongs to the bacterial ribosomal protein bL17 family.Part of the 50S ribosomal subunit. Contacts protein L32.",
	"func_sim": "Belongs to the bacterial ribosomal protein bL17 family."
	},
	{
	"uniprot_id": "A4YCI2",
	"sequence": "MSINATLLGQAISFALFVWFCIKFVWPPLMNAIEERQKKIADGLADAGRAAKDLELAQAKATEQLKEAKVTANEIIEQANKRKAQIVEEAKAEADAERAKIIAQGKAEIENERSRVKDDLRKQVAALAVLGAERILERSIDQAAHSDIVDKLVAEI",
	"function": [
	"F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.",
	"Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0)."
	],
	"subunit": [
	"F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains."
	],
	"similarity": [
	"Belongs to the ATPase B chain family."
	],
	"prompt": "Belongs to the ATPase B chain family.F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains.",
	"func_sim": "Belongs to the ATPase B chain family.F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0)."
	},
	{
	"uniprot_id": "P0A7U8",
	"sequence": "MANIKSAKKRAIQSEKARKHNASRRSMMRTFIKKVYAAIEAGDKAAAQKAFNEMQPIVDRQAAKGLIHKNKAARHKANLTAQINKLA",
	"function": [
	"Binds directly to 16S ribosomal RNA."
	],
	"similarity": [
	"Belongs to the bacterial ribosomal protein bS20 family."
	],
	"prompt": "Belongs to the bacterial ribosomal protein bS20 family.Binds directly to 16S ribosomal RNA.",
	"func_sim": "Belongs to the bacterial ribosomal protein bS20 family.Binds directly to 16S ribosomal RNA."
	},
	{
	"uniprot_id": "Q39YQ1",
	"sequence": "MFDKIEELEIRYQELESLLAVPTVIANQPEFRKLSREHNDLTGLVEAYRRYKKVLAEIEGNRELLADPEMKEMAEAELEDLERQQEELEGEIKLLLLPKDPNDDRNVILEIRAGTGGDESALFAGDLFRMYSRFAERNRWKVEVMSASESERGGFKEVVALIEGQAVFAKLKYESGTHRVQRVPETEAQGRIHTSACTVAVLPEAEDIEIDINPVDLKIDVYRASGAGGQHVNKTESAVRITHLPTGIVVECQDERSQIKNRSKAMKVLKSRILDGLQQEQNARIAADRKQQVGSGDRSERIRTYNFPQGRMTDHRIGLTLYRLDALMEGDIAEVVDSLRAHYQMEALKAQAEAA",
	"function": [
	"Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA."
	],
	"PTM": [
	"Methylated by PrmC. Methylation increases the termination efficiency of RF1."
	],
	"similarity": [
	"Belongs to the prokaryotic/mitochondrial release factor family."
	],
	"prompt": "Belongs to the prokaryotic/mitochondrial release factor family.Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.Methylated by PrmC. Methylation increases the termination efficiency of RF1.",
	"func_sim": "Belongs to the prokaryotic/mitochondrial release factor family.Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA."
	},
	{
	"uniprot_id": "Q8XHS6",
	"sequence": "MALKKFNPTTPSRRQMTMPTFEEVTTNAPEKSLLVSLKKTGGRNAQGKITVRHHGGGAKRKYRIIDFKRNKDGIPAKVATVEYDPNRSAYIALVVYADGEKRYILAPVGLKVGDTVVSGPEADIKPGNALQLKHMPVGTFVHNIELQAGKGGQMVRSAGTSAQLMAKEGNYATLRLPSGEMRYVRIECKATVGTVSNTTHEIVNIGKAGRKRHMGWRPTVRGSVMNPCDHPHGGGEGRSPIGRPSPVTPWGKPALGYKTRKNKKYSDRFIIKRRNAK",
	"function": [
	"One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome."
	],
	"subunit": [
	"Part of the 50S ribosomal subunit. Forms a bridge to the 30S subunit in the 70S ribosome."
	],
	"similarity": [
	"Belongs to the universal ribosomal protein uL2 family."
	],
	"prompt": "Belongs to the universal ribosomal protein uL2 family.One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome.Part of the 50S ribosomal subunit. Forms a bridge to the 30S subunit in the 70S ribosome.",
	"func_sim": "Belongs to the universal ribosomal protein uL2 family.One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome."
	},
	{
	"uniprot_id": "Q30Z47",
	"sequence": "MQAKATAKFVRVSPRKARLVAQNVKGKPVEDAMNILRFTPQKAGGLIFKVMHSALANAEQLPGIDVDAMVVKQVIINEGPTWKRFLPRSMGRANRILKRTSHITVILEES",
	"function": [
	"This protein binds specifically to 23S rRNA; its binding is stimulated by other ribosomal proteins, e.g. L4, L17, and L20. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome (By similarity).",
	"The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome."
	],
	"subunit": [
	"Part of the 50S ribosomal subunit."
	],
	"similarity": [
	"Belongs to the universal ribosomal protein uL22 family."
	],
	"prompt": "Belongs to the universal ribosomal protein uL22 family.This protein binds specifically to 23S rRNA; its binding is stimulated by other ribosomal proteins, e.g. L4, L17, and L20. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome (By similarity).The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome.Part of the 50S ribosomal subunit.",
	"func_sim": "Belongs to the universal ribosomal protein uL22 family.This protein binds specifically to 23S rRNA; its binding is stimulated by other ribosomal proteins, e.g. L4, L17, and L20. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome (By similarity).The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome."
	},
	{
	"uniprot_id": "B8F6P7",
	"sequence": "MARYLGPKLKLSRREGTDLFLKSGVRAIESKCKIDTAPGQHGARKPRLSDYGSQLREKQKVRRIYGILERQFRNYYKEANRLKGNTGENLLVLLEGRLDNVVYRMGFAATRAEARQLVSHKSIVVNGRVVNIPSYQVSVDDVIAVREKSKKQARIKASLELATQREKPTWLEVDATKMEGVFKRTPERSDLSADINEHLIVELYSK",
	"function": [
	"One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit.",
	"With S5 and S12 plays an important role in translational accuracy."
	],
	"subunit": [
	"Part of the 30S ribosomal subunit. Contacts protein S5. The interaction surface between S4 and S5 is involved in control of translational fidelity."
	],
	"similarity": [
	"Belongs to the universal ribosomal protein uS4 family."
	],
	"prompt": "Belongs to the universal ribosomal protein uS4 family.One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit.With S5 and S12 plays an important role in translational accuracy.Part of the 30S ribosomal subunit. Contacts protein S5. The interaction surface between S4 and S5 is involved in control of translational fidelity.",
	"func_sim": "Belongs to the universal ribosomal protein uS4 family.One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit.With S5 and S12 plays an important role in translational accuracy."
	},
	{
	"uniprot_id": "B3DPS4",
	"sequence": "MSDFVDRVTVHVKGGDGGNGSAGIRREKYKPLAGPNGGNGGDGGSVVFVADRNATSLLDYRFMPHRVAGSGTMGLGDNKDGSKGEDLILPVPCGTVVFEARGEQGKAKHPGAQLADLRHEGDRCVVAQGGAGGLGNIALANKTRRAPGFALLGELGEERDVILELKSIADVALVGFPSAGKSSLIAAMSSVKPKIADYPFTTLVPNLGVVIAGDSRYTIADVPGLIPGASEGKGLGLEFLRHIERTEIIAHVIDCATLEPDRDPMSDYHALENELALYADKLELPLGAIPIPERPRIVILNKIDVPEAKELAEFVRPEFEKLGLKVFEISTASHEGLKELNFALSALVHEMREEVANREQAEEEARVVIKPLETKGRRPRRADEGGSALEFTVERRELGNGEVFFEVRGVKPERWVMQTNFDNDEAVGYLADRLAKLGVEDELRRKGAHPGDEVRIGRGARMVEFDWDPTISAGAEMLDGSNLGARGKDLRLEELDPRTHRRSNAERRAQYHEMMDARAAVRDAMMAERKAGHWADPTVDDDRHDETSLFGHGESSEDGETEE",
	"function": [
	"An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control."
	],
	"subunit": [
	"Monomer."
	],
	"similarity": [
	"Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family."
	],
	"prompt": "Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family.An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control.Monomer.",
	"func_sim": "Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family.An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control."
	},
	{
	"uniprot_id": "Q1CA85",
	"sequence": "MLDPNMLRNELDAVAEKLARRGFKLDVEVLRQQEERRKVLQVETESLQAERNSRSKQIGAAKARGEDIEPLRLEVNALGEKLDAAKAELDKLQNEIRDLALSIPNLPDDSVPVGKNENDNIEVSRWGEPRKYDFDVKDHVSLGEMAGGLDFAAAVKLTGARFVVMKGQIARMHRALSQFMLDLHTEKHGYLEAYVPYLVNHATLYGTGQLPKFGEDLFHTKPLAEESDNSNYALIPTAEVPLTNLVRDEILEEDSLPLKLTAHTPCFRSEAGSYGRDTRGLIRMHQFDKVEMVQITRPEDSMAALEELTGHAEKVLQLLELPYRKVLLCTGDMGFGSSKTYDLEVWLPAQDTYREISSCSNMWDFQARRMQARYRNKTDRKTRLVHTLNGSGLAVGRTLVAVLENYQQADGRIQVPDVLRPYMGGLEYIG",
	"function": [
	"Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec)."
	],
	"catalytic activity": [
	"tRNA(Ser) + L-serine + ATP = L-seryl-tRNA(Ser) + AMP + diphosphate + H(+)",
	"tRNA(Sec) + L-serine + ATP = L-seryl-tRNA(Sec) + AMP + diphosphate + H(+)"
	],
	"pathway": [
	"Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1."
	],
	"subunit": [
	"Homodimer. The tRNA molecule binds across the dimer."
	],
	"domain": [
	"Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding."
	],
	"similarity": [
	"Belongs to the class-II aminoacyl-tRNA synthetase family. Type-1 seryl-tRNA synthetase subfamily."
	],
	"prompt": "Belongs to the class-II aminoacyl-tRNA synthetase family. Type-1 seryl-tRNA synthetase subfamily.Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).Homodimer. The tRNA molecule binds across the dimer.tRNA(Ser) + L-serine + ATP = L-seryl-tRNA(Ser) + AMP + diphosphate + H(+).tRNA(Sec) + L-serine + ATP = L-seryl-tRNA(Sec) + AMP + diphosphate + H(+).Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1.Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding.",
	"func_sim": "Belongs to the class-II aminoacyl-tRNA synthetase family. Type-1 seryl-tRNA synthetase subfamily.Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec)."
	},
	{
	"uniprot_id": "B6JPM4",
	"sequence": "MPKMKTNRGASKRFKVKKNLIKRGSAFKSHILTKKSPKRKANLNAPKHVHHTNAHSVMSLLCRA",
	"similarity": [
	"Belongs to the bacterial ribosomal protein bL35 family."
	],
	"prompt": "Belongs to the bacterial ribosomal protein bL35 family.",
	"func_sim": "Belongs to the bacterial ribosomal protein bL35 family."
	},
	{
	"uniprot_id": "Q2Y7W3",
	"sequence": "MPKDYSRTLRIADQIQRELADLIRNELKDPRIGMITLTGVEVSQDYAHAKVFYTTLHNESDNFLVQNGLENAAGFLRTQLLHRLKLRVIPQLHFIYDESIERGVRLSQLIDEAVASDRSEKETDST",
	"function": [
	"One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Associates with free 30S ribosomal subunits (but not with 30S subunits that are part of 70S ribosomes or polysomes). Required for efficient processing of 16S rRNA. May interact with the 5'-terminal helix region of 16S rRNA."
	],
	"subunit": [
	"Monomer. Binds 30S ribosomal subunits, but not 50S ribosomal subunits or 70S ribosomes."
	],
	"similarity": [
	"Belongs to the RbfA family."
	],
	"prompt": "Belongs to the RbfA family.One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Associates with free 30S ribosomal subunits (but not with 30S subunits that are part of 70S ribosomes or polysomes). Required for efficient processing of 16S rRNA. May interact with the 5'-terminal helix region of 16S rRNA.Monomer. Binds 30S ribosomal subunits, but not 50S ribosomal subunits or 70S ribosomes.",
	"func_sim": "Belongs to the RbfA family.One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Associates with free 30S ribosomal subunits (but not with 30S subunits that are part of 70S ribosomes or polysomes). Required for efficient processing of 16S rRNA. May interact with the 5'-terminal helix region of 16S rRNA."
	},
	{
	"uniprot_id": "A7EWR0",
	"sequence": "MICNARQKEKGGKPTGLEYLEVGSRVRDDESKRNKVKVDEDHGLYEFFRHKDKALSTPAEEGNHGRPWSAEELRGKSWEDLHSLWWICCKERNRIATESYERDRLEAGYGEEDSEKRDMTVRRTQRAIKQVLTERYYSWQEAQVVAKDDPEIDLSGQGPIYTPRDFEEDIEEEVLAESEGEVEQKPAQITA",
	"subunit": [
	"Component of the mitochondrial large ribosomal subunit. Mature mitochondrial ribosomes consist of a small (37S) and a large (54S) subunit. The 37S subunit contains at least 33 different proteins and 1 molecule of RNA (15S). The 54S subunit contains at least 45 different proteins and 1 molecule of RNA (21S) (By similarity)."
	],
	"similarity": [
	"Belongs to the universal ribosomal protein uL29 family."
	],
	"prompt": "Belongs to the universal ribosomal protein uL29 family.Component of the mitochondrial large ribosomal subunit. Mature mitochondrial ribosomes consist of a small (37S) and a large (54S) subunit. The 37S subunit contains at least 33 different proteins and 1 molecule of RNA (15S). The 54S subunit contains at least 45 different proteins and 1 molecule of RNA (21S) (By similarity).",
	"func_sim": "Belongs to the universal ribosomal protein uL29 family."
	},
	{
	"uniprot_id": "B8GNS2",
	"sequence": "MRHYEIVFMVHPDQSEQVSAMIERYRGLIEGDGGKIHRLEDWGRRQLAYPINKIHKAHYVLMNVECGEAALAELVSAFRFNDAVIRHMVMLMERAFTEASPLAKGREEDDSDSSARRARDDSDDDGDDDEDDRRASAD",
	"function": [
	"Binds together with bS18 to 16S ribosomal RNA."
	],
	"similarity": [
	"Belongs to the bacterial ribosomal protein bS6 family."
	],
	"prompt": "Belongs to the bacterial ribosomal protein bS6 family.Binds together with bS18 to 16S ribosomal RNA.",
	"func_sim": "Belongs to the bacterial ribosomal protein bS6 family.Binds together with bS18 to 16S ribosomal RNA."
	},
	{
	"uniprot_id": "B9LJ76",
	"sequence": "MYAIIRDRGMQYRVEPGQVLTIDLISAEPGSQIELGEVLLVGDAEQVKVGSPLVEGAVVRAEVLGEQKGDKIVVFRYRNKTRYRRRTGHRQRYTKIRISEIVA",
	"function": [
	"This protein binds to 23S rRNA in the presence of protein L20."
	],
	"subunit": [
	"Part of the 50S ribosomal subunit. Contacts protein L20."
	],
	"similarity": [
	"Belongs to the bacterial ribosomal protein bL21 family."
	],
	"prompt": "Belongs to the bacterial ribosomal protein bL21 family.This protein binds to 23S rRNA in the presence of protein L20.Part of the 50S ribosomal subunit. Contacts protein L20.",
	"func_sim": "Belongs to the bacterial ribosomal protein bL21 family.This protein binds to 23S rRNA in the presence of protein L20."
	},
	{
	"uniprot_id": "Q7MYG5",
	"sequence": "MSMQDPIADMLTRIRNGQAANKVAVTMPSSKLKVAIAKVLKEEGYIEDYKIEGDTKPELELVLKYFQGKAVVESIQRVSRPSLRIYKKKDELPQVMAGLGIAVVSTSKGVMTDRAARQAGLGGEILCYVA",
	"function": [
	"One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit."
	],
	"subunit": [
	"Part of the 30S ribosomal subunit. Contacts proteins S5 and S12."
	],
	"similarity": [
	"Belongs to the universal ribosomal protein uS8 family."
	],
	"prompt": "Belongs to the universal ribosomal protein uS8 family.One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit.Part of the 30S ribosomal subunit. Contacts proteins S5 and S12.",
	"func_sim": "Belongs to the universal ribosomal protein uS8 family.One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit."
	},
	{
	"uniprot_id": "Q5LU74",
	"sequence": "MLYWLTALSDGGDVWNLFRYITFRAGGAFMTALIFGFLFGRPLINVLRRKQGKGQPIRDDGPEGHFSKAGTPTMGGLLIVGALLTSTLLWARWDNPFVWMVLFVTLAYALIGFADDYAKVSKQNTKGVSGKMRLALGVIIAVIAALWASYNHPAELQNQLALPVFKDTLINLGLLYVPFAICVIVGSANAVNLTDGLDGLAIMPAMIAASTLGVIAYAVGRVDFTEYLDVHYVPGTGEILIFTAALFGAGLGFLWYNAPPAAVFMGDTGSLALGGALGAIAVATKHELVLAIVGGLFVVEALSVIIQVLYFKRTGKRVFLMAPIHHHYEKKGWAEPTIVIRFWIISLILAMIGLATLKVR",
	"function": [
	"Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I."
	],
	"catalytic activity": [
	"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + di-trans,octa-cis-undecaprenyl phosphate = di-trans,octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UMP"
	],
	"pathway": [
	"Cell wall biogenesis; peptidoglycan biosynthesis."
	],
	"similarity": [
	"Belongs to the glycosyltransferase 4 family. MraY subfamily."
	],
	"prompt": "Belongs to the glycosyltransferase 4 family. MraY subfamily.Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + di-trans,octa-cis-undecaprenyl phosphate = di-trans,octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UMP.Cell wall biogenesis; peptidoglycan biosynthesis.",
	"func_sim": "Belongs to the glycosyltransferase 4 family. MraY subfamily.Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I."
	},
	{
	"uniprot_id": "Q5L7Q8",
	"sequence": "MKIEDKLVTSVISGLKALYGQDVPAAQVQLQKTKKEFEGHLTLVVFPFLKMSKKGPEQTAQEIGEYLKANEPAVAAFNVIKGFLNLTVASATWIELLNEIHTDAQYGIVSADENAPLVMIEYSSPNTNKPLHLGHVRNNLLGNALANIVMANGNKVVKTNIVNDRGIHICKSMLAWQKYGKGETPESSGKKGDHLVGDYYVAFDKHYKAEVAELMEKGMSKEEAEAASPLMNEAREMLVKWEAGDPEVRALWQMMNNWVYAGFDETYRKMGVGFDKIYYESNTYLEGKEKVMEGLEKGFFFKKEDGSVWADLTAEGLDHKLLLRGDGTSVYMTQDIGTAKLRFADYPIDKMIYVVGNEQNYHFQVLSILLDKLGFEWGKSLVHFSYGMVELPEGKMKSREGTVVDADDLMAEMIATAKETSQELGKLDGLTQEEADDIARIVGLGALKYFILKVDARKNMTFNPKESIDFNGNTGPFIQYTYARIRSVLRKAAEAGIVIPEVLPANIELSEKEEGLIQMVADFAAVVRQAGEDYSPSGIANYVYDLVKEYNQFYHDFSILREENEDVKLFRIALSANIAKVVRLGMGLLGIEVPDRM",
	"catalytic activity": [
	"tRNA(Arg) + L-arginine + ATP = L-arginyl-tRNA(Arg) + AMP + diphosphate"
	],
	"subunit": [
	"Monomer."
	],
	"similarity": [
	"Belongs to the class-I aminoacyl-tRNA synthetase family."
	],
	"prompt": "Belongs to the class-I aminoacyl-tRNA synthetase family.Monomer.tRNA(Arg) + L-arginine + ATP = L-arginyl-tRNA(Arg) + AMP + diphosphate.",
	"func_sim": "Belongs to the class-I aminoacyl-tRNA synthetase family."
	},
	{
	"uniprot_id": "C5C0I0",
	"sequence": "MAKIKKGDLVVVISGNRDDRGKQGRVLEVLTDSNRVVVEGVRRVKKHTKVSQTQRGSRTGGIETIEAPIHVSNVMLVDPETKKGTRVGYRTEEVERNGRARTVRVRVAKRSGKDV",
	"function": [
	"One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.",
	"One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit."
	],
	"subunit": [
	"Part of the 50S ribosomal subunit."
	],
	"similarity": [
	"Belongs to the universal ribosomal protein uL24 family."
	],
	"prompt": "Belongs to the universal ribosomal protein uL24 family.One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.Part of the 50S ribosomal subunit.",
	"func_sim": "Belongs to the universal ribosomal protein uL24 family.One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit."
	},
	{
	"uniprot_id": "B1Y8I7",
	"sequence": "MTTPNPGQRLGLLGRKVGMMRIFTDDGDAVPVTVLDVSNNRVAQIKTVETDGYSAVQVAFGARKASRVTKPEAGHLAKAGVESGELLQEFRVSAEVAAECKPGSQLPIAMFQAGQQVDVQGTTIGKGFAGTIKRHHFGSQRASHGNSRSHNVPGSISMAQDPGRVFPGKKMSGHLGDDTVTTQNLDVVRVDEARQLLLVKGAVPGAKGGFVTVRPAVKVKLKKGAN",
	"function": [
	"One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit."
	],
	"subunit": [
	"Part of the 50S ribosomal subunit. Forms a cluster with proteins L14 and L19."
	],
	"PTM": [
	"Methylated by PrmB."
	],
	"similarity": [
	"Belongs to the universal ribosomal protein uL3 family."
	],
	"prompt": "Belongs to the universal ribosomal protein uL3 family.One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.Part of the 50S ribosomal subunit. Forms a cluster with proteins L14 and L19.Methylated by PrmB.",
	"func_sim": "Belongs to the universal ribosomal protein uL3 family.One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit."
	},
	{
	"uniprot_id": "Q68XR6",
	"sequence": "MLKSNNASKTATCKVGDKAAKKVFFRRRKGCPLSVPNAPVIDYKNPELLIKFVSEGGRMLPSRITNVCAKKQRKLNNAIKIARILALLPFVFQAK",
	"function": [
	"Binds as a heterodimer with protein bS6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit."
	],
	"subunit": [
	"Part of the 30S ribosomal subunit. Forms a tight heterodimer with protein bS6."
	],
	"similarity": [
	"Belongs to the bacterial ribosomal protein bS18 family."
	],
	"prompt": "Belongs to the bacterial ribosomal protein bS18 family.Binds as a heterodimer with protein bS6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit.Part of the 30S ribosomal subunit. Forms a tight heterodimer with protein bS6.",
	"func_sim": "Belongs to the bacterial ribosomal protein bS18 family.Binds as a heterodimer with protein bS6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit."
	},
	{
	"uniprot_id": "B1XJI0",
	"sequence": "MNATATQDRPIYWGTGRRKASIARVRLVPGSGKVVVNNRSGEDYFNRIPGYLAVLKSPLETLGLESEYDILVNAHGGGLTGQADAVKLGVARALCELDPDNRQPLKIEGYLTRDPRCKERKKYGLHKARKAPQFSKR",
	"similarity": [
	"Belongs to the universal ribosomal protein uS9 family."
	],
	"prompt": "Belongs to the universal ribosomal protein uS9 family.",
	"func_sim": "Belongs to the universal ribosomal protein uS9 family."
	},
	{
	"uniprot_id": "A8F4X1",
	"sequence": "MRISAAGGGTGGHLYPAVSILEKLAEMKKLNVTYFCLEKGIESKILPLEHPEYKLIKIDLKGLERPIWKPSNFTRLLKISQSESIIALEIKQCDFGLMTGGYISYPVGKVCKKLKKPFFIQEQNVVPGLANKALSLSAKKIFVAFDKTVEFFPKSVRNKILVTGNPVREKDNEEMLFGKDYVLVLGGSRGSEFINNLMEEVYKVEHNLKFVHSTGSKEWVDRLSIFENVKAVDYIYNASAAWKGARAVIARAGATTIGEMLYYGLPGILVPWDGATGSHQLYNALEIEKMGKALVLKECDATVSTLLKKLYQVLEMDKKPKMKINPAEIIAKTILEELK",
	"function": [
	"Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II)."
	],
	"catalytic activity": [
	"di-trans,octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-glucosamine = di-trans,octa-cis-undecaprenyl diphospho-[N-acetyl-alpha-D-glucosaminyl-(1->4)]-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UDP + H(+)"
	],
	"pathway": [
	"Cell wall biogenesis; peptidoglycan biosynthesis."
	],
	"similarity": [
	"Belongs to the glycosyltransferase 28 family. MurG subfamily."
	],
	"prompt": "Belongs to the glycosyltransferase 28 family. MurG subfamily.Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).di-trans,octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-glucosamine = di-trans,octa-cis-undecaprenyl diphospho-[N-acetyl-alpha-D-glucosaminyl-(1->4)]-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UDP + H(+).Cell wall biogenesis; peptidoglycan biosynthesis.",
	"func_sim": "Belongs to the glycosyltransferase 28 family. MurG subfamily.Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II)."
	},
	{
	"uniprot_id": "B8DWS4",
	"sequence": "MAELTIDPATIRKALDDFVEAYTPSETPTQEVGHVATAGDGIAHVTGLPGCMANELLTFEDGTLGLAFNLDAREIGVVILGDFVGIEEGQEVRRTGEVLSVPVGDGFLGRVVDPLGRPIDGMGEIKSEGRRILEAQAPDVMHRHPVDQPMSTGLKAIDAMTPIGRGQRQLIIGDRQTGKTAIAIDTIINQKKNWESGDPKKQVRCIYVAIGQKGSTIASVKQSLEEAGAMEYTTIVASPASDSAGFKYIAPYTGSAIGQHWMYNGKDVLIVFDDLSKQAEAYRSISLLLRRPPGREAYPGDVFYLHSRLLERCARVSDDLGGGSMTGLPIVETKANDVSAYIPTNVISITDGQIFLQSDLFNAGQRPAVDVGISVSRVGGAAQTKALKKVSGTLKISLARYRSLESFAMFASDLDAASKAQLNRGARLTELLKQPQFSPYSMEQEVVSVWAGTHGKFDDLAIADVLPFEHGLLEYVDRNTDILTTIRDTGDFTKETEEALDKAVDAFRETYVTKAGKPLVDKKTAPKSVTPVDQEQIKAGKAQEKK",
	"function": [
	"Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit."
	],
	"catalytic activity": [
	"ATP + H2O + 4 H(+)(in) = ADP + phosphate + 5 H(+)(out)"
	],
	"subunit": [
	"F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF(1) is attached to CF(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains."
	],
	"similarity": [
	"Belongs to the ATPase alpha/beta chains family."
	],
	"prompt": "Belongs to the ATPase alpha/beta chains family.Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF(1) is attached to CF(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains.ATP + H2O + 4 H(+)(in) = ADP + phosphate + 5 H(+)(out).",
	"func_sim": "Belongs to the ATPase alpha/beta chains family.Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit."
	},
	{
	"uniprot_id": "Q5SI56",
	"sequence": "MVSTLKRDEALFELIALEEKRQREGLELIASENFVSKQVREAVGSVLTNKYAEGYPGARYYGGCEVIDRVESLAIERAKALFGAAWANVQPHSGSQANMAVYMALMEPGDTLMGMDLAAGGHLTHGSRVNFSGKLYKVVSYGVRPDTELIDLEEVRRLALEHRPKVIVAGASAYPRFWDFKAFREIADEVGAYLVVDMAHFAGLVAAGLHPNPLPYAHVVTSTTHKTLRGPRGGLILSNDPELGKRIDKLIFPGIQGGPLEHVIAGKAVAFFEALQPEFKEYSRLVVENAKRLAEELARRGYRIVTGGTDNHLFLVDLRPKGLTGKEAEERLDAVGITVNKNAIPFDPKPPRVTSGIRIGTPAITTRGFTPEEMPLVAELIDRALLEGPSEALREEVRRLALAHPMP",
	"function": [
	"Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism."
	],
	"catalytic activity": [
	"(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine"
	],
	"pathway": [
	"One-carbon metabolism; tetrahydrofolate interconversion.",
	"Amino-acid biosynthesis; glycine biosynthesis; glycine from L-serine: step 1/1."
	],
	"subunit": [
	"Homodimer."
	],
	"similarity": [
	"Belongs to the SHMT family."
	],
	"prompt": "Belongs to the SHMT family.Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.Homodimer.(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine.One-carbon metabolism; tetrahydrofolate interconversion.Amino-acid biosynthesis; glycine biosynthesis; glycine from L-serine: step 1/1.",
	"func_sim": "Belongs to the SHMT family.Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism."
	},
	{
	"uniprot_id": "Q38W03",
	"sequence": "MKKEKIIVIVGPTGVGKTALSLQVAQQLKGEIISGDAMQVYRHLDIGTAKVTPAEQAIAPHHLIDVADIDERFTAFNFQQQGQQLITKITDRQHLPLIVGGTGLYLQALLYDMTLGSATDAEQDFSIRNKWQAYLEQHSETDLWQALAKIDPDAAAKIPAANTRRVIRALEVYETTGVLFSQQKPKELRYDTFIIGLNCERPVLYERINQRVDQMVDAGLIEEARWAYERRATSPQAVRGIGYKEFFPYFDGECSLEAAIDQVKQNSRHYAKRQLTWFRNQIPVNWYNLVEHQEADLARIQEDIQTWLQK",
	"function": [
	"Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A)."
	],
	"catalytic activity": [
	"adenosine(37) in tRNA + dimethylallyl diphosphate = N(6)-dimethylallyladenosine(37) in tRNA + diphosphate"
	],
	"subunit": [
	"Monomer."
	],
	"similarity": [
	"Belongs to the IPP transferase family."
	],
	"prompt": "Belongs to the IPP transferase family.Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).Monomer.adenosine(37) in tRNA + dimethylallyl diphosphate = N(6)-dimethylallyladenosine(37) in tRNA + diphosphate.",
	"func_sim": "Belongs to the IPP transferase family.Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A)."
	},
	{
	"uniprot_id": "A5N4N6",
	"sequence": "MGKKYKESTKLIDRKTLYTPLEAMELALKTAKANFDETIELSIKLGVDPRHADQQVRGAVVLPHGTGKKVRVLVLAKGDRIKEAEDAGADYVGAEEYVEKIQKENWFDFDVVVATPDMMGVVGRLGRILGPKGLMPNPKSGTVTFDVAKAIQEIKAGKVEYRVDKTSIVHVPIGKKSFEVQKLLDNFRVLMEAIIKAKPSAAKGQYLKSVAVSSTMGPGIKINSVKVLE",
	"function": [
	"Binds directly to 23S rRNA. The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release.",
	"Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA."
	],
	"subunit": [
	"Part of the 50S ribosomal subunit."
	],
	"similarity": [
	"Belongs to the universal ribosomal protein uL1 family."
	],
	"prompt": "Belongs to the universal ribosomal protein uL1 family.Binds directly to 23S rRNA. The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release.Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA.Part of the 50S ribosomal subunit.",
	"func_sim": "Belongs to the universal ribosomal protein uL1 family.Binds directly to 23S rRNA. The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release.Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA."
	},
	{
	"uniprot_id": "A7X5D6",
	"sequence": "MAKLQITLTRSVIGRPETQRKTVEALGLKKTNSSVVVEDNPAIRGQINKVKHLVTVEEK",
	"subunit": [
	"Part of the 50S ribosomal subunit."
	],
	"similarity": [
	"Belongs to the universal ribosomal protein uL30 family."
	],
	"prompt": "Belongs to the universal ribosomal protein uL30 family.Part of the 50S ribosomal subunit.",
	"func_sim": "Belongs to the universal ribosomal protein uL30 family."
	},
	{
	"uniprot_id": "B7LV13",
	"sequence": "MRIILLGAPGAGKGTQAQFIMEKYGIPQISTGDMLRAAVKSGSELGKQAKDIMDAGKLVTDELVIALVKERIAQEDCRNGFLLDGFPRTIPQADAMKEAGINVDYVLEFDVPDELIVDRIVGRRVHAPSGRVYHVKFNPPKVEGKDDVTGEELTTRKDDQEETVRKRLVEYHQMTAPLIGYYSKEAEAGNTKYAKVDGTKPVAEVRADLEKILG",
	"function": [
	"Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism."
	],
	"catalytic activity": [
	"AMP + ATP = 2 ADP"
	],
	"pathway": [
	"Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1."
	],
	"subunit": [
	"Monomer."
	],
	"domain": [
	"Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis."
	],
	"similarity": [
	"Belongs to the adenylate kinase family."
	],
	"prompt": "Belongs to the adenylate kinase family.Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.Monomer.AMP + ATP = 2 ADP.Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1.Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.",
	"func_sim": "Belongs to the adenylate kinase family.Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism."
	},
	{
	"uniprot_id": "Q3KMZ4",
	"sequence": "MGNLIKELQDEQCRTDLADFCVGDTIRVATNISEGGKERVQVFQGTVMARKGGGAGETVSLHRVAYGEGMEKSFLLNSPKIVSIEVVKRGKVSRARLFYLRGKTGKAAKVKELIGSRAAKK",
	"function": [
	"This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site."
	],
	"similarity": [
	"Belongs to the bacterial ribosomal protein bL19 family."
	],
	"prompt": "Belongs to the bacterial ribosomal protein bL19 family.This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site.",
	"func_sim": "Belongs to the bacterial ribosomal protein bL19 family.This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site."
	},
	{
	"uniprot_id": "Q83HZ5",
	"sequence": "MGIMCSGDVSERMNKTIELLKEQFLSIHSGRVNSGQFEKVMVDCEGASVPLVSLASIRVLNANTIVVTPYDSALLSQIDRALRNVPNIGTPGNDGECIKIVMPQLTEARRHEYVKQARVKAEEARVSARNIRRKARASLDAMGLAKDEIVRREKELDKLTKDVISVVDDLLRHKESELLRL",
	"function": [
	"Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another."
	],
	"similarity": [
	"Belongs to the RRF family."
	],
	"prompt": "Belongs to the RRF family.Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another.",
	"func_sim": "Belongs to the RRF family.Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another."
	},
	{
	"uniprot_id": "Q98FJ1",
	"sequence": "MAAFKTLDDIGNISGKRVLVRVDLNVPVADGKVTDATRIERIAPTIAELSGKGAKVILLAHFGRPKDGPSPEFSLEPIARATAEVLGRPVGFASDCVGDMAGSAVAAMNKGDVLLFENTRFYKAEEKNDPAFSERLAANGDIFVNDAFSAAHRAHSSTEGLARLLPSFAGRTMQAELEALEKGLGNPVRPVVAIVGGAKVSTKIDLLMNLVKKVDALVIGGGMANTFLAARGTDVGKSLCEHDLAPTAKQIMIEAAEAGCAIILPVDGVVAKEFKAGAACETVAISDVPADGMILDVGEKTVKTIGEWIDRAATLVWNGPLGAFEIEPFDHATVAAAKHAAARTKAGKLVSVAGGGDTVAALNHAGVADDFTYVSTAGGAFLEWMEGKPLPGVDVLKR",
	"catalytic activity": [
	"(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP"
	],
	"pathway": [
	"Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5."
	],
	"subunit": [
	"Monomer."
	],
	"similarity": [
	"Belongs to the phosphoglycerate kinase family."
	],
	"prompt": "Belongs to the phosphoglycerate kinase family.Monomer.(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP.Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.",
	"func_sim": "Belongs to the phosphoglycerate kinase family."
	},
	{
	"uniprot_id": "Q0A797",
	"sequence": "MAEDKVREFAETVGIPVERLVSQLEAAGISGRGPEDPLSDLDKATLLEYLRKGRDGGEQDDDQAPSKITLRRKKVSTLKMPASGGGGSGARGPRQTRTVNVEVRKKRTYVKRSVVEAEESKHDVERLERALIEDRKRAEERARREAEEAEARRREQEEAERRQAEAEALRQAEAEREATAETAGVADEADKAEPQPDPEAARLAAEKEEARRREEEKERRRLEQEARREREAEERAARKTGATAPAAKGKQKKGRESLSMGAGKPGRRGGKKGGRRAASGGEAAKQLQHGFAKPTQPVVREVEIPESITVGDLAQKMSVKAAVLIKEMMKQGVMATINQALDQDTAVLLVEEMGHKPVIVRADALEEEVLQDTSQAQEGDKAPRPPVVTVMGHVDHGKTSLLDNIRRAKVADAEAGGITQHIGAYHVETDRGMVTFLDTPGHEAFTAMRARGAQLTDIVVLVVAADDGVMPQTEEAVRHAKAAEVPMVVAVNKIDKPDADPDRVKQELSQMEVIPEEWGGDVQFIHVSAKQGEGLDDLLEAILLQAELMELGAVAEGNASGIVLESSLDKGRGPVATVLVQSGLLKKGDSLLCGTEYGRVRALIDETGKRVDEAGPSIPVVVLGLSGLPSAGDDMVVVDDEKKAREVAEMRKERQRDKRLAQQQAARMENLFNQMKEDEVNTVNLVVKADVQGSAEALQQSLANLSTDDIQVKVISSGVGAINESDVNLALASNAILIGFNVRADAAARRLVQENDVDLHYYSVIYDAIEQVKNAISGMLEPELEEHIIGLAEVKDVFRSSKLGAVAGCLVTEGAVRRKNPIRVLRDNVVIYEGELESLRRHKDDVTEVKSGTECGIGVKNYNDVRIGDQIECYERVEVRREL",
	"function": [
	"One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex."
	],
	"similarity": [
	"Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. IF-2 subfamily."
	],
	"prompt": "Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. IF-2 subfamily.One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex.",
	"func_sim": "Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. IF-2 subfamily.One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex."
	},
	{
	"uniprot_id": "Q7NZS2",
	"sequence": "MAHKKAGGSSRNGRDSEAKRLGVKVYGSELIPAGSIIVRQRGTKFHAGENVGQGKDHTLFAKVDGYVEFTVKGAQQRKTVNVVPYTGVDGE",
	"similarity": [
	"Belongs to the bacterial ribosomal protein bL27 family."
	],
	"prompt": "Belongs to the bacterial ribosomal protein bL27 family.",
	"func_sim": "Belongs to the bacterial ribosomal protein bL27 family."
	},
	{
	"uniprot_id": "Q3Z7T5",
	"sequence": "MVKKIREKKKIAVDELTDALAVAQSAVFTDYRGISTSELTTIRMKLREAGVGYRVLKNTLARRAADNTDHANIKSAFEGPVAMAYSSSDVVAPAKVLMDYLAGSKSTLKVTGGYLSNKLISVEEVAELAKLPSREVLISKVLAGMQSPIAGLAMVLNGPARGLAVVLQARMKQLEG",
	"function": [
	"Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors."
	],
	"subunit": [
	"Part of the ribosomal stalk of the 50S ribosomal subunit. The N-terminus interacts with L11 and the large rRNA to form the base of the stalk. The C-terminus forms an elongated spine to which L12 dimers bind in a sequential fashion forming a multimeric L10(L12)X complex."
	],
	"similarity": [
	"Belongs to the universal ribosomal protein uL10 family."
	],
	"prompt": "Belongs to the universal ribosomal protein uL10 family.Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors.Part of the ribosomal stalk of the 50S ribosomal subunit. The N-terminus interacts with L11 and the large rRNA to form the base of the stalk. The C-terminus forms an elongated spine to which L12 dimers bind in a sequential fashion forming a multimeric L10(L12)X complex.",
	"func_sim": "Belongs to the universal ribosomal protein uL10 family.Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors."
	},
	{
	"uniprot_id": "B5REG6",
	"sequence": "MRVLGIETSCDETGIAIYDDKKGLLANQLYSQVKLHADYGGVVPELASRDHVRKTVPLIQAALKEAGLTASDIDAVAYTAGPGLVGALLVGATVGRSLAFAWNVPAIPVHHMEGHLLAPMLEDNPPEFPFVALLVSGGHTQLISVTGIGQYELLGESIDDAAGEAFDKTAKLLGLDYPGGPMLSKMASQGTAGRFVFPRPMTDRPGLDFSFSGLKTFAANTIRSNGGDEQTRADIARAFEDAVVDTLMIKCKRALESTGFKRLVMAGGVSANRTLRAKLAEMMQKRRGEVFYARPEFCTDNGAMIAYAGMVRFKAGVTADLGVTVRPRWPLAELPAA",
	"function": [
	"Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction."
	],
	"catalytic activity": [
	"L-threonylcarbamoyladenylate + adenosine(37) in tRNA = N(6)-L-threonylcarbamoyladenosine(37) in tRNA + AMP + H(+)"
	],
	"cofactor": [
	"Binds 1 Fe(2+) ion per subunit."
	],
	"similarity": [
	"Belongs to the KAE1 / TsaD family."
	],
	"prompt": "Belongs to the KAE1 / TsaD family.Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.L-threonylcarbamoyladenylate + adenosine(37) in tRNA = N(6)-L-threonylcarbamoyladenosine(37) in tRNA + AMP + H(+).Binds 1 Fe(2+) ion per subunit.",
	"func_sim": "Belongs to the KAE1 / TsaD family.Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction."
	},
	{
	"uniprot_id": "P61531",
	"sequence": "MTANVCLDESVRPRLLDDFIGQDELRANMRVYLDAARERGQAMDHVLFYGNPGLGKTTLAQIMAGELGVNLVSTSGPVLERSGDLAAILTNLGRHDLLFVDEIHRMPIAVEEVLYPAMEDFKLDLVIGQGPGARTVKIDVEPFTLVGATTRIGLLSSPLRDRFGIISRLEYYTPADLARIVARTARIIGANLTEEGAIEIGRRARGTPRIANRLLRRVRDFATVHAGGVISADLASEALGRMEVDESGLDQMDRKLLEVLIEHYGGGPVGIKTLAVACAEEVRTIEDIYEPYLIQCGFLKRTPRGRVATAKAYRHLNLLG",
	"function": [
	"The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. RuvB forms 2 homohexamers on either side of HJ DNA bound by 1 or 2 RuvA tetramers; 4 subunits per hexamer contact DNA at a time. Coordinated motions by a converter formed by DNA-disengaged RuvB subunits stimulates ATP hydrolysis and nucleotide exchange. Immobilization of the converter enables RuvB to convert the ATP-contained energy into a lever motion, pulling 2 nucleotides of DNA out of the RuvA tetramer per ATP hydrolyzed, thus driving DNA branch migration. The RuvB motors rotate together with the DNA substrate, which together with the progressing nucleotide cycle form the mechanistic basis for DNA recombination by continuous HJ branch migration. Branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves cruciform DNA."
	],
	"catalytic activity": [
	"ATP + H2O = ADP + phosphate + H(+)"
	],
	"subunit": [
	"Homohexamer. Forms an RuvA(8)-RuvB(12)-Holliday junction (HJ) complex. HJ DNA is sandwiched between 2 RuvA tetramers; dsDNA enters through RuvA and exits via RuvB. An RuvB hexamer assembles on each DNA strand where it exits the tetramer. Each RuvB hexamer is contacted by two RuvA subunits (via domain III) on 2 adjacent RuvB subunits; this complex drives branch migration. In the full resolvosome a probable DNA-RuvA(4)-RuvB(12)-RuvC(2) complex forms which resolves the HJ."
	],
	"domain": [
	"Has 3 domains, the large (RuvB-L) and small ATPase (RuvB-S) domains and the C-terminal head (RuvB-H) domain. The head domain binds DNA, while the ATPase domains jointly bind ATP, ADP or are empty depending on the state of the subunit in the translocation cycle. During a single DNA translocation step the structure of each domain remains the same, but their relative positions change."
	],
	"similarity": [
	"Belongs to the RuvB family."
	],
	"prompt": "Belongs to the RuvB family.The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. RuvB forms 2 homohexamers on either side of HJ DNA bound by 1 or 2 RuvA tetramers; 4 subunits per hexamer contact DNA at a time. Coordinated motions by a converter formed by DNA-disengaged RuvB subunits stimulates ATP hydrolysis and nucleotide exchange. Immobilization of the converter enables RuvB to convert the ATP-contained energy into a lever motion, pulling 2 nucleotides of DNA out of the RuvA tetramer per ATP hydrolyzed, thus driving DNA branch migration. The RuvB motors rotate together with the DNA substrate, which together with the progressing nucleotide cycle form the mechanistic basis for DNA recombination by continuous HJ branch migration. Branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves cruciform DNA.Homohexamer. Forms an RuvA(8)-RuvB(12)-Holliday junction (HJ) complex. HJ DNA is sandwiched between 2 RuvA tetramers; dsDNA enters through RuvA and exits via RuvB. An RuvB hexamer assembles on each DNA strand where it exits the tetramer. Each RuvB hexamer is contacted by two RuvA subunits (via domain III) on 2 adjacent RuvB subunits; this complex drives branch migration. In the full resolvosome a probable DNA-RuvA(4)-RuvB(12)-RuvC(2) complex forms which resolves the HJ.ATP + H2O = ADP + phosphate + H(+).Has 3 domains, the large (RuvB-L) and small ATPase (RuvB-S) domains and the C-terminal head (RuvB-H) domain. The head domain binds DNA, while the ATPase domains jointly bind ATP, ADP or are empty depending on the state of the subunit in the translocation cycle. During a single DNA translocation step the structure of each domain remains the same, but their relative positions change.",
	"func_sim": "Belongs to the RuvB family.The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. RuvB forms 2 homohexamers on either side of HJ DNA bound by 1 or 2 RuvA tetramers; 4 subunits per hexamer contact DNA at a time. Coordinated motions by a converter formed by DNA-disengaged RuvB subunits stimulates ATP hydrolysis and nucleotide exchange. Immobilization of the converter enables RuvB to convert the ATP-contained energy into a lever motion, pulling 2 nucleotides of DNA out of the RuvA tetramer per ATP hydrolyzed, thus driving DNA branch migration. The RuvB motors rotate together with the DNA substrate, which together with the progressing nucleotide cycle form the mechanistic basis for DNA recombination by continuous HJ branch migration. Branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves cruciform DNA."
	},
	{
	"uniprot_id": "Q8MBF7",
	"sequence": "MRINPTTSGSGVSTLEKQTLGRIVQIIGPVLDVAFPPGKMPNIYNALVVKGRDSAGQPINVTCEVQQLLGNNRVRAVAMSATDGLTRGMEVIDMGAAISVPVGGATLGRIFNVLGEPVDNLGPVDTSTTSPIHRSAPAFIQLDTKLAIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEENIAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKETLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDSFPEQAFYLVGNIDEATAKAMNLEMESNLKK",
	"function": [
	"Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits."
	],
	"catalytic activity": [
	"ATP + H2O + 4 H(+)(in) = ADP + phosphate + 5 H(+)(out)"
	],
	"subunit": [
	"F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has four main subunits: a(1), b(1), b'(1) and c(9-12)."
	],
	"similarity": [
	"Belongs to the ATPase alpha/beta chains family."
	],
	"prompt": "Belongs to the ATPase alpha/beta chains family.Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has four main subunits: a(1), b(1), b'(1) and c(9-12).ATP + H2O + 4 H(+)(in) = ADP + phosphate + 5 H(+)(out).",
	"func_sim": "Belongs to the ATPase alpha/beta chains family.Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits."
	},
	{
	"uniprot_id": "Q7ANU4",
	"sequence": "MLVPKRVKYRREFRGNMRGRAKGGTEVAFGEYGLQAVEASWITNRQIEAARIAMTRYMKRGGKVWIKIFPHKSYTSKPIGVRMGKGKGAPEGWVSPVKRGKIMFEIAGVPEDVAREALRLAAHKLPVKTKIVKREEIGGEANES",
	"function": [
	"Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs."
	],
	"subunit": [
	"Part of the 50S ribosomal subunit."
	],
	"similarity": [
	"Belongs to the universal ribosomal protein uL16 family."
	],
	"prompt": "Belongs to the universal ribosomal protein uL16 family.Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs.Part of the 50S ribosomal subunit.",
	"func_sim": "Belongs to the universal ribosomal protein uL16 family.Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs."
	},
	{
	"uniprot_id": "Q2YTB4",
	"sequence": "MTATWEKKEGNEGLLTVTVPAEKVNKALDQAFKKVVKQINVPGFRKGKVPRPIFEQRFGVEALYQDAIDILLPDAYGEAIDETDIKPVAQPEVSVTQIEKGKDFIFEATVTVEPEVKLGDYKGLEIEKQETELSDDELQEAIDHSLGHLAEMVVKEDGVVENGDTVNIDFSGSVDGEEFEGGQAEGYDLEIGSGSFIPGFEEQLEGMKVDEEKDVVVTFPEEYHAEELAGKEATFKTKVNEIKFKEVPELTDEIANELDAEANTVDEYKENLRKRLAEQKATDAENVEKEEAITKATDNTTIDIPEAMVNTELDRMVSEFAQRIQQQGLDLQTYFQISGQDESQLREQMKDDAEQRVKTNLTLTAIAEAEKIEATDEDIDKELEKMSKQFNISVEDIKNTLGNTDIIKNDVRIQKVIDLLRDNAKFVEGTKED",
	"function": [
	"Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase."
	],
	"catalytic activity": [
	"[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)"
	],
	"subcellular location": [
	"About half TF is bound to the ribosome near the polypeptide exit tunnel while the other half is free in the cytoplasm."
	],
	"domain": [
	"Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own."
	],
	"similarity": [
	"Belongs to the FKBP-type PPIase family. Tig subfamily."
	],
	"prompt": "Belongs to the FKBP-type PPIase family. Tig subfamily.Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0).Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.About half TF is bound to the ribosome near the polypeptide exit tunnel while the other half is free in the cytoplasm.",
	"func_sim": "Belongs to the FKBP-type PPIase family. Tig subfamily.Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase."
	},
	{
	"uniprot_id": "P51416",
	"sequence": "SRGISRYITKKNRHNTPSRLELRKFCPFCCKHMIHAEIKK",
	"similarity": [
	"Belongs to the bacterial ribosomal protein bL33 family."
	],
	"prompt": "Belongs to the bacterial ribosomal protein bL33 family.",
	"func_sim": "Belongs to the bacterial ribosomal protein bL33 family."
	},
	{
	"uniprot_id": "A1W1J3",
	"sequence": "MKVRPSVKKMCDKCKVVRRKGVVRIICENPKHKQRQG",
	"similarity": [
	"Belongs to the bacterial ribosomal protein bL36 family."
	],
	"prompt": "Belongs to the bacterial ribosomal protein bL36 family.",
	"func_sim": "Belongs to the bacterial ribosomal protein bL36 family."
	},
	{
	"uniprot_id": "Q5N1Q7",
	"sequence": "MPIGVPSVPYRLPGSSFERWIDIYNRLAMERIIFLGQEVTDGLANSIVAQLLYLDSEDSSKPIYLYINSPGGSVTAGMAIYDTMQYIKSPVITICLGLAASMGAFLLCAGSKGKRLALPHSRIMIHQPLGGTGRRQASDIEIEAKEILRIKKLLNQIMADRTGQPLEKIEKDTDRDYFMSAEEAREYGLIDQVIAERPV",
	"function": [
	"Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins."
	],
	"catalytic activity": [
	"Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-\|-NHMec, and Leu-Tyr-Leu-\|-Tyr-Trp, in which cleavage of the -Tyr-\|-Leu- and -Tyr-\|-Trp bonds also occurs)."
	],
	"subunit": [
	"Fourteen ClpP subunits assemble into 2 heptameric rings which stack back to back to give a disk-like structure with a central cavity, resembling the structure of eukaryotic proteasomes."
	],
	"similarity": [
	"Belongs to the peptidase S14 family."
	],
	"prompt": "Belongs to the peptidase S14 family.Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.Fourteen ClpP subunits assemble into 2 heptameric rings which stack back to back to give a disk-like structure with a central cavity, resembling the structure of eukaryotic proteasomes.Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-\|-NHMec, and Leu-Tyr-Leu-\|-Tyr-Trp, in which cleavage of the -Tyr-\|-Leu- and -Tyr-\|-Trp bonds also occurs).",
	"func_sim": "Belongs to the peptidase S14 family.Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins."
	},
	{
	"uniprot_id": "A0A385DTA3",
	"sequence": "MAGQQGIYCAPDNIVPNRDRVDVGCAPDGAMQLWVMEYEVTGIGKGCAMCKAINPQQAEMLLKSNGIYNGSSYLYKVTRIEQVIVPPCNGLMAEQVVTYKDVVS",
	"subunit": [
	"Homodimer; disulfide-linked (PubMed:37138077). Interacts with the major capsid protein (PubMed:37138077)."
	],
	"subcellular location": [
	"Localizes at the portal vertex. Present in 2 copies in the virion."
	],
	"prompt": "Homodimer; disulfide-linked (PubMed:37138077). Interacts with the major capsid protein (PubMed:37138077).Localizes at the portal vertex. Present in 2 copies in the virion.",
	"func_sim": ""
	},
	{
	"uniprot_id": "A1JS52",
	"sequence": "MSKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGSARAFDQIDNAPEEKARGITINTSHVEYDTPSRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYMIVFMNKCDMVDDEELLELVEMEVRELLSAYDFPGDDIPVVKGSALKALEGVKEWEDKIIELAGYLDTYIPEPERAVDKPFLLPIEDVFSISGRGTVVTGRVERGIVKVGEEVEIVGIKDTVKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREDIERGQVLAKPGSIKPHTTFESEVYILSKDEGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNINMVVTLIHPIAMDDGLRFAIREGGRTVGAGVVAKVIA",
	"function": [
	"GTP hydrolase that promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis."
	],
	"catalytic activity": [
	"GTP + H2O = GDP + phosphate + H(+)"
	],
	"subunit": [
	"Monomer."
	],
	"similarity": [
	"Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily."
	],
	"prompt": "Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily.GTP hydrolase that promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.Monomer.GTP + H2O = GDP + phosphate + H(+).",
	"func_sim": "Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily.GTP hydrolase that promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis."
	},
	{
	"uniprot_id": "B7V7F7",
	"sequence": "MSQVNMRDMLKAGVHFGHQTRYWNPKMGKFIFGARNKIHIINLEKTLPMFNEALTFVERLAAGKNKILFVGTKRSAGKIVREEAARCGMPYVDHRWLGGMLTNYKTIRQSIKRLRDLETQSQDGTFDKLTKKEALMRSRDLEKLERSLGGIKDMGGLPDALFVIDVDHERIAITEANKLGIPVIGVVDTNSSPEGVDYVIPGNDDAIRAVQLYLNSMAEAVIRGKQGAATSADEFVEEAPAESAEG",
	"similarity": [
	"Belongs to the universal ribosomal protein uS2 family."
	],
	"prompt": "Belongs to the universal ribosomal protein uS2 family.",
	"func_sim": "Belongs to the universal ribosomal protein uS2 family."
	},
	{
	"uniprot_id": "Q0SPB8",
	"sequence": "MICGIDEVGRGCIFGPILSAAVVFKKKPNFIKELDDSKKLTKEKREYLSSLILENSYYAFGEISNITIEKINIHNASLLAMQTAYENLKLNCNLVFIDGKFVPKISAKNVKAIIKGDSIIDEIKAASIIAKVKRDKLMDEYDKIYPLYLLKKNKGYPTKEHKNAIKKYGVLSLHRKNFKLI",
	"function": [
	"Endonuclease that specifically degrades the RNA of RNA-DNA hybrids."
	],
	"catalytic activity": [
	"Endonucleolytic cleavage to 5'-phosphomonoester."
	],
	"cofactor": [
	"Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding."
	],
	"similarity": [
	"Belongs to the RNase HII family."
	],
	"prompt": "Belongs to the RNase HII family.Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.Endonucleolytic cleavage to 5'-phosphomonoester.Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.",
	"func_sim": "Belongs to the RNase HII family.Endonuclease that specifically degrades the RNA of RNA-DNA hybrids."
	},
	{
	"uniprot_id": "B6J6M5",
	"sequence": "MNELPLHLLNMRSLTRDHIEKLIQRANYFLTQGMEKNSVFETLKGHVVVNLFFEPSTRTRNSFEIAAKRLGAMVLNPNLKISAISKGETLFDTIKTLEAMGVYFFIVRHSENETPEQIAKQLSSGVVINAGDGNHQHPSQALIDLMTIKQHKPHWNKLCVTIIGDIRHSRVANSLMDGLVTMGVPEIRLVGPSSLLPDKVGNDSIKKFTELKPSLLNSDVIVTLRLQKERHDNSVDIDAFRGSFRLTPEKLYSAKPDAIVMHPGPVNREVEINSDVADNQQSVILQQVRNGVAMRMAVLELFLLRDFRFF",
	"function": [
	"Catalyzes the condensation of carbamoyl phosphate and aspartate to form carbamoyl aspartate and inorganic phosphate, the committed step in the de novo pyrimidine nucleotide biosynthesis pathway."
	],
	"catalytic activity": [
	"carbamoyl phosphate + L-aspartate = N-carbamoyl-L-aspartate + phosphate + H(+)"
	],
	"pathway": [
	"Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3."
	],
	"subunit": [
	"Heterododecamer (2C3:3R2) of six catalytic PyrB chains organized as two trimers (C3), and six regulatory PyrI chains organized as three dimers (R2)."
	],
	"similarity": [
	"Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family."
	],
	"prompt": "Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family.Catalyzes the condensation of carbamoyl phosphate and aspartate to form carbamoyl aspartate and inorganic phosphate, the committed step in the de novo pyrimidine nucleotide biosynthesis pathway.Heterododecamer (2C3:3R2) of six catalytic PyrB chains organized as two trimers (C3), and six regulatory PyrI chains organized as three dimers (R2).carbamoyl phosphate + L-aspartate = N-carbamoyl-L-aspartate + phosphate + H(+).Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3.",
	"func_sim": "Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family.Catalyzes the condensation of carbamoyl phosphate and aspartate to form carbamoyl aspartate and inorganic phosphate, the committed step in the de novo pyrimidine nucleotide biosynthesis pathway."
	},
	{
	"uniprot_id": "A0L171",
	"sequence": "MNIRPLHDRVIVKRLEVESTSAGGIVLTGSAAEKSTRGEVLAVGNGRILENGTVRPLDVKVGDVVIFNEGYGVKKEKIDGQEVLILSEADLMAIVG",
	"function": [
	"Together with the chaperonin GroEL, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. GroES binds to the apical surface of the GroEL ring, thereby capping the opening of the GroEL channel."
	],
	"subunit": [
	"Heptamer of 7 subunits arranged in a ring. Interacts with the chaperonin GroEL."
	],
	"similarity": [
	"Belongs to the GroES chaperonin family."
	],
	"prompt": "Belongs to the GroES chaperonin family.Together with the chaperonin GroEL, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. GroES binds to the apical surface of the GroEL ring, thereby capping the opening of the GroEL channel.Heptamer of 7 subunits arranged in a ring. Interacts with the chaperonin GroEL.",
	"func_sim": "Belongs to the GroES chaperonin family.Together with the chaperonin GroEL, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. GroES binds to the apical surface of the GroEL ring, thereby capping the opening of the GroEL channel."
	},
	{
	"uniprot_id": "B1Y8G2",
	"sequence": "MATPVSSNAELFERAQRSIPGGVNSPVRAFRAVGGTPRFIARAQGAYMWDAEGKQYIDYIGSWGPMILGHGHPAVLAAVQKAATEGFSFGAPTEREVELAETILALVPSCEQIRLVSSGTEAAMSAIRLARGATGRSKLIKFEGCYHGHADALLVKAGSGLATFGNPTSAGVPPEVVQHTLVLTYNDIEQLEEAFKIHGPELACVMIEPIAGNMNFVRATVPFMKRIRELCTQHGALLVFDEVMCGFRVALGSAQSLYAQAIPGFAPDVSVFGKVIGGGMPLAAFGASRKIMSLLAPLGPVYQAGTLSGNPVATACGLATLREISQPGFFEALGARTRRLVDGLSAAAADAGVPFVGDCQGGMFGFFFPRNRGEGLPQNYATVMATDQARFNSFFHGLLDRGVYLAPALYEAGFVSAAHSDADIDATVAAARAALQP",
	"catalytic activity": [
	"(S)-4-amino-5-oxopentanoate = 5-aminolevulinate"
	],
	"pathway": [
	"Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2."
	],
	"subunit": [
	"Homodimer."
	],
	"similarity": [
	"Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily."
	],
	"prompt": "Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily.Homodimer.(S)-4-amino-5-oxopentanoate = 5-aminolevulinate.Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.",
	"func_sim": "Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily."
	},
	{
	"uniprot_id": "Q7NEF8",
	"sequence": "MGQKVHPIGLRLGIIRDHRSRWFAKAGEYPALLAEDHKIRAYIVKKLASGGIADVDIERKADQVEITIRTARPGVVVGRGGAGIDELKANLEKLIGRRQIRINVVEVQRVDAEAALIAEYIVGQLERRVAFRRAVRQAIQRAQRAGVQGIKVMVAGRLNGAEIARSEWTREGRIPLHTLRADIDYAYKIAQTTYGTLGVKVWIFRGEILPGAGGPAAAPEEVAAQPKPDQRPRRRKKIQYEERTDEQ",
	"function": [
	"Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation."
	],
	"subunit": [
	"Part of the 30S ribosomal subunit. Forms a tight complex with proteins S10 and S14."
	],
	"similarity": [
	"Belongs to the universal ribosomal protein uS3 family."
	],
	"prompt": "Belongs to the universal ribosomal protein uS3 family.Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation.Part of the 30S ribosomal subunit. Forms a tight complex with proteins S10 and S14.",
	"func_sim": "Belongs to the universal ribosomal protein uS3 family.Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation."
	},
	{
	"uniprot_id": "A9L2Q6",
	"sequence": "MPRVKRGVTARARHKKVLKLAKGYYGARSRTYRVAVQAVTKAGQYAYRDRRQKKRQFRQLWIARINAAARQNGLSYSRFINGLKKASIEIDRKILADIAVFDKVVFATLVEKAKEALN",
	"function": [
	"Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit."
	],
	"similarity": [
	"Belongs to the bacterial ribosomal protein bL20 family."
	],
	"prompt": "Belongs to the bacterial ribosomal protein bL20 family.Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit.",
	"func_sim": "Belongs to the bacterial ribosomal protein bL20 family.Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit."
	},
	{
	"uniprot_id": "C1CSP2",
	"sequence": "MAISKEKKNEIIAQYARHEGDTGSVEVQVAVLTWEINHLNEHIKQHKKDHATYRGLMKKIGRRRNLLAYLRKNDVNRYRELINSLGLRR",
	"function": [
	"One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it helps nucleate assembly of the platform of the 30S subunit by binding and bridging several RNA helices of the 16S rRNA.",
	"Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome."
	],
	"subunit": [
	"Part of the 30S ribosomal subunit. Forms a bridge to the 50S subunit in the 70S ribosome, contacting the 23S rRNA."
	],
	"similarity": [
	"Belongs to the universal ribosomal protein uS15 family."
	],
	"prompt": "Belongs to the universal ribosomal protein uS15 family.One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it helps nucleate assembly of the platform of the 30S subunit by binding and bridging several RNA helices of the 16S rRNA.Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome.Part of the 30S ribosomal subunit. Forms a bridge to the 50S subunit in the 70S ribosome, contacting the 23S rRNA.",
	"func_sim": "Belongs to the universal ribosomal protein uS15 family.One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it helps nucleate assembly of the platform of the 30S subunit by binding and bridging several RNA helices of the 16S rRNA.Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome."
	},
	{
	"uniprot_id": "A7H2Q2",
	"sequence": "MKIIARNKKALFDYSIIERFEAGIVLKGSEVVALRAGRANLKDSFVRIIKSEIFLLNSHISLLHTTHSFYKHEERGARKLLMHRKQIDKLLGKVSIEGYTIVALDLYFNTKNKVKATLALAKGKNLHDKRETLKKKQADLEARAAMKNYK",
	"function": [
	"Required for rescue of stalled ribosomes mediated by trans-translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to translate the ORF on the tmRNA; the nascent peptide is terminated with the 'tag peptide' encoded by the tmRNA and targeted for degradation. The ribosome is freed to recommence translation, which seems to be the essential function of trans-translation."
	],
	"subcellular location": [
	"The tmRNA-SmpB complex associates with stalled 70S ribosomes."
	],
	"similarity": [
	"Belongs to the SmpB family."
	],
	"prompt": "Belongs to the SmpB family.Required for rescue of stalled ribosomes mediated by trans-translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to translate the ORF on the tmRNA; the nascent peptide is terminated with the 'tag peptide' encoded by the tmRNA and targeted for degradation. The ribosome is freed to recommence translation, which seems to be the essential function of trans-translation.The tmRNA-SmpB complex associates with stalled 70S ribosomes.",
	"func_sim": "Belongs to the SmpB family.Required for rescue of stalled ribosomes mediated by trans-translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to translate the ORF on the tmRNA; the nascent peptide is terminated with the 'tag peptide' encoded by the tmRNA and targeted for degradation. The ribosome is freed to recommence translation, which seems to be the essential function of trans-translation."
	},
	{
	"uniprot_id": "B2RM15",
	"sequence": "MSKICQITGKKAMVGNNVSHSKRRTKRVFDVNLFRKKFYWVEQDCWVVLRISAAGLRLINKIGLDAAIKRAAEKGFLNA",
	"similarity": [
	"Belongs to the bacterial ribosomal protein bL28 family."
	],
	"prompt": "Belongs to the bacterial ribosomal protein bL28 family.",
	"func_sim": "Belongs to the bacterial ribosomal protein bL28 family."
	},
	{
	"uniprot_id": "A6U3I7",
	"sequence": "MNTLNLDIVTPNGSVYNRDNVELVVMQTTAGEIGVMSGHIPTVAALKTGFVKVKFHDGTEYIAVSDGFVEVRKDKVSIIVQTAETAREIDVERAKLAKARAESHLENDDDNTDIHRAERALERANNRLRVAELK",
	"function": [
	"Produces ATP from ADP in the presence of a proton gradient across the membrane."
	],
	"subunit": [
	"F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c."
	],
	"similarity": [
	"Belongs to the ATPase epsilon chain family."
	],
	"prompt": "Belongs to the ATPase epsilon chain family.Produces ATP from ADP in the presence of a proton gradient across the membrane.F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c.",
	"func_sim": "Belongs to the ATPase epsilon chain family.Produces ATP from ADP in the presence of a proton gradient across the membrane."
	},
	{
	"uniprot_id": "P04969",
	"sequence": "MAAARKSNTRKRRVKKNIESGIAHIRSTFNNTIVTITDTHGNAISWSSAGALGFRGSRKSTPFAAQMAAETAAKGSIEHGLKTLEVTVKGPGSGREAAIRALQAAGLEVTAIRDVTPVPHNGCRPPKRRRV",
	"function": [
	"Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome."
	],
	"subunit": [
	"Part of the 30S ribosomal subunit (PubMed:30126986). Interacts with proteins S7 and S18. Binds to IF-3 (By similarity). Interacts with VmlR (PubMed:30126986). Interacts with BrxC (PubMed:33722570)."
	],
	"similarity": [
	"Belongs to the universal ribosomal protein uS11 family."
	],
	"prompt": "Belongs to the universal ribosomal protein uS11 family.Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome.Part of the 30S ribosomal subunit (PubMed:30126986). Interacts with proteins S7 and S18. Binds to IF-3 (By similarity). Interacts with VmlR (PubMed:30126986). Interacts with BrxC (PubMed:33722570).",
	"func_sim": "Belongs to the universal ribosomal protein uS11 family.Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome."
	},
	{
	"uniprot_id": "A4QK10",
	"sequence": "MLGDGKEGTSTIPGFNQIQFEGFYRFIDQGLIEELSKFPKIEDIDHEIEFQLFVETYQLVEPLIKERDAVYESLTYSSELYVSAGLIWKTSRNMQEQRIFIGNIPLMNSLGISIVNGIYRIVINQILQSPGIYYQSELDHNGISVYTGTIISDWGGRLELEIDKKARIWARVSRKQKISILVLSSAMGSNLREILENVCYPEIFLSFLTDKEKKKIGSKENAILEFYQQFSCVGGDPIFSESLCKELQKKFFHQRCELGRIGRRNINWRLNLNIPQNNIFLLPRDILAAADHLIGMKFGMGTLDDMNHLKNKRIRSVADLLQDQLGLALARLENVVKGTIGGAIRHKLIPTPQNLVTSTPLTTTYESFFGLHPLSQVLDRTNPLTQIVHGRKLSYLGPGGLTGRTANFRIRDIHPSHYGRICPIDTSEGINVGLIGSLSIHARIGDWGSLESPFYELFEKSKEARIRMLFLSPSQDEYYMIAAGNSLALNRDIQEEQAVPARYRQEFLTIAWEEVNLRSIFPFQYFSIGASLIPFIEHNDANRALMSSNMQRQAVPLSRSEKCIVGTGLERQVALDSGVPAIAEHEGKILSTDTEKIILSGDGNTISIPLIMYQRSNKNTCMHQKPQVRRGKCIKKGQILADGAATVGGELALGKNILVAYMPWEGYNFEDAVLISECLVYGDIYTSFHIRKYEIQTHVTTQGPERITKEIPHLEGRLLRNLDKNGIVMLGSWVETGDILVGKLTPQVAKESSYAPEDRLLRAILGIQVSTSKETCLKLPIGGRGRVIDVRWVQKKGGTSYNPEIIRVYISQKREIKVGDKVAGRHGNKGIISKILPRQDMPYLQDGRPVDMVFNPLGVPSRMNVGQIFECSLGLAGSLLDRHYRIAPFDERYEQEASRKLVFSELYEASKQTANPWVFEPEYPGKSRIFDGRTGDPFEQPVIIGKPYILKLIHQVDDKIHGRSSGHYALVTQQPLRGRSKQGGQRVGEMEVWALEGFGVAHILQEMLTYKSDHIRARQEVLGTTIIGGTIPKPEDAPESFRLLVRELRSLALELNHFLVSEKNFQINRKEV",
	"function": [
	"DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates."
	],
	"catalytic activity": [
	"RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate"
	],
	"subunit": [
	"In plastids the minimal PEP RNA polymerase catalytic core is composed of four subunits: alpha, beta, beta', and beta''. When a (nuclear-encoded) sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription."
	],
	"similarity": [
	"Belongs to the RNA polymerase beta chain family."
	],
	"prompt": "Belongs to the RNA polymerase beta chain family.DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.In plastids the minimal PEP RNA polymerase catalytic core is composed of four subunits: alpha, beta, beta', and beta''. When a (nuclear-encoded) sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription.RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate.",
	"func_sim": "Belongs to the RNA polymerase beta chain family.DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates."
	},
	{
	"uniprot_id": "A5U0A5",
	"sequence": "MSRIGKQPIPVPAGVDVTIEGQSISVKGPKGTLGLTVAEPIKVARNDDGAIVVTRPDDERRNRSLHGLSRTLVSNLVTGVTQGYTTKMEIFGVGYRVQLKGSNLEFALGYSHPVVIEAPEGITFAVQAPTKFTVSGIDKQKVGQIAANIRRLRRPDPYKGKGVRYEGEQIRRKVGKTGK",
	"function": [
	"This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center."
	],
	"subunit": [
	"Part of the 50S ribosomal subunit."
	],
	"similarity": [
	"Belongs to the universal ribosomal protein uL6 family."
	],
	"prompt": "Belongs to the universal ribosomal protein uL6 family.This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center.Part of the 50S ribosomal subunit.",
	"func_sim": "Belongs to the universal ribosomal protein uL6 family.This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center."
	},
	{
	"uniprot_id": "Q7U6R7",
	"sequence": "MGRIVGIDLGTTNSVVAVLEAGRPHVIANAEGGRTTPSVVGYSKDQELLVGQLARRQLVLSPRNTFSNLKRFVGRDWEELEDSSLAVPYTVRANDRGQVRVPCPVTEREYAPEELVASIIRKLVDDASTYLGESVEAAVVTVPAYFNDAQRQATRDAGRLAGIAVERILNEPTAAALAYGFDRSAVRRVLVFDLGGGTFDVSLLRIANGVFDVKATNGDTQLGGNDFDQRIVDWIADAFQAEHGVDLRRDRQALQRLTEAAEKAKQELSGVLTTPISLPFIATGENGPLHVETNLDRSTFEGLCPDLLDRLLMPVQSALRDSGWAADDIDDVVLVGGATRMPMVQQLVRTLVPLDPCQSVNPDEVVAIGAAVQAGILTGELRDLLLNDVTPLSLGLETVGGLMRVLIPRNTPIPVRQSDVFSTSEPNQSSVEIHVWQGERQMASDNKSLGRFRLSGIPPAPRGVPQVQVAFDIDANGLLQVSATDRTTGRKQSVSIQGGSNLNEDEVTALLAEAEARADEDRRKRNQIERRNRAQTLVAQAERRLRDAALELGPYGAERQQRAVEMAMRDVQDCLAQDDLQELDLCLSGLEEALFGLNRRLSAERQSDGRPLQGLRNTLGSLKDELFADDWDDDPWAAPSGPPRGRSLNRRDRDPWDDDFYR",
	"function": [
	"Acts as a chaperone."
	],
	"induction": [
	"By stress conditions e.g. heat shock (By similarity)."
	],
	"similarity": [
	"Belongs to the heat shock protein 70 family."
	],
	"prompt": "Belongs to the heat shock protein 70 family.Acts as a chaperone.By stress conditions e.g. heat shock (By similarity).",
	"func_sim": "Belongs to the heat shock protein 70 family.Acts as a chaperone."
	},
	{
	"uniprot_id": "B1JDW8",
	"sequence": "MPRRRVAAKREILDDPKYGSQILAKFMNHVMESGKKAVAERIVYGALDTVKARKNSDPLEIFEKALDAIAPLVEVKSRRVGGATYQVPVEVRPSRRNALAMRWLVDYARKRGEKSMALRLAGELLDAAEGKGAAVKKREDVHRMAEANKAFSHYRF",
	"function": [
	"One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA."
	],
	"subunit": [
	"Part of the 30S ribosomal subunit. Contacts proteins S9 and S11."
	],
	"similarity": [
	"Belongs to the universal ribosomal protein uS7 family."
	],
	"prompt": "Belongs to the universal ribosomal protein uS7 family.One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA.Part of the 30S ribosomal subunit. Contacts proteins S9 and S11.",
	"func_sim": "Belongs to the universal ribosomal protein uS7 family.One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA."
	},
	{
	"uniprot_id": "Q5HIC8",
	"sequence": "MAREFSLEKTRNIGIMAHIDAGKTTTTERILYYTGRIHKIGETHEGASQMDWMEQEQDRGITITSAATTAAWEGHRVNIIDTPGHVDFTVEVERSLRVLDGAVTVLDAQSGVEPQTETVWRQATTYGVPRIVFVNKMDKLGANFEYSVSTLHDRLQANAAPIQLPIGAEDEFEAIIDLVEMKCFKYTNDLGTEIEEIEIPEDHLDRAEEARASLIEAVAETSDELMEKYLGDEEISVSELKEAIRQATTNVEFYPVLCGTAFKNKGVQLMLDAVIDYLPSPLDVKPIIGHRASNPEEEVIAKADDSAEFAALAFKVMTDPYVGKLTFFRVYSGTMTSGSYVKNSTKGKRERVGRLLQMHANSRQEIDTVYSGDIAAAVGLKDTGTGDTLCGEKNDIILESMEFPEPVIHLSVEPKSKADQDKMTQALVKLQEEDPTFHAHTDEETGQVIIGGMGELHLDILVDRMKKEFNVECNVGAPMVSYRETFKSSAQVQGKFSRQSGGRGQYGDVHIEFTPNETGAGFEFENAIVGGVVPREYIPSVEAGLKDAMENGVLAGYPLIDVKAKLYDGSYHDVDSSEMAFKIAASLALKEAAKKCDPVILEPMMKVTIEMPEEYMGDIMGDVTSRRGRVDGMEPRGNAQVVNAYVPLSEMFGYATSLRSNTQGRGTYTMYFDHYAEVPKSIAEDIIKKNKGE",
	"function": [
	"Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome."
	],
	"similarity": [
	"Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily."
	],
	"prompt": "Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily.Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.",
	"func_sim": "Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily.Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome."
	},
	{
	"uniprot_id": "P65886",
	"sequence": "MTSVVVVGTQWGDEGKGKITDFLSADAEVIARYQGGDNAGHTIVIDNKKFKLHLIPSGIFFKEKISVIGNGVVVNPKSLVKELAYLHGEGVTTDNLRISDRAHVILPYHIKLDQLQEDAKGDNKIGTTIKGIGPAYMDKAARVGIRIADLLDREVFAERLKINLAEKNRLFEKMYDSTPLEFDDIFEEYYEYGQQIKQYVTDTSVILNDALDAGKRVLFEGAQGVMLDIDQGTYPFVTSSNPVAGGVTIGSGVGPSKINKVVGVCKAYTSRVGDGPFPTELFDEVGDRIREIGKEYGTTTGRPRRVGWFDSVVMRHSRRVSGITNLSLNSIDVLSGLDTVKICVAYDLDGKRIDYYPASLEQLKRCKPIYEELPGWSEDITACRSLDDLPENARNYVRRVGELVGVRISTFSVGPGREQTNILESVWSNI",
	"function": [
	"Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP."
	],
	"catalytic activity": [
	"IMP + L-aspartate + GTP = N(6)-(1,2-dicarboxyethyl)-AMP + GDP + phosphate + 2 H(+)"
	],
	"cofactor": [
	"Binds 1 Mg(2+) ion per subunit."
	],
	"pathway": [
	"Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2."
	],
	"subunit": [
	"Homodimer."
	],
	"similarity": [
	"Belongs to the adenylosuccinate synthetase family."
	],
	"prompt": "Belongs to the adenylosuccinate synthetase family.Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.Homodimer.IMP + L-aspartate + GTP = N(6)-(1,2-dicarboxyethyl)-AMP + GDP + phosphate + 2 H(+).Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.Binds 1 Mg(2+) ion per subunit.",
	"func_sim": "Belongs to the adenylosuccinate synthetase family.Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP."
	},
	{
	"uniprot_id": "B1LWR0",
	"sequence": "MSRKLEALDRRKARVRRALRAAANGRPRLSVFRSSKQIYVQVIDDVAGKTLASASSIDKALKGELKTGADVAAATAVGKLVAERAKAAGVTKVIFDRSGYIYHGRVKAVAEAAREGGLEF",
	"function": [
	"This is one of the proteins that bind and probably mediate the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance."
	],
	"subunit": [
	"Part of the 50S ribosomal subunit; part of the 5S rRNA/L5/L18/L25 subcomplex. Contacts the 5S and 23S rRNAs."
	],
	"similarity": [
	"Belongs to the universal ribosomal protein uL18 family."
	],
	"prompt": "Belongs to the universal ribosomal protein uL18 family.This is one of the proteins that bind and probably mediate the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance.Part of the 50S ribosomal subunit; part of the 5S rRNA/L5/L18/L25 subcomplex. Contacts the 5S and 23S rRNAs.",
	"func_sim": "Belongs to the universal ribosomal protein uL18 family.This is one of the proteins that bind and probably mediate the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance."
	},
	{
	"uniprot_id": "A5U5T0",
	"sequence": "MTEFSSFSAPKGVPDYVPPDSAQFVAVRDGLLAAARQAGYSHIELPIFEDTALFARGVGESTDVVSKEMYTFADRGDRSVTLRPEGTAGVVRAVIEHGLDRGALPVKLCYAGPFFRYERPQAGRYRQLQQVGVEAIGVDDPALDAEVIAIADAGFRSLGLDGFRLEITSLGDESCRPQYRELLQEFLFGLDLDEDTRRRAGINPLRVLDDKRPELRAMTASAPVLLDHLSDVAKQHFDTVLAHLDALGVPYVINPRMVRGLDYYTKTAFEFVHDGLGAQSGIGGGGRYDGLMHQLGGQDLSGIGFGLGVDRTVLALRAEGKTAGDSARCDVFGVPLGEAAKLRLAVLAGRLRAAGVRVDLAYGDRGLKGAMRAAARSGARVALVAGDRDIEAGTVAVKDLTTGEQVSVSMDSVVAEVISRLAG",
	"catalytic activity": [
	"tRNA(His) + L-histidine + ATP = L-histidyl-tRNA(His) + AMP + diphosphate + H(+)"
	],
	"subunit": [
	"Homodimer."
	],
	"similarity": [
	"Belongs to the class-II aminoacyl-tRNA synthetase family."
	],
	"prompt": "Belongs to the class-II aminoacyl-tRNA synthetase family.Homodimer.tRNA(His) + L-histidine + ATP = L-histidyl-tRNA(His) + AMP + diphosphate + H(+).",
	"func_sim": "Belongs to the class-II aminoacyl-tRNA synthetase family."
	},
	{
	"uniprot_id": "A1U605",
	"sequence": "MTQRKYFGTDGIRGRVGDSPITPEFMLHLGWAAGQAFKRAGQRNSVLIGKDTRLSGYMFESALEAGLAAAGVDVKLLGPMPTPAIAYLTRTFRASAGIVISASHNPHHDNGIKFFSSAGTKLDDALEAEIERWLDQPIEVCEPEELGKASRVDDAPGRYVEFCKSTVPNEFTLDGMHLVLDCAHGATYHVAPKVFRELGAKVTVIGAEPDGLNINLNVGSTHLGALKQAVAEKKADLGIAFDGDGDRVLMVDRDGSEVDGDELLYILASQRQAEGRLNGGVVGTLMTNLGVELALREIGVEFERAKVGDRYVMERLLANNWLIGGEGSGHMVIRDCTTTGDGIVSALQVLLAVRKSGKTMGELRAGMSKLPQKMINVRVAERFDPLGRADIVEAMARAEASLGDAGRILLRASGTEPLIRVMAEGQSADDITRVVEELALVVERSTP",
	"function": [
	"Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate."
	],
	"catalytic activity": [
	"alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate"
	],
	"cofactor": [
	"Binds 1 Mg(2+) ion per subunit."
	],
	"PTM": [
	"Activated by phosphorylation."
	],
	"similarity": [
	"Belongs to the phosphohexose mutase family."
	],
	"prompt": "Belongs to the phosphohexose mutase family.Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate.alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate.Binds 1 Mg(2+) ion per subunit.Activated by phosphorylation.",
	"func_sim": "Belongs to the phosphohexose mutase family.Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate."
	},
	{
	"uniprot_id": "Q7V2M3",
	"sequence": "MPKQLSFSNESREALEKGINTVANAVKVTIGPKAKNVVIERKFGSPDIVRDGSTVAKEINLDNPISNLGAKLIEQVASKTKESAGDGTTTATILTQIMVQEGLKNIAAGASPIELKKGMEKGLNFVLEKLRSKSIKINGSDIKKVATVSAGGDEDIGSIISKAMDIVTSDGVITVEESQSLETELDITEGMSFDRGYSSPYFVTDQERQICELENPKILITDQKISTLTNLVPILEEVQKSASPFLILAEDIEGEALTTLVLNKNSGVLNVSAVRAPSFGERRKAALEDIAILTGAKLISEDQSMKLEEVTLNDLGKAKKITISKDKTTIVAFDDTKDLVQERVEKLKREVEITESEYDKDKINERIAKLAGGVALIKVGAATETEMKYKKLRIEDSLNATKAAIEEGVVSGGGQTLIEISNELSNSRKEISDDLTTGIDIITNALLEPTKQIAKNAGFNGDVVIADIKRLGKGFNANNGEYENLNESGILDPTKVIRLALQDSVSIAAMIITTEVAVADIPEPEAAPGGPGADPMGGMGGMGGMGGMGGMGMPGMGGMGMPGMGGMGMPGMGGMGMPGMM",
	"function": [
	"Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding."
	],
	"catalytic activity": [
	"ATP + H2O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide."
	],
	"subunit": [
	"Forms a cylinder of 14 subunits composed of two heptameric rings stacked back-to-back. Interacts with the co-chaperonin GroES."
	],
	"similarity": [
	"Belongs to the chaperonin (HSP60) family."
	],
	"prompt": "Belongs to the chaperonin (HSP60) family.Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.Forms a cylinder of 14 subunits composed of two heptameric rings stacked back-to-back. Interacts with the co-chaperonin GroES.ATP + H2O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide.",
	"func_sim": "Belongs to the chaperonin (HSP60) family.Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding."
	},
	{
	"uniprot_id": "Q6G795",
	"sequence": "MARIAGVDIPREKRVVISLTYIYGIGTSTAQKILEEANVSADTRVKDLTDDELGRIREVVDGYKVEGDLRRETNLNIKRLMEISSYRGIRHRRGLPVRGQKTKNNARTRKGPVKTVANKKK",
	"function": [
	"Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites."
	],
	"subunit": [
	"Part of the 30S ribosomal subunit. Forms a loose heterodimer with protein S19. Forms two bridges to the 50S subunit in the 70S ribosome."
	],
	"similarity": [
	"Belongs to the universal ribosomal protein uS13 family."
	],
	"prompt": "Belongs to the universal ribosomal protein uS13 family.Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites.Part of the 30S ribosomal subunit. Forms a loose heterodimer with protein S19. Forms two bridges to the 50S subunit in the 70S ribosome.",
	"func_sim": "Belongs to the universal ribosomal protein uS13 family.Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites."
	},
	{
	"uniprot_id": "B6JKD3",
	"sequence": "MAVPDRRVSKTRAAKRRTHYSVKLAKPVKAKDGTWKLPHHINKFTKEY",
	"similarity": [
	"Belongs to the bacterial ribosomal protein bL32 family."
	],
	"prompt": "Belongs to the bacterial ribosomal protein bL32 family.",
	"func_sim": "Belongs to the bacterial ribosomal protein bL32 family."
	},
	{
	"uniprot_id": "Q2JUJ5",
	"sequence": "MMQTSRTLHNLGSKAASSAAPYQTECVESHQEANGVHYGKFALGPLERGQGITVGNALRRVLLSNLEGTAVTAVRIAGVTHEFSTVPGVREDVMEILLNMKELVLRSNAPDTQVGRLVAQGPGEVTAEKLQLPSEVEVINPRHHIATLAEGAILEMEFMIGRGRGYRAVDYSDSKSMAIDFLQIDSVFMPVRKVNYTVEAARVGQSLEKDRLILEIWTNGSLTPQEALSQAARILVGLFSPLQEVSFDTPPEPRQAEDNQKNQIPIEELQLSVRAYNCLKRAQINTVADLLVYTEEDLLEIKNFGQKSAEEVVQALKNRLGLTLPRERSKT",
	"function": [
	"DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates."
	],
	"catalytic activity": [
	"RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate"
	],
	"subunit": [
	"In cyanobacteria the RNAP catalytic core is composed of 2 alpha, 1 beta, 1 beta', 1 gamma and 1 omega subunit. When a sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription."
	],
	"domain": [
	"The N-terminal domain is essential for RNAP assembly and basal transcription, whereas the C-terminal domain is involved in interaction with transcriptional regulators and with upstream promoter elements."
	],
	"similarity": [
	"Belongs to the RNA polymerase alpha chain family."
	],
	"prompt": "Belongs to the RNA polymerase alpha chain family.DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.In cyanobacteria the RNAP catalytic core is composed of 2 alpha, 1 beta, 1 beta', 1 gamma and 1 omega subunit. When a sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription.RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate.The N-terminal domain is essential for RNAP assembly and basal transcription, whereas the C-terminal domain is involved in interaction with transcriptional regulators and with upstream promoter elements.",
	"func_sim": "Belongs to the RNA polymerase alpha chain family.DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates."
	},
	{
	"uniprot_id": "B1Z761",
	"sequence": "MPKRVLQGVVVSDKTDKTIVVKVERRFTHPVMKKTVRRSKNYHAHDEANTAKVGQTVFIEESRPYSKTKTWKLVEDQAAAAEAAGTAA",
	"function": [
	"One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA."
	],
	"subunit": [
	"Part of the 30S ribosomal subunit."
	],
	"similarity": [
	"Belongs to the universal ribosomal protein uS17 family."
	],
	"prompt": "Belongs to the universal ribosomal protein uS17 family.One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.Part of the 30S ribosomal subunit.",
	"func_sim": "Belongs to the universal ribosomal protein uS17 family.One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA."
	},
	{
	"uniprot_id": "Q8KD88",
	"sequence": "MVKIRLKRAGRKKMPFYQIVAADGRAPRDGKFLEVLGHYNPTAKPHTVTIEKDRVAYWLNVGAQPTDTVHSLIRGTGLLHEMNLKRRGLSESDIAAQMEAWRQKEAERRQKRLNAKLRRRQAKKAAEAAGSAEG",
	"similarity": [
	"Belongs to the bacterial ribosomal protein bS16 family."
	],
	"prompt": "Belongs to the bacterial ribosomal protein bS16 family.",
	"func_sim": "Belongs to the bacterial ribosomal protein bS16 family."
	},
	{
	"uniprot_id": "A6QEI0",
	"sequence": "MSDRIRVRYAPSPTGYLHIGNARTALFNYLYAKHYNGDFVIRIEDTDKKRNLEDGETSQFDNLKWLGLDWDESVDKDNGYGPYRQSERQHIYQPLIDQLLAEDKAYKCYMTEEELEAEREAQIARGEMPRYGGQHAHLTEEQRQQFEAEGRQPSIRFRVPQNQTYSFDDMVKGNISFDSNGIGDWVIVKKDGIPTYNFAVAIDDHYMQISDVIRGDDHISNTPKQIMIYEAFGWEPPRFGHMSLIVNEERKKLSKRDGQILQFIEQYRDLGYLPEALFNFIALLGWSPEGEEEIFSKEEFIKIFDEKRLSKSPAFFDKQKLAWVNNQYMKQKDTETVFQLALPHLIKANLIPEVPSEEDLSWGRKLIALYQKEMSYAGEIVPLSEMFFKEMPALGEEEQQVINGEQVPELMTHLFSKLEALEPFESAEIKKTIKEVQKETGIKGKQLFMPIRVAVTGQMHGPELPNTIEVLGKEKVLNRLKQYK",
	"function": [
	"Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu)."
	],
	"catalytic activity": [
	"tRNA(Glu) + L-glutamate + ATP = L-glutamyl-tRNA(Glu) + AMP + diphosphate"
	],
	"subunit": [
	"Monomer."
	],
	"similarity": [
	"Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily."
	],
	"prompt": "Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily.Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).Monomer.tRNA(Glu) + L-glutamate + ATP = L-glutamyl-tRNA(Glu) + AMP + diphosphate.",
	"func_sim": "Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily.Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu)."
	},
	{
	"uniprot_id": "Q8E2D0",
	"sequence": "MANVKLFDQTGKEVSSVELNEAIFGIEPNESVVFDVVISQRASLRQGTHAVKNRSAVSGGGRKPWRQKGTGRARQGSIRSPQWRGGGVVFGPTPRSYGYKLPQKVRRLALKSVYSAKVAEDKFVAVENLSFAAPKTAEFASVLSALSIDSKVLVILEEGNEFAALSARNLPNVTVATATTASVLDIVNADKLLVTKEAISTIEGVLA",
	"function": [
	"One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.",
	"Forms part of the polypeptide exit tunnel."
	],
	"subunit": [
	"Part of the 50S ribosomal subunit."
	],
	"similarity": [
	"Belongs to the universal ribosomal protein uL4 family."
	],
	"prompt": "Belongs to the universal ribosomal protein uL4 family.One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.Forms part of the polypeptide exit tunnel.Part of the 50S ribosomal subunit.",
	"func_sim": "Belongs to the universal ribosomal protein uL4 family.One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.Forms part of the polypeptide exit tunnel."
	},
	{
	"uniprot_id": "C6DDJ5",
	"sequence": "MSKIVKVIGREIIDSRGNPTVEAEVHLEGGFVGLAAAPSGASTGSREALELRDGDKSRFLGKGVTKAVAAVNGPIAQAVVGKDAKDQANIDKIMIDLDGTDNKSKFGANAILAVSLAAAKAAAASKGLPLYAHIAELNGTPGKYSMPLPMMNIINGGEHADNNVDIQEFMIQPVGAKTLKEAIRMGSEVFHTLAKVLKSKGMGTAVGDEGGYAPNLGSNAEALAVIAEAVKAAGYELGKDITLAMDCAASEFYKDGKYVLAGEGNKAFTSEEFTHFLEDLTKQYPIVSIEDGLDESDWAGFAYQTKVLGDKIQLVGDDLFVTNTKILKEGIEKGIANSILIKFNQIGSLTETLAAIKMAKDAGYTAVISHRSGETEDATIADLAVGTAAGQIKTGSMSRSDRVAKYNQLIRIEEALGDSAPFNGLKEVKGQ",
	"function": [
	"Catalyzes the reversible conversion of 2-phosphoglycerate (2-PG) into phosphoenolpyruvate (PEP). It is essential for the degradation of carbohydrates via glycolysis."
	],
	"catalytic activity": [
	"(2R)-2-phosphoglycerate = phosphoenolpyruvate + H2O"
	],
	"cofactor": [
	"Binds a second Mg(2+) ion via substrate during catalysis."
	],
	"pathway": [
	"Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5."
	],
	"subunit": [
	"Component of the RNA degradosome, a multiprotein complex involved in RNA processing and mRNA degradation."
	],
	"subcellular location": [
	"Fractions of enolase are present in both the cytoplasm and on the cell surface."
	],
	"similarity": [
	"Belongs to the enolase family."
	],
	"prompt": "Belongs to the enolase family.Catalyzes the reversible conversion of 2-phosphoglycerate (2-PG) into phosphoenolpyruvate (PEP). It is essential for the degradation of carbohydrates via glycolysis.Component of the RNA degradosome, a multiprotein complex involved in RNA processing and mRNA degradation.(2R)-2-phosphoglycerate = phosphoenolpyruvate + H2O.Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5.Binds a second Mg(2+) ion via substrate during catalysis.Fractions of enolase are present in both the cytoplasm and on the cell surface.",
	"func_sim": "Belongs to the enolase family.Catalyzes the reversible conversion of 2-phosphoglycerate (2-PG) into phosphoenolpyruvate (PEP). It is essential for the degradation of carbohydrates via glycolysis."
	},
	{
	"uniprot_id": "Q67N08",
	"sequence": "MRYLTAGESHGRALVTIVEGLPAGVPVDLAAIDRDLARRQSGYGRGGRMKIEQDRVQVLSGIRHGKTLGSPVALLVENRDWLNWTEVMSPAPLEAYTDPRAAQKVRTRPRPGHADLAGALKYDHADLRNVLERASARETAARVAAGSLAKQYLAPFGIRVAGYVRSIGPVEAQPPAGLDLDGIVARAEASPVRCPDPAASARMVEEIDAAKRDGDSLGGVVEVVAAGLPPGLGSHVHWDRKLDGALGAALLSIQAAKGVEIGDGFLGARRRGSEVHDEIGWSPDRGYFRYTNRAGGLEGGMTNGMDLVVRVAFKPIATLYKPLRSVEIDTHVEAAAGIERSDVCAVPAAAVIAECVTAFELARFVAEKFGGDSLEEALRNFRGYLEQIARR",
	"function": [
	"Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system."
	],
	"catalytic activity": [
	"5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate"
	],
	"cofactor": [
	"Reduced FMN (FMNH(2))."
	],
	"pathway": [
	"Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7."
	],
	"subunit": [
	"Homotetramer."
	],
	"similarity": [
	"Belongs to the chorismate synthase family."
	],
	"prompt": "Belongs to the chorismate synthase family.Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.Homotetramer.5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate.Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.Reduced FMN (FMNH(2)).",
	"func_sim": "Belongs to the chorismate synthase family.Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system."
	},
	{
	"uniprot_id": "Q957A2",
	"sequence": "MTNIRKSHPXMKIIXXSFIDLPAPSNISSWWNFGSLLGICLALQILTGLFLAMHYTSDTATAFNSVTHICRDVNYGWVLRYLHANGASMFFICLYLHVGRGLYYGSYMYTETWNVGVILLFAVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTNLVKWIWGGFSVDKATLTRFFAFHFLLPFIISAMVMVHLLFLHETGSNNPTGIPSNMDMIPFHPYYTIKDILGLLLMITVLLMLVLFSPDMLGDPDNYTPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALVLSILILIIIPLLHTSKQRSMAFRPLSQCLFWLLVADLFTXTWIGGQPVEHPYIIIGQLASILYFSIIIILMPXISFAENHLLKW",
	"function": [
	"Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis."
	],
	"cofactor": [
	"Binds 2 heme b groups non-covalently."
	],
	"subunit": [
	"The cytochrome bc1 complex contains 11 subunits: 3 respiratory subunits (MT-CYB, CYC1 and UQCRFS1), 2 core proteins (UQCRC1 and UQCRC2) and 6 low-molecular weight proteins (UQCRH/QCR6, UQCRB/QCR7, UQCRQ/QCR8, UQCR10/QCR9, UQCR11/QCR10 and a cleavage product of UQCRFS1). This cytochrome bc1 complex then forms a dimer."
	],
	"miscellaneous": [
	"Heme 1 (or BL or b562) is low-potential and absorbs at about 562 nm, and heme 2 (or BH or b566) is high-potential and absorbs at about 566 nm."
	],
	"similarity": [
	"Belongs to the cytochrome b family."
	],
	"caution": [
	"The full-length protein contains only eight transmembrane helices, not nine as predicted by bioinformatics tools."
	],
	"prompt": "Belongs to the cytochrome b family.Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.The cytochrome bc1 complex contains 11 subunits: 3 respiratory subunits (MT-CYB, CYC1 and UQCRFS1), 2 core proteins (UQCRC1 and UQCRC2) and 6 low-molecular weight proteins (UQCRH/QCR6, UQCRB/QCR7, UQCRQ/QCR8, UQCR10/QCR9, UQCR11/QCR10 and a cleavage product of UQCRFS1). This cytochrome bc1 complex then forms a dimer.Binds 2 heme b groups non-covalently.Heme 1 (or BL or b562) is low-potential and absorbs at about 562 nm, and heme 2 (or BH or b566) is high-potential and absorbs at about 566 nm.The full-length protein contains only eight transmembrane helices, not nine as predicted by bioinformatics tools.",
	"func_sim": "Belongs to the cytochrome b family.Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis."
	}
	]