Datasets:
habdine
/
Prot2Text-Data

Dataset card Data Studio Files
xet
Community
1
accession
stringlengths
6
10
name
stringlengths
6
11
Full Name
stringlengths
1
147
⌀
taxon
stringlengths
3
46
⌀
sequence
stringlengths
16
2.75k
function
stringlengths
6
5.51k
AlphaFoldDB
stringlengths
6
10
Q9I900
PA2AD_NAJSP
Phosphatidylcholine 2-acylhydrolase
Naja
MNPAHLLILAAVCVSPLGASSNRPMPLNLYQFKNMIQCTVPNRSWWDFADYGCYCGRGGSGTPVDDLDRCCQVHDNCYGEAEKISRCWPYFKTYSYECSQGTLTCKGGNDACAAAVCDCDRLAAICFAGAPYNDNNYNIDLKARCQ
PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
Q9I900
Q820N6
UVRC_NITEU
Excinuclease ABC subunit C
Nitrosomonas
MPDAHFDGKAFVLTLPAQPGVYRMLNAAGDVIYVGKAIDLRKRVSSYFQKSGLSPRIQLMVSQIAGIETTVTRSEAEALLLENNLIKSLAPRYNILFRDDKSYPYLLLTRHIFPRLAFYRGALDDRHQYFGPFPNAGVVKSSIQLLQKVFRLRTCENSVFDHRTRPCLLYQIKRCSGPCVGLITPEAYQQDVKSAAMFLQGKQDEVLKTIEQKMFTASDQQDYEQAAQLRDQMQALRKIQEKQFVDSGKALDADVIACAIEPDSHAVAVNLVMIRSGRHLGDKTFFPQNVYEADISTVLEAFVTQHYLNRSVPPLIILGQKIRVTLLQKLLSDQAGHKITLTTNPIGERRKWLDMAAENAQLALQQMLIQQASQEDRLQALQEALNLPGLARIECFDISHTMGEATIASCVVYDRFAMRNGEYRRYNITGIVPGDDYAAMRDVLQRRYAKLAMEEGKLPDLILIDGGKGQIRVASEVMIELGLNDIPLVGVAKGETRKPGLEQLILPWQEEALHLPDDHPALHLIQQIRDEAHRFAIQGHRAKRAKTRKISTLEQISGIGTKRRQSLLTRFGGLKGVKNASIEELQQTEGISRSLAEKIYRELR
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision.
Q820N6
Q1C6R0
NAGK_YERPA
GlcNAc kinase
Yersinia
MYYGFDMGGTKIELGVFDENLQRIWHKRVPTPREDYPQLLQILRDLTEEADTYCGVQGSVGIGIPGLPNADDGTVFTANVPSAMGQPLQADLSRLIQREVRIDNDANCFALSEAWDPEFRTYPTVLGLILGTGVGGGLIVNGSIVSGRNHITGEFGHFRLPVDALDILGADIPRVPCGCGHRGCIENYISGRGFEWMYSHFYQHTLPATDIIAHYAAGEPKAVAHVERFMDVLAVCLGNLLTMLGSPFGRGGWGVV
Catalyzes the phosphorylation of N-acetyl-D-glucosamine (GlcNAc) derived from cell-wall degradation, yielding GlcNAc-6-P.
Q1C6R0
B7J8G6
RLME_ACIF2
rRNA (uridine-2'-O-)-methyltransferase
Acidithiobacillus
MARSKSSEKWLKEHFKDPFVQRAMKEGYRSRASYKLLEIQQKDHLIRPGMRVLDVGAAPGGWTQVAAPLIGRKGRLVAVDRLAMDPVADATVICGDVYDDAILAACQEALPGGADLIMSDMAPNMSGIASVDQARAIDLAELALDMAHRWLVPGGALLIKVFMGSGAEELRRALRRDFKKIVVRKPEASRARSTEQYWLALDFQGVAQERLDNGGASSL
Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit.
B7J8G6
Q06655
LALBA_NOTEU
Lactose synthase B protein
Notamacropus
MMSLLSLLLLGIALPATQAIDYRKCQASQILKEHGMDKVIPLPELVCTMFHISGLSTQAEVNNHSNKEYGIFQISNNGWCAEKQEDVANSVCGILCSKFLDDDITDDIECAKKILQLPEGLGYWKAHETFCIEDLDQWRC
Regulatory subunit of lactose synthase, changes the substrate specificity of galactosyltransferase in the mammary gland making glucose a good acceptor substrate for this enzyme. This enables LS to synthesize lactose, the major carbohydrate component of milk. In other tissues, galactosyltransferase transfers galactose onto the N-acetylglucosamine of the oligosaccharide chains in glycoproteins.
Q06655
Q6FKS5
HAT1_CANGA
Histone acetyltransferase type B catalytic subunit
Nakaseomyces/Candida clade
MSIDDFKPEKWTISSNEALKLSLVSEDNAIQFSPTFTYPIFGTEEQIFGYKDLVIHLAFDAITFKPFLNVKFSSKFEGSEEELVNIKEKLLEYLPIDDTIYKDEEKWIDSFKKEQESIEAYKNDQNIDEYKIDNADFEIYKVNLQDPKMKRFHRRIQIFSLLFIEAASYIDEDDPKWEIFIVQTKKDKKFVGYATAYNYWYYPGANNFDSESKYRYRGKISQFLILPPYQGRGHGSHLYNSIVKNWRNDSSILEIVVEDPNESFDDLRDVNDLEMLYKDGFFNKLPQERPIPNAWIESTRLKYKIEKRQFSRLLEMILLSTGSNNFEYQVKQRLLIKNKDGLEGMEVSDIKDALNKSFESLREDYDRILGKCQFSNDADGPSKKKIKT
Catalytic component of the histone acetylase B (HAT-B) complex. Acetylates 'Lys-12' of histone H4 which is required for telomeric silencing. Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG. Involved in DNA double-strand break repair.
Q6FKS5
C4KZN4
RL5_EXISA
50S ribosomal protein L5
unclassified Exiguobacterium
MNRLQEKYKSDIVKAMMDKFNYDSVMQVPKIEKIVINMGVGDAVSNSKALDMAVEELTILSGQKPLVTKAKKSIAGFKLREGMPIGAKVTLRGERMYDFLDKLVTVSLPRVRDFRGVSKKAFDGRGNYTLGVKEQLIFPEIDYDKVSKVRGMDIVVVTTANTDEEARELLTLLGMPFQK
This is 1 of the proteins that binds and probably mediates 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.
C4KZN4
B0S8X7
ACSA_LEPBA
Acyl-activating enzyme
Leptospira
MPKERIVAPSKEFAKLANVSLKEYKSKYKESIEKPEKFWAEQAKRLTWFKKWTKVLRHDFAKAKVEWFVGGKLNVSYNCLDRHLDSPLKNKAALIWEGDNPDESKVLTYHDLHREVNHFANVLKKFKVKKGDRVLIYLPMVPELAIATLACTRIGAVHSVVFGGFSPEALLGRIEDCKPTLVITADGGYRGGKPIELKKNVDAALAETKFKVNDVIVVKRTGDEGNLNWKEGRDHWYHYLMKDPEVKKECPAVPMESEDPLFILYTSGSTGKPKGVLHTTAGYLLGANLTFATIFDYKDTDTYWCTADIGWITGHSYILYGPLSNGATSLMFEGVPSYPDMGRFWDVIDKYKVTVFYTAPTAIRALMREGLEHIKKRSLASLRLLGSVGEPINPEAWEWYYANIGKSKCPIVDTWWQTETGSIMISGIPGAIPQKPGSASWPFYGIQPVLVDNEGVELKGKGEISGNLCIAKPWPSMMRGVYGDPKRFFDTYFSQFKGYYFTGDGANRDKEGYFRITGRVDDVLNVSGHRIGSAEVESALVEHKSVAEAAVVGFPHDIKGQGIYAYVTVKQGVVTNDLLKKELIAMVEKVIGKIARPDVIHWAPGLPKTRSGKIMRRILRKIANNEFDTLGDISTLADPSVVQSLIDDKKKYHS
Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA.
B0S8X7
P39825
PROF_SCHPO
Profilin
Schizosaccharomyces
MSWQAYVDTSLLGTGKIDRAAIVSRAGDSVWAASAGFNLSPQEIQGLAAGFQDPPSMFGTGIILAGQKYITIRAEGRSIYGKLQKEGIICVATKLCILVSHYPETTLPGEAAKITEALADYLVGVGY
Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG. In S.pombe, it is essential for cytokinesis.
P39825
Q4QMR6
COAD_HAEI8
Pantetheine-phosphate adenylyltransferase
Haemophilus
MTSVIYPGTFDPITNGHLDIIERSAVIFPRVLVAVANSPSKKPLFSLEERVELVRQSVAHLSNVEVFGFSDLLANVIKQHNISAIIRGVRTTTDFEYELQLAALNRLLTKGVDSLFFPPAEKWAFVSSTIVREIYLHGGDVAELVPEPVFNALKAR
Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Q4QMR6
P02507
CRYAA_PELLE
Alpha-crystallin A chain
Pelophylax
MDITIQHPWFKRALGPFYPNRLFDQVFGEGMFDYDLFPFLSSTISPYYRQSFFRGFLDSGISEVRSDRDRVKHFSPEDLTVKILDDFVEIHGKHSERQDDHGYISREFHRRYRLPSNLNESSISCSLSADGILTFSGPKLMSSLDSSHGERPIPVSREEKPTSAPSS
Contributes to the transparency and refractive index of the lens. May act as a chaperone, preventing aggregation of various proteins under a wide range of stress conditions.
P02507
A5VB97
LEXA_RHIWR
LexA repressor
Rhizorhabdus
MLTRKQHELLCFINDRLLQTGVSPSFEEMKEALDLKSKSGVHRLISALEERNFIRRLPNRARALEVLRMPETATAKPTAAASGKAKAAAPAVPQAANENVLEIPLHGRIAAGLPIEALEGQSSLSVPAALLGPGEHYALEVAGDSMVEAGILDGDYALIRRAETARDGEIVVALIADAEATLKYFRREGAMIRLDPANRAYDPQRYKPDQVRIQGKLAGLLRRY
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
A5VB97
B8F877
NAGB_GLAP5
Glucosamine-6-phosphate isomerase
Glaesserella
MRLVPLDCAEQVSRWAARYIVDKINAFQPTAEKPFVLGLPTGGTPLQTYKELIKLYQAGEVSFKHVVTFNMDEYVGLPPEHKESYHYFMFHNFFNHIDIPVENVNILNGMAEDVDAECERYEAKIRSYGKIHLFMGGVGVDGHIAFNEPASSLSSRTRIKTLTEDTLIANSRFFDNDVNKVPKFALTVGVGTLMDAEEVLILVTGYNKALALQACVEGAVNHLWTISALQLHRRAVVVCDEPATQELKVKTVKYFKQLEQNIAR
Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion.
B8F877
O08970
TUFT1_MOUSE
Tuftelin
Mus
MNGTRNWCTLVDVHPESQTAGSVDILRLTLQSELTGDELEHIAQKAGRKTYAMMPGHSSGHSLASELVESHDGHEEIIKVYLKGRSGDKMTHEKNIDQLKSEVQYIQEARNCLQKLREDISSKLDRSPGDPLRQQEIQVVLEKPNGFSQSPMTLYSSPPEVDPSMSEDVESLKKTVQELLVKLREAERRHQSDRVAFEVTLSRYQREAEQSNVALQREEDRVEQKAAEIEELQRRLLGMEAEHQALLVKVREGEMALEELRIKNADCQTEREKSAALEKEVAGFREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKDATIQELKEKIAYLEAENLEMHDRMEHLIEKQVSHGNFSTQARAKTENLGSVRISKPPSPKPMPLIRVVET
Involved in the mineralization and structural organization of enamel.
O08970
A0PM42
EFTU_MYCUA
Elongation factor Tu
Mycobacterium
MAKAKFQRTKPHVNIGTIGHVDHGKTTLTAAITKVLHDKYPELNESRAFDQIDNAPEERQRGITINISHVEYQTEKRHYAHVDAPGHADYIKNMITGAAQMDGAILVVAATDGPMPQTREHVLLARQVGVPYILVALNKSDAVDDEELLELVEMEVRELLAAQEFDEDAPVVRVSALKALEGDPKWVESVEQLMDAVDESIPDPVRETDRPFLMPVEDVFTITGRGTVVTGRVERGIINVNEEVEIVGIRPTSTKTTVTGVEMFRKLLDQGQAGDNVGLLLRGIKREDVERGQVVVKPGTTTPHTEFEGQVYILSKDEGGRHTPFFNNYRPQFYFRTTDVTGVVTLPEGTEMVMPGDNTNISVKLIQPVAMDDGLRFAIREGGRTVGAGRVVKIIK
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
A0PM42
B2J0A6
RSMA_NOSP7
S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase
Nostoc
MIRPRKVFAQHWLKSEKALDAIIKAAECTESDRSPKGDCILEIGPGTGILTRRLLPLVQSLIAVEIDRDLCQLLSKQLGKTENFLLLQGDFLTLDLPSYLVAFPNFQKPNKVVANIPYNITGPIIEKLLGTIANPNPEPFDSIVLLVQKEVAERLYAKPGSKTFGALSVRVQYLAECELICTVPASAFHPAPKVDSAVVRLRPRKIEIPALNPRQLETFLKLGFGAKRKMLRNNLQSVIERDRLSHLLEQLKINPQARAEDISVQQWVILANELAVASGEQGVGNR
Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
B2J0A6
A9MJF0
HUTU_SALAR
Imidazolonepropionate hydrolase
Salmonella
MPESKYRQQTIRAPRGATLTAKSWLTEAPLRMLMNNLDPDVAENPHELVVYGGIGRAARNWECYDAIVDALTRLEADETLLIQSGKPVGVFKTHDNAPRVLIANSNLVPHWATWEHFNELDAKGLAMYGQMTAGSWIYIGSQGIVQGTYETFVEAGRQHYNGTLAGRWVLTAGLGGMGGAQPLAATLAGACSLTIECQQSRIDFRLRTRYVDEQAATLDDALARIAHYTRAGKAVSVALCANAADILPELVNRGVRPDLVTDQTSAHDPLHGYLPTGWRWEEYQEKALSDPQGTMQAAKRSMAAHVQAMLAFSKMGVPTFDYGNNIRQMAKEMGVENAFDFPGFVPAYIRPLFCRGIGPFRWVALSGDPQDIYKTDAKVKEIVAEDKHLHHWLDMARERIHFQGLPARICWVGLEWRQKLGLAFNEMVRCGEVSAPIVIGRDHLDSGSVASPNRETEAMRDGSDAVSDWPLLNALLNTASGATWVSLHHGGGVGMGFSQHAGMVIVCDGTDEAAARIRRVLHNDPATGVMRHADAGYDLAVECAVEQGLHLPMVAATQRKR
Catalyzes the conversion of urocanate to 4-imidazolone-5-propionate.
A9MJF0
Q38Y19
TPIS_LATSS
Triose-phosphate isomerase
Latilactobacillus
MRKPIIAGNWKMNMNPTQTTEFVNAIKANLPKFDQTESVIGAPAVDLPALLEAAKGTDLKVAAENCYFEEAGAFTGETSPKTLNEMGVDYVIIGHSERRDYFHETDEDINKKAHAIFKNNMTPIFCCGESLETREAGKAEEWVSNQVTEGLKGLSADQVSSMVIAYEPIWAIGTGKTASADQAQEICAVVRQTVAKLYDQTVADKVRIQYGGSVKPANVKEIMGKEDIDGGLVGGASMEPASFLDLVHFND
Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Q38Y19
Q5SPP5
EFR3B_DANRE
Protein EFR3 homolog B
Danio
MTGVCGCCGALRPRYKRLVDNIFPEDPEDGLVKANMEKLTFYALSAPEKLDRIGAYLSERLSRDVARHRYGYVCIAMEALDQLLMACHCQSINLFVESFLKMVRKLLEADKPNLQILGTNSFVKFANIEEDTPSYHRSYDFFVSRFSEMCHSGYEDPDIRTKIRMAGIKGLQGVVRKTVNDELQANIWDPQHMDKIVPSLLFNLQSGEGTESRSPSPLQASEKEKESPAELTERCFRELLGRAAYGNIKNAVTPVLMHLDNHSLWEGKTFAVRCFKIIMYSIQSQHSHLVIQQLLGHLDANSKSSATVRAGIVEVLLEVAAIAASGSVGPTVLEVFNTLLRHLRLSVDYELTGSYDCTNIGTKIIKEHEERQLQEAVIRTIGSFANTLPTYQRSEVMLFIMGKVPIPGLHPTLPSIGSGPEGNRMIQVMLLKSLRQVTCGFQTTNMLTALPNSFLDPMLSFALLEDAEIRLLVLEILVSLIDRHDNLPKFSNISIISDISVLKLKVDKCSRQDNLFMKKHAQHLYRHIYLCSKEQSSVQPHFEKLYSLLALISMELANEEVVVDLIRVALALQDLALSSEEMLPVYNRCAIHALSSAYLNLISQLTTVPAFCQHVHEVIEMRQKEIPYLLPEDVFIENPKIPKTLEKLEGDVLFQQAKITEVLGGSGYNTERLATPYVPQFTDEDRLSKRKSIGETISLQVEVDSRNSPEKEERTPAEEITFETLKNAIVDSVGVEEQEKERRRQVVEKFQKAPFEEIAAHCGARATMLQSKLNQIFEITIRPPPSPSGTITSSYGQTQSRSVPVYEMKFPDLCVY
Component of a complex required to localize phosphatidylinositol 4-kinase (PI4K) to the plasma membrane. The complex acts as a regulator of phosphatidylinositol 4-phosphate (PtdIns(4)P) synthesis. In the complex, efr3b probably acts as the membrane-anchoring component.
Q5SPP5
Q554U9
EIF3D_DICDI
eIF-3-zeta
Dictyostelium
MSLELNTIKVNPTGWGPVGKLEKFTDIPYAPFSKGDKIGKCSDWNSNVRNYQRQNYGSNAFNPFTFKLEDDEDSFTLVDYTRVQNKLKNKGKTYQKQFYQQNKRGGSNAGGRGGRGGMRGGRFGSNNKYWNDRRQRNRESSIEILSSWESKEEFDLSTFKQYTVEQLPEPETIGTYGQVKYYNKVYDRINAKNEKKLQKTENSVPLIPTSDDKVIRSEYMNGNVYATDSILAVLMSAQKSVYSWDIVVQKVGARLFFELRPGTSEHLTVNENLTAHHQDDKDPINTTSSLSQEATQVNLNYWQQVLSQNVEPFKFDNELPEGDEFENCVDVGYAYKKWDLGDDIVVLARTEIDGVVEGLPGQPPKFISIKAINEHDSNRFGIEFRKKLDSQRAAILATEIKNNSTKFAKWSIQSTLAGCEMLNLGFVSRDSIRDNNNHVILGTQFYPVADLNKQNGVDMKNCWGILKHIAQTCMKLANGKYLLHRDPNRNVINLYSVPENAFDQIEEETQEEEEEEQSKGWVEESRE
mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. In the eIF-3 complex, eif3d specifically recognizes and binds the 7-methylguanosine cap of a subset of mRNAs.
Q554U9
Q7NFN6
RIMP_GLOVI
Ribosome maturation factor RimP
Gloeobacter
MNPRDIVEQVTALAEPVAEQLGLQLVAVAYQTHTKPATLRVDIRHPTEGTGLDDCEKMSRALEALLDTRDDLIIGAYNLEVSSPGVERVLTTDREFMAFRGFPVMVKTFGPVDGKKQWEGRLLERDGENVYLTIAGRRVALPRPQVARVQLVQSLP
Required for maturation of 30S ribosomal subunits.
Q7NFN6
B3CQP5
LIPA_ORITI
Sulfur insertion protein LipA
Orientia
MCSDKNITATALVRPSWLRVKAPFSDEYQSTNELIKSLKLNTVCKEAACPNIGECWSKKHATVMILGSICTRACAFCNVSTGKPEQVDEYEPYRLSEAVMKLGLKHVVITSVDRDDISDGGASHFAKCITYIRERSPSTSIEVLTPDFLRKHDAWKIVAKARPDVYNHNIETVPSLYLKVRPGARYYNSLNLLHQVKIFDSSIFTKSGIMVGLGETKHEVLQVMDDLRAAEVDFLTIGQYLRPSARHIDVDRYVAPDEFDYYARVAKSKGFLMVSASPLTRSSYHAGEHFEKLKQMRLQNII
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
B3CQP5
P49258
CALL_DROME
Protein androcam
Sophophora
MSELTEEQIAEFKDAFVQFDKEGTGKIATRELGTLMRTLGQNPTEAELQDLIAEAENNNNGQLNFTEFCGIMAKQMRETDTEEEMREAFKIFDRDGDGFISPAELRFVMINLGEKVTDEEIDEMIREADFDGDGMINYEEFVWMISQK
May be involved in calcium-mediated signal transduction.
P49258
Q1XDB1
RPOZ_NEOYE
Plastid-encoded RNA polymerase omega subunit
Neopyropia
MNQHNSLDSSDITYKTEELLEATTNRYKITVQVANRAKRRKYEDVDIIDDPQVKPVIRAILEMVDEITQPEIISD
May be involved in RNA polymerase activity.
Q1XDB1
Q82QR5
RPOA2_STRAW
Transcriptase subunit alpha
Streptomyces
MLIAQRPSLTEEVVDEFRSRFVIEPLEPGFGYTLGNSLRRTLLSSIPGAAVTSIRVDGVLHEFTTVPGVKEDVTDLILNIKQLVVSSEHDEPVVMYLRKQGPGLVTAADIAPPAGVEVHNPDLVLATLNGKGKLEMELTVERGRGYVSAVQNKQVGQEIGRIPVDSIYSPVLKVTYKVEATRVEQRTDFDKLIVDVETKQAMRPRDAMASAGKTLVELFGLARELNIDAEGIDMGPSPVDAALAADLVMPIEELELTVRSYNCLKREGVHSVGELVARSEADLLDIRNFGAKSIDEVKAKLAGMGLGLKDSPPGFDPTAAALGADDDADAGFLETEHY
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Q82QR5
P28092
WNT7_EVATR
Protein Wnt-7
Evasterias
SGSCTTKTCWTTLPPFRLVGNILKQKYEKPVQVEPVRARRTRRPAFLKIKDIKNFKKPRPTDMVYLQRSPNYCDRDPRVGSLGTVGRQCNRTSIGTDSCDLMCCGRGYNTHQYTRIWQCNCKF
Ligand for members of the frizzled family of seven transmembrane receptors. Probable developmental protein. May be a signaling molecule which affects the development of discrete regions of tissues. Is likely to signal over only few cell diameters.
P28092
A0PLD8
Y450_MYCUA
Putative S-adenosyl-L-methionine-dependent methyltransferase MUL_0450
Mycobacterium
MVRTDRDRWDLATSVGATATMVAAQRALAADPQYALIDDPYAAPLVRAVDIDVYTRLVNGQIPVDVESGFDPARMPEAMACRTRFYDQFFVDATRSGISQVVILASGLDARAYRLGWPAGTVVHEVDMPQVIEFKTLTLADLGAKPTAERRTVAVDLRDDWAAVLQAAGFDKDVPSAWSAEGLLVYLPDDAQGALFDNVTALSATGSRLAFEFVPDTAVFNDERWRSHHARMSELGFEIDFNDLVYHGQRSHVIDHLARDGWQSASHTAKELHAANGLDYPDDDIAAVFADITYTSAVLGR
Exhibits S-adenosyl-L-methionine-dependent methyltransferase activity.
A0PLD8
Q03F61
YBEY_PEDPA
Endoribonuclease YbeY
Pediococcus
MDIQTFDHTKEENPKNLELITDILEFAGNYLHLDEETEISVTLMHNDEIHQINKEYRNVDRPTDVISFAINDADEDIIMDPEMAEEIPANIGDLMISVDKVAEQAEFLGHSYERELGFLCVHGFLHLNGYDHMEKEDQEKMFPLQKEIMNAYGLKR
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
Q03F61
P0DKN2
TUB1_LOPOL
OL105
Iotyrris
MARQMMTVGCLILIVVLLDMMVPVFNTCPGQYDECGNGPEEGECCGTHNYCCKNACTTYHHCHGGRDAGKLLRSLKKLKLTTH
Acts as a neurotoxin by inhibiting voltage-gated potassium channels (Kv).
P0DKN2
B3LMP9
MIC12_YEAS1
Found in mitochondrial proteome protein 51
Saccharomyces
MSKLGPLARSVKWTLSVGVIGSVFYLYRYSNNGYFYDHDATWLKQDHQVQDLVDRKEVVPGETRNRKLVVTDDGTAWSRTMGESIKDIWNEQIRNSVDWIYSWGKN
Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane.
B3LMP9
Q2JV01
PLSY_SYNJA
Lysophosphatidic acid synthase
unclassified Synechococcus
MPAWLSALLAALGGYLLGSIPTGYWVGRCWGGIDLRQAGSGSTGATNVLRTVGKGPALLVLLVDAAKGAAAVALGSALGSPWWVVVAALGAVIGHSRSCWLGFKGGKSVATSLGILLAMAWPVALATFGVWLLGIALTRIVSFSSLLAAVAAPLLMWALGQPLPYLLFALAGGVYVIAAHRRNIERLLAGSEPRIGQKWAQSP
Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Q2JV01
Q9JVC0
TRPB_NEIMA
Tryptophan synthase beta chain
Neisseria
MKNYHAPDEKGFFGEHGGLFVSETLIPALQELADAYKAAKNDPEFWEAFRHDLKHYVGRPSPVYHAARLSEHLGGAQIWLKREDLNHTGAHKVNNTIGQALLAKRMGKKRVIAETGAGQHGVASATVAARFGMTCDVYMGADDIQRQMPNVFRMKLLGANVVGVESGSRTLKDAMNEAMREWVARVDDTFYIIGTAAGPAPYPEMVRDFQCVIGNEAKAQMQEAIGRQPDVAVACVGGGSNAIGLFHPYIGEENVRLVGVEAGGLGVNTPDHAAPITSGAPIGVLHGFRSYLMQDENGQVLGTHSVSAGLDYPGIGPEHSHLHDIKRVEYTVAKDDEALEAFDLLCRFEGIIPALESSHAVAWAVKNAPKMGKDQVILVNLSGRGDKDINTVAKLKGIKL
The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
Q9JVC0
A7H295
SYE1_CAMJD
Glutamyl-tRNA synthetase 1
Campylobacter
MHEKLTTRFAPSPTGYLHIGGLRTALYNYLYARKNGGNFLLRIEDTDLKRNSKEATKAIIEAFKWCGLEHDGEVTYQSERFDLYKEYVKKLLDEGKAYYCYMSKEELEELRAKQEAAKERPRYDGRYREFTGTPPQGIEPVVRIKAPQSGEIVFKDGVKGEVRFKAEDIMDDFIIARSDGTPTYNFTVVIDDALMGVSDVIRGDDHLSNTPKQIVLYEALGFKIPQFFHVAMIHGEDGKKLSKRHGATDVMEYKEMGILPQALLNFLVRLGWSHGDDEVFSLEDLKKLFDPYHINKSASCYNAKKLEWLNTHYIKTLPFEEIKRQLKDLGFDLSVYEKAGFLLDLLRERAKTLHDIINGAKSIVNAPQNYDENAVQKFVNENNLELLQAFANTLKDPKTGKDFEDFTNDFLEKKEAKLKDLAQPIRIALTGSAVSPSIFEVLEFLGVDECKKRIENFLKVRGK
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).
A7H295
A6TF07
CYSG2_KLEP7
Sirohydrochlorin ferrochelatase 2
Klebsiella
MDHLPIFCQLRQRDCLLVGGGDVAERKARLLLDAGANVTVNALDFTPQFQVWADSQMLTLVQGEFIPSLLDNCWLAIAATDDETVNQQVSEAAEARRIFCNVVDAPRQASFIMPSIIDRSPLMVAVSSGGTSPVLARLLREKLESILPLHLGQLARYAGHLRARVKQQFATVGERRRFWEKLFVNDRLAQSLANDDRQAVADTTEQLLTEPLEHRGEVVLVGAGPGDAGLLTLKGLQQIQQADVVVYDRLVSDDIMNLVRRDADRVFVGKRSGYHCVPQEEINQILLREAQKGRRVVRLKGGDPFIFGRGGEELETLCEAGIPFSVVPGITAASGCSAYSGIPLTHRDFAQGVRLVTGHLKTGGELDWANLAVEKQTLVFYMGLNQAPAIREKLIAHGMAEDMPAAIVENGTAVTQKVVSGTLGQLDILAQQMASPALIIVGRVVGLRDKLNWFSNH
Multifunctional enzyme that catalyzes the SAM-dependent methylations of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 via precorrin-1. Then it catalyzes the NAD-dependent ring dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it catalyzes the ferrochelation of sirohydrochlorin to yield siroheme.
A6TF07
B2HQM5
THIC_MYCMM
Thiamine biosynthesis protein ThiC
Mycobacterium
MTVTVEPSITTGPIAGSSKAYREVAGPDGVTLRVPLRRVHLSTGADFDLYDTSGPYTDPNAVIDLAVGLPARPGLVRDRGTQLQRARAGEITAEMAFIAAREGMSAELVRDEVALGRAVIPANHNHPESEPMVIGKAFAVKVNANIGNSAVTSSIAEEVDKMVWATRWGADTIMDLSTGKNIHETREWILRNSPVPVGTVPIYQALEKVKGDPTELTWELYRDTVIEQCEQGVDYMTVHAGVLLRYVPLTAKRVTGIVSRGGSIMAAWCLAHHRESFLYTNFEELCDILARYDVTFSLGDGLRPGSIADANDAAQFAELRTLGELTKIAKAHGVQVMIEGPGHVPMHKIVENVRLEEELCEEAPFYTLGPLATDIAPAYDHITSAIGAAIIAQAGTAMLCYVTPKEHLGLPDRKDVKDGVIAYKIAAHAGDLAKGHPHAQERDNALSQARFEFRWNDQFALSLDPDTAREYHDETLPAEPAKTAHFCSMCGPKFCSMRITQDVRDYAAKHGLDSEEAIEAALEAGMAEKSAEFADHGNRVYLPITQ
Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction.
B2HQM5
Q83I60
KAD_TROW8
Adenylate monophosphate kinase
Tropheryma
MRAIMVGPPGSGKGTQCGLIQSRLGISVIATGDVFRERMKTDMALRDIVSSGGYVSDSTTNRIVEDCLDKEDVSSGFVLDGYPRTLQQLDFLEGFLKRRALTLDAVFSLEVATDLLIERLRARSKESGRTDDRDSVIARRLEIYTEMTLPIIDACEEKGLLHRIDASKGIEEVFQSIKDVFDRVTI
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.
Q83I60
Q2VEF8
PSAJ_SOLTU
PSI-J
Solanum
MRDLKTYLSVAPVLSTLWFGALAGLLIEINRFFPDALTFPFF
May help in the organization of the PsaE and PsaF subunits.
Q2VEF8
A7ZJC5
NADA_ECO24
Quinolinate synthase
Escherichia
MSVMFDPDTAIYPFPPKPTPLSIDEKAYYREKIKRLLKERNAVMVAHYYTDPEIQQLAEETGGCISDSLEMARFGAKHPASTLLVAGVRFMGETAKILSPEKTILMPTLQAECSLDLGCPVEEFNAFCDAHPDRTVVVYANTSAAVKARADWVVTSSIAVELIDHLDSLGEKIIWAPDKHLGRYVQKQTGGDILCWQGACIVHDEFKTQALTRLQEEYPDAAILVHPESPQAIVDMADAVGSTSQLIAAAKTLPHQRLIVATDRGIFYKMQQAVPDKELLEAPTAGEGATCRSCAHCPWMAMNGLQSIAEALEQEGSNHEVHVDERLRERALVPLNRMLDFAATLRG
Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate.
A7ZJC5
A9BEC8
PURA_PROM4
IMP--aspartate ligase
Prochlorococcus
MANVVVIGAQWGDEGKGKITDLLSRSADVVVRYQGGVNAGHTIVVEDKVLKLHLIPSGILYPETICLIGSGTVVDPKVMLKEIEMLIENDIDISGLQLASTAHVTMPYHRLIDQAMEKRRGEQKIGTTGRGIGPTYADKAQRNGIRVIDLLDEQKLRERLRIPLAEKNNVLQKIYKELPLDQEKVIEEYLEYGDRLRPHVVDCSRAIHQAARNRKNILFEGAQGTLLDLDHGTYPFVTSSNPVSGGACIGAGVGPTLIDRVIGVAKAYTTRVGEGPFPTELEGSLNDQLCDRGGEYGTTTGRRRRCGWFDGVIGKYAVEVNGLDCIAITKLDVLDELEEIKVCVAYQLDGQKIEYFPSSAEDFSRCKPIFKSLPGWKSSTAECKRLEDLPPSAMAYLRFLAELMEVPIAIVSLGASRDQTIVVEDPIHGPKRALLNI
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.
A9BEC8
A8YUL5
THII_LACH4
tRNA 4-thiouridine synthase
Lactobacillus
MEYTEVMVRYGELSTKGKNRKDFINRLASNVEKVLKDLPQIDFHPRHDRMHIVLNGAPFAEVDKRLKKVFGIQTYSPAIKIPKTLEDIEKTSLELMQETFKPGMTFKVNTKRSDHKFEYDTNQLNNLVGDYLFDHIDHLKAEMKHPDLVLRIEVRQDAVYISNQLLHGIGGMPVGTAGKAVMMLSGGIDSPVASYLAMKRGVDIEMVHFFSPPYTTEKALAKAKELTGILANYVGKINFIAVPFAEIQETIKEKLPEGYLMTVQRRFMLQLADRIRAKRGGLAIFNGESVGQVASQTLQSMVAINDVTTTPVIRPVATMDKTEIIKLAEDIGTFDLSIQPFEDCCTIFAPPRPKTKPKLDKAREYEARLDVEGLIQRAMDGIEVMPIYPNEKFINDKIEEDQDLL
Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS.
A8YUL5
B1XSV3
HIS6_POLNS
ImGP synthase subunit HisF
Polynucleobacter
MLTKRIIPCLDVTAGRVVKGVNFVGLRDAGDPVEIAKRYDTQGADELTFLDITATSDGRDLILHIIEDVASQVFIPLTVGGGVRTVADVRRLLNAGADKVSMNSSAVANPDLVSDAAAYYGSQCIVVAIDAKQTEAGNWEVFTHGGRTATGMDVVEWAKEVAKRGAGEILLTSINRDGSKDGFDLALTAAVSDAVSLPVIASGGVGNLQHLVDGITKGHADAVLAASICHYSEYTVGQAKEYMAAQGIPVRI
IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit.
B1XSV3
A8NR45
ACEA_COPC7
Threo-D(S)-isocitrate glyoxylate-lyase
Coprinopsis
MSSERAQFAAEVAEVERWWKSPRFARVNRPYTAADVVSKRGTIKINYPSDVQGKKLWKLLSEHAKNGTPSHTYGALDPVQVTQMAKYLETVYVSGWQSSSTASSSNEPGPDLADYPSNTVPNKVEHLFMAQLFHDRKQREARSRMSDAELANTPVIDYLRPIVADADTGHGGLTAVMKLTKMFVEKGAAGIHIEDQAPGTKKCGHMAGKVLVPIQEHINRLVAIRLQYDIMGVENLVVARTDSEAATLITSNIDDRDHPFIQGSTNPSLPPLNNVMVEAEAQGKTGDQLQAIEDGWIKAANLQLFPQALAQALANEGASRSTVEKLVARVSRLSWPQAVAVAQKEFGLKQVPYWNWDAPRTREGYYRYQGGTECAIHRANAFAPYADLLWMETKKPILAQAKEFAAGVHAVHPGQWLAYNLSPSFNWEAAGLNAQDMQAYVWELGKLGFVWQFITLAGLHSNAYISDLFAQNFAKTGMKAYVELVQSREREIGCDVLTHQKWSGADYADSLIKTVTGGVSSTAAMGAGVTESQFTSKL
Catalyzes the formation of succinate and glyoxylate from isocitrate, a key step of the glyoxylate cycle, which operates as an anaplerotic route for replenishing the tricarboxylic acid cycle. Required for growth on ethanol or acetate, but dispensable when fermentable carbon sources are available. Acts also on 2-methylisocitrate.
A8NR45
P05162
LEG2_HUMAN
S-Lac lectin 2
Homo
MTGELEVKNMDMKPGSTLKITGSIADGTDGFVINLGQGTDKLNLHFNPRFSESTIVCNSLDGSNWGQEQREDHLCFSPGSEVKFTVTFESDKFKVKLPDGHELTFPNRLGHSHLSYLSVRGGFNMSSFKLKE
This protein binds beta-galactoside. Its physiological function is not yet known.
P05162
A0A1L8HV70
DCK1_XENLA
Deoxyguanosine kinase 1
Xenopus
MATPPKRICIDVPASPSGNKCKVKRISIEGNIAAGKSTFVNILKKANEEWDVVPEPIARWCNIQSCKDEFEELTTSQKSGGNLLQMMYEKPERWSFTFQSYACLSRIRAQLKALGGKLKEAENPVLFFERSVYSDRYIFASNLYEAECMNETEWTVYQDWHDWMNSQFGADLELDGIIYLRAIPEKCLNRVYTRGREEEQGIPMEYLEKLHYKHETWLHHRTLRTDFEYLQEIPILTLDVNEDFRDNKQKQESLIEKVKEFLSTL
Phosphorylates the deoxyribonucleosides deoxyadenosine, deoxycytidine and deoxyguanosine with highest activity against deoxycytidine followed by deadenosine and deoxyguanosine . Shows only very minor activity against deoxyuridine and deoxythymidine .
A0A1L8HV70
Q6X893
CTL1_MOUSE
Solute carrier family 44 member 1
Mus
MGCCSSASAAQSSKREWKPLEDRSCTDIPWLLLFVLFCIGMGFICGFSVATGAAARLVSGYDSYGNICGQRNAKLEAIPNSGLDHTHRKYVFFLDPCNLDLINRKIKSIALCVAACPRQELKTLSDVQKFAEINGSALCSYNIKPSEYTLTSKSSGFCPKLPVPASAPIPFFHRCAPVNISCYAKFAEALITFVSDNSVLHRLISGVMTSKEIILGLCLLSLVLSMILMVIIRYISRVLVWILTVLVILGSLGGTGVLWWLYAKQRRSPKEAVIPEQLQIAEDNLRALLIYAISATVFTVILFLIMLVMRKRVALTIALFHVAGKVFIHLPLLVFQPFWTFFALVLFWAYWIMTLLFLGTTGSAVQNEQGFVEYKISGPLQYMWWYHVVGLIWISEFILACQQMTVAGAVVTYYFTRDKRNLPFTPILASVNRLIRYHLGTVAKGSFIITLVKIPRMVLMYIHSQLKGKENACARCMLKSCICCLWCLEKCLSYLNQNAYTATAINSTNFCTSAKDAFVILVENALRVAAINTVGDFMLFLGKVLIVCSTGLAGIMLLNYQQDYTVWVLPLIIVCLFAFLVAHCFLSIYEMVVDVLFLCFAIDTKYNDGSPGREFYMDKVLMEFVENSRKAMKEAGKGGAADARELKPMLRKR
Choline transporter. May be involved in membrane synthesis and myelin production.
Q6X893
A6TUB2
MNMA_ALKMQ
tRNA-specific 2-thiouridylase MnmA
Alkaliphilus
MKKDPKDTKVVIGMSGGVDSSVAALKLKEQGYDVIGIFMKNWDEPDEYGYCTAAEDYEDVRRVCEQIGIPYYTVNFEKEYWEKVFQYFLDEYKKGRTPNPDVMCNKEIKFKAFLEHALKLGADYLATGHYAQVDYKDGEYRLLRGVDSNKDQTYFLNTLGQYQLSKAMFPIGHIDKKKVREMALAHDLVTAKKKDSTGICFIGERNFKEFLSQYLPAQPGEMRDLSGNVKGKHDGLMYHTLGQRKGLGIGGSGSGEPWFVVSKDLKNNILYVVQGEDHPSLYTYGLLATDLHWVSEKEIPQTFTCTAKFRYRQPDQNVTVQLTGGDTCKVLFDGPQKAVTPGQAVVFYNGEACLGGGIIDETIKTVQEL
Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
A6TUB2
Q32RY5
YCF3_STAPU
Photosystem I assembly protein Ycf3
Staurastrum
MPRSQRNDNFIDKTFTIVADILLRIIPTTQREKEAFTYYRDGMSAQSEGEYAEALLNYYEAMRLEIDPYDRSYILYNIGLIHTSNGEHVKALEYYFQALERNPSLPQALNNMAVICHYRGEQAIEQGDSENSEIWFDQAASYWKQAIALAPNNYIEAENWLKITGRLKE
Essential for the assembly of the photosystem I (PSI) complex. May act as a chaperone-like factor to guide the assembly of the PSI subunits.
Q32RY5
Q0VPJ1
ACCD_ALCBS
Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta
Alcanivorax
MSNSNWLEKILPAVRRPQESRRNNIPEGLWRKCPRCEGVVYRPELDRNMDVCPKCDHHLRISARRRLKLFLDEGVQTEIGTELSPVDRLKFKDSKKYKDRLVAAQKATDEKDALVVLKGALHGEPLVACAFEFSFMGGSMGSVVGERFVRAVNVCLEQKLPLVCFAASGGARMQEALFSLMQMAKTSAALEKMRQAGLPFISVLTDPVYGGVSASLAMLGDVNVAEPNALIGFAGPRVIEQTVRQKLPEGFQRSEFLLEHGAIDMIVSRHDMRETLYRLLANMMGWPPLALDD
Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.
Q0VPJ1
O75496
GEMI_HUMAN
Geminin
Homo
MNPSMKQKQEEIKENIKNSSVPRRTLKMIQPSASGSLVGRENELSAGLSKRKHRNDHLTSTTSSPGVIVPESSENKNLGGVTQESFDLMIKENPSSQYWKEVAEKRRKALYEALKENEKLHKEIEQKDNEIARLKKENKELAEVAEHVQYMAELIERLNGEPLDNFESLDNQEFDSEEETVEDSLVEDSEIGTCAEGTVSSSTDAKPCI
Inhibits DNA replication by preventing the incorporation of MCM complex into pre-replication complex (pre-RC) . It is degraded during the mitotic phase of the cell cycle . Its destruction at the metaphase-anaphase transition permits replication in the succeeding cell cycle . Inhibits histone acetyltransferase activity of KAT7/HBO1 in a CDT1-dependent manner, inhibiting histone H4 acetylation and DNA replication licensing . Inhibits the transcriptional activity of a subset of Hox proteins, enrolling them in cell proliferative control .
O75496
A8LY49
ARGC_SALAI
N-acetyl-glutamate semialdehyde dehydrogenase
Salinispora
MGIRVAVVGASGYAGGELLRLVAGHPEFELVTATAHSQAGHRLHTVHPQLIGLDLVLAETDPAALADADLVFLALPHGESAALAAQLPPKTRVVDLGADHRLADPYAWANYYGGTHAGQWTYGLSELPGQRERVAAATRVANPGCYATAIILALAPLIAAGAAQPADVVVVAASGVSGAGRAAKAHLLAGEVMGDLSPYRVGAHQHVPEIKQATGATSLSFTPVLAPMPRGILATVTAVPARGVDPQAVLAEAYADAPFVHVLPEGRWPHTAATLGSNSCHLQATVDVDAGRLIVVSGLDNLGRGAAGQAVQNANIMVGLPETTGLSAWGVTP
Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
A8LY49
Q6FF10
CRCB_ACIAD
Putative fluoride ion transporter CrcB
Acinetobacter
MYSSLLSIACGAVLGAWLRWFVGLKFNSTFQNFPLGTILVNLVGGFIIGFAIALFANMQLSSNYKLFVITGFCGALTTFSTFSAEVIDLLQQQKYGFAIALITIHLMGSLLCTVLGLLSYQWLSQH
Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Q6FF10
Q9ZMD9
RL21_HELPJ
50S ribosomal protein L21
Helicobacter
MSYAIFKHGGKQYKVVEGDIVLLDKMNKEPKALVELVEVLAVSKEGKLSCGKPFVNGAKIEAEVINEGRSKKVITFKKRRRKDSKTKRGFRRDFTRVRITKIVA
This protein binds to 23S rRNA in the presence of protein L20.
Q9ZMD9
C5CG19
FMT_KOSOT
Methionyl-tRNA formyltransferase
Kosmotoga
MKIVFMGTPDFAAEHLRKLVEKKYNVVGVFSQPDKPKGRGKKLIPTPVKQVAREYGIPVFQPKSVNKGEGFEALKELKPDIIITVAYGKLLKQQVFELPPLGCYNVHASLLPKYRGAAPIQRALENGEKETGITIFKIDEGMDSGPIALQERIEISSDDNFGTLKKKLCNLGKKLLIEFLKKISAGEIKLTPQDHSQATYAPKITKEDTILIEFDNGERVFNKIRAYDPEPGVTTRLGELRVKLFGAGICDNCCVDAEPGQIISISKDSMVVACKKGAVKISKIQFPGKKVITVWQAKSGRLIEEGIKLGG
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.
C5CG19
Q93Z53
PKP3_ARATH
Pyruvate kinase isozyme B2, chloroplastic
Arabidopsis
MAAYGQISSGMTVDPQVLSSSRNIGVSLSPLRRTLIGAGVRSTSISLRQCSLSVRSIKISEDSRKPKAYAENGAFDVGVLDSSSYRLADSRTSSNDSRRKTKIVCTIGPSSSSREMIWKLAEAGMNVARLNMSHGDHASHQITIDLVKEYNSLFVDKAIAIMLDTKGPEVRSGDVPQPIFLEEGQEFNFTIKRGVSLKDTVSVNYDDFVNDVEVGDILLVDGGMMSLAVKSKTSDLVKCVVIDGGELQSRRHLNVRGKSATLPSITDKDWEDIKFGVDNQVDFYAVSFVKDAKVVHELKNYLKTCSADISVIVKIESADSIKNLPSIISACDGAMVARGDLGAELPIEEVPLLQEEIIRRCRSIHKPVIVATNMLESMINHPTPTRAEVSDIAIAVREGADAIMLSGETAHGKFPLKAVNVMHTVALRTEASLPVRTSASRTTAYKGHMGQMFAFHASIMANTLSSPLIVFTRTGSMAVLLSHYRPSATIFAFTNQRRIMQRLALYQGVMPIYMEFSDDAEDTYARSLKLLQDENMLKEGQHVTLVQSGSQPIWREESTHLIQVRKIKIGG
Required for plastidial pyruvate kinase activity.
Q93Z53
Q464W5
CRCB3_METBF
Putative fluoride ion transporter CrcB 3
Methanosarcina
MYTILLVGIGGFIGATLRYVFGGWIQNSFVNFPVGTLTINTIGSFFLGLIMYFSEYQGLFSDQTRIFLTIGILGAFTTLSTFGYESFRLLDDSKLMLMSINVVSTVLFSMMAVYLGKTVALGVSSYLLGGMK
Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Q464W5
Q8NFM4
ADCY4_HUMAN
Adenylyl cyclase 4
Homo
MARLFSPRPPPSEDLFYETYYSLSQQYPLLLLLLGIVLCALAALLAVAWASGRELTSDPSFLTTVLCALGGFSLLLGLASREQRLQRWTRPLSGLVWVALLALGHAFLFTGGVVSAWDQVSYFLFVIFTAYAMLPLGMRDAAVAGLASSLSHLLVLGLYLGPQPDSRPALLPQLAANAVLFLCGNVAGVYHKALMERALRATFREALSSLHSRRRLDTEKKHQEHLLLSILPAYLAREMKAEIMARLQAGQGSRPESTNNFHSLYVKRHQGVSVLYADIVGFTRLASECSPKELVLMLNELFGKFDQIAKEHECMRIKILGDCYYCVSGLPLSLPDHAINCVRMGLDMCRAIRKLRAATGVDINMRVGVHSGSVLCGVIGLQKWQYDVWSHDVTLANHMEAGGVPGRVHITGATLALLAGAYAVEDAGMEHRDPYLRELGEPTYLVIDPRAEEEDEKGTAGGLLSSLEGLKMRPSLLMTRYLESWGAAKPFAHLSHGDSPVSTSTPLPEKTLASFSTQWSLDRSRTPRGLDDELDTGDAKFFQVIEQLNSQKQWKQSKDFNPLTLYFREKEMEKEYRLSAIPAFKYYEACTFLVFLSNFIIQMLVTNRPPALAITYSITFLLFLLILFVCFSEDLMRCVLKGPKMLHWLPALSGLVATRPGLRIALGTATILLVFAMAITSLFFFPTSSDCPFQAPNVSSMISNLSWELPGSLPLISVPYSMHCCTLGFLSCSLFLHMSFELKLLLLLLWLAASCSLFLHSHAWLSECLIVRLYLGPLDSRPGVLKEPKLMGAISFFIFFFTLLVLARQNEYYCRLDFLWKKKLRQEREETETMENLTRLLLENVLPAHVAPQFIGQNRRNEDLYHQSYECVCVLFASVPDFKEFYSESNINHEGLECLRLLNEIIADFDELLSKPKFSGVEKIKTIGSTYMAATGLNATSGQDAQQDAERSCSHLGTMVEFAVALGSKLDVINKHSFNNFRLRVGLNHGPVVAGVIGAQKPQYDIWGNTVNVASRMESTGVLGKIQVTEETAWALQSLGYTCYSRGVIKVKGKGQLCTYFLNTDLTRTGPPSATLG
Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling.
Q8NFM4
A4QCD6
SSRP_CORGB
Small protein B
Corynebacterium
MAKKKKKVDENNSVLATNRKARHDYHIIDTWEAGVVLLGTEIKSLREGKVSLVDSFATIDNGEIWLQHLHIPQYSMGSWTNHTPKRTRKLLLHRNEIDSLMGKVRDGNRTLVPLKLYLKNGRVKLELGLAQGKQDYDKRQDIKRRTEEREVTRELGRRIKGINA
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.
A4QCD6
Q8GBD3
CH10_ACEP3
Chaperonin-10
Acetobacter
MTKFRPLHDRVVVRRLEGEQKTAGGIIIPDTAQEKPMEGEVVAVGPGARNEQGQIVALDVKAGDRVLFGKWSGTEVKIDGEELLIMKESDIMGVVTA
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.
Q8GBD3
Q6Q972
PCB_PRODI
Chlorophyll a/b light-harvesting protein Pcb
Prochloron
MGMQTYGNPDVEYGWWAGNSRLAGFSGKWLAAHVAQAALIVFWAGAICLFEVARYTADVPLGEQNLILIPHMASLGLGIGEGGQIVDTFPYFAVGVVHLVSSAVIGAGGLYHSLRGPAILKEGPARAPKFDFDWGDGKRLGFILGHHLILLGLGALFLVLWAVFFGIYDPVIGEVRTVTSPTLNPFTIFGYQTHFVETNTLEDLIGGHVYVAIIEISGGLWHIFCPPFKWAQRLIIYSGEGLLAYALGGLAIMGFTAAVYCAFNTLAYPVEFYGPPLDFRFSFAPYFIDTADLPSGQYTARAWLCNVHFFLAFFVLQGHLWHALRTLGFDFKRIPAALGSLSEDVVDAKA
The antenna complex functions as a light receptor, it captures and delivers excitation energy to photosystem II (PSII). The Prochlorales pcb genes are not related to higher plant LHCs.
Q6Q972
B0TLB5
TUSA_SHEHH
Sulfur carrier protein TusA
Shewanella
MNDQFSAAQHQLDALGLRCPEPVMMVRKSVRRMNDGETLLIIADDPATTRDIPSFCEFMDHTLIASQTESTPYQYLIKKGL
Sulfur carrier protein which probably makes part of a sulfur-relay system.
B0TLB5
Q9HIQ4
THIE_THEAC
Thiamine-phosphate pyrophosphorylase
Thermoplasma
MKLEGRRIKGLYLVTEDYSRKNFFNIIEEAIIGGVDIVQYRDKSNPRSVRLDVARKVKQICNRYDILFFIDDDVQLAIEVQADGVHIGKDDMPLPDARRIFDGLIGYSTYGDREMAIFAEKNGADYVAFGPFFHTDTKKDADVYDIHVLEGIHKYIRIPVFVIGGINISNIRTFSGYGIDGVAVVSAIFSDPDPERAARELKAALYNYVLSSA
Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
Q9HIQ4
Q4JAB4
CDC62_SULAC
ORC1-type DNA replication protein 2
Sulfolobus
MDDIKNLIEDLLGGDTVFNNTKILNPEYIPSNLPHRENQIKEMTVSFRDLILNPGSSSIRLVIIGRTGTGKSVTTKKFGLKLREIAHERNLRLEYVHVNCHRQRTLYLILQEISQGLRLQLPNRGLSSQETFRIIYDYLEKRNIHLVITLDEFDYFVSTAPLEDIYFLVRVYDELNVTTKRLHYIFIVREITSLSGLDKSIKDHIIKNIIDFPPYKSTELYDILADRVYNEKAFKENSVSEDVLRFIAEVHGFDKGGSGNARISIETLELAGKIADSENSPIVTLEHAKKANSKINPELSALIDSIKELDLHQLIFLKALVLLHDQEGIDFFPIGKIEQRYVELSKNFGEEPRRHTQIFEYVRRMKLMGLINTRQSGRGMRGRTTLVSLPIPISMEFKDLINTEIRKRLEQSRIS
Involved in regulation of DNA replication.
Q4JAB4
B6JDC7
ATPF1_AFIC5
F-type ATPase subunit b 1
Afipia
MLHEAETWVAVAFVLMVALFIYFGAHRMIGEALDRRSARIRKELDDARQLKEEAQKLVAEYRSRRESAEREAQEIVAAAQADAERIAQEAKAKMEDFVARRTKAAESKIAQAETQAVADVRAAAAEAAAAAAANVLSQTVKGSIADNLIEKSIRELGGKLN
Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
B6JDC7
B3QZW0
RS4_PHYMT
30S ribosomal protein S4
16SrX (Apple proliferation group)
MSRYTGSIWKVSRRLNYSLSETGKELIKRPYAPGMHGKKRIKAKDYGLQLQEKQKVRFTYGISEKQFKKIFKDAGKLKGIHGEMFLFLLESRLDNVVYRLGFAKTRQQARQLVNHGHILVDGKKVDIPSYSLRVGQIITLKEKSKDLIIVKEALANKLNRVDYISLNKELVGKYVRIPHRDELLPNIKEQLIVEFYNRK
With S5 and S12 plays an important role in translational accuracy.
B3QZW0
Q5R146
THIG_IDILO
Thiazole synthase
Idiomarina
MLRIADRDFHSRLFIGSGKYSSADIMQKSLAASGSELVTLALKRVELERPTDDIVTPIQNLGLQLLPNTSGAKTAQDAIFAARLAREALGTHWLKLEIHPDPNYLLPDPIETLKAAETLVKEGFTVLPYCGADPVLCKRLEEVGCAAVMPLGAPIGSNQGLLTRDFLRIIIEQASLPVIVDAGIGAPSHAVEAMEMGADAVLVNTAIATANDPVAMSKTFRDAVIVGRQAFEAGLSQNASLKASASSPLTEFLESL
Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S.
Q5R146
P40358
JEM1_YEAST
DnaJ-like protein of the ER membrane 1
Saccharomyces
MILISGYCLLVYSVILPVLISASKLCDLAELQRLNKNLKVDTESLPKYQWIAGQLEQNCMTADPASENMSDVIQLANQIYYKIGLIQLSNDQHLRAINTFEKIVFNETYKGSFGKLAEKRLQELYVDFGMWDKVHQKDDQYAKYLSLNETIRNKISSKDVSVEEDISELLRITPYDVNVLSTHIDVLFHKLAEEIDVSLAAAIILDYETILDKHLASLSIDTRLSIHYVISVLQTFVLNSDASFNIRKCLSIDMDYDKCKKLSLTISKLNKVNPSKRQILDPATYAFENKKFRSWDRIIEFYLKDKKPFITPMKILNKDTNFKNNYFFLEEIIKQLIEDVQLSRPLAKNLFEDPPITDGFVKPKSYYHTDYLVYIDSILCQASSMSPDVKRAKLAAPFCKKSLRHSLTLETWKHYQDAKSEQKPLPETVLSDVWNSNPHLLMYMVNSILNKSRSKPHSQFKKQLYDQINKFFQDNGLSESTNPYVMKNFRLLQKQLQTYKEHKHRNFNQQYFQQQQQQQQHQRHQAPPAAPNYDPKKDYYKILGVSPSASSKEIRKAYLNLTKKYHPDKIKANHNDKQESIHETMSQINEAYETLSDDDKRKEYDLSRSNPRRNTFPQGPRQNNMFKNPGSGFPFGNGFKMNFGL
Acts as a DnaJ-like chaperone required for nuclear membrane fusion during mating.
P40358
O12988
CRYAA_COLLI
Alpha-crystallin A chain
Columba
RALGPLIPSRLFDQFFGEGLLEYDLLPWFSSTISPYYRQSLFRSVLESGISEVRSDREKFTIMLDVKHFSPEDLSVKIIDDFVEIHGKHSERQDDHGYISREFHRRYRLPANVDQAAITCSLSNDGMLTFSGPKVPANMDASHGERPIP
Contributes to the transparency and refractive index of the lens. May act as a chaperone, preventing aggregation of various proteins under a wide range of stress conditions.
O12988
Q05509
GLME_CLOTT
Methylaspartate mutase
Clostridium
MELKNKKWTDEEFFKQREEVLKQWPTGKEVDLQEAVDYLKKVPTEKNFADKLVRAKEAGITLAQPRAGVALLDEHINLLRYLQDEGGADLLPSTIDAYTRQNRYEECEIGIKESEKAGRSLLNGFPGVNHGVKGCRKVLESVNLPLQARHGTPDSRLLAEIIHAGGWTSNEGGGISYNIPYAKSVPIDKCLKDWQYCDRLVGFYEEQGVHINREPFGPLTGTLVPPSMSNAVGITEALLAAEQGVKNITVGYGECGNMLQDIAALRCLEEQTNEYLKAYGYNDVFVTTVFHQWMGGFPQDESKAFGVIVTATTIASLAGATKVIVKTPHEAIGIPTKEANASGIKATKMALNMLEGQRMPMSKELETEMAIIKAETKCILDKMFELGKGDLAVGTVKAFETGVMDIPFGPSKYNAGKMMPVRDNLGCVRYLEFGNVPFTEELKNYNRERLAERAKFEGREVSFQMVIDDIFAVGKGRLIGRPENK
Catalyzes the carbon skeleton rearrangement of L-glutamate to L-threo-3-methylaspartate ((2S,3S)-3-methylaspartate).
Q05509
Q54X03
PMM1_DICDI
Phosphomannomutase 1
Dictyostelium
MSLVPNTICLFDVDGTLTKPRNVITPEMKDFLAGLRTKVELGVVGGSDINKIKEQLGENCINEFHYLFAENGLLSFKDGSLLATQDIKKFLGEENIKKFINFVLHYIADLDIPIKRGTFVEFRNGMINISPIGRNCSQQEREEFEKYDLEHKIRPTMVSILKEKFQSLGLQYSIGGQISFDVFPIGWDKTYCLRHLPEDKYKTIYFFGDKTFVGGNDYEIANDPRITKSFTVTSPTDTKNFLSELFYKQ
Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions.
Q54X03
Q54P59
SARAF_DICDI
Transmembrane protein 66
Dictyostelium
MKHNYYILFLILISSLFLSNKVVESYGHRNNNKGGDSKILLKDVQVLTLRSGEMTKARRSSPIQQMECIGGTATKELELYPKTIQCYNMGSNGVDVQWKCEATLDSTVRLGTIDVSCEGYSYPEDPYITADSCGVFYQLEYTNEQRRKAALAEEETSWVQIIFCIAFIGLILYAVFNWCGSPQGDDDSNTAQNNTATDNNYPGGFPGNNNNNNNNNNNSNNNNYGGNYQGYPNLNNNNNAGGCAQPNNGGGGGGGWFQPGLWTGLASGYLFGRIHSNRNHHHYYNPSPSYNRPRSSYSSGSSGGSGISSSSSSYSGTSRR
Negative regulator of store-operated Ca(2+) entry (SOCE) involved in protecting cells from Ca(2+) overfilling.
Q54P59
Q5HMA8
PTPB_STAEQ
Phosphotyrosine phosphatase B
Staphylococcus
MKIIFVCSGNTCRSPLAESIAKSLLPHDSIASRGLFAVEGQAISKESLELIHKYDLPEPSRAQAFHIDDLDADIILTMTQAHKDLIFSMYGRQSNVFTLNEYVGDTQEIDDPFGGSFDVYEQTYTKIYDLVDKIKFKHE
Dephosphorylates the phosphotyrosine-containing proteins.
Q5HMA8
Q99004
AMELY_BOVIN
Class II amelogenin
Bos
MGTWILFACLLGAAYSMPLPPHPGHPGYINFSYEVLTPLKWYQNMLRYPYPSYGYEPVGGWLHHQIIPVVSQQSPQNHALQPHHHNPMVPAQQPVVPQQPMMPVPGQHSMTPIQHHQPNLPLPAQQSFQPQPIQPQPHQPLQPQPPVHPIQRLPPQPPLPPIFPMQPLPPVLPDLPLEAWPATDKTKREEVD
Plays a role in the biomineralization of teeth. Seems to regulate the formation of crystallites during the secretory stage of tooth enamel development. Thought to play a major role in the structural organization and mineralization of developing enamel.
Q99004
Q746S3
NUOA2_GEOSL
NUO1 2
Geobacter
MQPAGISHSLFPSLPPEFLPLALYTLAASILIGVLLLAAWWLGAKTTNRNKELPYESGAIPTGSARLAYPVPFYLIAIFFIVFDVEAAFIFAWATAWRELGLQGLVHITFFIVILLLGLVWLWLKGGLDWGPSRARRGHVRD
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Q746S3
Q52910
LNT_SINMW
Apolipoprotein N-acyltransferase
Sinorhizobium
MERLAGRIILLSGVSRAFVGFLAGLLAVLAQPPFGIFAAAFVSFPVLVWLIDGVAPDPSDGAFRRLRQPAAIGWSFGFGYFLGGLWWLGNALLVEADAFAWAIPLAVVGLPAVLGVFYALAVVIARCLWSDGWGRIAALALGFGIAEWLRGFVFTGFPWNAIGYAAMPMPLMMQSASVVNLSTINMLAVFVFAAPALIWTGKGARTGLAIAVALFTAHIAFGFYRLAQPAPPSAAPQMAVRVVQPVIDQAKKLDDRERASIFEDHLSLTAAPVQGGGKRPDIVVWPETSIPFILTDNPDALARIAEVLKDGQILVAGAVRAEDAGAGLPSRYYNSVYVIDDRGQIIGAADKVHLVPFGEYLPYEDLLTSWGLSSIAASMPGGFSAARMRPVLTLPGGRRLYPMICYEAIFADEVDANARLADVLLNVTNDAWFGDTPGPRQHFHQAQLRAVETGIPMIRAANTGISAVVDARGVLVLVLGYNYRGVLDTILPGKLPTLTDVPTRSRIFWLSMAILSIVASFSRFGFNIRKN
Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Q52910
A4SD47
MNMA_CHLPM
tRNA-specific 2-thiouridylase MnmA
Chlorobium
MKQETTVLVGISGGVDSAVAACMLVDEGYRVIGLNIKVLDSPESNPALQPSSLVISNREEFRIPVYTLNLSKRFREDVIGYFQEEYLAARTPNPCIVCNKKIKWAGLLEAADMLNADLVATGHYASTAFLGGRCRLYQGADKKKDQSYFLWMLQQKELLKTILPLGTLAKPEVRELARSYGVPAAEKKESQEICFVPGDDYCRYLEQAIPDLAERVRGGELVDASGRVIGHHRGYPFYTIGQRRGLGASTGEPIYVTSIDPVHNRIHTGKKTDLLSRELTASGMNWIGIEPPKKPFEATARIRYRDAPTPCRVTPLEDNRATISFHSPKSAITRGQAAVIYRDDEVLGGGSIVETTQ
Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
A4SD47
Q33C21
CEMA_NICTO
Chloroplast envelope membrane protein
Nicotiana
MAKKKAFTPLFYLASIVFLPWWISFSVNKCLESWVTNWWNTGQSEIFLNNIQEKSLLEKFIELEELLFLDEMVKEYSETHLEEFGIGIHKETIQLIKIQNENRIHTILHFSTNIICFIILSGYSILGNENLAILNSWAQEFLYNLSDTVKAFSILLLTDLCIGFHSPHGWELMIGSIYKDFGFVHSDQIISGLVSTFPVILDTIFKYWIFRYLNRLSPSLVVIYHSMND
May be involved in proton extrusion. Indirectly promotes efficient inorganic carbon uptake into chloroplasts.
Q33C21
B6DD50
TXF17_LYCSI
Toxin-like structure LSTX-N17
Lycosa
MNSKIFAVLLLLGLLSCVLSDQYCPKSSITACKKMNIRNDCCKDDDCTGGSWCCATPCGNFCKYPADRPGGKRAAGGKSCKTGYVY
Has antibacterial activity.
B6DD50
B8IFR7
RNPH_METNO
tRNA nucleotidyltransferase
Methylobacterium
MRPSKRAPEELRKVTLERGVARYAEGSCLVTFGETRVLCTASLEERGPSWLRGSGKGWITAEYAMLPRATHERNRREVNAGKPSGRTQEIQRLIGRSLRAVVNLPAIGERQIVIDCDVLQADGGTRTASITGAWVALHECFTWMRSRSIISVDPMRDHVAAVSCGIHKGTPILDLDYAEDSAAETDANFVITGSGGIVEVQGTAEVTPFSEEEFLGLLRLAKSGVAQLVALQKQAVG
Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation.
B8IFR7
Q318J5
RL24_PROM9
50S ribosomal protein L24
Prochlorococcus
MLDSLKQKKNFQRIKMRIKTGDLVKVINGKDKGKTGEVLKTIPLENRVVVKGINLRTKHVKPTQEGETGRILTEEASLHASNVMFFSKDKNLTSKIEYFIDKQGVKKRRLKKTGEVID
One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.
Q318J5
P47049
UBX6_YEAST
UBX domain-containing protein 6
Saccharomyces
MYEMSGIDSLFHDRVVHDYSHTSEQVIVVYISSAAGDNSWLHQWFKPGNLSDEERENILWVRLVNGTKECLLFKSIFPSSSAPSINILQNGLLECSIQGNSLSREQDPWETFINGLQSVFKGQVTKRKLFSKSNEEYQRVKRMIQNDKLERKYVFQNTNDPQRKPQKWKQLTVTDNVSYKSQKGFLAQNYCTLQLKLPNGYTISNTFPPQTKLHKVRMWLDYNCYDDGTPYLFHRNIPRVTLTRNDELKSLQELDLLPRSTLILEPLEANNKTFDYMEQSSLLHKVYSGLTSFWAKEPEVDASSSRLGYQRLGTNVSNSANYSLQKLSSLDMVSDGGGGGGGDSMTPSAYTTPRMYPSNGTSQLRQNVSELNLSSNNSASNTKVRTLGYSNNNGNN
Involved in CDC48-dependent protein degradation through the ubiquitin/proteasome pathway.
P47049
B7IQU6
NUOK_BACC2
NDH-1 subunit K
Bacillus cereus group
MSSVPASAYLTLAIILFCIGLFGALTKRNTVIVLVCIELMLNAANLNLVAFSKLGLFPNLTGQIFSLFTMAVAAAEAAVGLAILIALYRNRTTVQVDEMDTLKG
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
B7IQU6
P08301
COXX_PARDE
Heme O synthase
Paracoccus
MGPAEAGFGDYVALLKPRVMSLVVFTAFVGLWIAPQPVNPFVAFCAVLFIALGGGASGALNMWYDADIDAVMRRTAGRPVPSGRVTSQEPLAVGIALSGLSVMMLGAGGNWFAAGFLAFTIFFYAVVYTIWLKRSTPQNIVIGGAAGAFPPMIGWALPTGGIGIESLLMFALIFFWTPPHFWALALFMKDDYSKAGVPMLTVTHGRKVTRCHIFAYTLVLAPFALWLGFTSVGGPLYLAVSVVLNALFIAGGWQILRRSEDQAQADGYRVEKRYFRLSLYYTFLHFLALLVQHWVGGW
Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
P08301
Q9M9E1
AB40G_ARATH
Pleiotropic drug resistance protein 12
Arabidopsis
MEGTSFHQASNSMRRNSSVWKKDSGREIFSRSSREEDDEEALRWAALEKLPTFDRLRKGILTASHAGGPINEIDIQKLGFQDTKKLLERLIKVGDDEHEKLLWKLKKRIDRVGIDLPTIEVRFDHLKVEAEVHVGGRALPTFVNFISNFADKFLNTLHLVPNRKKKFTILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGKLDQELKQTGRVTYNGHGMNEFVPQRTAAYIGQNDVHIGEMTVRETFAYAARFQGVGSRYDMLTELARREKEANIKPDPDIDIFMKAMSTAGEKTNVMTDYILKILGLEVCADTMVGDDMLRGISGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRNYVHIFNGTALISLLQPAPETFNLFDDIILIAEGEIIYEGPRDHVVEFFETMGFKCPPRKGVADFLQEVTSKKDQMQYWARRDEPYRFIRVREFAEAFQSFHVGRRIGDELALPFDKTKSHPAALTTKKYGVGIKELVKTSFSREYLLMKRNSFVYYFKFGQLLVMAFLTMTLFFRTEMQKKTEVDGSLYTGALFFILMMLMFNGMSELSMTIAKLPVFYKQRDLLFYPAWVYSLPPWLLKIPISFMEAALTTFITYYVIGFDPNVGRLFKQYILLVLMNQMASALFKMVAALGRNMIVANTFGAFAMLVFFALGGVVLSRDDIKKWWIWGYWISPIMYGQNAILANEFFGHSWSRAVENSSETLGVTFLKSRGFLPHAYWYWIGTGALLGFVVLFNFGFTLALTFLNSLGKPQAVIAEEPASDETELQSARSEGVVEAGANKKRGMVLPFEPHSITFDNVVYSVDMPQEMIEQGTQEDRLVLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIDGNITISGYPKNQQTFARISGYCEQTDIHSPHVTVYESLVYSAWLRLPKEVDKNKRKIFIEEVMELVELTPLRQALVGLPGESGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELFLLKRGGEEIYVGPLGHESTHLINYFESIQGINKITEGYNPATWMLEVSTTSQEAALGVDFAQVYKNSELYKRNKELIKELSQPAPGSKDLYFPTQYSQSFLTQCMASLWKQHWSYWRNPPYTAVRFLFTIGIALMFGTMFWDLGGKTKTRQDLSNAMGSMYTAVLFLGLQNAASVQPVVNVERTVFYREQAAGMYSAMPYAFAQVFIEIPYVLVQAIVYGLIVYAMIGFEWTAVKFFWYLFFMYGSFLTFTFYGMMAVAMTPNHHIASVVSSAFYGIWNLFSGFLIPRPSMPVWWEWYYWLCPVAWTLYGLIASQFGDITEPMADSNMSVKQFIREFYGYREGFLGVVAAMNVIFPLLFAVIFAIGIKSFNFQKR
(Microbial infection) Involved in resistance response to the pathogenic oomycetes Phytophthora infestans and Phytophthora capsici.
Q9M9E1
B4UJU7
ATP6_ANASK
F-ATPase subunit 6
unclassified Anaeromyxobacter
MTAATLVTLALSLSLAQHDAAPAPAPAAVEQHGAAPEAAASADPHAAPAGEHGAAVEAHAAAAGEHGEAAGHEGGHDESLGAVMLHHVTDGYVIEHPGFCNGAFAWNCEWDLRATFGDALKFGKLDLTPTKHVIMMWLASALLLVVVLAAVRKKSLVPRGLYNFIELLVAFVRNEIAVKNIGEKDADRFTPYLVTAFFFILFLNLFGLLPFSATATANLSVTVAMALFTFFITQYAAIRAMGMGGYVAHLTGGVPKSLAPLWLIMVPVEFLGLFTKPFALTVRLFANMLAGHFVILALLGLIFALGTPWVAFGSVPMALSIFLLELFVAFVQAYIFTMLSSLFIGAGLVHHGDDHGHAEEHGHAGPGMGSEHGSHVAGASPGHG
Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
B4UJU7
O34330
YOBL_BACSU
DNase YobL
Bacillus
MKVFEADSLLFEADKRTKEYKELRSQMVKLKKAFKEVANLDDSEFSGKGADNIKAFYHGHVGVTDQWIDLIDMKIAFLSSMSATLEDAKMSDAYIEESFLEHELANAYAKSKSIMSEQKKAMKDILNNINDILPLEIFSTEDFKDKLSSADDKREKTIDKLNKLDEDLKTEYAETEPNEQFIQQDFKKLQESTGKGKNATPIHYNAKAYRESDIHKKKGDIEKHSEAYLSVKKEEAKEREIKELKKKLNDGVSDPDEYLEIAKKVGYENLEPTQVQLAVQIEQAKQLEGAGEITWDIVKGVGVGLYDVGKDTVTGIWDFITDPGETLSALGNAAMHPVKTYDAISAAIEESYQKDMVNGDAYSRSRWVTYAIGSVAVAVVGTKGAGAINKADAAGKVINKASQAGKKIKDVKIPDLLPYNPKYKLALADNVPYNVVDSQNLKNELLTNAKKIPDGTRKPFTGQKKSPPWLNKEKYDAYEIEGKVKAKGKVKDVSRRVYTMKDIDINQKTEFGVTNLQLMKNGNAPYAKDGTQINLHHLIQEEPGPMLEIPNSLHTKYSDVIHQLKSDGESFRNDKVLKAQYESFRKRYWKWRAKQFENEN
Toxic component of one of 6 LXG toxin-immunity modules in this strain. They promote kin selection, mediate competition in biofilms, and drive spatial segregation of different strains, indicating that LXG toxins may help avoid warfare between strains in biofilms. Mediates intercellular competition during biofilm formation; disruption of the operon disadvantages the bacteria, but overexpression of the cognate immunity protein restores growth in competition with wild-type. Overexpression alone in situ causes growth arrest but not cell lysis, a large decrease in chromosomal DNA content and the production of anucleate cells. No effect is seen on rRNA. Co-overexpression with cognate immunity protein YobK does not cause growth arrest. The toxic effect is dependent on the epsA and tapA operons which are required for biofilm formation.
O34330
B7K336
COXX_RIPO1
Heme O synthase
Rippkaea orientalis
MIGTNVAPRHENWLQVVKSYYQLTKPRIIPLLLITTAAAMWIASEGRVDLFTLFITLIGGTLAAAAAQVMNCIYDRDIDYEMLRTRARPIPSGRVQSRHAFIFAVILAILSFSLFALFVNLLSGLLAMSGIVFYMLVYTHLLKRNSPQNIVIGGAAGSIPPLVGWAAVTGDLGWAPWILFAIIFLWTPPHFWALALMIKDDYAQVNVPMMPVVEGEESTVRQIWWYTLLMIPCTFLLVYPLGVSGAVYGGIAIILGAMFIQKAWQLKQAPFDQVLARSLFKFSIFYLMLLCTAMVIDSLPLTHQVMVALGDNLNLLLSLIPLN
Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
B7K336
O26125
RS14Z_METTH
30S ribosomal protein S14 type Z
Methanothermobacter
MIVLPRKYGKASRKCSRCGDHSALVRRYGLMLCRQCFRELAPKIGFKKYN
Binds 16S rRNA, required for the assembly of 30S particles.
O26125
A6H4Q6
COX1_VANPO
Cytochrome c oxidase polypeptide I
Vanderwaltozyma
MLQRWLYSTNAKDIAVLYFIFSVFCGMAGTGMSMIIRLELAGPGNQYLGGNHQLFNTLVTGHAILMVFFLVMPALIGGFGNYLLPLMIGASDMSYPRLNNISFWLLPPALVCLVTSTLVESGAGTGWTVYAPLSGIQSHSGPSVDLAIFALHMTSISSLLGAINFIVTTLNMRTNGMSMHKMPLFVWAIFITAFLLLLSLPVLSAGVTLLLMDRNFNTSFYEVAGGGDPVLYQHLFWFFGHPEVYIMIVPAFGVISHIVSTYSKKPVFGEISMVYAMASIGLLGFLVWSHHMYVVGLDCDTRAYFTSATMIIAIPTGIKIFSWLATIYGGSIRLAVPMMYAIAFLFLFTLGGFTGVALANASLDVAFHDTYYVVAHFHYVLSMGAVFSMFAGYYYWSPHILGLNYNEKLAQIQFWLIFVGVNVIFLPMHFLGINGMPRRIPDYPDAFAGWNYVSSIGSFIAMISLILFIYILFDQLYNGLENKINNKSVTFMKAPDFVESNNKFNLNTIKTSSIEFLLNSPPAVHSFNTPAVTN
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
A6H4Q6
O20106
RR4_CYPSP
30S ribosomal protein S4, chloroplastic
unclassified Cypella
RFKKIRRLGALPGLTSKRPRSGSDLKNQLRSGKRSQYRIRLEEKQKLRFHYGLTERQLLKYVHMAGKAKGSTGQVLLQLLEMRLDNILFRLGMASTIPGARQLVNHRHILVNGRIVDIPSYRCKPRDIITTKDKERSKVLIQNYIASSSHEELPNHLTIDPLQYKGLVNQIIDSKWVGLKINELLVVEYYSRQT
With S5 and S12 plays an important role in translational accuracy.
O20106
Q9I434
PHNW_PSEAE
AEP transaminase
Pseudomonas
MSTAERAPILLTPGPLTTSYRTRRAMMVDWGSWDSDFNELTASVCQRLLKIVGGEGSHTCVPLQGSGTFAVEAAIGTLVPRDGKVLVLINGAYGKRLAKICEVLQRPFSTLETEENVPTTAADVERLLAADPAISHVALIHCETSTGILNPLEAIAKVVERHGKRLIVDAMSSFGAIGIDARKVPFDALIAASGKCLEGVPGMGFVFARSAALEASAGNCHSLAMDLQDQHAYMRKTGQWRFTPPTHVVAALHEALSQYEEEGGLPARQRRYASNCETLLGEMARLGFRSFLPAEIQAPIIVTFHAPRDPRYRFADFYQRVREKGFILYPGKLTQVETFRVGCIGHVDAAEMRQAVAAIGEALRELEVLEI
Involved in phosphonate degradation.
Q9I434
Q5WDF8
SECA_ALKCK
Protein translocase subunit SecA
Alkalihalobacillus
MLGLLRKIVGDPAQKQLKKNEKIVDQVEALADEMKQLSDEQLKNKTTEFKAKLEEGASLNDIVVPALAVAREAAGRVLNEYPYRVQLLGALALHQGNIAEMKTGEGKTLVGTIAVYVQALEGKGVHIVTVNNYLARRDLENYGRIFQFLGLTVGLNENGLTREEKQKAYAADVTYSTNNELGFDYLRDNMVLYKEQMVQRPLHFALIDEVDSILIDEARTPLIISGSVERKTKLYGQANTFVRVLKRDADYTYDEKTKSVQLTDEGVNKAERAFNIDNLYDQKHVQLNHHINQSLKAHVAMHRDADYVVEDGEVVIVDQFTGRLMKGRRYSDGLHQALEAKEGLEVQRESITLASITFQNYFRMYQKLAGMTGTAKTEEEEFRNIYGMDVMVIPTNKPVAREDRPDLIYKTMQGKFNAVVNEIAELHKTGRPVLVGTVNVETSEVVSKMLTRKRIPHHVLNAKNHEREAEIIEKAGHKGAVTIATNMAGRGTDIKLGPGVKELGGLHVLGTERHESRRIDNQLRGRAGRQGDVGSSQFYLSMEDELMRRFGSDNMKAMMEKLGMEDDQPIESSLVSRAVETAQKRVEGNNFDARKQVLQFDDVMREQREIIYRQRMEVLEADNLKTIVENMMKATVERVVQTHCPESLVQEEWDLAAVATYINGQLLSENGISEKELKGKEQEELIELITEKVLAAYHAKEAEVSSEQMREFEKVIMLRTVDRKWMNHIDQMDQLRQGIHLRAYGQNDPLREYRFEGFNMFEAMIAEIEEEVSMYVMKAQVQQNLKREEVAEGKAVRPSANGQEDKKAKRKPVRKAENIGRNDPCICGSGKKYKNCCGANR
Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
Q5WDF8
Q7NSI9
CHED2_CHRVO
Probable chemoreceptor glutamine deamidase CheD 2
Chromobacterium
MNHAEGMNSHQYYDKHFQITAVKVFPGEFHATNQSRLLVTLLGSCVAVCLSDRISGVAGMNHFLLPEGSLDLGAGTSAARFGVNAMELLITDMQKLGAMRNRLEAKIFGAGNVLDGMTVVKVGERNTNFIRSYLANEQIPILAEDLLGECARKVYFFTATGKVLIKKLKKSGAAIKQEQPYRGRIVDQGEGAKTGDIDLFI
Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
Q7NSI9
B9KBD1
MNMA_THENN
tRNA-specific 2-thiouridylase MnmA
Thermotoga
MKVGVALSGGVDSAVALYLLLKEGHEVKAFHMKTKEDEFFLKKEIKKKVCCSPSDTADAIRIARSLGVEIEIVDVREVFREKVIEPFKRDLLRGLTPNPCVHCNRYVKFGYFMDYVLSQGFDAFASGHYARVEFSGKYGKKVIKKGVDGKKDQSYFLARIEPWRIEKLLFPNGIYTKEEIRRIAEEAGIHVAKKQESQDVCFIPDGSIENFLKDEGITLSEGKVITEKGEVVGHHRGYPLYTVGQRKGLKIEKFGERLYVREKIPESNVVVVSGLEGVFFSGLIAVDPVWHVDLPEEFRCVCRVRKKAEEAPAIVRVKNSEVEVRFEKKIFAVTPGQIAAFYDEDTLLGGAIIKEGIP
Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
B9KBD1
Q15YN3
RS3_PSEA6
30S ribosomal protein S3
Pseudoalteromonas
MGQKVHPTGIRLGISKPWTSTWYANTADYADNLFNDHQVRQYLTKALKTASLSKIVIERPAKSIRVTIHTARPGVVIGKKGEDVEKLRKHVSKLAGVPAQINIAEVRKPELDGQLVADSIASQLERRVMFRRAMKRAVQNAMRIGAKGIKVQVSGRLGGAEIARAEWYREGRVPLHTFRADIDYATSEANTTYGIIGVKVWIFKGEVLGGLPLTQEQPAQPKKKGRSPKREG
Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation.
Q15YN3
Q2GCH7
RUVC_NEOSM
Holliday junction resolvase RuvC
Neorickettsia
MSYVALGVDPGLLRTGWAVVEYDGLCNVRYIDSGIVKTASQGSLSARLEKIHRGISDVIEKVNPSVAVLEKVFVNNNPYSSLNLAYCRGALILTLALKGLFIVEFAPSVLKKRITGNGRATKAQVKYMVEQLLGLDPCLSKYSDLYDALALAASVTRYDIMEAKGT
Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group.
Q2GCH7
C0ZPL4
PAND_RHOE4
Aspartate 1-decarboxylase alpha chain
Rhodococcus erythropolis group
MFRTMMKSKIHRATVTHADLHYVGSVTVDQDLMDAADLLEGEQVCIVDIDNGARLETYVIAGERGTGVIGINGAAAHLVKPGDLVILIAYGVMNEQEVKEYSPRVVFVDADNKQIELGSDPAHAPEGSGLITPRMLSTLEASRESSLV
Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
C0ZPL4
A4SG11
RUVB_CHLPM
Holliday junction ATP-dependent DNA helicase RuvB
Chlorobium
MKIELLTTPADAAEVRIEEQIRPARMEDFTGQQRLTDNLKVFISAARMREEALDHVLLSGPPGLGKTTLAHIIAAEMGSSIRATSGPLLDKAGNLAGLLTGLKRGDVLFIDEIHRMPPAVEEYLYSAMEDFRIDIMIDSGPSARAVQLKIEPFTLVGATTRSGLLTSPLRARFGINSRFDYYSPDLLEGIVMRASGILSIGIDQDAASEIAGRSRGTPRIANRLLRRARDFAQVEKAAVISRRIAMKTLECLDIDEEGLDDMDKKIMDTIVNRFSGGPVGVASLAVSVGEEQDTIEEVYEPYLIQAGYLSRTPRGRVATRQALLRFSDGSVSRHTGGLFDADGNLS
The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing.
A4SG11
A5N6J2
MINE_CLOK5
Cell division topological specificity factor
Clostridium
MDLFRAFSKPSSKDIAKERLRLILINDRCSMPQEVLEDIKEDILKVLSKYMEINYAEIDVRMTITEKVEEDPVALVANIPVKKVKYNK
Prevents the cell division inhibition by proteins MinC and MinD at internal division sites while permitting inhibition at polar sites. This ensures cell division at the proper site by restricting the formation of a division septum at the midpoint of the long axis of the cell.
A5N6J2
Q6ZJU3
TIF6A_ORYSJ
OsJAZ9
Oryza sativa
MERDFLGAIWRKEEAAGKPEEHSDYRGGGGGASAAMQWQFPATKVGAASSAFMSFRSSAAAAREEDPKEAAVFDRFSLSGFRPPPRPSPGDAFDGAAAMKQRQFGFNGRQQYAAAAQHGHREQGVDSYGVAAPHHFPSPSPSPRHPVPFGHANPMLRVHSLPNVAGGSPYRNQSFSVGNSVAGSTVGVYGGPRDLQNPKVTQMTIFYDGLVNVFDNIPVEKAQELMLLASRASIPSPPSAARKSDSPISAAAKLTVPEALPARQIVVQKPEASVPLVSGVSNPITIVSQAVTLPKSFSSSNDSAGPKSGGLPLAVTPLSQASPSQPIPVATTNASAIMPRAVPQARKASLARFLEKRKERVSSVAPYPSSKSPLESSDTIGSPSTPSKSSCTDITPSTNNCEDSLCLGQPRNISFSSQEPPSTKLQI
Repressor of jasmonate responses.
Q6ZJU3
A9MRG2
RPIA_SALAR
Phosphoriboisomerase A
Salmonella
MTQDELKKAVGWAALQYVQPGTIVGVGTGSTAAHFIDALGTMKGQIEGAVSSSDASTEKLKGLGIHVFDLNEVDSLGIYVDGADEINGHMQMIKGGGAALTREKIIASVAEKFICIADASKQVDILGKFPLPVEVIPMARSAVARQLVKLGGRPEYRQGVVTDNGNVILDVYGMEILDPIALENAINAIPGVVTVGLFANRGADVALIGTPDGVKTIVK
Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
A9MRG2