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2.75k
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5.51k
AlphaFoldDB
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Q7U351
YIDC_BLOFL
Membrane protein YidC
Candidatus Blochmannia
MESQRSFFIIVFLIVSFILWKIWDDEHHINLLNIENNHSTLQPYSIQSHESNQNTPITHTNNPYSHIITIKTDVFLLKINTYSGNIEEAYLNNYQENLNSQKPLKLLHTSKENKYQAYIDIETLNEYFTNDLNQKNKKHYLYYSNTTNQCEYILKNNENKLQFDLTYQGPNNIIYTKRYLLNRNDYSIYITYIIDNQSTYPIHIKLYGNLIQSIHSDVIQSKHNDHCPLYTYQEAAYSTDTEKYQKYNLKDIKHTNLNIHSTNGWIALLQKYFIIALLPITPKDNTFYTTYLNNHDISIGFKSDFIHIPPGKKNELQSILWMGPKIQDNMKLVAPNLDLVIDYGWLWFISHPLFKLLQFIHTYTIDNWGISIILITVIIRLIMYPLTKAQYTSMAKIRMLQPKLISIQEEYKHDKYQYHQKTIELYKKEKVNPLGGCLPLLIQMPIFLALYYMLSESVELRHAKFAFWIKDLSDQDPYYILPIIMGITMFFIQKLSPTTITDPIQKKIMNIMLVIFTIFFLWFPSGLVLYYIISNIITIIQQQVIYHDLSKKGLHNKK
Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins.
Q7U351
A7HKM4
PTH_FERNB
Peptidyl-tRNA hydrolase
Fervidobacterium
MIVIGLGNPGEKYSNTRHNVGFMVLDRLSNSWKKGPNYLYSDINISGEKIKLIKPMTYMNLSGEVFKYLPHDDIIVVYDDLDLPLGKIRIRKNGSAGGHNGIKSIISFIGQDFPRIRVGIGPKPENIDAADYVLSNFTKEEFEVLDKIINLCTEAIEYIVENGIDKAMNRYNSIEISTGK
The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
A7HKM4
Q3K5Z8
RL14_PSEPF
50S ribosomal protein L14
Pseudomonas
MIQTQSMLDVADNSGARRVMCIKVLGGSHRRYAGIGDIIKVTVKEAIPRGKVKKGQVMTAVVVRTRHGVRRADGSIIRFDGNAAVLLNNKQEPIGTRIFGPVTRELRTEKFMKIVSLAPEVL
Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome.
Q3K5Z8
B8FTI4
MSCL_DESHD
Large-conductance mechanosensitive channel
Desulfitobacterium
MWKEFKEFAMKGNVIDLAVGVIIGGAFGKIVTSLVNDVIMPLVGLLLGQMDFSNAFITLGKGDFATIAEAQAAKVPTLNYGLFINNVVDFLIIAFTIFIVIKQINRFNRKKEVKEEVAEEKATKPCPYCYVEIHKEATRCPHCTSVLESP
Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell.
B8FTI4
Q969R5
LMBL2_HUMAN
Lethal(3)malignant brain tumor-like protein 2
Homo
MEKPRSIEETPSSEPMEEEEDDDLELFGGYDSFRSYNSSVGSESSSYLEESSEAENEDREAGELPTSPLHLLSPGTPRSLDGSGSEPAVCEMCGIVGTREAFFSKTKRFCSVSCSRSYSSNSKKASILARLQGKPPTKKAKVLHKAAWSAKIGAFLHSQGTGQLADGTPTGQDALVLGFDWGKFLKDHSYKAAPVSCFKHVPLYDQWEDVMKGMKVEVLNSDAVLPSRVYWIASVIQTAGYRVLLRYEGFENDASHDFWCNLGTVDVHPIGWCAINSKILVPPRTIHAKFTDWKGYLMKRLVGSRTLPVDFHIKMVESMKYPFRQGMRLEVVDKSQVSRTRMAVVDTVIGGRLRLLYEDGDSDDDFWCHMWSPLIHPVGWSRRVGHGIKMSERRSDMAHHPTFRKIYCDAVPYLFKKVRAVYTEGGWFEEGMKLEAIDPLNLGNICVATVCKVLLDGYLMICVDGGPSTDGLDWFCYHASSHAIFPATFCQKNDIELTPPKGYEAQTFNWENYLEKTKSKAAPSRLFNMDCPNHGFKVGMKLEAVDLMEPRLICVATVKRVVHRLLSIHFDGWDSEYDQWVDCESPDIYPVGWCELTGYQLQPPVAAEPATPLKAKEATKKKKKQFGKKRKRIPPTKTRPLRQGSKKPLLEDDPQGARKISSEPVPGEIIAVRVKEEHLDVASPDKASSPELPVSVENIKQETDD
Putative Polycomb group (PcG) protein. PcG proteins maintain the transcriptionally repressive state of genes, probably via a modification of chromatin, rendering it heritably changed in its expressibility. Its association with a chromatin-remodeling complex suggests that it may contribute to prevent expression of genes that trigger the cell into mitosis. Binds to monomethylated and dimethylated 'Lys-20' on histone H4. Binds histone H3 peptides that are monomethylated or dimethylated on 'Lys-4', 'Lys-9' or 'Lys-27'.
Q969R5
Q1L867
FNDC5_DANRE
Irisin
Danio
MWGIKGSFAVLLLLFLAYIFASSVNADSLSAPLNVTIKALEGNSAIVTWDILEGDPVIGFAITQQKKDVRMLRFIQEVNTTTRSCALWDLEEDTEYIVHVQSISMSGTSPPSEPVLFRTPKESEKLASKSPDEVTMEEVGQAAQLRAGELIIIVVVLVMWAGVIALFCRQYDIIKDNEPNNNKDKAKNSSECSTPEHPTGGLLRSKV
May mediate beneficial effects of muscular exercise.
Q1L867
A8MPH9
FOSLD_DROME
Fos-related antigen
Sophophora
MIALKATEMQHNNNALQQQQQLQHQLLQQHQQQHQQQLQQQLNSPDNNYIWATTHNANISRNNAMLQLQQQQLRAPWITDCNKQHHINNNNSMNVNYNQQLTQQPQQQQQQTQYMQHNYNNYTQQQQQQHLVPATTSQSNSHFYQCNQQQQQQQFLAPTTTTAAVVVAAAHQQHQTQQQHQSQQQQQHQRQDYASLQMGRQLGNFETGQSVLTLTTPTLTPTTTRNIEDTLGHLLSDTQTDRVAGCAGFAVPKVLPNAIDVLGMGIPTGVSSLPLQQTFDLSLGQGSESEDSNASYNDTQMNEEQDTTDTSSAHTDSTSYQAGHIMAGSVNGGGVNNFSNVLAAVSSSRGSASVGSSNANTSNTPARRGGGRRPNRSTNMTPEEEQKRAVRRERNKQAAARCRKRRVDQTNELTEEVEQLEKRGESMRKEIEVLTNSKNQLEYLLATHRATCQKIRSDMLSVVTCNGLIAPAGLLSAGSSGSGASSHHNHNSNDSSNGTITGMDATLNSTGRSNSPLDLKPAANIDSLLMHIKDEPLDGAIDSGSSLDQDGPPPSKRITLPPMSTMPHVHLSTILTPTGASSGSLQTPITSTAPGGFGSAFPVTSNGSSINNINSIGNNMNSPTLNAHNKVPKERPNTLAFQRPLGQMHLTMANNKAGGPTQIQGVPIQTPSTGTFNFDSLMDGGTGLTPVSGPLVPNSSSTNKHPLELPTPTAEPSKLVSL
Developmentally regulated transcription factor AP-1 binds and recognizes the enhancer DNA sequence: 5'-TGA[CG]TCA-3'. May play a role in the function or determination of a particular subset of cells in the developing embryo. It is able to carry out its function either independently of or in conjunction with Jra.
A8MPH9
Q9XXD7
ZIG5_CAEEL
2 Ig domain protein zig-5
Caenorhabditis
MPSPLNHHLSCFVLSVILLGSHVSTSKIPIAPQSVCEGLIEPSVLSIDKPLENIKANRGDSLVLRCAFYASPQPTIVWYHRGKRVDSHPAAHFETLLSATNLGQSVVESALRIDCLDERTAGEYFCEATSPCTQPVVTSSTVTINKAPKSITGTCKSIRQPLESPPIVSDFTLSRIELPGGVAQLACRVRGVPTPKTKWFKIEEDESLSTIDGQPNYMHLSNGDLLIVGDEETISESFRCVASNPLGSVHQDASVIYMMA
Together with zig-8, required postembryonically to maintain the position of ASI and ASH head neuron cell bodies and ventral nerve cord axons of PVQ, PVP and HSN neurons by preventing their displacement that could occur during body growth and movement. May act by reducing L1CAM-like protein sax-7 (long isoform) adhesion.
Q9XXD7
Q0TFN6
NAPA_ECOL5
Periplasmic nitrate reductase
Escherichia
MKLSRRSFMKANAVAAAAAAAGLSVPGVARAVVGQQEAIKWDKAPCRFCGTGCGVLVGTQQGRVVACQGDPDAPVNRGLNCIKGYFLPKIMYGKDRLTQPLLRMKNGKYDKEGEFTPITWDQAFDVMEEKFKTALKEKGPESIGMFGSGQWTIWEGYAASKLFKAGFRSNNIDPNARHCMASAVVGFMRTFGMDEPMGCYDDIEQADAFVLWGANMAEMHPILWSRITNRRLSNQNVTVAVLSTYQHRSFELADNGIIFTPQSDLVILNYIANYIIQNNAINQDFFSKHVNLRKGATDIGYGLRPTHPLEKAAKNPGSDASEPMSFEDYKAFVAEYTLEKTAEMTGVPKDQLEQLAQLYADPNKKVISYWTMGFNQHTRGVWANNLVYNLHLLTGKISQPGCGPFSLTGQPSACGTAREVGTFAHRLPADMVVTNEKHRDICEKKWNIPSGTIPAKIGLHAVAQDRALKDGKLNVYWTMCTNNMQAGPNINEERMPGWRDPRNFIIVSDPYPTVSALAADLILPTAMWVEKEGAYGNAERRTQFWRQQVQAPGEAKSDLWQLVQFSRRFKTEEVWPEELLAKKPELRGKTLYEVLYATPEVSKFPLSELAEDQLNDESRELGFYLQKGLFEEYAWFGRGHGHDLAPFDDYHKARGLRWPVVNGKETQWRYSEGNDPYVKAGEGYKFYGKPDGKAVIFALPFEPAAEAPDEEYDLWLSTGRVLEHWHTGSMTRRVPELHRAFPEAVLFIHPLDAKARDLRRGDKVKVVSRRGEVISIVETRGRNRPPQGLVYMPFFDAAQLVNKLTLDATDPLSKETDFKKCAVKLEKV
Catalytic subunit of the periplasmic nitrate reductase complex NapAB. Receives electrons from NapB and catalyzes the reduction of nitrate to nitrite.
Q0TFN6
Q02957
KRA61_RABIT
Keratin, glycine/tyrosine-rich of hair
Oryctolagus
MCGYYGNYYGGRGYGCCGYGGLGYGYGGLGCGLGSYYGCGYRRLGCGYGCGYGYGYGSRSLCGCGYGYGSGYGSGFGYYY
In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins.
Q02957
Q7TWC5
FAC17_MYCBO
Acyl-CoA synthetase
Mycobacterium tuberculosis complex
MTPTHPTVTELLLPLSEIDDRGVYFEDSFTSWRDHIRHGAAIAAALRERLDPARPPHVGVLLQNTPFFSATLVAGALSGIVPVGLNPVRRGAALAGDIAKADCQLVLTGSGSAEVPADVEHINVDSPEWTDEVAAHRDTEVRFRSADLADLFMLIFTSGTSGDPKAVKCSHRKVAIAGVTITQRFSLGRDDVCYVSMPLFHSNAVLVGWAVAAACQGSMALRRKFSASQFLADVRRYGATYANYVGKPLSYVLATPELPDDADNPLRAVYGNEGVPGDIDRFGRRFGCVVMDGFGSTEGGVAITRTLDTPAGALGPLPGGIQIVDPDTGEPCPTGVVGELVNTAGPGGFEGYYNDEAAEAERMAGGVYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLMRYPDATEVAVYPVPDPVVGDQVMAALVLAPGTKFDADKFRAFLTEQPDLGHKQWPSYVRVSAGLPRTMTFKVIKRQLSAEGVACADPVWPIRR
Catalyzes the activation of medium/long-chain fatty acids as acyl-coenzyme A (acyl-CoA), which are then transferred to the multifunctional polyketide synthase (PKS) type III for further chain extension.
Q7TWC5
Q5E6Q6
TIG_ALIF1
PPIase
Aliivibrio
MQVTVETKEGLERVLTITVPAANIEDAVSAELRNIAKNRRFDGFRKGKVPMKMVAKMYGQAVRNDVMGEVMQRHFIEAIVKEKINPAGAPTFTPVEFAEGKDLVFTASFEVYPEVALQGLDKVVVEKPQVEVKDEDVAEMLETLRKQQSTWADADIAAEDGTRATINFVGSIDGEEFEGGKAENFPLEMGQGRMIPGFEDGIKGKKAGEELTIDVNFPEEYHAENLKGKAAQFAIKVVKVESRELPELNDEFVAKFGAEGGVEGLKAEVRKNMERELAQAVKNKIKEQAINGLVEQNNIDVPSALIDQEVQVLRQQAVQRFGGNADTAPELPRELFEEQAKRRVVVGLLLGEVIKSEELKADDEKVKALINEMASAYEDPTEVVAYYEGNEQMMNNMRNVALEEQAVEAILAKAQVSEKAFGFNELMNQQPA
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.
Q5E6Q6
A5CV84
RS14_CLAM3
30S ribosomal protein S14
Clavibacter
MAKKSKIARNEQRKVIVERYAAKRLELKKALVDPNGTDESREAARAGIQRLPRDASPIRVRNRDGIDGRPRGNLSKFGISRVRFRDMAHRGELPGITKSSW
Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site.
A5CV84
P01323
INS2_RAT
Insulin-2 A chain
Rattus
MALWIRFLPLLALLILWEPRPAQAFVKQHLCGSHLVEALYLVCGERGFFYTPMSRREVEDPQVAQLELGGGPGAGDLQTLALEVARQKRGIVDQCCTSICSLYQLENYCN
Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.
P01323
A8G451
AROB_PROM2
3-dehydroquinate synthase
Prochlorococcus
MNKRKILVPLGEKSYEVTLEAGILNNISEELLKIGITKKRKILVISNEEISNLYGKKFLNNLKDNKFQAKMFLIKAGESYKNLKTLSEIYDVAFEFGLDRNSIIIALGGGIVGDVSGFAAATWLRGIEYIQIPTTLLSMVDSSVGGKTGVNHPKGKNLIGAFNQPKAVFIDPETLKSLPKREFSAGMAEVIKYGVIRDKELFEYLEIDKNKNELINLKNEYLIKIINSSIKTKSHVVSQDEHENGVRAILNYGHSFGHVIENLCGYGKFLHGEAISIGMNIAGKIAIEKGLWSKEELERQRVLLESYDLPTEIPKINKEDVLTILMGDKKVRDGKMRFILPKEIGAVDIYDDVEDSLFLKFFS
Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
A8G451
A7HPE1
AROA_PARL1
5-enolpyruvylshikimate-3-phosphate synthase
Parvibaculum
MASPSNHSASSLTAEPSGALLGSITVPGDKSISHRALIFGALAVGETRIGGLLEGEDVLATAETMRRLGAEVERHADGTWSVHGVGVGGLKEPDQPLDFGNSGTGARLVMGLVAGHPITATFIGDASLSRRPMGRVIAPLTETGATFHAREGGRLPLTLTGAGRALPITYRLPVASAQVKSAVLLAGLNAPGVTTVIEETPTRDHTERMLRAFGAHIEVEDGPRGLIVIRLTGEPELKPCRISVPGDPSSAAFPVVAALLTPGSEITVTGITLNPHRAGLYTTLMEMGGDIEVMNQREEGGEPVADLRVRASRLKGIEVPPARAASMIDEYPVLAIAAAFAEGETRMLGIHELRVKESDRIAATASGLRANGVKVHESDDGMVVEGRSGEVGGGGHVATHIDHRIAMSFLVMGLAAQKPVTVDDAAMIATSFPNFTGLMRGLGASFVGRAQ
Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.
A7HPE1
P73672
ISPG_SYNY3
1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase
unclassified Synechocystis
MVTASLPTPVQPEFDTTIHRRKTRPVPVGAVTVGGGHPVVVQSMINEDTLDVDGSVAGIRRLHEIGCEIVRVTVPSMAHAKALADIKQKLQATYQAVPLVADVHHNGMKIALEVAKHVDKVRINPGLYVFEKPDAQREGYSDQEFAEIGEKIRETLEPLVISLRDQGKSMRIGVNHGSLSERMLFTYGDTPEGMVQSALEFIKICESLDFRNLVVSMKASRVPVMLAAYRLMVKRMDELGMDYPLHLGVTEAGDGEYGRIKSTAGIATLLADGIGDTIRVSLTEAPEKEIPVCYSILQALGLRKTMVEYVACPSCGRTLFNLEDVLHEVREATKHLTGLDIAVMGCIVNGPGEMADADYGYVGKQAGYIALYRGREEIKRVPETDGVQELINLIKADGRWVDP
Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.
P73672
Q038E3
MIAA_LACP3
Isopentenyl-diphosphate:tRNA isopentenyltransferase
Lacticaseibacillus
MDKPAKRIVMIVGPTAVGKSDLGVYLAQQLHGEVINGDAYQIYRHMDIGTAKITPEEMQGVPHHLLDIADPTVAYSVAKFKKAATAMIDTVADRQQLPILVGGTGFYLNSLRLNLPLGGKAPPTAIRQRWQVALATNGQSWLWQQLAQRDPDAAQQIAPANTRRVIRALEVGELTGRRFSDQPQPAPLFSTLVIGLTTDRAVLYDRINARVDAMMQAGLLAEVEQLLKTVPADAQAMQAIGYKELVPYLHGQAELANCVALIKQHSRHFAKRQLTYFRNQMPTHWFDLVAHPEDKNAIVTLVQQWLKQR
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).
Q038E3
P06134
ADA_ECOLI
O6-methylguanine-DNA alkyltransferase
Escherichia
MKKATCLTDDQRWQSVLARDPNADGEFVFAVRTTGIFCRPSCRARHALRENVSFYANASEALAAGFRPCKRCQPEKANAQQHRLDKITHACRLLEQETPVTLEALADQVAMSPFHLHRLFKATTGMTPKAWQQAWRARRLRESLAKGESVTTSILNAGFPDSSSYYRKADETLGMTAKQFRHGGENLAVRYALADCELGRCLVAESERGICAILLGDDDATLISELQQMFPAADNAPADLMFQQHVREVIASLNQRDTPLTLPLDIRGTAFQQQVWQALRTIPCGETVSYQQLANAIGKPKAVRAVASACAANKLAIIIPCHRVVRGDGTLSGYRWGVSRKAQLLRREAENEER
The methylation of Ada by methylphosphotriesters in DNA leads to its activation as a transcriptional regulator that activates the transcription of its own gene, ada, and other alkylation resistance genes, alkA, alkB and aidB.
P06134
B1YHS1
XPT_EXIS2
Xanthine phosphoribosyltransferase
Exiguobacterium
MKRLEEMIKQEGLVLSDQVLKVDSFLNHQVDPTLMWEIAYEFMDRFKDAGITRILTIEAGGIAPAMMTALRLGVPMVYARKTKSLTLNEGTISAEVYSFTKQQTSTITVAEQYLQAGERVLIIDDFLANGEAAFGLAKLVEQAGAEVAGFGIVIEKSFQPGRQKLLDAGFRVESLARIKKLEAGEATFVDPVTV
Converts the preformed base xanthine, a product of nucleic acid breakdown, to xanthosine 5'-monophosphate (XMP), so it can be reused for RNA or DNA synthesis.
B1YHS1
B8B3I4
ORR22_ORYSI
Two-component response regulator ORR22
Oryza sativa
MLLGALRMEERKGLMGRERDQFPVGMRVLAVDDDPVCLKVLETLLRRCQYHVTSTNQAITALKLLRENRDMFDLVISDVHMPDMDGFKLLELVGLEMDLPVIMLSVNGETKTVMKGITHGACDYLLKPVRIEELRNIWQHVVRRKFGNRERNNLDFSKECNKPQSADTDHGPYQPTCGSSDQNGRSSRKRKELHGEDDDEGDDNDYQENDEPSAAKKPRVVWSVELHRKFVAAVNQLGIDKAVPKRILELMNVEKLTRENVASHLQKYRLYLKRLGAVASQQASIVAAFGGRDPSFLHIGAFEGLQSYQPFAPSAALPSFNPHGLLTRTSAAAAFGLQELAAPSSTIQTSTGNVTVGHCLEENQQANLAQGLTAAIGQPQLQQNWIHQEGNGLSDVFSGSSLTNTLSSTLQRVPSSSLPPQELLECKQAKVSMPPSIRIPPSSSALLERTLGVSTNLGDSSISQQGALPIDGGFSADRLPLHSSFDGAVATKLDTSLAASQREIGQQGKFSVSMLVSPSDNLALAKNAKTGASSSGSTIILPLDTARHSDYLQFGGASNSLQKMDGQKQDHIQSSNIIWSSMPSTQLPSDTQIHNTQSQRLDSGSFNHNIGAHLADQTNASASILPQMKFDTRISEEKMKQKNTYDLGSSKLQGGFNSSGCNFDGLLNSIIKVEKDDLPFMDNELGCDLFPLGACI
Transcriptional activator that binds specific DNA sequence. Functions as a response regulator involved in His-to-Asp phosphorelay signal transduction system. Phosphorylation of the Asp residue in the receiver domain activates the ability of the protein to promote the transcription of target genes. May directly activate some type-A response regulators in response to cytokinins.
B8B3I4
I7C6E8
C7A52_PANGI
Oleanic acid synthase
Panax
MELFYVPLLSLFVLFISLSFHFLFYKSKPSSSGGFPLPPGKTGWPIIGESYEFLSTGWKGYPEKFIFDRMTKYSSNVFKTSIFGEPAAVFCGAACNKFLFSNENKLVQAWWPDSVNKVFPSSTQTSSKEEAIKMRKMLPNFFKPEALQRYIGLMDQIAANHFESGWENKNEVVVFPLAKSYTFWIACKVFVSVEEPAQVAELLEPFSAIASGIISVPIDLPGTPFNSAIKSSKIVRRKLVGIIKQRKIDLGEGKASATQDILSHMLLTSDESGKFMGEGDIADKILGLLIGGHDTASSACTFVVKFLAELPQIYEGVYQEQMEIVKSKKAGELLKWEDIQKMKYSWNVACEVLRLAPPLQGAFREALSDFTYNGFSIPKGWKLYWSANSTHINSEVFPEPLKFDPSRFDGAGPPPFSFVPFGGGPRMCPGKEYARLEILVFMHHLVKRFKWEKVIPDEKIVVNPMPIPANGLPVRLFPHKA
Component of the oleanane-type triterpene saponins (e.g. ginsenosides or panaxosides) biosynthetic pathway . Catalyzes the carboxylation of beta-amyrin at the C-28 position to form oleanolic acid during ginsenoside biosynthesis, a class of tetracyclic triterpenoid saponins.
I7C6E8
B8HN58
RPIA_CYAP4
Phosphoriboisomerase A
unclassified Cyanothece
MTTAPDPVKLMKQAVAQTAAARVTSGAVVGLGTGSTTALMIQCLGERLAKGELANIKGVPTSFQASVLAKQYGIPLVTLDEVEKIDLAIDGADEVDPQKNLIKGGGAAHTREKVVDALADLFIVVVDSSKLVDQLGSTFPVPVEVLPMALTPVMRAVTRLGGEPQLRMGVKKDGPVITDQGNMVLDVKFAAIPDPAELEKTLNNIPGVVENGIFVNLAKVILVGELKDGQPSVREIS
Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
B8HN58
P35481
CYT_CYPCA
P12
Cyprinus
MYLKVIVLFLAVTLVVESTGIPGGLVDADINDKDVQKALRFAVDHYNGQSNDAFVRKVSKVIKVQQQVAAGMKYIFTVKMEVASCKKGGVKTMCAVPKNPSIEQVIQCKITVWSQPWLNSLKVTENTCM
Cysteine proteinase inhibitor.
P35481
Q5HH86
MECA_STAAC
Adapter protein MecA
Staphylococcus
MRIERVDDTTVKLFITYSDIEARGFSREDLWTNRKRGEEFFWSMMDEINEEEDFVVEGPLWIQVHAFDKGVEVTISKSKNEDMMNMSDDDATDQFDEQVQELLAQTLEGEDQLEELFEQRTKEKEAQGSKRQKSSARKNTRTIIVKFNDLEDVINYAYHSNPITTEFEDLLYMVDGTYYYAVYFDSHVDQEVINDSYSQLLEFAYPTDRTEVYLNDYAKIIMSHNVTAQVRRYFPETTE
Enables the recognition and targeting of unfolded and aggregated proteins to the ClpC protease or to other proteins involved in proteolysis.
Q5HH86
Q2USD7
DDI1_ASPOR
DNA damage-inducible protein 1
Aspergillus subgen. Circumdati
MTVELLKAIVESETSVPPSAQRIVYNNQLLGDDARTLEQVGIGEGDMLGVHVTLRSPQAPTRTAGGPSAPAAQQNLQRRQAMNPDPETIRLHILGDPRVREAVRRQNPELADAASDAQRFRDVFLNQQRREAQLEAEKEARIAMLNADPFNPENQRQIEEIIRQNAVTENLHNAMEHHPESFGRVTMLYIPVEVNGHKLNAFVDSGAQVTIMSPECATACNIMRLVDQRYGGIAKGVGTANILGRVHSAQIKIGSMFLPCSFTVMEGKHIDLLLGLDMLRRHQACIDLRRGALVIQDQAVPFLGEADIPKHLQDGFEDEPLVKGADGAEVGARTGAVTHQAQGPGGASSSTAPPSRPAPAQSSRWPQDSIAKITELGFTREEAMRALDAANGDLDGAIGFLI
Probable aspartic protease. May be involved in the regulation of exocytosis. Acts as a linker between the 19S proteasome and polyubiquitinated proteins via UBA domain interactions with ubiquitin for their subsequent degradation. Required for S-phase checkpoint control.
Q2USD7
C3M9S7
TAL_SINFN
Probable transaldolase
Sinorhizobium
MKFFVDTADVKEIRELNDLGLLDGVTTNPSLILKSGRDIVEVTKEICSIVEGPVSAEVTATEYSEMMKEAAALSRIADNICIKLPLTLDGLKACKALTSDGHHTNVTLCFSANQALLAAKAGATFVSPFIGRLDDIAFDGMDLIREIRQIFDNYGYETEILAASIRTVNHVKEAALIGADVVTAPPATLKALVKHPLTDKGLEMFLADWAKTGQKIG
Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
C3M9S7
B5LMQ1
PSBN_CICAR
Protein PsbN
Cicer
METATLIAISISGLIVSFTGYALYTAFGQPSQQLRDPFEEHGD
May play a role in photosystem I and II biogenesis.
B5LMQ1
Q8TKT8
CDPAS_METAC
CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase
Methanosarcina
MLPAYLSNPFAAVFGGGKPIDGGRTYKDGRRILGDGKTYRGLFSGIFCGFLAGCIEIWLSMRGFEIMGIKMPTFGPNYASALIVVLALPSGALFGDMFKSFFKRRMGLKRGASLPLVDQLDFVVGAWFFTYLAAPEWFVSNFTTGIALTVLIMTPLLHLTTNIIGYFIGVKKEPW
Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.
Q8TKT8
P33026
SETB_ECOLI
Sugar efflux transporter B
Escherichia
MHNSPAVSSAKSFDLTSTAFLIVAFLTGIAGALQTPTLSIFLTDEVHARPAMVGFFFTGSAVIGILVSQFLAGRSDKRGDRKSLIVFCCLLGVLACTLFAWNRNYFVLLFVGVFLSSFGSTANPQMFALAREHADKTGREAVMFSSFLRAQVSLAWVIGPPLAYALAMGFSFTVMYLSAAVAFIVCGVMVWLFLPSMRKELPLATGTIEAPRRNRRDTLLLFVICTLMWGSNSLYIINMPLFIINELHLPEKLAGVMMGTAAGLEIPTMLIAGYFAKRLGKRFLMRVAAVGGVCFYAGMLMAHSPVILLGLQLLNAIFIGILGGIGMLYFQDLMPGQAGSATTLYTNTSRVGWIIAGSVAGIVAEIWNYHAVFWFAMVMIIATLFCLLRIKDV
Involved in the efflux of sugars. The physiological role may be the detoxification of non-metabolizable sugar analogs. Can transport lactose and glucose.
P33026
A1BJ36
EFTU_CHLPD
Elongation factor Tu
Chlorobium
MAKESYKRDKPHVNIGTIGHVDHGKTTLTAAITSVLAKQGLAQQRDFGSIDKAPEERERGITISTAHVEYQTKKRHYAHIDCPGHADYIKNMITGAAQMDGAILVVAGTDGPMPQTREHILLARQVNVPALVVYLNKVDIADPELIELVELELRELLTEYNFPGDDIPIIKGSALKALDGDLEGEKSIMELMDAVDEFIPEPLRDIDKPFLMPVEDVFSISGRGTVGTGRIERGRIKINEEVEIVGIKPTRKSVVTGIEMFQKLLDEGQAGDNAGLLLRGVDKTELERGMVIAKPGTIKPHTKFKAEVYILRKEEGGRHTPFFNGYRPQFYFRTTDVTGSVTLPEGVEMVMPGDNLSVDVELIVPIAMDENLRFAIREGGRTVGAGSVTKIIE
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
A1BJ36
Q29MT7
NUBP1_DROPS
Cytosolic Fe-S cluster assembly factor NUBP1 homolog
Sophophora
MQAPPPEHCPGVESEQAGQVSACAGCPNQSICSDPNKKREDPGKALVAAALKDVKHKLLILSGKGGVGKSTVTTLLTRYLARSYPDSNFGVLDIDICGPSQPRLMGALGENVHQSGSGWSPVGIDDNVCLMSIGFLLGSVDDAIIWRGPKKNGMIRQFLSEVDWGNLDLLLLDTPPGTSDEHLSVVSYLKDDSSPDSVHAIIVTTPQEVALLDVRKEINFCKKQQIPIVGVIENMSGFQCGHCGHSSEIFPAKTGGAAAMCAEMEVPLLGSLPLDPAIAKACDAGEDITSVKNPTTEALEGICSKIMSSFN
Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. The NUBP1-NUBP2 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins.
Q29MT7
A4JC72
CRCB_BURVG
Putative fluoride ion transporter CrcB
Burkholderia cepacia complex
MFPSIVAIFVGAGLGAVLRWFLGLALNAFVPAMPLGTLAANLLGGYAIGIAAVVFTSRVGLPPEWRLFVITGFLGGLTTFSTYSVEVMTHALQGEFGWAFAVAVLHLTGSFTLTALGMWTASAWFAPA
Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
A4JC72
P06700
SIR2_YEAST
Silent information regulator 2
Saccharomyces
MTIPHMKYAVSKTSENKVSNTVSPTQDKDAIRKQPDDIINNDEPSHKKIKVAQPDSLRETNTTDPLGHTKAALGEVASMELKPTNDMDPLAVSAASVVSMSNDVLKPETPKGPIIISKNPSNGIFYGPSFTKRESLNARMFLKYYGAHKFLDTYLPEDLNSLYIYYLIKLLGFEVKDQALIGTINSIVHINSQERVQDLGSAISVTNVEDPLAKKQTVRLIKDLQRAINKVLCTRLRLSNFFTIDHFIQKLHTARKILVLTGAGVSTSLGIPDFRSSEGFYSKIKHLGLDDPQDVFNYNIFMHDPSVFYNIANMVLPPEKIYSPLHSFIKMLQMKGKLLRNYTQNIDNLESYAGISTDKLVQCHGSFATATCVTCHWNLPGERIFNKIRNLELPLCPYCYKKRREYFPEGYNNKVGVAASQGSMSERPPYILNSYGVLKPDITFFGEALPNKFHKSIREDILECDLLICIGTSLKVAPVSEIVNMVPSHVPQVLINRDPVKHAEFDLSLLGYCDDIAAMVAQKCGWTIPHKKWNDLKNKNFKCQEKDKGVYVVTSDEHPKTL
NAD-dependent deacetylase, which participates in a wide range of cellular events including chromosome silencing, chromosome segregation, DNA recombination and the determination of life span. Involved in transcriptional repression of the silent mating-type loci HML and HMR and telomeric silencing via its association with SIR3 and SIR4. Plays a central role in ribosomal DNA (rDNA) silencing via its association with the RENT complex, preventing hyperrecombination, and repressing transcription from foreign promoters, which contributes to extending life span. Probably represses transcription via the formation of heterochromatin structure, which involves the compaction of chromatin fiber into a more condensed form, although this complex in at least one case can still bind euchromatic levels of positive transcription regulators. Although it displays some NAD-dependent histone deacetylase activity on histone H3K9Ac and H3K14Ac and histone H4K16Ac in vitro, such activity is unclear in vivo and may not be essential.
P06700
Q8R015
BL1S5_MOUSE
Protein Muted homolog
Mus
MSGGGTETPVACDAAQGGKKRDSLGTPGAAHLIIKDLGEIHSRLLDHRPVTQGEIRYFVKEFEEKRGLRELRVLKNLENTIQETNECLLPKCRETMECGLGETLQRLQAANDSICRLQQREQERKKVINDYLTASEKRRLVQWEEFVSGQPQRRAEVDEEHRRAVERLREQYAAMEKDLAKFSTF
Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. Plays a role in intracellular vesicle trafficking.
Q8R015
Q49KU3
NU1C_EUCGG
NADH-plastoquinone oxidoreductase subunit 1
Eucalyptus
MIIDTTEVQDLNSFSRLESLKEVYGIIGMFLPILTLVLGITIGVLVIVWLEREISAGIQQRIGPEYAGPLGILQALADGTKLIFKENLFPSRGDTRLFSIGPSIAVISILLSYSVIPFSYHLVLSDLNIGVFLWIAISSIAPIGLLMSGYGSNNKYSFLSGLRAAAQSISYEIPLTLLCVINISLSNSSSTVDIVEAQSKYGFWGWNLWRQPIGFFIFLISSLAECERLPFDLPEAEEELVAGYQTEYSGIKFGLFYVASYLNLLVSSLFVTVLYLGGWNISIPYIFVPELFEINKVGRVFGTTIGIFITLAKTYFFLFISITTRWTLPRLRIDQLLNLGWKFLLPISLGNLLLTTSFQLLSL
NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Q49KU3
Q9X215
KGUA_THEMA
GMP kinase
Thermotoga
MKGQLFVICGPSGAGKTSIIKEVLKRLDNVVFSVSCTTRPKRPHEEDGKDYFFITEEEFLKRVERGEFLEWARVHGHLYGTLRSFVESHINEGKDVVLDIDVQGALSVKKKYSNTVFIYVAPPSYADLRERILKRGTEKEADVLVRLENAKWELMFMDEFDYIVVNENLEDAVEMVVSIVRSERAKVTRNQDKIERFKMEVKGWKKL
Essential for recycling GMP and indirectly, cGMP.
Q9X215
Q9ZK61
SYV_HELPJ
Valyl-tRNA synthetase
Helicobacter
MKQEPTTYQPEEIEKKIYEICSHRGYFEINGNEKIQEKGKRFCLMMPPPNVTGILHIGHALTLSLQDILVRYKRMDGYKTLYQPGLDHAGIATQNVVEKQLLSQGVKKEDLGREKFIQKVWEWKEKSGGAILEQMKRLGVSTAFSRTRFTMDKGLQRAVKLAFLKWYEKGLIVQDNYMVNWCTKDGALSDIEVEYEERKGALYYIRYYLENQKDYLVVATTRPETLFGDSAIMVNPNDERYKHLVGQQVILPLINRTIPIIADAHVEMGFGTGCVKVTPGHDFNDYEVGKRHHLETIKIFDEKGILNAHCGEFENLERLEARDKVVAALKENALLEKIEEHVHQVGHCYRCHNVVEPYVSKQWFVKPEIAQSSIEKIQQGLARFYPSNWINNYNAWMRELRPWCISRQLFWGHQIPVFTCENNHQFVSLDTPLSCPTCKSEKLEQDKDVLDTWFSSGLWAFSTLGWGQEKSDLFNESDLKDFYPNTTLITGFDILFFWVARMLFCSESLLGELPFKDIYLHALVRDEKGEKMSKSKGNVIDPLEMIEKYGADSLRFTLANLCATGRDIKLSTTHLENNKNFANKLFNAASYLKLKQESFKDKERLNEYQTALGRYAKSRLNLVTKEVRNALDNYRFNDATTLLYRFLWGEFCDWFIEFSKVENEAIDELGSVLKEALKLLHPFMPFISESLYHKLSNTELENAHSIMVMPYPKEIAQDEKLEHEFEVIKDCIVSLRRLKIMLETPPIVLKEASVGLREKIENTERLQNYAQKLAKLEKVSVITYKPLKSVSDVGEFCQTYADLENLDLSPLIARLKKQLEKLEKEKLKLNLHNENFVKNAPKSVLEKARESLKTLLEKEGKIQQELDLLEQP
Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner.
Q9ZK61
O76387
PTH2_CAEEL
Probable peptidyl-tRNA hydrolase 2
Caenorhabditis
MSENIPDIDPNELLPNAPGQHQDLGVDNPPEPDNASIRAERGSPTPSSVTVDNAPSLPDRSFSHLPINDPFSGEIPEVPIPSSAISISSQALSDPVPTPSDTSRPGILRNDEQGSTSSHPVDPQEPNEVNNEYLAHLLDLGFDEYTAVLALKRTNSAGVEQAVAWIVERSNESDFDEDSSSSENEADEEMGAVQSVAGRTHKMVLVANMSLKMGTGKIAAQVGHATLGVYRQAMNSENGQNAIAAWTRHGQVKIVVKGQSTEQLMDLCKVAKDAGCYYYLVQDAGYTQIPAGSRTVLGIFGTVEQVDSVTGGLKLL
The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
O76387
Q0S4V4
NB1_RHOJR
Ferric nitrobindin
Rhodococcus
MDENSTLSPAHSDAAASSSANTPPLPYVPSALAPFAGLWRGEGEGAYPTIDDFAYTEEIEFAPTGKPFLAYRSRTREAGSGRPLHSESGFLRLVGEDEAELLVAQPTGFTEIHRGQVREGTIELSMVVLSASPDAKPVHSIRRQLSVRGGDLTYDLWMAHDLTPLTHHLHGHLRRD
Heme-binding protein able to scavenge peroxynitrite and to protect free L-tyrosine against peroxynitrite-mediated nitration, by acting as a peroxynitrite isomerase that converts peroxynitrite to nitrate. Therefore, this protein likely plays a role in peroxynitrite sensing and in the detoxification of reactive nitrogen and oxygen species (RNS and ROS, respectively). Is able to bind nitric oxide (NO) in vitro, but may act as a sensor of peroxynitrite levels in vivo.
Q0S4V4
A4FQV7
PCKG_SACEN
Phosphoenolpyruvate carboxykinase [GTP]
Saccharopolyspora
MTSLTIPGLDQAPTTHARLLSWVREVAELTTPDRVVWCDGSQDEWQRLTEQLVEAGTFKRLEKKPNSFYAASDPSDVARVEERTFICSREEKDAGVTNYWMQPDEMKAIMTELYRGCMRGRTMYVIPFCMGPLDADKPKLGVEITDTAYVVVSMHIMTRMGSKVLERLGEDEDFVEALHSVGAPLEPGQQDVPWPCNDTKYITHFPEERKIWSFGSGYGGNALLGKKCFSLRIASAMARDEGWLAEHMLILKLISPEDKVHYVAAAFPSACGKTNLAMLQPTIPGWRVESLGDDIAWMRFGEDGRLYAVNPEAGFFGVAPGTNWKTNPNAMRTIDQGNSLFTNVALTDDGDVWWEEMEGEPQHLTDWKGRDWTPQSDEKAAHPNSRYCTPMSQCPILAPEWDDPNGVPISAILFGGRRKTTIPLVNEAFDWQHGVFMGATLSSEKTAAAAGKVGEVRRDPMAMLPFIGYNVGDYFQHWVNVGKEADSSKLPRIFYVNWFRRDESGKKIVWPGFGENSRVLKWIVERLDGNAAAEDTPIGRVPSADQIDLSGLDTPREDVETALHVDVEEWKAELPLIEEWFASIGDSLPSSMRDEFEALKQRLGA
Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle.
A4FQV7
Q82TZ7
PYRH_NITEU
Uridine monophosphate kinase
Nitrosomonas
MPVVYKRILLKLSGEALMGDGHYGIDRAVVEHIVVEVAGVLQLGVEVAIVVGGGNIFRGMKSAGDGMDRVTADYMGMLATTMNALALHDAMRRNGVVSRVQSALRIDQVVEPYVRGKALRYLDERKVVVFAAGTGNPFFTTDTAAALRGMEMNANIVLKATKVDGIYTSDPLKNKDAQRFQSLTFDEAISKNLQVMDATALTLCRDQKLPINVFSIFKTGALKRVIMGEDEGTSVFV
Catalyzes the reversible phosphorylation of UMP to UDP.
Q82TZ7
Q8YF70
URED1_BRUME
Urease accessory protein UreD 1
Brucella
MLIINDNNLSGLSLQRVNGTGELSVQFKDGRSRISRLYQEGAAKIRMPQAVTGPLEAILINTSGGLTGGDRLKWDVALDDGASAVITTQACERIYRSGGGEARIATRLKAAKGTRLAWLPQETILFNRSILSRRLDVELEEGAQMLVVEATVFGRLAMGERVVAARFADRWRVRLGGRVIHAEEFRLGPDVGAELQATAVAGGACAMATVLMVCEQAGRHLETARAIIGEEGGCSLWRVGKASKLVVRLYAPDSYALRRRLCPLVALLNGKAGLPKVWTI
Required for maturation of urease via the functional incorporation of the urease nickel metallocenter.
Q8YF70
Q9HE08
MTNB_SCHPO
Methylthioribulose-1-phosphate dehydratase
Schizosaccharomyces
MDDFLKKDLGCLRSGDLKKCGELICEICRDLYTSGWVTGTGGGITIRSGDAIVIAPSGVQKERMELHHLFVMSLITREYMRMPALRLKPSQCTPLFLAVYTLRDAYACIHTHSQEAILLSTLFADSDHFSATGFEVLSYIPKGSKNNGFHKPTDKIKIPFINNTAHESDLHDSLQEAINLYPDTCAVIVRDHGIYCWGDTWQDTKMNTEAVEFLFQAYLRRRRLQKPE
Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P).
Q9HE08
P97351
RS3A_MOUSE
Protein TU-11
Mus
MAVGKNKRLTKGGKKGAKKKVVDPFSKKDWYDVKAPAMFNIRNIGKTLVTRTQGTKIASDGLKGRVFEVSLADLQNDEVAFRKFKLITEDVQGKNCLTNFHGMDLTRDKMCSMVKKWQTMIEAHVDVKTTDGYLLRLFCVGFTKKRNNQIRKTSYAQHQQVRQIRKKMMEIMTREVQTNDLKEVVNKLIPDSIGKDIEKACQSIYPLHDVFVRKVKMLKKPKFELGKLMELHGEGGSSGKAAGDETGAKVERADGYEPPVQESV
May play a role during erythropoiesis through regulation of transcription factor DDIT3.
P97351
Q5KVD0
HIS6_GEOKA
ImGP synthase subunit HisF
Geobacillus thermoleovorans group
MITKRIIPCLDVKDGRVVKGVQFVQLRDAGDPVELAKAYDEQGADELVFLDISASHEGRKTMVDVVERVAAQLAIPFTVGGGIHSLEDMKRMLRAGADKVSLNTAAVLHPTLITEGADFFGSQCIVVAIDAKYDETLGSWRVYTHGGRNATNWEVVAWAQEAVRLGAGEILLTSMDADGGKNGFDIELTRRVSEAVPVPVIASGGAGKAEHFLEAFEKGKADAALAASIFHYKETSVGQVKAYLKEKGVNVR
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.
Q5KVD0
Q9PQM4
SYV_UREPA
Valyl-tRNA synthetase
Ureaplasma
MKKKLSKKYSFKEVEANKLLFWQENNLFKAQINSTKKPFTIVLPPPNVTGHLHIGHAYDFTLSDILMRYKKLKGYDSFIIPGTDHAGIATQTKFEKNLKVNAQTNRFNLGRELFLEKLKIWKDEQINYIHKQWNALGLGLDYSNYLFTLDPIVVQTVREVFVKMFNEHIIYRDKKLVNWDIQLKTAISNIEVIHKEVEQKLYYIKYLSQDQKDFVVVATSRPETMFGDKYLVINPKDKRYFHLHNKIFINPINNIEMTVILDDYIDIEFGTGVMKCTPAHDFNDYELAKKHNLEIINIMNADGTLNEKCGEFKGLDRLEARSLIIDKLQKNNHLLKVESYRTSVGFSERTNEIVEPYLSHQWFIKMDSLIKDTIKMQDDCNNKVDFYPNRFNKTLLTWLKNTEDWCISRQLWWGHQIPVWYHKKTNQIYCDTIPPKDLENWIQDEDVLDTWFSSGMWPLLTTKWNYNSHFFDRYFPTSLIVTGMDILFFWVSRMMNFSQYLVEKKPFKDVLIHGLIRDSQGRKMSKSLGNGIDPFDIIDKYGLDAMRLFFASCTTIGEDLNFSTERLGANWNYLNKIWNIAKYIENLDEINDNLNFEDVDKFCDVNKWILTELSKLTLEINKNMDKYNLVVATKYLYDFIWNTFASYYLEYTKVLLQDLTLKNETIKTIRYVFNKILIMLQPFAPNISEEIWLCLNQTNNSILLQEYPIINFEFETIIIDKIAKIILEIRKLRLEENINNRINLCFELISPNDAFYKSKIKLVNLLLILVNAEINEIKKTSSNNYTYELVIDDFILKTSYEKPIDYVFQMKKASEQLNYLENEIQRATNLLNNSGFINKAPAQLIIKEKNKLINLKKEHANLLKTLTDLKQKVK
Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner.
Q9PQM4
A6MMM7
PSAJ_DIOEL
PSI-J
Dioscorea
MRNIKTYLSTVPVLTTLWFGSLAGLLIEINRLFPDALLFPFFSF
May help in the organization of the PsaE and PsaF subunits.
A6MMM7
Q04688
ELG_DROME
DNA-binding protein Ets97D
Sophophora
MNSSNDLSDELIRRLSVGGALEEVIASEMFEDSIDVETEAEPDDIIIVHMDIREPLSMLKSLVEQKIGVCLNYYTFWLQDAQELESHKNLVDQCVKGEGLVQINVQIQTIRKRINIADVLKPTEAALAALAEEVVGQLSPPETASQKSSSSESPIKTPLKRMHKEDSEEESVEGKDVKPVLNWVLDSKFKREQIRLKIPEAANEWTHAHVTYWLEWAVKQFELVGINMSDWQMNGQELCAMTHEEFNQKLPRDPGNIFWTHLQLLKECNFVSVVHKRAEEQRKPKQPRIMSANSISTNSGGSLSLEQRIMRKSYQSVKSSDSVESTTSSMNPSNYTTIGSGNNGQVQLWQFLLEILTDCEHTDVIEWVGTEGEFKLTDPDRVARLWGEKKNKPAMNYEKLSRALRYYYDGDMISKVSGKRFAYKFDCDLKLLIGYDANELSTLVSEGKTAPERVAATETITEDT
May have a role in germline development.
Q04688
Q253F8
OBG_CHLFF
GTP-binding protein Obg
Chlamydia
MFLDRITIELRAGKGGNGVVAWRKEKYLPKGGPYGGNGGVGGSIIIESATHVYSFESYRNIRFLKAEDGQAGATNNRSGRNGKDLVLVVPEGTLLRDVETQEILYDFTKDGERLVICRGGKGGKGNTFFKTSTNRAPTKATPGKPGEVRQVEFELKLIADIGLVGFPNAGKSTLFNTLARTEVRVGAYPFTTLQPVLGLVPCQEKLYQKPWIIADIPGIIEGAHQNRGLGLDFLKHIERTRLLLFVIDICGCERSSPEEDLRILIDELLHYKENLADKSRIIALNKIDDLLPDERQERLESFQRLFPSEKFVLLSGLTGEGVDLLNSLFTNRLAI
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.
Q253F8
Q88NC7
ALGK_PSEPK
Alginate biosynthesis protein AlgK
Pseudomonas
MACEGRTMISDTYKVRVNLGLCALAAAITLAGCAGLPDQRLANEALKRGDTALAERNYKALADLGYSEAQVGLADIKVATRDPSQIKEAEATYRAAAATSPRAQARLGRLLVAKPDSTQAEREEAETLLKQAAKQGQSNTLIPLAMLYLSYPQSFPKVNAQQQIDQWRAAGNPEAGLAQVLLYRTQGTYDQHLGEVEKICKAALNTTDICYVELATVYQKRGQADQQAALLGQLKSAYARGAVPATRVDSVARVLADRSLGQTDEKTAKELLEQVAPANPASWVSLAQLVYDFPELGDTDQLMAYIDKGREAEQPRAELLLGRLYYEGKTLPADAQKAEQHLQAAAEAGEISAHYYLGQLYRRGYLGNVEPQKAVDHLLAAARGGQNSADYALAQLFSEGHGIRPQPGNAWVFAQLSQANPTPQSAELLQQLDQQLTPDQRNQAQQLLDQEKRARGSLAQGANSTLALEALQDDEKEVDGEDSL
May be involved in the polymerization of mannuronate to alginate.
Q88NC7
P35745
ACYP2_RAT
Acylphosphate phosphohydrolase 2
Rattus
MAEPLKSVDYEVFGTVQGVCFRMYTEGEAKKRGLVGWVKNTSKGTVTGQVQGPEEKVNSMKSWLSKVGSPSSRIDRADFSNEKTISKLEYSNFSIRY
Its physiological role is not yet clear.
P35745
P96045
DBH_STRTR
DNA-binding protein HU
Streptococcus
MANKQDLIAKVAEATELTKKDSAAAVDAVFASIEEFLAAGEKVQLIGFGNFEVRERAARQGRNPQTGETISIAASKVPAFKAGKALKDAVK
Histone-like DNA-binding protein which is capable of wrapping DNA to stabilize it, and thus to prevent its denaturation under extreme environmental conditions.
P96045
C3KAH5
RL31_PSEFS
50S ribosomal protein L31
Pseudomonas
MKADIHPAYETIEVTCSCGNKFETRSNLCKPLGTDVCNECHPFYTGKQKTLDTGGRVQRFADRFGAFGKKPAATPAE
Binds the 23S rRNA.
C3KAH5
Q9VEB3
RPF2_DROME
Ribosome biogenesis protein RPF2 homolog
Sophophora
MSLLRIRKPKTRKGKKVLLAREPQLIESARTMLFLDGRKCGGNVKLCMKDLQALKKPLVKVLNRKNDITPFDDPSSLEFLTMKNDAALFTFGSTSKKRPDNIILGRIFENEVLDMFELGIKRYQAISEFKNEKIGACVKPCLVFNGPKWAQTEELRRLRNLFIDTFQREKVDSIRLQGIEHVLSFTVTDDMNILMRSYRILLKKSGQRTPRIELEEIGPSADFSIRRTKIASEDLYKQARKQPKQLKVGKKKNISTDALGNTKGRVHLGKQQTGSIQTRRVKALRKTPEEKKENRQRKKVALKAAAAEALASQGNNPFSS
Required for normal assembly of the mitotic spindle. May be involved in both centrosome-dependent and centrosome-independent spindle assembly programs.
Q9VEB3
A1S8K6
DNAJ_SHEAM
Chaperone protein DnaJ
Shewanella
MSKRDYYEVLGVGRDASEREIKKAYKRLAMKYHPDRNPGDKEAEASFKEVKEAYEILTDTDKKAAYDQFGHAGVDPNRGGGGFGGGGDFGDIFGDVFGDIFGGGRRGGQRQAARGSDLRYNLELSLEEAVRGLTKELKVPTLVGCDSCDGSGAKKGSSATTCGTCHGMGQVQMRQGFFAVQQTCPTCHGRGKIIKDPCSKCHGNGRVEKTKTLSVKIPAGVDTGDRIRLAGEGEAGEFGAPPGDLYVQVTVREHPIFVRDGNNLYCEVPISFAKAALGGEIEVPTLDGKVSLKIPAETQTGRMFRLRGKGVKSVRSHAVGDLLCKVVMETPVNLSERQKELLREFEASLTGESKKHSPKAEGFFDGVKKFFQDLNN
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
A1S8K6
Q8RI74
VATE_FUSNN
V-ATPase subunit E
Fusobacterium
MSSLDNLVAEILQQAEKEANRILVKVKAENLEFTENENKKIQKEIENIQWKTNEEAISLKERIISNANLKSRDMVLQAKEELVDKVLKMTLERLKNLDSDSYLDFVENALKTLNISKNAEIILTKKMKDVLGKEIFGYKVSDDIVESGCNIKDGNVIYNNEFSSLLEFNKEDLEREILKKIFG
Produces ATP from ADP in the presence of a proton gradient across the membrane.
Q8RI74
A7I3U2
RL1_CAMHC
50S ribosomal protein L1
Campylobacter
MAKNSKRFNELLKKVDDSKIYNINEAVETVKTLASAKFDETVEISLKLNVDPKYADQMVRGSVVLPAGTGKKVRVAVIAKDAKADEAKNAGADIVGSEELIEEIQKGNINFDVLIATPNLMGLVGKVGRILGPKGIMPNPKTDTVTMDITNAVKNAKSGQVNFRVDKQGNINAGIGKVSFSKEQICNNLTTFIKEINKHKPATSKGRYIKSGALSLTMSPSLSLDTQELLDLK
Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA.
A7I3U2
Q66K79
CBPZ_HUMAN
Carboxypeptidase Z
Homo
MPPPLPLLLLTVLVVAAARPGCEFERNPAGECHRPPAADSATCVDLQLRTCSDAAYNHTTFPNLLQHRSWEVVEASSEYILLSVLHQLLEGQCNPDLRLLGCAVLAPRCEGGWVRRPCRHICEGLREVCQPAFDAIDMAWPYFLDCHRYFTREDEGCYDPLEKLRGGLEADEALPSGLPPTFIRFSHHSYAQMVRVLRRTASRCAHVARTYSIGRSFDGRELLVIEFSSRPGQHELMEPEVKLIGNIHGNEVAGREMLIYLAQYLCSEYLLGNPRIQRLLNTTRIHLLPSMNPDGYEVAAAEGAGYNGWTSGRQNAQNLDLNRNFPDLTSEYYRLAETRGARSDHIPIPQHYWWGKVAPETKAIMKWMQTIPFVLSASLHGGDLVVSYPFDFSKHPQEEKMFSPTPDEKMFKLLSRAYADVHPMMMDRSENRCGGNFLKRGSIINGADWYSFTGGMSDFNYLHTNCFEITVELGCVKFPPEEALYILWQHNKESLLNFVETVHRGIKGVVTDKFGKPVKNARISVKGIRHDITTAPDGDYWRLLPPGIHIVIAQAPGYAKVIKKVIIPARMKRAGRVDFILQPLGMGPKNFIHGLRRTGPHDPLGGASSLGEATEPDPLRARRQPSADGSKPWWWSYFTSLSTHRPRWLLKY
Cleaves substrates with C-terminal arginine residues. Probably modulates the Wnt signaling pathway, by cleaving some undefined protein. May play a role in cleavage during prohormone processing.
Q66K79
A5EY31
GATA_DICNV
Glutamyl-tRNA(Gln) amidotransferase subunit A
Dichelobacter
MSDLHHKTVAELATLLHNKTLSSVELTQHFLSRIQQYNPKLNAYICTTADRALADAKASDERRQKGAAHSPLDGIPMGHKDLFCTKGIATTAGSKMLERFIPSYTATVVARLEAAGSVLTGKLSMDEFAMGSSNERSYFGAVYNPWDEQRIPGGSSGGSAAAVAARLIPYATGSDTGGSVRQPAAYCGITGIKPTYGTCSRWGMIAYASSLDQAGVLAKTAQDCALILNEMAGHDPKDSTSNPKALTQFDHELNRDLDGITIGLPSNYLAGLDAKIAEKLQQTAALYEKLGATIKEITLSATDVAIASYYLISSAEASSNLERFDGVHYGYRCANPKDLSDLYERSRSEGFGAEVKRRIMIGTYALSAGYYDAYYEQARRGRRAILNSFLQAFKECDVILGPTTPTTAYPLGSKVDDPVAMFLGDLYTVSANLAGLPALSHPAGFIDGLPVGCQLIGAHFSEPQLLNLAHRFQQETDFHQQIPEHYR
Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
A5EY31
Q4JVI8
UVRC_CORJK
Excinuclease ABC subunit C
Corynebacterium
MTSVSYRPEPGSIPTDPGVYTFRDAHERVIYVGKAKNLRARLSNYFQDLDQLHPRTRAMVQSANHVQWTVVSSELEALNLEYTWIKRFNPRFNVMYRDDKTYPMLAISVKEQIPRAFMYRGPRRKGVRYFGPYPKAWAIRETLESLTRVFPIRTCSAGVYRRHEALGRPCLLGYIDRCSAPCVGKITPEDHRALVDQFSSFLAGNTEPVLRRVRKEMEQASENLDFERAASLRDQLQAMQKSMERQAVVFSDNTDADLIAFVADELEAAVQIFHVRGGRIHGQRGWVVEREDLSEEKLVADFITQFYGETAELAKATETQVGGASGPEVDRDLARAINPAAAQDLGDLVGDVQVTPVPREILVHAMPDDADDLAAWLTSLRGSNMQIRVPQRGDKKALMTTAETNATQALAQHKLKRAGDITARSAALKELQEALWMDESPLRIECTDISHIQGTDVVASLVVFEDGLPKKADYRRYKIRDAAGDGHSDDVASIAEVVRRRFKRYQQDKSAVPAGDDAGDLLEGETELEDNSAEGTDPATEKRKFAYPPQLFIVDGGLPQVNAAQEVLDELGVNDVTLVGIAKRLEEIWVPGEEYPIIVPRNSPALYLVQNLRDEAHRFAITFHRQQRSARMRRSKLDDIPGLGPKRRKQLVKEFGSVARVKEASVEDIAALPGFGPKLAQLIHDALNAE
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.
Q4JVI8
Q54TE7
GPN2_DICDI
ATP-binding domain 1 family member B homolog
Dictyostelium
MGFGQVVIGPPGSGKTVYCNGMSQFLQSIGRKVSIINLDPSNENIPYEPAVNIQELIDFQTVVNETDLGPNGGLIFCMEYLEKNLDWLKEKLLPLKDHYIIFDCPGQVELYTHYKIISNILDNIMKWSFRLTVIQVFDSFYCKNPSNFISILLVSLSGMVRIELPHINVLSKMDLIEQNGPLDFNLDFYTDVLDLKYLDAFLDKDPRLKKYSKLNKAIAGVIEDFSLVSFIPLNIMDKKSVANLIASIDKSNGYIYGSLDTNTAILEIQERETQWNFDKYQETQEKYYKSYEDDDVIFENDQDEDYDEFSKYLNR
Small GTPase required for proper localization of RNA polymerase II and III (RNAPII and RNAPIII). May act at an RNAP assembly step prior to nuclear import.
Q54TE7
A7MPB4
NUOH_CROS8
NDH-1 subunit H
Cronobacter
MSWLTPDVIEILLSILKAVVILLVVVSCGAFMSFGERRLLGLFQNRYGPNRVGWGGSLQLVADMIKMFFKEDWIPRFSDRVIFTLAPMIAFTSLLLAFAIVPVSPTWVVADLNIGILFFLMMAGLGVYAVLFAGWSSNNKYSLLGAMRASAQTLSYEVFLGLSLMGVVAQAGSFNMTDIVNNQAHLWNVIPQFFGFITFAIAGVAVCHRHPFDQPEAEQELADGYHIEYSGMKFGLFFVGEYIGIVTVSALIVTLFFGGWQGPWLPPFIWFALKTAFFMMMFILIRAALPRPRYDQVMSFGWKVCLPLTLINLLVTAAVILWQTAA
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. This subunit may bind ubiquinone.
A7MPB4
O14233
RNA14_SCHPO
mRNA 3'-end-processing protein rna14
Schizosaccharomyces
MNSDDNVEADASSNIIKDSPKIKEQENTSTVNESDVLATSTTASSGVKRKRLPNDLVGQLRDKIQENPNDISSWYALVEEYGSKGKHEELRETYEQMLRPFPYVPRVWVDYISSELAFNDFHAVELLFSRCLVKVLSVDLWTLYLSYIRRINPDGEGQSRSTITQAYEFVINTIGVDILSGPIWSEFVDFLRSGPANSTWEQQQKLDHVRRIYQRAITTPIHNIEKLWRDYDAFENSVNRATARKFVAEKSPVYMAARAAMRELSNLTEGLRVYDFTFERKYTKVERIAYSRWMNWIKWEQSDPLDLQHGTMLQNRIAYAFEQAMLYVPLCPQIWLDGFSYFLSISDEQRALQTIRRGMRYCPSNFVLHVRYAEHEEANNRTSEIRSTYESLIAALAREISQLDSKASSSSESSTDGNPQEKKLPEHLVKRKSRLVRQYSLAWCCLINAIRRTEGVKAARAIFTKARKAPYQSHEIYIASAMMEHHCSRDPVIASRIFELGMRHFGDVPAYVYKYLSYLIAINDETNARALFEKAIPRIAADEAKPIYQKWLDYESNYGDLNAAIALSQRMAVVYPQESTQAIFLSRYGLKDDAEEEERETKEAEKIRELSVRLNGGNGFPGHVHNNREDDEVSIASTSSKSNVEMEDTRLLPASLELANTQGASNPPTSALPTVPVPLPSIITEFLDELPAPQVITGPRIQPTKLIDHIIKSDIPFIRLRNANAHLKRARFN
Component of the cleavage factor IA (CFIA) complex, which is involved in the endonucleolytic cleavage during polyadenylation-dependent pre-mRNA 3'-end formation.
O14233
Q7T0P6
DFI8B_XENLA
Differentially expressed in FDCP 8 homolog B
Xenopus
MEYDDKLVRFRQGHLNPFDKKGGAERHPADSETQPCKDSSTSSPLSVPEYNYPDRVMDLGVSEDHFSRPVGLFLASDVQQLRQAIEECKQEILELPENSDRQKDAVVRLIHLRLKLQELNDPLEDEPNLRVLLEHRFYKEKSKSVKHLCDKCSTFIWGLIQTWYTCTGCSYSCHSKCLNLITKPCVRSKVSHQAEYELSICPEAGLDSQDYRCAECRTPISLRAVPSEARQCDYTGQYYCISCHWNDLAVIPARAIHNWDFEPCKVSRYSMRYLALMLGRPVLKLREINPLLFNYVEELVEIRKLRQDILLMKPYFITCKEAMEDRLLLQLQDRQHFVENDDMYSLQDLLDISSGRLGCSLTEIHTTFAKHIKLDCERCQAKGFMCELCKEGDILFPFDSHTSVCQDCAAVFHRDCYYENSTSCPRCMRLNLRKQVQNPGAEP
Positively regulates lysosome peripheral distribution and ruffled border formation in osteoclasts. Involved in bone resorption.
Q7T0P6
A5CWN5
DAPF_VESOH
PLP-independent amino acid racemase
Candidatus Vesicomyosocius
MLINFTKMHGLGNDFMVVDNLAGDITFNAKKITNLANRAFGIGFDQLLVVETSNIRGVDFRYVIYNSNGSEVEQCGNGARCFARFVNYKNLTHSNPITVKTRSNIISLHLNDDNTVCVDMGKPSFNPADIPLLVPQQSEYYQIEGFDLGAISIGNPHCVMLVKDVNTIDVNTIALKIQQSELLPNQANIGFMQILNTHEINLRVYERGSEETLACGSGACAAVAYGVEQGLLKKNVVVHLSGGDALIEYTQGGHIFLSGPAQFVFEGQVEI
Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan.
A5CWN5
P13927
EFTU_MYCGE
Elongation factor Tu
Mycoplasma
MAREKFDRSKPHVNVGTIGHIDHGKTTLTAAICTVLAKEGKSAATRYDEIDKAPEEKARGITINSAHVEYSSDKRHYAHVDCPGHADYIKNMITGAAQMDGAILVVSATDSVMPQTREHILLARQVGVPKMVVFLNKCDIASDEEVQELVAEEVRDLLTSYGFDGKNTPIIYGSALKALEGDPKWEAKIHDLIKAVDEWIPTPTREVDKPFLLAIEDTMTITGRGTVVTGRVERGELKVGQEVEIVGLKPIRKAVVTGIEMFKKELDSAMAGDNAGVLLRGVERKEVERGQVLAKPGSIKPHKKFKAEIYALKKEEGGRHTGFLNGYRPQFYFRTTDVTGSIALAENTEMVLPGDNASITVELIAPIACEKGSKFSIREGGRTVGAGTVTEVLE
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
P13927
A0A0H2XEA6
HO_XANC8
Heme oxygenase
Xanthomonas
MMQALGQGHIDADTYAQVLRRHHRLLAGFEEQLSDWLVTLVGSGWQYRRRVPALREDLRVLGQPVDAAVPPPASSEAARWGMLYVIEGSQLGGRVIARMLRKRQPGLAHALHYFELADEDPAGWRRFQAVLEQRLQSAAARADAIAGAQAMFAHFHTCLAAEARP
Catalyzes the opening of the heme ring to form the open-chain tetrapyrrole biliverdin IX with the release of iron and carbon monoxide (CO).
A0A0H2XEA6
P39636
ROCC_BACSU
Amino-acid permease RocC
Bacillus
MQNHKNELQRSMKSRHLFMIALGGVIGTGLFLGSGFTISQAGPLGAIAAYIIGGFLMYLVMLCLGELAVAMPVAGSFQAYATKFLGQSTGFMIGWLYWFSWANTVGLELTSAGILMQRWLPSVPIWIWCLVFGIVIFLINALSVRSFAEMEFWFSSIKVAAIILFIVIGGAAVFGLIDFKGGQETPFLSNFMTDRGLFPNGVLAVMFTLVMVNFSFQGTELVGIAAGESESPEKTLPKSIRNVIWRTLFFFVLAMFVLVAILPYKTAGVIESPFVAVLDQIGIPFSADIMNFVILTAILSVANSGLYAASRMMWSLSSNQMGPSFLTRLTKKGVPMNALLITLGISGCSLLTSVMAAETVYLWCISISGMVTVVAWMSICASQFFFRRRFLAEGGNVNDLEFRTPLYPLVPILGFCLYGCVLISLIFIPDQRIGLYCGVPIIIFCYAYYHLSIKKRINHETIEKKQTEAQ
Putative transport protein involved in arginine degradative pathway. Probably transports arginine or ornithine.
P39636
A2BPR2
HIS6_PROMS
ImGP synthase subunit HisF
Prochlorococcus
MVALRLIPCLDVAHGRVVKGVNFVNLRDSGDPVELACRYSDEGADELVFLDIRASVENRNTLVDLVSRTAKSVKIPFTVGGGIDSVSSINDLLRAGADKVSLNSSAVRNPDLISKSSREFGNQCIVIAIDARRKVNKFGEWEVYVKGGRENTGIDVLSWAKKVEELGAGEILLTSMDGDGTQNGYDLNLTESVANIVDIPVIASGGAGSLEDIFDVFKEGRASAALLASLLHDKKLTLKEIKTFLLEKKLSIRPYE
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.
A2BPR2
A7GRH0
RL19_BACCN
50S ribosomal protein L19
Bacillus cereus group
MQQLIAEITKSQLKTDLPSFRPGDTLRVHVKVVEGTRERIQIFEGVVIKRRGGGISETFTVRKVSYGVGVERTFPIHTPRIAKIEVLRRGKVRRAKLYYLRNLRGKAARIKEIR
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.
A7GRH0
Q9CCN9
GNGF_MYCLE
Putative gluconeogenesis factor
Mycobacterium
MISPGSPPSIVALGGGHGLYVTLSAARRLTPYVTAIVTVADDGGSSGRLRSELGVVPPGDLRMALAALASDSPYGRLWATILQHRFGGSGALAGHPIGNLMLAGLSEVLADPVAALDEVGRILGVKGRVLPMCPIALQIEADVSGLEADPRIFRLIRGQVAIASTPGKVRRVRLLPVDPPATRQAVDAIMAANLVVLGPGSWFTSVIPHVLVPGLVTALRATTARRALVLNLAAGPGETAGFSVERHLHVLAQHAPGFTVHDIIIDADRVPNNREREQLRRAATLLQAEVHFVDVARPGTSLHDPGKLATALDGVRVGNQDSSAPTVAATEQIRLDGKRPQTGVNGPVGKGPRGDDAWR
Required for morphogenesis under gluconeogenic growth conditions.
Q9CCN9
Q5M2U9
MRAY_STRT2
UDP-MurNAc-pentapeptide phosphotransferase
Streptococcus
MTMSLIAGVAAFVLTVLAMPHFITYYKIKKIGGQQMHEDVKQHLAKAGTPTMGGTVFLVVAILISLIFNFHVFTEGHPAYGATAGILFVILIYGIIGFLDDFLKIFHQINEGLKPWQKMALQIVAGLLFYFIHVLPSGTNSLAIGGLTIQLGVFYVLFVLFWIVGFSNAVNLTDGIDGLASVSVVISLIAYGIIAFVKGELAILTIIITMIGALLGFFVFNHKPAKVFMGDVGSLSLGAMLAVISIALRVEWTLLLIGVVYVLETASVMLQVSYFKYTKRKYGEGRRIFRMTPFHHHLELGGISGKGEKWSEWKVDAFLWTIGALASSITLWMVLGNVMK
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.
Q5M2U9
P06310
KV230_HUMAN
Ig kappa chain V-II region RPMI 6410
Homo
MRLPAQLLGLLMLWVPGSSGDVVMTQSPLSLPVTLGQPASISCRSSQSLVYSDGNTYLNWFQQRPGQSPRRLIYKVSNRDSGVPDRFSGSGSGTDFTLKISRVEAEDVGVYYCMQGTHWP
V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition . Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens . The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen .
P06310
Q8NFJ6
PKR2_HUMAN
GPRg2
Homo
MAAQNGNTSFTPNFNPPQDHASSLSFNFSYGDYDLPMDEDEDMTKTRTFFAAKIVIGIALAGIMLVCGIGNFVFIAALTRYKKLRNLTNLLIANLAISDFLVAIICCPFEMDYYVVRQLSWEHGHVLCASVNYLRTVSLYVSTNALLAIAIDRYLAIVHPLKPRMNYQTASFLIALVWMVSILIAIPSAYFATETVLFIVKSQEKIFCGQIWPVDQQLYYKSYFLFIFGVEFVGPVVTMTLCYARISRELWFKAVPGFQTEQIRKRLRCRRKTVLVLMCILTAYVLCWAPFYGFTIVRDFFPTVFVKEKHYLTAFYVVECIAMSNSMINTVCFVTVKNNTMKYFKKMMLLHWRPSQRGSKSSADLDLRTNGVPTTEEVDCIRLK
Receptor for prokineticin 2. Exclusively coupled to the G(q) subclass of heteromeric G proteins. Activation leads to mobilization of calcium, stimulation of phosphoinositide turnover and activation of p44/p42 mitogen-activated protein kinase.
Q8NFJ6
B8G6R9
RS3_CHLAD
30S ribosomal protein S3
Chloroflexus
MGRKVHPIGFRLGYIKDWQSKWFAEGETYTKQLHEDIELRKLISKELQSAGVSRIEIERSANKIEISVYTAKPGIVIGKRGTNVDTLKSALEKKTGKKIKLNIKEISQPELDAQLVAESIGEQITKRVSYKRAMKQAVQRAMRLGAQGVKIRCSGRLAGAEMARVHEEAEGRVPRHTLRADIDYAQVHAHTTYGRIGVKVWIYKGDVFPNQSAKASVEQPATAPASERRERAPRRNSNASA
Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation.
B8G6R9
Q04KK7
OBG_STRP2
GTP-binding protein Obg
Streptococcus
MSMFLDTAKIKVKAGNGGDGMVAFRREKYVPNGGPWGGDGGRGGNVVFVVDEGLRTLMDFRYNRHFKADSGEKGMTKGMHGRGAEDLRVRVPQGTTVRDAETGKVLTDLIEHGQEFIVAHGGRGGRGNIRFATPKNPAPEISENGEPGQERELQLELKILADVGLVGFPSVGKSTLLSVITSAKPKIGAYHFTTIVPNLGMVRTQSGESFAVADLPGLIEGASQGVGLGTQFLRHIERTRVILHIIDMSASEGRDPYEDYLAINKELESYNLRLMERPQIIVTNKMDMPESQENLEEFKKKLAENYDEFEELPAIFPISGLTKQGLATLLDATAELLDKTPEFLLYDESDMEEEVYYGFDEEEKAFEISRDDDATWVLSGEKLMKLFNMTNFDRDESVMKFARQLRGMGVDEALRARGAKDGDLVRIGKFEFEFVD
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.
Q04KK7
Q9QXY4
OGFR_RAT
Zeta-type opioid receptor
Rattus
MDDPDCDSTWEEESEEDGEDGQADDTTDEDTGDDDGDAEEARPSLFQSRMTGYRNWRAMQDMQRYRHNYPDLTDQDCNGDMCNLSFYKNEICFQPNGALIEDILQNWKDNYDLLEENHSYIQWLFPLREPGVNWHAKPLTLKEVEAFKSSKEVRERLVRAYELMLGFYGFHLEDRGTGAVCRAQNFQPRFHNLNSHSHNNLRITRILKSLGELGLEHYQAPLVRFFLEETLVQHKLPSVRQSALDYFLFAVRCRHQRRELVYFAWEHFKPRREFVWGPRDKLRRFKPQTIPQPLTGPGQADKDEGSRDPSQEAGTQGRTCGSGRDLSGDSGTAEDPSLLNTKPSDGGTLDGNQRDEAKSLSPKESKKRKLEGNRQEQVPGEADPQGVSEVEKIALNLEECALSPISQEPREAEPPCPVARVANEVRKRRKVEEGAEGDGVVSNTQMQASALPPTPSECPEAQKDGNGPEDSNSQVGAEDSKSQVGPEDPNSQVGLEDPNSQVGPEDPNSQVGPEDPNSQVGPEDPNSQVGPEDPNSQVVGPEQAASKSPVEDPDSDTMGTSVDESEELARIEASAEPPKP
Receptor for opioid growth factor (OGF), also known as Met-enkephalin. Seems to be involved in growth regulation.
Q9QXY4
A4WSI3
LFTR_CERS5
Phenyalanyltransferase
Cereibacter
MTPPALTPRLLLRAYALGIFPMAESRDDPEIHWVDPRRRGIFPLDGFHISRSLARRIRRMDWTVTVNEDFAGTVRACADRDDTWINPTIFRLYVGLHALGHAHSLEVREGDALVGGVYGVTLGRAFFGESMFSRRTDASKVALAFLIDRLRAGGFTLFDTQFLTPHLASLGAIEIPRADYHRRLGEALAGKAEFAPPGYSPDPASVVQRSSQTS
Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
A4WSI3
E3PJ87
GSPC2_ECOH1
Type II secretion system protein C beta
Escherichia
MARVVFRDARIYLIQWLTKIRHTLNQRQSLNTDKEHLRKIVRGMFWLMLLIISAKVAHSLWRYFSFSAEYTAVSPSANKPPRADAKTFDKNDVQLISQQNWFGKYQPVATPVKQPEPASVAETRLNVVLRGIAFGARPGAVIEEGGKQQVYLQGERLDSHNAVIEEINRDHVMLRYQGKIERLSLAEEGHSTVAVTNKKAVSDEAKQAVAEPAASAPVEIPTAVRQALTKDPQKIFNYIQLTPVRKEGIVGYAVKPGADRSLFDASGFKEGDIAIALNQQDFTDPRAMIALMRQLPSMDSIQLTVLRKGARHDISIALR
Involved in a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of folded proteins across the outer membrane.
E3PJ87
Q5KXA4
NUSB_GEOKA
Antitermination factor NusB
Geobacillus thermoleovorans group
MKRHEAREKALQALFQIDVGRIPPDEALHNVTGGGDIDPFLRQLVFGVVEHQEEIDELLRANLEKWTLERVANVDRAILRMATYEMKYADDVPVSVSLDEAVELAKKFGDWKSGSFVNGVLSKVKAALQK
Involved in transcription antitermination. Required for transcription of ribosomal RNA (rRNA) genes. Binds specifically to the boxA antiterminator sequence of the ribosomal RNA (rrn) operons.
Q5KXA4
P63336
6PGL_NEIMA
6-phosphogluconolactonase
Neisseria
MFVWHEYENAAEAAQSLADAVADALQGALDEKGGAVLAVSGGRSPIAFFNALSQKDLDWKNVGITLADERIVPTVHADSNTGLVREYLLKNKAEAAMWIPMVEDGKTETELHPDAVVDYALKHYKQPDVLVLGMGNDGHTASIFPKAPQFQTAIDGSAGVALVHTTPVTAPHERVSMTLDAIAHTGHVFLAIRGEEKKAVFDQAAQGENREYPINLVLNHQGVNCHVFYAE
Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
P63336
Q8NX16
RLMN_STAAW
tRNA m2A37 methyltransferase
Staphylococcus
MITAEKKKKNKFLPNFDKQSIYSLRFDEMQNWLVEQGQQKFRAKQIFEWLYQKRVDSIDEMTNLSKDLRQLLKDNFTVTTLTTVVKQESKDGTIKFLYELQDGYTIETVLMRHDYGNSVCVTTQVGCRIGCTFCASTLGGLKRNLEAGEIVSQVLTVQKALDATEERVSQIVIMGIGEPFENYDEMMDFLRIVNDDNSLNIGARHITVSTSGIIPRIYDFADEDIQINFAVSLHAAKDEVRSRLMPINRAYNVEKLIEAIQYYQEKTNRRVTFEYGLFGGVNDQLEHARELAHLIKGLNCHVNLIPVNHVPERNYVKTAKNDIFKFEKELKRLGINATIRREQGSDIDAACGQLRAKERQVETR
Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. Confers resistance to some classes of antibiotics.
Q8NX16
Q9KTX1
ISPG_VIBCH
1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase
Vibrio
MQHESPIKRRPSTRIYVGDVPIGDGAPIAVQSMTNTRTTDVAATVAQIKSLEKVGADIVRVSVPTMEAAEAFKLIKQQVSVPLVADIHFDYRIALKVAEYGVDCLRINPGNIGNEARIRSVVDCARDKGIPIRIGVNGGSLEKDLQLKYGEPTPEALVESAMRHVDILDRLNFDQFKVSVKASDVFLAVDSYRLLAKKIDQPLHLGITEAGGARAGSVKSAVGLGMLLAEGIGDTLRISLAADPVEEIKVGFDILKSLRIRSRGINFIACPSCSRQEFDVIGTVNALEQRLEDVLTPMDVSIIGCVVNGPGEAEVSHLGLAGSNKKSAFYEDGVRQKERFDNDDLVAQLEAKIRAKAARLDEKNRIDIKHVEQD
Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.
Q9KTX1
Q85FN7
PSBK_ADICA
Photosystem II reaction center protein K
Adiantum
MTVSYSIYLENSLHFGDALLAKLPEAYAIFDPIVDVMPVIPVFFLLLAFVWQAAVSFR
One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
Q85FN7
D3EZK2
FTSH3_CONWI
ATP-dependent zinc metalloprotease FtsH 3
Conexibacter
MTGDPPERRSNGDRLPAERPPSNEGQTPPRKPGRNEPGSPPDWRVTPAPDGRGTPRRGRNGGGMRPFRFPGGRWGILVFILVLLGLNWWISSNALAPSERVRVPYSPNFIQQVRDGNVKEISSTGASIQGDFRADVTYPPKDDKDSVTAKKFSTEVPAFADTDELSKLLQDNDVTVNASPADNGPSLLVSILLGFGPVILIIALFVFLSRRMAGAAGGGMMSFGRSRARRSEGGEAQVTFRDVAGIDEAEAELNEIVDFLKNPQKYQRLGGKIPKGVLLSGQPGTGKTLLARAVAGEAGVPFFSMSASEFVEMIVGVGASRVRDLFRQAKEAAPAIIFIDELDAIGRARGGGRGSFGGNDEREQTLNQILTEMDGFEPTTAVIVIAATNRPEILDAALLRPGRFDRRVTVAAPDRNGRLMILKVHTRSVPLADDVDLESIASSTPGMVGADLANLVNEAALLAARRGHVKVTNSDVADALEKVVLGAERKVMMSDDDRRRTAYHESGHAIVGMLTAGADPVRKVSIIPRGQALGVTFSSPDADKYNYDERYLVGKIKVALGGRVAEEIVFGDLTTGAESDIQQLTGIARQMVGRWGMSRAIGPIAVLPSEGNGPLLPGVAETSESTQRLVDEEVRRIVDSAHAEVTRLLREHRANLDSLVAGLLDQETLDEADAYEAAGLEHMRPERVEPPAPRPSRRDGGRSVAAGPVPHGLEAPERPAQIAAPGADEPEPPTNGSGELGGSVRAGDA
Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
D3EZK2
A4XKA5
DNAJ_CALS8
Chaperone protein DnaJ
Caldicellulosiruptor
MAQKKDYYEILGVPRNATQEEIKRAYRRLAKQYHPDANPGNKEAEEKFKEINEAYEVLSDPEKRRKYDQFGHAAFDPTYGAQGGGFSGGFTGGFADFDFGSFGDIFEDLFEGFDIFGSSRRRKEAPRKGADIQVDLELTLKESVFGCEKEIPIYRTEKCSVCGGSGVRPGATPVRCQKCGGTGQIRSRQATFFGEFTTIKTCDACGGVGTIITDPCRECGGTGTVRRQRRVKINIPAGIDDGQVITLGGEGESGIKGGPNGDLHIRIKIAPHPVFKRVGQDLYVEVPITFVNAALGGEIEIPTLDGKTKIRVEPGTQNGDEVRIKGKGVPYLRGRGRGDLVVKFVIEVPKKLSEKQKELLRKFEELSSEEGYEKRKHFWDRIREAFS
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
A4XKA5
Q17QW3
RDH14_BOVIN
Retinol dehydrogenase 14
Bos
MAVGTAAALLAALGGILWLAARRFVGSSVQRLHQGRDSGLMRGKTVLITGANSGLGRATAAELLRLGARVIMGCRDRERAEEAAGQLRREVCPAGGPDSGPNSGGAGELVVKELDLASLSSVRSFCQEMLQEEPRLDVLINNAGVFQCPYMKTEDGFEMQFGVNHLGHFLLTNLLLGLLKSSAPSRIVVVSSKLYKYGDINFEDLNSEQSYNKSFCYSRSKLANILFTRELARRLEGTSVTVNVLHPGIVRTNLGRHIHIPLLVRPLFNLVSWAFFKTPEEGAQTAVYLASSPEVEGVSGRYFGDCKEEELLPKAMDESVARKLWDISEVMVGILK
Retinol dehydrogenase with a clear preference for NADP. Displays high activity towards 9-cis, 11-cis and all-trans-retinol. Shows a very weak activity towards 13-cis-retinol. Has no activity towards steroid.
Q17QW3
Q48F01
GLPK_PSE14
Glycerokinase
Pseudomonas
MTDTQNKNYIIALDQGTTSSRAIIFDRDANVVSTAQSEFVQHYPQAGWVEHDPMEIFATQTACMTKALAQADLHHNQIAAIGITNQRETTVIWERDTGRPIYNAIVWQCRRSTEICQQLKRDGLEEYIKDTTGLVIDPYFSGSKVKWILDNVEGSRERARKGELMFGTIDTWLIWKFTGGKVHVTDYTNASRTMLFNIHTLEWDQRMLDVLDIPREILPEVKASSEVYGHSKSGIPIAGIAGDQQAALFGQMCVEPGQAKNTYGTGCFLLMNTGKKAVKSAQGMLTTIGCGPRGEVAYALEGAVFNGGSTVQWLRDELKLINDALDTEYFASKVKDSNGVYLVPAFTGLGAPYWDPYARGALFGLTRGVKVDHIIRAALESIAYQTRDVLDAMQQDSGERLKSLRVDGGAVANNFLMQFQADILGTHVERPQMRETTALGAAFLAGLAIGFWSSLDELRNKAVIERVFEPSCEEAHREKLYAGWQKAVARTRDWEPHENEE
Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate.
Q48F01
Q8RZQ8
SWT1A_ORYSJ
Bidirectional sugar transporter SWEET1a
Oryza sativa
MEHIARFFFGVSGNVIALFLFLSPVVTFWRIIKKRSTEDFSGVPYNMTLLNCLLSAWYGLPFVSPNNILVTTINGTGSVIEAIYVVIFLIFAERKARLKMMGLLGLVTSIFTMVVLVSLLALHGQGRKLFCGLAATIFSICMYASPLSIMRLVIKTKSVEFMPFLLSLSVFLCGTSWFIYGLLGRDPFIAIPNGCGSFLGLMQLILYAIYRNHKGATPAAAAGKGDAADEVEDAKKAAAAVEMADAKTNKVVADDADADADGKSADDKVASQV
Mediates both low-affinity uptake and efflux of sugar across the plasma membrane.
Q8RZQ8
B8JES4
TRMFO_ANAD2
Folate-dependent tRNA(M-5-U54)-methyltransferase
Anaeromyxobacter
MGDTRVTVIGGGLAGTEAAWQLARAGVAVELVEMKPERRSPAHVLPGLAELVCSNSLRSDNPLNAVGLLHEELRRLGSLVLGCADETRVPAGDALAVDRERFSEAVTARLTGHAGVRIVHRELEELPPPPALAVIATGPLTADALAARLAETTGGRLHFYDAIAPIVAAESIDRSIAYARSRYGKGSGDDYLNLPLDEAQYHAFVEALLQGEKVAAHGFEEPRYFEGCLPIEVMAERGLEVLAHGPLKPVGLEDPRTGRRPHAVVQLRREDVDGTAWNLVGFQTRLTWPEQRRIFRAFLPGLANAEFVRLGQIHRNTFVDAPRVLAPDLSVRAAPHLFLAGQITGVEGYVESAACGLMAARAVLDRLAGRAFRPPPPATALGALHRHLTGEAHPPGYDYQPSNVVFALFPPLTGRHRGKAGRKEAHVERARKELAPWIDSAPPTAVPAAPAAG
Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs.
B8JES4
Q2KZM3
IHFA_BORA1
Integration host factor subunit alpha
Bordetella
MGNAMLAEPRTLTKAELAELLFERVGLNKREAKDIVDTFFEEIREALARGDSVKLSGFGNFQVRDKPPRPGRNPKTGETIPIAARRVVTFHASQKLKSTVEQSGNPAEVSDDEAAE
This protein is one of the two subunits of integration host factor, a specific DNA-binding protein that functions in genetic recombination as well as in transcriptional and translational control.
Q2KZM3
P0A3A9
EFTU_RICRI
Elongation factor Tu
spotted fever group
MAKAKFERTKPHVNIGTIGHVDHGKTSLTAAITIVLAKTGGAQATAYDQIDAAPEEKERGITISTAHVEYETKNRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAKQVGVPAMVVFLNKIDMVDDPDLLELVEMEVRELLSKYGFPGDEIPIIKGSALQALEGKPEGEKAINELMDAVDSYIPQPVRATDKPFLMPIEDVFSISGRGTVVTGRVESGIIKVGEEIEIVGLKDTQKTTCTGVEMFRKLLDEGQAGDNVGILLRGTKREEVERGQVLAKPGSIKPHDKFEAEVYVLSKEEGGRHTPFTNDYRPQFYFRTTDVTGTIKLPADKQWVMPGDNATFTVELIKPIAMQEGLKFSIREGGRTVGAGVVTKINN
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
P0A3A9
Q8WUQ7
CATIN_HUMAN
Renal carcinoma antigen NY-REN-24
Homo
MGRDTRSRSRSAGRRGRRRQSQSGSRSRSRSHGRRNRRRREDEGRRRRRRRSRERRSDSEEERWQRSGMRSRSPPRPKWHSRDGSSQSDSGEEQSRGQWARRRRRARSWSPSSSASSSASPGRSQSPRAAAAALSQQQSLQERLRLREERKQQEELMKAFETPEEKRARRLAKKEAKERKKREKMGWGEEYMGYTNTDNPFGDNNLLGTFIWNKALEKKGISHLEEKELKERNKRIQEDNRLELQKVKQLRLEREREKAMREQELEMLQREKEAEHFKTWEEQEDNFHLQQAKLRSKIRIRDGRAKPIDLLAKYISAEDDDLAVEMHEPYTFLNGLTVADMEDLLEDIQVYMELEQGKNADFWRDMTTITEDEISKLRKLEASGKGPGERREGVNASVSSDVQSVFKGKTYNQLQVIFQGIEGKIRAGGPNLDMGYWESLLQQLRAHMARARLRERHQDVLRQKLYKLKQEQGVESEPLFPILKQEPQSPSRSLEPEDAAPTPPGPSSEGGPAEAEVDGATPTEGDGDGDGEGEGEGEAVLMEEDLIQQSLDDYDAGRYSPRLLTAHELPLDAHVLEPDEDLQRLQLSRQQLQVTGDASESAEDIFFRRAKEGMGQDEAQFSVEMPLTGKAYLWADKYRPRKPRFFNRVHTGFEWNKYNQTHYDFDNPPPKIVQGYKFNIFYPDLIDKRSTPEYFLEACADNKDFAILRFHAGPPYEDIAFKIVNREWEYSHRHGFRCQFANGIFQLWFHFKRYRYRR
Involved in the regulation of innate immune response . Acts as negative regulator of Toll-like receptor, interferon-regulatory factor (IRF) and canonical NF-kappa-B signaling pathways . Contributes to the regulation of transcriptional activation of NF-kappa-B target genes in response to endogenous pro-inflammatory stimuli .
Q8WUQ7
P50687
COX2_DASNO
Cytochrome c oxidase polypeptide II
Dasypus
MPYPLQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIITLMLTTKLTHTSTMDAQEVETVWTILPAVILILIALPSLRILYMMDEINNPLLTIKAMGHQWYWSYEYTDYEDLNFDSYMVPTSDLKPGELRLLEVDNRLVLPMELSIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQATLMATRPGLYYGQCSEICGSNHSFMPIVLELVPLKHFEDWSTSML
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.
P50687
B9MBA4
ATPE_ACIET
F-ATPase epsilon subunit
Diaphorobacter
MNTIHVDVVSAEESIFSGEARFVALPGEAGELGIYPRHTPLITRIKPGSVRIELPDGNEEFVFVAGGILEVQPDCVTVLSDTAIRGRDLDDQKAQEAKAAAEEALKNAKSEIDLARAQSELAVMAAQIAALRKFRQKR
Produces ATP from ADP in the presence of a proton gradient across the membrane.
B9MBA4
Q9M622
RMR1_ARATH
ReMembR-H2 protein JR700
Arabidopsis
MRLVVSSCLLVAAPFLSSLLRVSLATVVLNSISASFADLPAKFDGSVTKNGICGALYVADPLDGCSPLLHAAASNWTQHRTTKFALIIRGECSFEDKLLNAQNSGFQAVIVYDNIDNEDLIVMKVNPQDITVDAVFVSNVAGEILRKYARGRDGECCLNPPDRGSAWTVLAISFFSLLLIVTFLLIAFFAPRHWTQWRGRHTRTIRLDAKLVHTLPCFTFTDSAHHKAGETCAICLEDYRFGESLRLLPCQHAFHLNCIDSWLTKWGTSCPVCKHDIRTETMSSEVHKRESPRTDTSTSRFAFAQSSQSR
Involved in the trafficking of vacuolar proteins. Functions probably as a sorting receptor for protein trafficking to the protein storage vacuole (PSV) by binding the C-terminal vacuolar sorting determinant (VSD) of vacuolar-sorted proteins.
Q9M622
P12131
NDHH_MARPO
NADH-plastoquinone oxidoreductase subunit H
Marchantia
MMILTKNKPMIVSMGPHHPSMHGVLRLIVTLDGEDVLDCEPVLGYLHRGMEKIAENRTIVQYLPYVTRWDYLATMFTEAITVNAPEKLTNIQVPKRASYIRIIMLELSRIASHLLWLGPFMADIGAQTPFFYIFREREMIYDLFESATGMRMMHNYFRIGGVAVDLPYGWIDKCLDFCDYFLPKINEYERLITNNPIFLKRVEGIGTVTREEAINWGLSGPMLRASGVQWDLRKVDHYECYDELDWKIQWQKEGDSLARYLVRIGEMKESVKIIQQALKAIPGGPFENLEARRLNQGKNSEWNLFEYQFISKKPSPTFKLPKQEHYVRVEAPKGELGIFLIGDDSVFPWRLKIRSPGFINLQILPQLVKGMKLADIMTILGSIDIIMGEVDR
NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
P12131
Q03IJ9
ILVC_STRTD
Ketol-acid reductoisomerase type I
Streptococcus
MAVQMEYEKDVKVPALDGKKIAVIGYGSQGHAHSQNLRDTGHDVIIGVRPGKSFDKAKEDGFDTYTVAEATKLADVIMILAPDEIQQELYEAEIAPNLEAGNAVGFAHGFNIHFEFIKVPADVDVFMCAPKGPGHLVRRTFEEGFGVPALYAVYQDATGNAKDIAMDWCKGIGAARVGLLETTYKEETEEDLFGEQAVLCGGLTALIETGFEVLTEAGYAPELAYFEVLHEMKLIVDLIYEGGFKKMRQSISNTAEFGDYVSGPRVITEQVKENMKAVLADIQNGKFANDFVNDYKAGRPKLTAYREEAANLEIEKVGAELRKAMPFVGQNDDDAFKIYN
Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.
Q03IJ9
Q48864
SAIA_LATSK
Sakacin-A immunity factor
Latilactobacillus
MKADYKKINSILTYTSTALKNPKIIKDKDLVVLLTIIQEEAKQNRIFYDYKRKFRPAVTRFTIDNNFEIPDCLVKLLSAVETPKAWSGFS
Imparts immunity to sakacin-A to naturally sensitive host strains.
Q48864