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 |
|---|---|---|---|---|---|---|
Q87S09 | EX7L_VIBPA | Exodeoxyribonuclease VII large subunit | Vibrio | MLSKTNQNIFTVSRLNAEVRLLLENEMGIVWLVGEISNFSAPVSGHWYLTLKDSRAQVKCAMFRGNNRRVTFKPANGNQVLVKARLSLYEPRGDYQLIIESMQPEGDGRLQQEFEELKMKLAAEGLFAQTNKLPLPEHPKRVGIITSKTGAALYDILDVLKRRDPSLPVVIYPTMVQGDDAAIQIAQAIGRANSRNECDVLIVGRGGGSLEDLWCFNNEILARTIAASQIPIISAVGHEVDMTIADFVADVRAPTPSAAAELVSRDNSHKDQSLVAKQHKLASAMRYYLSQQKQQSAQLLHRLERQHPSYQLQRQSQQLDELDMRLRRAMQRFIDTRQQAVERKHHRLQLNSPVKHLAQQKSRLERVEHKLLDTMDRKLLTMRHQLAIAAEKLDTVSPLATLKRGYSITQTEQGKVVTSADDVKTGDLLVTRLANGEIHSTVS | Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides. | Q87S09 |
P47987 | PLLP_RAT | Plasma membrane proteolipid | Rattus | MAEFPSKVSTRTSSPAQGVGASVSAMRPDLGFVRSALGVLALLQLVLGLLVWALIADTPYHLYPAYGWVMFVAVFLWLVTIVFFIIYLFQLHMKLYMVPWPLVLLVFFVAATVLYITAFVACAAAVDLTSLRGSRPYNQRSAASFFACLVMIAYGLSAFFSFQAWRGVGSNAATSQMAGGYS | Appears to be involved in myelination. Could also participate in ion transport events as addition of plasmolipin to lipid bilayers induces the formation of ion channels, which are voltage-dependent and K(+)-selective. | P47987 |
Q9YGK5 | COLI2_CYPCA | Met-enkephalin | Cyprinus | MVRGVRMLCPAWLLALAVLCAGGSEVRAQCWEDARCRDLTTDENILNCIQLCRSDLTDETPVYPGESHLQPPSELEQAEVLEPLSPAALAPAEQMDPESSPRHELKRSYSMEHFRWGKPVGRKRRPIKVYTNGVEEESAESLPAEMRRELATNEVNHPQEDSALIQQKKKDGSYKMKHFRWSSPPAGKRYGGFMKSWDERSQKPLLTLFKNVINKEHQKKDQ | Endogenous opiate. | Q9YGK5 |
A5FIY0 | MRAY_FLAJ1 | UDP-MurNAc-pentapeptide phosphotransferase | Flavobacterium | MLYYLFEYFDKTLDVPGTGVFQYITFRSALAFMLSLLLSTIYGKRVINFLRRQQVGETVRELGLAGQNEKAGTPTMGGLIIIFATLVPVFLFARLHNIYIVLLIVTTLWMGTIGFVDDYIKIFKKDKQGLKGIFKVIGQVGLGIIVGAVLYFNPAVTVRTDTGKTDVFKTAANTTVVLPAPVEEKSTATTIPFVKNNEFDYAEVLSFMGDGYEKWAWLVFIPVVIFIITAVSNGANLTDGIDGLAAGTSAVSVLALGIFTFVSGNIIFSNYLNIMYIPNSGEMTVFISAFVGALIGFLWYNSFPASVFMGDTGSLTIGGIIAVLAIAVRKEILIVLFCGIFLAESASVIIQVTYFKYTKKRFGEGRRIFLMSPLHHHYQKKGYHESKIVTRFWIVAVMLAILSIVTLKLR | 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. | A5FIY0 |
A9MXG7 | WECG_SALPB | UDP-N-acetyl-D-mannosaminuronic acid transferase | Salmonella | MTNNAAAPLYSLRGLPLIGWRDMSHALNYLFADGQLKQGTLVAINAEKLLTAEDNPEVRALIAAAEFKYADGISVVRSIRKKFPQAQVSRVAGADLWEALMARAGKEGTPVFLVGGKPEVLAQTEAKLRTQWNVNIVGSQDGYFTPEQRQALFARIHASGAKIVTVAMGSPKQELLMRDCREVHPHALYMGVGGTYDVFTGHVKRAPKIWQNLGLEWLYRLLSQPRRITRQMRLLRYLRWHYTGDL | Catalyzes the synthesis of Und-PP-GlcNAc-ManNAcA (Lipid II), the second lipid-linked intermediate involved in enterobacterial common antigen (ECA) synthesis. | A9MXG7 |
B0UMS9 | PROA_METS4 | Glutamyl-gamma-semialdehyde dehydrogenase | Methylobacterium | MSVLSLKPRAGADDVDALMREIGRRARAASRRMALVPARAKDMALRAAAAAIRDAAPVILEANAADLAEARGANLPAATLDRLALTPGRVEAIAAAVEAIAGLPDPVGRQLAAFERPNGLAIERISTPLGVVGVIYESRPNVTADAGALCLKAGNAAVLRAGSESLRSAAAIARAMADGLAAQGLPAEAIQLVPTRDRAAVGAMLAGLDGCIDVIVPRGGKSLVARVQSEARVPVFAHLEGICHVFVHARADLAMAREILRNSKLRRTGICGAAETLLVDRACAGTHLAPLVADLLEAGCAVRGDAETQAVDPRVTPATEADWRTEYLDAVIAVRVVDGLDAAIDHVETYGSHHTDAIVTADEAAAERFLAEVDSAIVVHNASTQFADGGEFGFGAEIGIATGRMHARGPVGVEQLTTFKYRVHGSGQVRP | Catalyzes the NADPH-dependent reduction of L-glutamate 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate. | B0UMS9 |
Q9PU47 | PDLI3_CHICK | Alpha-actinin-associated LIM protein | Gallus | MPQNVILPGPAPWGFRLSGGIDFNQPLIITRITPGSKASTANLCPGDIIVAINGLSTENMTHNDAQERIKAAAHQLSLRIERAETKLWSPQVSEDGKANPYKINLEAEPQEFKPIGTAHNRRAQPFVAAANIDDKRQVVSSSYNSPIGLYSSGNIQDALHGQLRSLIPNASQNDPAPAAVPQSDVYRMLHSNQEEPSQPRQSGSFKVLQNLVSEEDGRPVGTRSVKAPVTKIPTGLPGAQKVPQCDKCGSGILGTVVKARDKYRHPECFVCSDCNLNLKQKGYFFVEGQLYCEAHARARMRPPEGYEAVTVYPKC | May play a role in the organization of actin filament arrays within muscle cells. | Q9PU47 |
B8GBH2 | FABZ_CHLAD | Beta-hydroxyacyl-ACP dehydratase | Chloroflexus | MLSIQEIMALIPHRYPFLLVDRIVELEPGVRAVGEKLVSANEPYFQGHFPGNPIMPGVLILEALAQTGAVAALSLPEHAGKLVLFAGIDGARFKRVVRPGDTLRLEVQLERMRRGIGKGQARATVADQLACEAELLFAVTDPTK | Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs. | B8GBH2 |
Q3J474 | DTD_CERS4 | Gly-tRNA(Ala) deacylase | Cereibacter | MRALIQRVSEASVTVEGELLGEIGPGLLILVCAMQGDGEAQASALAARIAKLRIFRDEAGKMNRSVRDTGGAALVVSQFTLAADTSRGNRPGFSAAAPPADGERLYRHFAAEIAACGIPTATGRFGADMKVRLLNDGPVTIWMET | An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo and helps enforce protein L-homochirality. | Q3J474 |
A0A2K9RFZ8 | TPS3_VITAC | Terpene synthase 3 | Vitex | MCSLSTLSPNFSNAYGSKSVSSTASRFPCWQRSNETWKTQSREVIHWTYVVRCKEVLNEARQGHMNLPHVTLQNDLCEREALKEDMPLLNEYKMEECIRYIKNMLGSMDDGRITVSPYDTAWIALIRDIEGRDIPQFPSSLEWIANNQLSDGSWGDEQFFLAYDRLLNTLACVVALTYWKVHADKSEKGILFIKENISKLGDANVEQMTCGFEVVFPALLTKAKDLGIHGIPYDAPVMQEIFATKDRKMERVPKELLHKVPTCLLHNLEGLGNVDALGKLDWPKLLKLQTPKGSYITSPAASAFAVMETKDKDCLAFINYVVNKFNGGAPTVYPVDIYARLWAVDRLQRLGISRFFEPEIKNCLDYVYRFWTEKGVFSARESEFCDIDDTSMSIRLLRLHGYDIKPNALKHFKKDNMFTCYVGQGFESPSPIFNLYRASQVLFPGETILEEARDFSYNFLRERLEKNDLLDKWLISKHLPDEIKCGLEMPWYASLPRVEARFYIENYGVDDIWIGKSLYRMPEINDPVYLELAKLDYKRCQTQHQLEWRHIQQWYEDSSLEEFGISKKDLLLAYFLAAASIFEPGRSGQRLAWVKSQIMSHILTTYFSIKEASSSEQRKSSTKLENEQGRGQSRKTTIQRFITIFFGSLQEIMRDANEQIGKDISNLLFDIWRVWLEKLGEGNEEIQEVELLVSTINICGGHIASKDILSHSEYKTLSRLTNKICHQLRQLDMGNEELIAIEWRKNKTTDSIYREIEKDMQLLVQLVLQDSSNGISKDIKQTFLLAAKTFYYRAYFPTEQIGNHISKVLFEPVV | Involved in the biosynthesis of labdane-type diterpenoid including cleroda-dienols, and peregrinol lactones and furan derivatives, dopaminergic diterpenoids that can bind to dopamine receptors in the human pituitary gland, have probably ability to lower prolactin levels, and are used to treat menstrual cycle disorders (e.g. premenstrual syndrome and mastodynia) (Probable). Terpene synthase that produces syn-copalyl diphosophate from geranylgeranyl diphosphate (GGPP) . | A0A2K9RFZ8 |
C5D5M0 | LEU1_GEOSW | Alpha-isopropylmalate synthase | unclassified Geobacillus | MRKINIFDTTLRDGEQSAGINLNLQEKLEIARQLERLGVDIIEAGFPASSKGDFQAVKQIAETIKTCSVTGLARSVQSDIDAAWEALKGGAEPRLHLFIATSPIHMKYKLQMTPEQVIETAVESVKYAKRYFPIVQWSAEDACRSELPFLAKIITEVIKAGATVINIPDTVGYITPKEYGNIFTFLSNNVPNIEKVSLSAHCHDDLGMAVANSLAAIEHGATQIEGTINGIGERAGNAALEEIAVALYIRKDYYQAETRLNLQEIKRTSNLVSKLTGVVIPPNKAVIGKNAFAHESGIHQDGVLKEKTTYEIISPELVGVQSNSMVLGKHSGRHALRNRVEELGYTLSDEEVNKLFVRFKELADKKKDITDDDLVALIFEEKFDHFKDFYQLSSLQVQYGTNQIPTAVVVLKDGQGNEIQEAATGAGSVEALYNTLERCFKTSVTLLDYRIESVSGGRDALAQVFVKVRVNDIETSGRGTAQDVLEASAKAYINAVNRVFMIETMRAENQKVAMQ | Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate). | C5D5M0 |
P45606 | PHOB_SHIDY | Phosphate regulon transcriptional regulatory protein PhoB | Shigella | MARRILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKRESMTRDIPVVMLTARGEEEDRVRGLETGADDYITKPFSPKELVARIKAVMRRISPMAVEEVIEMQGLSLDPTSHRVMTGEEPLEMGPTEFKLLHFFMTHPERVYSREQLLNHVWGTNVYVEDRTVDVHIRRLRKALEPGGHDRMVQTVRGTGYRFSTRF | This protein is a positive regulator for the phosphate regulon. Transcription of this operon is positively regulated by PhoB and PhoR when phosphate is limited. | P45606 |
C3P8W4 | TATA_BACAA | Sec-independent protein translocase protein TatA | Bacillus cereus group | MFSNIGFPGLILILVAVLILFGPKKLPEIGKALGETLKEFKKSTKELTDDAFQEKEKKEKM | Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system. | C3P8W4 |
Q7VL12 | BIOD2_HAEDU | Dethiobiotin synthase 2 | Haemophilus | MGKIIFVSGIDTDIGKTIATGFYAKRLMQQGFSVITQKMIQTGCQHISADIIKHRQLQGIELTAEDLNGITCPYLFRYPCSPHLAAEMENNPILPSKIAQASALLAQKYDYVLLEGAGGLAVPYNSQQTTLDYIVEQQLPLILVTSAKLGSINHTLLSLIVCQQHKIEMEAVIYNTYPLEDEKIAKSTQLYLQQYIKQHFPNTEFLVMDRQ | Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring. | Q7VL12 |
A9GXK6 | RS18_SORC5 | 30S ribosomal protein S18 | Sorangium | MNGRNNDMGRNGGADYDDRDFGRTPDLNADAPGRRRTGRKRVCRYCADKALVIDYKDPQALKYFISERGKVVPRRISGNCARHQRKVTLSIKRARNIALLPFTVTA | Binds as a heterodimer with protein S6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit. | A9GXK6 |
Q1QL43 | DAPA_NITHX | 4-hydroxy-tetrahydrodipicolinate synthase | Nitrobacter | MASKTKFRGSYTALVTPFKNGSVDEAAFRSLVSWQIGEGVHGLVPVGTTGESPTLSHDEHRKVVEWCIDEARGRVPVIAGAGSNSTREAVDLAVHAEKAGADAVLVVTPYYNKPTQEGMYHHFKTVNDAIGIPIIIYNIPSRSVVDLSVETMARLFELKNIAGVKDATANVARVSLQRHAMGPDFIQLSGEDMTALAFMAAGGHGCVSVVANVAPKLCASLMSAVLKGDYATGLAIQDRLVPLHAAIFKEPGLAGAKHGLKLLGRLDEVVRLPLLPVTPPTGKVIRDAMVHAGLLN | Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA). | Q1QL43 |
Q3Z1P4 | SAFA_SHISS | Two-component-system connector protein SafA | Shigella | MYATTVKNKITQRDNYKEIMSVIVVVLLLTLTLIAIFSAIDQLGISEMGRIARDLTHFIINSLQD | Connects the signal transduction between the two-component systems EvgS/EvgA and PhoQ/PhoP, by directly interacting with PhoQ and thus activating the PhoQ/PhoP system, in response to acid stress conditions. | Q3Z1P4 |
Q49KZ2 | ATPE_EUCGG | F-ATPase epsilon subunit | Eucalyptus | MTLNLCVLTPNRIVWDSEVKEIILSTNTGQIGVLPNHAPIATAVDIGILRIRLNDQWLTMALMGGFARIGNNEITILVNDAEKGSDIDPQEAQETLELAEANLRKAEGKRQTIEANLALRRARTRVEAINAIS | Produces ATP from ADP in the presence of a proton gradient across the membrane. | Q49KZ2 |
B3QBW6 | RS8_RHOPT | 30S ribosomal protein S8 | Rhodopseudomonas | MSTHDPISDLITRIRNAQMRSKSKVSTPGSKMRANVLDVLKAEGYIRGYATVEHPSGRSELEIELKYFDGEPVIREIERVSRPGRRVYASVKNLPRVNNGLGISVLSTPKGIMADHDARDANVGGEVLFTVF | One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit. | B3QBW6 |
A0LPG9 | ISPE_SYNFM | 4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase | Syntrophobacter | MRGIRKGHALALRVGTPAKINLWLEIVRKREDGYHDLSSLMLPVAVYDHVEVAWSHEGGVRLSCDSAEVPDDRGNLAWRAADAYLEAAGVTRGVSIRLEKNIPVGAGMGGGSSDAAAVLLALNRLSENPLSEAVLHRLAVGLGADVPFFLHCVPALATGIGERLLPVHGIPDYPLLLVKPPISVSTGWVYGSLKLTRGESRIKLRSFLDRPWHLSEVLRNDLETVTLNEYPQLGQIKCWLMENGAVGSLMSGSGPTVFGVFAEQRLADGAGELARRVWKDCRVDVTRVLGTPVSARS | Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol. | A0LPG9 |
Q66KJ9 | MET14_XENTR | Methyltransferase-like protein 14 | Silurana | MNSRLQEIRARQTLRRKLLAQQLGAESADSIGAVLNSKDEQREIAETRETSRASYDTSATVSKRKMPEEGEADEEVIEECKDAVEPQKEEENLPYREEIYKDSSTFLKGTQSLNPHNDYCQHFVDTGHRPQNFIRDVGLADRFEEYPKLRELIRLKDELISKSNTPPMYLQADLESFDLRELKSEFDVILLEPPLEEYFRETGIAANEKWWTWEDIMKLDIEGIAGSRAFVFLWCGSGEGLDFGRMCLRKWGFRRSEDICWIKTNKDNPGKTKTLDPKAIFQRTKEHCLMGIKGTVHRSTDGDFIHANVDIDLIITEEPEIGNIEKPVEIFHIIEHFCLGRRRLHLFGRDSTIRPGWLTVGPTLTNSNFNSETYASYFNTPNSPLTGCTEEIERLRPKTPPPKSDRGFGASRGGGRGGPSAGRGERGRERNRGSFRGDRGNFRGRGGPHRGVFAPR | The METTL3-METTL14 heterodimer forms a N6-methyltransferase complex that methylates adenosine residues at the N(6) position of some mRNAs and regulates the circadian clock, differentiation of embryonic stem cells and cortical neurogenesis. In the heterodimer formed with mettl3, mettl14 constitutes the RNA-binding scaffold that recognizes the substrate rather than the catalytic core. N6-methyladenosine (m6A), which takes place at the 5'-[AG]GAC-3' consensus sites of some mRNAs, plays a role in mRNA stability and processing. | Q66KJ9 |
C4YH38 | IRC6_CANAW | Increased recombination centers protein 6 | Candida | MIPNHILILGSPNSGKLRIANLISKNEEIPNLEDVELHSGLIVKASLRTKYYFLKLNILIDEYSESKGATDEKKLSELHKWYQEFKSEEFGELREVLDGLMFTINMKTDSISFIRDALEIIEQIKISLGDEENLHDWGGFIAVVGSCPENQIVEDDLILEIEDMVLSQGLEFINLSTEGENEYKEKQGKDRIVELIESHDWTNLEMLKVDSKQYETNKLAKMESMKQKLINEKEELDLDDIFSKLNLARDHAQSLTQDERDKYANKVIEEIIDFL | Involved in gross chromosomal rearrangements (GCRs) and telomere healing. | C4YH38 |
B9MBT7 | GLPK_ACIET | Glycerokinase | Diaphorobacter | MTYLLALDQGTSSSRSIVFDERGRIVAQAQRELPQIYPRPGWVEHDPREIWRTQLATAQDALREARITAQDVRALGITNQRETTVLWNRRTGQPVHHAIVWQDRRAEPACAQLREQGHAAAIQAKTGLLIDAYFSGTKLQWLLDHVPGARDAAEAGELAFGTVDSWLIWQLTGGTRHVTDVSNASRTMLFNVHTNQWDDELLQLLRIPRALMPEVLPSASDFGATDAALLGGPIAIGGVAGDQQSALFGQACFTAGMAKNTYGTGCFMLMHTGSRFQKSENGLLTTSAAQASRSPEYAMEGSVFVGGAVVQWLRDGLRAISASSEVQALAESVPDSGGVMMVPAFTGLGAPYWKPDARGTITGLTRGTTIAHIARAALESIAYQSAALLAAMSRDAVAAGGAPVSELRVDGGACVNDLLMQFQADLLGIPVVRPAVVETTALGAAYLAGLASGVYASTDELSALWQAERRFTPTLPRSQAEALMARWEHAVAQAVLPG | Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate. | B9MBT7 |
Q96376 | LIS_CLABR | S-linalool synthase | Clarkia | MQLITNFSSSSSELQFLVDKVKRESLSSSSSNTQNLFLSTSPYDTAWLALIPHPHHHHHHGRPMFEKCLQWILHNQTPQGFWAAAGDNISDTDDDVTLDCLLSTLACLVALKRWQLAPDMIHKGLEFVNRNTERLVMKQKPSDVPRWFTIMFPAMLELAGASSLRVDFSENLNRILVELSQNRDDILTREEVDEKKQYSPLLLFLEALPAQSYDNDVLKQIIDKNLSNDGSLLQSPSATARAYMITGNTRCLSYLHSLTNSCSNGGVPSFYPVDDDLHDLVMVNQLTRSGLTEHLIPEIDHLLLKVQKNYKYKKASPKSLYSIAAELYRDSLAFWLLRVNNHWVSPSIFCWFLDDDEIRDHIETNYEEFAAVLLNVYRATDLMFSGEVQLVEARSFATKNLEKILATGNIHKTNADISSSLHKMIEHELRVPWTARMDHVENRIWIEEIASSALWFGKSSYLRLSCFHKMSLQQLAVKNYTLRQLVYRDELAEVERWSKERGLCDMGFCREKTGYCYYAFAASTCLPWSSDVRLVLTKAAVVITVADDFFDVEGSMVDLEKLTDAVRRWDAEGLGSHSKTIFEALDDLVNEVRLKCFQQNGQDIKNNLQQLWYETFHSWLMEAKWGKGLTSKPSVDVYLGNAMTSIAAHTMVLTASCLLGPGFPVHQLWSQRRHQDITSLLMVLTRLLNDIQSYLKEEDEGKINYVWMYMIENNQASIDDSVRHVQTIINVKKQEFIQRVLSDQHCNLPKSFKQLHFSCLKVFNMFFNSSNIFDTDTDLLLDIHEAFVSPPQVPKFKPHIKPPHQLPATLQPPHQPQQIMVNKKKVEMVYKSYHHPFKVFTLQKKQSSGHGTMNPRASILAGPNIKLCFS | Involved in the biosynthesis of the acyclic monoterpene S-linalool, a major component of the strong sweet scent of the C.breweri flowers. | Q96376 |
Q6B8R6 | RPOC2_GRATL | Plastid-encoded RNA polymerase subunit beta'' | Agarophyton tenuistipitatum | MTQDKSIEPFFLNKVVDKSQLRQLIIWAFRNYGIARASNMADTLKDLGFLYATKAGISLSLEDLRIPPAKNNLLKTTIDLINDTDTKYRKGEITAVERFQKVIDTWNSASDTLKKQVIKYFTEKDPLNSIYMMAFSGARANISQVRQLVGMRGLMADPQGQIIDLPISSNFREGLTITDYFISSYGARKGLVDTALRTADSGYLTRRLVDVAQDVIIREADCNTSKGIVLESMIDNRKTLVSLHQALIGRVLAEDLFNPAGSKLVAKLNTEISPDLANEIISLGISSVLVRSPITCESIKSVCQSCYGWNLAHGRIVDLGEAVGIIAAQSIGEPGTQLTMRTFHTGGVFTGELAQTVISSSDCQVEYPSNIILSDTRTRHGDHAFLVEKDIKLKLLDFNKKQTSLSLVKGSLLFVKHLEYITSGQVIAEYPISNRLITEKAQKAVLADFSGSIYLMDLSVSNIQSEQQTFKNVIKGGVIWILAGHVFSIPYNTQLIISENDFIDENHLIGKTEFVSRYEGRVRILKKKQDFIQDIVIITSSKTYINIDVLTKFYNGYTNHFLITNQQDKFILKTLPNQTIVDQQLIAELITNIYRTNTGGIIKYLDLSVSDKKVDLNSKKDYYDIVDGGYVLWIGEETHEINKDISLLLVSHGQLIDEGTEIVKNIFTNSSGIVDIIQKEGIVREIIIKPGILYPHSKFYDHKSKSRGFLKPGEIISNDLKTDKLVYWEYFYVKNQSYTLIRPVIVYSIPSKTIQFKYSADSFNSHICSLKLVKRIYFRDGERVKSVSGIDIVKTYLIAELNKDSLNLKCTLQLNLDSNNRSISRMRIVTMDKLSLKDENNIASTKDLYTRTRLLVTNNQYIKSGTVVAQTELFSSLEGQVVSIQKNKSSNPRILLITSLDTKVFSINNNQNIKVNINDLIYAGDEIATNIISYISGQVISIRDNQITVRLGQPYLISEGSFLHVNNQALIQRGENIATLIFERVKTGDIVQGLPRIEEILEARKKSDSFFNPHVVLDSKFRQYVNQGLNLYDATRLSLLILQLYLVKELQLVYQSQGVEIADKHIEVIVRQMTSKVKIENGGDTDHLPGEIIELQKIEMLNKALRLASKEEALYYPILLGITKASLNTESFISAASFQETTKVLTDAAISCKLDWLRGLKENVIIGRLIPAGTGFNIYNNMQLNYQDEKYSYTKNLLSLPQNTKNLNFEDIIVDDRNAHMYSRNNNL | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | Q6B8R6 |
P33739 | MS2B_DROSE | Male accessory gland secretory protein 355B | Sophophora | MNYFAVLCIFSCICLWQFSDAAPFISVQSSSQSRSQKVMNGMLRTLYDYSVQDSVNDATGHLIHTHKSNFNSDVMSPEEIERVRQQLNMA | This protein is transferred from male to female during mating and may affect egglaying and behavior after mating. | P33739 |
A8F7A0 | MINC_PSELT | Probable septum site-determining protein MinC | Pseudothermotoga | MTIDLIDFKMTKEGLVLVIKDYDNLEDVVNQLTSKISQMSGFFAAGDKIMLMIENNEKHSHDMPRIISILKKMGIEVSQILMGVTAKEGINVRGRMKMVEEGETKSGTKVVKKNLRSGQALVHSGDVIVIGNVHSGAEIMAGGSIVVFGNVKGILRAGLNESDSIVAALSMEPSLIQISEYILREAGSYDEPVVVHVKQNKIVIESAKDVKFQ | Cell division inhibitor that blocks the formation of polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings. Prevents FtsZ polymerization. | A8F7A0 |
A1WVM7 | BIOB_HALHL | Biotin synthase | Halorhodospira | MTETDTWHWDQPQIHALFELPLPELLFRAQEVHRRHFNPGQVQACTLVSIKTGACAEDCTYCSQSARYDTGLEREALIDVETVREAAQRARASGATRLCMGAAWRGPKDRDLETLVAMVRAVKAEGLEACLSAGLLAEGQAERLAEAGLDYFNHNLDTSPSYYDQVVTTRSYEQRLQTLERIRDAGMRVCCGGIVGLGEARADRVEMLATLANLPVPPQSVPINRLIPIPGTPLEAAEPVDPFEIVRTIAATRLVLPRSYVRLAAGREQMSDELQALCLSAGANSLFLGERLLTTDNPDADADHRLLHRLGMTLEPRTHSCAELEP | Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism. | A1WVM7 |
Q28934 | IAPP_SAGOE | Amylin | Saguinus | NTATCSMHRLADFLGRSSNNFGAILSPTNVGS | Selectively inhibits insulin-stimulated glucose utilization and glycogen deposition in muscle, while not affecting adipocyte glucose metabolism. | Q28934 |
A0RUZ0 | EF1B_CENSY | aEF-1beta | Cenarchaeum | MAQLLVIVKILPKGTEVDLDEMMEGLKGGLKGGIVLRRYAKEPLAFGLHFVKAEFILEDKEGQNDALEATVRSAKGVSEYEVLNMSRMSVDMK | Promotes the exchange of GDP for GTP in EF-1-alpha/GDP, thus allowing the regeneration of EF-1-alpha/GTP that could then be used to form the ternary complex EF-1-alpha/GTP/AAtRNA. | A0RUZ0 |
Q9HS17 | GLCDH_HALSA | Glucose 1-dehydrogenase | Halobacterium | MDAIVVSKADRTPRLVDRPRPDPTPGSVLVRTLRVGVDGTDHEVIAGTHGGFPEDADELVLGHEAIGVVADPTDTRFSAGQLVAPTVRRPRGDPTPQFDRGQPDMAAPGTYVERGIDGADGFMADYFTSPADALVALPDSLAAHGFLTEPVSVAEKAIELALASRSAFDWRPDSALVLGNGSLGLLTLAILAARDDTETLYCLGRRSRPDPTIDIIERLGATYIDSRTTPVADIPAAHQPVDMVYEATGHAKHAFDAIDALAPAGVAALLGVPAAGWTFEVPGSDLHRSLVLENKAVVGSVNSNARHFRAAADTLAALPDWLCDAIVTGVHDTAAFADAFRDGETSIKTAVQFDTR | Catalyzes the NAD(P)(+)-dependent oxidation of D-glucose to D-gluconate via gluconolactone. Can utilize both NAD(+) and NADP(+) as electron acceptor. Is involved in the degradation of glucose through a modified Entner-Doudoroff pathway. | Q9HS17 |
Q5ZT08 | TSAD_LEGPH | tRNA threonylcarbamoyladenosine biosynthesis protein TsaD | Legionella | MLVLGIESSCDETGVAVYDSESGLLSHALHSQIATHRVHGGVVPELASRDHVNYLVPLVDEVLTKAQIRKNQLDGIAYTAGPGLIGALLVGSCFAKSLAYALNIPALAIHHLEAHLLAAKMETPSLDFPFIALLVSGGHCQLIEVNNIGEYRLLGDTLDDAVGEAFDKTAKLMGIPYPGGAVLANLADQCLSTPYQFPRPMTDRPGLDFSFSGLKTHALNTWNQSEKKESDRSEIAKAFQQAVVETLIIKCKRAIKESQSKRLVVAGGVGANKALRSALQKWIKDIQGEVYFPALEYCTDNGAMVAYAGCLRMMRGEIDGGLGVIVKPRWPLA | Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction. | Q5ZT08 |
Q38X21 | PYRF_LATSS | OMP decarboxylase | Latilactobacillus | MTNPVIIALDFPNWQKTDQFLQQFPKDEALFVKIGMELFYQEGPQLIKTLKARDYRIFLDLKLYDIPNTVQSAMTVIGQLGVDYTTIHAAGGQTMLQAGAAGLKAGAKQANVKPAKLLAITQLTSTNEAQMQQEQLVSVSLPESVAHYAQLAQQSDCDGVICSAQEITTIKSKTATDFLCVTPGIRPATSQNNDQKRAVTPLEAAQMHSNGIVVGRPITQASDPYQAYQAIKSEWESFK | Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP). | Q38X21 |
P55305 | CATA_EMENI | Spore-specific catalase | Aspergillus subgen. Nidulantes | MATSITAGLQKAQQAVQDTATKNKKIVDISHDTVNVHTDQEQRTDFGVAITDPDHWLRVTNETHSGPSLLEDHIARERIHRFDHERIPERVVHARGTGAYGNFTLKESIEDLTYAGVLTDTSRNTPVFVRFSTVQGSRGSADTVRDVRGFAVKFYTDEGNWDIVGNNIPVFFIQDAIKFPDFVHAVKPEPHNEVPQAQTAHNNFWDFVYLHPEATHMFMWAMSDRAIPRSYRMMQGFGVNTFSLVNKEGKRHFVKFHWIPHLGVHSLVWDEALKLAGQDPDFHRKDLMEAIDNKAYPKWDFAIQAIPEEDQDKFEFDIFDATKVWPEEQVPLRVVGELELNRNIDEFFPETEQVAFCTSHIVPGIDFSDDPLLQGRNFSYQDTQISRLGVNWEEIPINRPVCPFLNHNRDGAKRHRITKGTVNYWPNRFEANPPASDKGFKSHPAPITGRKRRDLTPKFKEYHNQAQLFYNSLSEVEKVHVKKAFSFELDHCDDPIVYERLAGQRLAEIDLPLAQAVAEMVGAPIPTKALRDNHGKTSVRLSQFDFTPKAPGIISRRIAIIIGDGYDKIAFNGMKAAILAAQALPFVIGTKRSAIYAQGEDKNSSKGVIPDHMYDGMRSTMFDATFIPGGSHIETLQKNGQIRYWIAETFGHLKALGAMGEAAQLVKEVLGNVMGVQIAGADSAEPVEWYGVVTARGPESAESLSEGFKVLKDAGDFTSKFFYQISQHRNWQRELDGLASTVAF | Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. | P55305 |
A0T0K5 | RR7_PHATC | 30S ribosomal protein S7, chloroplastic | Phaeodactylum | MSRRNISKKRFPETDAIYNSYLVSLLISRILKSGKKTIAKKIVYQAFDIIKKKTNEDPLTVFEKAIRNASPIVEVKARRVGGSTYQVPVEVTGFRATNLSLRWIIRYGDQRVGRSMAIKLANEIIDTANDIGNTIKKKEETHKMAEANKAFAHFRY | One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. | A0T0K5 |
Q21A81 | AROC_RHOPB | 5-enolpyruvylshikimate-3-phosphate phospholyase | Rhodopseudomonas | MSFNTFGHMFRVTTFGESHGVAIGCVVDGCPPLIALTEADIQRDLDRRRPGQSRFTTQRQEADQVKILSGVMVHPQSGLQVTTGAPIALLIENTDQRSKDYSEIKDKFRPGHADFTYEAKYGIRDYRGGGRSSARETATRVAAGAIARKVVPGITVRAALVQMGPHQIDRDNWDWEEVGNNPFFCPDKDKAKFFEDYLDGIRKNGSSIGAVIEVVADGVPAGWGAPIYAKLDTDIAAALMSINAVKGVEIGDGFATAALTGEQNADEMRAGNDGPSFLSNHAGGILGGISTGQPVVARFAVKPTSSILAPRKTVDRDGHDTDILTKGRHDPCVGIRAVSVAEAMVACVLADHLIRHRGQIGG | Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. | Q21A81 |
P56738 | CFPA_TREPH | Cytoplasmic filament protein A | Treponema | AILELPQSPNVFHPEKPSAVG | Component of the cytoplasmic filaments that run the length of the organism just underneath the cytoplasmic membrane. | P56738 |
Q31JM9 | ENGB_HYDCU | Probable GTP-binding protein EngB | Hydrogenovibrio | MQHPLYQQATYLKSAPDLSHCPEDFGYEVAFAGRSNAGKSSALNVITSQRGLAKTSKTPGRTQLINFFECDEQRKLVDLPGYGYAKVNVNTKRAWERSLSQYIEVRSSLKGLIMMVDSRMPPTEIDLMMLDWTLTLNLPVHILLTKSDKLKKGPAQNSLLKMRQLLNEKYPHATVQLFSSLKRQGLDEVWAKLDEWMEYERPVKSQPETKES | Necessary for normal cell division and for the maintenance of normal septation. | Q31JM9 |
Q60CK8 | GATA_METCA | Glutamyl-tRNA(Gln) amidotransferase subunit A | Methylococcus | MHRKTLAELAAGLERREFSSVELTQAHLARIERLDPALNSFITTTPEIALAQARAADERLAKGEAGPLTGIPIAQKDIFCTKGVRTSCGSRMLDSFVSPYDACVVERFNAAGAVMLGKLNMDEFAMGSSNETSYYGPVKNPWNTATVPGGSSGGSAAAVAARLVPGATGTDTGGSIRQPAAFCGITGLKPTYGRVSRWGMIAFASSLDQAGPMARTAEDCAIMLQIMAGFDERDSTCVDRPVPDYRAALGNDLDGLRIGLPKEFFGEGLDPAIAGLIHAAVDEYRRLGAIVREISLPNMHLSVPAYYVVAPAECSSNLARFDGVRFGHRCENPTDLADLYTRSRGEGFGAEVKRRILIGTYALSAGYYDAYYLKAQKIRRLISEDFRRAFEEVDVIMGPTAPSVAFEFGAKSADPIAMYLSDIYTIAVNLAGLPGMSIPVGFSNGLPVGMQIIGGYFSEDRLLNVAHRYQQATDWHTRTPAGIAD | 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). | Q60CK8 |
P9WHQ8 | HGPRT_MYCTO | Hypoxanthine-guanine phosphoribosyltransferase | Mycobacterium tuberculosis complex | MHVTQSSSAITPGQTAELYPGDIKSVLLTAEQIQARIAELGEQIGNDYRELSATTGQDLLMITVLKGAVLFVTDLARAIPVPTQFEFMAVSSYGSSTSSSGVVRILKDLDRDIHGRDVLIVEDVVDSGLTLSWLSRNLTSRNPRSLRVCTLLRKPDAVHANVEIAYVGFDIPNDFVVGYGLDYDERYRDLSYIGTLDPRVYQ | Purine salvage pathway enzyme that catalyzes the transfer of the ribosyl-5-phosphate group from 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to the N9 position of the 6-oxopurines hypoxanthine and guanine to form the corresponding ribonucleotides IMP (inosine 5'-monophosphate) and GMP (guanosine 5'-monophosphate), with the release of PPi. | P9WHQ8 |
Q98959 | 3SA3A_NAJAT | Cardiotoxin-3a | Naja | MKTLLLTLVVVTIVCLDLGYTLKCNKLVPLFYKTCPAGKNLCYKMFMVATPKVPVKRGCIDVCPKNSLLVKYVCCNTDRCN | Shows cytolytic activity on many different cells by forming pore in lipid membranes. In vivo, increases heart rate or kills the animal by cardiac arrest. In addition, it binds to heparin with high affinity, interacts with Kv channel-interacting protein 1 (KCNIP1) in a calcium-independent manner, and binds to integrin alpha-V/beta-3 (ITGAV/ITGB3) with moderate affinity. | Q98959 |
A9VI09 | SYA_BACMK | Alanyl-tRNA synthetase | Bacillus cereus group | MKQLTGAQIRQMFLDFFQEKGHAVEPSASLVPHEDPSLLWINSGVATLKKYFDGRVIPQNPRITNAQKSIRTNDIENVGKTARHHTFFEMLGNFSIGDYFKEEAITWAWEFLTSDKWIGFDKELLSVTIHPEDEEAFTIWNEKMGVPKERIIRLEENFWDIGEGPSGPNTEIFYDRGESYGNDFSDPELYPGGENERYLEVWNLVFSQFNHNPDGSYTPLPKKNIDTGMGLERMTSIVQDVPTNFDTDLFMPMIGATESISGEKYRNGDLEKDMAFKVIADHIRTVTFAVGDGALPSNEGRGYVLRRLLRRAVRYSKKLNINRPFMFELVPVVGEVMKDFYPEVLEKKDFIAKVVKNEEERFHETLHDGESILAEVIAKAKEEKTTVISGVDAFRLYDTYGFPIELTEEYAEEAGMTVDQAGFENEMEKQRERARAARQDVDSMQVQGGVLGEVKVASEFVGYGTVATESNVVALVKNGEYTDSLQAGEEGQLMLDVTPFYAESGGQIADRGYLLADGVKVVVKDVQKAPNGQNLHKVVVEEGTLTKDAAVKAVIDTKNRSSVVKNHTATHLLHQALKDILGTHVNQAGSLVTSERLRFDFSHFGQVQADELEKIERIVNEKIWESIDVAISQKAIEEAKEMGAMALFGEKYGDVVRVVQVGDYSLELCGGCHVDNTASIGIFKIVAESGIGAGTRRIEAVTGKSAYELMNDQVGLLKEAAGKMKTNPKDILTRVDGLFTEVKQLQKENESLAAKLSNIEAGNLTDSVMTVDGVNVLAAKVNVADMNNLRTMMDDLKNKLESAVVVLASVNDDKVNILAGVTKDLISQGYHAGKLVKEVASRCGGGGGGRPDMAQAGGKNPAQVEEALAFVQEYVKSVSK | Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | A9VI09 |
Q9ZFA3 | SYE1_CERS4 | Glutamyl-tRNA synthetase 1 | Cereibacter | MPAASDKPVVTRFAPSPTGYLHIGGGRTALFNWLYARGRKGTFLLRIEDTDRERSTPEATDAILRGLTWLGLDWDGEVVSQFARKDRHAEVAREMLERGAAYKCFSTQEEIEAFRESARAEGRSTLFRSPWRDADPTSHPDAPFVIRMKAPRSGETVIEDEVQGTVRFQNETLDDMVVLRSDGTPTYMLAVVVDDHDMGVTHVIRGDDHLNNAARQTMVYEAMGWEVPVWAHIPLIHGPDGKKLSKRHGALGVEEYQAMGYPAAGMRNYLARLGWSHGDDEFFTSEQAMDWFDLGGIGRSPARLDFKKLESVCGQHIAVMEDAELMREIAAYLAAARKPALTDLQAARLEKGLYALKDRAKTFPELLEKARFALESRPIVADDAAAKALDPVSRGILRELTPMLQAASWSKQDLEAILTAFASEKGMGFGKLAAPLRTALAGRTVTPSVYDMMLVIGRDETIARLEDAAAA | 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). | Q9ZFA3 |
Q88XW2 | RS13_LACPL | 30S ribosomal protein S13 | Lactiplantibacillus | MARIEGIDLPRDKRIVIGLTYIYGIGNTSAQKILAEAGVSEDVRVRDLTPDQEDKIRAVVDGYKTEGDLRREVSLNIKLLQEIGSYRGMRHRRGLPVRGQHTKNNARTRKGKKVSIAGRKK | Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites. | Q88XW2 |
B4EUT8 | NQRE_PROMH | NQR-1 subunit E | Proteus | MEHYISLFVRAVFIENMALAFFLGMCTFLAVSKNVKTAFGLGIAVTVVLGLSVPLNNLVYNYVLRANALMEGVDLSFLNFITFIGVIAALVQILEMILDRYFPSLYNALGIFLPLITVNCAIFGGVSFMAQRDYNFSESIVYGFGSGIGWMLAIVLLASIREKMKYADVPSGMKGLGVTFVTTGLMALGFMSFSGVQL | NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol. | B4EUT8 |
Q214F0 | CTAA_RHOPB | Cytochrome aa3-controlling protein | Rhodopseudomonas | MPAVPADRPMHAVRIWLAIIAGLIAVMVLVGGATRLTESGLSIVEWKPITGTLPPLSVEQWTQAFDAYKTIPQYRELNAGMTLAQFKTIFWWEWSHRLLGRVIGAAFLLPFLWFLWRGDLGGGLKRRLWIIFGLGALQGAVGWWMVASGLSQRVEVSQVRLATHLVLALLIFAGIVWTLRQLTPRPAIVAPLRLRLTAAVLLGLTFVQLYLGALVAGLRAGRIYNTWPQIDGALIPSAARLWFEQPWWKNLFDNHLTVQFDHRMLAYALWALAVLHAIDAWRARAAAGGALALAVAITLQAALGIVTLLYAVPIGLGLAHQAMAILVLTLAVLQLARFSPGVVQTAQHAAAPSLGQPAQGRG | Catalyzes the conversion of heme O to heme A by two successive hydroxylations of the methyl group at C8. The first hydroxylation forms heme I, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme A. | Q214F0 |
Q91YP2 | NEUL_MOUSE | Neurotensin endopeptidase | Mus | MITLCLSALRGLHRAGGSRIRLRMTLGREAASPLQAMSSYTAAGRNVLRWDLSPEQIRTRTEELIAQTKQVYDTVGTINLEDVTYENCLQVLADIEVKYIVERTMLDFPQHVSSDREVRAASTEADKRLSRFDIEMSMREDVFQRIVHLQETCDLEKIKPEARRYLEKSIKMGKRNGLHLPEHVKNEIKSMKKRMSELCIDFNKNLNEDDTSLVFSKAELGALPDDFIDSLEKTDEDKYKVTLKYPHYFPVMKKCCVPETRRKMEMAFHTRCKEENTIILQQLLPLRAQVAKLLGYNTHADFVLELNTAKSTSHVATFLDDLSQKLKPLGEAEREFILSLKKKECEERGFAYDGKINAWDLHYYMTQTEELKYSVDQESLKEYFPIEVVTEGLLSIYQELLGLSFEQVADAHVWNKSVSLYTVKDKATGEVLGQFYLDLYPREGKYNHAACFGLQPGCLLPDGSRMMSVAALVVNFSQPIAGRPSLLRHDEVRTYFHEFGHVMHQICAQTDFARFSGTNVETDFVEVPSQMLENWVWDIDSLRKLSKHYRDGHPITDELLEKLVASRLVNTGLLTLRQIVLSKVDQSLHTNASLDAASEYAKYCTEILGVAATPGTNMPATFGHLAGGYDGQYYGYLWSEVFSMDMFHSCFRKEGIMNPEVGMKYRNLILKPGGSLDGMDMLQNFLQREPNQKAFLMSRGLNAS | Hydrolyzes oligopeptides such as neurotensin, bradykinin and dynorphin A. Acts as a regulator of cannabinoid signaling pathway by mediating degradation of hemopressin, an antagonist peptide of the cannabinoid receptor CNR1. | Q91YP2 |
Q8RSQ3 | PHNX_PSEPU | Phosphonoacetaldehyde phosphonohydrolase | Pseudomonas | MNYKNPTHLQAAILDWAGTVVDFGSFAPTQIFVEAFAEFDVEVSIEEARGPMGMGKWDHIRTLCDQPQIAERYRKVFGRTPTDDDVTAIYQRFMPLQIEKIAVHSALIPGALETLTGLRQNGLKIGSCSGYPKVVMDKVVELAAKNGYVADHVVATDETPNGRPWPAQALANVIALGIDDVAACVKVDDTVPGILEGRRAGMWTVALVCSGNALGLTYEGYRALDPNTLEAERKRIHAMFEGSRPHYLIDTINELPGVITDINQRLARGEMPQAV | Involved in phosphonate degradation. | Q8RSQ3 |
Q38S11 | COX2_HYBUN | Cytochrome c oxidase polypeptide II | Hybomys | MAYPFQLGLQDATSPIMEELTNFHDHTLMIVFLISTLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAVILILIALPSLRILYMMDEINNPALTVKTMGHQWYWSYEYTDYEDLCFDSYMIPTNDLKPGELRLLEVDNRVVLPMELPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQATVSSNRPGLFYGQCSEICGSNHSFMPIVLEMVPLKYFEDWSASMI | 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. | Q38S11 |
Q6D7E7 | NADA_PECAS | Quinolinate synthase | Pectobacterium | MNILFDSNETIYPFPPKPRPLSVDAKQHYRSRIKTLLRERNAVMVAHYYTDPEIQALAEETGGCVADSLEMARFGSTHSASTLLVAGVRFMGETAKILNPEKTILMPTLEAECSLDLGCPIDAFSRFCDAHPDRTVVVYANTSAAVKARADWVVTSSIAVELIEHLDSLGEKIIWAPDRHLGSYVQKQTGADVLCWQGACIVHDEFKTQALQRMKILYPDAAILVHPESPQSVVEMADAVGSTSQLIQAAKTLPQRELIVATDRGIFYKMQQACPEKTLLEAPTAGEGATCRSCAHCPWMAMNGLEAIANGLEQGGHAHEIHVDAALREGALIPLNRMLDFAASLKLRVKGNA | Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate. | Q6D7E7 |
Q8DHY4 | MURG_THEVB | Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase | Thermosynechococcus | MLGQRKLLIAASGTGGHLFPALAVAQELPEYEIHWLGVRDRLENQLIPPHYPLHTVNFSGLQGKTPWAKLRPLWQFWGVFWQTRQLLKQGDFQGVFTTGGYIAAPAILAARSLGRVAILHESNALPGKVTRWLAPWCTLVALGTPASLAYLQSKRLNLRVTGTPVRPDILHPGNLELPIPKAVPLIVVMGGSQGAVAINRLVRATVHRWLEAGAWVVHLTGNHDLDAPTIQHPHYLVFPFFEPMGPLLHRADIAISRAGASTLAELTLTATPALLIPYPYAAEDHQTVNAEVLVRAGAAEMIPQSALTGDRLGQIILEWLGQPQKLQAMAENARQLAMPNSSQQVADLIRRLIPAP | Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II). | Q8DHY4 |
O17389 | TYB_CAEEL | Tetrathymosin beta | Caenorhabditis | MAAVTELPKMNQELAGAVREGLELKKVETTEKNVLPTKEDVAEEKQHVERIHEIEHFDSTKLHSTPVKEKIVLPSADDIKQEKQHLELTDKINNFPSENLKKTETIEKNVLPSPTDVAREKTLQMAASFDKSALHHVETIVSTDVRVTEAQ | Plays an important role in the organization of the cytoskeleton by regulating actin polymerization in two ways. Firstly, by binding to and sequestering actin monomers (G actin) inhibits actin polymerization. Secondly, by binding directly filamentous actin (F actin) promotes actin polymerization. Regulates the formation of cortical actin in oocytes conferring them enough rigidity to sustain the contractions during ovulation. | O17389 |
Q9ZEY8 | LEU1_BUCAI | Alpha-isopropylmalate synthase | Buchnera | MKSKVVIFDTTLRDGEQALQASLSVKEKLQIALSLEKCGIDILEIGFPVSSPGDFKSVQTISKNIKNSRICSLARCIEKDIDAAGEAMSSSDSFRIHIFLATSTLHMESKLKKNFNEIIDMAVFSVKKALRYTDDIEFSCEDATRTTMDNLCRIVETLIKSGVKTINIPDTVGYTVPNELSCIIKNLFERVPNIHKSIISVHCHDDLGMAVGNSISAIQAGARQIEGTINGIGERAGNTALEEIIMAIKVREDILSVSTNINYKEIYRTSKIVSQICNMPIPSNKAIVGSNAFAHSSGIHQDGVLKNRKNYEIMEPSSIGLKEVKLNLTSRSGRAAVKHYMDEMGYNNSDYNIDELYTAFLKLADKKGQVFDYDLEALAFINKQQDEWEYFSLKFFSVQSISNSLSTASVKLLCGKKTYTESSTTSNGPVDAIYQALNRIACFPIILQKFQLVAKGKGKDALGQVDILVEHKKRKFHGVGLATDIIEASAQAMINVLNNIWKAKQVNKKLKILKDFKKK | Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate). | Q9ZEY8 |
B1WWK9 | CYB6_CROS5 | Cytochrome b6 | Crocosphaera subtropica | MFSKQVTDSKVYQWFNDRLEIQAISDDITSKYVPPHVNIFYCLGGITLVCFLVQFATGFAMTFYYKPTVTEAFSSVQYIMNEVNFGWLIRSIHRWSASMMVLMMILHVFRVYLTGGFKKPRELTWMTGVILAVITVSFGVTGYSLPWDQVGYWAVKIVSGVPAAIPVVGDQMVELLRGGQSVGQATLTRFYSLHTFVFPWLIAVFMLAHFLMIRKQGISGPL | Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. | B1WWK9 |
B5FCQ1 | RUVA_ALIFM | Holliday junction ATP-dependent DNA helicase RuvA | Aliivibrio | MIGRLRGNLLEKQPPELLIEVSGIGYEVQMPMSCFYELPEVGSEAIIYTHYVVREDAQLLYGFNTKNERALFREVIKANGVGPKLGLAILSGMTAAQFVQSVEREDISTLVKLPGVGKKTAERLVVEMKDRLKGWGAGDLFTPATDAAPMDDGSEFITSPQSAVDEAVSALIALGYKPQQASKTVSQVAKPDMTSEVLIRESLKSMI | 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. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB. | B5FCQ1 |
Q9X5D0 | AROC_CORGL | 5-enolpyruvylshikimate-3-phosphate phospholyase | Corynebacterium | MLGMLRWTTAGESHGQALIATVEHMPAGVPVTKDEVSYQLARRRLGYGRGARMKFEQDALTFLTGIRHGLTLGSPISIMIGNTEWDKWTTIMSSDALDMEDPDNVAAMSSGRGAKLTRPRPGHADYAGMLKYGFDDARNVLERSSARETAARVAAATVARSFLRETLGVEVLSHVISIGASEPYTGAEPTFADIQAIDDSPVRAFGKDAEESMIAEIEAAKKAGDTLGGIVEVIVEGLPIGLGSHISGEDRLDAQIAAALMGIQAIKGVEIGDGFEEARRRGSEAHDEVFLDDNGVYRNTNRAGGLEGGMTNGETLRVRAGMKPISTVPRALKTIDMENGKAATGIHQRSDVCAVPAAGVVAEAMVTLVLARAVLQKFGGDSLSETKSNIDTYLKNIEERMKFEGLEDGA | Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. | Q9X5D0 |
O43598 | DNPH1_HUMAN | c-Myc-responsive protein RCL | Homo | MAAAMVPGRSESWERGEPGRPALYFCGSIRGGREDRTLYERIVSRLRRFGTVLTEHVAAAELGARGEEAAGGDRLIHEQDLEWLQQADVVVAEVTQPSLGVGYELGRAVAFNKRILCLFRPQSGRVLSAMIRGAADGSRFQVWDYEEGEVEALLDRYFEADPPGQVAASPDPTT | Catalyzes the cleavage of the N-glycosidic bond of deoxyribonucleoside 5'-monophosphates to yield deoxyribose 5-phosphate and a purine or pyrimidine base. Deoxyribonucleoside 5'-monophosphates containing purine bases are preferred to those containing pyrimidine bases. | O43598 |
Q3J049 | FOLD_CERS4 | Methenyltetrahydrofolate cyclohydrolase | Cereibacter | MTAKRIDGKAFAAGVRARVAEEVARLKEGHGIVPGLAVVLVGEDPASQVYVGAKGKQTVEVGMASFEHRLPAGTSEAELLALIDRLNHDPAVHGILVQLPLPAHLNADLVINALDPAKDVDGFHISNVGRLGTGQKSMVPCTPLGCLMMLRDHLGALSGLNAVVVGRSNIVGKPMAQLLLGESCTVTIAHSRTRDLAAVCRGADILVAAVGRPEMITGDFVKPGATVIDVGINRIERDGKTKLVGDVDYASAAEVAGAITPVPGGVGPMTIACLLANTLTACCRANGLPEPQGLTA | Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate. | Q3J049 |
Q14H27 | RPIA_FRAT1 | Phosphoriboisomerase A | Francisella | MFFNKKNNQDELKKLAATEAAKSITTEITLGVGTGSTVGFLIEELVNYRDKIKTVVSSSEDSTRKLKALGFDVVDLNYAGEIDLYIDGADECNNHKELIKGGGAALTREKICVAAAKKFICIIDESKKVNTLGNFPLPIEVIPMARSYIARQIVKLGGQPVYREQTITDNGNVILDVYNLKIDNPLKLETELNQITGVVTNGIFALKPADTVIMATKDSNIVVL | Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate. | Q14H27 |
C5DD31 | RRG9_LACTC | Required for respiratory growth protein 9, mitochondrial | Lachancea | MKPVLQGALAWIYAGYKTASRGHLLPYTRHQKFHSSSLISEQAKRAKDLIKLVNSSSLSNSESQSLDWRSDLKVPEWKRQKLALKDKFKGQQWNPKKKLSREQMENVRLLKRHFPETSATELSERFQVSPEVIRRILKSKWQPNEEEQLQLQTRWKRRSERVNEILGSPEHQKLPPKKLVLGSGRTDTDLQVKSVRRTAVKAGRNSSSPKGKQKLNLLSKLIS | Required for respiratory activity and maintenance and expression of the mitochondrial genome. | C5DD31 |
Q606D6 | ILVD_METCA | Dihydroxy-acid dehydratase | Methylococcus | MTDKHPRPHSSQVVDGMERAPSRAMLHAVGFADADFAKPQIGIASTWAMVTPCNMHINKLAEDAARGVDGGGGKAVIFNTITISDGISMGTEGMKYSLVSREVIADSIETVVACQGYDGVVAIGGCDKNMPGCLIALARLNRPAVFVYGGTILPGCHDGKKLDVVSVFEAVGARANHRIDDAELHAIESNAIPGPGSCGGMYTANTMASAIEALGMSLPGSSAQVAISRAKELDCERAGAQVLKLLDLGLKPRDIMTKKAFENAITVVIALGGSTNAVLHLLAMANACGVDLKLDDFTRIGRKVPMLADLKPSGRYSMAELVEIGGIQPLMKTLLDAGLLHGDCMTVTGKTLEENLADAPDYPAGQDMIRSLDNPIKKDSHLVILKGNLAPEGAVAKITGKEGLSFTGTARVFDCEEAALTAILDGTIVKGDVIVIRYEGPKGGPGMREMLSPTSAVMGKGLGKEVALITDGRFSGGTHGFVVGHITPEAYTGGPLAIVRDGDTITIDAETRELSLHVTDDEIGRRLAQWTQPAPRYTKGVLAKYARLVSPASEGAVTDDGL | Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively. | Q606D6 |
Q9V780 | LAP1_DROME | Protein lap1 | Sophophora | MPLLSKCFPCFKFKREEVIDKLDYSNTPLTDFPEVWQHERTLEELYLSTTRLQALPPQLFYCQGLRVLHVNSNNLESIPQAIGSLRQLQHLDLNRNLIVNVPEEIKSCKHLTHLDLSCNSLQRLPDAITSLISLQELLLNETYLEFLPANFGRLVNLRILELRLNNLMTLPKSMVRLINLQRLDIGGNEFTELPEVVGELKSLRELWIDFNQIRRVSANIGKLRDLQHFEANGNLLDTLPSELSNWRNVEVLSICSNSLEAFPFSVGMLKSLVTFKCESNGLTELPDSISYLEQLEELVLSHNKLIRLPSTIGMLRSLRFLFADDNQLRQLPDELCSCQQLSVLSVANNQLSALPQNIGNLSKMKVLNVVNNYINALPVSMLNLVNLTSMWLSDNQSQPLVPLQYLDASTKTQLTCFMLPQVTFKMNSIQAQQQAQEQYEFVYANQQQPHASPSRRICFAEEATILSNAKAQPAPNYPSFVAAPPTPTPDQMAGSVRLMRSPTPYPKELRQMSKYVRQAQAATSSANASEVREARVVTNGQIHCDSNNANQDVVDQATTSAIYGIAPETTHIYGVYQQPQQMAHPVPTQEYYGLPLVNYEAHYQQLYVEANTPLPTTHLNGDQDYELQPLQQQPMQQQALPTPRLEPPPYHIARVYTKKTPEDLNLYESMRQRKQQQQLQEQTIYQDALNSNSNFKTTAIGAQDVEESVDQLDYQNNISNNLEPNPEEEDQELDDTMSQHSLNSTATNNTSKASHKKSTWIFGVHKNPTVKQVTLKWENSIGFDIAELLNQVGIFVSSITPNTNAARLLNLNDKLLEIDGYDLTNANLSDAKRVLLNCGTVMNIMLSRK | May have a role in assembling adherens junctions. | Q9V780 |
A3QEG3 | TTCA_SHELP | tRNA 2-thiocytidine biosynthesis protein TtcA | Shewanella | MSEETLSKKQITRLNKLQKRLRREVGSAIADYNMIEEGDTVMCCLSGGKDSYAMLDILVNLLQRAPVNFNLVAVNLDQKQPGFPEDILPAYLDSLKVPYHILEKDTYSIVKDKIPEGKTTCSLCSRLRRGTLYGFAQKIGATKIALGHHRDDIIETMFLNMFYAGKLKAMPPKLLSDDGANVVIRPLAYSREKDIAEYAELKAFPIIPCNLCGSQENLKRAAVKEMLKSWDKQFPGRIETIFTAMQNTSPSQGVDRDQFDFVSLKQDPDAPMKGDVAESDLPAFDFLDLANSGHIDLDAAKRSSDLLKIDVVSTYTP | Catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(2)C32). The sulfur atoms are provided by the cysteine/cysteine desulfurase (IscS) system. | A3QEG3 |
Q97L49 | SSRP_CLOAB | Small protein B | Clostridium | MAKKNTENNTLADNRKAWHDYFIEETYECGVELVGTEVKSIKNGKANLKDSYAEIRNGEVFACNMHVSPYKEGNIFNVDPLRKRRLLLHKSEIDKLLGFTSQKGYTLVPIALYLKNRRVKVKLAVAVGKKNYDKRDALKEKDARREIDRAMKNNR | 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. | Q97L49 |
A3MKT0 | LPXA_BURM7 | Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase | pseudomallei group | MSRIHPTAIIEPGAQLHETVEVGPYAIVGSHVTIGARTTIGSHSVIEGHTTIGEDNRIGHYASVGGRPQDMKYKDEPTRLVIGDRNTIREFTTIHTGTVQDTGVTTLGDDNWIMAYVHIGHDCRVGSHVILSSNAQMAGHVEIGDWAIVGGMSGVHQFVRIGAHSMLGGASALVQDIPPFVIAAGNKAEPHGINVEGLRRRGFSPDAISALRSAYRILYKNSLSLEEAKVQLSELAQAGGDGDAAVKSLVDFVESSQRGIIR | Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. | A3MKT0 |
Q2NAH8 | SYP_ERYLH | Prolyl-tRNA synthetase | Erythrobacter | MSNIRHALTVKREDDFAAWYQAVIAEADLAEESGVRGCMVIKPWGYGIWERIQRLLDDRIKATGHENVYFPIFIPLSNFEREAEHVEGFAKEMAVVTHHRLIGDGEGGLIPDPEAKLEEPLVVRPTSETIFGDAMARWIQSWRDLPLLTNQWANVVRWEMRTRMFLRTSEFLWQEGHTAHATAEEAKEHTLTMLEVYRAHAEEDLALPVIAGEKPENERFPGAVETWSIEAMMQDGKALQAGTSHYLGTNFSEAANIKFQDREGGEKYCHTTSWGVSTRMIGGVIMTHGDDDGLKVPPRIAPYQVVILPMLRDKPEDDALLAYCEDLRGKLITESAMGEPVRVLLDKKPGKAAAKRWNWVRKGAPIVIEVGGRDMENGVVSLLRRDELWNEETGKPAFQAPTPAQLTDEIASMLDSIQAGMFGTAQTWRNANVMSGCTSFEQLRDHYSDGKKHVGWVEVQWSKPTGQELEKVVEKLKDLKLTIRNVPMDTPAPTGSCIFTGKPAVEWIYVAKAY | Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). | Q2NAH8 |
O69652 | CDS1_MYCTU | L-cysteine desulfhydrase Cds1 | Mycobacterium tuberculosis complex | MSGGACIAVRSLSRSWTDNAIRLIEADARRSADTHLLRYPLPAAWCTDVDVELYLKDETTHITGSLKHRLARSLFLYALCNGWINENTTVVEASSGSTAVSEAYFAALLGLPFIAVMPAATSASKIALIESQGGRCHFVQNSSQVYAEAERVAKETGGHYLDQFTNAERATDWRGNNNIAESIYVQMREEKHPTPEWIVVGAGTGGTSATIGRYIRYRRHATRLCVVDPENSAFFPAYSEGRYDIVMPTSSRIEGIGRPRVEPSFLPGVVDRMVAVPDAASIAAARHVSAVLGRRVGPSTGTNLWGAFGLLAEMVKQGRSGSVVTLLADSGDRYADTYFSDEWVSAQGLDPAGPAAALVEFERSCRWT | A cysteine desulfhydrase that generates hydrogen sulfide, H(2)S. The H(2)S produced by this enzyme stimulates respiration in M.tuberculosis, mediated primarily via cytochrome bd with a lesser contribution from cytochrome bc1/aa3. H(2)S modulates the balance between respiration and glycolysis, and also contributes to redox homeostasis. Probably eliminates toxic levels of Cys (which can induce oxidative stress). | O69652 |
C5K3T8 | DRE2_BLAGS | Anamorsin homolog | Blastomyces | MASTGRVLLLSPPSLSSHPEKLNAILGSHTRDRTDLQMLDRLVHGLVSLPASTYDIVLLLTGADNTLAEPYSLVTRDIIQQVVHSLKPAGKLRSQDNKAWGLRSSGNNSDDDNDNDELTFRNEAILAGLVFDDNGELLKPDVAAQQAVPLKLGRRKKEKERRHPSGNDVTNGKVNAPSSNGVNASTSTATATATTTTTTTPKTNPAPSGVGFIDFSDDYGVPMEEDPQGSDDELIDEDELLGEDDMGRPIVQPPECRPKPGKRRRACKDCSCGLSQKLEAEDKAKRATADKALETIMAPTMKLGSSELAEVDFTVQGKVGSCGNCSLGDAFRCDGCPYIGLPAFKPGEEVRLLNNDVQL | Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the scaffold complex CFD1-NBP35. Electrons are transferred to DRE2 from NADPH via the FAD- and FMN-containing protein TAH18. TAH18-DRE2 are also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit RNR2. | C5K3T8 |
P50537 | MAE1_SCHPO | Malate permease | Schizosaccharomyces | MGELKEILKQRYHELLDWNVKAPHVPLSQRLKHFTWSWFACTMATGGVGLIIGSFPFRFYGLNTIGKIVYILQIFLFSLFGSCMLFRFIKYPSTIKDSWNHHLEKLFIATCLLSISTFIDMLAIYAYPDTGEWMVWVIRILYYIYVAVSFIYCVMAFFTIFNNHVYTIETASPAWILPIFPPMICGVIAGAVNSTQPAHQLKNMVIFGILFQGLGFWVYLLLFAVNVLRFFTVGLAKPQDRPGMFMFVGPPAFSGLALINIARGAMGSRPYIFVGANSSEYLGFVSTFMAIFIWGLAAWCYCLAMVSFLAGFFTRAPLKFACGWFAFIFPNVGFVNCTIEIGKMIDSKAFQMFGHIIGVILCIQWILLMYLMVRAFLVNDLCYPGKDEDAHPPPKPNTGVLNPTFPPEKAPASLEKVDTHVTSTGGESDPPSSEHESV | Permease for malate and other C4 dicarboxylic acids. | P50537 |
B2KC93 | RIMP_ELUMP | Ribosome maturation factor RimP | Elusimicrobium | MRDIKAIESVVADGLANQGYEVVDLIVQNQGSKKLFQFFVDKEGGINLDDVEKASRLIDSIIEMENLIEGAYILEASSPGIKRVLKKPEHFKKFIGQRAKITLKQMIENRANFTGLIAGANETEMTLDDGTTQFKFKYEDIKKANLDPVLEF | Required for maturation of 30S ribosomal subunits. | B2KC93 |
Q98NP5 | RS4_RHILO | 30S ribosomal protein S4 | Mesorhizobium | MSKRESAKYKIDRRLGENIWGRPKSPVNKREYGPGQHGQRRKGKLSDFGLQLRAKQKLKGHYGDVSEKQFRKVYEEADRRKGDTSENLIGLLESRLDAVVYRAKFVPTIFAARQFVNHGHVNVNGKRVNIGSYRCKPGDVIEVREKSKQLVIVLESVGLAERDVPDYIEADHNKMVATFSRIPGLADVPFAVQMEPNLVVEFYSR | With S5 and S12 plays an important role in translational accuracy. | Q98NP5 |
Q5HAK5 | RUVA_EHRRW | Holliday junction ATP-dependent DNA helicase RuvA | Ehrlichia | MIGSITGNVEEIRDSYIILNVGNIGYIIYVSHKVLQTCKVGDNIKLYIETYVNRDNITQLYGFLNRQEQDYLKMLVTINGINYKTALSILSKLSPEQIFSAVVNNDKIAFKGNGIGEKLAGRIITELQYKINKMPIEETFSIIENDDSLAALISLGYEKLKAFNVIQEIKSKTPDASTQEVIRKALQKLSQ | 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. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB. | Q5HAK5 |
P85302 | AMPC_PSEFL | Cephalosporinase | Pseudomonas | ATDIRQVVDSTVEPLMQQQDIAGLSVAVIQNGKAQYFNYGVANKDSKQPITENTLFEIGSVSKTFTATLAGYALANGKLKLSDPASQYLPALRGDKFDHISLLNLGTYTAGGLPLQFPEESDNTGKMISYYQHWKPAFAPGTQRLYSNPSIGLFGHLAAQSLGQPFEKLMEQTVLPKLGLKHTFISVPETQMSLYAQGYDKAGKPVRVSPGALDAEAYGIKTSTSDLIHYVEVNMHPAKLEKPLQQAIAATHTGYYTVDGMTQGLGWEMYPYPIKVDALVEGNSTQMAMEPHKVNWLTPPQAAPLDTLVNKTGSTGGFGAYVAYVPSKGLGVVILANKNYPNAERVKAAHAILSAMDQ | This protein is a serine beta-lactamase with a substrate specificity for cephalosporins. | P85302 |
A5CW25 | RPOB_VESOH | Transcriptase subunit beta | Candidatus Vesicomyosocius | MAYSFTEKKRIRNNFGSRESILTEPDLLAIQIDSFNSFIQADNKIKQDIGLHNVLQSVFPITAVNGYAQIEYVDYQLKEPKFNVEECKLRGVTFASTLRVKLNLVLFDKNGSTLKKKRKVKQIIEEDVYLGQLPLMTETGTFVINGTERVVVSQLHRSPGVIFEHDKGKTHSSGKILFSSRIIPYRGSWLDFEYDHHEHLYVRIDRRRKLPVTTLLRAMGLSSEDILETFFEKTPVKLKAKSCDLSMLPIHLQRTIAEFDIVVNQHVVVEKGRRITAKHVKLLGKAGIKSINAPLEYLLDKVICADIINKDTGEILISANTITSEEVLELLNTNKVKKIEILYINSSETGAYISDTLRLDETQTEIEARMSIYHVMRPGEPATEDAVNLLFNNLFFKNDRYDLSKVGRMKLNRRLGISRETGEHVLTNDDIIRVIKLLINIKDGNDSVDDIDTLANRRVRAIGEMIENQFRIGLVRVEKAVREGLNLAETDELTPQDLINSKPVSAAVREFFGSSQLSQFMDQVNPLSGVTHKRRISALGPGGLTRERAGFEVRDVHPSHYGRLCPIETPEGPNIGLINTLAVYAKTNSYGFLETPYQIVKNGKVTKEVIYVSAIDEITHTIAQANALVDDRGKLMDDLISCRHKNEFVLVDSSEVTLIDIDSKQISSVAASLIPFLEHDDANRALMGSNMQRQAVPVLKAEKPLVGTGIERVVAKDSRVCVTAKHGGVVEAVDASRIVIRVDSKKTKANELGVDIYNLTKYSRSNQNTCINQKPLVRTGDKITFGDVLADGPSTDMGELALGQNMKIAFMPWNGYNFEDSILISEKVVQEDRYTTIHIEELTAYSRDTKLGPEEITSDIPNVSESALSKLDEVGVVYVGARVKGGDILVGKVTPKSETVLSPEEKLLRAIFGEKANNVKDSSLRIGASKSGVVIDVQVFTRDRVEKDIRALSIDAERLERIKKDIDDEFSIIDGDIFRRIRLKLLGNVLSKAIGDIRIGERLSIKLMKKFDNKDIAKFKVENATVNKEVAVLVKQAKAKKVEFEKFFKKEKAKINEGAELPPGVMKMVKVYVATRKTLQVGDKMAGRHGNKGVISRVSPVEDMPYLADGSTIDIVLNPLGVPSRMNVGQVLEVHLGYAAKGLGYKIAAILDERRPDMVKQIRVFLDKVYNLHGKKEDLTLFSNEEIIELANNLREGVPMATPVFDGIREQDIKSLLRLADLPESGQEQLYDGRTGEPFDRHVTVGYMHMLKLNHLVDDKMHARSTGPYSLVTQQPLSGKAQFGGQRFGEMEVWALEAYGAAHTLREMLTVKSDDVAGRAKMYKSIVDGKNLTESVMPESFNVLVKEIRSLGIDVELEQH | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | A5CW25 |
Q6ED65 | EMAL5_RAT | Echinoderm microtubule-associated protein-like 5 | Rattus | MAARSAPSCHLRLEWVYGYRGHQCRNNLYYTAAKEIVYFVAGVGVVYSPREHRQKFYRGHSDDIISLALHPERVLVATGQVGKEPYICVWDSYTVQTVSVLKDVHTHGIACLAFDLDGQRLVSVGLDSKNAVCVWDWKRGKMLSMAPGHTDRIFDISWDLYQPNKLVSCGVKHIKFWSLCGNALTPKRGVFGKTGDLQTILCLACARDELTYSGALNGDIYVWKGINLIRTIQGAHTAGIFSMNACEEGFATGGRDGCIRLWDLTFKPITVIDLRETEQGYKGLSVRSVCWRGDHILVGTQDSEIFEIVVHERNKPFLIMQGHCEGELWALAVHPTKPLAVTGSDDRSVRIWSLVDHALIARCNMDEPIRCAAVNADGVHLALGMKDGSLTVLRVRDMTEVVHIKDRKEAIHELKYSPDGTYLAVGCNDSSVDIYGVAQRYKKVGECVGSLSFITHLDWSSDSKYLQTNDGSGKRLLYKMPGGKEVTSKEEVKGMHWASWTCVAGLEVNGIWPKYSDINDINSVDGNYVGQVLVTADDYGVVKLFRYPCLRKGAKFRKYIGHSAHVTNVRWSHDYQWVISIGGADHSVFQWKFIPERKLKDALHIAPQESLTESNSDESDSDLSDVPELDSEIEQETQLTYHRQVYKEDLPQLKEQCKEKQKSATSKRRERAPGNSIRLHFIHGYRGYDCRSNLFYTQIGEIVYHVAAVGVIYNRQQNTQRFYLGHDDDILCLAIHPLKDYVATGQVGRDPSIHVWDTETIKPLSILKGYHQYGICAVDFSADGKRLASVGIDDSHTIVLWDWKKGEKLSVARGSKDKIFVVKMNPYVPDKLITAGIKHMKFWRRAGGGLIGRKGYVGTLGKNDTMMCAVYGWTEEMAFSGTSTGDVCIWRDVFLVKTVKAHDGPVFSMHALEKGFVTGGKDGVVALWDDSFERCLKTYAIKRADLAPGSKGLLLEDNPSIRAISLGHGHILVGTKNGEILEVDKSGPVTLLVQGHMEGEVWGLATHPYLPICATVSDDKTLRIWDLSPSHCMLAVRKLKKGGRCCCFSPDGKALAVGLNDGSFLMANADTLEDLVSFHHRKDVISDIQFSPGSGKYLAVASHDSFVDIYNVTSSKRVGVCKGATSYITHIDWDSRGKLLQVNTGAKEQLFFEAPRGKKQTIPSVEVEKISWATWTSVLGLCCEGIWPIIGEVTDVTASCLTSDKMVLATGDDLGFVKLFRYPAKGKFGKFKKYVAHSTHVTNVRWTYDDSMLVTLGGADMSLMVWTSEVERHREKKNCDSEESDTDSEEDGGYDSDVTRENEISYTIRALSTNIRPMFGVKPHLQQKEPSVDERQGVVRGSRPPVSRAPPQPEKLQSNNVGKKKRPIEDLVLELAFGYRGRDCRNNVHYLNDGDDIIYHTASVGILHNVATGTQSFYQEHNDDILCLTVNQHPKFINIVATGQVGDSADMSATAPSVHIWDAVNKQTLSILRCSHSKGVCSVSFSATGKLLLSVGLDPEHTVTIWRWQEGAKIASRGGHNQRIFVAEFRPDSDTQFVSVGIKHVKFWTLAGRALLSKKGLLSTLEDARMQTMLAVAFGANNLTFTGTISGDVCVWKDHILCRVVARAHNGPVFAMYTTLRDGLIVTGGKERPSKEGGAVKLWDQELRRCRAFRLETGQVTDCVRSVCRGKGKILVGTRNSEIIEVGEKNAACNILVNGHVDGPIWGLATHPSRDFFLSAAEDGTVRLWDIADKKMLNKVNLGHAARTVCYSPEGDMVAIGMKNGEFIILLVSSLKIWGKKRDRRCAIHDIRFSPDSRYLAVGSSENSVDFYDLTLGPTLNRISYCKDIPSFVIQMDFSADSRHLQVSSGCYKRHVYEVPSGKHLVDHAAIDRITWATWTSILGDEVMGIWSRHAEKADVTCACVSHSGISLVTGDDFGMVKLYDFPCPEKFAKHKRFLGHSPHVTNIRFTSGDRHVVSAGGDDCSVFVWKCVHTPH | May modify the assembly dynamics of microtubules, such that microtubules are slightly longer, but more dynamic. | Q6ED65 |
A9L9A5 | ACCD_LEMMI | Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic | Lemna | MEKLWLNSMFSNGKLEHKYRLSRSMDSLGPIRYSSGSEDPVLNAMDNKVSSWNDSGSCNFSNVEHFLDIIDIWSFISDDTFLVRDSNGDSFSIYFDIENQIFEIDNDSTFINELESSFSSYLDSSSMNSGSKKSSRYYYRYMYDTQSSWNNHINSCIDSYLRYEISIDSYISGETHNYSDNYVYNFICNESISGNESRNSAIRTSVNGSDFNIRGRSNDLDINKKYRHLWVQCENCYGLNYKQFFRSRLNICEHCGYHLKMSSSERIELLIDPGTWDPLDENMVSTDPIEFHSEEEPYRDRIDSYQKKTGLTEAVQTGIGELNGIPIAIGVMDFQFMGGSMGSVVGEKITRLIEYATNKSLPVIIVCASGGARMQEGSLSLMQMAKISSALYNYQLNKKLFYVAILTSPTTGGVTASFGMLGDIIIAEPNAYIAFAGKRVIEQTLNKTVPDGSQAAEYLFQKGLFDLIVPRNLLKGVLGELFQLHGFFPLT | 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. | A9L9A5 |
Q55C77 | FCL_DICDI | GDP-4-keto-6-deoxy-D-mannose-3,5-epimerase-4-reductase | Dictyostelium | MTETTSKRTVLVTGGSGLVGKGIEKYVKETDKSNDVWVFMRSSDCDLKSRESTRSYFEKIKPTHVIHLAARVGGLFSNMKYKVEFFRENIDINDNVLACCKEFNVVKCVSCLSTCIFPDKTTYPIDETMIHNGPPHPSNEGYAYAKRMIDVLNRAYNEEYGCKFTSVIPTNIYGPHDNYHLTDGHVIPGLIHKTYLAMKNNQDLTIMGTGKPLRQFIYSYDLAKYFVWTLNNYEEMSPLILSVGEEDEISIADVARLITEAMEFKGKLIFDTSKADGQYKKTASNLKLKSLVPDLTFTPIQQAIKESCQWFIDNYETARK | Catalyzes the two-step NADP-dependent conversion of GDP-4-dehydro-6-deoxy-D-mannose to GDP-fucose, involving an epimerase and a reductase reaction. | Q55C77 |
Q74IR9 | ISPT_LACJO | Isoprenyl transferase | Lactobacillus | MSESKKPLNHLAIIMDGNGRWAKKRHLPRFVGHRHGMDNIRNIALAANKLGIKVLTLYAFSTENWARPTDEVNYLMRLPIDFFDKFMPELMENNVRVNIMGFVDELPEKTYLVTQKAMAETANNTGMVLNFAFNYGSRREITAGVQEIARKVKVGEIDIDDISEKMVSDHLLTHSLAPYEDPDLLIRTSGEERLSNFLLWQMAYTEFSFSDKLWPDFDKTDLEELVKDYQGRNRRFGKV | Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids. | Q74IR9 |
Q1RQI9 | THIO_MALSM | Allergen Mala s 13 | Malassezia | VQVISSYDQFKQVTGGDKVVVIDFWATWCGPCKMIGPVFEKISDTPAGDKVGFYKVDVDEQSQIAQEVGIRAMPTFVFFKNGQKIDTVVGADPSKLQAAITQHSA | Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. | Q1RQI9 |
F1MMS9 | ITA3_BOVIN | Integrin alpha-3 light chain | Bos | MGPGPSRAAGVLRPLLGMLALMVAASNRAASAFNLDTRFLVVKEAGNPGSLFGYSVALHRQTERQQRYLLLAGAPRDLAVPDGYTNRTGAVYLCPLTAHKNDCERMDIKEKSNPNHIIEDMWLGVTVASQGPAGRVLVCAHRYTQVLWSGSEDQRRMVGKCYVRGNDLELDARDDWQTYHNEMCNSNTDYLETGMCQLGTSGGFTQNTVYFGAPGAYNWKGNSYMIQRKDWDLSEYSYKDPEDQGNLYIGYTMQVGSAILHPTNITIVTGAPRHQHVGAVFLLSQEAGGDLRRRQVLEGTQVGAYFGSAIALADLNNDGWQDLLVGAPYYFERKEEVGGAIYIFMNQAGTSFPDHPSLLLHGPSRSAFGFSVASIGDVNQDGFQDIAVGAPFEGLGKVYIYHGSSRGLLRQPQQVIHGEQLGLPGLATFGYSLSGQMDVDENFYPDLLVGSLSDRIVLLRARPVINILHKTLVAKPSILDPAFCTATSCVQVELCFAYNQSAGNPNYRRNITLAYTLEADRDRRPPRLHFARSQSAVFHGFFSMPEMRCQTLELLLMDNVRDKLRPITISMNYSLPLRLPDRPQLGLGSLDAYPVLNQAQALENHTEVQFQKECGQDNRCDSNLQMRAAFVSELGQRLSRLQYRRDLRKLLLSINVTNTPSRKRAGEDAHEALLTLEVPPTLLLSSVRPPGACQANETIVCELGNPFKRNQRMELLIAFEVIGVTLHTRELQAQLQLSTSSHQDDLRPMTLPLLVDYTLQASLSMVNHRLQSFFGGTVMGESGMKTVEDVGSPLKYEFQVGPMGEGLAALGTLVLGLEWPYEVSNGKWLLYPTEITVHGNGSWHCQPPGDLINPLNLTLSVPGDGPPSPQRRRRQLDPGGGQGPPPVTLAAAKKAKSEIQLSCGSDHTHCVWLECPIPDAPVITNVTIQARVWNSTFIEDYRDFDRVRVASWATLFLRTGVPTINMENKTVRFSVDIDSDLVEELPAEIELWLVLVAVSAGLLLLGLIILLLWKCGFFKRARTRALYEAKRQKAEMKSQPSETERLTEDY | Integrin alpha-3/beta-1 is a receptor for fibronectin, laminin, collagen, epiligrin, thrombospondin and CSPG4. Integrin alpha-3/beta-1 provides a docking site for FAP (seprase) at invadopodia plasma membranes in a collagen-dependent manner and hence may participate in the adhesion, formation of invadopodia and matrix degradation processes, promoting cell invasion. Alpha-3/beta-1 may mediate with LGALS3 the stimulation by CSPG4 of endothelial cells migration. | F1MMS9 |
Q869U7 | RS18_DICDI | 40S ribosomal protein S18 | Dictyostelium | MSSSLVFQGEFQHIIRIYNTNVDGRRKIQYALTCVKGVGRRFANLVCKKADIDTSKRAGELSKDEVERLTTIMNHPRQYNIPTWFLNRQKDIKDGKYSHCLANQIDVKFREDLERLKKIRAHRGVRHHFGLRVRGQKTKTTGRRGRTVGVAGRR | Located at the top of the head of the 40S subunit, it contacts several helices of the 18S rRNA. | Q869U7 |
P32048 | SYKM_YEAST | Lysyl-tRNA synthetase | Saccharomyces | MNVLLKRRSLTFAPRWLWCKCRSSRSRPYSLAHAVDTSKMEATRRNGQIVKDLGRYYPSMSESALHDLCQEYKEVTIADFNERFLGNPATLHHEDNPNLLLSINGRIKSIRFSGQKIVFIDLYNGSSGLKNDTQLQLIVNYNKIGGSSEDKANFSEYMNFLKKGDYIKALGYPGFSQSRVKMLSLICNKLPIVLSVSQLPLPSRLNDETKIKSNRVVDYQLNGTQTLLVRARIIKLLRKFLDDRNFVEVETPILSSKSNGAMAKPFITSSKDFDHLELRIAPELWLKRLIISGLQKVYEIGKVFRNEGIDSTHNAEFSTLEFYETYMSMDDIVTRTEDLFKFLITNLQKFFQDTRLPVPKTFSELHLALSENNWKFRKVEFLPTLNKELGIDLMNSGLDINKPSELLKALPKDIAKKYFPSADNTGQLSSLQILNKLSDVFLEQRHCQSTLPTVIYHQPAILSPLAKTDPQNKQVTKRFEVFIKGKEYINAYEEENCPQLQLQKFLQQKQINELTGNKTETLSPVIDYQYVETMKYGMPPVGGFGLGIDRLCMLFCDKKRIEEVLPFGCVDDVNRQ | Catalyzes the attachment of lysine to tRNA(Lys) in the mitochondrion. | P32048 |
B0UWF1 | TORD_HISS2 | Chaperone protein TorD | Histophilus | MITLNTEEKIFIYSWLKNILSHELTEQQLQQYQQGVFTPLFDFLSEQDLAKQINTVRNSLMQLSNLPLAHLELAADFAQLFLLNGENSALPYASAYLSEKELNQHIAFIDHLLFKYQLKFDHNLREPSDHLAVYLELLITLEKSGQKEKSFNFIQHYLLAWLIPFNKKVQKIKTETSFYQAITEILITLLNKNVKLS | Involved in the biogenesis of TorA. Acts on TorA before the insertion of the molybdenum cofactor and, as a result, probably favors a conformation of the apoenzyme that is competent for acquiring the cofactor. | B0UWF1 |
P0AC14 | DHPS_ECOL6 | Dihydropteroate pyrophosphorylase | Escherichia | MKLFAQGTSLDLSHPHVMGILNVTPDSFSDGGTHNSLIDAVKHANLMINAGATIIDVGGESTRPGAAEVSVEEELQRVIPVVEAIAQRFEVWISVDTSKPEVIRESAKVGAHIINDIRSLSEPGALEAAAETGLPVCLMHMQGNPKTMQEAPKYDDVFAEVNRYFIEQIARCEQAGIAKEKLLLDPGFGFGKNLSHNYSLLARLAEFHHFNLPLLVGMSRKSMIGQLLNVGPSERLSGSLACAVIAAMQGAHIIRVHDVKETVEAMRVVEATLSAKENKRYE | Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. | P0AC14 |
B2GAU2 | ATPD_LIMF3 | F-type ATPase subunit delta | Limosilactobacillus | MSRLDQKTVANRYARAIFELAQEDGQLDQTYQELVSVRQVFLDNPSLAPLLAGVDLGIKEKQALVDQVKEGASKYVANLLQMAFDYRRMSDMVAIVDEFERRYDEKHKRVHAEVVTAVQLDETRRNQLRDNLAARLGAQEIVLNEKVDPTILGGVVVKTANQTLDGSIKTKIEQIRRLIVK | This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. | B2GAU2 |
B8I4D2 | FLIW_RUMCH | Flagellar assembly factor FliW | Ruminiclostridium | MLVKTTHFGEINIKDEDIIEFSEGIVGFEDIHRYGIIRNQNSDSPFSWLQAVEKSELAFAVVDPFVIKKDYDFVLSDEYVKALDINDPSQVNVYAIVVVPDDLTKISMNLKAPVIVNKDNRKAAQVILDTDEYTVRHYIMDELQKQEV | Acts as an anti-CsrA protein, binds CsrA and prevents it from repressing translation of its target genes, one of which is flagellin. Binds to flagellin and participates in the assembly of the flagellum. | B8I4D2 |
Q7L2Z9 | CENPQ_HUMAN | Centromere protein Q | Homo | MSGKANASKKNAQQLKRNPKRKKDNEEVVLSENKVRNTVKKNKNHLKDLSSEGQTKHTNLKHGKTAASKRKTWQPLSKSTRDHLQTMMESVIMTILSNSIKEKEEIQYHLNFLKKRLLQQCETLKVPPKKMEDLTNVSSLLNMERARDKANEEGLALLQEEIDKMVETTELMTGNIQSLKNKIQILASEVEEEEERVKQMHQINSSGVLSLPELSQKTLKAPTLQKEILALIPNQNALLKDLDILHNSSQMKSMSTFIEEAYKKLDAS | Component of the CENPA-CAD (nucleosome distal) complex, a complex recruited to centromeres which is involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation. May be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex . Plays an important role in chromosome congression and in the recruitment of CENP-O complex (which comprises CENPO, CENPP, CENPQ and CENPU), CENPE and PLK1 to the kinetochores . | Q7L2Z9 |
B2RL45 | RPOB_PORG3 | Transcriptase subunit beta | Porphyromonas | MTPTTNNKRINFASIKNPLFYPDFLEVQLKSFHDFLQLDTPPERRKKEGLYKVFAENFPITDTRNNFVLEFLDYYIDPPKYSIEECLSRGLTYSVPLKAKLKLYCTDPDHEDFATVIQDVFLGPIPYMTSSGTFVINGAERVIVSQLHRSPGVFFGQSLHTNGTKLYSARIIPFKGSWIEFATDINNVMYAYIDRKKKLPVTTLLRAIGFEADKDILDIFNLAEEVKVTKANLKKCIGRKLAARVINTYIDDLSDEDTGEVVSMERITVVVDREVELTEDNIEAILNSNTQTILLHRNDSNTSDYSIIFNTLQKDPCNSEKEALYYVYRQLRNAEPADDASAREVITNLFFSDKRYDLGDVGRYRINKKLNLNIDPDIKVLTNEDIIEIIKYLIELVNSKASVDDIDHLSNRRVRTVGEQLYNQFGIGLARMARTVRDRMNVRDNEVFTPIDLVNAKTISSVVNSFFGTNALSQFMDQTNPLAEITHKRRLSALGPGGLSRERAGFEVRDVHYTHYGRLCPIETPEGPNIGLISSLCVYAKISDLGFITTPYREVKNGKVDFSDNGLKYYTAEEEEEKTVAQGNAPLDENGRFVRERVKARYESDFPLVTPDEVDLMDVSPTQIASIAAALIPFLEHDDANRALMGSNMMRQAVPLLRPESPIVGTGIEGKLVKDSRTQIVAERGGEVVFVDASCIKIRYDRTADEEFVSFDDAIVTYYLPKYRKTNQSTTIDLHPICSKGDRVEAGQILTEGYSTQGGELALGRNVQVAYMPWKGYNYEDAIVLNERMVREDFFTSVHVDEYILEVRETKRGLEELTSDIPNVSEDATRDLDENGIVRIGAHIEPGDILIGKITPKGESDPTPEEKLLRAIFGDKAGDVKDASLKATPSLRGVVIDTKLFSKAAKKKSRTSTKETVSKLDETYAKRQQQLHERLIEKLTELTKGKTCCGVKDYLNVELIKAGSKLTKKDLEALDFNVIQLSDWTNDAHTNELIKAVAVNYLKHSKEIEAELRRRKLDETIGDELPAGIVQMAKVYIAKKRKIQVGDKMAGRHGNKGIVSKIVRQEDMPFLADGTPVDICLNPLGVPSRMNLGQIFEAVLAWAGRKMNVKFATPIFDGASLNDMNEWTDKAGLPRDGKTYLYDGGTGERFDQPATVGVTYFLKLGHMVDDKMHARSIGPYSLITQQPLGGKAQFGGQRFGEMEVWALEAFGASHILQEILTVKSDDVVGRSKAYEAIVKGDPMPTPGIPESLNVLLHELKGLGLSFSLD | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | B2RL45 |
Q9NV29 | TM100_HUMAN | Transmembrane protein 100 | Homo | MTEEPIKEILGAPKAHMAATMEKSPKSEVVITTVPLVSEIQLMAATGGTELSCYRCIIPFAVVVFIAGIVVTAVAYSFNSHGSIISIFGLVVLSSGLFLLASSALCWKVRQRSKKAKRRESQTALVANQRSLFA | Plays a role during embryonic arterial endothelium differentiation and vascular morphogenesis through the ACVRL1 receptor-dependent signaling pathway upon stimulation by bone morphogenetic proteins, such as GDF2/BMP9 and BMP10. Involved in the regulation of nociception, acting as a modulator of the interaction between TRPA1 and TRPV1, two molecular sensors and mediators of pain signals in dorsal root ganglia (DRG) neurons. Mechanistically, it weakens their interaction, thereby releasing the inhibition of TRPA1 by TRPV1 and increasing the single-channel open probability of the TRPA1-TRPV1 complex. | Q9NV29 |
P39325 | YTFQ_ECOLI | Galactofuranose-binding protein YtfQ | Escherichia | MWKRLLIVSAVSAAMSSMALAAPLTVGFSQVGSESGWRAAETNVAKSEAEKRGITLKIADGQQKQENQIKAVRSFVAQGVDAIFIAPVVATGWEPVLKEAKDAEIPVFLLDRSIDVKDKSLYMTTVTADNILEGKLIGDWLVKEVNGKPCNVVELQGTVGASVAIDRKKGFAEAIKNAPNIKIIRSQSGDFTRSKGKEVMESFIKAENNGKNICMVYAHNDDMVIGAIQAIKEAGLKPGKDILTGSIDGVPDIYKAMMDGEANASVELTPNMAGPAFDALEKYKKDGTMPEKLTLTKSTLYLPDTAKEELEKKKNMGY | Part of the ABC transporter complex YtfQRT-YjfF involved in galactofuranose transport (Probable). Binds to both alpha- and beta-galactofuranose . | P39325 |
Q323B4 | SYM_SHIBS | Methionyl-tRNA synthetase | Shigella | MTQVAKKILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTDFAGFNISYDNYHSTHSEENRQLSELIYSRLKENGFIKNRTISQLYDPEKGMFLPDRFVKGTCPKCKSPDQYGDNCEVCGATYSPTELIEPKSVVSGATPVMRDSEHFFFDLPSFSEMLQAWTRSGALQEQVANKMQEWFESGLQQWDISRDAPYFGFEIPNAPGKYFYVWLDAPIGYMGSFKNLCDKRGDSVSFDEYWKKDSTAELYHFIGKDIVYFHSLFWPAMLEGSNFRKPTNLFVHGYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYYTAKLSSRIDDIDLNLEDFVQRVNADIVNKVVNLASRNAGFINKRFDGVLASELADPQLYKTFTDAAEVIGEAWESREFGKAVREIMALADLANRYVDEQAPWVVAKQESRDADLQAICSMGINLFRVLMTYLKPVLPKLTERAEAFLNTELTWDGIQQPLLGHKVNPFKALYNRIDMRQVEALVEASKEEVKAAAAPVTGPLADDPIQETITFDDFAKVDLRVALIENAEFVEGSDKLLRLTLDLGGEKRNVFSGIRSAYPDPQALIGRHTIMVANLAPRKMRFGISEGMVMAAGPGGKDIFLLSPDAGAKPGHQVK | Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | Q323B4 |
A5D2S1 | RBFA_PELTS | Ribosome-binding factor A | Pelotomaculum | MSFRSERVAEAIKKEVSDMLRNELKDPRIGFVTITSVEVSKDLRYANIYASVFGSPDDQKETIEALKKAQGFIRGELGKRIRLRYTPEITFKLDQSIGRGSRVLALMEEVREKGGGQDE | One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Associates with free 30S ribosomal subunits (but not with 30S subunits that are part of 70S ribosomes or polysomes). Required for efficient processing of 16S rRNA. May interact with the 5'-terminal helix region of 16S rRNA. | A5D2S1 |
B9FDE0 | BSK3_ORYSJ | Receptor-like cytoplasmic kinase 173 | Oryza sativa | MGGRVSKAVACCCCRSQHHGVVVESSEKTAEEDHGESYELPAFQEFSFEQLRLATSGFAVENIVSEHGEKAPNVVYKGKLDAQRRIAVKRFNRSAWPDPRQFLEEAKSVGQLRSKRLANLLGCCCEGDERLLVAEYMPNDTLAKHLFHWEAQAMKWPMRLRVVLYLAEALEYCTSKGRALYHDLNAYRVLFDDDCNPRLSCFGLMKNSRDGKSYSTNLAFTPPEYMRTGRITPESVIYSFGTLLLDVLSGKHIPPSHALDLIRDRNFNMLTDSCLEGQFSNEEGTELVRLASRCLHYEPRERPNVRSLVQALAPLQKDLETPSYELMDIPRGGATSVQSLLLSPLAEACSRKDLTAIHEILEKTGYKDDEGTANELSFQMWTNQMQDTLNSKKKGDNAFRQKDFSSAIDCYSQFIEVGTMVSPTIYARRCLSYLMNDKAEQALSDAMQALVISPTWPTAFYLQAAALLSLGMENEAQEAIKDGCAHETSSSSGH | Probable serine/threonine kinase that acts as positive regulator of brassinosteroid (BR) signaling downstream of BRI1. | B9FDE0 |
B3PMP1 | RS3_META1 | 30S ribosomal protein S3 | Metamycoplasma | MGQKVNPNGFRYGITKAHNSVWYADKMQFASHLLEDQKIYDFFDKKVRQLQIGNVQIKRNQNGLILIYVYTAKPAVMLGTNGENIKNLTKDLQKILKNKKANISIQVIELKKPDLNARLLAEDIAIKLENRGSFRLAQKFAIKAALKAGAKGIKTSVSGRLNGVDMARTEGYNEGEMKLHTLRQDVDYAATTAKTTYGILGVKVWVSLGEILSDEQKAKQEEMDLLNAPKDRRVRRGGERHASTKKN | Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation. | B3PMP1 |
Q8VCK7 | SYCN_MOUSE | Syncollin | Mus | MSLLCPLLLALALVAVPGAHGNCPVPADLKKSDGTRTCARLYEKSDPYYDNCCQGPVLSVEPGTDLPYLPSGWSNTASSLVVGQRCEITVWSLPGKHGKTRKFTAGSYPRLEEYRKGIFGDWSDSISALYCKCY | Functions in exocytosis in pancreatic acinar cells regulating the fusion of zymogen granules with each other. May have a pore-forming activity on membranes and regulate exocytosis in other exocrine tissues. | Q8VCK7 |
B0B7N3 | RL10_CHLT2 | 50S ribosomal protein L10 | Chlamydia | MKEEKKLLLREVEEKITASQGFILLRYLGFTATHSRSFRNNLSGVSAEFEVLKKKIFFKALETSGVEMDPEDSEGHLGVVFAYGDPVSAAKQVLDFNKQHNDSLVFLAGRIDNASLSGREVEAVAKLPSMKELRQQVVGLIAAPMSQVVGIMNSVLSGVVSCVDQKAEKTQE | Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors. | B0B7N3 |
Q02294 | CAC1B_RAT | Voltage-gated calcium channel subunit alpha Cav2.2 | Rattus | MVRFGDELGGRYGGTGGGERARGGGAGGAGGPGQGGLPPGQRVLYKQSIAQRARTMALYNPIPVKQNCFTVNRSLFVFSEDNVVRKYAKRITEWPPFEYMILATIIANCIVLALEQHLPDGDKTPMSERLDDTEPYFIGIFCFEAGIKIIALGFVFHKGSYLRNGWNVMDFVVVLTEILATAGTDFDLRTLRAVRVLRPLKLVSGIPSLQVVLKSIMKAMVPLLQIGLLLFFAILMFAIIGLEFYMGKFHKACFPNSTDAEPVGDFPCGKEAPARLCDSDTECREYWPGPNFGITNFDNILFAILTVFQCITMEGWTDILYNTNDAAGNTWNWLYFIPLIIIGSFFMLNLVLGVLSGEFAKERERVENRRAFLKLRRQQQIERELNGYLEWIFKAEEVMLAEEDKNAEEKSPLDAVLKRAATKKSRNDLIHAEEGEDRFVDLCAAGSPFARASLKSGKTESSSYFRRKEKMFRFLIRRMVKAQSFYWVVLCVVALNTLCVAMVHYNQPQRLTTALYFAEFVFLGLFLTEMSLKMYGLGPRSYFRSSFNCFDFGVIVGSIFEVVWAAIKPGTSFGISVLRALRLLRIFKVTKYWNSLRNLVVSLLNSMKSIISLLFLLFLFIVVFALLGMQLFGGQFNFQDETPTTNFDTFPAAILTVFQILTGEDWNAVMYHGIESQGGVSKGMFSSFYFIVLTLFGNYTLLNVFLAIAVDNLANAQELTKDEEEMEEAANQKLALQKAKEVAEVSPMSAANISIAARQQNSAKARSVWEQRASQLRLQNLRASCEALYSEMDPEERLRYASTRHVRPDMKTHMDRPLVVEPGRDGLRGPAGNKSKPEGTEATEGADPPRRHHRHRDRDKTSASTPAGGEQDRTDCPKAESTETGAREERARPRRSHSKEAPGADTQVRCERSRRHHRRGSPEEATEREPRRHRAHRHAQDSSKEGKEGTAPVLVPKGERRARHRGPRTGPRETENSEEPTRRHRAKHKVPPTLEPPEREVAEKESNVVEGDKETRNHQPKEPRCDLEAIAVTGVGSLHMLPSTCLQKVDEQPEDADNQRNVTRMGSQPSDPSTTVHVPVTLTGPPGEATVVPSANTDLEGQAEGKKEAEADDVLRRGPRPIVPYSSMFCLSPTNLLRRFCHYIVTMRYFEMVILVVIALSSIALAAEDPVRTDSFRNNALKYMDYIFTGVFTFEMVIKMIDLGLLLHPGAYFRDLWNILDFIVVSGALVAFAFSSFMGGSKGKDINTIKSLRVLRVLRPLKTIKRLPKLKAVFDCVVNSLKNVLNILIVYMLFMFIFAVIAVQLFKGKFFYCTDESKELERDCRGQYLDYEKEEVEAQPRQWKKYDFHYDNVLWALLTLFTVSTGEGWPMVLKHSVDATYEEQGPSPGFRMELSIFYVVYFVVFPFFFVNIFVALIIITFQEQGDKVMSECSLEKNERACIDFAISAKPLTRYMPQNKQSFQYKTWTFVVSPPFEYFIMAMIALNTVVLMMKFYDAPYEYELMLKCLNIVFTSMFSLECILKIIAFGVLNYFRDAWNVFDFVTVLGSITDILVTEIANNFINLSFLRLFRAARLIKLCRQGYTIRILLWTFVQSFKALPYVCLLIAMLFFIYAIIGMQVFGNIALDDGTSINRHNNFRTFLQALMLLFRSATGEAWHEIMLSCLGNRACDPHANASECGSDFAYFYFVSFIFLCSFLMLNLFVAVIMDNFEYLTRDSSILGPHHLDEFIRVWAEYDPAACGRISYNDMFEMLKHMSPPLGLGKKCPARVAYKRLVRMNMPISNEDMTVHFTSTLMALIRTALEIKLAPAGTKQHQCDAELRKEISSVWANLPQKTLDLLVPPHKPDEMTVGKVYAALMIFDFYKQNKTTRDQTHQAPGGLSQMGPVSLFHPLKATLEQTQPAVLRGARVFLRQKSATSLSNGGAIQTQESGIKESLSWGTQRTQDVLYEARAPLERGHSAEIPVGQPGALAVDVQMQNMTLRGPDGEPQPGLESQGRAASMPRLAAETQPAPNASPMKRSISTLAPRPHGTQLCNTVLDRPPPSQVSHHHHHRCHRRRDKKQRSLEKGPSLSVDTEGAPSTAAGSGLPHGEGSTGCRRERKQERGRSQERRQPSSSSSEKQRFYSCDRFGSREPPQPKPSLSSHPISPTAALEPGPHPQGSGSVNGSPLMSTSGASTPGRGGRRQLPQTPLTPRPSITYKTANSSPVHFAEGQSGLPAFSPGRLSRGLSEHNALLQKEPLSQPLASGSRIGSDPYLGQRLDSEASAHNLPEDTLTFEEAVATNSGRSSRTSYVSSLTSQSHPLRRVPNGYHCTLGLSTGVRARHSYHHPDQDHWC | Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. This alpha-1B subunit gives rise to N-type calcium currents. N-type calcium channels belong to the 'high-voltage activated' (HVA) group. They are involved in pain signaling. Calcium channels containing alpha-1B subunit may play a role in directed migration of immature neurons. Mediates Ca(2+) release probability at hippocampal neuronal soma and synaptic terminals . | Q02294 |
A8E2V9 | PA2B_TRIGS | Phosphatidylcholine 2-acylhydrolase | Trimeresurus | MRTLWIVAVLLVGEGSLIQLWEMIFQEMGKGAAKKYGLYGCNCGMGHRGRPVDATDRCCSVHKCCYKKLTDCDPKTDRYSYSWENGAIVCGGDDPCRKEVCECDKATTICFRDNLDTYDKKYKIYLKFLCKKPEPC | PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. | A8E2V9 |
P17692 | CDGT_BACS8 | Raw-starch-digesting amylase | Bacillus | MKKFLKMTAAFSLGLSLAFGLFSPAQAAPDTSVSNKQNFSTDVIYQIFTDRFSDGNPANNPTGAAFDGTCTNLRLYCGGDWQGIINKINDGYLTGMGVTAIWISQPVENIYSIINYSGVNNTAYHGYWARDFKKTNPAYGTIADFQNLIAAAHAKNIKVIIDFAPNHTSPASSDQPSFAENGRLYDNGTLLGGYTNDTQNLFHHNGGTDFSTTENGIYKNLYDLADLNHNNSTSDVYLKDAIKMWLDLGIDGIRMDAVKHMPFGWQKSFMAAVNNYKPVFTFGEWFLGVNEVGPENHKFANESGMSLLDFRFAQKVRQVFRDNTDNMYGLKAMLEGSAADYAQVDDQVTFIDNHDMERFHASNANRRKLEQALAFTLILARVPAIYYGTEQYMSGGTDPDNRARIPSFSTSTTAYQVIQKLAPLRKSNPAIAYGSTQERWINNDVLIYERKFGSNVAVVAVNRNLNAPASISGLVTSLPQGSYNDVLGGLLNGNTLTVGSGGAASNFTLAAGGTAVWQYTAATATPTIGHVGPMMAKPGVTITIDGRGFGSSKGTVYFGTTAVSGANITSWEDTQIKVKIPAVAGGIYNIKVANAAGTASNVYDNFEVLSGDQVSVRFVVNNATTALGQNLYLTGNVSELGNWDPAKAIGPMYNQVVYQYPNWYYDVSVPAGKTIEFKFLKKQGSTVTWEGGSNHTFTAPSSGTATINVNWQP | This endo-type adsorbable amylase is capable to digest raw starch. | P17692 |
Q9LZR3 | CSLA9_ARATH | Protein RESISTANT TO AGROBACTERIUM TRANSFORMATION 4 | Arabidopsis | MELGDTTSVIPDSFMGYRDDITMQMSMVLDQIRAPLIVPALRLGVYICLTMSVMLFVERVYMGIVISLVKLFGRKPDKRFKYEPIKDDIELGNSAYPMVLIQIPMFNEREVYQLSIGAACGLSWPSDRIVIQVLDDSTDPTIKDLVEMECSRWASKGVNIKYEIRDNRNGYKAGALKEGMKKSYVKSCDYVAIFDADFQPEADFLWRTVPYLLHNPKLALVQARWKFVNSDECLMTRMQEMSLDYHFTVEQEVGSSTYAFFGFNGTAGIWRISALNEAGGWKDRTTVEDMDLAVRASLKGWKFLYLGSLKVKNELPSTFKAYRYQQHRWSCGPANLFRKMAFEIMTNKNVTLWKKVHVIYSFFVVRKLVAHIVTFIFYCVILPATVLVPEVTVPKWGAVYIPSVITLLNAVGTPRSLHLMVFWILFENVMSLHRTKATFIGLLEGGRVNEWIVTEKLGDVKAKSATKTSKKVIRFRFGDRIHVLELGVGMYLLFVGCYDAFFGKNHYYLYLFAQAIAFFIAGFGQIGTIVPNH | Possesses glucomannan synthase and mannan synthase activities in vitro. Mannan synthase consists of a 4-beta-mannosyltransferase activity on mannan using GDP-mannose. The beta-1,4-mannan product is the backbone for galactomannan synthesis by galactomannan galactosyltransferase. Galactomannan is a noncellulosic polysaccharides of plant cell wall . Required for lateral root development . | Q9LZR3 |
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