UniProt ID
stringlengths 6
10
| Protein Sequence
stringlengths 5
15.6k
| Functional Description
stringlengths 6
12.4k
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A6UZK0 | MARLKEIYRKEIAPKLKEELQLANVMEVPRVTKITLNMGLGEAVGDKKIIENAVADLEKITGQKPIVTYARKSIAGFKIREGWPIGVKVTLRSDRMYEFLDRLLSISLPRVRDFRGLNAKSFDGRGNYSMGVKEQIIFPEIDYDKIDALRGLDITLTTTARTDDEGRALLRAFKFPFRN | This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs. Part of the 50S ribosomal subunit; part of the 5S rRNA/L5/L18/L25 subcomplex. Contacts the 5S rRNA and the P site tRNA. Forms a bridge to the 30S subunit in the 70S ribosome. Belongs to the universal ribosomal protein uL5 family. |
Q96316 | MGSTVAAALLLFLAAVPAVFAATFKVGDISGWTSNLDYTVWLTGKTFRVGDTLEFVYGLSHSVSVVDKAGYDNCDSSGATQNFADGDTKIDLTTVGTMHFLCPTFGHCKNGMKLAVPVLAAAPSPSTPSSPPSTPSTPSSPPSTPSTPSSPPSPPSPPSPSLPPSSLPPSASPPTNGTPDSETLTPPPAPLPPSLSPNAASKGVMSYGIIGVTMILMYAVMT | Probably acts as an electron carrier involved in oxygen activation and/or lignin formation. |
Q41709 | MLLRTAAASSLSLFNPNAEPSRSVPVLANNASRLVVRAAKGSTNHRALTGVIFEPFEEVKKELDLVPTVPQASLARQKYVDESEAAVNEQINVEYNVSYVYHALFAYFDRDNVALRGLAKFFKESSEEEREHAEKLMEYQNRRGGKVKLQSIVMPLSEFDHADKGDALHAMELALSLEKLTNEKLLHLHSVATKNGDVQLADFVESEFLGEQVESIKRISEYVAQLRRVGKGHGVWHFDQMLLHEGGHLA | Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation (By similarity). 4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O Oligomer of 24 subunits. There are two types of subunits: L (light) chain and H (heavy) chain. The major chain can be light or heavy, depending on the species and tissue type. The functional molecule forms a roughly spherical shell with a diameter of 12 nm and contains a central cavity into which the insoluble mineral iron core is deposited (By similarity). Belongs to the ferritin family. |
Q5HPY6 | MAKNIAKALLDIEAVSLSPNDLFTWSSGIKSPIYCDNRITLGYPEVRNAIRDGLIQLIKEHFSNVEIISGTATAGIPHAAYISEKMELPMNYVRSKSKSHGKQNQIEGAKSENKNVVVVEDLISTGGSSITAVEALEEAGANVLGVVAIFTYGLAKADETFNKAHIPFYTLSDYNELIEVAKDDGKISLNDIQTLVDWRDNLS | Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. Homodimer. Belongs to the purine/pyrimidine phosphoribosyltransferase family. PyrE subfamily. |
A9HHS1 | MKSGIHPDYHEINVIMTDGTEYKTRSCYAQPGATLRLDIDPKSHPAWTGVQRMLDTGGQVAKFNKKFGGLGRRAKA | Binds the 23S rRNA. Part of the 50S ribosomal subunit. Belongs to the bacterial ribosomal protein bL31 family. Type A subfamily. |
B0XWL3 | MKHLASSIALTLLLPAVQAQQTVWGQCGGQGWSGPTSCVAGAACSTLNPYYAQCIPGATATSTTLTTTTAATTTSQTTTKPTTTGPTTSAPTVTASGNPFSGYQLYANPYYSSEVHTLAMPSLPSSLQPKASAVAEVPSFVWLDVAAKVPTMGTYLADIQAKNKAGANPPIAGIFVVYDLPDRDCAALASNGEYSIANNGVANYKAYIDAIRAQLVKYSDVHTILVIEPDSLANLVTNLNVAKCANAQSAYLECVDYALKQLNLPNVAMYLDAGHAGWLGWPANLGPAATLFAKVYTDAGSPAAVRGLATNVANYNAWSLSTCPSYTQGDPNCDEKKYINAMAPLLKEAGFDAHFIMDTSRNGVQPTKQNAWGDWCNVIGTGFGVRPSTNTGDPLQDAFVWIKPGGESDGTSNSTSPRYDAHCGYSDALQPAPEAGTWFQAYFEQLLTNANPSF | The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the disaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose. Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains. Has a modular structure: a carbohydrate-binding module (CBM) at the N-terminus, a linker rich in threonines, and a C-terminal exocellobiohydrolase catalytic module. The genes for catalytic modules and CBMs seem to have evolved separately and have been linked by gene fusion. Belongs to the glycosyl hydrolase 6 (cellulase B) family. |
A5VQY7 | MKLNDLRDKPGSVKARKRVGRGIGSGTGKTGGRGVKGQKSRSGVSINGFEGGQMPIYRRLPKRGFTNIFAKSFNVVSLGRIQAAIDAGKLDAKAVVNLDSLKAAGVIRRAKDGVRILSDGELKAKVAFEVAGASKAAVEKIEKAGGSIKLPEAAAE | Binds to the 23S rRNA. Part of the 50S ribosomal subunit. Belongs to the universal ribosomal protein uL15 family. |
Q2FPN5 | MSAKQLMFNENARHALLEGVNKVANTVKITLGPKGRNVVLDKAGGPVVTNDGVTIAKEIELKDKFENVGAKLIKEVASKTQDTTGDGTTTATVLAQAMITEGIKNITAGANPIEIKKGILKAVDAAVASIKAKSIEVKDKETINRIAIISANNDEEIGNLISEAMDRVGYNGVITVENSKTLETTLEHVEGMQFDRGYISPYMVTDQERRVVEFEEPYILITDRKISSLKTLIPVLEMIAQSGKPLLIIADDVDGEAQTALILNIIRGAIKVCAVKAPEFGDVRKEVLQDIAILTGGTVISEERNLAIEDVTLDMLGQARTVKVDQDKTTIVGGKGKKSDIDTRKKLIESQLNITEKKYDKTTLQNRLAKLSGGVAVIKAGAATETEVKEKKMRIDDALNATKAAVEEGYVAGGGVTLFRAIKALESMKADPEQMIGVNIVKRALEEPLRQIADNAGREGAEVIAMIKSNASETYGYNAKTDTYEDLLQAGVLDPTKVVRSGLQNAASIAGMLLSTEAVVVDFDEEKDKTSAAIII | Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. ATP + H2O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide. Forms a cylinder of 14 subunits composed of two heptameric rings stacked back-to-back. Interacts with the co-chaperonin GroES. Belongs to the chaperonin (HSP60) family. |
Q8HYA9 | MKFTIAFAGLLGVFLTPALADYSISVNDDGNSGGSGQQSVSVNNEHNVANVDNNNGWNSWNALWDYRTGFAVTRLFEKKSCIVHKMKKEAMPSLQALDALVKEKKLQGKGPGGPPPKSLRYSVNPNRVDNLDKFGKSIVAMCKGIPTYMAEEIQGANLISYSEKCISANILWILNISFCGGIAEN | Has mitogenic activity and may be involved in maintaining the integrity of the gastric mucosal epithelium. Shows abundant granular cytoplasmic staining, with perinuclear accentuation suggestive of the Golgi apparatus. Highly expressed specifically in surface cells of the antrum mucosa from where it is secreted. Belongs to the gastrokine family. |
Q5R878 | MEGSKTSNNSTMQVSFVCQRCSQPLKLDTSFKILDRVTIQELTAPLLTTAQAKPGETQEEETNSGEEPFIETPRQDGVSRRFIPPARMMSTESANSFTLIGEASDGGTMENLSRRLKVTGDLFDIMSGQTDVDHPLCEECTDTLLDQLDTQLNVTENECQNYKRCLEILEQMNEDDSEQLQMELKELALEEERLIQELEDVEKNRKIVAENLEKVQAEAERLDQEEAQYQREYSEFKRQQLELDDELKSVENQMRYAQMQLDKLKKTNVFNATFHIWHSGQFGTINNFRLGRLPSVPVEWNEINAAWGQTVLLLHALANKMGLKFQRYRLVPYGNHSYLESLTDKSKELPLYCSGGLRFFWDNKFDHAMVAFLDCVQQFKEEVEKGETRFCLPYRMDVEKGKIEDTGGSGGSYSIKTQFNSEEQWTKALKFMLTNLKWGLAWVSSQFYNK | Plays a central role in autophagy. Acts as core subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate; different complex forms are believed to play a role in multiple membrane trafficking pathways: PI3KC3-C1 is involved in initiation of autophagosomes and PI3KC3-C2 in maturation of autophagosomes and endocytosis. Involved in regulation of degradative endocytic trafficking and required for the abcission step in cytokinesis, probably in the context of PI3KC3-C2. Essential for the formation of PI3KC3-C2 but not PI3KC3-C1 PI3K complex forms. Involved in endocytosis. May play a role in antiviral host defense (By similarity). Beclin-1-C 35 kDa localized to mitochondria can promote apoptosis; it induces the mitochondrial translocation of BAX and the release of proapoptotic factors. A homodimeric form is proposed to exist; this metastable form readily transits to ATG14- or UVRAG-containing complexes with BECN1:UVRAG being more stable than BECN1:ATG14 (By similarity). Component of the PI3K (PI3KC3/PI3K-III/class III phosphatidylinositol 3-kinase) complex the core of which is composed of the catalytic subunit PIK3C3, the regulatory subunit PIK3R4 and BECN1 associating with additional regulatory/auxilliary subunits to form alternative complex forms. Alternative complex forms containing a forth regulatory subunit in a mutually exclusive manner are PI3K complex I (PI3KC3-C1) containing ATG14, and PI3K complex II (PI3KC3-C2) containing UVRAG. PI3KC3-C1 displays a V-shaped architecture with PIK3R4 serving as a bridge between PIK3C3 and the ATG14:BECN1 subcomplex. Both, PI3KC3-C1 and PI3KC3-C2, can associate with further regulatory subunits, such as RUBCN, SH3GLB1/Bif-1 and AMBRA1 (By similarity). PI3KC3-C1 probably associates with PIK3CB (By similarity). Interacts with AMBRA1, GOPC, GRID2 (By similarity). Forms a complex with PPP2CA and AMBRA1; AMBRA1 and BECN1 components of the complex regulate MYC stability via different pathways. Interacts with BCL2 and BCL2L1 isoform Bcl-X(L); the interaction inhibits BECN1 function in promoting autophagy by interfering with the formation of the PI3K complex. Interacts with cytosolic HMGB1; inhibits the interaction of BECN1 and BCL2 leading to promotion of autophagy. Interacts with USP10, USP13, VMP1, DAPK1, RAB39A. Interacts with the poly-Gln domain of ATXN3; the interaction causes deubiquitination at Lys-402 and stabilizes BECN1. Interacts with SLAMF1. Interacts with TRIM5; the interaction causes activation of BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2. Interacts with active ULK1 (phosphorylated on 'Ser-317') and MEFV simultaneously. Interacts with WDR81 and WDR91; negatively regulates the PI3 kinase/PI3K activity associated with endosomal membranes. Interacts with LAPTM4B; competes with EGFR for LAPTM4B binding; regulates EGFR activity. Interacts with TRIM50. Interacts with TRIM16. Interacts with ATG14; this interaction is increased in the absence of TMEM39A (By similarity). Interacts with WASHC1; preventing interaction with AMBRA1 and the DCX(AMBRA1) complex and subsequent ubiquitination (By similarity). Interacts with TRIM17 (By similarity). Interacts with BCL2L10/BCL-B (via BH1 domain) (By similarity). Interaction with ATG14 promotes translocation to autophagosomes. Expressed in dendrites and cell bodies of cerebellar Purkinje cells. The C-terminal evolutionary conserved domain (ECD) contains poly-Gln-binding domains such as the ATXN3 poly-Gln motif, consistent with structural docking models revealing two highly scored poly-Gln-binding pockets in the ECD (By similarity). As some binding is observed with BECN1 lacking the ECD, other domains of BECN1 may also interact with ATXN3 (By similarity). Phosphorylation at Thr-119 by DAPK1 reduces its interaction with BCL2 and BCL2L1 and promotes induction of autophagy. In response to autophagic stimuli, phosphorylated at serine residues by AMPK in an ATG14-dependent manner, and this phosphorylation is critical for maximally efficient autophagy. Polyubiquitinated by NEDD4, both with 'Lys-11'- and 'Lys-63'-linkages (By similarity). 'Lys-11'-linked polyubiquitination leads to degradation and is enhanced when the stabilizing interaction partner VPS34 is depleted (By similarity). Deubiquitinated by USP10 and USP13, leading to stabilize the PIK3C3/VPS34-containing complexes (By similarity). Polyubiquitinated at Lys-402 with 'Lys-48'-linkages (By similarity). 'Lys-48'-linked polyubiquitination of Lys-402 leads to degradation (By similarity). Deubiquitinated by ATXN3, leading to stabilization (By similarity). Ubiquitinated at Lys-437 via 'Lys-63'-linkage by the DCX(AMBRA1) complex, thereby increasing the association between BECN1 and PIK3C3 to promote PIK3C3 activity (By similarity). Proteolytically processed by caspases including CASP8 and CASP3; the C-terminal fragments lack autophagy-inducing capacity and are proposed to induce apoptosis. Thus the cleavage is proposed to be an determinant to switch from autophagy to apoptosis pathways affecting cellular homeostasis including viral infections and survival of tumor cells. Expanded poly-Gln tracts inhibit ATXN3-BECN1 interaction, decrease BECN1 levels and impair starvation-induced autophagy (By similarity). Belongs to the beclin family. |
C0HKK5 | GIIPCGESCVFIPCITSIVGCSCKSKVCYKN | Probably participates in a plant defense mechanism. The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin. This is a cyclic peptide. Belongs to the cyclotide family. Bracelet subfamily. This peptide is cyclic. The start position was chosen by similarity to Oak1 (kalata B1) for which the DNA sequence is known. |
A1E9I6 | MNPLIAAASVIAAGLAVGLASIGPGVGQGTAAGQAVEGIARQPEAEGKIRGTLLLSLAFMEALTIYGLVVALALLFANPFV | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has four main subunits: a(1), b(1), b'(1) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta, b and b' chains. In plastids the F-type ATPase is also known as CF(1)CF(0). Belongs to the ATPase C chain family. |
Q82GG6 | MAKIIAFDEEARRGLERGMNQLADAVKVTLGPKGRNVVLEKKWGAPTITNDGVSIAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVREGLRNVAAGANPMALKRGIEKAVEAVSGALLEQAKDVETKEQIASTASISAADTQIGELIAEAMDKVGKEGVITVEESQTFGLELELTEGMRFDKGYISAYFATDMERMEASLDDPYILIANSKISSVKDLLPLLEKVMQSGKPLLIIAEDVEGEALSTLVVNKIRGTFKSVAVKAPGFGDRRKAMLGDIAILTGGEVISEEVGLKLENASIDLLGRARKVVITKDETTIVDGAGSADQVAGRVNQIRAEIENSDSDYDREKLQERLAKLAGGVAVIKAGAATEVELKERKHRIEDAVRNAKAAVEEGIVAGGGVALIQASSVFEKLELTGDEATGANAVRLALEAPLKQIAVNGGLEGGVIVEKVRNLPVGHGLNAATGEYVDMIAEGIIDPAKVTRSALQNAASIAALFLTTEAVIADKPEKAAAGGAPGGMPGGDMDF | Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. ATP + H2O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide. Forms a cylinder of 14 subunits composed of two heptameric rings stacked back-to-back. Interacts with the co-chaperonin GroES. Belongs to the chaperonin (HSP60) family. |
D6VYI6 | MALEEVVRYLGPHNEIPLTLTRDSETGHFLLKHFLPILQQYHDTGNINETNPDSFPTDEERNKLLAHYGIAVNTDDRGELWIELEKCLQLLNMLNLFGLFQDAFEFEEPETDQDEEDPSHSKLPENKTKSENSKDNISSKRINNLQDMSLDSDAHRELGSPLKKLKIDTSVIDAESDSTPNTARGKPNDDINKGPSGDNENNGTDDNDRTAGPIITFTHDLTSDFLSSPLKIMKALPSPVVNDNEQKMKLEAFLQRLLFPEIQEMPTSLNNDSSNRNSEGGSSNQQQQHVSFDSLLQEVNDAFPNTQLNLNIPVDEHGNTPLHWLTSIANLELVKHLVKHGSNRLYGDNMGESCLVKAVKSVNNYDSGTFEALLDYLYPCLILEDSMNRTILHHIIITSGMTGCSAAAKYYLDILMGWIVKKQNRPIQSGTNEKESKPNDKNGERKDSILENLDLKWIIANMLNAQDSNGDTCLNIAARLGNISIVDALLDYGADPFIANKSGLRPVDFGAGTSKLQNTNGGDENSKMVSKGDYDGQKNGKAKKIRSQLLKNPPETTSLINDVQNLLNSISKDYENETVQYNEKLEKLHKELNEQREELANSREQLANVKQLKDEYSLMQEQLTNLKAGIEEEEESFREESKKLGIIADESSGIDWDSSEYDADEPFKVEFLSDFLEDKLQKNYEGDISKLLEAESKEQIMEQIRNQLPAEKIQSMLPPTVLLKARINAYKRNDKHLTNVLDTISTKQSELENKFRRVLSLCLKIDENKVDNMLDGLLQAISSEDPQDIDTDEMQDFLKKHAS | Part of a complex involved in cell-cycle-dependent transcription. SWI4 and SWI6 are required for formation of the cell-cycle box factor-DNA complex. The repeated element in the upstream region of HO (5'-CACGAAAA-3') is called the cell cycle box (CCB). Component of the transcription complex MCB-binding factor (MBF) composed of SWI6 and MBP1. Component of the transcription complex SCB-binding factor (SBF) composed of SWI6 and SWI4. Interacts with MSA1 and STB1. Phosphorylated by CDC28 and dephosphorylated by CDC14. Present with 3340 molecules/cell in log phase SD medium. |
A0A0A0NW69 | MTPPVTAPYCRFEKLGASDLDGDETLLGVIEHRTGHTGVSLAEGCPRTAVHTTTREDESFAEAWHAEGPKESGSHDGVAWARTPDYLFGVARVPEGGRYAAGTAAVYTGIFDLIGTLGYPSLARTWNYVSGINTPNADGLEVYRDFCVGRAEALDARGIDPATMPAATGIGAHGGGITCYFIAARAGDRVNMENPAVLTAHRYPQRYGPRPPVFSRATWLSPPGADDGRLFVSATAGIVGHETVHHGDVAAQCEVSLENIARVIGAENLGRHGLRRGYALADVDHLKVYVRHREDISTVRRICAERLSREATVAVLHTDIARTDLLVEIEGVVA | Involved in the biosynthesis of the macrocyclic amino acid-linked polyketides rapamycin which is a potent immunosuppressant that prevents T-cell proliferation through initial binding to the immunophilin FKBP12. Catalyzes the hydrolysis of chorismate via a 1,4-conjugate elimination of water to yield (4R,5R)-4,5-dihydroxycyclohexa-1,5-dienecarboxylic acid (DCDC). chorismate + H2O = (3R,4R)-3,4-dihydroxy-3,4-dihydrobenzoate + pyruvate Monomer. Cells lacking this gene are unable to produce rapamycin. Belongs to the FkbO/Hyg5 family. Extended N-terminus. |
Q8LFR7 | MSGLQAQDSACSLDKPSKDVVATETKPKKRICCACPDTKKLRDECIVEHGESACTKWIEAHILCLRSEGFKV | Copper chaperone for cytochrome c oxidase (COX). Binds 2 copper ions and delivers them to the Cu(A) site of COX (By similarity). Belongs to the COX17 family. |
B5BFZ9 | MKRTKSIHHASFRKSWSARHLTPVALAVTAVFMLAGCEKSDETVSLYQNADDCSAANPGKSAECTAAYNNALKEAERTAPKYATREDCVAEFGEGQCQQAPAQAGMAPENQAQAQQSSGSFWMPLMAGYMMGRLMGGGAGFAQQPLFSSKNPASPAYGKYTDAAGKNYGAAQPGRTMTVPKTAMAPKPATTTTVTRGGFGESVAKQSTMQRSAAGTSTRSMGG | Belongs to the UPF0441 family. |
A4IIL4 | MTHWFHRNPLKATAPVSFNFYGVASTQAASKICSDLRSTRARLLELFSDITCNHEMMKNATDAYFSLLLGFIDSLDGGTQDNKLRYIQNFKWTDTLQGNAPSAQQDAVFELVSMGFNVALWYTKYASRLAGKEDITEEEAKEVHRSLKIAAGVFKHLKENHIPKLITPVEKGRDLETRVIDAYTVQCQAEAQEVTIARAIELKHNPGLIAALAYETANYYQKVDHTLATLDPVYIAKWRSYTQLKMCFYMAYSYCYHGQTLLSADKCGEAIRSLQEAEKFYGKAEALCKEYGETKGPGTTAKPSGHLFFRKMGTLVRNTLEKCQRENGFIYFQKVPPEAPQLELKANYGLVEPVPFEFPAMTSQWSPETHTGFDLTKRPKDDSAKPKKEEEVKPMKEPDIKPQKDSGCQIS | Belongs to the BROX family. |
B8DYT2 | MKEEVLGLPIDKIEKKIKEYDFSPRISNIGYVKHVGDGVAEVSLLNSAFIGEMVVFESGIQGMVLSLKEDSVGVILFGKDEYVKEGDVVYSTSKILQVPTGNGFLGRVIDPLGNPIDGGGLIFPEAYVPIDNEAPSIFDREPVKEPLYTGIRTIDALIPIGHGQRELILGDRQTGKTTIALDTIISQKNYGTICIYVAIAQKRTNIARIVQTLREYGALSNTIVIATFPDEPPALRYIAPMAGCAMGEYFMRQGERVLIVYDDLTKHANTYREVALLLRRVPGREAYPGDIFYLHAHLLERAAKLNKRLGGGALTALPIAETLSGEISTYIPTNLISITDGQIYLDTNLFNAGIRPAINVGLSVSRVGGSAQPKGMRQVAGRLRLDLAQYREYAMFLEFGTELDMATKKKIERGRRVEELLKQGAHEVQPIEEQIISFYLANGGFLDNYPVEKVKDVVIKYIAYLKLKYSSVLTFLREELQLSDQIIYQLHNIFQEFEKEVYANSTGS | Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF(1) is attached to CF(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase alpha/beta chains family. |
A6VIL1 | MELNIKMDRSRELFEESRKYLVGGVNSPVRSFKPFPFFVKSAKDCFLYDEDGNEFIDYCLAYGPMVLGHANENILNAVKSQMDLGTAYGVPSEKEIILAKEVINRIPCAEMVRFVNSGTEATMGAIRLARGVTKRNKIIKFEGAFHGAHDYVLVKTGSGALTHGAPNSPGIPEDTTKNTLLIPFNDEDAVKKVISENKDEIACIILEPVMGNVGCILPKDGYLQFLREITEENGIILIFDEVITGFRLSKGGAQEYYGIKSDLATVGKILGGGFPIGAITGKKEYMEQFSPNGQIYQAGTFNGNPVSVTAGIETLKNLDDKFYKETTKKADILSSFLRETAEKYNVPAKVYNVASIFQIYFNDKEIVTYEDAKSSDTEKFMRYFYTLLENGVFIAPSQFECCFTSIKHNDEVLEKTMNAIDIAMKKL | (S)-4-amino-5-oxopentanoate = 5-aminolevulinate Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2. Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily. |
Q96QX4 | MASSIICQEHCQISGQAKIDILLVGDVTVGYLADTVQKLFANIAEVTITISDTKEAAALLDDCIFNMVLLKVPSSLSAEELEAIKLIRFGKKKNTHSLFVFIIPENFKGCISGHGMDIALTEPLTMEKMSNVVKYWTTCPSNTVKTENATGPEELGLPLQRSYSEHLGYFPTDLFACSESLRNGNGLELNASLSEFEKNKKISLLHSSKEKLRRERIKYCCEQLRTLLPYVKGRKNDAASVLEATVDYVKYIREKISPAVMAQITEALQSNMRFCKKQQTPIELSLPGTVMAQRENSVMSTYSPERGLQFLTNTCWNGCSTPDAESSLDEAVRVPSSSASENAIGDPYKTHISSAALSLNSLHTVRYYSKVTPSYDATAVTNQNISIHLPSAMPPVSKLLPRHCTSGLGQTCTTHPNCLQQFWAY | Transcription regulator of both male and female germline differentiation. Suppresses genes involved in spermatogonial stem cells maintenance, and induces genes important for spermatogonial differentiation. Coordinates oocyte differentiation without affecting meiosis I (By similarity). Forms both hetero- and homodimers with SOHLH1. Translocates from the cytoplasm into the nucleus and the translocation is dependent on SOHLH1 expression. |
Q6GBX9 | MQLNSNGWHVDDHIVVAVSTGIDSMCLLYQLLNDYKDSYRKLTCLHVNHGVRSASIEEARFLEVYCERHHIDLHIKKLDLSHSLDRNNSIQNEARIKRYEWFDEMMNVLEADVLLTAHHLDDQLETIMYRIFNGKSTRNKLGFDELSKRKGYQIYRPLLAVSKKEIKQFQERYHIPYFEDESNKDNKYVRNDIRNRIIPAIDENNQLKASHLLKLKQWHDEQYDILQYSAKQFIQEFVKFDEQSKYLEVSRQAFNNLPNSLKMVVLDCLLSKYYELFNISAKTYEEWFKQFSSKKAQFSINLTDKWIIQIAYGKLIIMAKNNGDTYFRVQTIEKPGNYIFNKYRLEIHSNLPKCLFPLTVRTRQSGDTFKLNGRDGYKKVNRLFIDCKVQQWVRDQMPIVLDKQQRIIAVGDLYQQQTIKQWIIISKNGDE | Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2) The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding. Belongs to the tRNA(Ile)-lysidine synthase family. |
B5FUB0 | MTSSYLHFPDFDPVIFSIGPVALHWYGLMYLVGFVFAMWLAVRRANRPGSGWTKNEVENLLYAGFLGVFLGGRIGYVLFYNFPLFLDNPLYLFRVWDGGMSFHGGLIGVILVMIIFARRTKRSFFQVSDFIAPLIPFGLGAGRLGNFINGELWGRVDPDFRFAMLFPGSRAEDIALLPSHPQWQPIFDTYGVLPRHPSQLYELALEGVVLFIILNLFIRKPRPMGAVSGLFLIGYGAFRIIVEFFRQPDAQFTGAWVQYISMGQILSIPMIIAGAIMMVWAYRRRPQQHVS | Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins. 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-cysteinyl-[prolipoprotein] = H(+) + S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[prolipoprotein] + sn-glycerol 1-phosphate Protein modification; lipoprotein biosynthesis (diacylglyceryl transfer). Belongs to the Lgt family. |
P77868 | MLDLTPQSKKISIQIGGMTCQSCANRIEKVLNKKPFVQQAGVNFAAEEAQVVFDATQASEAQIIEIIHKTGFSAHIKQANELPIEENTSIPWRLIVLWIINIPFLIGMLGMIGGSHNLMLPPIWQFALASIVQLWLAIPFYRGAIGSIRGGLTNMDVLVSTGTLTIYLYSAFMLFYHANHAMGHVYFEASVMVIGFVSLGKFLEDRTKKHSLNSLSMLLQLTPKKVTVLRNEKWIEIALDQVNIGEIIRANQGERIAADGVIESGNGWCDESHLTGESRPEEKQKGGKVLAGAMVTEGSIIYRANQLGSQTLLGDMMNALSDAQGSKAPIARFADKVTSVFVPVVLVISLVTFALTYILTNDSVSSLIHAVSVLVIACPCALGLATPAAIMVGLGKAVNAGVWFKDAAAMEETAHVDTVVLDKTGTLTKGELEISALWQPQSAVYSEDDLYRFAAAVERQANHPIAKAIVQAAEXKMLEIPTALFSKMEVGQGIQAELEQVGTIKVGKPDYCGLILPKNLEDIWQIASIVAVSINDEPIGAFALTDTLKNDSLHAIQRLQQQNIDVVIMSGDQQSVVDYIAKQLGIKKAFGKLTPRDKAEQIQKLKDLGHIVAMVGDGINDAPALASANVSFAMKSSSDIAEQTASATLMQHSVNQLVDALFIARATLKNIKQNLFFALIYNILGIPLAAFGFLSPIIAGAAMALSSISVLMNALRLKKVRF | ATP + H2O = ADP + H(+) + phosphate Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily. |
Q5P224 | MDDKEILLANPRGFCAGVERAIEIVEQALARFGAPIYVRHEVVHNKFVVDGLRAKGAIFVEELDEVPTGQTVIFSAHGVPQAVRSEAERRGLRVFDATCPLVTKVHLEVARMREQGREIVMIGHKGHPEVEGTMGQVGDGIHLVEVVQDVANIEVADPQQLAYVTQTTLSVDDAATLVAALRARFPAIVGPKKDDICYATQNRQDAVKFMAPRVDVVFVVGSRNSSNSNRLREVAELLGVPAYLVDNAEGIEPIWLEDKKRVGVTAGASAPEVLVDAVVERLKELGASSVRTLEGVPERVTFPLPRELQTPD | Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis. H2O + isopentenyl diphosphate + 2 oxidized [2Fe-2S]-[ferredoxin] = (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin] dimethylallyl diphosphate + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin] Binds 1 [4Fe-4S] cluster per subunit. Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from (2E)-4-hydroxy-3-methylbutenyl diphosphate: step 1/1. Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 6/6. Belongs to the IspH family. |
A2REZ8 | MKLLLFITIAYLLGSIPTGLWIGQYFYHINLREHGSGNTGTTNTFRILGVKAGTATLAIDMFKGTLSILLPIIFGMTSISSIAIGFFAVLGHTFPIFANFKGGKAVATSAGVLLGFAPLYLFFLASIFVLVLYLFSMISLASVVSAIVGVLSVLTFPAIHFLLPNYDYFLTFIVILLAFIIIIRHKDNISRIKHHTENLIPWGLNLSKQVPKK | Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP. an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + phosphate Lipid metabolism; phospholipid metabolism. Probably interacts with PlsX. Belongs to the PlsY family. |
Q8AA39 | MNISYNWLKEYVNFDLTPDETAAALTSIGLETGGVEEVQTIKGGLEGLVIGEVLTCEEHPNSDHLHITTVNLGDGEPVQIVCGAPNVAAGQKVVVATLGTKLYDGDECFTIKKSKIRGVESTGMICAEDEIGIGTDHAGIIVLPAEAVPGTLAKDYYNIKSDYVLEVDITPNRADACSHYGVARDLYAYLIQNGKQATLQRPSVDGFKVENHDLDIEVVVENSEACPHYAGVTVKGVTVKESPEWLQNKLRLIGVRPINNVVDITNYIVHAFGQPLHCFDAGKIKGNEVIVKTLPEGTPFVTLDEVERKLSERDLMICNKEEAMCIAGVFGGLDSGSTEATTDVFIESAYFHPTWVRKTARRHGLNTDASFRFERGIDPNGVIYCLKLAALMVKELAGGTISSEIKDVCVAVPQDFMVELSYEKVNSLIGKVIPVETIKSIVTSLEMKIMNETVDGLTLAVPPYRVDVQRDCDVIEDILRIYGYNNVEIPTTLNSSLTTKGEHDKSNKLQNLVAEQLVGCGFNEILNNSLTRAAYYDGLENYSSNHLVMLLNPLSADLNCMRQTLLFGGLESIAHNANRKNADLKFFEFGNCYYFDADKKNPEKVLATYSEDYHLGLWVTGKKVANSWAHPDENSSVYELKAYVENILKRLGLDLHNLVVGNLTDDIFATALSVHTKGGKRLASFGVVTKKLLKAFDIDNEVYYADLNWKELMKAIRSVKISYKEISKFPAVKRDLALLLDKNVQFAEIEKIAYDTEKKLLKEVELFDVYEGKNIEAGKKSYAVSFLLQDETQTLNDKMIDKIMSKLVKNLEDKLNAKLR | ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) + L-phenylalanyl-tRNA(Phe) Binds 2 magnesium ions per tetramer. Tetramer of two alpha and two beta subunits. Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. |
Q48UR6 | MKQLEELLSTSFDIQFNDLTLLETAFTHTSYANEHRLLNVSHNERLEFLGDAVLQLIISEYLFAKYPKKTEGDMSKLRSMIVREESLAGFSRFCSFDAYIKLGKGEEKSGGRRRDTILGDLFEAFLGALLLDKGIDAVRRFLKQVMIPQVEKGNFERVRDYKTCLQEFLQTKGDVAIDYQVISEKGPAHAKQFEVSIVVNGAVLSKGLGKSKKLAEQDAAKNALAQLSEV | Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism. Endonucleolytic cleavage to 5'-phosphomonoester. Homodimer. Belongs to the ribonuclease III family. |
Q8B0H9 | MSVTVKRIIDSTVIVPKLPANEDPVEYPADYFRKSKEIPLYINTTKSLSDLRGYVYQGLKSGNVSIIHVNSYLYGALKDIRGKLDKDWSSFGINIGKAGDTIGIFDLVSVKALDGVLPDGVSDASRTSADDKWLPLYLLGLYRVGRTQMPEYRKKLMDGLTNQCKMINEQFEPLVPEGRDIFDVWGNDSNYTKIVAAVDMFFHMFKKHECASFRYGTIVSRFKDCAALATFGHLCKITGMSTEDVTTWILNREVADEMVQMMLPGQEIDKADSYMPYLIDFGLSSKSPYSSVKNPAFHFWGQLTALLLRSTRARNARQPDDIEYTSLTTAGLLYAYAVGSSADLAQQFCVGDNKYTPDDSTGGLTTNAPPQGRDVVEWLGWFEDQNRKPTPDMMQYAKRAVMSLQGLREKTIGKYAKSEFDK | Encapsidates the genome in a ratio of one N per nine ribonucleotides, protecting it from nucleases. The encapsidated genomic RNA is termed the NC and serves as template for transcription and replication. Replication is dependent on intracellular concentration of newly synthesized N, termed N(0), which corresponds to the protein not associated with RNA. In contrast, when associated with RNA, it is termed N. During replication, encapsidation by N(0) is coupled to RNA synthesis and all replicative products are resistant to nucleases (By similarity). Homomultimerizes to form the nucleocapsid. Binds to viral genomic RNA. N in nucleocapsid binds the P protein and thereby positions the polymerase on the template. Interaction of N(0) with the P protein prevents the uncontrolled aggregation of N(0) (By similarity). The nucleocapsid is synthesized in the cytoplasm, and is subsequently transported via microtubules to the cell periphery. Belongs to the vesiculovirus nucleocapsid protein family. |
B1JVN8 | MAEIKNYTLNFGPQHPAAHGVLRLVLELDGEVIQRADPHIGLLHRATEKLAESKTFIQSVPYMDRLDYVSMMVNEHGYVLAIEKLLGIEVPERAQYIRVLFDEITRVLNHLMWIGAHALDVGAMAVFLYAFREREDLMDVYEAVSGARMHAAYYRPGGVYRDLPDAMPQYKASKIRNEKALAKMNEARSGSVLDFIDDFFTRFPKCVDEYETLLTDNRIWKQRLVGIGVVSPERALQMGLTGPMLRGSGIAWDLRKKQPYEVYDRMDFDVPVGVNGDCYDRYLVRVEEMRQSILIAKQCIEWLRKNPGPVMTDNHKVAPPSRVGMKTNMEDLIHHFKLFTEGFHVPEGEAYAAVEHPKGEFGIYLVSDGANKPYRLKIRAPGFAHLASLDEMARGHMIADAVTIIGTQDIVFGEIDR | 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. a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+) NDH-1 is composed of 14 different subunits. Subunits NuoB, C, D, E, F, and G constitute the peripheral sector of the complex. Belongs to the complex I 49 kDa subunit family. |
Q98Q55 | MINVNEFKPGITFEDEGNIYVVLTAQHSKQGRGQANVKAKVKNLRTGSTTLKSYTGGDKVQKAHIEKKPMDYLYNDGSNIILMDQESFEQIEIDVKKVEWELNFLTEGMKILVRQYQNEILDIEIPINIELKVINAPDAVKGNTTTNPQKKVIVETGYELEVPMFIKEGETIIVSSETGKYGGKSSK | Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase. Protein biosynthesis; polypeptide chain elongation. Belongs to the elongation factor P family. |
O73847 | MHNWKGVWLCSLFLTFGQLWNGILLAYPLDCKDEQGSYTRCTSISLEKLLDRAIQHAELLYRVSEESCTIFEDNFAPFSLVSQRSRNFNSCYTKGLRLPSSKSEAQQVSDKWLLHSVLVLVQSWIEPFVYLQRTLDTYNSLPGSLVNKTKWVSDKLPSLEQGIVVLIRKMLHEGLITTDFQQSVIEIEPSPEITDSSARDYMILNCFRKDAHKMETFLKLLKCRQIKKLNCY | Pituitary gland. Belongs to the somatotropin/prolactin family. |
A5FS84 | MRYSRLFGKTQREIPSDAETISHQLLLRSGMIAQLTAGVYSFMPLAWRSIQKIETIIRQEMNKAGCQELAMPVLQPVEIWQQSGREAPFGQTLFHLKDRKDRNLVLGPTHEEVITDLASRYIQSYRDLPQRLYQIQAKFRDEPRPRGGLIRVREFIMKDMYSFDASPEGLDDSYQTMKQAYESVYRRCGLESMVIDADSGAIGGKASHEFMIVAESGEDSIIYCPKCSYAANAEKAVFKKKTLSKETLKDLEEVATPGQKAISDVARFLAVKPENTLKAVFYMADGKFVMAVIRGDLDINEVKLKNLLKCNDLRLAEDGEVKAAGVVAGSASPVGLKNILIVADDSVENGSNFVAGANKDGFHLKNVNCGRDFRADKMADIALAAEGSACPFCDGTFASKRGVEVGHIFKLGTFLSERFGANFTDAEGVSHPIIMGCYGMGVGRLLAAAIEQNHDEKGIIWPMPIAPYQVYICGLFLDNPVVRESAEKIYKELEAKSIEVLFDDRELTAGVKFNDADLLGIPLRLTISPRNLDKGGVEFKLRRNKESELVPLDSIVERVIATIKSESDL | 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). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS. ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro) Homodimer. Consists of three domains: the N-terminal catalytic domain, the editing domain and the C-terminal anticodon-binding domain. Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 1 subfamily. |
Q5HTR3 | MKNSIISYPRIGANRELKFAIEKYFKNQSSKEELLKSAKDLRIRHWQEIQKAGIDFIPSNDFSLYDNVLDAAVLFNIVHTKYKNLNLDALDEYFAQSRGYQGENGDVTALAMKKWFNTNYHYLVPECDNADIIALTGDKIFKEYLEAKELGIESKPVLIGIFTLFKLIAFKDEKTQKLAKEKLLNAYIELFDKLNELKVTWLELDEPYLVYDLSKEDIALFEEFYQELLNHKKDLKILLQSYFGDLRDIYPKLLESKFDALGLDFIEGKQSLALVQKYGFAKDKILFAGLINGKNIYTNDYAKSLKLIKELQKYTQNIILNTSCSLLHVPYSTEFESKLDSNYLKLFSFAKEKLQELKDLKEILNSSEENPLFRANQELFKNIPERLDEKVKARLKALKKEDFTRTPSFKERALIQKEFLKLPLLPTTTIGSFPQSADVRSNRLAFKQEKISAQNYTEFNQQKIKECIQIQEEIGLDVLVHGEFERNDMVEYFGENLKGFLFTQNGWVQSYGTRCVKPPVIWGDVSRTKPITLAWSKFAQSLSQKIVKGMLTGPVTILNWSFPREDISLKESTEQIALAIRDEVLDLENAGIKIIQIDEAALREKLPLRKSDWHSEYLDWAIPAFNLVHSGVKAKTQIHTHMCYSEFSDILKEIDAMDADVISFEASRSNLSLLDTLKAIRFKTEVGPGVYDIHSPRVPSVEELSLTIEKILNKLPKEQIWINPDCGLKTRAYEEVIASLKNLVTATQKIREQL | Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation. 5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = L-methionine + tetrahydropteroyltri-L-glutamate Binds 1 zinc ion per subunit. Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetE route): step 1/1. Belongs to the vitamin-B12 independent methionine synthase family. |
B5E4L5 | MMNMQNMMRQAQKLQKQMEQSQAELAAMQFVGKSAQDLVQATLTGDKKVVSIDFNPAVVDPEDLETLSDMTVQAINSALEQIDETTKKKLGAFAGKLPF | Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection. Homodimer. Belongs to the YbaB/EbfC family. |
B0FZP3 | MMSSSSSEIDVVKTRIPTYDEDDDTIFYAYETKPDFVNKEPNTVSDASCNTEEQQKTVNDVLIHCQVIYDAMQNLDKKIDVIRRKVSKIQRFRARFLWTNRKRYGYKNYSYQLAKKLKRQKMKKNEVHESFSYPESYSPTLPVSRRENNSPSNLPRPSFRMEEYQRAEPEEDPILSRTPSPVHPSDFSEHNYQPYYASDGAMHGSSSGPCLGNPGANSIYNTYSTDHASAAQPSVTGSLFGNDCYIEEGSITKHPSTWSVEAVVLFLKQTDPLALCPLVDLFRSHEIDGKALLLLTSDVLLKHLGVKLGTAVKLCYYIDRLKQGKCFEN | Putative Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. May be involved in spermatogenesis during sexual maturation (By similarity). Belongs to the SCM family. |
Q6BJG4 | MIRVIQPPLIASKQLFRRYLATGGTFTNKTSQLDRATLTIKDGPVFSGYSFGANKNISGEAVFTTSLVGYPESMTDPSYKGQILCFTQPLIGNYGVPSSTLKDEFNLLKHMESPSVQCIGIVVADVALEYSHWTAVESLQQWCQRSGVAAISGVDTRQLVSYLREKGSSLAKITIGEEYDADEDAAFEDPGSVNLVHKVSTKAPFHISCPEKYAKGLHIAVLDCGAKENILRCLVERGASLTVFPYNYPIDKIANKFDGIFISNGPGDPTHCSSTTENLAKTMEKYHDLPIFGICLGHQLLALASGARTIKMKYGNRAHNIPALDLTTGKCHITSQNHGYSVDAETLDSDWEPYFTNLNDLSNEGMKHKSRPIFSTQFHPEAKGGPLDTAFLFDKFFENIEQYRATNGLNLGNVDDSLLVDILPKGRVL | 2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1. Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate. Belongs to the CarA family. |
P41054 | MAGTDREKALDAALAQIERQFGKGAVMRMGDRSKEPIEVIPTGSTALDVALGVGGLPRGRVIEVYGPESSGKTTLTLHAVANAQKAGGQVAFVDAEHALDPEYAQKLGVDIDNLILSQPDNGEQALEIVDMLVRSGALDLIVIDSVAALVPRAEIEGEMGDSHVGLQARLMSQALRKITSALNQSKTTAIFINQLREKIGVMFGSPETTTGGRALKFYASVRLDIRRIETLKDGTDAVGNRTRVKVVKNKVAPPFKQAEFDILYGQGISREGGLIDMGVEHGFVRKAGAWYTYEGDQLGQGKENARNFLKDNPDLANEIEKKIKEKLGVGVRPEEPTATESGPDAATAESAPAVPAPATAKVTKAKAAAAKS | Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage. Belongs to the RecA family. |
Q6HBW7 | MIKPLIEFCVGNLASGSQAALEKLEKDPNLDVMEYGCLGYCGICFEGPFALVNGEVVQGSTVEELVNNVYEYLDENPMF | Belongs to the UPF0349 family. |
P54043 | MIIMDVSVQRRMAAEILKCGIERVWIDPTQLDRVKMAMSKDDIRALIKEGVIKKKQKKGISSARVKKLKEQRKKGRRRGPGSRRGAAGARTPPKERWMATIRALRKTLKQLRDSGKIDRKVYRKLYRMAKGGAFRSRSHLFLYMREHELLK | Binds to the 23S rRNA. Part of the 50S ribosomal subunit. Belongs to the eukaryotic ribosomal protein eL19 family. |
P0DMV3 | MDTILLTGLFAAFFTTFAFAPQSIKTIRTRNTEGISVVMYIMFLTGVISWIAYGIMRSDFAVLIANIVTLFLAAPVLVITLINRRKKHV | The homodimer mediates transmembrane sugar transport down a concentration gradient. Transport is probably effected by rocking-type movements, where a cargo-binding cavity opens first on one and then on the other side of the membrane. Homodimer. |
P61791 | DDCGTLFSGCDTSKDCCEGYVCHLWCKYK | Inhibitor of voltage-gated potassium channels of the Kv4/KCND family (By similarity). Blocks calcium channels (Cav). Expressed by the venom gland. The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin. Belongs to the neurotoxin 10 (Hwtx-1) family. 19 (HpTX2) subfamily. |
Q8K9G6 | MINLIPMTVRGAEKLREELEQLKNVKRPRITVQIAEARKHGDLKENAEYHSAREEQSFCEGRIQEIESKLSNSQIIDITKISNDGRVVFGSTVTILNIKNNAVFTYQIVGDDESDFKKNLISINSPMSRGLIGKTVNTIAIIHTPSGNVKYKILKIDYI | Necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by cleavage factors such as GreA or GreB allows the resumption of elongation from the new 3'terminus. GreA releases sequences of 2 to 3 nucleotides. Belongs to the GreA/GreB family. |
P85447 | FLSLIPHAINAVSALAKHF | Has antimicrobial activity. Expressed by the skin glands. Belongs to the frog skin active peptide (FSAP) family. Phylloseptin subfamily. |
P48205 | MGKIIGIDLGTTNSCLAIMDGKTAKVIENAEGHRTTPSVVAYTDSGEILVGQAAKRQAVTNPDNTFFAIKRLIGRKYDDKAVQEDIKKKVPYAVIKADNGDAWVATKEGKKMAPPQVSAEVLRKMKKTAEDYLGEPVTEAVITVPAYFNDSQRQATKDAGKIAGLEVKRIINEPTAAALAYGVDSKKGEQTVAVYDLGGGTFDISIIEISDVDGDNQIEVLSTNGDTFLGGEDFDLALMNYLIDEFKKEQGIDLHNDKLALQRVREAAEKAKVELSPAQQTDVNLPYITADATGPKHLNIKVTRAKFESLVSDLVMRSLEPCKKALEDAGLSKSDITEVLLVGGQTRMPLVQEKVKEFFGKEPRKDVNPDEAVAVGAAIQGGVLAGDVKDVLLLDVTPLSLGIETMGGVMTKLIERNTTIPTKKSQVFSTAEDNQPAVTIHVLQGEREMASANKSLGRFDLADIPPAPRGMPQIEVTFDIDANGILNVSAKDKATGKEQNIVIKSSSGLSEEDIEKMVQDAEANAEADKKFHDLVTARNTADNLIHSSRKAIQELGDKVTAAEKEKIEEACKELEAATKGDDKQAIEAKTKALEEAFAPIAQKAYAEQAQAAGAQGGAKAEEPKKEEDVVDADFEDVEDDKK | Acts as a chaperone. By stress conditions e.g. heat shock (By similarity). Belongs to the heat shock protein 70 family. |
Q2JFF1 | MARLSGVDLPREKRVEIALTYIFGIGRSRSRDTLAATAVNPDTRVRDLSEEEIVRLRDWIDANYRVEGDLNREIKQDIRRKMEIGCYQGLRHRRNLPVHGQRTHTNARTRKGPRRAIAGKKKAGKK | Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites. Part of the 30S ribosomal subunit. Forms a loose heterodimer with protein S19. Forms two bridges to the 50S subunit in the 70S ribosome. Belongs to the universal ribosomal protein uS13 family. |
C9XVF1 | MDYTIEHVLTRKIAGFHLVGPWEKTVPQGFEQLTLWVDNFHIQPQAWLAVYYDNPQQVAPEKLRADTVVEVPADFTLPENSVGVILTDLPGGQYAVARARVENHDFGTPWLAFFTRLHQDVRYQMAARPCFEIYLNDGKRDGYWEIDMYIPVQTSGE | Inhibits the supercoiling activity of DNA gyrase. Acts by inhibiting DNA gyrase at an early step, prior to (or at the step of) binding of DNA by the gyrase. It protects cells against toxins that target DNA gyrase, by inhibiting activity of these toxins and reducing the formation of lethal double-strand breaks in the cell. Interacts with DNA gyrase. Belongs to the DNA gyrase inhibitor family. |
B8EAH3 | MPATMSQAFIGNFLGNSPKWYKTAILSFLIINPLLFFYVDPFVAGWVLVLEFIFTLAMALKCYPLQPGGLLAIEAVAIGMTSASQVLHEIEANLEVLLLLVFMVAGIYFMKQLLLFGFTKIITKVRSKVLVSLMFCLASAFLSAFLDALTVIAVIIAVAVGFYSIYHKVASGKDFGADHDHTSEGKNAAGEDQLNEEELGAFRGFLRNLLMHAGVGTALGGVCTMVGEPQNLIIAAQANWQFGEFAVRMSPVTVPVLISGILTCYLVEKFGIFGYGAKLPTAVHRILCEYAAHEDARRTNKDNMKLIVQALVGVWLIAGLALHLASVGLIGLSVIILTTAFNGVTDEHALGKAFEEALPFTALLAVFFAVVGVIIDQHLFAPVIQWALGYEGNTQLVIFYIANGLLSMVSDNVFVGTVYINEVKAALINGQITRDQFDLLAVAINTGTNLPSVATPNGQAAFLFLLTSALAPLIRLSYGRMVWMALPYTIVLSIVGVMAIQTGFLEQATQYFYDSHTIIHHSAKEVLGTVSGH | Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons. 3 H(+)(out) + 2 Na(+)(in) = 3 H(+)(in) + 2 Na(+)(out) Belongs to the NhaB Na(+)/H(+) (TC 2.A.34) antiporter family. |
Q28LW5 | MAGHSKWANIQHRKGRQDKLRAKVFSKMSKEITVAAKMGDPDPDKNPRLRLAVKEAKSVSVPKDVIERAIAKATGGDSENYDEIRYEGYGPNGVAVIVETMTDNKNRTASTVRSTFTKNGGNLGETGSVGFMFDRKGQVTYPLSAGDADTIMMAAIEAGAEDVETNEGDGDEDLGGHVIWCADTDLNDVSNALEADLGESESTKLVWRPTTTTELGLEDAQKLMRLIDALEEDDDVQTVTANFEISDEVMAQLSE | Belongs to the TACO1 family. |
B8D7A0 | MHIIKTIKVLYREIKILKKSNKKIGLVPTMGNLHDGHIKLILLAKKYSDIIIVSIFINPMQFDNLSDLKNYPKTFMKDSIILKKYHVDILFFPHINEIYPNGIEHQTFVEVIKLSKILEGQSRPGHFRGVTTIITKLFNFIQPDFAFFGEKDYQQLLIIKILVKELNYMIKIISLPTIRLKNGLALSSRNNYLSSQENEIAPYLYKIIKKTCEKIIKEDDNIRPKIIHESKILLIKKGFSVDIFDIYDYKNLEHPSKKVKKVILLASVWLGNTRLIDNKKIILNY | Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+) Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. Homodimer. The reaction proceeds by a bi uni uni bi ping pong mechanism. Belongs to the pantothenate synthetase family. |
A0JM59 | MGDAEDFCPHLDSIGEVTKEDLILKSKGTCESCGVGGPNLWACLQDGCQSVGCGESYVDHSTLHAQAKKHNLTVNLTTFRVWCYACEKEVFLDPRGPPASQTTSPRLSHRDFPTSAHPLKSVPIAVGDDGESESDEDDIKPRGLTGMKNIGNSCYMNAALQALSNCPPLTQFFLECGGLVRTDKKPALCKSYQKLISELWHKKRPSYVVPSSLYHGIKLINPLFRGYSQQDTQEFLRCLMDQLHEELKEPVPLETQEREEEDRDDQREGERGGTVEEDFLSCDSGGEMGDGEGGGGVGTLSEMELLIREEVGRGLSEKEKLKERKLSYCHRRTSSEQADEDADVDTAMIPEPDNDAYVHCSSRSCSPHPVESISKHSSTPPRSSPLRTSHSYVLKKAQVLSGGKKRSEVRYRSVISDIFDGSILSLVQCLTCDRVSTTIETFQDLSLPIPGKEDLAKLHSTIHQSAVSKAGTCGDSYAAQGWLSFFMDYIRRFVVSCIPSWFWGPMITLEDCLAAFFAADELKGDNMYSCERCKKLRNGVKYCKVLRLPEILCIHLKRFRHEVMYSFKIGSHVSFPLEGLNLRPFLAKECVSRITTYDLLAVICHHGSASSGHYISYCQNVINGQWYEFDDQYVTEVHETVVQNAEAYVLFYRKSSEEAERERQKVVSLAAMKESGLLQFYISREWLNKFNTFAEPGPISNQSFLCSHGGIPPNKYHYIDDLVVILPQSVWEYLYNRFGGGPAVNHLYVCSICQVEIEALAKRRKTEIDTFIKLNKAFQAEEAPSVIYCISMQWFREWEAFVKAKDSDPPGPIDNSKVALTKSSGQVQLKQGADYGQISEETWNYLLNVYGGGPEIAIRQTVAQYQEAEHLHGEQKIEAETRAG | Deubiquitinating enzyme involved in beta-2 adrenergic receptor (adrb2) recycling. Acts as a regulator of G-protein coupled receptor (GPCR) signaling by mediating the deubiquitination beta-2 adrenergic receptor (adrb2). Plays a central role in adrb2 recycling and resensitization after prolonged agonist stimulation by constitutively binding adrb2, mediating deubiquitination of adrb2 and inhibiting lysosomal trafficking of adrb2. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By similarity). Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal). The UBP-type zinc finger binds 3 zinc ions. However, it does not bind ubiquitin, probably because the conserved Arg in position 55 is replaced by a Glu residue (By similarity). Belongs to the peptidase C19 family. USP20/USP33 subfamily. |
Q2VYH4 | MSGKARLAGVLGWPVSHSRSPRLHGFWLEQMGIDGAYLPLAVAPEHLETVIRALPRMGFAGANVTVPHKEAVMRLVDHLDPLARRIGAVNTLVVRQDGTLEGRNTDAYGFFENLRQGCPLWEPTSGPAAVIGAGGAARAVVAALADAGVPEIRLANRSRERAATLAADLGGPVTVVDWAERAESLEGCALLVNTTTLGMTGQSSLDLDLAALPTTSVVNDIVYVPLVTDLLARATARGNPIVDGLGMLLHQAVPGFEAWFGQRPQVSDQLRAFVLS | Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA). NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. Homodimer. Belongs to the shikimate dehydrogenase family. |
Q12HP9 | MQLNSTEISDLIKQRIEQFEVVSEARNEGTIVAVSDGIIRINGLADVMQGEMIELPGNRYAIALNLERDSVGAVVMGSYAGLAEGVKVKTTGRILEVPVGRGLLGRVLNTLGEPIDGKGPVDNDGYSPIEVIAPGVIERQSVDEPVQTGYKTVDSMIPIGRGQRELVIGDRQTGKTALAIDAIINQKESGIKCVYVAIGQKASTIANVVRKLEEHGALANTIVVVATASEAAALQYLAPYSGCSMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLKRPPGREAYPGDVFYLHSRLLERASRVNANYVEKFTKGAVTGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLETDLFNSGLRPAVNPGISVSRVGGAAQTKIIKKLSGGIRTALAQYRELAAFSQFASDLDDATRAQLEHGERVTELMKQKQYAPMSVAAQAVVIYAAEKGYLKSVALNKVGHFEAALLSFMNSEYAALMTNINATGDYNADIEGEIKAALDKFVATQTW | Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF(1) is attached to CF(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase alpha/beta chains family. |
A9BNI6 | MTTLGTPYSPHATKVMLLGSGELGKEVLIALQRLGVETIAVDRYENAPGQQVAHHARTITMSDPAQLKALIEAEKPDLVVPEIEAIATPMLEELEAAGVVTVIPTARAARLTMDREGIRRLAAETLGLATSPYRFCDSQQELQAAIDGTDGQPAIGFPCVVKPVMSSSGKGQSKLDGPDDVAKAWDYAMAGGRVSHGRVIVEGFIDFDYEITQLTVRAKGADGQVQTHFCDPIGHIQQSGDYVESWQPHPMHPAALQKSRDIAKAVTDDLGGLGLFGVELFVKGEQVWFSEVSPRPHDTGLVTLATQWQSEFELHARAILGLPVDASLRNPGASAVIYGGQDAEGLVFDGVDEALAVPGTDLRLFGKPESFVKRRMGVALARAQDVEQARTNAKLAAGKVKPRKP | Involved in the de novo purine biosynthesis. Catalyzes the transfer of formate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR). Formate is provided by PurU via hydrolysis of 10-formyl-tetrahydrofolate. ATP + formate + N(1)-(5-phospho-beta-D-ribosyl)glycinamide = ADP + H(+) + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate Purine metabolism; IMP biosynthesis via de novo pathway; N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (formate route): step 1/1. Homodimer. Belongs to the PurK/PurT family. |
A9MTL3 | MAVTKLVLVRHGESQWNKENRFTGWYDVDLSEKGVSEAKAAGKLLKEEGFSFDFAYTSVLKRAIHTLWNVLDELDQAWLPVEKSWKLNERHYGALQGLNKAETAEKYGDEQVKQWRRGFAVTPPELTKDDERYPGHDPRYAKLSEKELPLTESLALTIDRVIPYWNDTILPRMKSGERVIIAAHGNSLRALVKYLDNMSEDEILELNIPTGVPLVYEFDENFKPLKHYYLGNADEIAAKAAAVANQGKAK | Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. Homodimer. Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily. |
Q4A872 | MNKKYAKKFKKKPCQFCEAKLFYIDYKDIEVLQRFINTFGKIQPSRITGNCAKHQRKLALAVKRARFVALLPFIGDRIRGNYDKTRV | 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. Part of the 30S ribosomal subunit. Forms a tight heterodimer with protein S6. Belongs to the bacterial ribosomal protein bS18 family. |
Q9CLE1 | MLVGIISLFPEMFKAITEFGVTGRAVKQNLLQVRCWNPRDFTHDKHKTVDDRPYGGGPGMLMMVQPLRDAIQAAKAEVGEGAKVIYLSPQGRKLDQAGVKELAQHQKLILLCGRYEGIDERLIETEVDEEWSVGDYVLTGGELPAMTLIDAVARFIPGVLGKQASADEDSFAEGLLDCPHYTRPEVLDGLAVPPVLMSGNHEEIRKWRLRQSLERTWLRRPELLESLALTDEQRKLLKQIKAEHS | Specifically methylates guanosine-37 in various tRNAs. guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine Homodimer. Belongs to the RNA methyltransferase TrmD family. |
Q5LTN6 | MAQNPLSKPTACLVLADGTVFYGTGFGATGQTVAELCFNTAMTGYQEIMTDPSYAGQIVTFTFPHIGNVGVTPEDDETTDPVAAGMVVKWDPTAASNWRAAEELKGWLARRGRIAIGGVDTRRLTRAIRQQGAPHVALAHDPEGKFDLAALIAAARGFAGLEGMDLAKDVTCAQSYRWDEMRWAWPEGYARQEAPKHKVVAIDYGAKRNILRCLASSGCDVTVLPATATAAEVLAHAPDGVFLSNGPGDPAATGEYAVPMIREILDTTSLPVFGICLGHQMLALALGGRTVKMNHGHHGANHPVKDLETGKVEITSMNHGFAVDAQSLPEGVVETHRSLFDGSNCGIRMSERPVFSVQYHPEASPGPQDSFYLFERFAAAMDAQKAEV | 2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1. Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3. Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate. Belongs to the CarA family. |
P19071 | MLLNKDRFGKLTSKSLDSIAALGLREANAELPCLFRNNSIESSSKTPPEPLSPLAFELSTNLKKSASALAWNVQYFVDTYGLSNVGFLTLTFRDHVTDPKEAQRRFNSLKTNILAKRYRAYIRVMEPMKSGRIHYHLLVALHSDIRTGFDFPAVYRQDYSSANKAIRSEWSFWRKTAPKYGFGRTELMPVRSNSEGIGRYVGKYISKGIESRTEQFKGVRLVEYSRKAKSLLRASSSFLTGLMSGVANFRYSFITSRTIWAVNQLLTAYAVFSALVGRITGVILL | Essential for autonomous replication of the phasyl DNA replicon. |
Q46IE5 | MAASQNPIQGSLFGGNEESDLNKAEKLKGSERSNVNLSHQQLKEDASLRPRIKQTPKNPNQIIDLDELSRLAIEEPKWSHHNLPKIDDLTPALRHYVELKKENPDRVLLYRLGDFFECFFEDAITLSKLLEITLTSKEAGKKIGKIPMAGIPHHASDRYCTELIKKGLSIAICDQLEAAPTKGNKLIKRGITRLITPGTILEEGMLSAKKNNWLASVLLEAKSNQEIIDWSLAKIDVSTGEFIVQEGQGSNNLRHELIKLNAAEVISEKKSISNKIWYEGLIEITEFNRTSFSNLEAITTIKNHYCLNNIDSLGIHSNSLSIRTIGGLISYLNKTHPNIDDKSNNEIKTNICIDYPRIKNSRSGLIIDSQTRRNLEITSTQKDGKFQGSLLWAIDKTLTAMGARCIRRWIEEPTKDVNAIKNRQNIIGFLVKSSTLRKNIRKTLRAMGDLERLSGRAGAQQAGARDLVAIAEGINRLPLIKNYLNEPIFDKTKYFDSIINIDKDLIELASKINNQIIDNPPLSLTEGGLFYDGINPVLDGLRNQLDDHNIWLNSQELEERKKSNINNLKLQYHRSFGYFLAVSKSKAINVPDHWIRRQTLTNEERFVTPGLKEREGKIFQVRARISELEYELFCDLRKLTGSKSNIIRQAAKAISHLDVLTGLAELAANHNYIQPQIIDMNEQDKSRKLSIIDGRHPVVEQILVDKVFVPNDIELGSKTDLIILSGPNASGKSCYLRQVGLLQIMAQIGSWIPAKSAHMGIADQVFTRVGAVDDLASGQSTFMVEMIETAFILNNATENSLVLLDEIGRGTSTFDGLSIAWSVSEFLAKKIKSRSIFATHYHELNQISEYIENVENYKVVVEYKNHSLSFLHKVERGGANKSYGIEAARLAGVPPDVVNNARLILKNLEKNNSNTIQITKPIESCK | This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity. Belongs to the DNA mismatch repair MutS family. |
Q08A38 | MDQLAHLYHAHMAELNRRVGEICQRENLSGLVIHSGQPHRQFLDDLNYPFKVNPQFKAWLPILDTPNCWVIANGQDKPTLVFYRPVDFWHKVNDVPQAFWTEHFDIQLLTKPDRIADFLPKDLASWAYIGEHLDVADVLGFAARNPDAVMNYLHYHRADKTQYELECMRRANQIAVKGHLAAKNAFYDGASEFEIQQRYLLEIGQGENEVPYGNIVALNQNAAILHYTALEHVKPAQRLSFLIDAGASYHGYAADITRTYSFEKNRFYELIVALDKVQLAIIEQMKPGVKYVDLHIATHHYIGQLLIDFGLANGTAEQLVAQGVTSAFFPHGLGHMLGLQVHDMGGYSHDERGTHIAAPEAHPFLRCTRVLAANQVLTIEPGLYIIDTLLNQLSATAKQAINWTTVDEMRPFGGIRIEDNVIVHQDRVENMTREFGLVD | Splits dipeptides with a prolyl residue in the C-terminal position. Hydrolysis of Xaa-|-Pro dipeptides. Also acts on aminoacyl-hydroxyproline analogs. No action on Pro-|-Pro. Binds 2 manganese ions per subunit. Belongs to the peptidase M24B family. Bacterial-type prolidase subfamily. |
C3LWU0 | MELTMKKVSVIAAAVAATLAAGSAFAVDFNGYFRAGTGISGNGNADQAVNKAGTGRLGNENDNYYEFGFAEELKTGEQTWKVESMIAQGNSGANGWEDGDFNVAQFNVQAKGLLASDQEAVMWAGKRYYQRKDIHITDFYFLNTSGTGGGIENLSVGNQKLSVALVQDGDNTNSSGYIFDARLANIGLWENASLELAMAYNFATEKDSKNEVADDGVLVSAILHQGLSNGFNQTVFQYGTAGYGAQAANFWGAGSYYARGTEAFNDASGFRLLNWGVINLGENWEMGHQLAYLAGSDIGGQFGGDGANKNTYTGKSFDIDQYSVVVRPMYKWNDTMRTVFEAGYNAGEKISNGGLATEDFGNAKFTVAQAWAMGDSFWARPELRVYGTYLLDTENDKAFGDDDTEFVVGIQVEAWW | Involved in the transport of maltose and maltodextrins. Homotrimer formed of three 18-stranded antiparallel beta-barrels, containing three independent channels. By maltose. Belongs to the porin LamB (TC 1.B.3) family. |
C0PXG7 | MLKTISPLISPTLLKVLAEMGHGDEIIFSDAHFPAHSLGPQVIRADGLSVSDLLRAIIPLFELDSYAPPLVMMAAVEGDTLDPSVEARYRDALSLEAPCPDIVRIDRYAFYERAQKAFAIVITGECAKYGNILLKKGVTP | Involved in the anomeric conversion of L-fucose. alpha-L-fucose = beta-L-fucose Carbohydrate metabolism; L-fucose metabolism. Homodecamer. Belongs to the RbsD / FucU family. FucU mutarotase subfamily. |
A3DGC7 | MTGLDRKKDDEIIEVLRMMAPGTSLREGLDNILLARTGALIVIGDSEKVLSLVDGGFYINKDYTPAHIYELAKMDGAIILSKDLKKILYANALLVPDTSIPTAETGTRHKTADRVAKQTGEVVVSISQRRNIITIYMGSRKYILRETPVILAEANQALQTLEKYKVALVEAINNLNILEIEDIVTLDDVAFVLQRTEMLMRVAAEIERYISELGSEGRLISLQLDELLTNVDADELFIIEDYAIRTDLRSDEILEKLRQLSYDELMNLVNICSILGYSPNADAFEMVISPRGYRLLSKIPRVPVNIIRNLVKKFSNLQGILNASIEELDDVAGIGEVRARIIWDGLRRVQEQIFLDSRKL | Participates in a DNA-damage check-point that is active prior to asymmetric division when DNA is damaged. DisA forms globular foci that rapidly scan along the chromosomes during sporulation, searching for lesions. When a lesion is present, DisA pauses at the lesion site. This triggers a cellular response that culminates in a temporary block in sporulation initiation. Has also diadenylate cyclase activity, catalyzing the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP). c-di-AMP acts as a signaling molecule that couples DNA integrity with progression of sporulation. The rise in c-di-AMP level generated by DisA while scanning the chromosome, operates as a positive signal that advances sporulation; upon encountering a lesion, the DisA focus arrests at the damaged site and halts c-di-AMP synthesis. 2 ATP = 3',3'-c-di-AMP + 2 diphosphate Homooctamer. Belongs to the DisA family. |
P37238 | MGETLGDSPVDPEHGAFADALPMSTSQEITMVDTEMPFWPTNFGISSVDLSVMEDHSHSFDIKPFTTVDFSSISAPHYEDIPFTRADPMVADYKYDLKLQEYQSAIKVEPASPPYYSEKTQLYNRPHEEPSNSLMAIECRVCGDKASGFHYGVHACEGCKGFFRRTIRLKLIYDRCDLNCRIHKKSRNKCQYCRFQKCLAVGMSHNAIRFGRMPQAEKEKLLAEISSDIDQLNPESADLRALAKHLYDSYIKSFPLTKAKARAILTGKTTDKSPFVIYDMNSLMMGEDKIKFKHITPLQEQSKEVAIRIFQGCQFRSVEAVQEITEYAKNIPGFINLDLNDQVTLLKYGVHEIIYTMLASLMNKDGVLISEGQGFMTREFLKNLRKPFGDFMEPKFEFAVKFNALELDDSDLAIFIAVIILSGDRPGLLNVKPIEDIQDNLLQALELQLKLNHPESSQLFAKVLQKMTDLRQIVTEHVQLLHVIKKTETDMSLHPLLQEIYKDLY | Nuclear receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. Once activated by a ligand, the nuclear receptor binds to DNA specific PPAR response elements (PPRE) and modulates the transcription of its target genes, such as acyl-CoA oxidase. It therefore controls the peroxisomal beta-oxidation pathway of fatty acids. Key regulator of adipocyte differentiation and glucose homeostasis. ARF6 acts as a key regulator of the tissue-specific adipocyte P2 (aP2) enhancer. Acts as a critical regulator of gut homeostasis by suppressing NF-kappa-B-mediated pro-inflammatory responses. Plays a role in the regulation of cardiovascular circadian rhythms by regulating the transcription of ARNTL/BMAL1 in the blood vessels (PubMed:19041764). PDPK1 activates its transcriptional activity independently of its kinase activity. Heterodimer with other nuclear receptors, such as RXRA. The heterodimer with the retinoic acid receptor RXRA is called adipocyte-specific transcription factor ARF6. Interacts with NCOA6 coactivator, leading to a strong increase in transcription of target genes. Interacts with coactivator PPARBP, leading to a mild increase in transcription of target genes. Interacts with NOCA7 in a ligand-inducible manner. Interacts with NCOA1 and NCOA2 LXXLL motifs. Interacts with ASXL1, ASXL2, DNTTIP2, FAM120B, MAP2K1/MEK1, NR0B2, PDPK1, PRDM16, PRMT2 and TGFB1I1. Interacts (when activated by agonist) with PPP5C. Interacts with HELZ2 and THRAP3; the interaction stimulates the transcriptional activity of PPARG. Interacts with PER2, the interaction is ligand dependent and blocks PPARG recruitment to target promoters. Interacts with NOCT. Interacts with FOXO1 (acetylated form). Interacts with ACTN4 (By similarity). Interacts (when in the liganded conformation) with GPS2 (PubMed:25519902). Interacts with CRY1 and CRY2 in a ligand-dependent manner (PubMed:28683290). In the absence of hormonal ligand, interacts with TACC1 (PubMed:20078863). Redistributed from the nucleus to the cytosol through a MAP2K1/MEK1-dependent manner (By similarity). NOCT enhances its nuclear translocation. Highest expression in white and brown adipose tissue. Also found in liver, skeletal muscle, heart, adrenal gland, spleen, kidney and intestine. Isoform 2 is more abundant than isoform 1 in adipose tissue. It appears first at 13.5 dpc and increases until birth. Expressed in a circadian manner in the aorta. The 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors. O-GlcNAcylation at Thr-84 reduces transcriptional activity in adipocytes. Phosphorylated in basal conditions and dephosphorylated when treated with the ligand. May be dephosphorylated by PPP5C. The phosphorylated Ser-112 form is recognized by PER2 and repressed, dephosphorylation at Ser-112 induces adipogenic activity. Ser-112 phosphorylation levels are reduced by 65% in brown adipose tissue compared to white adipose tissue. Mice develop abnormalities in circadian variations in blood pressure and heart rate, in parallel with a reduction of diurnal variations in the sympathetic nerve activity, and impaired rhythmicity of ARNTL/BMAL1 in the blood vessels. Belongs to the nuclear hormone receptor family. NR1 subfamily. |
A7HLB7 | MAKKVVAQVRLVLEAGKATPAPPVGPALGQRGVNLMEFCKKFNAVTADKAGLLIPVIVTVYDDRSFTFITKTPPASFLLKRAAKINSGSSEPKRKVAGKVTRQQIKEIAELKMQDLNANDLEAAMKIIEGTARSMGLEVVD | Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Part of the ribosomal stalk of the 50S ribosomal subunit. Interacts with L10 and the large rRNA to form the base of the stalk. L10 forms an elongated spine to which L12 dimers bind in a sequential fashion forming a multimeric L10(L12)X complex. One or more lysine residues are methylated. Belongs to the universal ribosomal protein uL11 family. |
B8ZPP6 | MKLQKPKGTQDILPAESAKWQYVEGFAREIFKRYNYAEVRTPIFEHYEVISRSVGDTTDIVTKEMYDFYDKGDRHITLRPEGTAPVVRSYVENKLFAPEVQKPSKFYYMGPMFRYERPQAGRLRQFHQIGVECFGSSNPATDVETIAMAAHFLKEIGIQGVKLHLNTLGNPESRAAYRQALIDYLTPLKETLSKDSQRRLEENPLRVLDSKEKEDKVAVENAPSILDFLDEESQTHFDAVRQMLENLGVDYIIDTNMVRGLDYYNHTIFEFITEIEGNDLTVCAGGRYDGLVAYFGGPETAGFGFGLGVERLLLILEKQGVALPIENALDVYIAVLGDGANVKALELVQALRQQGFKAERDYLNRKLKAQFKSADVFAAKTLITLGESEVESGQVTVKNNQTREEVQVSLETISQNFSEIFEKLGFYTQ | ATP + L-histidine + tRNA(His) = AMP + diphosphate + H(+) + L-histidyl-tRNA(His) Homodimer. Belongs to the class-II aminoacyl-tRNA synthetase family. |
O69268 | MSKIIGIDLGTTNSCVSVLEGGEPKVIPNPEGNRTTPSVVAFKNGERQVGEVAKRQSVTNPNTIISIKSKMGTAEKVTVEDKDYTPQEVSAMILQYLKGYAEDYLGEKVTKAVITVPAYFNDAQRQATKDAGKIAGLEVERIINEPTAAALRYGLDKQDQDQKVLVFDLGGGTFDVSILELGDGVFEVLATAGDNKLGGDDFDDAIIEYLVAEFKKENGIDLSKDKMAMQRLKDAAEKAKKDLSGVTSTQISLPFITAGEAGPLHLEISLTRAKFDEITLPLVNRTVGPVRQALSDAGLSTSEIDQVILVGGSTRIPAVQEAVRKETNKEPHRGVNPDEVVAMGAAVQGGVLTGDVKDVVLLDVTPLSLGIETMGGVFTKLIDRNTTIPTSKSQVFSTAADNQPAVDIHVLQGERSMAADNKTLGRFQLADIPPAPRGVPQIEVTFDIDKNGIVSVKAKDLGTNKEQTIVIQSDSGLSEAEIERMVKDAEANRDADAKRKEEADLRNEADQLVFQVDKTITDLGEQITEDEKKSVEDARDELKKALEAGELEGIKAAKEKLEGVLQPLVMKVYEQAAAAAQARQGGEADAGAGKKDDGVVDADFEEVKDDK | Acts as a chaperone. By stress conditions e.g. heat shock (By similarity). Belongs to the heat shock protein 70 family. |
Q6GH25 | MFIIKSILYRLIQMIVVLFVISTLAFILMKLSPGNPVDKILHLDVAQVSTEQINATKDKLGLNDSLLVQWWHWMNHLLHFNLGKSFESKEPVTQILFNYAPITLLISFSTLVVSLCISIPLGIIAAKRFHKLSDKVIRVISTLSISLPAFFIGIILLFIVTNLMNIDSVILSQFILPVLTLSLGMCAYIIRLVRSNLLILLKSNIVQASRLRGMNERYILIHDLLKPTILPIIPLLGISLGSLIGGTVVIENLFDIPGIGYLLMDSIKSRDYPVIQGCVLFIGFFVVIINTIADLLTLLLDPKQRLQLGNPKNKTNTPLISESSDRHA | Part of the ABC transporter complex NikABCDE (Opp2) involved in nickel import. Probably responsible for the translocation of the substrate across the membrane. The complex is composed of two ATP-binding proteins (NikD and NikE), two transmembrane proteins (NikB and NikC) and a solute-binding protein (NikA). Belongs to the binding-protein-dependent transport system permease family. OppBC subfamily. |
Q5GTJ4 | MFIILAAGHGKRMNSGLPKVLHKIGNFSMLQHIIYNARQLNPENISVVANLPLIERLKCLEDIQLITQESTLGTGDAVKTAVRNMKELSDSNIIVVQYGDTPLIKNSTITQMVSCLEGKALVCLGFKTSNKEYGRLIIENGSLREIVETQDDENSDEEFLANAGIMVAYAKNLRELVEKIECNGSTYEYYLTDIVSIAVKSNLNVGYVTTDEEEATGINSRNDLAKAEFYFQENRRKFFTDSGVTLVAPETVFFSLDTQIGMDSIIYPYVFFGPGVRIGPGAKIGPFTKCEDTTIGDGAIVGNFVEAKASDIGTNTKIKHLSYIGNTEVGRESNIGAGTVVCNYDGKKKHRTNIGSNCFVGANSSLIAPLNVHDESVIAAGSIIVKDVPKKRLVITRRKQMVKKIK | Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain. acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = diphosphate + UDP-N-acetyl-alpha-D-glucosamine Binds 1 Mg(2+) ion per subunit. Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2. Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1. Bacterial outer membrane biogenesis; LPS lipid A biosynthesis. Homotrimer. In the N-terminal section; belongs to the N-acetylglucosamine-1-phosphate uridyltransferase family. In the C-terminal section; belongs to the transferase hexapeptide repeat family. |
Q3UW15 | MSSLYYANALFSKYPAASSVFAPGAFPEQTSCAFASNPQRPGYGAGPGAPFSASVQGLYSGGGAMAGQSAAGVYAAGYGLEPSSFNMHCAPFEQNLSGVCPGDPAKAAGAKEQRDSDLAAESNFRIYPWMRSSGPDRKRGRQTYTRYQTLELEKEFHYNRYLTRRRRIEIAHTLCLTERQIKIWFQNRRMKWKKENKTSGPGTTGQDKAEAEEEEEE | Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Forms a DNA-binding heterodimer with transcription factor PBX1. Belongs to the Antp homeobox family. |
B7L8T9 | MNNAPHLYFAWQQLVEKSQLMLRLATEEQWDELITSEMAYVNAVQEIAHLTEEVAPSTTMQEQLRPMLRLILDNESKVKQLLQIRMDELAKLVGQSSVQKSVLSAYGDQGGFVLAPQDNLF | Dual-function protein that regulates the transcription of class 2 flagellar operons and that also acts as an export chaperone for the filament-capping protein FliD. As a transcriptional regulator, acts as an anti-FlhDC factor; it directly binds FlhC, thus inhibiting the binding of the FlhC/FlhD complex to class 2 promoters, resulting in decreased expression of class 2 flagellar operons. As a chaperone, effects FliD transition to the membrane by preventing its premature polymerization, and by directing it to the export apparatus. Homodimer. Interacts with FliD and FlhC. Belongs to the FliT family. |
Q0I5W9 | MNLNATLIGQLIAFAIFVWFCMKYVWPPIIKAIEERQRSIANALASAEAAKKEQSDTKVLVEQEINQARIKAQEIVDLANKRRNEILEEVKIEAEALREKIIEQGHAEIESERKRVQEELRIKVASLAIAGAEKIVGRNIDEAANNDIIDKLVADL | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
Q44457 | MIMAKAAAQKASAPTIDTALLAKLTGGLTDRKTIAKIGADIGHLYSEFLPDTFHSETGIAIDVEYIGSESGLMTDLIANVGQNVAVADCSLRNWCPNFMMAVGNGFVIALMERMLGASPDSIGDPDERNLSHIELDLAAMVLGRIAGVLRSGVNAPGGFEATIDPPFNANGKSAFDEMIAGLYGVTIRMKIDIGKVSSEFSLIVPQRPLLKTSIVAPKASAQALKKQEEWMDMISQQVKRSQVTLEARIKLETLTLRTISRLVAGDVIPFQDLKQDDIGVEVSANGSKLYNCEFGKSGDRYMVRVKNNVSTDDEILRHLMG | FliM is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation (By similarity). Belongs to the FliM family. Truncated N-terminus. |
B7L8T2 | MPLHNLTRFPRLEFIGAPTPLEYLPRFSDYLGREIFIKRDDVTPMAMGGNKLRKLEFLAADALREGADTLITAGAIQSNHVRQTAAVAAKLGLHCVALLENPIGTTAENYLTNGNRLLLDLFNTQIEMCDALTDPNAQLEELATRVEAQGFRPYVIPVGGSNALGALGYVESALEIAQQCEGAVNISSVVVASGSAGTHAGLAVGLEHLMPESELIGVTVSRSVADQLPKVVNLQQAIAKELELTASAEILLWDDYFAPGYGVPNDEGMEAVKLLARLEGILLDPVYTGKAMAGLIDGISQKRFKDEGPILFIHTGGAPALFAYHPHV | Catalyzes the alpha,beta-elimination reaction of D-cysteine and of several D-cysteine derivatives. It could be a defense mechanism against D-cysteine. D-cysteine + H2O = H(+) + hydrogen sulfide + NH4(+) + pyruvate Homodimer. Belongs to the ACC deaminase/D-cysteine desulfhydrase family. |
A9RAH2 | MIYSPTEQFEIKPLLTVNNMLTLSVNNYVMYVALVVTLMYSSVFLLNRTYLGFNRWGVALLAVYDTILNMVKSQMGARGGMYFPFMFTLFTFMLVANLVSMMPYSFAMSAQLVAIVSFSLSLWFGCVLMGLSKHGWGFFALFVPGGTPLALVPVLVLIETLSYSSRAISLGLRLSANVLSGHLLMLILGTLMFNLMGSSMLGFMGGFMPVMGVIAIVVTEFAIGMMQAYVFTILLSSYIKDSVYLH | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane (By similarity). F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c (By similarity). Belongs to the ATPase A chain family. |
S6CQU2 | MKLTCVVIVAVLLLTACQLITADDSRGTQKHRSLRSTTKVSKSTSCMKAGSYCRSTTRTCCGYCAYFGKFCIDFPSN | Omega-conotoxins act at presynaptic membranes, they bind and block voltage-gated calcium channels (Cav). Expressed by the venom duct. The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin. The cysteine framework is VI/VII (C-C-CC-C-C). Found in injectable (milked) (IV) venom. Belongs to the conotoxin O1 superfamily. |
A3D738 | MKPQWQQYINIIKQVVKPALGCTEPIAAAYAAAVARALLGVEPDSIAVQVSDNLYKNSMGVFVPGTGKIGLAIAAAAGAIAGNPDAGLEVLAVITPEQVAKAQALIDAGKVTVERTETAEFIYCCVIAKKGDREALVKICGGHTLIAEKRLNGESVFSVDSTQAKATGSICEGVDITIESIYRFAQEVPFEEIKFILEASELNGKLSDEGMANPYGLEVGRTMKSGIAAGIIGEDLLNKIVMLTAAASDARMGGANLPAMSNLGSGNQGIAATIPVVLTAQCYKVSEEQLARALIMSHLGAIYIKSHYPPLSAFCGNTVTSAAASMAMVYLAGGSFEQSCFAIQNVISDSSGMVCDGAKASCAMKVSTSSSAAVRSFLMALSSHNVSGQGIIATDVEKTIKNIGKMILNGMSSTDVTIIDIMSA | Belongs to the UPF0597 family. |
Q3IPJ2 | MKHLPKHLRPRWRYLAVGLESWPDADIDRRAFQRELWFAAQNLIGDAGSAALDGSVLHFRFEDGDGEAVIRARRGEVDALRAVLATLSTVDGHPLGVVVRGVSGTVRACEEKYIRGPQEGTEERTVAFAGADRPAVVRNDRVTVELSGGPVGATALDIRDN | Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor. Consists of a catalytic RNA component and at least 4-5 protein subunits. Belongs to the eukaryotic/archaeal RNase P protein component 2 family. |
A9GWT4 | MKCPFCGHLEDRVIDSRAGGAGEVIRRRRECASCERRFTTYERVEDILPTVVKKDGRRESFDRQKLVRGLRIACNKRPVSTDQIEAIADAIEREAQESERREILSTELGERVMNHLRTLDEVAYVRFASVYRSFRDIDQFMVELGKLVKAKAP | Negatively regulates transcription of bacterial ribonucleotide reductase nrd genes and operons by binding to NrdR-boxes. Binds 1 zinc ion. Belongs to the NrdR family. |
B5YD92 | MEITEIKLKKRDKIGKQYAKKYRRSNLIPGVVYGAHLKENIHVLVEKKDLWNLIKKGHSKEQHILRLIIEDGENTITENAILQDIQIDPIKDDLLHVDFHAVSLEEVVDVYVPVVLVGESKGVKQGGILQHGVEEILIRALPLDVPPHIEVDITDLEIGDSITVGDLNLPENIKVLTPADEVIVNIIPPKGYTEEASTEESQTESQS | This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance. Part of the 50S ribosomal subunit; part of the 5S rRNA/L5/L18/L25 subcomplex. Contacts the 5S rRNA. Binds to the 5S rRNA independently of L5 and L18. Belongs to the bacterial ribosomal protein bL25 family. CTC subfamily. |
C0MCC1 | MFVKKGDKVRVIAGKDKGVEAVVLKALPKVNKVIVEGVAIIKKHQKPNSENPQGAIVEKEAPIHASNVQVLDKNGVAGRVGYKFVDGKKVRYNKKSGEVLD | One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. Part of the 50S ribosomal subunit. Belongs to the universal ribosomal protein uL24 family. |
C6DHQ1 | MTPEILPIEQYDDQLAEKTERLRGMMAPFNAPEPVVFRSPVSHYRMRAEFRIWHEGDELYHIMFDQQTKQRIRVDRFPAASELINRLMPELLAAIQPDSVLRRKLFQIDYLSTLSGEVIVSLLYHRALDEEWQEHARALRDSLTAQGFRLQLIGRATKTKICLDRDYVDECLPVAGRDMIYRQVENSFTQPNAAINIQMLEWALDATAGSTGDLLELYCGNGNFSLALARNFERVLATEIAKPSVAAAQYNIAANQIENVQIIRMAAEEFTQAMQGVRQFNRLQGIDLTSYQCETIFVDPPRSGLDDETVKLVQAYPRILYISCNPETLSHNLQTLSETHDIRRLALFDQFPYTHHMECGVLLEKRQ | Dual-specificity methyltransferase that catalyzes the formation of 5-methyluridine at position 54 (m5U54) in all tRNAs, and that of position 341 (m5U341) in tmRNA (transfer-mRNA). S-adenosyl-L-methionine + uridine(54) in tRNA = 5-methyluridine(54) in tRNA + H(+) + S-adenosyl-L-homocysteine S-adenosyl-L-methionine + uridine(341) in tmRNA = 5-methyluridine(341) in tmRNA + H(+) + S-adenosyl-L-homocysteine Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family. TrmA subfamily. |
D2Y2I6 | MKASMFLALAGLVLLFVVGYASESEEKEFPRELLSKIFAVDDFKGEERGCKGFGDSCTPGKNECCPNYACSSKHKWCKVNLGK | Lethal neurotoxin. Selectively blocks tetrodotoxin-sensitive voltage-gated sodium channels (Nav). Does not affect tetrodotoxin-resistant voltage-gated sodium channels or calcium channels (By similarity). Monomer. Expressed by the venom gland. The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin. Belongs to the neurotoxin 10 (Hwtx-1) family. 15 (Hntx-3) subfamily. |
P0C9F2 | MVRLFRNPIKCIFYRRSRKIQEKKLRKSLKKLNFYHPPEDCCQIYRLLENVPGGTYFITENMTNDLIMVVKDSVDKKIKSIKLYLHGSYIKIHQHYYINIYMYLMRYTQIYKYPLICFNKYYNI | Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Belongs to the asfivirus MGF 100 family. |
P81010 | TIMSHNVP | The N-terminus is blocked. Glycosylated. Causes an allergic reaction in human. The MW of the complete protein is 65 kDa with a pI of 3.6. |
Q7UH36 | MNPILVLLCVIALGLLVGRVSFRGISLGTSAILFVALLAGHYGWTIPTGFGTLGLALFVYCVGISAGPTFFRGLASHGRAMAITGSVIVLTGVAVTWTSARLLGLPAELAGGLMAGAMTSTPALGAITQSSSDPAAVAVGFGVAYPIGIIAVVLFVQIAIKLFAKPGDSDGTDSASETSGQSSAEIAESNSIGRRVVRIANPVVSGKRPSDIVAFADSPCQMSRVQREGRWRPTPPDYQFEIGDDVMLVGGASEIRRVSETLGELQDTAEPVVDADRERRYVVVTSPEIYGRTLKELRLRSKYGVTIVRVQRHDVEFVPSARTRIEFGDGLVAVGEPDALAKIANAVGHRPRTVNETDLLSLVAGIVLGIFVGNLSLQIGEFSMSLGIAGGPLMVGLILGHFRRLGPIRGSYPPAAMLLMTEGGLALFLADAGLNAGANVVEVLMERGAMLCVAAAAIAIIPLLVGFAGSRYFGGRTLWQSLGATCGGMTSTPGLAVLTGATDSSQPATSYVAAYPVALVLITVAAPWLVELIG | Belongs to the AAE transporter (TC 2.A.81) family. |
P10951 | MKFLSIISLAVSLVAAAPVEVGLDTGVANLEARQSSTRNELESGSSSNCPKVIYIFARASTEPGNMGISAGPIVADALESRYGASQVWVQGVGGPYSADLASNFIIPEGTSRVAINEAKRLFTLANTKCPNSAVVAGGYSQGTAVMASSISELSSTIQNQIKGVVLSAITKNLQNLGRIPNFSTSKTEVYCALADAVCYGTLFILPAHFLYQADAATSAPRFLAARIG | Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants (PubMed:33606796). Degrades cutin, a macromolecule that forms the structure of the plant cuticle (PubMed:33606796). Allows pathogenic fungi to penetrate through the cuticular barrier into the host plant during the initial stage of fungal infection (By similarity). cutin + H2O = cutin monomers. Partially inhibited by berberine; higher inhibitory effects are observed with longer chain polyester substrates. The 2 disulfide bonds play a critical role in holding the catalytic residues in juxta-position; reduction of the disulfide bridges results in the complete inactivation of the enzyme. Belongs to the cutinase family. |
Q7SHY3 | MSGTIPHFWAQPFRYIRWSAREKPAYFYSCVIAGLGPVFLTVVPPVRKYFGDVNPAPIPVTYPIPTGPRKQLTGYDDDTEEA | Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. This subunit binds ubiquinone. Complex I is composed of about 40 different subunits. Belongs to the complex I NDUFA3 subunit family. |
Q11S31 | MKFFIDTANLNEIREAQELGILDGVTTNPSLMAKEGISGKDNVFKHYKAICDIVDGDVSAEVIATDYKGIIEEGEELITIDPKIVVKVPMIKDGIKAIKYFSQKGIRTNCTLVFSAGQALLAAKAGATYVSPFIGRLDDISQDGMELIAQIVGIYRNYDYQTEVLAASVRHTMHLINCAEVGADVVTCPLNVITGLLNHPLTDSGLAKFLADHKKVNG | Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = beta-D-fructose 6-phosphate + D-erythrose 4-phosphate Carbohydrate degradation; pentose phosphate pathway; D-glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage): step 2/3. Belongs to the transaldolase family. Type 3B subfamily. |
B4EAH3 | MSTWLLPENIADVLPSEARKIEELRRRLLDRFRSYGYEMVMPPLLEYLESLLTSGGADLRLRTFKLVDQLSGRTLGLRADITPQVARIDAHLLNRQGVTRLCYAGHVMHTRPRGLHATREQIQIGAEIYGHAGLEADLEIQQLMLDALHLAGLSRIRLDLGHAGVLAALLARDAQAAERGESLYDALSGKDVPLLNELTDDLGADTRAALRALPNLYGDASVLAEARTRLPVLPEITRALDDLAQLASQPKGVEVAIDLADLRGYAYHSGAMFSAYIDGVPNAIARGGRYDHVGQAYGRARPATGFSLDLRELARISPVEARGTAILAPWAQDDALGAAVAALRDAGEVVIQALPGHDHVLDEFACDRSLVERNGAWVVEPR | Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine. Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9. Heteromultimer composed of HisG and HisZ subunits. This function is generally fulfilled by the C-terminal part of HisG, which is missing in some bacteria such as this one. Belongs to the class-II aminoacyl-tRNA synthetase family. HisZ subfamily. |
B4EYV7 | MARQTPIARYRNIGISAHIDAGKTTTSERILFYTGVNHKIGETHEGSATMDWMEQEQERGITITSAATTAFWSGMAKQFEPHRVNIIDTPGHVDFTIEVERSMRVLDGAVMVYCAVGGVQPQSETVWRQANKYHVPRIAFVNKMDRMGANFLRVVEQIKTRLAANPVPLQIPVGAEEDFTGVVDLIKMKAIRWNEEDQGVTFEYEDIPADLQDLAEEWHNNLIESAAEASEDLMDKYLGGEELSEAEIKSALRKRVLDNEIILVTCGSAFKNKGVQAMLDAVIEYLPAPTDVPAIKGILPDGKDTPAERHSSDEEPFSALAFKIATDPFVGNLTFFRVYSGVVNSGDTVLNPVKDKKERFGRIVQMHANKREEIKEVRAGDIAAAIGLKDVTTGDTLCAIDAPIILERMEFPEPVISVAIEPKTKADQEKMGIALNRLAQEDPSFRVSSDEESGQTIIAGMGELHLDVLVDRMRREFKVEANVGKPQVAYRETIREEITDVEGKHAKQSGGRGQYGHVVIDLSPLPSGGEENYVFVNDIVGGVIPKEFIPAVDKGIQEQLKSGPLAGYPVVDIKARLHFGSYHDVDSSEIAFKIAASMAFKEGFMKAKPILLEPIMKVEIETPEDYMGDVIGDLNRRRGMVEGMDDLPTGKIIRAQVPLAEMFGYATDLRSQTQGRASYSMEFLKYNEAPSNVAQAIIEARKAK | Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily. |
Q73NP0 | MNCIFLGPPGAGKGTLAFEVSKSYKIPHISTGDLFRAAIKEQTDLGKKVKAVIDSGALVSDDLTIALVKERLERDDTKKGFILDGFPRTIAQADALEDIVKIDSVINFDISDDEVIKRLSGRRVCSSCGQSFHIEFVKPKKEGICDSCSGDLMIRPDDKIEAIQKRLETYRNQTAPLIDYYTKKDLIVNIDARPASEKVLASFKVKFPH | Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. AMP + ATP = 2 ADP Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1. Monomer. Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis. Some bacteria have evolved a zinc-coordinating structure that stabilizes the LID domain. Belongs to the adenylate kinase family. |
Q8NA28 | MPIKPVGWICGQVLKNFSGRIEGIQKAIMDLVDEFKDEFPTILRLSQSNQKREPAQKTSKIRMAIALAKINRATLIRGLNSISRSSKSVAKLLHPQLACRLLELRDISGRLLREVNAPRQPLYNIQVRKGSLFEIISFPAKTALTSIIYASYAALIYLAVCVNAVLKKVKNIFQEEESIRQNREESENCRKAFSEPVLSEPMFAEGEIKAKPYRSLPEKPDISDYPKLLANKQSNNIQVLHSVFDQSAEMNEQI | May play a role in testicular development/spermatogenesis and may be an important factor in male infertility. Highly expressed in testes and pancreas. Low levels found in the heart, lungs, and brain. Very low expression detected in the placenta. No expression seen in skeletal muscle, liver, kidney, thymus, small intestine, colons, spleen, leukocytes, prostate gland, and ovary. In the adult testes, expression was about 6.44-fold higher than in the embryo testes. No expression in testes of patients with Sertoli-cell-only syndrome. In patients with arrest at spermatogonium and primary spermatocyte stages, no expression was detected. In patients with arrest at the spermatid stage, expression level was weak or absent. Variable expression was seen in patients with spermatogenic arrest. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. |
V6RV03 | MTSTTPPKLNALEILDLRSSPPAFTTPSKRINEGSDVARFLTSLAYRDIGVFILQLNRALCPRNQSSSPLPRTFPLNSKPATTPSVQTLQALLAKIGSFIDEAPPDPGPRRFGNVSFRKWHAIFEERLSELLDEGLLGETLKVGDGKAKEEVSLYLLGGFGSVQRLDYGTGHELSFVAFLGCLWKLGFFKDGEQGGEIEREIVLKIIEPYLNVVRKLILTYTLEPAGSHGVWGLDDHSFMPYIFGSAQLTRPINENEPMPLEGSVKGAPKPSDVTKAVVVEDQRQVNMYFSAIGFINDVKKGPFWEHSPILFDISGIRDGWGKINKGMIKMFNAEVLSKFPVVQHFPFGSLFSWDVDPDATTPTQSVHMVNQPAMAAPTPSGPGTSAPWAQATRMPPSGPGIPYSRMPPPGPNSGSLARPPRNTSGTGSTDAQITVTKAPWARDS | PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex (By similarity). [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0) Belongs to the PTPA-type PPIase family. |
Q9HII0 | MLITEIFHSIQGEGPYAGLPMLFVRTNVCNIRCEWCDTKYSFYGGKEIPLSELLGIVKEAKEGWVCFTGGEPLVQRDALAFVKSVVDMGKNVLIETNGTISIRNFVFSDRIFIDMDVKPPSAKVTKGFLMDNLRYLRKQDYLKIVIKDDTDLDFAIDFVDRYGEGLSFVFQPAWGSDIRRIADRIVGTGYNVRVLPQIHKIIYGDVPGV | Catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-carboxy-7-deazaguanine (CDG), a step common to the biosynthetic pathways of all 7-deazapurine-containing compounds. 6-carboxy-5,6,7,8-tetrahydropterin + H(+) = 7-carboxy-7-deazaguanine + NH4(+) Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Binds 1 S-adenosyl-L-methionine per subunit. Purine metabolism; 7-cyano-7-deazaguanine biosynthesis. Homodimer. Belongs to the radical SAM superfamily. 7-carboxy-7-deazaguanine synthase family. |
B1J9E8 | MLKSLLAIGLGAMVGAWLRWGLGMKLNALFPAVPPGTLLANLIGGYIIGLAIAFFSASPSLSPEWRLLLITGFCGGLTTFSTFSAEVVSLIQEGRILWALGSIALHVSGSLLMTAAGLATFYFISGR | Important for reducing fluoride concentration in the cell, thus reducing its toxicity. Belongs to the CrcB (TC 9.B.71) family. |
B5XMX0 | MKVTFSQLKEAFNQVLLKRGVAAETADACADMFARTTESGVYSHGVNRFPRFIQQLDNGDIIPEAKPQRITSLGAIEQWDAQRSIGNLTAKKMMDRAMELASDHGIGLVALRNANHWMRGGSYGWQAAEKGYIGICWTNSIAVMPPWGAKECRIGTNPLIVAIPSTPITMVDMSMSMFSYGMLEVNRLAGRELPVDGGFDDEGNLTKEPGVIEKNRRILPMGYWKGSGLSIVLDMIATLLSNGSSVAEVTQENSDEYGVSQIFIAIEVDKLIDGATRDAKLQRIMDFITTAERADENVAVRLPGHEFTRLLEENRRDGITVDDSVWAKIQAL | Catalyzes the reduction of 2,3-diketo-L-gulonate in the presence of NADH, to form 3-keto-L-gulonate. 3-dehydro-L-gulonate + NAD(+) = 2,3-dioxo-L-gulonate + H(+) + NADH 3-dehydro-L-gulonate + NADP(+) = 2,3-dioxo-L-gulonate + H(+) + NADPH Homodimer. Belongs to the LDH2/MDH2 oxidoreductase family. DlgD subfamily. |
Q9CKU1 | MNLMINLKPLTFLPFFGRLVFLSGVIYNTAWANTVIPVDNSRPDETFSQTSPKQHLFSQKPKPTEPTSSASSQQISLTIEQLASRPDLVLRALIPALKNNDMRGVEILLPIYAKQSPDPFLLKWAQAVVARKQGKLNESVRLYRQIIAEKPNLQPARLQLAIALTQNRENEAAKAQFNQLRSENLPAPLLTLIDSYIDTINQRDSWNVYGGVNYLHENNVNNAPPKGTKAEGFTPSSQPEKAHGLSYFINLSKNWSLAHGFFTEFSADINGKYYWDNHKYDEFSTRLNLGGGYRNAKTEVKLMPFVEQFWYVGGENATKDARTLHRYSKSSGINLDVDYWLTPNWKISTVLEYTEQRYIQPQRQNSNGNSYSISNTLIYMPNSQQFWFVGLDYYQKNTRLKAYAFERQGIRLGWGQEWPKGISTRLQTSYATRTYRAPSAEKNMIFAPSFFKVVQKNHEYGVNFTIWHRSLHWLGITPKITWAYQKTTSNNPFSEYDRNRIYLTFSKTF | Required for correct export to the cell surface of some cell outer membrane lipoproteins (tested with PM1514) upon heterologous expression in E.coli and probably also in Pasteurella. Consists of a soluble N-terminal domain and C-terminal probable beta-barrel in the outer membrane with 14 predicted beta-strands. Belongs to the Slam family. |
A1KS31 | MVLDGFAAHFDAYLENIVREGKSEHTVAAYRRDLEELFALLAQMPSEDVGGVPQDLSRRDFTAALRRLSQRGLNARTLARKLSSWRQYCVWLVERGLLHTDPTADIKPPKQPERVPKALPQEWLNRMLDLPVDGGDPLAVRDHALFELMYGSGLRVSEIHGLNADDVYLDEAWVHVTGKGRKQRQVPLTGKSVEALKNYLPLRQTASDGKALFTGRNGTRLSQRQIQKRLAQWAAQNGDGRHVSPHMMRHSYAGHLLQASRDIRAVQELLGHSSLSTTQIYTKLDFDHIARLYDEAHPRAKRRDE | Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC-XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids. Forms a cyclic heterotetrameric complex composed of two molecules of XerC and two molecules of XerD. Belongs to the 'phage' integrase family. XerC subfamily. |