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Q2VLG5

MSKLRMVLLEDSGSADVRRHFVNLSPFTIAVVLLLRACFVTSSLGGTTKELRLVDGENKCSGRVEVKIQEEWGTVCNNGWSMEAVSVICNQLGCPTAIKATGWANSSAGSGRIWMDHVSCRGNESALWDCKHDGWGKHSNCTHQQDAGVTCSDGSDLEMRLTNGGNMCSGRIEIKFQGQWGTVCDDNFNINHASVVCKQLECGSAVSFSGSANFGEGSGPIWFDDLICNGNESALWNCKHQGWGKHNCDHAEDAGVICSKGADLSLRLVDGVTECSGRLEVRFQGEWGTICDDGWDSHDAAVACKQLGCPTAITAIGRVNASEGFGHIWLDSVSCQGHEPAVWQCKHHEWGKHYCNHNEDAGVTCSDGSDLELRLRGGGSRCAGTVEVEIQRLLGKVCDRGWGLKEADVVCRQLGCGSALKTSYQVYSKIQATNMWLFLSSCNGNETSLWDCKNWQWGGLTCDHYEEAKITCSAHREPRLVGGDIPCSGRVEVKHGDTWGSVCDSDFSLEAASVLCRELQCGTVVSILGGAHFGEGNGQIWTEEFQCEGHESHLSLCPVAPRPEGTCSHSRDVGVVCSRYTEIRLVNGKTPCEGRVELKTLNAWGSLCNSHWDIEDAHVLCQQLKCGVALSTPGGAHFGKGNGQVWRHMFHCTGTEQHMGDCPVTALGASLCPSGQVASVICSGNQSQTLSSCNSSSLGPTRPTIPEESAVACIESGQLRLVNGGGRCAGRVEIYHEGSWGTICDDSWDLSDAHVVCRQLGCGEAINATGSAHFGEGTGPIWLDEMKCNGKESRIWQCHSHGWGQQNCRHKEDAGVICSEFMSLRLTSEASREACAGRLEVFYNGAWGSVGRSNMSETTVGVVCRQLGCADKGKINSASLDKAMSIPMWVDNVQCPKGPDTLWQCPSSPWEKRLARPSEETWITCDNKMRLQEGPTSCSGRVEIWHGGSWGTVCDDSWDLNDAQVVCQQLGCGPALKAFKEAEFGQGTGPIWLNEVKCKGNESSLWDCPARRWGHSECGHKEDAAVNCTDISTRKTPQKATTGQSSLIAVGILGVVLLAIFVALFLTQKRRQRQRLTVSSRGENLVHQIQYREMNSCLNADDLDLMNSSENSNESADFNAAELISVSKFLPISGMEKEAILRHTEKENGNL

Involved in clearance and endocytosis of hemoglobin/haptoglobin complexes by macrophages and may thereby protect tissues from free hemoglobin-mediated oxidative damage. May play a role in the uptake and recycling of iron, via endocytosis of hemoglobin/haptoglobin and subsequent breakdown of heme. Binds hemoglobin/haptoglobin complexes in a calcium-dependent and pH-dependent manner. Induces a cascade of intracellular signals that involves tyrosine kinase-dependent calcium mobilization, inositol triphosphate production and secretion of IL6 and CSF1 (By similarity). After shedding, the soluble form (sCD163) may play an anti-inflammatory role. Interacts with CSNK2B. The SRCR domain 3 mediates calcium-sensitive interaction with hemoglobin/haptoglobin complexes. A soluble form (sCD163) is produced by proteolytic shedding which can be induced by lipopolysaccharide, phorbol ester and Fc region of immunoglobulin gamma. This cleavage is dependent on protein kinase C and tyrosine kinases and can be blocked by protease inhibitors. The shedding is inhibited by the tissue inhibitor of metalloproteinase TIMP3, and thus probably induced by membrane-bound metalloproteinases ADAMs (By similarity). Phosphorylated.

O76554

MLIIIQSLLLATTASLCIADTPVPTQIRLVHDLLDNYDKKAKPMWDNSKPINVSFSMDLYQILELNEPQQYILLNAWIIERWFDEFLYWNPDDYENITELRLPYDSIWLPDTTLYNSLVMKDDDTRRLLNSKLTTDTHRRAALIELLYPTIYKFSCLLDLRFFPFDVQVCTMTFSSWTYDQKGIDYFPYSDKIGTSNYLENEGWYILQTKIKRQEVKYACCPNNYTLLQLTLYLRRKPLFYLVNLIIPTSIITLIAIVGFFTTSSASGMREEKVSLGITTLLSMSILMLMVSDQMPTTSTFIPLIGWFILAMIIVISLGTVVSSVIIAIQKRGSLGERMSKRALKFAKVLAWFTCTSLPPHVEKEHMMEAFDAPTPLVEVRPLQLASVKESVRNKWVSGARRATQRGNSGLALISDKSTDPLIHLSPTAHQPDESISPSAPPVPSSSPLPPPLTPGPADDVVSVASELSSKFLTSRMRPKSQKDNTFAAMQSSIKANRQLAVAEFEWFATVVERTCFVIFVVAFLIITFGINFIGFIHWHQAGVEYGG

Subunit of the non-synaptic neuronal acetylcholine receptor (AChR), which may play a role in chemotaxis towards choline. After binding choline or acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. The functional receptor is a heteromer of deg-3 and des-2. Interacts with ric-3; which is required for proper receptor folding. Enriched in the sensory endings of sensory neurons. Belongs to the ligand-gated ion channel (TC 1.A.9) family. Acetylcholine receptor (TC 1.A.9.1) subfamily.

P31998

TSPNINGFWVMLENDEQIEFPIKPLIDHARPTFRQIMSRFSDLAEAYIEKRNFERAYMPRYGLQRNLTDMSLRRYAFDFYEMTSKAPARA

Involved in aphid transmission, cell-to-cell and systemis movement, encapsidation of the viral RNA and in the regulation of viral RNA amplification. Genome polyprotein of potyviruses undergoes post-translational proteolytic processing by the main proteinase NIa-pro resulting in the production of at least ten individual proteins. The P1 proteinase and the HC-pro cleave only their respective C-termini autocatalytically. 6K1 is essential for proper proteolytic separation of P3 from CI (By similarity). Belongs to the potyviridae genome polyprotein family.

D6VUJ6

MTDYILPGPKALSQFRVDNLIKDINSYTNSTSVINELRSCYIHYVNGIAQNLSEQDTKLLEVLLTYDSALDIANDPLARQLNDAVANNLPSSALGEDTYLIRVVPRSGTISPWSSKATNIAHVCGLQDKVQRIERGLALLIKTVPGFPLLENLNDISLKCVYDRMTQQLYLTEPPNTMSIFTHEEPKPLVHVPLTPKDTKQSPKDILSKANTELGLALDSGEMEYLIHAFVETMKRDPTDVELFMFAQVNSEHCRHKIFNADWTIDGIKQQFTLFQMIRNTHKLNPEYTISAYSDNAAVLDSENDAFFFAPNSTTKEWTSTKERIPLLIKVETHNHPTAVSPFPGAATGSGGEIRDEGATGRGSKTKCGLSGFSVSDLLIPGNEQPWELNIGKPYHIASALDIMIEAPLGSAAFNNEFGRPCINGYFRTLTTKVLNHQGKEEIRGFHKPIMIAGGFGTVRPQFALKNTPITPGSCLIVLGGQSMLIGLGGGAASSVASGEGSADLDFASVQRGNPEMERRCQQVIDACVALGNNNPIQSIHDVGAGGLSNALPELVHDNDLGAKFDIRKVLSLEPGMSPMEIWCNESQERYVLGVSPQDLSIFEEICKRERAPFAVVGHATAEQKLIVEDPLLKTTPIDLEMPILFGKPPKMSRETITEALNLPEANLSEIPSLQDAIQRVLNLPSVGSKSFLITIGDRSVTGLIDRDQFVGPWQVPVADVGVTGTSLGETIISTGEAMAMGEKPVNALISASASAKLSVAESLLNIFAADVKSLNHIKLSANWMSPASHQGEGSKLYEAVQALGLDLCPALGVAIPVGKDSMSMKMKWDDKEVTAPLSLNITAFAPVFNTSKTWTPLLNRNTDDSVLVLVDLSAKQETKSLGASALLQVYNQVGNKSPTVYDNAILKGFLESLIQLHQQKEDIVLAYHDRSDGGLLITLLEMAFASRCGLEINIDGGDLESQLTNLFNEELGAVFQISAKNLSKFEKILNENGVAKEYISIVGKPSFQSQEIKIINSTTNDVIYANSRSELEQTWSKTSYEMQKLRDNPKTAEEEFASITDDRDPGLQYALTYNPADDMKIGLELSSQRPKVAILREQGVNGQMEMAWCFQQAGFNSVDVTMTDLLEGRFHLDDFIGLAACGGFSYGDVLGAGAGWAKSVLYHEGVRSQFSKFFNERQDTFAFGACNGCQFLSRLKDIIPGCENWPSFERNVSEQYEARVCMVQISQEKDNSSEESVFLNGMAGSKLPIAVAHGEGKATFSKSAEQLEKFEKDGLCCIRYVDNYGNVTERFPFNPNGSTNGIAGIKSPNGRVLAMMPHPERVCRLEANSWYPEGKYEEWGGYGPWIRLFRSARRWVG

Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate (By similarity). ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 1/2. Present with 40800 molecules/cell in log phase SD medium. In the N-terminal section; belongs to the FGAMS family.

Q8MCM3

MKEYRVYLERARSRQQDFLYPLIFREYIYGLAYSHIDRSIFVENGGYDNKYSLLNVKRLITQMYQQNHLIISTNDSNKNPFLGYNKNFYSQIIAEGFAIVVEIPFFLQLSSSLEEAEIIKSYKNVRSIHSIFPFLEDKFTYLNYVSDIRIPYPIHLEILVQILRYWVKDAPFFHLLRLFLYDFCNWNCFIPTKKSISTFSKSNPRLFLFLYNFYVCEYESIFLFLRNKSSHLRLKSFSVFNERIFFYAKREHLVEVFSKDFSYTLPFFKDPNIHYVRYQGKCILASKNGPFLMNKWKHYFIHLWQCFFDVWSQPRTININQLSEHSIQLLGYFSNVRLNRSVVRSQMLQNTFLIEIVSKKLDIIVPIIPIIRSLAKAKFCNVLGHPISKPVWADSSDFDIIERFLRICSNLCHYYHGSSKKKSLYRIKYILRLSCIKTLACKHKSTVRAFLQTSGSEELLEEFFTEEEEILPWNFQILSLICHSKSFTSHGFHSNRIWYLDILFSNDLE

Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns. Belongs to the intron maturase 2 family. MatK subfamily.

Q3SKN1

MAVTLAALVERFGGELVGDSARSVRQVAPLDRACADDIGFVSQSKYLAELATTGAGAVILPPDARDATDLPRILTPNPYLYFARVSALLNPPPRPAAGVHPAATVAADAEVAADASIAAGAVIGSGARIGARSVIGANSVVGDGARVGEDCLLHANVSLYHGCQVGDRVILHAGCVIGADGFGFAPNEGRWEKIPQIGRVLIGDDVEVGACTTIDRGALEDTVIEEGVKLDNLIQVAHNVVIGAHSAIAACTGIAGSAKIGRHCTIGGAAMIFGHIEIADGTRISTNTLITKSLPKRGTYTSALPFSEHEVWQKNAVHMRNLDKLVTRVKQLEKRLNELENKT

Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine = a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + H(+) + holo-[ACP] Bacterial outer membrane biogenesis; LPS lipid A biosynthesis. Homotrimer. Belongs to the transferase hexapeptide repeat family. LpxD subfamily.

Q96IG3

MGEPRAGAALDDGSGWTGSEEGSEEGTGGSEGAGGDGGPDAEGVWSPDIEQSFQEALAIYPPCGRRKIILSDEGKMYGRNELIARYIKLRTGKTRTRKQVSSHIQVLARRKSREIQSKLKDQVSKDKAFQTMATMSSAQLISAPSLQAKLGPTGPQASELFQFWSGGSGPPWNVPDVKPFSQTPFTLSLTPPSTDLPGYEPPQALSPLPPPTPSPPAWQARGLGTARLQLVEFSAFVEPPDAVDSYQRHLFVHISQHCPSPGAPPLESVDVRQIYDKFPEKKGGLRELYDRGPPHAFFLVKFWADLNWGPSGEEAGAGGSISSGGFYGVSSQYESLEHMTLTCSSKVCSFGKQVVEKVETERAQLEDGRFVYRLLRSPMCEYLVNFLHKLRQLPERYMMNSVLENFTILQVVTNRDTQELLLCTAYVFEVSTSERGAQHHIYRLVRD

Transcription factor which plays a key role in the Hippo signaling pathway, a pathway involved in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein MST1/MST2, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Acts by mediating gene expression of YAP1 and WWTR1/TAZ, thereby regulating cell proliferation, migration and epithelial mesenchymal transition (EMT) induction. Binds to the SPH and GT-IIC 'enhansons' (5'-GTGGAATGT-3'). May be involved in the gene regulation of neural development. Binds to the M-CAT motif. Interacts with YAP1 and WWTR1/TAZ.

Q9LEX5

MSLIGRLNLGRRFCTAVPRRSEDIMSNPDCRPSDLCLRVSYLIRCVGDLDTAAKYARLAVFTSIKSESTTTICQSIIGGMLRDKRLKDAYDLYEFFFNQHNLRPNSHCWNYIIESGFQQGLVNDALHFHHRCINSGQVHDYPSDDSFRILTKGLVHSGRLDQAEAFLRGRTVNRTTYPDHVAYNNLIRGFLDLGNFKKANLVLGEFKRLFLIALSETKDDLHHSNYENRVAFLMATFMEYWFKQGKQVEAMECYNRCVLSNRLLVCAETGNALLKVLLKYGEKKNAWALYHELLDKNGTGKGCLDSDTIKIMVDECFDMGWFSEAMETYKKARPKNDYLSDKYIITRFCENRMLSEAESVFVDSLADDFGYIDVNTYKTMIDAYVKAGRIHDAIKTSNKMIDATLKEVSHLF

Belongs to the PPR family. P subfamily.

A0AZ71

MNRIKQTFAALAEQGRKGLIPFITAGDPDPAKTVEFMHALAAGGADVIELGVPFSDPMADGPVIQRSSERALARGVTLKSVLADVKRFRETDPKTPVVLMGYANPIERMGVDAFAAEAHAAGVDGVLVVDYPPEEAGVFAEKMRAAQIDPIFLLAPTSTDERIADVGKIASGYVYYVSLKGVTGAGNLDVSSIAGKIPAIKSRVPVPVGVGFGIRDAETARAVAEVSDAVVIGSRLVQLLESAAPEGAAAALKTFIAELRAALDGAGNTAR

The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. Tetramer of two alpha and two beta chains. Belongs to the TrpA family.

Q9ZTA4

MGSKPWLHPAPQYKTLETFWDDEDDAPGPRCAHTLTAVAATKTHGPRLILFGGATAIEGGSSSVPGIRLAGVTNTVHSYDILTRKWTRLKPAGEPPSPRAAHAAAAVGTMVVFQGGIGPAGHSTDDLYVLDMTNDKFKWHRVVVQGDGPGPRYGHVMDLVSQRYLVTVTGNDGKRALSDAWALDTAQKPYVWQRLNPDGDRPSARMYASGSARSDGMFLLCGGRDTLGAPLGDAYGLLMHRNGQWEWTLAPGVAPSPRYQHAAVFVGARLHVSGGVLRGGRVIDAEASVAVLDTAAGVWLDRNGQVTSARGSKGQIDQDPSFELMRRCRHGAASVGIRIYVHGGLRGDVLLDDFLVAENSTFQSDISSPLLASDRTQQSSTPRFSYAARPPSGSEPSFSMSEGLSLDENSLEKLTEASAAEAEVASSVWRAAQLGAGTLDEEPSTSDASSPIVESTTDGTANEGDVRLHPRAVVVAKETVGSLGGMVRQLSLDQFQNESRRMVPMNNSDVPQPTKKFTRQKSPQGLHKKVIAALLRPRNWKPPGNRKFFLDSYEVGELCYAAEQIFMHEQTVLQLKAPIKVFGDLHGQFGDLMRLFDEYGFPSTAGDITYIDYLFLGDYVDRGQHSLETITLLLALKIEYPENVHLIRGNHEAADINALFGFRLECIERMGENDGIWAWTRFNQLFNYLPLAALIENKIICMHGGIGRSISTVEQIEKIERPITMDAGSLVLMDLLWSDPTENDSIEGLRPNARGPGLVTFGPDRVTEFCKRNKLQLIIRAHECVMDGFERFAQGQLITLFSATNYCGTANNAGAILVVGRGLVIVPKLIHPLPPPILSPENSPEHSGDDAWMQELNIQRPPTPTRGRPQPDFDRSSLAYI

Phosphatase involved in elongation process, probably by acting as a regulator of brassinolide signaling. H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate Binds 2 manganese ions per subunit. Interacts with CDG1 and CDL1. Expressed in mature cauline leaves and at the tip of influorescence, including flowers. Expressed at lower level in young tissues relative to older ones. Belongs to the PPP phosphatase family. BSU subfamily.

P33936

MSRSAKPQNGRRRFLRDVVRTAGGLAAVGVALGLQQQTARASGVRLRPPGAINENAFASACVRCGQCVQACPYDTLKLATLASGLSAGTPYFVARDIPCEMCEDIPCAKVCPSGALDREIESIDDARMGLAVLVDQENCLNFQGLRCDVCYRECPKIDEAITLELERNTRTGKHARFLPTVHSDACTGCGKCEKVCVLEQPAIKVLPLSLAKGELGHHYRFGWLEGNNGKS

Required for electron transfer from ubiquinol, via NapC, to the periplasmic nitrate reductase NapAB complex. Binds 4 [4Fe-4S] cluster. Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.

P82765

MAITKKILLPFVLTILFVISSVHCSDDTQGFGIKQEYKQCYTPDPCRKGGNDECERFCVAKSGLLYGKCINDGSKDVCCCLTK

Belongs to the DEFL family.

Q54SZ9

MKQKLLLFIFSILILLIAAEAKMFKDIWKSCGKSTDTFQIKNVTISPDPPVRGQTVSIYASGELKDTISGGDVNIQIKFGIITIIRETKPICSSDNPFPCPIQPGDYTHSVDIAIPDNAPRGKYSGNFVLTDQANDEIACINVNMQL

Catalyzes the intermembrane transfer of phosphatidylglycerol and phosphatidylinositol. Monomer. Belongs to the NPC2 family.

A1UEH2

MPSVSVWVRSLAPMTTWTRAAIGALGEDLAVKHLDSLGMRVLERNWRCRYGELDVIAEDPAARAVVFVEVKTRTTDHFGGVAEAVTPQKVRRLRRLAGLWLAGRDERWAAVRIDVIGVRIGRQATPEITHLTGVA

Belongs to the UPF0102 family.

Q9Y7C9

MRYQASPALVKAPRALLCIHGAGCSPAIFRVQLSKLRAALRENFEFVYVTAPFPSSAGPGILPVFADLGPYYSWFESSSDNNHNGPSVSERLAAVHDPIRRTIVDWQTQHPHIPIVGAIGFSEGALVTTLLLWQQQMGHLPWLPRMSVALLICPWYQDEASQYMRNEVMKNHDDDNDSKDTEWQEELVIRIPTLHLQGRDDFALAGSKMLVARHFSPREAQVLEFAGQHQFPNRPRDVLEVINRFRKLCVTAQTLE

Esterase; part of the gene cluster that mediates the biosynthesis of lovastatin (also known as mevinolin, mevacor or monacolin K), a hypolipidemic inhibitor of (3S)-hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR) (PubMed:10334994, PubMed:12929390, PubMed:21495633). The first step in the biosynthesis of lovastatin is the production of dihydromonacolin L acid by the lovastatin nonaketide synthase lovB and the trans-acting enoyl reductase lovC via condensation of one acetyl-CoA unit and 8 malonyl-CoA units (PubMed:10334994, PubMed:10381407, PubMed:19900898, PubMed:22733743). Dihydromonacolin L acid is released from lovB by the thioesterase lovG (PubMed:23653178). Next, dihydromonacolin L acid is oxidized by the dihydromonacolin L monooxygenase lovA twice to form monacolin J acid (PubMed:12929390, PubMed:21495633). The 2-methylbutyrate moiety of lovastatin is synthesized by the lovastatin diketide synthase lovF via condensation of one acetyl-CoA unit and one malonyl-CoA unit (PubMed:19530726, PubMed:21069965). Finally, the covalent attachment of this moiety to monacolin J acid is catalyzed by the transesterase lovD to yield lovastatin (PubMed:10334994, PubMed:17113998, PubMed:18988191, PubMed:19875080, PubMed:24727900). LovD has broad substrate specificity and can also convert monacolin J to simvastatin using alpha-dimethylbutanoyl-S-methyl-3-mercaptopropionate (DMB-S-MMP) as the thioester acyl donor, and can also catalyze the reverse reaction and function as hydrolase in vitro (PubMed:19875080). LovD has much higher activity with LovF-bound 2-methylbutanoate than with free diketide substrates (PubMed:21069965). Esterase that catalyzes the release of covalently bound dihydromonacolin L from LovB during lovastatin biosynthesis. dihydromonacolin L-[lovastatin nonaketide synthase] + H2O = dihydromonacolin L carboxylate + H(+) + holo-[lovastatin nonaketide synthase] Polyketide biosynthesis; lovastatin biosynthesis. Strongly reduced lovastatin biosynthesis. Low levels of lovastatin are released due to complementation by other esterases. Lovastatin acts as a hypolipidemic agent that works as inhibitor of (3S)-hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR) which reduces HMG-CoA to mevalonate and is the key step in cholesterol biosynthesis (PubMed:6933445). Lovastatin, simvastatin and related compounds are widely used to treat hypercholesteremia and reduce the risk of cardiovascular disease (PubMed:6933445). Furthermore, statins such as lovastatin were found to be anticancer agents (PubMed:29236027, PubMed:29932104). Belongs to the LovG family.

O21414

MTNLRKTHPLMKIVNSSFIDLPAPSNISSWWNFGSLLGICLIIQILTGLFLAMHYTSDTMTAFSSVTHICRDVNYGWLIRYLHANGASMFFICLFLHVGRGLYYGSYMYLETWNIGVLLLFAVMATAFMGYVLP

Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis. Binds 2 heme b groups non-covalently. The cytochrome bc1 complex contains 11 subunits: 3 respiratory subunits (MT-CYB, CYC1 and UQCRFS1), 2 core proteins (UQCRC1 and UQCRC2) and 6 low-molecular weight proteins (UQCRH/QCR6, UQCRB/QCR7, UQCRQ/QCR8, UQCR10/QCR9, UQCR11/QCR10 and a cleavage product of UQCRFS1). This cytochrome bc1 complex then forms a dimer. Heme 1 (or BL or b562) is low-potential and absorbs at about 562 nm, and heme 2 (or BH or b566) is high-potential and absorbs at about 566 nm. Belongs to the cytochrome b family. The full-length protein contains only eight transmembrane helices, not nine as predicted by bioinformatics tools.

Q75CI4

MVFRAGIGRIGLIRGLATQAAEVSATRYKSFKIYRWNPDTPAEKPRMQEYKVDLNKCGPMVLDALIKIKNEQDPTLTFRRSCREGICGSCAMNIGGRNTLACLCKIDQAENKDVKIYPLPHMYVVKDLVPDLTNFYKQYKSIQPYLQKASKPADGREHLQSIADRKKLDGLYECILCACCSTACPSYWWNNEQYLGPAVLMQAYRWMVDSRDGAGAGRREQLQNAMSVYRCHTIMNCTRTCPKGLNPGKAIAEIKKALAFA

Iron-sulfur protein (IP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). a quinone + succinate = a quinol + fumarate Binds 1 [2Fe-2S] cluster. Binds 1 [3Fe-4S] cluster. Binds 1 [4Fe-4S] cluster. Carbohydrate metabolism; tricarboxylic acid cycle; fumarate from succinate (eukaryal route): step 1/1. Component of complex II composed of four subunits: a flavoprotein (FP), an iron-sulfur protein (IP), and a cytochrome b composed of a large and a small subunit. Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family.

Q9UK15

MDLVLRVADYYFFTPYVYPATWPEDDIFRQAISLLIVTNVGAYILYFFCATLSYYFVFDHALMKHPQFLKNQVRREIKFTVQALPWISILTVALFLLEIRGYSKLHDDLGEFPYGLFELVVSIISFLFFTDMFIYWIHRGLHHRLVYKRLHKPHHIWKIPTPFASHAFHPIDGFLQSLPYHIYPFIFPLHKVVYLSLYILVNIWTISIHDGDFRVPQILQPFINGSAHHTDHHMFFDYNYGQYFTLWDRIGGSFKNPSSFEGKGPLSYVKEMTEGKRSSHSGNGCKNEKLFNGEFTKTE

Catalyzes a dehydrogenation to introduce C5-6 double bond into lathosterol in cholesterol biosynthesis. a Delta(7)-sterol + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = a Delta(5),Delta(7)-sterol + 2 Fe(III)-[cytochrome b5] + 2 H2O 2 Fe(II)-[cytochrome b5] + 2 H(+) + lathosterol + O2 = 7-dehydrocholesterol + 2 Fe(III)-[cytochrome b5] + 2 H2O The histidine box domains may contain the active site and/or be involved in metal ion binding. The disease is caused by variants affecting the gene represented in this entry. Belongs to the sterol desaturase family.

C3LSX1

MWFKNCMVYRVNREVNFNADQLEKQLAEFRFTPCGSQDKQKFGWVSALGKHGDMMTHVSENRILVCAKREEKMLPASVIKDSLNAKVEEMEAEEGRPLKKKEKDALKEDIVIDLLPRAFSKSQLTFVLIMPTEGLILVDAGSYKKAEDVLSLLRKTMGSLPVVPAIPEIAVETTLTQWVKDGNLPQGFSLMEEAELKSLLDDGATIRCKKQELSSDEILSHIQANKVVTKLAINWQDRIRFVLAEDCSIKRLAYSDELKEQNDDIPHEDRAARLDADFSLLCGEMSVFLPDLFNALGGLPHPEA

May be involved in recombination. Belongs to the RdgC family.

Q94AE6

MELLSSSPAQLLRPNLSSRALLPPRTSIASSHPPPPRFLVMNSQSQHRPSISCASPPPGDNGFPAITTASPIESARIGEVKRETKETNVSVKINLDGHGVSDSSTGIPFLDHMLDQLASHGLFDVHVRATGDTHIDDHHTNEDVALAIGTALLKALGERKGINRFGDFTAPLDEALIHVSLDLSGRPYLGYNLEIPTQRVGTYDTQLVEHFFQSLVNTSGMTLHIRQLAGKNSHHIIEATFKAFARALRQATESDPRRGGTIPSSKGVLSRS

D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O Binds 2 manganese ions per subunit (PubMed:26095028, PubMed:27717128). Substrate binding triggers a switch in the coordination state of the Mn(2+) active site between six- and five-coordinate species; this switch is critical to prime the active site for catalysis, by facilitating the formation of a high-energy imidazolate intermediate (PubMed:26095028). Weakly inihibited by inorganic phosphate (Pi) (PubMed:26095028). Competitive inhibition by 2-hydroxy-3-(1,2,4-triazol-1-yl) (e.g. C348), a potential herbicide (PubMed:27717128). Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9. A number of isoforms are produced. According to EST sequences. Belongs to the imidazoleglycerol-phosphate dehydratase family.

Q48BG5

MSSGRIVQIIGAVIDVEFPRDSVPSIYNALEVQSAAGTTLEVQQQLGDGVVRTIAMGSTEGLKRGLEVTDSGAAISVPVGKATLGRIMDVLGNPIDEAGPIATEERWGIHRPAPSFAEQAGGNDLLETGIKVIDLVCPFTKGGKVGLFGGAGVGKTVNMMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMKDSNVLDKVALVYGQMNEPPGNRLRVALTGLTMAEKFRDEGNDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGTLQERITSTKNGSITSIQAVYVPADDLTDPSPATTFAHLDATVVLSRDIASLGIYPAVDPLDSTSRQLDPNVIGQEHYDTARGVQYVLQRYKELKDIIAILGMDELSETDKQLVNRARKIQRFLSQPFFVAEVFTGASGKYVSLKDTIAGFKGILNGDYDHLPEQAFYMVGGIEEAIEKAKKL

Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. 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.

B1I0X9

MSPNTPLVLVILDGWGCGDRVEGNAIAQADTPNWNRYRSVWPRTVLKCSGEDVGLPPGQMGNSEVGHLNLGAGRIVYQDLTRITRAVRDGSFFENAVLRTSIEASRRNGHALHLMGLLSDGGVHSHISHLFALLELAGRLDQRSVYVHAFLDGRDVPPANALEYVEALEDKLKTLGYGAVASVIGRYYAMDRDRRWERTARAYRAMVYGEGLRASSARQAVEKGYERGETDEFIQPTVIVRDGRPVAQVRDGDALVFFNFRPDRARQITRSFTDAEFGGFERGPAPAFPDFVCLTQYDRTIVAPVAFGPQELTNTLGNVLSRHGLRQLRLAETEKYAHVTFFFNGGVEQRDPGEDRLLIPSPKVPTYDLKPEMSAREVTDAFLANIEKYDIIIMNYANPDMVGHTGDLSAAIKAVETVDECLGRVVEAVLARGGTVLVSGDHGNAEHMCDAEGCPLTAHTCNPVPLLIIGEAVAGRSLRPGSLQDVAPTILDLLGLPKPPEMTGTSLLS

Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate Binds 2 manganese ions per subunit. Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. Monomer. Belongs to the BPG-independent phosphoglycerate mutase family.

Q1RG24

MQQLQNIIETAFERRAEITPANADTVTREAVNQVIALLDSGALRVAEKIDGQWVTHQWLKKAVLLSFRINDNQVIEGAESRYFDKVPMKFANYDEARFQKEGFRVVPPAAVRQGAFIARNTVLMPSYVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLSGGVGIGGVLEPLQANPTIIEDNCFIGARSEVVEGVIVEEGSVISMGVYIGQSTRIYDRETGEIHYGRVPAGSVVVSGNLPSKDGKYSLYCAVIVKKVDAKTRGKVGINELLRTID

(S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = (S)-2-succinylamino-6-oxoheptanedioate + CoA Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 1/3. Homotrimer. Belongs to the transferase hexapeptide repeat family.

Q601V6

MKINILTLFPRYFEVFCRESIIGKAIKHKKITINVVNFRDFSKNKHKKVDDYVYGGGPGLLLQIQPVVDALEKVGGLKIALSPQGQKFDQGVARKLAKEDEITILCGHYEGFDQRIIDNFIDFELSLGDFILTGGEIAAMAIIDAIIRLKPDIINPESLKNETFNDFLLDFPQYSRPANFRGLEVPNVLISGNHREIGEWRQEQRELITKKKRPDLWEKFLKIKNKK

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.

D3DL07

MNVTPLDELQWKSPEWIQVFGLRTENVLDYFAESPFFDKTSNNQVIKMQRQFSQLNDPNAAVNMTQNIMTLPDGKNGNLEEEFAYVDPARRQILFKYPMYMQLEEELMKLDGTEYVLSSVREPDFWVIRKQRRTNNSGVGSAKGPEIIPLQDYYIIGANIYQSPTIFKIVQSRLMSTSYHLNSTLESLYDLIEFQPSQGVHYKVPTDTSTTATAATNGNNAGGGSNKSSVRPTGGANMATVPSTTNVNMTVNTMGTGGQTIDNGTGRTGNGNMGITTEMLDKLMVTSIRSTPNYI

Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. The Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins. Component of the Mediator complex, which is composed of at least 21 subunits that form three structurally distinct submodules. The Mediator head module contains MED6, MED8, MED11, SRB4/MED17, SRB5/MED18, ROX3/MED19, SRB2/MED20 and SRB6/MED22, the middle module contains MED1, MED4, NUT1/MED5, MED7, CSE2/MED9, NUT2/MED10, SRB7/MED21 and SOH1/MED31, and the tail module contains MED2, PGD1/MED3, RGR1/MED14, GAL11/MED15 and SIN4/MED16. The head and the middle modules interact directly with RNA polymerase II, whereas the elongated tail module interacts with gene-specific regulatory proteins. MED6 interacts directly with SRB4/MED17 and SRB7/MED21. Present with 4824 molecules/cell in log phase SD medium. Belongs to the Mediator complex subunit 6 family.

D6W3G9

MMDGSITRKVTSTLSNQLATWKWKLQLSLLERKLATINNDYFLLQWELLFITNEVMKWKEMIAFLESQLFCTTQNFVAQETHDRETFQSLVDDYNKQLSENNLIISVLKSRPQLSSFPIYLSDEVCSHLKFVIAELNSLIIVFFISLVFLWVSIEV

Involved in chromosome segregation during meiosis. Involved in meiotic telomere clustering (bouquet formation) and telomere-led rapid prophase movements. Interacts with MPS3.

Q8ER61

MDSCGLIVEYNPFHNGHQYHINQARNVSNSTCIIAIMSGNFLQRGEPAIIDKFHRTKAALHGGADIVIELPYTFAVQNSDRFANGAIQTLNKFGVSSVCFGSESGSMDPFFQAYKTIKNSSEAFDNLLKDNLSDGLSFPDAATAVYETLGLTEGNLDLSKPNNILGFSYVKAIQEYAPTIKPLTIQRKNNDFHDESINGSIASATSIRKQILQSDSMDDDVHNAIPIETLHQLQSYKDKTAIWHDFEQYFPLLRYRVLTMSIKELQNIQGVVEGLEYRIQQTASDALSFVDWMHKIKTKRYTWTRIQRIFIHILTNTKKDENYVDESPSYIRILGMNKQGQQYLNYHKKNFDVPIITSIANTTHSMLAIEERATKAYYSIIPAKLQRKMFKQELQGPIII

Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of elongator tRNA(Met), using acetate and ATP as substrates. First activates an acetate ion to form acetyladenylate (Ac-AMP) and then transfers the acetyl group to tRNA to form ac(4)C34. acetate + ATP + cytidine(34) in elongator tRNA(Met) = AMP + diphosphate + N(4)-acetylcytidine(34) in elongator tRNA(Met) Belongs to the TmcAL family.

Q6ENG3

MNWRSEHIWIELLKGSRKRGNFFWACILFLGSLGFLAVGASSYLGKNIISVLPSQQILFFPQGVVMSFYGIAGLFISAYLWCTILWNVGSGYDRFDRKEGVVCIFRWGFPGIKRRVFLRFLMRDIQSIRIQVKEGLFPRRILYMEIRGQGAIPLTRTDEKFFTPREIEQKAAELAYFLRIPMEVF

Seems to be required for the assembly of the photosystem I complex. Belongs to the Ycf4 family.

Q046C5

MTKGILGRKVGMTQIFTKNGILVPVTVIEATPNVVLQVKTNESDGYEAVQVGYQDMREVLSNKPAKGHAAKAKTSPKRFIREIRDVELKDYEVGSEITVDSFSEGDVVDVTGTTRGHGTQGNIKRWGQSRGPETHGSRYHRIPGSMGSIINRVPKGKKLPGHMGGKKVTVQNLVIEKVVPEKNVLLVKGNVPGAKNSLIFVKSAAKAAK

One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. Part of the 50S ribosomal subunit. Forms a cluster with proteins L14 and L19. Belongs to the universal ribosomal protein uL3 family.

A1UJY9

MDPTIAAGALIGGGLIMAGGAIGAGIGDGIAGNALIAGIARQPEAQGRLFTPFFITVGLVEAAYFINLAFMALFVFATPVA

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 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 C chain family.

A4SV75

MKHIVQQIHFIGIGGTGMSGIAEVLLNLGYQVSGSDLVEGAATKRLKELGAVIHIGHDPKNVGTAEAVVISTAVAGNNPEVLAARAAKIPVIQRAVMLGELMRLKQGIAIAGTHGKTTTTSLVASVLAEGDLDPTFVIGGKLNSAGANARLGRGDFIVVEADESDASFLQLFPAMEVVTNIDADHMDTYQHDMARLKQAFVQFIQRMPFYGVAVLCIDDANVRDIIPFVSQPILRYGLSEDADIRASNVRADGTRMHFTVERRTVRRHGNKPGPLNVTLNLPGLHNVRNALAAIGIATELGVGDQAIIKALSEFSGVGRRFQRYGDIPLASGGKFTLIDDYGHHPVEMAATLAAARGAYPDRRLVLAFQPHRFTRTRDCFGEFVQVLKNFDALVLTEVYPAGEAKIPGADGKSLMKAALVDDKTSKALLNSAAVAFASSVAEMPEKLGQVLKDGDVLITMGAGSISALPHTLSEAKHV

Cell wall formation. ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine Cell wall biogenesis; peptidoglycan biosynthesis. Belongs to the MurCDEF family.

P32545

MYGIEYTTVLTFLISVILLNYILKSLTRIMDFIIYRFLFVIVILSPFLNAQNYGINLPITGSMDTPYINSTQEEMFLTSTLCLYYPTEADTEISDNSWKDTLSQLFLTKGWPTGSVYFKDYTDIASFSVDPQLYCDYNLVMMKYDAALQLDMSELADLILNEWLCNPMDITLYYYQQTDEANKWISMGSSCTIKVCPLNTQTLGIGCLTTDTNTFEEVATAEKLAITDVVDGVNHKLSVTTNTCTIRNCKKLGPRENVAVIQVGGSDILDITADPTTAPQTERMMRVNWKKWWQVFYTIVDYVNQIVQVMSKRSRSLNSAAFYYRV

Calcium-binding protein that interacts with rotavirus cell receptors once the initial attachment by VP4 has been achieved. Rotavirus attachment and entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors. Following entry into the host cell, low intracellular or intravesicular Ca(2+) concentration probably causes the calcium-stabilized VP7 trimers to dissociate from the virion. This step is probably necessary for the membrane-disrupting entry step and the release of VP4, which is locked onto the virion by VP7. Homotrimer; disulfide-linked. 2 Ca(2+) ions bound at each subunit interface in the trimer hold the trimer together. Interacts with the intermediate capsid protein VP6. Interacts with the outer capsid protein VP5*. The outer layer contains 780 copies of VP7, grouped as 260 trimers. Immature double-layered particles assembled in the cytoplasm bud across the membrane of the endoplasmic reticulum, acquiring during this process a transient lipid membrane that is modified with the ER resident viral glycoproteins NSP4 and VP7; these enveloped particles also contain VP4. As the particles move towards the interior of the ER cisternae, the transient lipid membrane and the non-structural protein NSP4 are lost, while the virus surface proteins VP4 and VP7 rearrange to form the outermost virus protein layer, yielding mature infectious triple-layered particles. N-glycosylated. The N-terminus is blocked possibly by pyroglutamic acid. Some rotavirus strains are neuraminidase-sensitive and require sialic acid to attach to the cell surface. Some rotavirus strains are integrin-dependent. Some rotavirus strains depend on ganglioside for their entry into the host cell. Hsp70 also seems to be involved in the entry of some strains. In group A rotaviruses, VP7 defines the G serotype. Produced by alternative initiation at Met-30 of isoform 1. Belongs to the rotavirus VP7 family.

Q9N5R9

MSGKRAVLNKDLFFQRAERLYEHWEKGADGLDSIKSLAFVYGETDNPYTKTSALFTWLFGHEIADTVLLLLKDHIYILGSNRKVEFFGSVTGDNQSSGKVPTVSTLLRDKTDKDAGNFEKLIDHIKSAGGDVGNFVKEKFSSEFVSSWNKALEEGGVNKNDVTLAFTHLFAVKDDKEMDLIRKSAQATTASWTAARARYVEIIDQEKRVRHSVLSNEFAAFMKDSKVQQALAKYEADTCYDPIVMSGGNYSFKWNHESSESHLHSQFGTIITSFGARLSEYCTNLTRTMLIFPSSELETAYEAILAAELAVIAALKPGAKLSDVYKIGIDTLTEKSPKLAETLNKKELGFATGIEFRESRLAISAKCDEVVKAGMVFIVYIGVDSIPNKNKGEKGKPAAIAISDTILVKEEGDNEILTEKAKSRLKSNVIKFKEEQENREAEKDNDQKKMLGRGQRSVVLTDQTRNKTTNEELRKERQKELGVQLNELAKARLSKQGGGTDEKKSKKSNVSYKTEERFPQDADVQKMLIFVDRKYDSVVVPIFGIPVPFHISMIKNCSQSVEGDFTYLRINFATPGSQVGKDSGQFPHPLAHYMKELTFRASNIKDHHSDSTAPSHNLSTAFRLIKEMQKRFKTEEAEEREKEGAVKQDKLILSQNKLNPKLKDLLIRPNIIQKRITGSLEAHTNGFRYTSLRGDRIDVLYNNIKHAFFQPCDNEMIILLHFHLKNPVLWGKKKYKDVQFYTEVGEITTDLGKYHHMQDRDDMQSEQQEREMRRRLNAAFNSFCEKVSRLTNDQFEFDSPFAGLGFFGVPYRSATTLKPTASCLVNLTEWPTFIVTLSEVELVHFERVSLQLKNFDMVFIFKDYKIKPQMVAQIPMSSIDKIKEWLHTCDIWYSEGIQSLNWAKVMKTITDDLEAFFEEGGWSFLNVESDNEEAMDDSDDSDAYDPEEEDASAGSGSESDEDESEGEETESDDDDEGSLDSDESEGKDWSDLEEEAANADKRREVEEPSRDRDRKRPHSSKSGPSHKRRK

Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II (By similarity). In embryos, promotes cell cycle progression and chromosomal segregation (PubMed:25446273, PubMed:30336114). Plays a role in the development of the anterior pharynx during embryonic development (PubMed:30336114). Component of the FACT complex, a stable heterodimer of spt-16 and hmg-3 or hmg-4. Expressed in the germline and somatic cells. Expressed throughout development (PubMed:30336114). First expressed in embryos at the 1-cell stage (PubMed:30336114). RNAi-mediated knockdown in embryos results in failed hatching in 83% of animals (PubMed:30336114). In addition, these embryos lack the anterior pharynx (PubMed:30336114). RNAi-mediated knockdown at the L4 larval stage results in failed development of the anterior pharynx (PubMed:30336114). RNAi-mediated knockdown at this stage results in defective cell cycle initiation, duration and completion in embryos, and abnormalities in chromosome segregation (PubMed:25446273, PubMed:30336114). Belongs to the peptidase M24 family. SPT16 subfamily. Although related to the peptidase M24 family, this protein lacks conserved active site residues suggesting that it may lack peptidase activity.

Q4WT84

MESSRGPPRVKNKAPAPIQISAEQLLREAVDRQEPALQAPTQRFADLEELHEYQGRKRKEFEDYVRRNRLNMNNWMRYASWELEQKEFRRARSIFERALDVNPTSVVLWIRYIESEMRNRNINHARNLLDRAVTILPRVDKFWYKYVYMEETLGNIQGTRQVFERWMSWEPDEGAWSAYIKLEKRYNEFERARAIFQRFTIVHPEPRNWIKWARFEEEYGTSDLVREVYGMAIETLGEDFMDEKLFIAYAKFEAKLKEYERARAIYKYALDRLPRSKAMALHKAYTTFEKQFGDREGVEDVILSKRRVQYEEQLKENPRNYDVWFDFARLEETSGDPDRVRDIYERAIAQIPPSQEKRHWRRYIYLWIFYAIWEEMEAKDVDRARQIYTECLKLIPHKKFTFAKIWLLKAQFDIRQMDLQAARKTLGQAIGMCPKDKLFRGYIDLERQLFEFVRCRTLYEKQIEWNPANSQSWIKYAELERGLDDSERARAIFELGIDQPMLDMPELVWKAYIDFEEYEGEYDRVRQLYERLLQKTDHVKVWINYARFEINVPEEEEEEEEEEEEERPVSDEAKRRARAVFERAHKVFKEKEMKEERVELLNAWRAFEHTHGSPEDIKKIEEQMPRRVKKRRKLDDDRYEEYMDYVFPADDQAAASLTKILQAAHRWKQTGGQVVP

Involved in pre-mRNA splicing and cell cycle progression. Required for the spliceosome assembly and initiation of the DNA replication (By similarity). Associated with the spliceosome. Belongs to the crooked-neck family.

Q45666

MTTEDHSYKDKKVISIGIVSELTGLSVRQIRYYEERKLIYPQRSSRGTRKYSFADVERLMDIANKREDGVQTAEILKDMRKKEQMLKNDPQVRKKMLEGQLNAHFRYKNR

Transcription regulator that actives the transcription of genes required for nitrogen assimilation such as nrgAB (ammonium transport), nasABCDEF (nitrate/nitrite assimilation), ureABC (urea degradation) and gabP (GABA transport), during nitrogen limitation (PubMed:8799114, PubMed:9603886, PubMed:10231480, PubMed:10864496, PubMed:11719184, PubMed:12823818). Also represses glnRA and gltAB in the absence of ammonium (PubMed:8799114, PubMed:9603886, PubMed:10231480, PubMed:10864496, PubMed:11719184, PubMed:12823818). On the contrary of the MerR members, which require longer DNA sites for high-affinity binding, TnrA requires a DNA sequence of 17 nucleotides as minimal binding site (PubMed:10231480, PubMed:25691471). Under conditions of nitrogen excess, the DNA-binding activity is inhibited by the formation of a stable complex with feedback-inhibited GlnA (PubMed:11719184, PubMed:25691471). The presence of glutamine and AMP increases the inhibitory activity of glutamine synthetase by more than 1000-fold (PubMed:11719184). Homodimer (PubMed:10864496, PubMed:25691471). Under conditions of nitrogen excess, TnrA forms a stable complex with feedback-inhibited GlnA. Interacts with GlnK-AmtB complex. Under poor nitrogen source such as nitrate, TnrA is associated with the cell membrane via the ammonium uptake proteins AmtB and its cognate regulator GlnK (PubMed:21435182). Without usable nitrogen source, TnrA is released from the membrane to the cytoplasm where it is degraded by proteolysis (PubMed:21435182). The presence of 4 mM ATP leads to concomitant solubilization of GlnK and TnrA (PubMed:17001076). GlnK and Amtb are required for the membrane association of TnrA (PubMed:17001076). Under conditions of nitrogen excess, repressed by GlnR. Under conditions of nitrogen-limited growth, it positively regulates its own expression. TnrA mutant is impaired in its ability to utilize allantoin, gamma-aminobutyrate, isoleucine, nitrate, urea and valine as nitrogen sources. During nitrogen-limited growth, transcription of the nrgAB, nasB, gabP, and ure genes is significantly reduced in the tnrA mutant. In contrast, the level of glnRA expression is 4-fold higher in the tnrA mutant than in wild-type cells during nitrogen restriction. The amino acid sequences of the N-terminal DNA binding domains of TnrA and GlnR are highly similar, and both proteins bind to DNA sequences with a common consensus sequence. In contrast, the C-terminal signal transduction domains of TnrA and GlnR have no homology.

A4IQD8

MRQMWNGWLLALQLFTVIPIRRSIEWNDIHVRWLVRSMPLAGAAIGALAAGTYALCSMFSFGTPLFLALFLLWLGIWLAGGLHADGWMDVSDAFFSYRDAKRRQQIMSDSRVGAFAVLSLACLLSFRWLFLYETIKAEIPPALFVAIPLLSRSGAAWLLSVGKLAKSTGMAASVREYISWRDAVWALVLAFLALSLLLVFGGVPVWTSAALAVAMALLALGAKPWVEKQFGGVTGDVLGALIEGGETLLWGVVWLLHSSAMG

Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate. adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+) adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate = adenosylcob(III)alamin 5'-phosphate + GMP + H(+) Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7. Belongs to the CobS family.

Q5E2Q1

MTKEQKLQLAEIRTMIPEMRRVECIHFVGIGGAGMSGIAEVLLNEGYHISGSDMAENTVTVRLAQKGAEIFFGHQASNVAKASVVVVSTAIDPSNPEIVAAKENRIPVIRRAEMLAELMRYRHGIAVAGTHGKTTTTALTTQIYSEAGLDPTFVNGGLVKNAGTNARLGSSRFLIAEADESDASFLHLQPMVSIVTNIEADHMDTYGGDFETLKQTFIDFLHNLPFYGQAVMCVDDPVVRELLPQVSRQVITYGFSDDADVRLINYRQVGQQSFFTVQRKDRTDLDIVLNIPGKHNALNATAAIAVATEEDVEDEAILTALLNFEGAGRRFDQLGEFETGNGSAMLVDDYGHHPTEVDVTIKAARAGWAEKRLVMIFQPHRYSRTRDLYDDFANVLDNVDVLIMLDVYSAGETPIAGADGRALCRTIRGRGKIDPVFVPTIEALPPVLANIIQEGDLILTQGAGDVGKLAKQLASMELNIETMKKLG

Cell wall formation. ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine Cell wall biogenesis; peptidoglycan biosynthesis. Belongs to the MurCDEF family.

B2K6M5

MKVSIFKTLYFQVLTAITIGVLLGHFYPEIGAQMKPLGDGFVKLIKMIIAPVIFCTVVTGIAGMESMKAVGRTGAIALLYFEIVSTLALLIGLVVVNVAQPGVGMNIDPATLDAKAVALYAEQASQQGIIPFLLDIIPGSVVGAFASGNILQVLLFAVLFGFALHRLGEKGQLIFNVIESFSRVIFGVINMIMRLAPLGAFGAMAFTIGKYGVGSLVQLGQLILCFYLTCILFVVLVLGTIAKFNGFNIFKFIRYIKEELLIVLGTSSSESVLPRMLDKMENAGCKKSVVGLVIPTGYSFNLDGTSIYLTMAAVFIAQATNTHMDIMHQVTLLVVLLLSSKGAAGVTGSGFIVLAATISAVGHLPLAGLALILGIDRFMSEARALTNLVGNGVATIVVAKWCKQLDNDQLQAVLSNKVLPNVKSSVSVS

Responsible for the transport of dicarboxylates such as succinate, fumarate, and malate from the periplasm across the membrane. Belongs to the dicarboxylate/amino acid:cation symporter (DAACS) (TC 2.A.23) family.

P0DTK4

MSYLQPPLFTTVSSDWVAPDLSTLPSWEGAKRVAIDCETRDPDLRKLGPGAGRRPNSYITGISFAIEDGPGGYLPIRHEGGGNLPLEGVLAYLRAQAKVFTGDLVGANLPYDLDFLAGDGIEFERVRYFRDIQIADPLICELHDSYSMQAIAERWGFHGKDEALLRAAAVDYGIDPKKDMWMLPAKFVGKYAEEDTRLPLNILRRQEREIDEQDLWGVYNLESKLLPILTGLRRRGVRIDCDRLDMIERWALEKETEALAQVRSITGHRIAVGDVWKPEVIAPALEHIGIKLNKTSQGKPNIDKELLGSIDHPVADLLERARKVNKLRTTFASSVRDHMVNGRLHGTFNQLRRQKDDESDGTAGAAYGRLSSEHPNLQQQPARDEFAMMWRAIYLPEEGQHWASNDYSQQEPRMAVHYACLAKDLIGHQAWLSAIEARDKYRNDPNTDNHQMMADMAGIKRKDAKEIYLGLSYGMGGAKMCRKLGLPTMMAVRGPRFQLFDVNSPEGQRLVAEGARRFEAAGPEGQALLDTFDHKVPFIKKLAKACEARAKAVGYITTLSGRRCRFPKDKDGNYDWTHKGLNRLIQGSSADQTKMAMVACAEAGLDIIIQVHDEIAFSVHDMKEAAEAAHIMRTCTPLELPSKVDVEIGQSWGHSMGWDGNPPS

DNA polymerase that replicates the viral genomic DNA (Probable). Also incorporates 5-hydroxymethyl-2'-deoxyuridine (5-hmdU) instead of dTMP into DNA during replication, as an early step in the pathway of thymidine hypermodifications of the viral genome (PubMed:34522950). As a final result of the pathway of hypermodification, 5-aminoethyl-2'-deoxyuridine (5-NedU) substitutes for about 30% of thymidines in the viral DNA (PubMed:34522950, PubMed:29555775). These modifications probably prevent degradation of viral genome by the host restriction-modification antiviral defense system (PubMed:34522950). a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1) Belongs to the DNA polymerase type-A family. DpoZ subfamily.

A5K4D8

MHNFAKIFRSNFIDINAANKFEIFLKTILRIYKTPARTHLLAHAADISAIYAVRQIYNYMKNDEEGRTVLKEKPLLIRQDIQFNELKKLPKNTLGYKYMKFLETYKLHAHDREVSHFFTDLNYSYILTRYRQIHDIGHVVYNLNISIESEAALKLIELVQTKLPITLLAILVAPFMTPIYRFQYIFKDSLPSNFLSPNFDFTYTDAYNYVDELSIKQYEYNLTDYFHVEKRNDRNFYTKMYQHYFDNINNSSAVRGSIIYGFENKSSNDIIYDQPNREYIFLKNLKKKYLLFQYKPRKNLLRELYPWAYMAGVSTTKPLHSIHIEKWLDKDIDLFRRTYNISPLPDHLNLMAGIN

Component of the coenzyme Q biosynthetic pathway. May play a role in organizing a multi-subunit COQ enzyme complex required for coenzyme Q biosynthesis. Required for steady-state levels of other COQ polypeptides. Cofactor biosynthesis; ubiquinone biosynthesis. Component of a multi-subunit COQ enzyme complex. This protein may be expected to contain an N-terminal transit peptide but none has been predicted. Belongs to the COQ4 family.

Q5UQ72

MIDDESVPWIEKYRPKKLEDITQSQNLLDLFKNSTKKGEMTHFLFYGPPGTGKTSAILAMGREIFKEHFQNRVIEFNASDDRGINAVREKITNEAKKYVAEIKLEDGTIIPSYKIIILDEADSMTDEAQDALRVIIEQYSTATRFCFICNYITKITDAIKSRCSSVYFKKLSDECMVEKLNDISLKESMELPKNILHTIIDVSNGDMRKAIMLLQNFKYTYNFKKNLTKKLKDMTLLELKTILFMTKKSSITSTISEEDVYEISASITLDKAKGIIDDTIDCNNIVEVSNLSKKIIAMGFPIDNILTQLNKCILESNKLDVNQISKIIIYSGDILLKMKECGNEYIQLLNYLAYVNRVSKHFD

Part of the RFC clamp loader complex which loads the PCNA sliding clamp onto DNA. Belongs to the activator 1 small subunits family. RfcS subfamily.

Q7M9I4

MNATIKEIALPNKTETFEFGAIAKQANGSVLYRCGKSVLLASVCYESDERVKEDFLPLTVQYIEKSYAAGKFPGGFIKRESKPGDFETLTSRIIDRSLRPLFPKGYAHPTQITVMVLSAQNDADLQTMALNAASAALFVSDIPLRKPVHGLRIGKINGALVVNPTTKEMSESTLDLFVSGVEEDLLMIEMRTLASDEINNTCFVGDCGMVAASASDILKIHQANEMKEEELLEALELAKTSIKKASACYVEAFTPLAKPDAILELKPDITSSEIYQYIKENHAIAIKEAITRMAKSERHSDLKRIAKEIASSERAQESEWSFEAVYETVGKYKREAVRALILEERRRADGRGLKEVRPIDIQTNILPNAHASALFTRGETQALVVATLGGDMDAQSYELLTEKGSSKERFMVHYNFPSFSVGEAGMVGAPGRRELGHGNLAKRALEPTIEEWGAQTIRLVSEILESNGSSSMATVCGGSLALKAAGINTTALVAGVAMGLIVEAEKHAILTDIMGLEDHDGDMDFKIAGTSTGITAMQMDIKLGGLSMEILKEALYQAKEGREHILGIMEKAQSEIIINDEILPSLQIFSINPGRIVDIIGQAGKTIKEIIERFEVAIDLNRDNGEVKVTGSNKQKVEAAKEHILSISNQEAPQRVRVADVYSAGEVFKGKVKKIVDFGAFIELPKGGDGLLHVSKIVQHRDQRIDEVIKEGEEIEVQILSINKNKVELGRATRPN

Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction. phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n) Belongs to the polyribonucleotide nucleotidyltransferase family.

B7N762

MIDDDGYRPNVGIVICNRQGQVMWARRFGQHSWQFPQGGINPGESAEQAMYRELFEEVGLSRKDVRILASTRNWLRYKLPKRLVRWDTKPVCIGQKQKWFLLQLVSGDAEINMQTSSTPEFDGWRWVSYWYPVRQVVSFKRDVYRRVMKEFASVVMSLQENTPKPQNASAYRRKRG

Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage. Belongs to the Nudix hydrolase family. RppH subfamily.

Q5VH43

MEKFQGYLEFDGARQQSFLYPLFFREYIYVLAYDHGLNRLNRNRSIFLENADYDKKYSSLIVKRLILRMYEQNRLIIPTKDLNKNLGHTNLFYYQMISVLFAVIVEIPFSLRLGSSVEGKKLKKSSNLQSIHSIFPFLEDKFSHFNYVLDVLIPYPIHLEILVQTLRYRVKDASSLHFFRFCLYEYCNWKNFDSKKKSILNPRFLLFLYNSHVCEYESIFLFLRKRSSHLRSTSYEVFFERILFYGKIQHFLKVFINNFPSILGLFKDPFLHYVRYHGKCILATKDTPLLMNKWKYYFVNLWQCYFFVWFKSQRVNINQLSKDNLKFLGYLSSLRLNPLVDRSQMLENSFLIDNVRIKLDSKIPIYSIIGSLAKNKFCNVLGHPISKATWTDSSDSDILNRFVRICRNISHYYSGSSKKKNLYRIKYILRLCCVKTLARKHKSTVRAFLKRLGSGLLEEFLTGEDQVLSLIFPRSDYASKRLYRVRVWYLDILYLNDLVNHE

Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns. Belongs to the intron maturase 2 family. MatK subfamily.

Q8CN23

MNQMNQTIIDAFHFRHATKEFDPTKKISDEDFNTILETGRLSPSSLGLEPWHFVVVQNKELREKLKAYSWGAQKQLDTASHFVLIFARKNVTAHTDYVQHLLRGVKKYEESTIPAFENKFDDFQESFHIADNERTLYDWASKQTYIALANMMTSAALLGIDSCPIEGFDLDKVTEILSDEGVLDTEQFGISVMVGFGYRAQEPKHGKVRQNEDDIISWIE

Belongs to the nitroreductase family.

Q7W6P3

MTDAAPNQPVNESQKLSKSFEPAEIETRWYDEWAKRGYFDAGRHVETGTDPQPYVIQFPPPNVTGTLHMGHAFNQTIMDGLVRYHRMLGDDTVFVPGTDHAGIATQIVVERQLDAQKVSRHDLGREKFVEKVWEWKEQSGSTITGQVRRLGASADWPREYFTMDARMSRGVAETFVRLYQQGLIYRGKRLVNWDPKLLTAVSDLEVQSEEVDGHMWHILYPFVDGPQTITDQDGNTVTLRGMTIATTRPETMLADGALCVHPDDPRYKHLLGKLVELPLCDRNIPIIADDFVDPDFGTGCVKITGAHDFNDYACALRHDIPLIVIFTLDAHINENGPKQFQGLERYEARQAVVAELQAQQYLVKVEPHKMMQPKGDRTGVVLEPMLTDQWFVAMSKPAPASTLNPGKSITEVALEAVADGRIAFYPENWATIYNQWLNNIQDWCISRQLWWGHQIPAWYSEDGQVFVARSEQEAQEQARAAGVAGPLTRDPDVLDTWFSSALVPFTTFGWPEDTPDLRRYLPSSVLVTGFDIIFFWVARMVMLTMHMTGSVPFKHVYVHGLIRDADGQKMSKSKGNTLDPVDLIDGIDLEGLVRKRTFGLMNPKQAGAIEKATRRQYPDGIPAFGTDALRFTMAAYATLGRNINFDLKRCEGYRNFCNKLWNATRFVLMNTEGHALDGDGGELSFADRWIVSQLQALEAEVERGFADYRFDNVANALYRYVWDEYCDWYLELAKVQIQQGTPAQQLGTRRTLIRVLEAVLRLAHPVIPFITEELWQKVALVAGKRTAGAVASVSVQPYPRANPQAVDAEAEAAVAELKSQVEAVRALRGEMNLSPAQRVPLVAEGPTDVLSRNAPYLAALAKLSEVEVVAALPDAGAPVQVVGDARLMLHVEIDVAAECARLDKEIARLEGEIAKANGKLGNASFVERAPAAVVEQEKARLAQFSETLKKVRGQRVKLGA

Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner. ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val) Monomer. ValRS has two distinct active sites: one for aminoacylation and one for editing. The misactivated threonine is translocated from the active site to the editing site. The C-terminal coiled-coil domain is crucial for aminoacylation activity. Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily.

Q54BU9

MESYGLGQLKNFEYLDHTADIMFHTWGKDLKEALEQMVLIMNNYMVELDSVELDDSATEQTISVNGHDMDSLLFALLDEFLFVFSTEFIIFKQVQIISFDRENFSIKAIGKGVELDKSKHTTGTEIKAITYSCMKIEENPDKSDIHVIVDI

Component of the tRNA-splicing ligase complex required to facilitate the enzymatic turnover of catalytic subunit RtcB. Belongs to the archease family.

Q5L789

MFSDKMILIAGPCVIEEEETTLEIAAKIQEIVAPYADHIHWIFKSSYDKANRSSIHSYRGPGLKEGLRILSKVKQTFGVEILTDVHSPEEARAAAEVCDILQIPAFLCRQTDLLVAAAETQAVINIKKGQFLSPWDMQGPVDKVLSTGNSKIILTERGCSFGYNNLVSDMRAIAVLSKMGFPVVFDGTHSVQLPGGLKTHSGGQTEFIPTLTRAALAAGAHGLFIETHTNPAIAKSDAASMLSLKAFEVLLPVWNQLYQCVRSFEMASV

D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Belongs to the KdsA family.

Q755P0

MAPAQAKRIKTLSVARPIVYGNTAKKMGDVRPAIAPSEHTHMWTIFVRGPQGEDISYFIKKVVFKLHETYPNPVRVVDAPPFELTETGWGEFEINVKVHFVDEANEKMLNFYHHLRLHPYTEEDGRRSDGDEVSSVFYDEIVFNEPNEAFFAKMIEQPGNLLPSNKTPDCVFSLQLEQEEIDRIQQGIGKVDEEIEQLKQKLEQDLAK

Component of the SWR1 complex which mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling. Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4 and H2A. The NuA4 complex is also involved in DNA repair. Yaf9 may also be required for viability in conditions in which the structural integrity of the spindle is compromised (By similarity). Component of the SWR1 chromatin-remodeling complex and of the NuA4 histone acetyltransferase complex. The coiled-coil domain is required for assembly into the NuA4 complex. Belongs to the YAF9 family.

O59418

MGKIHRPRKGSLAFSPRKRAKSIVPRIRSWPKETEVRMLGFAGYKAGMTHILMIDDEPGLTNGKEIFMPVTIIETPPLRVFGIRAYRQGYLGLETAGEVIVPDFELDNYTPSKKGKGRKFTFYQFLGRRIATLPKDYTQEEFEQKLGALEDMIKEGEIVEVRALVSTQPWVIKLKKKPEVMEYAIGGTSVEEKFNYIKEKLGKEIRVGEVLKEGELLDVIAVTKGKGTQGPVKRWGIKLRAHKDSKGRRKVGSIGPWHPARVMWTVPMAGQMGFHHRTELNKRLIAIGENGKLVIDGNEIEITPKGGFPHYGIVRGDFMMIAGSVPGAIKRIIRVRPAIRPPKKKPPVQRPQITYVSVESKQ

One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. Part of the 50S ribosomal subunit. Forms a cluster with proteins L14 and L24e. Belongs to the universal ribosomal protein uL3 family.

B9IU58

MTRKNTTTNPWAKFHGPNLGYVIEQYDLYVTGAGSVDPELQELFEIFGAPSFQDDVVTGDNTATHFSPQNTGNIEKILKVVQLVEQIRSFGHTLAHINPMEDAANGQSLLEKAMNELSDADLKAIPAKTVWQDAPEGIHTALDVIHRLKEVYTQTLAYEFSHIQDSEERAWLHQMVESNSLRQPLSNQKRTALLKRLTAVEGFEQFLHKTFVGQKRFSIEGVDMLVPVLDEIVLEGAKNGVEDVMIGMAHRGRLSVLAHVLEKPYSHMFAEFKHAKIEGAVANSGWTGDVKYHLGREQVVSNEEVSTRVTLANNPSHLEFVNPVVEGFARAAQENRKKSGLPEQDTSKSFVILVHGDAAFPGQGIVSETLNLSRLNAYQTGGTIHVIANNAVGFTTDSYDSRSTKYSSDLAKGFDIPIVHVNADDPEACLAAANLAIQYRMLFKKDFLIDLIGYRRYGHNEMDDPAVTQPQVYKKIKNHPTVRAIYADQLQAAGVLNADEIETITQFTQEQLKSDYAQVPPADTSDATIHVKVPDVVAKGIQSIDTGVELDSLRAINEGLLSWPEGFNVYPKVKKILERRKDALEENGKIEWALAESLAFASILQEGTPIRLTGQDSQRGTFAHRHIVLHDTDTNETYSPLHRLPNINASFSVHNSPLSEAAVVGYEYGYNVFAPETLVMWEAQYGDFSNTAQALFDQYVSAGRAKWGQKSGLVLLLPHGYEGQGPEHSSARPERFLQLAAENNWTVANLTSAAQYFHILRRQASILGTEAVRPLVLMTPKSLLRHPLTLSTASQLSEGRFQPALEQENLGMKPNKVKRLVLSTGKMAIDLAAEIESGKHEYNLDEIHIVRIEQLYPFPAEKVQSIIKRFKNLEEIIWVQEEPRNMGAWHYMAPILFELAGDKVKTGYIGRPDRSSPSGGDPFAHKAEQELIVSHALDVKYNFRQDKLEIEVFSN

E1 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the decarboxylation of 2-oxoglutarate, the first step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2). (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase] + 2-oxoglutarate + H(+) = (R)-N(6)-(S(8)-succinyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase] + CO2 Homodimer. Part of the 2-oxoglutarate dehydrogenase (OGDH) complex composed of E1 (2-oxoglutarate dehydrogenase), E2 (dihydrolipoamide succinyltransferase) and E3 (dihydrolipoamide dehydrogenase); the complex contains multiple copies of the three enzymatic components (E1, E2 and E3). Belongs to the alpha-ketoglutarate dehydrogenase family.

A1SMA5

MKRNGFVPSNSVGRRGIPSNSTSSAIASAGGAVVWTGAGAGRVRARPEQVSVGPGTMSCVTDPREEHRLIAEEIEEARWRYYVLDSPTIDDADFDRRMRRLEALEEEFPELRTPDSPTQTVGGAVSTDFTSHPHLRRMESLDNAFSVEEVEAWYARLRRDGVEDPALLCELKVDGLAINLLYEEGRLVRALTRGDGTTGEDVTSNVKTITSVPHRLTGTDEFPVPALVEVRGEVFLPVEAFERLNESLLEAGKAPFANPRNSAAGSLRQKDPRITASRALGMVCHGIGERRGFEPQAQSHAYDALAAWGLPTSDQVRVVSTLKGVEGYIENAGARRHTIVPYEIDGVVVKVDDVALQRRLGSTSRAPRWAIAFKYPPEEVNAKLLEIRVNVGRTGRVTPYAVMEPTKVAGSTVENATLHNFYEVERKDVRPGGPGDPGDTVILRKAGDVIPEILGPVLALRPEGLQPWVPPTTCPSCGTPLVEQKEGDKDRRCPNHEKCPGQLRERVFFVASRNAFDIEGLGYEAAVALLDAEVIANEGDVFDLDAAALLRAPLFTRAPKKDEDGPQLSANGQRLLDNLDKAKQVPLWRVLVALSIRHVGPKAGRALATEFGSMAAIRAATEEQLAAAEGVGPTIAEAVIEWFKEPWHVEIVDKWERAGVTMADERDESTPRTLAGLTVVVTGSLVDFSRDSAKEAILSRGGKAAGSVSKKTDYVVVGENAGSKADKAEQLGVPVLDEAGFKTLLDGGPAAL

DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA. NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-nicotinamide D-nucleotide. Belongs to the NAD-dependent DNA ligase family. LigA subfamily.

P84934

MSFLKKSLFLVLFLGLVSFSICEEEKRETEEEENEDEIEEQSEEKKRFEPVPPGFTPFRQT

May produce in vitro relaxation of rat arterial smooth muscle and constriction of intestinal smooth muscle (By similarity). May target bradykinin receptors (BDKRB). Expressed by the skin glands. Belongs to the frog skin active peptide (FSAP) family. Bradykinin-related peptide subfamily.

A3NT94

MTDKLIIFDTTLRDGEQSPGASMTKEEKIRIAKQLERMKVDVIEAGFAASSNGDFDAIQTIASQVKDSTICSLARANDKDIQRAADALKPANSFRIHTFIATSPLHMEKKLRMTPDQVFEQARLAVRFARKFTDNIEFSPEDGSRSDMDFLCRVLEAVIAEGATTINIADTVGYGVPELYGNLVKTLRERIPNSDKAIFSVHCHNDLGMAVANSLAGVKIGGARQVECTINGLGERAGNTSLEEIVMAVKTRKDYFGLDLGIDTTQIVPASKLVSQITGFVVQPNKAVVGANAFAHASGIHQDGVLKARDTYEIMRAEDVGWTANKIVLGKLSGRNAFKQRLQELGVSLDSEAELNAAFARFKDLADRKAEIFDEDIIAIVTEEESALAQEHEHYKFVSLAQRSETGERPQAKVVFAVDGDEVAGEASGNGPVDATFNAIETEVGSGAELLLYSVNAITTGTQAQGEVTVRLSKSGRIVNGVGTDPDIVAASAKAYIAALNKLYSNADKLNPQRA

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). 3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+) Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 1/4. Homotetramer. Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 1 subfamily.

A9MKC8

MQEQYRPEEIESKVQLHWDEKRTFEVTEDESKEKYYCLSMLPYPSGRLHMGHVRNYTIGDVIARYQRMLGKNVLQPIGWDAFGLPAEGAAVKNNTAPAPWTYDNIAYMKNQLKMLGFGYDWSRELATCTPEYYRWEQKFFTELYKKGLVYKKTSAVNWCPNDQTVLANEQVIDGCCWRCDSKVERKEIPQWFIKITAYADELLSDLDKLDHWPDTVKTMQRNWIGRSEGVEITFDVKGYDNTLTVYTTRPDTFMGATYLAVAAGHPLAQKAAANNPELAVFIDECRNTKVAEAEMATMEKKGVDTGFKAIHPLTGEEIPVWAANFVLMEYGTGAVMAVPGHDQRDYEFATKYGLTIKPVILAADGSAPDLSTQALTEKGVLFNSGEFDGLAFEAAFNAIADKLAAKGVGERKVNYRLRDWGVSRQRYWGAPIPMVTLEDGTVIPTPEDQLPVILPEDVVMDGITSPIKADPAWAKTTVNGTPAMRETDTFDTFMESSWYYARYTCPQYQEGMLDSKAANYWLPVDIYIGGIEHAIMHLLYFRFFHKLMRDAGMVTSDEPAKQLLCQGMVLADAFYYVGENGERNWVSPVDAIVERDEKGRIVKAKDAAGHELVYTGMSKMSKSKNNGIDPQVMVERYGADTVRLFMMFASPADMTLEWQESGVEGANRFIKRVWKLVYEHTAKGSVAALNVDTLNDDQKALRRDVHKTIAKVTDDIGRRQTFNTAIAAIMELMNKLAKAPQDSEQDRALMQEALLAVVRMLNPFTPHVCFTLWQALEGEGDIDNAPWPVADDKAMVEESTLIVVQVNGKVRGKITVPVNATEEQVRERAGQEHLVAKYLDGVTVRKVIYVPGKLLNLVVG

ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu) Belongs to the class-I aminoacyl-tRNA synthetase family.

A8A674

MSEQNNTEMTFQIQRIYTKDISFEAPNAPHVFQKDWQPEVKLDLDTASSQLADDVYEVVLRVTVTASLGEETAFLCEVQQGGIFSIAGIEGTQMAHCLGAYCPNILFPYARECITSMVSRGTFPQLNLAPVNFDALFMNYLQQQAGEGTEEHQDA

One of the proteins required for the normal export of preproteins out of the cell cytoplasm. It is a molecular chaperone that binds to a subset of precursor proteins, maintaining them in a translocation-competent state. It also specifically binds to its receptor SecA. Homotetramer, a dimer of dimers. One homotetramer interacts with 1 SecA dimer. Belongs to the SecB family.

Q5NHW4

MPRSLKKGPFVDHHLLKKVFEAQESNSKKPIKTWSRRSMIVPDMIGLTIAVHNGQQHVPVLMTEEMVGHKLGEFVVTRNYRGHAADKKAKKK

Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA. Belongs to the universal ribosomal protein uS19 family.

B0UW20

MSVIPMVVEQTSRGERSYDIYSRLLKERVIFLTGEVEDRMANLIVAQLLFLEAEDPAKDINIYINSPGGSVTAGMAIYDTMQFIKPNVRTLCIGQACSMGAFLLAGGTAGKRAALPHARVMIHQPLGGFRGQASDIQIHAQEILKIKQTLNERLAFHTGQSIEQIEQDTDRDNFMSAEQAKLYGLVDDVLIKR

Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs). Fourteen ClpP subunits assemble into 2 heptameric rings which stack back to back to give a disk-like structure with a central cavity, resembling the structure of eukaryotic proteasomes. Belongs to the peptidase S14 family.

F2EL82

MGSFANGQNGSELGIQTPATGSNAALEPPTTSAAAPRCPRLGMAMVAARAAALVMALLSVSLMVSAKQRGTLAIFGIEIPLYAKWSLSDSLQSLVGISAAAAAYSLAQLLSIAHTALKKAPVVPSRRYAWMLLAGDQVFAYAMLSAGSAAAAVANLNRTGVRHTALPNFCKPLPRFCDLSAASIACAFLGCAFLAASAVIDVIWLSRL

Homodimer and heterodimers. Belongs to the Casparian strip membrane proteins (CASP) family.

B2IIK5

MSGFNDSPVPESAEKADGLLSQERGTQDPLVNTRKLFVKSYGCQMNVYDAERMADLLAPEGYAETSAPEDADLVILNTCHIREHAAEKVFSELGKLRLLKAEQQAAGRPVKIVVAGCVAQAEGEEILRRQKAVDLVVGPQSYHRLPDLLRRVAHTPGLVDTEFPAEDKFDHLVAPQPEKIAERGVGAFVTVQEGCDKFCSFCVVPYTRGAETSRPVEAILAEVETLIASGVREVTLIGQNVNAYHGFDAMTGAPASLASLMARVAAMPGLLRIRYTTSHPNDMGEDLIAAHRDIPALMPFLHLPVQSGSDKILAAMNRRHKAGDYLELIASIRAARPDIALSSDFIVGFPGETEADFEATLALIEQVGFASAFSFKYSQRPGTPGADRPDQIDEDVKAQRLARLQALLEEQRQAFNKAMIGRVLPVLFEKPGRHPGQIAGKTPYLQALYAEGDKALIGTVQPVEILEAGPNSFHGRLLARETGQESAQGQESAQGMERMEQNARAWEVPV

Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine. [sulfur carrier]-SH + AH2 + N(6)-dimethylallyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine = 2-methylsulfanyl-N(6)-dimethylallyladenosine(37) in tRNA + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Monomer. Belongs to the methylthiotransferase family. MiaB subfamily.

Q8D8J6

MIDQKVIVALDYDNQADALAFVDRIDPASCRLKVGKEMFTLFGPDFVRELHKRGFSVFLDLKFHDIPNTCSKAVRAAAELGVWMVNVHASGGERMMTASREILEPYGKDRPLLIGVTVLTSMEQSDLAGIGLDVAPQEHVIRLATLTKNSGLDGVVCSAQESSLLKNELGKEFKLVTPGIRPLGSEQGDQRRIMTPLEAVQAGSDYLVIGRPITQAVDPAAVLQAINTSLTK

Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP). H(+) + orotidine 5'-phosphate = CO2 + UMP Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2. Homodimer. Belongs to the OMP decarboxylase family. Type 1 subfamily.

Q2W019

MINPVYVAIDTTEAARAIALAERLKGQVGGFKLGLEYFTANGPAGMEAVSGLGMPLFVDLKLHDIPNTVAAAMKGVVRLGAAITTIHASGGAAMIRAAVDAANDEAAKLGIAPPAVVAVTVLTSLDQAGAEQVGFERPVLDQVKRLATLAQDSGAAGIVCSPLEVEAVRALCGPDFKLVIPGIRPAWSEAGDQKRFLTPAEARAKGADVLVIGRPITAAADPAEAAGRIKAELGL

Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP). H(+) + orotidine 5'-phosphate = CO2 + UMP Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2. Homodimer. Belongs to the OMP decarboxylase family. Type 1 subfamily.

B4SBZ2

MGLLDAGITQHNVLITSVDNVLNWARLSSLWPMGFGLACCAIEMMATNASNYDLERFGIFPRSSPRQSDLMIVAGTVTMKMAERVIRLYEQMPEPRYVLSMGSCSNCGGPYWEHGYHVLKGVDRVIPVDVFVPGCPPRPESLIGGLMKVQELIRMEQIGLSRADALKKLAEKSVDPQFVIERERKAAGA

NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+) Binds 1 [4Fe-4S] cluster. 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 20 kDa subunit family.

Q58NQ4

MMQESGTETKSNGSAIQNGASGGNHLLECSLREVRSNGETPSVEIGAADLTHLQQQQALQVARQLLLQQQQQQQQQQQQQQQQQVSGLKSPKRNDKQPALQVPVSVAMMTPQVITPQQMQQILQQQVLTPQQLQVLLQQQQALMLQQQQLQEFYKKQQEQLQLQLLQQQHAGKQPKEPQQQQVATQQLAFQQQLLQMQQLQQQHLLTLQRQGLLTIQPGQPTLPLQPLAQGMIPTELQQLWKEVTSSHTAEEAASNNHSSLDLSTTCVSSSAPSKTSLIINPHASTNGQLSVHTPKRESLSHEEHSHSHPLYGHGVCKWPGCEAVCEDFQSFLKHLNSEHALDDRSTAQCRVQMQVVQQLELQLAKDKERLQAMMTHLHVKSTEPKATPQPLNLVSSVTLSKTASEASPQSLPHTPTTPTAPITPVTQGPSVITTTSMHNVGPIRRRYSDKYNVPISSADIAQNQEFYKNAEVRPPFTYASLIRQAILESPEKQLTLNEIYNWFTRMFAYFRRNAATWKNAVRHNLSLHKCFVRVENVKGAVWTVDEQEFQKRRPQKISGNPSLIKNIQTSHTYCTPLNAALQASMAENSIPLYTTASMGNPTLGNLANVMREELNGAMEHTNSNGSDSSPGRSPMQAMHPVHVKEEPLDPDENEGPLSLVTTANHSPDFDHDRDYEDEPVNEDIE

Transcriptional repressor. The leucine-zipper is required for dimerization and transcriptional repression.

Q9TYW1

MRVLFAVFSLIMACQAYDAVLFSNSREIGGTPAAKLVESATAEEPVVFIVNPDFTLGQFSVKANAYTSEPSADYLAKSVKNSNFHESQYFSHQIEATQAQWLSSADQYSAGSPIYIIYGEEWTSMEQLAEQLISKIDNSVGIITSTDAVAHEKSSRVKRVATDEFNSDSENSAAAEANGGFPFPLVIPPYNQTFYSVKPTNGHSCLFYLEGLTVVVEQKKEKVLYYANAYIPGSNFTWAYSETDVTCPNGTIGDFIFKIHLTLENDITGMQGTSKKAFTMKKGDKIDFDLTFTGDLFGYWALNKASASNLAISGYDPYKSASVDGSKVVNGSATQYTKLNSVAGWSLACGQSQAVFFPTNEQSVRIGVALMNTQIQLFNYQNPEKWVESAHFTLQTEDCTGTFSSGSWMGIVSALVLIAGLMFGYVMLQSVQTMDRFDDPKQRQIVINVRE

Accessory subunit of the proton-transporting vacuolar (V)-ATPase protein pump, which is required for luminal acidification of secretory vesicles (By similarity). In the germline, required for the trafficking of the receptor RME-2 to the oocyte cell membrane where it regulates the uptake of yolk proteins (PubMed:22768351). Also, plays an essential role in osmoregulation in the embryo, probably by regulating the proper formation of the eggshell (PubMed:22768351). Accessory component of the multisubunit proton-transporting vacuolar (V)-ATPase protein pump. Expressed in pharynx, hypodermis, intestine, vulval hypodermis and the H-shape excretory cell. Expressed in larvae and adults. RNAi-mediated knockdown at the L1 larval stage causes arrest followed by death at the L3/L4 larval stages (PubMed:22768351). RNAi-mediated knockdown at the L4 larval stage does not affect development into adults (PubMed:22768351). However, only 26% of the progeny hatched into larvae which die at the L3 larval stage. RNAi-mediated knockdown at the L4 larval stage or in the germline causes egg compression in their uterus (PubMed:22768351). Fewer oocytes are produced in the oviduct and are endomitotic (PubMed:22768351). This results in a reduced rate of ovulation over time (PubMed:22768351). Oocytes fail to endocytose vitellogenin due to a failure to traffic receptor rme-2 to the cell membrane (PubMed:22768351). Also, embryos display osmotic sensitivity and defect in osmoregulation and cytokinesis probably due to an abnormal eggshell (PubMed:22768351). Belongs to the vacuolar ATPase subunit S1 family.

Q2P334

MEQGVIERARELRRRIENADHRYYDLADPEITDAQYDQLFRELQELEQKYPELVTADSPSMRVGGAVRKSFVKVRHSIPMLSLANAFDEVEVKNFVDRIFRRMGSSNPLEFSVEPKFDGLAISLRYELGKFVQGVTRGDGDVGEDVSENIRTIRSVPLKLKGNNVPAILEVRGEVYMPRDGFSEFNKRAMARGEKLLANPRNGAAGSLRQLDSRISAQRPLSFFAYGVGLIQVEQDLFEEIPQSIASTHSAMLAQLRAWGFPVSSLVEVVQGSDGLLAYYQRIGEARDGLPFDIDGVVYKLDDLAGQREMGFVSRAPRWALAHKFPAQEQSTTVEAIEIQIGRTGAATPVARLKPVHVAGVIVTNATLHNADQIARLDVRVGDTVIVRRAGDVIPEVAAVVADQRPPATQSWQMPTQCPVCGSEIVREEGQAVWRCSGELTCPAQRKEAFRHFVSRRAMDVDGLGEKFIEVLVDSGVVQGVADLYLLTVDQLLQLRMISTAESPHAFLREAREHLASGAYAQLEATLVGIGVDLAGEREVPQTWQADLLRAGLPTFDWNRKKIATKWAENLIEAIETSRDTTLERFLFALGIEHVGESTAKALSAWFGDLDLIRHLPWPLFKRVPDIGGEVARSLGHFFDQPGNQKAIDHLLARKVRIGDTHPPSPKLRGELRLANLLEDLEIPKVTPIRAAQIATAFGSIDALRNGGPEPLVEAGVPQSVAESLATWLLVPANDTLAVNAQKKLSALLAMMPEAGEEKTGPLDGQTVVITGTLAALTRDAAKQRLEALGAKVAGSVSKKTAFLVAGEEAGSKLDKAQSLGVEIWDEARLLAFLGEHGQQR

DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA. NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-nicotinamide D-nucleotide. Belongs to the NAD-dependent DNA ligase family. LigA subfamily.

Q9KVZ7

MALDLAEYDRLARLGVAQFWDGRSSALENDEERSQGGERSGVLGGRNMDGFLAMIEGIVRKNGLPDAEVCIKGRPNLTLPGYYRPTKLWDVLVFDGKKLVAAVELKSHVGPSFGNNFNNRAEEAIGTAHDLATAIREGILGDQLPPFTGWLILVEDCEKSKRAVRDSSPHFPVFPDFKGASYLTRYEVLCRKLILKGFTPRPQSLLRPALRVLGATIASFRKPRVCAHLRHGWPAMYPVGQSRIRVNF

A P subtype restriction enzyme that recognizes the double-stranded sequence 5'-CTCGAG-3' and cleaves after C-1. Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates. Belongs to the XhoI type II restriction endonuclease family.

Q31SV2

MSTLRLLISDSYDPWFNLAVEECIFRQMPATQRVLFLWRNADTVVIGRAQNPWKECNTRRMEEDNVRLARRSSGGGAVFHDLGNTCFTFMAGKPEYDKTISTSIVLNALNALGVSAEASGRNDLVVKTAEGDRKVSGSAYRETKDRGFHHGTLLLNADLSRLANYLNPDKKKLAAKGITSVRSRVTNLTELLPGITHEQVCEAITKAFFAHYGERVEAEIISPDKTPDLPNFAEIFARQSSWEWNFGQAPAFSHLLDERFSWGGVELHFDVEKGHITRAQVFTDSLNPAPLEALAGRLQGCLYRADMLQQECEALLVDFPDQEKELRELSTWIAGAVR

Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes. (R)-lipoate + ATP + L-lysyl-[lipoyl-carrier protein] = (R)-N(6)-lipoyl-L-lysyl-[lipoyl-carrier protein] + AMP + diphosphate + H(+) Protein modification; protein lipoylation via exogenous pathway; protein N(6)-(lipoyl)lysine from lipoate: step 1/2. Protein modification; protein lipoylation via exogenous pathway; protein N(6)-(lipoyl)lysine from lipoate: step 2/2. Monomer. In the transfer reaction, the free carboxyl group of lipoic acid is attached via an amide linkage to the epsilon-amino group of a specific lysine residue of lipoyl domains of lipoate-dependent enzymes. Belongs to the LplA family.

Q8LBU0

MAFLLNNASISSHLRSSSSQKTGDALSISRRGFHIEPGTREKALLAEDSALKRFKSHKKSVHKLKRIGDVLTVVVVAGCCYEIYVKAVMKKEALAAGKSS

Carbohydrate metabolism; tricarboxylic acid cycle. Component of complex II composed of eight subunits in plants: four classical SDH subunits SDH1, SDH2, SDH3 and SDH4 (a flavoprotein (FP), an iron-sulfur protein (IP), and a cytochrome b composed of a large and a small subunit.), as well as four subunits unknown in mitochondria from bacteria and heterotrophic eukaryotes. May be due to a competing acceptor splice site.

Q5PEH7

MTTPAPLTGLLPLNPEQLARLQAATTDLTPEQLAWVSGYFWGVLNPRSGAVAVTPAPEGKMPGVTLISASQTGNARRVAEALRDDLLAANLNVTLVNAGDYKFKQIASEKLLVIVTSTQGEGEPPEEAVALHKFLFSKKALKLENTAFAVFSLGDTSYEFFCQSGKDFDSKLAELGGERLLDRVDADVEYQAAASEWRARVVDVLKSRAPVAAPSQSVATGAVNDIHTSPYTKDAPLTATLSVNQKITGRNSEKDVRHIEIDLGDSGLRYQPGDALGVWYQNDPALVKELVELLWLKGDEPVTVDGKTLPLAEALEWHFELTVNTANIVENYATLTRSESLLPLVGDKAQLQHYAATTPIVDMVRFSPAQLDAQALIGLLRPLTPRLYSIASAQAEVESEVHITVGVVRYDIEGRARAGGASSFLAGRVEEEGEVRVFIEHNDNFRLPANPQTPVIMIGPGTGIAPFRAFMQQRAADGAEGKNWLFFGNPHFTEDFLYQVEWQRYVKEGVLNRIDLAWSRDQKEKIYVQDKLREQGAELWRWINDGAHIYVCGDARCMAVDVEKALLEVIAEFGAMDIESADEYLSELRVERRYQRDVY

Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component. 3 H2O + hydrogen sulfide + 3 NADP(+) = 4 H(+) + 3 NADPH + sulfite Binds 1 FAD per subunit. Binds 1 FMN per subunit. Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen sulfide from sulfite (NADPH route): step 1/1. Alpha(8)-beta(8). The alpha component is a flavoprotein, the beta component is a hemoprotein. Belongs to the NADPH-dependent sulphite reductase flavoprotein subunit CysJ family. In the N-terminal section; belongs to the flavodoxin family. In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.

P17974

MRRCMPLVAASVAALMLAGCGGGDGDPSLSTASVSATDTTTLKPAATSTTSSVWLTLAKDSAAFTVSGTRTVRYGAGSAWVEKSVSGSGRCTSTFFGKDPAAGVAKVCQLLQGTGTLLWRGVSLAGAEFGEGSLPGTYGSNYIYPSADSVTYYKNKGMNLVRLPFRWERLQPTLNQVFDANELSRLTGFVNAVTATGQTVLLDPHNYARYYGNVIGSSAVPNSAYADFWRRLATQFKSNPRVILGLMNEPNSMPTEQWLSGANAELAAIRSANASNVVFVPGNAWTGAHSWNQNWYGTPNGTVMKGINDPGHNLVFEVHQYLDGDSSGQSANCVSATIGAQRLQDFTTWLRSNGYRGFLGEFGAASNDTCNQAVSNMLTFVKNNADVWTGWAWWAGGPWWGGYMYSIEPSNGVDKPQMSVLAPYLK

Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans. Belongs to the glycosyl hydrolase 5 (cellulase A) family.

Q7MGS7

MTELKNDRYLRALLKEPVDCTPVWMMRQAGRYLPEYKATRAQAGDFMSLCKNAELASEVTLQPLRRFPLDAAILFSDILTIPDAMGLGLRFSTGEGPIFDNPITCKADVEKIGVPDPEGELQYVMNAVRQIRKDLNGDVPLIGFSGSPWTLATYMVEGGSSKAFTKIKKMMYAEPQTLHLLLDKLADSVIEYLNAQIKAGAQSVMVFDTWGGVLTPRDYNLFSLQYMHKIVDGLIRENDGRRVPVTLFTKNGGMWLEQIAATGCDAVGLDWTINIADAKARVGDKVALQGNMDPSMLYASHDRIREEVASILEGFGHGGTGHVFNLGHGIHLDVPPENAGVFVEAVHELSKPYHQ

Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III. 4 H(+) + uroporphyrinogen III = 4 CO2 + coproporphyrinogen III Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 4/4. Homodimer. Belongs to the uroporphyrinogen decarboxylase family.

Q0W3X9

MQLLLIHSDFIEYEVKKSTPVAEKIEDAVRSGRMEEALTAFAAVEKPDESNPQYVIEKGLEAIIKVAEQVKTTRVMLYPYAHLSANLSSPKMAVEVLKGLEAALKGKGFEVARAPFGWYKAFTIKCKGHPLSELSRTIRPEGVEAVSVTPAVAAEKPEVVSEAVKAEEKLKSYFYILDVDGQLKDPKTFDYKGHDKLKAFVDYEMAKKRAVDREPPHVELMRRLELADYEPGSDPGNMRWYPKGRAMKNMLEQFVLSEAAKKGAMEVETPIMYDMEHPTLKKYLDRFPARQYTVIADKKNLFLRFAACFGQFLMNHDMTISYRNLPLKMIELTRYSFRKEQRGELVGLRRLRAFTMPDMHTLCTDMDGAIKEFGDQYEMCINTLDTIGIDIKTDYEVAIRFTKDFYNNNTPFIQSLVKRAGKPVIVEMWEERFFYFVLKFEFNYIDSLNKASALSTVQIDVENAERYDINYVDQNGNRQRPIILHCSPSGAIERCIYGLLEKEAMESEKGAVPMLPVWLSPTQVRIVTISEKHVPFAEALADRMCNVRVDIDDREETVGKKIRDAGKEWIPYVVTIGDAEMNGDKIPVVVRAESQQNKPAKVEMTVEELVERIHKETACLPYRPLPVVRSLAKRPKFVGSI

Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr). ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + H(+) + L-threonyl-tRNA(Thr) Binds 1 zinc ion per subunit. Homodimer. The N-terminal domain is an archaea-specific tRNA-editing domain that hydrolyzes incorrectly charged L-seryl-tRNA(Thr). Catalysis of tRNA editing is performed by the charged tRNA itself. Belongs to the class-II aminoacyl-tRNA synthetase family.

P38190

MLHVYAYIQYIPIAAYSSSSSIRVIFLLFLTLSFLMWLSISFSSCSCPFLFPSSSSSLSSSYVSSSSSFSSDICSSSMSSSRVKSSSSSSSSLAFSPTYNSVSTSFSTSSCSKLDIPVSFLLAA

Almost completely overlaps SAS3. Product of a dubious gene prediction unlikely to encode a functional protein. Because of that it is not part of the S.cerevisiae S288c complete/reference proteome set.

B5FJG6

MTWFIDRRLNGKNKSTVNRQRFLRRYKAQIKQSISEAINKRSVTDVDSGESVSIPTDDISEPMFHQGRGGLRHRVHPGNDHFIQNDRIERPQGGGGGGSGSGQGQASQDGEGQDEFVFQISKDEYLDLLFEDLALPNLKKNQHRQLNEYKTHRAGFTSNGVPANISVVRSLQNSLARRTAMTAGKRRELHALETELETISHSEPAQLLEEERLRREIAELRAKIERVPFIDTFDLRYKNYEKRPEPSSQAVMFCLMDVSGSMDQATKDMAKRFYILLYLFLSRTYKNVEVVYIRHHTQAKEVDEHEFFYSQETGGTIVSSALKLMDEVVKERYDPGQWNIYAAQASDGDNWADDSPLCHEILAKKLLPVVRYYSYIEITRRAHQTLWREYEHLQATFDNFAMQHIRDQEDIYPVFRELFQKQSANQSV

Belongs to the UPF0229 family.

B2IHW6

MGLIATPQPVVGTPPAQDNYFLSINDQLADKGFLVTSTDELINWARTGSLMWMTFGLACCAVEMMQMSMPRYDCERFGFAPRGSPRQSDVMIVAGTLTNKMAPALRKVYDQMPEPRYVISMGSCANGGGYYHYSYSVVRGCDRIVPVDIYVPGCPPSAEALLYGVLLLQKKIRRTGTIER

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(+) Binds 1 [4Fe-4S] cluster. 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 20 kDa subunit family.

Q640Q7

MADSGPAGGAALAAPAPGPGSGSTGPRVYFQSPPGAAGEGPGGADDDGPVRRQGKVTVKYDRKELRKRLNLEEWILEQLTRLYDCQEEEIPELEIDVDELLDMESDDTRAARVKELLVDCYKPTEAFISGLLDKIRGMQKLSTPQKK

Inhibitor of PPP1CA. Has over 50-fold higher inhibitory activity when phosphorylated. Ubiquitous. Highly expressed in testis. Detected at low levels in the other tissues tested. Highly expressed in cardiac muscle, bladder and aorta (at protein level). Phosphorylated primarily on Thr-57 by PKC (in vitro). An unknown Ser is also phosphorylated by PKC (in vitro). Belongs to the PP1 inhibitor family.

P21987

MIINHNMSAINANRVLGXTNADITKDL

Component of the core of the flagella. The flagellum consists of an outer layer composed of repeating units of FlaA around a core that contains one or all of five antigenically related polypeptides. Belongs to the bacterial flagellin family.

P29754

MALNSSTEDGIKRIQDDCPRAGRHSYIFVMIPTLYSIIFVVGIFGNSLVVIVIYFYMKLKTVASVFLLNLALADLCFLLTLPLWAVYTAMEYRWPFGNHLCKIASASVSFNLYASVFLLTCLSIDRYLAIVHPMKSRLRRTMLVAKVTCIIIWLMAGLASLPAVIHRNVYFIENTNITVCAFHYESRNSTLPIGLGLTKNILGFLFPFLIILTSYTLIWKALKKAYEIQKNKPRNDDIFRIIMAIVLFFFFSWVPHQIFTFLDVLIQLGVIHDCKIADIVDTAMPITICIAYFNNCLNPLFYGFLGKKFKKYFLQLLKYIPPKAKSHSSLSTKMSTLSYRPSDNMSSAAKKPASCSEVE

Receptor for angiotensin II, a vasoconstricting peptide, which acts as a key regulator of blood pressure and sodium retention by the kidney. The activated receptor in turn couples to G-alpha proteins G(q) (GNAQ, GNA11, GNA14 or GNA15) and thus activates phospholipase C and increases the cytosolic Ca(2+) concentrations, which in turn triggers cellular responses such as stimulation of protein kinase C. Interacts with MAS1 (By similarity). Interacts with ARRB1 (By similarity). Interacts with FLNA (via filamin repeat 21); increases PKA-mediated phosphorylation of FLNA (By similarity). C-terminal Ser or Thr residues may be phosphorylated. Belongs to the G-protein coupled receptor 1 family.

Q3SH82

MQVVHTVADLRAALSEADRSAFVPTMGNLHAGHVSLVELAKRHGGPVVASIFVNPLQFGAGEDFERYPRTLAADCDKLAEAGCDLVFAPDTSALYPVAQTFRVDVPAALAEDLCGAFRPGHFAGVATVVLKLFNLVRPQVAVFGRKDYQQLLVVREMVRQFNLPIDIVAGATLRDPDGLAMSSRNGYLSAAERAQAPQLQRELAAIVAAIDGGARNFAALAAAARQRLTGAGWRVDYVEIRDAESLKTATQETEALVVLAAAWLGQTRLIDNLEVTSAAGIAA

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.

A0JXB3

MTLRVLGVDPGLTRCGIGVVDVEKNRRATMVAVGVVGTSPDESLDQRLLLIATSIDDWLDRYEPHVLAVERVFSQLNVSTVMGVAQASGVVIAAAARRGIPVALHTPSEVKAAVTGSGTSNKDAVTKLVTKILRLDAPPRPADAADALALAITHAWRAGSGAAIATTGPGSQSLTPAQRAWAEAEAKARRAR

Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group. Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction). Binds 1 Mg(2+) ion per subunit. Belongs to the RuvC family.

B4E8S4

MTKLTARQQQVFDLIRRAIERSGFPPTRAEIAAELGFSSPNAAEEHLRALARKGVIELAAGASRGIRLLGVDDAPHQFTLPHAALMQLSLPLVGRVAAGSPILAQEHISQHYACDPALFTSKPDYLLKVRGLSMRDAGILDGDLLAVQKRTEAKDGQIIVARLGDDVTVKRLMRRPGGLELIAENPDYENIFVKAGSADFALEGIAVGLIRSGEL

Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair. Hydrolysis of Ala-|-Gly bond in repressor LexA. Homodimer. Belongs to the peptidase S24 family.

A9H3L2

MAREPREGGRGGRDREREGDDLVDKLVTINRVAKVVKGGRRFAFAALVVVGDQKGRVGYGAGKAREVPEAIRKATDRAKRAMIRVPMKEGRTLHHDVAGHFGAGKVVLRSADAGTGIIAGGPMRAVFESLGINDVVAKSLGTRNPHNMVKATFAALERCASPRTVANRRGKKVSDILGRRDVAGTGEAAADV

With S4 and S12 plays an important role in translational accuracy. Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body. Part of the 30S ribosomal subunit. Contacts proteins S4 and S8. The N-terminal domain interacts with the head of the 30S subunit; the C-terminal domain interacts with the body and contacts protein S4. The interaction surface between S4 and S5 is involved in control of translational fidelity. Belongs to the universal ribosomal protein uS5 family.

Q1MIV1

MNTQTTPSPQFYLTAPAACPYLPHEMERKVFTHLVGPRAAEMNDILTQGGFRRSQNIAYRPACESCRACVSVRILAQEFEPTKSMKRVLAANSDVIATEFAAQPSSEQYSLFRRYLDFRHQQGGMSDMTVLDYAIMVEDTHVNTRIIEYRRREEGSGLEQRPKGELLAAALTDTMSDGLSMVYSYFNPALEQRSLGTFMILDHVRRTKALGLPHVYLGYWVQGSRKMDYKTRFQPQEHLTPRGWERFDPSSMPESTHD

Functions in the N-end rule pathway of protein degradation where it conjugates Leu from its aminoacyl-tRNA to the N-termini of proteins containing an N-terminal aspartate or glutamate. L-leucyl-tRNA(Leu) + N-terminal L-glutamyl-[protein] = H(+) + N-terminal L-leucyl-L-glutamyl-[protein] + tRNA(Leu) L-leucyl-tRNA(Leu) + N-terminal L-aspartyl-[protein] = H(+) + N-terminal L-leucyl-L-aspartyl-[protein] + tRNA(Leu) Belongs to the R-transferase family. Bpt subfamily.

Q48Y18

MKIIRVQDQIEGGKIAFTLLKDSLAKGAKTLGLATGSSPISFYQEMVKSPLDFSDLTSINLDEYVGLSVESDQSYDYFMRQNLFNAKPFKKNYLPNGLATDVEAEAKRYNQIIAEHPIDFQVLGIGRNGHIGFNEPGTSFEEETHVVDLQESTIEANSRFFTSIEDVPKQAISMGIASIMKSEMIVLLAFGQEKADAIKGMVFGPITEHLPASILQKHDHVIVIVDEAAASQLD

Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion. alpha-D-glucosamine 6-phosphate + H2O = beta-D-fructose 6-phosphate + NH4(+) Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosphate from N-acetylneuraminate: step 5/5. Belongs to the glucosamine/galactosamine-6-phosphate isomerase family. NagB subfamily.

Q39580

MASGSSKAVIKNADMSEEMQADAVDCATQALEKYNIEKDIAAYIKKEFDRKHNPTWHCIVGRNFGSYVTHETKHFIYFYLGQVAILLFKSG

Consists of at least 3 heavy chains (alpha, beta and gamma), 2 intermediate chains and 8 light chains. Belongs to the dynein light chain family.

Q924C9

MIEAIGNQYVVARPVYSTKAFGEEFKKTYGHHKTFLDHLKGCCSCSSQKAKKIALSLFPIASWLPAYKIKEWLLSDIVSGISTGLVAVLQGLAFALLVNIPPAYGLYAAFFPVITYFFLGTSRHISVGPFPVLSMMVGVVVTRVASGSDTSPALSSSSAENDSMIEEKVMVAASVTVLSGIIQLLLGVLQIGFVVIYLSESLISGFTTAAAIHVLVSQLKFMLQLTVPAHSDPFSIFKVLESVFSQIQKTNIADLVTSVIILVVVFVVKEINQRYRSKLPVPIPIELIMTVIATGISYGCNFEQRFGVAVVGNMSLGFQPPITPSVEVFQDTIGDCFGIAIVGFAVAFSVASVYSLKYDYPIDGNQELIALGVSNIFTGAFKGFAGSTALSRSGVQESTGGKTQVAGLLSAVIVLIVIVAIGFLLQPLQKSVLAALALGNLKGMLMQFAEIGRLWKKDKYDCLIWIMTFIFAIVLGLGLGLAASVAFQLLTIVFRTQFPKCSTLANVGRSNIYKNKKNYADVYEPEGVKIFRCPSPIYFANIGFFKQKLIDAVGFNPLRILRKRNKALKKIRKLQKQGLIQVTPKGFICTSDGFKDSDEELDNNQIEELDQPINTTDLPFEIDWNADLPLNITIPKISLHSLILDFSAVSFLDISSMRGLRTILQEFIRIKVDVYIVGTDDDFIDKLARCEFFDDEVTDSIFFLTIHDAILHIWMKKDYSTSKFNSSQEKERKFDFTINTNGGLRNRECQVPVETKF

Chloride/bicarbonate exchanger. Mediates the efficient absorption of chloride ions in the colon, participating in fluid homeostasis. Plays a role in the chloride and bicarbonate homeostasis during sperm epididymal maturation and capacitation (By similarity). Interacts with PDZK1, CFTR, SLC26A6 and SLC9A3R1. Localized in sperm membranes. Midpiece of sperm tail. Colocalizes with CFTR at the midpiece of sperm tail (By similarity). N-glycosylation is required for efficient cell surface expression, and protection from proteolytic degradation. Belongs to the SLC26A/SulP transporter (TC 2.A.53) family.

Q4FPU1

MSRATKIALLDYGMGNLHSASKALSAVGAEVSITNDPKVVAAADKIFFPGVGAMRDCIAGMHEAGIDDVIRQAIFNKPVMAICVGMQALFEQSAENGGTPCLSILDGTVPAFNPEWKDEKGVQIKVPHMGWNTISGMNFEHPLWNGIEDKAHFYFVHSYYCEPADSSQVAAICDYGQPFCASILQDNLFATQFHPEKSHTAGLQLLKNFVDWDI

IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF. 5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H(+) + L-glutamate H2O + L-glutamine = L-glutamate + NH4(+) Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9. Heterodimer of HisH and HisF.

Q32P96

MASVNRNSEIIKKLKTDKRLLEEINERRESNCLVERSNQVSLLRVQKRHFHGAYKSFTHDQVKKPVPDSDRSSWVKLSLFVHKEKRHFPPKNNAIFG

Belongs to the SPATA45 family.

Q9ZDS1

MHQSTLLKPVSCYGIGVHTGKRTQLTIEPAKENTGIIFIRTDISSENNYIEASYCNVSDTLLSTTISNNHKIQISTIEHLMAALWGCSIDNAIIKIDGPEVPIMDGSSKPFVFMIECAGKKLQNAPKKYLKILKEVKVVNKDCELYCTPSEHMAVDLTIDFSSKAIGRQNLSFGMQESFTKNIADARTFGFIRDVEYLKSKGLAQGASFENAIGIDEHDKVLNPSGLRYADEFVRHKLLDLFGDLYTSGISVVSAIKGYKTSHAFNNELLHKIFSDTTSYKFVTSNEL

Catalyzes the hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis. a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine + H2O = a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + acetate Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 2/6. Belongs to the LpxC family.

B4EX28

MSENFHILLLNGPNLNLLGTREPETYGHLTLNDIVQSLSADAQALNVKLTHFQSNAEHELINKIHAARGNVDYILINPAAFTHTSVALRDALLGVNIPFIEIHLSNVYSREPFRHHSYLSDIATGVICGLGAEGYRFALQAAVNRLS

Catalyzes a trans-dehydration via an enolate intermediate. 3-dehydroquinate = 3-dehydroshikimate + H2O Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. Homododecamer. Belongs to the type-II 3-dehydroquinase family.

P19759

MVHFTAEEKAIIMSLWGKVNIEEAGGEALGRLLVVYPWTQRFFETFGNLSSASAIMGNPKVKAHGKKVLTSFGEAVKNMDNLKGAFAKLSELHCDKLHVDPENFKLLGNVMVIILATHFGKEFTPDVQAAWQKLVSGVATALAHKYH

The epsilon chain is a beta-type chain of early mammalian embryonic hemoglobin. Heterotetramer of two alpha chains and two epsilon chains in early embryonic hemoglobin Gower-2; two zeta chains and two epsilon chains in early embryonic hemoglobin Gower-1. Red blood cells. Belongs to the globin family.

B3WDL8

MPNSTGKIAQVIGPVVDVAFPINGDLPEINNALTVAKKDGSQLVLEVALELGDGVMRTIAMDSTDGLQRNMAVQDTGGPISVPVGKDTLGRVFNVLGDPIDGGEAFGPDHRRDSIHRDAPKFEDLNTSSEILETGIKVIDLLEPYLRGGKVGLFGGAGVGKTVLIQELIHNIAEEHGGISVFTGVGERTREGNDLYFEMKESGVLENTAMVFGQMNEPPGARMRVALTGLTIAEYFRDVEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGQLQERITSTKKGSVTSIQAIYVPADDYTDPAPATTFAHLDATTNLERRLTEQGIYPAVDPLESSSSALTPEIVGDEHYKVATEVQQVLQRYRELQDIISILGMDELSDEEKVVVARARRIQFFLSQNFNVAERFTGQPGSYVPVEETVKGFKAILDGKYDDYPEDAFRSVGRIEEVVEKAKKMGFAPDDQNTDADEKPAAQAAAN

Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. 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.

B5Z9F8

MKDSHQTIGVFVRPTHYQNPLFEELERAKEWVLKLLEDEGFESFMIDSLDGAQDERLIEKAYAFLCLGGDGTILGALRMTHSYNKPCFGVRIGNLGFLSAVELNGLKDFLQDLKQDRIKLEEHLALEGRIGKISFYAINEIVIAKKKALGVLDIKAYAGHTPFNTYKGDGLIIATPLGSTAYNLSAHGPIVHALSQSYILTPLCDFSLTQRPLVLGAEFCLNFCAHEDALVVIDGQATYDLKANQPLYIQKSPTTTKLLQKNSRDYFKVLKEKLLWGESPSKKR

Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP. ATP + NAD(+) = ADP + H(+) + NADP(+) Belongs to the NAD kinase family.

Q6HCK7

MWNEFKKFAFKGNVIDLAVGVVIGAAFGKIVSSLVKDIITPLLGMVLGGVDFTDLKITFGKSSIMYGNFIQTIFDFLIIAAAIFMFVKVFNKLTSKREEEKEEEIPEPTKEEELLGEIRDLLKQQNSSKDRA

Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell. Homopentamer. Belongs to the MscL family.

Q8L4J8

MSVNGENKVSGGDSSSSDRPVRVYADGIFDLFHFGHARAIEQAKKSFPNTYLLVGCCNDEITNKFKGKTVMTESERYESLRHCKWVDEVIPDAPWVLTTEFLDKHKIDYVAHDALPYADTSGAGNDVYEFVKSIGKFKETKRTEGISTSDIIMRIVKDYNQYVLRNLDRGYSREELGVSFEEKRLRVNMRLKKLQEKVKEQQEKIQTVAKTAGMHHDEWLENADRWVAGFLEMFEEGCHKMGTAIRDGIQQRLMRQESEENRRLLQNGLTISKDNDDEQMSDDNEFAEEDCVNVSNKGIETVKK

Plays an important role in the biosynthesis of the phospholipid phosphatidylcholine (PubMed:12461134, PubMed:19667100). Catalyzes the formation of CDP-choline (PubMed:12461134, PubMed:19667100). CTP + H(+) + phosphocholine = CDP-choline + diphosphate Optimum temperature is 30 degrees Celsius. Phospholipid metabolism; phosphatidylcholine biosynthesis; phosphatidylcholine from phosphocholine: step 1/2. By cold treatment. No visible phenotype under normal growth conditions. Belongs to the cytidylyltransferase family.

Q7Z3Z0

MSLRLSSASRRSCPRPTTGSLRLYGGGTSFGTGNSCGISGIGSGFSSAFGGSSSGGNTGGGNPCAGFTVNERGLLSGNEKVTMQNLNDRLASYLDSVHALEEANADLEQKIKGWYEKFGPGSCRGLDHDYSRYFPIIDDLKNQIIASTTSNANAVLQIDNARLTADDFRLKYENELALHQSVEADVNGLRRVLDEITLCRTDLEIQYETLSEEMTYLKKNHKEEMQVLQCAAGGNVNVEMNAAPGVDLTVLLNNMRAEYEALAEQNRRDAEAWFNEKSASLQQQISEDVGATTSARNELTEMKRTLQTLEIELQSLLATKHSLECSLTETESNYCAQLAQIQAQIGALEEQLHQVRTETEGQKLEYEQLLDIKLHLEKEIETYCLLIGGDDGACKSGGYKSKDYGSGNVGSQVKDPAKAIVVKKVLEEVDQRSKILTTRLHSLEEKSQSN

Essential for the proper assembly of type I and type II keratin protein complexes and formation of keratin intermediate filaments in the inner root sheath (irs) (By similarity). Plays a role in the cytoskeleton organization (PubMed:26902920). Heterodimer of a type I and a type II keratin (PubMed:26902920). Heterodimer with type II keratin KRT5 leading to the formation of keratin intermediate filament (KIF) network (PubMed:28899683). Interacts with KRT6A to form filaments (By similarity). Strongly expressed in skin and scalp, and weak expression observed in thymus and tongue. In the hair follicle, expressed in Henle layer, Huxley layer and in the inner root sheath cuticle of the hair follicle. Expression extends from the bulb region up to the point of differentiation into the three layers. Also present in the medulla of beard hair (at protein level). The disease is caused by variants affecting the gene represented in this entry. There are two types of cytoskeletal and microfibrillar keratin: I (acidic; 40-55 kDa) and II (neutral to basic; 56-70 kDa). Belongs to the intermediate filament family.

P28386

VGFKAGVREYKLTYYTPEYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVPGEADQYMSYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPAYIKTFQGPPHGIQVERDKLNKYGRPTLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQAETGEIKGHYLNATAGTCEEMIKRAVFARELGVPIIMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGIHFRVLAKALRMSGGDHIHSGTVVGKLEGERDITLGFVVLLRDDYIEKDRSRGIYFTQDWVSLPGVIPVASGGIHVWHMPALTEISGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLAREGNAIIC

RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site. 2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O D-ribulose 1,5-bisphosphate + O2 = (2R)-3-phosphoglycerate + 2-phosphoglycolate + 2 H(+) Binds 1 Mg(2+) ion per subunit. Heterohexadecamer of 8 large chains and 8 small chains; disulfide-linked. The disulfide link is formed within the large subunit homodimers. The disulfide bond which can form in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover. The basic functional RuBisCO is composed of a large chain homodimer in a 'head-to-tail' conformation. In form I RuBisCO this homodimer is arranged in a barrel-like tetramer with the small subunits forming a tetrameric 'cap' on each end of the 'barrel'. Belongs to the RuBisCO large chain family. Type I subfamily.

A1AS38

MKNQNTPIAFEGFPFIAGFAALTLLTALSAGKLCSAILYGFSALFALLTLFSLYFFRNPQRTPPADERAVVAPADGTVIVVDRVPVTPLGHEALKISIFMSVFNVHVNRVPFSGRVVELTHTPGKFFDVRDSRSSCENERSTIVLETVSGLRMAFVQVAGLIARRIVCYARNGEMLERGKRYGLIRFGSRLDVYLPPDVQPLVKLGDKTIAGETVLGRLG

Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2 Binds 1 pyruvoyl group covalently per subunit. Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2. Heterodimer of a large membrane-associated beta subunit and a small pyruvoyl-containing alpha subunit. Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain. Belongs to the phosphatidylserine decarboxylase family. PSD-A subfamily.

A4WPB7

MTQSLTIRRPDDWHLHLRDGAMLEGVLPETTRHFARAIVMPNLVPPVVTGAEAAAYRERIMAALPAGARFEPLMVLYLTETTDPADVRAAAASGLVKAVKLYPAGATTNSASGVRDFDRVRGVLETMAEIGLPLCVHGEVTDPAVDIFDREAVFLERVLEPIRRATPGLRVVLEHVTTRDGLDYVRGGGPDMAGTLTTHHLIINRNHILAGGIRPHYYCLPVAKRETHRLALREAATGGEGCFFLGTDSAPHADAAKESACGCAGCFTATNTLSILAHVFEEEGALDRLEGFVALNGPAFYRLPPNEERITLRKGEPLVLPARIETGAGPVTLFDPGFPLLWHVES

Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. (S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate Binds 2 Zn(2+) ions per subunit. Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. Homodimer. Belongs to the metallo-dependent hydrolases superfamily. DHOase family. Class II DHOase subfamily.