Datasets:

vinesmsuic

/

SwissProtCLAP_random_10k

like 0

Q44662

MRRIQSIARSPIAIALFMSLAVAGCASKKNLPNNAGDLGLGAGAATPGSSQDFTVNVGDRIFFDLDSSLIRADAQQTLSKQAQWLQRYPQYSITIEGHADERGTREYNLALGQRRAAATRDFLASRGVPTNRMRTISYGNERPVAVCDADTCWSQNRRAVTVLNGAGR

Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. The Tol-Pal system is composed of five core proteins: the inner membrane proteins TolA, TolQ and TolR, the periplasmic protein TolB and the outer membrane protein Pal. They form a network linking the inner and outer membranes and the peptidoglycan layer. The N-terminus is blocked. Belongs to the Pal lipoprotein family.

Q7ZAL7

MKRELLLEKIDELKEIMPWYVLEYYQSKLSVPYSFTTLYEYLKEYRRFLEWLLDSGVANCHHIAEIELSVLENLTKKDMEAFILYLRERPLLNANTRQNGVSQTTINRTLSALSSLFKYLTEEVENADGEPYFYRNVMKKVSTKKKKETLASRAENIKQKLFLGNETIEFLEYIDCEYQNKLSKRALAFFNKNKERDLAIIALLLASGVRLSEAVNLDLKDINLNVMVIDVTRKGGKRDSVNVASFAKPYLANYLDIRKNRYKAENQDIALFLSEYRGVPNRIDASSVEKMVAKYSQDFKVRVTPHKLRHTLATRLYDATKSQVLVSHQLGHASTQVTDLYTHIVNDEQKNALDKL

Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. Essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. FtsK is required for recombination. Belongs to the 'phage' integrase family. XerS subfamily.

Q49Y16

MIGLIIIVVIVLVALLLLFSFVPVGLWISAIAAGVKVGIGTLVGMRLRRVSPRKVISPLIKAHKAGLHLTTNQLESHYLAGGNVDRVVDANIAAQRADINLPFERGAAIDLAGRDVLEAVQMSVNPKVIETPFIAGVAMNGIEVKAKARITVRANIARLVGGAGEETIIARVGEGIVSTIGSSEHHTQVLENPDNISKTVLSKGLDSGTAFEILSIDIADVDISKNIGADLQTEQALADKNIAQAKAEERRAMAVAQEQEMKAKVQEMRSKVVEAEAEVPLAMAEALRSGNLGVKDYYNLKNVEADTGMRNSINQRTNQKDDESPDK

Found in functional membrane microdomains (FMM) that may be equivalent to eukaryotic membrane rafts. FMMs are highly dynamic and increase in number as cells age. Flotillins are thought to be important factors in membrane fluidity. Homooligomerizes. Belongs to the flotillin-like FloA family.

P55214

MADDQNCAPELEKADPSGEDGVDAKPDRSSIISSILGKKKKNASACPVKTARDRVPTYLYRMDFEKMGKCIIINNKNFDKVTGMDVRNGTDKDAEALFKCFRSLGFDVVVYNDCSCAKMQDLLRKASEEDHSNSACFACVLLSHGEENLIYGKDGVTPIKDLTAHFRGDRCKTLLEKPKLFFIQACRGTELDDGVQADSGPINETDANPRYKIPVEADFLFAYSTVPGYYSWRNPGKGSWFVQALCSILDEHGKDLEIMQILTRVNDRVARHFESQCDDPCFNEKKQIPCMVSMLTKELYFGR

Involved in the activation cascade of caspases responsible for apoptosis execution. Cleaves and activates sterol regulatory element binding proteins (SREBPs). Overexpression promotes programmed cell death (By similarity). Cleaves phospholipid scramblase proteins XKR4, XKR8 and XKR9 (By similarity). Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Asp-Glu-Val-Asp-|-. Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a 20 kDa (p20) and a 11 kDa (p11) subunit. Interacts with BIRC6/bruce. Interacts with HSPA5 (By similarity). Cleavages by granzyme B or caspase-10 generate the two active subunits. Propeptide domains can also be cleaved efficiently by caspase-3. Active heterodimers between the small subunit of caspase-7 and the large subunit of caspase-3, and vice versa, also occur (By similarity). Belongs to the peptidase C14A family.

P24420

MRVSGSASSQDIISRINSKNINNNDSNEVKRIKDALCIESKERILYPQNLSRDNLKQMARYVNNTYVHYSGNCVLLSACLHYNIHHRQDILSSKNTASPTVGLDSAIVDKIIFGHELNQSYCLNSIDEVEKEILNRYDIKRESSFIISAENYIAPIIGECRHDFNAVVICEYDKKPYVQFIDSWKTSNILPSLQEIKKHFSSSGEFYVRAYDEKHD

Part of a Salmonella virulence gene cluster. Decreased virulence in mice. In Salmonella spp. the spv gene cluster is encoded on a highly transmissible plasmid. Belongs to the SpvD family.

B6IUW3

MHFLEFEKPIADLEGKIEELRTLTDGGDINIADEVKKLQEKVDKLLRSTYAKLTPAQKVQVARHPERPHCLDYIQRLITDFTPLAGDRLFAEDRAIVGGLGRFRGRSVVVIGQERGHDTESRVRHNFGMAKPEGYRKAQRLLQLADRFRLPVVTLVDTAGAFPGVSAEERGQAEAIARSIETCLRLKVPLVSAVIGEGGSGGAIAIATADRVLMLEHAIYSVISPEGCASILWRSAANASDAAQALRLTAQDLKELGVIDRVVMEPVGGAHRRREEMIATLGNAIEDALDDLREQDGATLRLNRRQKFLDIGQKGLG

Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA. acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein] Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD). Belongs to the AccA family.

Q10075

MNIVKRAVPELLRGMTNATPNIGLIKNKVVSFEAVGQLKKSFYKRQLPKQCLAFDSSLGKDVFLRALQEGRMENYFSLAQQMVTQNEPAFCGLGTLCMILNSLKVDPGRLWKGSWRWYDQYMLDCCRSLSDIEKDGVTLEEFSCLANCNGLRTITKCVKDVSFDEFRKDVISCSTIENKIMAISFCRKVLGQTGDGHFSPVGGFSESDNKILILDVARFKYPCYWVDLKLMYESMFPIDKASGQPRGYVLLEPMHIPLGVLTVGLNKYSWRNVSKHILQQAATVKNADNLAEILLSINQSSIPLIQERSNSSKSGDFEHFKECIRSTKTYHLFLKHTNTNVEYITMAFWAIFSLPMIQKALPKGVLEEIQSLLKEVEISEINTQLTALKKQLDSLTHCCKTDTGCCSSSCCKNT

Required for detoxification of heavy metals such as cadmium and arsenate. [Glu(-Cys)](n)-Gly + glutathione + H(+) = [Glu(-Cys)](n+1)-Gly + glycine By cadmium, copper and zinc. Belongs to the phytochelatin synthase family.

D5USX8

MPIGKSAAAVTPRRIAVLSVHTSPLAQPGMGDAGGMNVYIWQTSLELAARGIEVEIFTRATSSSDAPIVEAAPGIRVRNVVAGPFEGLDKTDLPAQLCAFAAGVQRAEAREEPGYFDLIHSHYWLSGQVGWLARDRWGVPLVHTAHTLAAVKNRALAEGDTAEPQARIIGEQQVSDEADRLIVNTEVEASQLADLHDVPLDRIDVVYPGADLATYTPGDGAGARRELGIAPDELVLTFVGRIQPHKAPDLLLRAAAPLIHAHPDRRIRILVVGGPSGTGLERPDALIALARELGIEHAVTFEPPRPPAGLAEVYRASDLVVVPSYSESFGLVAVEAQACGTPVVAAKVGGLSVAVADGVSGRLIDGHDPQEWTAVLDELTANAELRTELAAGATEHARRFSWARTADGLLNSYAKAIEARQEATQTVRRRRRRAGVRA

Catalyzes the transfer of a N-acetyl-glucosamine moiety to 1D-myo-inositol 3-phosphate to produce 1D-myo-inositol 2-acetamido-2-deoxy-glucopyranoside 3-phosphate in the mycothiol biosynthesis pathway. 1D-myo-inositol 3-phosphate + UDP-N-acetyl-alpha-D-glucosamine = 1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside 3-phosphate + H(+) + UDP Homodimer. Belongs to the glycosyltransferase group 1 family. MshA subfamily.

C0HJV3

SWDSIWKSAKNKMDKIMRQKVAKWMAKKEGKSVEEVQAKVDAMSKKDIRLHVISHYGKKAFEQLSKSLE

Insecticidal and antimicrobial peptide. Has insecticidal activity against larvae of flesh fly S.carnaria. Has antibacterial activity against Gram-positive bacterium B.subtilis B-501 (MIC=1.25 uM) and Gram-negative bacterium E.coli DH5alpha (MIC=2.5 uM). Expressed by the venom gland. Both the N-terminus (1-33) and the C-terminus (38-69) of the mature peptide form alpha-helices which probably disrupt target cell membranes. The linker region (34-37) probably derives from a processing quadruplet motif (PQM), found in propeptides of many zodatoxins, hinting at a fusion of two originally separate membrane-active peptides. LD(50) is 40 ug/g in larvae of flesh fly S.carnaria. Belongs to the cationic peptide 06 (cytoinsectotoxin) family.

A9MND7

MIEADRLISAGATIAEEVADRAIRPKLLAEYVGQPQVRSQMEIFIQAAKLRGDALDHLLIFGPPGLGKTTLANIVANEMGVNLRTTSGPVLEKAGDLAAMLTNLEPHDVLFIDEIHRLSPVVEEVLYPAMEDYQLDIMIGEGPAARSIKIDLPPFTLIGATTRAGSLTSPLRDRFGIVQRLEFYQVPDLQHIVGRSARHMGLEMSDDGALEVARRARGTPRIANRLLRRVRDFAEVKHDGAISAEIAAQALDMLNVDAEGFDYMDRKLLLAVIDKFFGGPVGLDNLAAAIGEERETIEDVLEPYLIQQGFLQRTPRGRMATVRAWNHFGITPPEMP

The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. ATP + H2O = ADP + H(+) + phosphate Forms a complex with RuvA. Belongs to the RuvB family.

Q9ZBX1

MIDLRLLREDPDRVRASQRARGEDVALVDSLLSADERRRSSGVRFDELRAEQKGLGKLIGKAAGDEKAELLKRAEQLKTDVKAADAERDAADAETQELLQRLGNLVHPDVPVGGEEDFVTLETHGTHRDFAAEGFEPRDHLELGQLLGAIDVERGAKVSGSRFYFLTGVGALLELALVNAAIAQATAAGFTPMLTPALVRPQSMAGTGFLGQAAQDVYHLDKDDLYLVGTSEVPLAAYHMDEILDGDRLPLRYAGFSPCFRREAGSHGKDTRGIFRVHQFDKVEMFSYVLPEDSQAEHQRLLEWEKQWLTSLELPFRVIDVASADLGSSAARKYDCEAWIPTQGKYRELTSTSDCTEFQSRRLSIRVREGKKVRPLATLNGTLCAVPRTIVAILENHQQADGSVRVPEVLRPYLGGREVLEPVAK

Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec). ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) + L-seryl-tRNA(Ser) ATP + L-serine + tRNA(Sec) = AMP + diphosphate + H(+) + L-seryl-tRNA(Sec) Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1. Homodimer. The tRNA molecule binds across the dimer. Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding. Belongs to the class-II aminoacyl-tRNA synthetase family. Type-1 seryl-tRNA synthetase subfamily.

P40170

MSTKDFIEKDYYKVLGVPKDATEAEIKKAYRKLARENHPDANKGNVKAEERFKEISEANDILGDPKKRKEYDEARALFGNGGFRPGPGAGGGGTFNFDLGDLFGGGAQGGGGQGGAGGFGGGLGDVFGGLFNRTGGGPGTGTRTQPRRGQDIESEVTLSFTEAIEGATVPLRMSSQAPCKACSGTGDKNGTPRVCPTCVGTGQVARGSGGGFSLTDPCPDCKGRGLIAEDPCEVCKGSGRAKSSRTMQVRIPAGVSDGQRIRLRGKGTPGERGGPAGDLYVVVHVKEHPVFGRRGDNLTVTVPVTYAEAALGGEVRVPTLGGPSVTLKLPAGTPNGRTMRARGKGAVRKDGTRGDLLVTVEVSVPKDLTGKARDALQAYREATADEDPRAELFQAAKGA

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins. Binds 2 Zn(2+) ions per monomer. Homodimer. The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity. Belongs to the DnaJ family.

A9WHY7

MNNILAIALGAAIGANLRYGIGLWAAQRFGTAWPYGTFIINLLGCLGIGLLLTLISTRLTLSEPVRLMLVTGLLGGFTTFSTFGYESFSLLSSGNWLPAIGYMVGSVVGGLIAVIIGVGLGRWFGG

Important for reducing fluoride concentration in the cell, thus reducing its toxicity. Belongs to the CrcB (TC 9.B.71) family.

Q99V75

MVTQNKKILIITGSFGNGHMQVTQSIVNQLNDMNLDHLSVIEHDLFMEAHPILTSICKKWYINSFKYFRNMYKGFYYSRPDKLDKCFYKYYGLNKLINLLIKEKPDLILLTFPTPVMSVLTEQFNINIPVATVMTDYRLHKNWITPYSTRYYVATKETKQDFIDVGIDPSTVKVTGIPIDNKFETPINQKQWLIDNNLDPDKQTILMSAGAFGVSKGFDTMITDILAKSANAQVVMICGKSKELKRSLIAKFKSNENVLILGYTKHMNEWMASSQLMITKPGGITITEGFARCIPMIFLNPAPGQELENALYFEEKGFGKIADTPEEAIKIVASLTNGNEQLTNMISTMEQDKIKYATQTICRDLLDLIGHSSQPQEIYGKVPLYARFFVK

Processive glucosyltransferase involved in the biosynthesis of both the bilayer- and non-bilayer-forming membrane glucolipids. Is able to successively transfer two glucosyl residues to diacylglycerol (DAG), thereby catalyzing the formation of beta-monoglucosyl-DAG (3-O-(beta-D-glucopyranosyl)-1,2-diacyl-sn-glycerol) and beta-diglucosyl-DAG (3-O-(beta-D-glucopyranosyl-beta-(1->6)-D-glucopyranosyl)-1,2-diacyl-sn-glycerol). Beta-diglucosyl-DAG is the predominant glycolipid found in Bacillales and is also used as a membrane anchor for lipoteichoic acid (LTA). a 1,2-diacyl-3-O-(beta-D-glucopyranosyl)-sn-glycerol + UDP-alpha-D-glucose = a 1,2-diacyl-3-O-(beta-D-Glc-(1->6)-beta-D-Glc)-sn-glycerol + H(+) + UDP a 1,2-diacyl-sn-glycerol + UDP-alpha-D-glucose = a 1,2-diacyl-3-O-(beta-D-glucopyranosyl)-sn-glycerol + H(+) + UDP Glycolipid metabolism; diglucosyl-diacylglycerol biosynthesis. Belongs to the glycosyltransferase 28 family. UgtP subfamily.

A4VJ19

MGNLSVNQNKLQKRLRRLAGEAVTDFNMIEDGDKVMVCLSGGKDSYTMLDVLLYLQKVAPIRFEVVAVNMDQKQPGFPEHVLPEYLKSIGVEYHIIEKDTYSVVKEKIPEGKTTCSLCSRLRRGTLYTFADEIGATKMALGHHRDDILETFFLNMFYGGTLKAMPPKLLSDDGRNVVIRPLAYCSEADIEAYSKMKEFPIIPCNLCGSQENLQRQVVKEMLQEWERKSPGRTEIMFRALQNVVPSQLADRNLFDFKSLRIDDSATPRFVDVMSL

Catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(2)C32). The sulfur atoms are provided by the cysteine/cysteine desulfurase (IscS) system. AH2 + ATP + cytidine(32) in tRNA + S-sulfanyl-L-cysteinyl-[cysteine desulfurase] = 2-thiocytidine(32) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[cysteine desulfurase] Binds 1 [4Fe-4S] cluster per subunit. The cluster is chelated by three Cys residues, the fourth Fe has a free coordination site that may bind a sulfur atom transferred from the persulfide of IscS. tRNA modification. Homodimer. The thiolation reaction likely consists of two steps: a first activation step by ATP to form an adenylated intermediate of the target base of tRNA, and a second nucleophilic substitution step of the sulfur (S) atom supplied by the hydrosulfide attached to the Fe-S cluster. Belongs to the TtcA family.

A1JIQ4

MSETASWQPSAPIANLLKRAAIMAEIRRFFADRGVLEVETPTMSQATVTDIHLVPFQTRFVGPGAADGLTLYMMTSPEYHMKRLLAAGSGSIYQLGRSFRNEEAGRHHNPEFTMLEWYRPHYDMYRLMDEVEDLLQQILDCDSSERLSYQQAFLRHLDIDPLSADKAQLREAAAKLDLSNIADTEEDRDTLLQLLFTVGVEPHIGRDKPAFVYHFPASQASLAVISTEDHRVAERFEVYFKGIELANGFHELTDGDEQLKRFEQDNRSREKRGLPQHPIDMNLIDALKHGLPDCSGVALGVDRLVMLALGAEKLSDVIAFPVGRA

With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P. Homodimer. Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.

Q2YBQ4

MGTGIEMLSRKEQHNANKLHKRLRRLVGTAIADFNMIESGDRVMVCLSGGKDSYALLDILRSLQAHAATQFELIAVNLDQKQPGFPEHVLPNYLTSIGMPFRIVEQDTYSVVKRLIPEGKTTCSLCSRLRRGVLYRVADELGATKIALGHHRDDILETLLLNLFHGGKLKTMPPKLVSDDGKHIVIRPLAYCKEKDLAAYAEMENFPIIPCNLCGSQKNMQRQVVKEMLQQWDKKFPGRLENMFSSLQNIQPSHLLDSSLYDFHGLKTGNGPVVDGDRAFDPEPFEPGVEELLSLNKD

Catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(2)C32). The sulfur atoms are provided by the cysteine/cysteine desulfurase (IscS) system. AH2 + ATP + cytidine(32) in tRNA + S-sulfanyl-L-cysteinyl-[cysteine desulfurase] = 2-thiocytidine(32) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[cysteine desulfurase] Binds 1 [4Fe-4S] cluster per subunit. The cluster is chelated by three Cys residues, the fourth Fe has a free coordination site that may bind a sulfur atom transferred from the persulfide of IscS. tRNA modification. Homodimer. The thiolation reaction likely consists of two steps: a first activation step by ATP to form an adenylated intermediate of the target base of tRNA, and a second nucleophilic substitution step of the sulfur (S) atom supplied by the hydrosulfide attached to the Fe-S cluster. Belongs to the TtcA family.

P02661

MKLLILTCLVAAALALPRAHRRNAVSSQTQQENSSSEEQEIVKQPKYLSLNEEFVNNLNRQRELLTEQDNEIKITMDSSAEEQATASAQEDSSSSSSSSEESKDAIPSATEQKNIANKEILNRCTLEQLQRQIKYSQLLQQASLAQQASLAQQASLAQQALLAQQPSLAQQAALAQQASLAQQASLAQQASLAQKHHPRLSQVYYPNMEQPYRMNAYSQVQMRHPMSVVDQAQFSVQSFPQLSQYGAYPLWLYFPQDMQYLTPEAVLNTFKPIAPKDAENTNVW

Important role in the capacity of milk to transport calcium phosphate. Mammary gland specific. Secreted in milk. Belongs to the alpha-casein family.

Q5XI52

MTPEFDEEVVFENSPLYQYLQDLGHTDFEICSSLSPKTETCLTTEEPQTPPTRVLQKQGILLKLTETIKSWTLSSQYSKKDDLLHKLDTGFRLDALDAILQQEVLLQEDVELIELLDPSILSAGHPQQENGHLPTLCSLATPNIWDVSMLFAFISLLIMLPTWWIVSSWLVWGIILFLYLIIRVLKFWRTAKLQMTLKKYRVRLEDMAANSRAFTNLVRKSLRLIQETEVISRGFTLLLDRVSAACSFNKAAQHPSQHLIGLRKAVYRTVRANFQAARLATLYMLKNYPLNSESDNVTNYICVVPFKELGLGLSEDQISEEEARNLTDGFSLPALKVLFQLWVAQSSEFFRRLALLLSTANSPSGPLLTAALLPHRILSDVTQGLPHAHTACLDELKRSYEFFRYFETQHQSVPQRLPKTQPKWRELNNVHTAVRSLQLHLKALLNEVIILEDELEKLVCTKETQELLSEAYPVLEQRLKLIEPHVQASNSCWEEAISQVDRLLRRNTDQKGKPGVACENPHCTAAPLLRPTLHIEDRDPIPEEQELEAYVDGIDIESEFRKDSLYHVSQEDRERQKREQEESKRVLQELKSVLGFKASEAERQKWKQLLFSDHAVLKSLSPVEPVESVSNSETPMNSDTEQAHSEATEEETSKPCASDKEDTRTEYMCDGPPKGQSKDTSGDQGHLLQGAHQCESEAKPPQAAAAGATAPPTPRDSPRLSIKQRLARLQLSPEYTFTAGLAAEVAARSLSFTTMQEQTFGDEEDEDKEQLVEGGERELEEK

Plays a pivotal role in the establishment of adherens junctions and their maintenance in adult life. Required for morphogenesis of the preimplantation embryo, and for the implantation process. Interacts with USH2A (via the cytoplasmic region); the interaction associates VEZT with the USH2 complex at the stereocilia base (By similarity). Interacts with myosin MYO7A and the cadherin-catenins complex (By similarity). Belongs to the vezatin family.

Q1I788

MNPQRKKRLFLILGLLAGVGVAVGFALSALQQNINLFYTPTQIANGEAPLDTRIRAGGMVEKGSVQRSADSLDVRFVVTDYTKSVPITYRGILPDLFREGQGIVALGKLNADGVVVADEVLAKHDEKYMPPEVTKALKESGQAASDAGAKP

Heme chaperone required for the biogenesis of c-type cytochromes. Transiently binds heme delivered by CcmC and transfers the heme to apo-cytochromes in a process facilitated by CcmF and CcmH. Belongs to the CcmE/CycJ family.

Q9D3B4

MGWLFLKVLLVGMAFSGFFYPLVDFSISGKTRAPQPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVTSVGGLPVNETTLAEVLRQEGYVTAMIGKWHLGHHGSYHPNFRGFDYYFGIPYSNDMGCTDAPGYNYPPCPACPQRDGLWRNPGRDCYTDVALPLYENLNIVEQPVNLSGLAQKYAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPLAHPQRQSLYRASLREMDSLVGQIKDKVDHVARENTLLWFTGDNGPWAQKCELAGSVGPFFGLWQTHQGGSPTKQTTWEGGHRVPALAYWPGRVPANVTSTALLSLLDIFPTVIALAGASLPPNRKFDGRDVSEVLFGKSQMGHRVLFHPNSGAAGEYGALQTVRLNHYKAFYITGGAKACDGSVGPEQHHVAPLIFNLEDAADEGMPLQKGSPEYQEVLQQVTRALADVLQDIADDNSSRADYTQDPSVIPCCNPYQTTCRCQPV

Displays arylsulfatase activity at acidic pH towards the artificial substrate p-nitrocatechol sulfate (PubMed:25135642). Catalyzes the hydrolysis of the 3-sulfate groups of the N-sulfo-D-glucosamine 3-O-sulfate units of heparin (PubMed:22689975). an aryl sulfate + H2O = a phenol + H(+) + sulfate Hydrolysis of the 3-sulfate groups of the N-sulfo-D-glucosamine 3-O-sulfate units of heparin. Binds 1 Ca(2+) ion per subunit. The 63-kDa precursor protein localizes to pre-lysosomal compartments and tightly associates with organelle membranes, most likely the endoplasmic reticulum. In contrast, proteolytically processed fragments of 34-, 18- and 10-kDa are found in lysosomal fractions and lose their membrane association. Highly expressed in the spleen, kidney, liver, brain, and testis (at protein level). N-glycosylated with both high mannose and complex type sugars. The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity. The 63-kDa precursor undergoes proteolytic processing in two steps, yielding two fragments in the first step (apparent molecular masses of 44 and 18 kDa). In the second step, the 44-kDa fragment is processed further to the 34- and 10-kDa chains. The 10-kDa chain is a cleavage product of the 44-kDa fragment but linked to the 18-kDa chain through a disulfide bridge. Mice accumulate heparan sulfate in visceral organs and the central nervous system and develop neuronal cell death and behavioral deficits (PubMed:22689975). This accumulated heparan sulfate exhibits unique non-reducing end structures with terminal N-sulfoglucosamine-3-O-sulfate residues (PubMed:22689975). Belongs to the sulfatase family.

A6VH05

MAEKKAEKRAEKRKFNTEAWEPKTQIGRMVKEGTISDINYIMDKGLPLLEPEIVDALLPDLEEQVLDVKLVQRMHKSGRRARYRATVVVGNKNGYVGVGMGKSKEVGPAIRKAIAHAKLSLIKVRIGCGSWECGCGYPHSIPFTAKGACGSVKVELLPAPRGVGLVAGNVAKAVLGLAGIKDAWTKTFGDTRTTYNFAEATFDALNNLNFVRCLPAQKEKLGLTEGRVL

With S4 and S12 plays an important role in translational accuracy. Part of the 30S ribosomal subunit. Contacts protein S4. 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.

Q3TFR2

MSLVAEAFVSQIAATEPWPENATLYQQLRGEQILLSDNAASLAVQAFLQMCNLPVKVVCRANAEYMSPSGKVPFIHVGNQVVSELGPIVQFVKAKGHSLSDGLDEVQKAEMKAYMELVNNMLLTAELYLQWCDEATVGEITIARYGSPYPWPLNHILAYQKQWEVKRKMKAIGWGNKTLDQVLEDVDQCCQALSQRLGTQPYFFNKQPTELDALVFGHLYTILTTQLTSDELSEKVKNYSNLLAFCRRIEQHYFEDWGKGRLS

Involved in transport of proteins into the mitochondrion. Interacts with MTX1/metaxin-1. Associates with the mitochondrial contact site and cristae organizing system (MICOS) complex, composed of at least MICOS10/MIC10, CHCHD3/MIC19, CHCHD6/MIC25, APOOL/MIC27, IMMT/MIC60, APOO/MIC23/MIC26 and QIL1/MIC13. This complex was also known under the names MINOS or MitOS complex. The MICOS complex associates with mitochondrial outer membrane proteins SAMM50, MTX1 and MTX2 (together described as components of the mitochondrial outer membrane sorting assembly machinery (SAM) complex) and DNAJC11, mitochondrial inner membrane protein TMEM11 and with HSPA9. The MICOS and SAM complexes together with DNAJC11 are part of a large protein complex spanning both membranes termed the mitochondrial intermembrane space bridging (MIB) complex (By similarity). Belongs to the metaxin family.

B4EBR4

MLDIQLLRKDLDGVAKRLADRGYTLDVAAFSALEAERRAIQTHTEELQARRNSLSKQIGAMKGKGEDTSAVMAEVSGIGDDMKASEAKLGEIQARLSDLMLGMPNVAHESVPVGKDEADNVEVRRWGTPRQFDFEVKDHVDVGTPLGLDFETGAKLAGARFTMLRGPIARLHRALAQFMIDTHTQQHGYTETYTPYIVNPEILYGTGQLPKFADDMFRVEKGGAENTVTQYLISTSEISLTNTVRESIVDGAALPIKLTAHSPCFRSEAGSYGRDTRGMIRQHQFDKVEMVQVVAPETSYAALDEMVGHAEAILQKLGLPYRVITLCTGDMGFSAAKTFDLEVWLPAQNTYREISSCSNTEAFQARRMQARFRNAQGKPELVHTLNGSGLAVGRTLVAVLENYQNADGSVTVPEVLRPYMGGMERIDAPAQTS

Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec). ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) + L-seryl-tRNA(Ser) ATP + L-serine + tRNA(Sec) = AMP + diphosphate + H(+) + L-seryl-tRNA(Sec) Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1. Homodimer. The tRNA molecule binds across the dimer. Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding. Belongs to the class-II aminoacyl-tRNA synthetase family. Type-1 seryl-tRNA synthetase subfamily.

Q108U1

MAAAVQRGLPVAGGGESSESEDDGWEIGYLDRASQKLTSPLPTEEKNEIFKKALTTGDISLVEELLDSGISVESSFRYGWTPLMYAASVANVELVRVLLDRGANASFEKDKHTVLITACSARGSQEQILKCVELLLSRNADPNVACRRLMTPIMYAARDGHPQVVALLVAQGAEVNAQDENGYTALTWAARQGHKNVVLKLLELGANKMLQTKDGKTPSEVANKNKHPEIFSLLSLTLNPLEGKLQQLTKEETICKLLTTDSDKEKDYIFSSYAAFGDLEIFLYGLGLEHMTDLLKERDISLRHLLTMRKDEFSKNGIASRDQQKILAALKELAVEEIKFGELPEVAKLEISGDEFLSFLLKLNKQCGHLITAVQNIITELPVSSHKIVLEWASPQNFTSVCEELVSNVEDLSEEVCKLKDLIQKLQNERENDPTHIPSVEEASPWRSRILKRTAVTVCGFGFLLFICKLTFQRK

Plays a central role during spermatogenesis by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons. Its association with pi-bodies suggests a participation in the primary piRNAs metabolic process. Required prior to the pachytene stage to facilitate the production of multiple types of piRNAs, including those associated with repeats involved in the regulation of retrotransposons. May act by mediating protein-protein interactions during germ cell maturation (By similarity). Interacts with DDX4, PIWIL1, RANBP9 and TDRD1. Component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis. Specifically localizes to pi-bodies, a subset of the nuage which contains primary piRNAs (By similarity).

Q8DDC8

MANYFNTLNLREQLDQLGRCRFMDRSEFATEADYLKGKKVVIVGCGAQGLNQGLNMRDSGLDVAYALRQAAIDEQRQSYKNAKENGFEVGSYETLIPQADLVVNLTPDKQHTNVVETVMPLMKEGAALGYSHGFNVVEEGMQIRKDLTVVMVAPKCPGTEVREEYKRGFGVPTLIAVHPENDPKGEGWDIAKAWAAATGGHRAGCLESSFVAEVKSDLMGEQTILCGMLQAGSIVCYEKMVAEGIDPGYAGKLLQYGWETITEALKFGGITHMMDRLSNPAKIKAFELSEELKDLMRPLYNKHMDDIISGHFSSTMMADWANDDANLLGWRAETGETAFENYPSTDVEISEQEYFDNGILMVAMVRAGVELAFEAMTASGIIDESAYYESLHELPLIANTIARKRLYEMNVVISDTAEYGNYLFANVATPLLREKFMPSVGTDVIGKGLGETSNQVDNATLIAVNETIRNHPVEYIGEELRGYMTDMKRIAVGG

Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. (2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2-acetolactate + H(+) + NADPH (2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP(+) = (S)-2-ethyl-2-hydroxy-3-oxobutanoate + H(+) + NADPH Binds 2 magnesium ions per subunit. Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 2/4. Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 2/4. Belongs to the ketol-acid reductoisomerase family.

Q6CNR2

MTVSRLLKDRVRYAPYLKKVKPVEELIPLFKDGQYIGWSGFTGVGAPKAVPEALIKHVEENNLQGKLRFNLFVGASAGPEECKWAEHDMILRRAPHQVGKPIAKAINDGRIQFFDKHLSMFPQDLTYGYYSRNRTDGKILDYTIIEATAIKEDGSIVPGPSVGGSPEFISVSDKIIIEVNTATPSFEGLHDIDMPVNPPFRQPYPYTAVDQKNGLDSIPVDPERVVAVVESTQRDVVGPNTPSDATSQSIARHLVEFFENEVRHGRLPENLHPLQSGIGNIANAVIEGLTDSSFKNLTVWTEVLQDSFLDLFENGALDYATATSIRLTEAGFQKFFDNWDDFSKKLCLRSQVVSNNPELIRRLGVIAMNTPVEVDIYAHANSTNVSGSRMLNGLGGSADFLRNAKLSIMHAPAARPTKTDPTGISTIVPMASHVDQTEHDLDVLVTDQGLADLRGLSPRERAREIIKNCAHPDYQPILTDYLDRSEHYAKLHKCMHEPHMLKNAFKFHLNLSEKGTMKVDNWD

Presumably involved in regulating the intracellular acetyl-CoA pool for fatty acid and cholesterol synthesis and fatty acid oxidation. acetyl-CoA + H2O = acetate + CoA + H(+) Belongs to the acetyl-CoA hydrolase/transferase family.

Q1QSU9

MHAAVERFLHSLSGHASPATLDAYRRDLTALARFLEASGIDDWAALDVAQVRRFMGAERTRGLAPRSLARRRAALSRFADHLVRSGILDHNPVALTQTPRQPRHLPRPVDVDQLARFLDTPHDGTPLAVRDQAMLELFYSCGLRLAELTALDVTDLDARRLRVVGKGNKPRQMPIGRRAQAALADWYRLRGQLAGHDEPALFVGQRGARLGHRAVQKRLAQLARERGLAEHLHPHRLRHSFASHLLESSQDLRAVQELLGHANLSTTQVYTRLDWQHLADAYDQAHPRARRRAPPDDT

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.

Q70LM6

MSRKKVDNIYPLTPMQEGMLFHSLLDEGSESYFEQMRFTIKGLIDPAILEQSLNALIERHDILRTVFLLEKVQKPRQIVLRERKTKVQVLDITHLSEGEQAAYLEDFAQKDRQASFDLAKDVLIRLTLVRTSADTHTLFWSHHHILLDGWCIPIVLNDFFQIYQQRKGGLPVELGPVYPYSTYISWLGEQDAEEAKASWAEYISGYEPTSFIHKQGGKNSYRQAELVFAIEQGLTDSLNKLAKQLHVTLNNLFRAIWGLMLQRQCNTEDVVFGSVVSGRPSHLPNVEQMVGLFINTVPIRVQAGAEQTFSELVKQVQQEALSLAKYHYLSLADIQGNQQLIDHILLFQNYPMGQQFLTRLNQYNEEFTLTHLSAFEQTNYDLNVMVTPSDVITIKYIYNAAVFSEEQLLHISRQLTTIMTQVTNAPDILLQKLEVVDPAEKQLQLHSFNDTYRHYPTDKLIHQIFEERAEREPERIALVMGEQVLTYRELNEKANQLAKLLRARGIGPESMVSLLTERSAEMMIAILAIFKAGGAYLPIDPSHPKERIEYILQDSRSELLLVNHRFLGAVDFADRIIDLEAAEIYQGAADNLECVSHANHLAYVIYTSGSTGKPKGVMIEHASLLNIIFALQELYPLLENDAYLLKTTYTFDVSVAEIFGWILGSGRLVILDPGAEKEPAHIWETMVNHGVTHVNFVPSMLIPFVDYVRDQQQESPLRYIFAAGEAMPSELVGKVYEALPGVILENIYGPTESTIYATKYSLAKDSQDVLVPIGKPLANIQTHIVNKHGQLQPVGVPGELCIAGASLARGYWNNEALTNEKFVPHPFAAGQRMYRTGDLARYRQDGNIEYLGRIDHQVKIRGYRIELDEIRAQLIQEASIRDAVVIARTDHNGQAYLCAYFIADKQWTVNALREALRQTLPDYMVPSHFIQMEEFPLTSSGKIDRKALPLPDGRVHTGNVYLAPRNPVEELVVRIWEEVLNVSQVGVHDNFFELGGHSLLATQVLSRTAKLFHVRLPMREIFTHQTVAELARRIQALRHGAEADKHSPIQPSALQRADELPLSYAQQRLWFLDRLIPDSAMYNIPVGFRLRGTVDELVLERALNEIIQRHESLRTTFVDVDGRALQVIHTDVHLSLGVTDLRDKPAAAKDAEWKQMAEEDAATPFRLDQWPLLRAMLIRLEEQESVLWLNVHHIISDGWSMDVLVNELSEVYETLLKGEALPLAALPIQYRDYAVWQREKSQDDVWKEQLRYWKNKLDGSEPLLPLPTDRPRAVVQSYRGDHLSFYVPGEVGQKLRELGRQEGATLFMTLLAAFKSFLYRYTHANDILIGTPVAGRNRQEIENLIGFFVNMLVLRTDLSDDPTFVELLRRVRETAFDAFANEDVPFEKLVDELQIERSLSYSPLFQVLFAVQGMSTGVREGETLAIAPDEVTLNQTTKFDLTLTMIEAADNGLKGVFEYSTDLFDRTTIERMAEHFGNLLQAIAADPGQKIVELPLLGGAEQSRMLVEWNQTDVAYSLDLLVHERVARIAQELPEQFAVIGEQGALTYAQLDAKANQLAHALLKRGIGSEDLVGICVERSSEMQIGQLAILKAGAAYVPMDPAYPRERLAFMIKDAGMSLVLTQERLLDALPQEAAALLCLDRDWQEIAAESTAAPAIKTNADQLAYVIYTSGSTGTPKGVEIEHGSLLNLVNWHQRAYSVSAEDRASQIAGTAFDASVWETWPYLTAGATICQPREEIRLSPEKLRDWLVETGITISFLPTPLAENLLPLPWPTGAALRYMLTGGDTLHQYPTADVPFTLVNQYGPTENTVVATAGAVPVLGERESAPTIGRPIDNVSVYVLDENRQPVPVGVVGELYIGGKSLARGYRNRPDLTEASFVPNPFSPIEGARMYRTGDLVRYAADGSIEFIGRADDQVSIRGFRVELGEIESALYAHPAVAESVVIVREDVTPGVKRLVAYAVLHEGEERQTSELRQSLKEMLPDYMVPSAIVLMEALPLTPNGKVDRRALPLPDVAQTEWEGSFVEPQSDVERKLAEIWQEVLGVETIGVHDNFFELGGDSILTIQIVSRANQAGLQLTPKHLFDAQTLAELAASAVVLEKAPEMQAEQGIVTGELPLTPIQTWFFEQDVRHVHHWNQSVMLAVREELDMTALTQAFAALPRQHDALRLRFQQVNGTWQAAHGEIADEDVLLVADLSSVPEAEREARMRHITDELQASLDIEKGPLHRAAYFQLGAEQRLFIVIHHLVVDGVSWRIILEDLQTAYEQVKAGQKIAWPQKTTSFKSWAEELTTYAEQSAVDEYWTGMDSEQACGLPVDHPQGKNTEGLAVQVKAKLSADETRALLQEVPAAYRTQINDVLLSALTRTITDWTNKRALYVSVEGHGREPIVDGVDVSRTVGWFTSLYPVLLETEPDLAWGDLLKSIKEQVRAIPDKGIGYGIHRYLSRDGQTAEMLRAKPQPEISFNYLGQFGQGQTTDAALFQIIPNWSASNVSEDETRLYKLDVMSMVAQDQLEMSWTFSRDLYEPGTIEKLAHDYVQALRAIIAHCRTEQAGGYTPSDFPLAELDQNSLDKFIGHNRLIENVYTLTPLQEGMLFHSLYEQAGGDYVVQLALKLEHVNVEAFSAAWQKVVERHAILRTSFLWSGLEKPHQVVHAKVKTFVERLDWRHLTAAEQEAGLQTYLEQDRKRGFDLARPPLMRWTLIRLDASTFQFVWSFHHMLLDGWSTPIVFQDWQAFYAAASHGKEASLPAIPPFSAYIAWLKRQNLEEAQQYWRDYLQGFGVPTPLGMGKSGGSAGQPKEYADHKLLLSERATANLLAFARKHQLTLNTVVQGAWALILARYAGEAEVVFGTTNLGRPTDLPDAEAMVGLFINTLPVRVLFPEQTTVIDWLQSLQQAQSEMRQYEFTPLVDIQSWSEVPRGQSLFDSIFVFENYLSGTSVDSESGMLLGEVKAVEQTSYPLTLVVAPGEELMLKLIYETGRFEQPAMDKVLAQLSSVLEAIMREPHEQLADLSIITEAERHKLLVEWNATDMPYERNLVMHQLFEAQVEATPDAQALVVGTERLTYAELNKRANQLAHYLRAQGVGPEVLVAVLMERTTEMIVALLGIIKAGGAYVPIDPAYPQDRIGYTLDDSQAAIVLTQERLLPMLPEHTAQVICLDRDWACMAVQPEANVPNLAAPTNLSYVIYTSGSTGLPKGVAIQHSSVIAFIFWAKTVFSAEEMSGVLASTSICFDLSVYEIFVTLSCGGKVILADNALHLPSLPAAKEVTLINTVPSAAKELVRMNAIPPSVRVVNLAGEPLPNTLAQSLYALGHVQKVFNLYGPSEDTTYSTYVQVTKGAKTEPTIGRPLANTQAYVLDAKLQPVPLGLPGELYLGGDGLARGYLKRPKMTAERFLPNPFHPDPDARMYSTGDLVRYLPDGQLEYLGRIDHQVKIRGYRIELGELEAVLRSHPQIKEAVVVAKEDKLGEKRLVAYITTKDGECGDRAVLTSWAKAKLPEFMVPSFFVWLDAMPLTPNGKIDRKQLPEPEWGQVASAAGYVAPRNQTEVLVASIWADVLGIEQVGVHDNFFELGGHSLLATRVASRLRETFAKEVPIRAIFERPTVAELSETLGAIGQNETEAQMLPVSREAHLPLSFAQQRLWFLDRLMPDSTLYNIPSAVRLLGDLDIAAWEKSLQVLIQRHESLRTTFGDVDGEAVQVIHSRLDGKLNVIDLRGMPADEREAEAHRLAGLEAATPFDLSQGPLLRTTLIRLAEQECVFLFNLHHIIFDGWSIGIFLKEMRALYEAFVREEAPELAEITVQYADYAVWQRKWLEGEVLAEQLAYWKEKLSGAEPLLALPTDQPRPAVQTHDGAMHTIKLSGELYAKLNKLSQEEGATLFMTLLAAFQVLLYRYSGQEDILVGSPVAGRNRQETEPLIGFFINTLVLRTDLSGEPTFRELLARVRETAFEAYAHQDLPFEKLVDELELERSLSYSPLFQVMFVLQNFQLNLDEKAGIRVADFEMDKHLVTSKYDLTLTMAEKQNGLFATFEYNTALFHEATMERLSQHFIQLLEAIVHMPDQGIARLPLLNQSERAQLLVEWNDTTTAYPRNKRVDQLFRETALLYPERLAVVAGNQTLTYAELERRANQTANYLQQKGVRPGALVGLCVKRSLEMLIGMLGILKAGGAYVPLDPDYPEERLAYMMGDAGITVLLTQEQLMPGLPSGERTTIALDRDWPLIAKESEQAPDVDTTAESLAYVIYTSGSTGLPKGTLVVHRGIVRLVKETDYVTITEQDVFLQASTVSFDAATFEIWGSLLNGAKLVLLPPELPSLAEIGQAIQSHHVTTLWLTAGLFTLMVDHHKEYLSGVRQLLVGGDIVSVPHVKKALEIAGLTVINGYGPTENTTFTCCNPVTVMPESAHTFPIGRPIKNTTAYVLDRHMQPVPIGVTGELYIGGDGLAEGYLNRPDLTAERFVPNPFATDQAARLYRTGDLVRYLPDGLIEFIGRLDNQVKIRGFRIELSEVEAVLAKHPAITASVVIVHENEAGMKQLVAYAVKDAEQELGTAELRQHFKAHVPDYMVPAAFVMLDALPLTPNGKVDRKALPAPVLERSREEDAFAAATSHVEQTLADIWCAVLRMDRIGIHDNFFELGGDSILSIQIVARANKAGIHLTPKQLFDQQTIAELAKVAGQSTKVDAEQGNVTGEVPLLPIQTWFFEQKQPTPHHWNQSMLLQVNEPLEEECLSQAVAQLLAHHDALRLRYTFADGQWKQTYADVDSEVPLQVEDLSMSPPAQQARKIEKLAQQAQASLDLQNGPLLKVVYFDLGYDRPGRLLMVIHHLAVDGVSWRILIEDLQTAYGQAEKGNKIQLPPKTTSYKAWAEKLHKYASSERMLVDQDYWLKAADELSGHPLPVHDWAENTEANGRMWTIHLEEEETDALLQKVPSRYRVQINDILLTALALAYGKWTGESALLVNLEGHGREELFEDVDLSRTVGWFTSMYPLLIQLEPNTSSEDALARVKEKLQQIPHKGLGYGLLRYMAQDPELVEKLKAIPQAPLSFNYLGQFHQAADAKALLAYAEGERGANSGPDNRRTHLIDVVGAVTEGKLGLSFLYNGRLYSESHIETFARHYTDALQSLIQAEKQSYRAEDFEDADLSQSALNKVLARLKNRKGNELHGGSH

Activates the 3rd to 6th amino acids (Ala, D-Leu, Ala and D-Val) in linear gramicidin and catalyzes the formation of the peptide bond between them. This enzyme is also responsible for the epimerization of the 4th (D-Leu) and the 6th (D-Val) amino acids. Binds 4 phosphopantetheines covalently. Large multienzyme complex composed of 4 subunits; LgrA, LgrB, LgrC and LgrD. Four module-bearing peptide synthase with a C-terminal epimerization domain. Each module incorporates one amino acid into the peptide product and can be further subdivided into domains responsible for substrate adenylation, thiolation, condensation (not for the initiation module), and epimerization (optional). Linear gramicidin is a pentadecapeptide antibiotic produced during sporulation. Belongs to the ATP-dependent AMP-binding enzyme family.

A0A0N7KTZ5

MVKICCIGAGYVGGPTMAVIALKCPAIEVVVVDISKPRVDAWNSDQLPIYEPGLDEVVKECRGRNLFFSTDVEKHVAEADIIFVSVNTPTKTRGLGAGKAADLTYWESAARMIADVSKSDKIVVEKSTVPVKTAEAIEKILTHNSKGINYQILSNPEFLAEGTAIEDLFKPDRVLIGGRETPEGKKAVQALKEVYAHWVPEDRIITTNLWSAELSKLAANAFLAQRISSVNAISALCEATGANVSEVAYAVGKDTRIGPKFLNASVGFGGSCFQKDILNLVYICECNGLPEVANYWKQVIKINDYQKSRFVNRVVASMFNTVSGKKIAVLGFAFKKDTGDTRETPAIDVCHGLLGDKAQISIYDPQVTEDQIQRDLSMAKFDWDHPRHLQPTSPTAFKQVSVVWDAYEATKGAHGLCILTEWDEFKTLDYQRIFDNMQKPAFVFDGRNVVDPEKLREIGFIVYSIGKPLDAWLKDMPAVA

Involved in the biosynthesis of UDP-glucuronic acid (UDP-GlcA), providing nucleotide sugars for cell-wall polymers. H2O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH + UDP-alpha-D-glucuronate Nucleotide-sugar biosynthesis; UDP-alpha-D-glucuronate biosynthesis; UDP-alpha-D-glucuronate from UDP-alpha-D-glucose: step 1/1. Belongs to the UDP-glucose/GDP-mannose dehydrogenase family.

C4GS13

MKIKTRFAPSPTGYLHVGGARTALYSWLFSRHLGGEFVLRIEDTDLGRSTQEAIDAIMDGMNWLNLDWDEGPYFQTKRFDRYNAVIDQMLDAGTAYRCYCSKERLEALREAQMANGEKPRYDGHCRDSQCTHGADEPSVVRFRNPQEGSVIFDDKIRGPIEFSNQELDDLIIRRTDGSPTYNFCVVIDDWDMEITHVIRGEDHINNTPRQINILKALGAPVPEYAHVSMILGDDGKKLSKRHGAVGVMQYRDDGYLPEALLNYLVRLGWSHGDQEIFSIEEMTQLFTLDAVSKSASAFNTEKLQWLNHHYINSLPPEQVAVHLSWHVEQLGIDTRNGPELVEIVKLLGERCKTLKEMAESCRYFYEEFDAFDVDAAKKHLRPIARQPLEAVKVKLAAITEWTTENVHNAIQGTADELGVGMGKVGMPLRVAVTGVGQSPGMDVTVHAIGQARTLARIDKALAFISEREAQQ

Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu) Binds 1 zinc ion per subunit. Monomer. Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily.

A0R8B4

MKDIATPNRTKDIVEKYGFSFKKSLGQNFLIDTNVLNRIVDHAEIGSESGAIEIGPGIGALTEQLAKRAKKVVAFEIDQRLLPILDETLAPYGNVTVINKDVLKADVHEVFSEQFEEGQDVMVVANLPYYITTPILFKLLEEKLPVRGFVVMMQKEVGDRLAAKPGTKEYGSLSIAIQYYTEVETVMTVPRTVFVPQPNVDSAIIRLLKRPKPVVEVTDEIFFFEVVRASFAQRRKTLMNNLSNNLNGFPKDKELLDRILTEVGIDPKRRGETLSIEEFATLSNALVLHKLS

Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits. adenosine(1518)/adenosine(1519) in 16S rRNA + 4 S-adenosyl-L-methionine = 4 H(+) + N(6)-dimethyladenosine(1518)/N(6)-dimethyladenosine(1519) in 16S rRNA + 4 S-adenosyl-L-homocysteine Belongs to the class I-like SAM-binding methyltransferase superfamily. rRNA adenine N(6)-methyltransferase family. RsmA subfamily.

Q8LFX6

MANMNALQQMIFPDENAPIHRKKSVTAASVKSKGTVLGQKKPGGARKALNDITNKSGIHAKAAASSKNKQIASAAVKEIDIAGERFLHDHSKCIKEQQNLWDDHYSADLMLLHHGSSIKEKHLNWDIEKMDAKDDLTYEEPEEMASPKFSDWLKNSTPWRSPIRHGSMMPSTPLAWRFDSCEFTLKEDSDDLF

Required for the maintenance of centromeric cohesion during interkinesis, until meiosis II (PubMed:24206843, PubMed:26272661). Required for regular configuration and segregation of sister chromatids in meiosis II (PubMed:24506176). Also required for centromere cohesion during meiosis I (PubMed:26272661). Involved in spindle organization at the end of telophase I and in meiosis II (PubMed:24506176). Required to prevent precocious release of pericentromeric cohesins during meiosis, but not for cohesion establishment and monopolar orientation of kinetochores at meiosis I (PubMed:24206843). Involved also in somatic development (PubMed:24206843). Regulates mitotic cell division and ploidy stability in somatic cell types (PubMed:24506176). May be involved in the organization of microtubules dynamics (PubMed:24506176). Involved in abiotic stresses and mono- or divalent ions tolerance and may play a role in maintaining meristematic activity under saline conditions (PubMed:24134393). PANS1 and GIG1 are part of a network linking centromere cohesion and cell cycle progression through control of APC/C activity (PubMed:26272661). Regulates the number of dividing cells in root meristem and is necessary for the anaphase onset control through an APC/C-mediated pathway (PubMed:26261921). Involved in maintaining correct chromosome arm cohesion under stress conditions (PubMed:26261921). Interacts directly with the anaphase promoting complex/cyclosome (APC/C) through the CDC27B and CDC20-1 subunits. Excluded from the nucleolus. Expressed in somatic and reproductive tissues (PubMed:24206843). Expressed in inflorescence, young buds, roots and basal portion of young leaves (PubMed:26272661). Expressed in proliferating cells such as apical meristems of roots and shoots, expanding cotyledons and leaves, root vascular tissues, and in stomatal precursor cells (PubMed:26261921). Cell cycle regulated with a peak at late M/early G1 phase mitosis (PubMed:24206843). Peak of expression during metaphase (PubMed:26261921). Strongly expressed up to mid-prophase I and decreases during late prophase (PubMed:26272661). Not induced by stress (PubMed:26261921). The DEN-box is not essential for the meiotic function. Reduced fertility when homozygous (PubMed:24206843, PubMed:24506176). High level of gametophytic aneuploidy (PubMed:24506176, PubMed:26272661). Occurrence of split sister centromeres at metaphase I (PubMed:26272661). Pans1 and pans2 double mutants are lethal when homozygous (PubMed:24206843). Increased mono- or divalent ions sensitivity resulting in primary root growth inhibition and increased lateral root density (PubMed:24134393). Hypersensitivity to microtubule-depolymerizing drugs and higher frequency of anaphase bridges under stress conditions (PubMed:26261921). Patronus is Latin for protector.

B2V1T2

MKVILLQDVKKIGKKGEVIEASDGYARNFLFPRKLAQEATDSNMHILNNKKENERKKKLAEIEAAQKLAGELKGKEITIKTKIGESGKLFGAITSKDIASLIKTQYNVEIDKKKIVMDTIKLAGNYDIEVKLYPEVSTKMKVNILPQ

Binds to the 23S rRNA. Belongs to the bacterial ribosomal protein bL9 family.

A1W2T4

MAELATIARPYAEALYKACTDQAGVDLNGATAWVDELAAIAANPQLRQLADNPKVTGEQVFDVIVGVARSALPDLAKNFLRTVIDNGRVQALPEIAAQFRTLVNRSHGTSDAVVYSAFPLDAGALTDVGATLEKRFGRKLNLSVQLDETLIGGVRVVVGDEVLDTSVKARLEQMKAALTA

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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. 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 delta chain family.

O25788

MQKTSNTLALGSLTALFFLMGFITVLNDILIPHLKPIFDLTYFEASLIQFCFFGAYFIMGGVFGNVISKIGYPFGVVLGFVITATGCALFYPAAHFGSYGFFLGALFILASGIVCLQTAGNPFVTLLSKGKEARNLVLVQAFNSLGTTLGPIFGSLLIFSTTKMGDNASLIDKLADAKSVQMPYLGLAVFSLLLALIMYLLKLPDVEKEMPKETTQKSLFSHKHFVFGALGIFFYVGGEVAIGSFLVLSFEKLLNLDSQSSAHYLVYYWGGAMVGRFLGSVLMNKIAPNKYLAFNALSSIVLIALAIIIGGKIALFALTFVGFFNSIMFPTIFSLATLNLGHLTSKASGVISMAIVGGALIPPIQGAVTDMLTATESNLLYAYGVPLLCYFYILFFALKGYKQEENS

Intake of glucose and galactose. Belongs to the major facilitator superfamily. FHS transporter (TC 2.A.1.7) family.

B3M8G0

MMIWVPALIFLSACLLPRSNGTPLEWDFAVTLRTKIQFLDSSWQTIATAAHEFDELSALTFDESEELIYFNDRQHQNGSIFSLRRDAYAASHVAQQAIQRTGNESVGGLAYDPLNRNLFWSDTLQRKIFFASIDSPPSQPPKVLVDLSQEGARPEGVAVDICRRKLYWTNSNITHPTVERIDVDGSNRVIIADSDIDMPKGIVVDQLSDRLFWIDDLKGVFFAVMSSNLDGSDRQVVLKDKHHEPQNLALTNDAIFWTDRTTKAVWSHPKRAAVKATTTVRPEVESSTDGTESESKQESEPVEDCPLVRVANLSEEARGIVARTGFYQRLQKDAHCSSIVRKIKLRLDEMSEKKEVRSLVDERMDQLERDHCMNGGSYISKRDLCICPAGFKGSRCEIRECHNYCVHGTCQMSDLAYPKCYCQPGFTGERCEVSNCAGLCLNGGHCRLGETEKDQPSCECPANFAGERCEQNSTQICSLFCRLLKHEPEIHVPFGCHDICEELALDNSTNIAIPQYQHLEVCQTPFVWTSSVIIILVVGIVFSLLLITTIIHGIRRLYKPKRPRIRKTFVVRKQPRTNSAGDTPLTNRPMTAEQCEITIENCCNMNICETPCFDPKLVEQTLAKSSCKEDKKILIHNMEDDLY

Has a role in spermatogenesis and oogenesis. Belongs to the cueball family.

Q9W743

MSSTVSLLFCCLFLQLCPSAQQYHGEKGISVPDHGFCQPISIPLCTDIAYNQTIMPNLLGHTNQEDAGLEVHQFYPLVKVQCSPELRFFLCSMYAPVCTVLEQAIPPCRSLCERARQGCEALMNKFGFQWPERLRCENFPVHGAGEICVGQNTSDNSPSGPTARPSPYLPDSITFQPHPHRDFTCPRQLKVPPYLAYRFLGEKDCGAPCEPGKANGLMYFKEEEVRFARLWVGIWAILCCISTLFTVLTYLVDMRRFSYPERPIIFLSGCYFMVAVAYTAGFLLEERAVCVERFSEDSYRTVAQGTKKEGCTILFMILYFFGMASSIWWVILSLTWFLSAGMKWGHEAIEANSQYFHLAAWAVPAVKTITILAMGQVDGDVLSGVCYVGINSVDSLRGFVLAPLFVYLFIGTSFLLAGFVSLFRIRTIMKHDGTKTEKLEKLMVRIGVFSVMYTVPATIVLACYFYEQAFRDTWEKTWLVQTCKGYAVPCPNYNFAPMSPDFTVFMIKYLMTMIVGITSSFWIWSGKTLQSWRRFYHRLSNGSKGETAV

Receptor for Wnt proteins. Acts in both canonical and non-canonical Wnt pathways. Although different papers report differing Wnt preferences, wnt5a, wnt8b and wnt11 have been proposed as synergists. In the canonical Wnt pathway, acts via beta-catenin to promote the expression of the dorsal genes siamois, twin and nodal3 and to establish the dorsal axis of the embryo and induce dorsal mesoderm formation. In a non-canonical Wnt/planar cell polarity (PCP) pathway, acts with sdc4 and dvl2/dsh to regulate convergent extension cell movements during gastrulation. Triggers phosphorylation of dvl2/dsh and its translocation to the plasma membrane. In a third branch of Wnt signaling, acts in a non-canonical pathway via trimeric G proteins, and independently of dvl2/dsh, to recruit protein kinase C (PKC) to the membrane and thus activate PKC. PKC signaling controls cell sorting and tissue separation during gastrulation. Interacts with wnt11 and sdc4. The extracellular domain interacts with the extracellular domain of pcdh8/papc. Associated to the plasma membrane in the presence of FZD7 and phosphatidylinositol 4,5-bisphosphate (PIP2). Localized in recycling endosomes in other conditions. Expressed in the animal region of cleavage stage embryos. During gastrulation, broadly expressed on the dorsal side of the embryo in deep mesodermal cells surrounding the blastopore lip and in presumptive anterior neuroectoderm. During neurulation, becomes progressively more restricted to the dorsal epidermis, neural plate, and neural tube. Expressed in the cranial neural crest of neurulae and tailbud embryos as well as the pronephros of tailbud embryos. Localized to the brain of neurulae, tailbud embryos and tadpoles. In tadpoles, strongly expressed in the eye and developing heart. Expressed both maternally and zygotically. Expressed at low levels during cleavage stages, with zygotic expression increasing at the start of gastrulation, remaining constant through the gastrulation stages and then decreasing from late neurula stage onwards. Lys-Thr-X-X-X-Trp motif interacts with the PDZ domain of Dvl (Disheveled) family members and is involved in the activation of the Wnt/beta-catenin signaling pathway. The FZ domain is involved in binding with Wnt ligands. The extracellular domain interacts with Wnt proteins and the intracellular C-terminus transmits the Wnt signal. Belongs to the G-protein coupled receptor Fz/Smo family.

D9PU59

MKEVIAIIRPKNMKKTRDVLESLGFPSFNATRVLGRGKQRAIIDEVTIPSPSPEIDEVRGTMRYIPKRMIQITVEDPDVQLVVEAIMKVNHTGKIGDGKIFVCPVDDAMRIRTGDRGTEAL

Could be involved in the regulation of nitrogen fixation. Belongs to the P(II) protein family.

B7ZUY4

MKRRNADCSKLRRPLKRNRITEGIYGSTFLYLKFLVVWALVLLADFVLEFRFEYLWPFWLFIRSVYDSFRYQGLAFSVFFVCVAFTSDIICLLFIPVQWLFFAASTYVWVQYVWHTERGVCLPTVSLWILFVYIEAAIRFKDLKHFHVDLCRPFAAHCIGYPVVTLGFGFKSYVSYKMRLRKQKEVQKENEFYMQLLQQALPPEQQLIQRQEREAEEAAAAAAAAASKSIHDVDSPAVAQNGSAGGKKPSSNTLPELEYREKERGKNESKKQHNHNQNHHSSTSSSILPSVDNKAQEMEYMENHVNSKRLSSSDLLGSTENLLKDEHSSSSSSSTSSNSNKNYKNASGGGGGGGSSSPRGHGTANGSVPSSSGPSSSASSSSKGDRKQKYGGGKNSASHRDPVENCIPNNQLSKPEALVRLEQDVKKLKADLQASRQTEQDLRSQLGSLGTSERSIRSELGQLRQENELLQNKLHNAVQAKQKDKQTLGQLEKRLKAEQEARAAAEKLLAEEKKRKKLEEATAARAVALAAATRGECTESLRRRISELEAECKKLTLDIKVKEDQIRELELKVQELHKYKENEKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQKIAEVMAVMPSVVYSADTGSMTPVTPHYSSKFMDTSPSGLDPNASVYQPLKK

May play a role in the regulation of neuronal activity. Belongs to the macoilin family.

Q31GJ9

MSKFIKSFQYGKHEVRFETGEIARQADGAVMVAMGDTQLLVTVVGAKNAKAGQDFFPLTVQYQEKAYAAGRIPGGFLKREGRPSEKETLTSRLIDRPIRPLFPKGFMNEVQVIATVVSLDPEIGTEVPAMLGTSAALSISGIPFDGPIGAAVVGYKDNDYILNPSSQELQESDLELSVAGTSDAVLMVESEASELSEEIMLGAVMFGHEQMQVAIDAIKELKAEVGKPAWNWEAAEEDIDLKTKVFDAIRSDIEAAYDIADKMDRYAAIDAAKTKVMEALAATEENPEGYDAGDIEKMVGKLQKEIVRGRIIAGEPRIDGRDTQTIRSIDCQVGILPKVHGSALFTRGETQAIVVTTLGTEKDAKMVDDLTGSYNDRFMLHYNFPPYSVGECGRVGSPGRREIGHGMLARRGVAALLPTADEFPYTIRVVSEITESNGSSSMATVCGTSMSLMHAGVPLAAPIAGIAMGLVKEESGFAVLSDILGDEDHLGDMDFKVAGTEQGVTALQMDIKITGITQEIMHIALKQAKEGRLHILKEMEKAIGSSNQDVATTAPRFFTVKVKPEKVREIIGKGGATIRSITEETGVTIEIDDDGNVKIAAVDDESANAAKARIAEITAEPEIGKVYDAKVVKIVDFGAFVSYMPGREGLVHVSQIADERVEDVNEYLKEGQEIKVRLTDVDKQGRVKLSIKAV

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) Component of the RNA degradosome, which is a multiprotein complex involved in RNA processing and mRNA degradation. Belongs to the polyribonucleotide nucleotidyltransferase family.

G3HE95

MGAAAWAPPHLLLRVSLLLLLLLPLRGRLAGSWDLAGYLLYCPCMGRFGNQADHFLGSLAFAKLLNRTLAVPPWIEYQHHKPPFTNLHVSYQKYFKLEPLQAYHRVISLEEFMEKLAPIHWPPEKRVAYCFEVAAQRSPDKKTCPMKEGNPFGPFWDQFHVSFNKSELFTGISFSASYKEQWIQRFPPEEHPVLALPGAPAQFPVLEEHRALQKYMVWSDEMVKTGEAQISTHLIRPYVGIHLRIGSDWKNACAMLKDGTAGSHFMASPQCVGYSRSTATPLTMTMCLPDLNEIQRAVKLWVRALNARSIYIATDSESYVPEIQQLFKEKVKVVSLKPEVAQVDLYILGQADHFIGNCVSSFTAFVKRERDLHGRQSSFFGMDRPSQPRDEF

Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue found in the consensus sequence C2-X(4,5)-[S/T]-C3 of EGF domains, where C2 and C3 are the second and third conserved cysteines. Specifically uses GDP-fucose as donor substrate and proper disulfide pairing of the substrate EGF domains is required for fucose transfer. Plays a crucial role in NOTCH signaling. Initial fucosylation of NOTCH by POFUT1 generates a substrate for FRINGE/RFNG, an acetylglucosaminyltransferase that can then extend the fucosylation on the NOTCH EGF repeats. This extended fucosylation is required for optimal ligand binding and canonical NOTCH signaling induced by DELTA1 or JAGGED1 (By similarity). Fucosylates AGRN and determines its ability to cluster acetylcholine receptors (AChRs) (By similarity). GDP-beta-L-fucose + L-seryl-[protein] = 3-O-(alpha-L-fucosyl)-L-seryl-[protein] + GDP + H(+) GDP-beta-L-fucose + L-threonyl-[protein] = 3-O-(alpha-L-fucosyl)-L-threonyl-[protein] + GDP + H(+) Activated by manganese and, to a lesser extent, by other divalent metals such as cobalt and calcium. Inhibited by copper, ferric and zinc ions. Optimum pH is 5.5-8.0. Protein modification; protein glycosylation. N-glycosylated. Contains high mannose-type carbohydrates. Belongs to the glycosyltransferase 65 family.

Q4V6V6

MHTDIIIGDQFAANNNYWVMQSPELDYRHELMGRLHKIEPADVELEVLAAAAAAANNNNNTSSNNNHSSNSSSNNSNGSQTPNGNNNSSLATGGHQHHQFHHHLHHHHSHQHHHQHHHLHQHHSHSLQSGESGASEAWPHLPAPSYASDVPHAQQQQLQPAGSPNSNSNGAYGCAPLYDGAPYEVALGYGGAVVASTGGATSSDKEYLYETKNKEALYADPLDDPYQRPVLWDDITTSIQNIDPENALMLSSSGSSNNNGSSNSSSNTGESATSQLPQVKMEAIDESLLETFSTPLLSPLEIKTEKQQRQQQHQHQQQQQQQQQQQQQHQQQHQQQYQQQHYQQHYQQQHLYQHHPSLALPGLPPAVDVVELQLQQQHQQQQHLQHNNSSSSSPKLATPGDNSGNTSSYQQQYASQLVSGSGGGYLNGSSSNSYGYSWHSSQSFHTKYQIHPPSAAASATASATATPTAQLGAQQQQQQQQQQQLQQLCPPAAPSTPSTSSSSISSSSASSASRHMFVPPLTPPSSDPGSPGSSMVAAAAAAAAQRRTTPPPPYQQGHVMGLINPPPTLQLLGGAATGSNNSCTTTLTTLTPASAIQQQQQQPQQQQVPQQQPPPTPRSSGGGRRGRHSHHQPGTAAHIASLMSVRTVRYNRRNNPELEKRRIHHCDFVGCSKVYTKSSHLKAHQRIHTGEKPYTCQWPECEWRFARSDELTRHYRKHTGAKPFKCIVCERSFARSDHLALHMKRHLPKNK

Transcriptional regulator which promotes dendrite growth by suppressing, either directly or indirectly, the expression of the microtubule-severing protein spas (PubMed:21368042). Determines multipolar neuron morphology in postmitotic neurons by positively regulating the expression of genes involved in nuclear positioning including several dynein genes and the nuclear migration protein nudC (PubMed:26490864). Highly enriched in the peripheral nervous system but is absent from the central nervous system (PubMed:21368042). Expressed in neurons with more than one dendrite including da neurons, bd neurons and the dmd1 neuron but undetectable in neurons with single dendrites such as external sensory organ neurons and chodonotal neurons (PubMed:26490864). Severely reduced growth of microtubule-based dendritic branches and elevated levels of microtubule-severing protein spas (PubMed:21368042). Gradual conversion of multipolar neurons into the bipolar or unipolar morphology (PubMed:26490864). Belongs to the krueppel C2H2-type zinc-finger protein family.

A7H3M3

MYRFAPSPTGDMHIGNLRAAIFNYICARQKNMDFILRIEDTDKSRNIKGKEEEIKEILNLFGISWQHYYIQSENLKFHRQMALKLVSEKKAFACFCTEEELEAKKELAKKQGKAYRYDGTCEKLADIDVLECEKSFVIRLKKPTHTMKFTDFIKGELSFEPENIDSFVIMRTDKTPTYNFACAVDDMLENVTCIIRGEDHVSNTPKQEHIRASLGYDKAMTYAHLPIILNEEGVKMSKREAHSSVKWLLESGILPSAITNYLIMLGNKTPYEIFTLEEAIKWFDISKVSKAPARFDLKKLLQINREHIKMIKDDELNKILDLNKDLAQLAKFYTQEASTIKELKEKMRAIFNTKDFGEFETECKILKELLKDIELFENYEDFKNKLLNKSSLKGKKFFMPLRIILTGNIHGPELSDLYPYIKNFIHELARI

Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu) Monomer. Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily.

P19364

ALTALEKQSIQDIWTILKAVGLEFLQVKMFGKLFADHPEYKAHFDNFLTAIFSVAEDLVPKLRAHLHRVIDAFDLVIFALGRESLRGSLKDLGIFHTGRDIVDPVESLTGFKLMVAVIEEGLDTFRAVPEYSKGLEGRFGNVDNINENAPFR

Artemia hemoglobin is a dimer of two similar sized subunits. Each subunit represents a globin chain which exists in two forms (alpha and beta), thus making possible three different phenotypes (HB1, alpha(2), HB2, alpha/beta, HB3, beta(2)). The globin chain is a polymer of eight heme-binding covalently linked domains. Belongs to the globin family.

Q48C80

MLIIPAIDLKDGACVRLRQGRMEDSTVFSDDPVAMAAKWVDGGCRRLHLVDLNGAFEGQPVNGDVVTAIARRYPNLPIQIGGGIRSLETIEHYVKAGVSYVIIGTKAVKEPEFVAEACRAFPGKVIVGLDAKDGFVATDGWAEVSSVQVIDLAKRFEADGVSAIVYTDIAKDGMMQGCNIPFTAALAAATRIPVIASGGIHNLGDIQALLNAKAPGIIGAITGRAIYEGTLDVAEAQALCDREQR

1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide = 5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9. Belongs to the HisA/HisF family.

Q5PQL7

MVKISFQPAVAGVKAEKADKAAASGPASASAPAAEILLTPAREERPPRHRSRKGGSVGGVCYLSMGMVVLLMGLVFASVYIYRYFFLAQLARDNFFHCGVLYEDSLSSQIRTRLELEEDVKIYLEENYERINVPVPQFGGGDPADIIHDFQRGLTAYHDISLDKCYVIELNTTIVLPPRNFWELLMNVKRGTYLPQTYIIQEEMVVTEHVRDKEALGSFIYHLCNGKDTYRLRRRATRRRINKRGAKNCNAIRHFENTFVVETLICGVV

Negative regulator of amyloid-beta peptide production. May inhibit the processing of APP by blocking its access to alpha- and beta-secretase. Binding to the beta-secretase-cleaved APP C-terminal fragment is negligible, suggesting that ITM2C is a poor gamma-secretase cleavage inhibitor. May play a role in TNF-induced cell death and neuronal differentiation (By similarity). Interacts with BACE1. Interacts with APP. Interacts with STMN2 (By similarity). Type I membrane-bound, as well as soluble, furin has a pre-eminent role in ITM2C proteolytic processing. PCSK7 and PCSK5 may also be involved although to a lesser extent. The soluble form of PCSK7 is incapable of processing ITM2C. Fails to undergo shedding by ADAM10 and intramembrane cleavage by SPPL2B (By similarity). Belongs to the ITM2 family.

P49785

MLKKQTVWLLTMLSLVVVLSVYYIMSPESKNAVQMQSEKSASDSGEVATEKAPAKQDTKEKSGTETEKGKEDGTKGTKDSSADKETSAEASEKGTVVTETADDDLFTTYRLDLEDARSKEREELNAIVSSDDATAKEKSEAYDKMTALSEVEGTEKQLETLIKTQGYEDALVNAEGDKINITVKSDKHSKSKATAIIDLVAKEIKTMKDVAVTFEPSK

Involved in forespore engulfment. Forms a channel with SpoIIIAH that is open on the forespore end and closed (or gated) on the mother cell end. This allows sigma-E-directed gene expression in the mother-cell compartment of the sporangium to trigger the activation of sigma-G forespore-specific gene expression by a pathway of intercellular signaling. Interacts with SpoIIQ. Localizes to the engulfing septal membranes during spore formation. Specifically expressed in the mother cell during sporulation under the control of the sigma-E factor.

Q0I8Z9

MAQPRIGQTVVVDVPATTANIGPGFDCLGAALDLNNRFTMRRIDGDGERFELIIEGQEGSHLRGGPDNLVYRAAQRVWKAAGQEPIAIEARVRLAVPPARGLGSSATAIVAGLVGANALVGEPLSREKLLELAIDIEGHPDNVVPSLLGGLCMTAKAASQRWRVVRCEWMHSIKAVVAIPAIRLSTSEARRAMPKSVPVGDAVVNLGALTLLLQGLRTGNGDLISDGMHDRLHEPYRWRLIKGGQEVKEAALSAGAWGCAISGAGPSILALCSEERGPAVSHAMVKAWEAAGVASRAPLLNLQTAGSHWQPKDAE

Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate. ATP + L-homoserine = ADP + H(+) + O-phospho-L-homoserine Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 4/5. Belongs to the GHMP kinase family. Homoserine kinase subfamily.

Q9IA24

MSSYFVNPTFPVSLPSGQDSFLGQIPLYTTGYDALRHFPASYGAATLQDKSYSSPCYYQQSNSVIACNRASYDYGASCFYPEKDLASVSPSGSGKHRAQDDFFSSDQHYKPDCAQNKILSEEGNDRKYSTPIYPWMQRMNSSSSSVFGPHGRRGRQTYTRFQTLELEKEFHFNRYLTRRRRIEIANALCLTERQIKIWFQNRRMKWKKENKLLNTTESNSEEAEDKTGE

Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Belongs to the Antp homeobox family.

A4SV19

MLLIPAIDLKDGHCVRLEQGDMDKATVFSEDPGAMAAHWISKGARRLHLVDLNGAFAGKLKNESAIKSILKAVGNEIPVQLGGGIRDLETIERLLDDGISTVIIGTAAVKNPGFVQDACTAFPGHVMVGLDARDGKVATDGWSKITGHEVIDLAKKFEDWGVEAIIYTDIGRDGMLKGVNIEATMKLAQAIRIPVIASGGLSNNQDIEALCKAEEEGVMGVIAGRSIYAADLDLAAAQKYADELTLKYAKKII

1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide = 5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9. Belongs to the HisA/HisF family.

Q8XD03

MSVIKMTDLDLAGKRVFIRADLNVPVKDGKVTSDARIRASLPTIELALKQGAKVMVTSHLGRPTEGEYNEEFSLLPVVNYLKDKLSNPVRLVKDYLDGVDVAEGELVVLENVRFNKGEKKDDEILSKKYAALCDVFVMDAFGTAHRAQASTHGIGKFADVACAGPLLAAELDALGKALKEPARPMVAIVGGSKVSTKLTVLDSLSKIADQLIVGGGIANTFIAAQGHDVGKSLYEADLVDEAKRLLTTCNIPVPSDVRVATEFSETAPATLKSVNDVKADEQILDIGDASAQELAEILKNAKTILWNGPVGVFEFPNFRKGTEIVANAIADSEAFSIAGGGDTLAAIDLFGIADKISYISTGGGAFLEFVEGKVLPAVAMLEERAKK

(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5. Monomer. Belongs to the phosphoglycerate kinase family.

G8ZI35

MPELNFRAIEEKWQKRWLEAKVFEPNIKDKPKEKKFYITVAFPYLSGHLHVGHARTYTIPDVIARFKRMQGYNVLFPMGWHITGSPIVGIAERIKNRDPHTIWIYRDVYKVPEEILWTFEDPVNIVKYFMKAAKETFIRAGFSVDWSREFYTTSLFPPFSKFIEWQFLKLKEKGYIVKGAHRVRWDPVVGTPLGDHDLMEGEDVPILEYVIIKFELKEGDETIYLPAATLRPETVYGVTNMWINPNATYVKAKVKRGGKEETWIISKEAAYKLSFQDREIEVIEEFKGEKLIGKYVRNPVTGDEVIILPAEFVDPDNATGVVMSVPAHAPFDHVALEDLKRESEILVKYDIDPRIVEEITYISLIKLEGYGEFPAVEEVQKLGIKSQKDREKLEQATKTIYKAEYHKGIFKVPPYDGKPVQEVKELIAKEMMEKGIAEIMYEFAEKNVISRFGNRAVIKIIHDQWFIDYGNSEWKEKARKALARMKIYPETRRAQFEAIIDWLDKKACARKVGLGTPLPWDPEWVIESLSDSTIYMAYYTISRHINRLREEGRLDPEKLTPEFFDYIFLEEFSEEREKELEKKTGIPAEIIHEMKEEFEYWYPLDWRCSGKDLIPNHLTFFIFNHVAIFREEHWPKGIAVNGFGTLEGQKMSKSKGNVLNFIDAIEENGADVVRLYIMSLAEHDSDFDWRRKEVGKLRRQLERFYELISQFAEYEAKENVELKTIDKWLLHRLNKAIEGTTKALEEFRTRTAVQWAFYSIMNDLRWYMRRTEGRDDEAKRFVLRKLADIWVRLMAPFTPHICEELWEKLGGEGFVSLAKWPEPVDEWWNEEVEVEEDFIKSLIEDIKEIIEVAKIESPKRAYIYTAPEWKWKVYEVVAEKREFKSAMAELMKDEEIRKHGKEVAKLVQAIIKERAFDVKRIDEEKVLRESKDFLEKELGLEVIINPEEDKGGKKRQAIPLKPAVFIE

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

O04058

MENGTHVNGSANGFCIKDPLNWGVAAEALTGSHLDEVKKMVGEFRKPVVKLGGETLTVSQVAGISAAGDGNMVKVELSEAARAGVKASSDWVMESMNKGTDSYGVTTGFGATSHRRTKNGGALQKELIRFLNAGIFGNGTESSHTLPHSATRAAMLVRINTLLQGYSGIRFEILEAITKFLNNNITPCLPLRGTITASGDLVPLSYIAGLLTGRPNSKAVGPAGEVLNAESAFAQAGVEGGFFELQPKEGLALVNGTAVGSGMASMVLFEANVLALLSEVLSAIFAEVMQGKPEFTDHLTHKLKHHPGQIEAAAIMEYILDGSDYVKAAQKVHEMDPLQKPKQDRYALRTSPQWLGPQIEVIRSATKMIEREINSVNDNPLIDVSRNKALHGGNFQGTPIGVSMDNTRLAIAAIGKVTIAQFSELVNDFYNNGLPSHLSGGRNPSLDSGFKGGEIAMASYCSELQFLANPVTNHVQSAEQHNQDVNSLGLISARKTAEAVDILKLMSSTYLVALCQSIDLRHLEENMKSTVKNTVSQVAKKVLTMGVNGELHPSRFCEKDLLRVVDREYVFAYADDPCLTTYPLMQKLRQVLVDHALNNGETEKNANTSIFQKIATFEDELKAILPKEVESVRVAFENGTMSIPNRIKACRSYPLYRFVREELGGAT

This is a key enzyme of plant metabolism catalyzing the first reaction in the biosynthesis from L-phenylalanine of a wide variety of natural products based on the phenylpropane skeleton. L-phenylalanine = (E)-cinnamate + NH4(+) Phenylpropanoid metabolism; trans-cinnamate biosynthesis; trans-cinnamate from L-phenylalanine: step 1/1. Homotetramer. Contains an active site 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ala-Ser-Gly. Belongs to the PAL/histidase family.

B0TYI2

MLHYPQIDPVALHLGPIKVHWYGLMYLFGIFAGWYLLRYRAKVKSWAPIKPEQAGDLTFYIALGVILGGRIGYIIFYNLPYYFHNPLQMFFLWDGGMSFHGGFIGVLIAFALYARKLGVNFFDLGEFVAPVVPIGLGAGRIGNFINGELWGKVTDSPIGMIFPTGGPLPRYPSQLFEFFLEGVVLFTVLWLVSIKKRPRYLILGLFMFLYGSARFICEFFRQPDPQYGYIFFNWMTMGQILSIPMIVLGAIILIIVFIRTRKNKCENI

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.

Q14BI1

MDLHQSPTARLLQKWCSHESPFGCRRHYNSRKKLKLIRVIGLVMGLVAVSTVPFSISAFTETDSQSNRGEASDMSGPRVAQGHRQRTLLDLNDKIRDYTPQPPASQEDQAENSTEHTQGDYPKDIFSLEERRKGAIILHVIGMIYMFIALAIVCDEFFVPSLTVITEKLGISDDVAGATFMAAGGSAPELFTSLIGVFIAHSNVGIGTIVGSAVFNILFVIGMCALFSREILNLTWWPLFRDVSFYIVDLLMLITFFLDNVIMWWESLLLLTAYFAYVVFMKFNVQVERWVKQMISRNNVIKVTVPEAQAKSPTAGDKDGPTLPSKPRLQRGGSSASLHNSLMRNSIFQLMIHTLDPLAEELGSYGKLKYYDTMTEEGRFREKASILHKIAKKKCQVDENERQNGAANHVEKIELPNSTSTEVEMTPSSEASEPVQNGNLSHNIEAADAPKATETAEEEDDQPLSLSWPTNTRKQATFLIVFPIVFPLWITLPDVRKPASRKFFPITFFGSITWIAVFSYLMVWWAHQVGETIGISEEIMGLTILAAGTSIPDLITSVIVARKGLGDMAVSSSVGSNIFDITVGLPLPWLLYTIIHRFSPVTVSSNGLFCAIVLLFIMLLFVILSIALCKWRMNKILGFIMFGLYFVFLVVSVLLEDKVLVCPVSI

Calcium, potassium:sodium antiporter that transports 1 Ca(2+) and 1 K(+) in exchange for 4 Na(+) (By similarity). Required for learming and memory by regulating neuronal Ca(2+), which is essential for the development of synaptic plasticity (PubMed:16407245). Ca(2+)(out) + K(+)(out) + 4 Na(+)(in) = Ca(2+)(in) + K(+)(in) + 4 Na(+)(out) Mice display a significan reduction in Ca(2+) flux in cortical neurons, leading to a profound loss of long term potentiation and an increase in long term depression at hippocampal Schaffer/CA1 synapses, and clear deficits in specific tests of motor learning and spatial working memory (PubMed:16407245). Mice do not show any obvious loss of photoreceptor function in cones (PubMed:16407245). Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19) family. SLC24A subfamily.

Q1CRN4

MSKIAKTAIISPKAEINKGVEIGEFCVIGDGVKLDEGVKLHNNVTLQGHTFIGKNTEIFPFAVLGTQPQDLKYKGEYSELIIGEDNLIREFCMINPGTEGGIKKTLIGDKNLLMAYVHVAHDCVIGSHCILANGVTLAGHIEIGDYVNIGGLTAIHQFVRIAKGCMIAGKSALGKDVPPYCTVEGNRAFIRGLNRHRMRQLLESKDIDFIHVLYKRLFRPVPSLRESAKLELEEHANNPFVKEICSFILESSRGVAYKSSEYSSEEKQEE

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] + UDP-N-acetyl-alpha-D-glucosamine = a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine + holo-[ACP] Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 1/6. Homotrimer. Belongs to the transferase hexapeptide repeat family. LpxA subfamily.

A0MF70

MVPSLERGISITSSFNLDRMFDSSPGKEQQQPHLAETTMPESQTQDSLGGSPVETSRPMTSRLISRRQDKQQSETEMMKDRFTKLLLGEDMSGGGKGVSSALALSNAITNLAASIFGEQTKLQPMAPDRRARWKKEIDWLLSVTDHIVEFVPSQQISKEGVCTEIMVTRQRGDLLMNIPALRKLDAMLIDTLDNFRGHNEFWYVSRDSEEGKQARNERTKDKWWLPPVKVPPNGLSESARRMLHFQKDSVSQVQKAAMAINAQVLSEMAIPDSYIESLPKNGRVSLGDSLYKSITEEWFDPEQFLSTLDLSTEHKVLDVKNRIEASIVIWKRKLHLKDNKSSWGSAVSLEKRELFEERAETILVLLKQKFPGLPQSSLDISKIQYNKDVGHAVLESYSRILESLGYTEMSRIDDVLYADSLARKQCTGEETSDGGKIATETDSASAGSSNYSGEEIEKLESQNSSKTTLLDFIGWSDNSSKGQSEKPPKSPRMTPKKLSYLEKLENLNGFRSPKDRH

Guanine-nucleotide exchange factor (GEF) that acts as an activator of Rop (Rho of plants) GTPases by promoting the exchange of GDP for GTP. Interacts with ARAC11/ROP1 and ARAC10/ROP11. Interacts with PRK6 (PubMed:26961657). Localizes to the apical region of the pollen tube plasma membrane. Expressed in pollen grains and pollen tubes. The PRONE (plant-specific Rop nucleotide exchanger) domain is responsible for the GEF activity. Extended C-terminus.

B8ZKS3

MEFMLDTLNLDEIKKWSEILPLAGVTSNPTIAKREGSINFFERIKDVRELIGSTPSIHVQVISQDFEGILKDAHKIRRQAGDDIFIKVPVTPAGLRAIKALKKEGYHITATAIYTVIQGLLAIEAGADYLAPYYNRMENLNIDSNSVIRQLALAIDRQNSPSKILAASFKNVAQVNNALAAGAHAVTAGADVFESAFAMPSIQKAVDDFSDDWFVIQNSRSI

Catalyzes the reversible formation of fructose 6-phosphate from dihydroxyacetone and D-glyceraldehyde 3-phosphate via an aldolization reaction. beta-D-fructose 6-phosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone Belongs to the transaldolase family. Type 3A subfamily.

Q7K0S9

MDIIQKSIFNSGPHSRGIYEPPLGYFTPYNTPPYIAAYSDSGSWLADHHQHHQQQHQQHQQQMQHIRFPTPPITPPRPIAGYGYRQRTQSVIMKARGQQDELCRSPVEFPDDSKSCSSSSECGTASDFVCNWTDCDRVFDTLDALAQHVTQRHAIASLTDGLYYCRWRGCQRSERGFNARYKMLVHTRTHTKEKPHRCHLCEKSFSRAENLKIHIRSHSGEKPYKCSFEGCQKAYSNSSDRFKHTRTHSMEKPYMCKVAGCQKRYTDPSSLRKHVKTFKHSIHLIASQPLTLPSVPCLLEASSESAFTCLPAASSVESTSSSSSARYYDDSNNEPSDYSLKPKQDAEFSPSYWLGDRQHSYLHSEDFFVKMDVESPLDLRIHRI

Transcription factor which represses a set of lipase genes involved in fat catabolism. Specifically expressed in gut, fat body and Malpighian tubules of sugar-fed larvae. Strongly and rapidly induced in larvae by maltose, trehalose, glucose, fructose or saccharose, but not by lactose or galactose. Belongs to the GLI C2H2-type zinc-finger protein family.

Q66KN9

MSVSVFSVVSRFLDEYVSSTPQRLKLLDAYLLYILLTGALQFLYCLLVGTFPFNSFLSGFISSVGSFILAVCLRIQINPQNKSDFQGISPERAFADFLFANTILHLVVVNFIG

Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation (By similarity). N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. Protein modification; protein glycosylation. Component of the oligosaccharyltransferase (OST) complex. Belongs to the DAD/OST2 family.

B0TD37

MTEQPLKVLFVSAEVVPFAKAGGLADVAGSLPRALASSGVDVRVAMPRHGQIPRGAYVTDYMVEVDARKETAVIREGRIEALPGGKSVPVYFIDNYQYFGRENIYGYSDDGERWGFFSRALLEMLEPIDFIPDILHFNDWQCGPAIALLKEEYRHHPAYRRIASVLTVHNLEYQGHFGRDILQFIGLRQDLFRPDALEFYGQVNFMKAGLVFADLINTVSRTYAEEIQTSEYGWGLDGLLRLRHSDLFGIVNGIDVEVYDPATDPHIPHHYSADNIEGKKRNKAELQRQFGLPVSEAPLLGLVHRLVDQKGIDLFEGIEEALFREDLQLVVVGQGDPRYEGLFRRLKQHFPEKVGLFIGFDTPLAQRVYGGSDFFLMPSRFEPCGLGQLIAFRYGAIPIVRSTGGLADTVTDVRFPNGNGVVFEAYQPDRFLEAIRRGLHLYRQKDRWQQLIAKVMRLDHSWRRSADEYMQLYGRARRKVNPEL

Synthesizes alpha-1,4-glucan chains using ADP-glucose. [(1->4)-alpha-D-glucosyl](n) + ADP-alpha-D-glucose = [(1->4)-alpha-D-glucosyl](n+1) + ADP + H(+) Glycan biosynthesis; glycogen biosynthesis. Belongs to the glycosyltransferase 1 family. Bacterial/plant glycogen synthase subfamily.

B7GHM5

MEKGMVAMNEWIEKSKTYLWLPFTQMKDYEQHPLVIESGEGIFLTDVNGKTYYDGYSSLWLNVHGHRKKEIDDAIRAQLERIAHSTLLGAANIPAIALAEKLIEWTPSHLTRVFYSDSGAEAVEIALKIAFQYWRNIGENKKQKFVTLANGYHGDTVGAISVGAIDIFHTVYEPLMFTSYKAPFPLVYRHPSNDPNVVRDEALGALEALFAEHHEEIAAMIVEGMIQGAGGMHVMPKGYLKGVEQLCRQYNILFIVDEVATGFGRTGKRFAIEHEDVQPDIMTVAKGITGGYLPIAATLTTEAIYEAFYGDYTEFKTFFHGHSYTGNQLGCAAALANIQIFERERLIEQIQQKATFVAEQLASFNELNHVGDVRQLGLMCGIELVRDRRTHEPYPWTERMGYRTTLTMREKGMLTRPLGDVIVFMPPLASTFEQLEAMIAMMKEAIIETTEKRG

Catalyzes the transfer of the alpha-amino group from S-adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only aminotransferase known to utilize SAM as an amino donor. (8S)-8-amino-7-oxononanoate + S-adenosyl-L-methionine = (7R,8S)-7,8-diammoniononanoate + S-adenosyl-4-methylsulfanyl-2-oxobutanoate Cofactor biosynthesis; biotin biosynthesis; 7,8-diaminononanoate from 8-amino-7-oxononanoate (SAM route): step 1/1. Homodimer. Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. BioA subfamily.

B0KN41

MKEGIHPNYEVVAVTCSCGNKFETRSTLGNVLSIDVCNLCHPFYTGKQKVLDTGGRVQKFADRFGMFGTKK

Binds the 23S rRNA. Binds 1 zinc ion per subunit. Part of the 50S ribosomal subunit. Belongs to the bacterial ribosomal protein bL31 family. Type A subfamily.

O82277

MGLKGYSVGEGGGEIVEVQGGHIIRATGRKDRHSKVFTSKGPRDRRVRLSAHTAIQFYDVQDRLGYDRPSKAVDWLIKKAKTAIDKLELGETTTTTTRQEPVNTKPESPTLVFQRENNDQTQFVAANLDPEDAMKTFFPATTTTNGGGGTNINFQNYPHQDDNNMVSRTTTPPPNLSQDLGLSLHPFQGNNNTVVVPETNNFTTTHFDTFGRISGWNHHDLTMTSSSSSEHQQQEQEERSNGGFMVNHHPHHHHHQPSMMTLLNSQQQQVFLGGQQQQQQRGTLQSSLFPHSFRSWDHHQTTSDHHHHQNQASSMFASSSQYGSHGMMMMQGLSFPNTTRLLHGEEATQPNSSSSPPNSHL

Plays a pivotal role in the control of morphogenesis of shoot organs by negatively regulating the expression of boundary-specific genes such as CUC genes, probably through the induction of miRNA (e.g. miR164). Participates in ovule develpment (PubMed:25378179). Interacts with AHP1, AHP2 and AHP3 (PubMed:11158442). Interacts with SPL (PubMed:25527103, PubMed:25378179). Mostly detected in lateral organs, such as leaves and flowers. Expressed in cotyledons, particularly in the vascular region, in leaves, roots, stems, buds, flowers and immature siliques. First observed in the distal and middle regions of cotyledons of heart-shaped embryos. Later localized in bending cotyledon, and mature embryos, but no signals were detected in the presumptive shoot apical meristem (SAM) and the boundary region during embryogenesis. Expressed during ovule development (PubMed:25378179).

P75370

MVNPVLVFDQVSLRYNGAPLLENINFTISPGEHICLLGKSGVGKTSLLNCITNTKTISKGTIYFNGIASNNKDYKQLKKQFSFLDQVPNLIDTDFVYDAIWREAKNNLKWWQRLFLVEPQSLREQIIQILEEVNLKEYVTYIIKDLSGGQKQRVEVAKLFFANSQVLLVDEPTTGLDLINAHKIMELIIQFARQKAMTLIFVTHDVEFALKYSDRIIALKNKALVLDQATNKLTKQKLMQIYHD

Part of a high-affinity transport system. Belongs to the ABC transporter superfamily.

P0C599

MSSVVKSKSKNPYAAVRVDPDSDYITPGTLDLEQLFWSGPGVQYTHVNQVWPGIYIGDEKTALERPGLRDLGITHVLNAAEGKWNNVLTGADYYSDTNIQYYGIEADDKPTFNISQFFHPAAQFIHEALSQPHNVLVHCVMGRSRSATLVLAYLMMEHSLSVVDAIEHVRQRRCILPNHGFLKQLRALDITLQEARLKQKTQTQGQEKPR

Dual specificity phosphatase able to dephosphorylate phosphotyrosine, phosphoserine and phosphothreonine residues, with a preference for phosphotyrosine as a substrate. Dual specificity phosphatase able to dephosphorylate phosphotyrosine, phosphoserine and phosphothreonine residues within the same substrate, with a preference for phosphotyrosine as a substrate (By similarity). Involved in the modulation of AMPK and MAPK1/2 signaling pathways (By similarity). H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate Belongs to the protein-tyrosine phosphatase family. Non-receptor class dual specificity subfamily.

A4SIE3

MSSPISAVSQMLERNQALFVGKRLLVCGTLEDDYPRQLAELASSLTVFTTDYCYYRSQQATLGDAILFDHQLGGAPRFDALLLLMPKAKAEAQYLLAMMTPLLEAGADLFLAGENRGGINGADKLLAPYGNKPVKRDSARRCSLYHGELSKPVIPFELDAWFSRYECKAGDTELTVLALPGVFSADELDPGSQMLLAAVPPMTGELLDFGCGAGVIGSVLAKRNPGLEVKMVDISALALESSRRTLAINGLQGQVQASDVYSDITGKFDHIVSNPPFHAGLKTFYAATETFLAKAPEYLSANGGLTIVANAFLRYQPILETHFKRTDIISSDAKFKVYLSKV

Specifically methylates the guanine in position 1207 of 16S rRNA in the 30S particle. guanosine(1207) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(1207) in 16S rRNA + S-adenosyl-L-homocysteine Monomer. Belongs to the methyltransferase superfamily. RsmC family.

P17646

MDIAGSLCNASEGPVLRPEARVSGNGDLQFLGWNVPPDQIQHIPEHWLTQLEPPASMHYMLGVFYIFLFCASTVGNGMVIWIFSTSKALRTPSNMFVLNLAVFDFIMCLKAPIFIYNSFHRGFALGNTGCQIFAAIGSYSGIGAGMTNAAIGYDRLNVITKPMNRNMTFTKAIIMNVIIWLYCTPWVVLPLTQFWDRFVPEGYLTSCTFDYLTDNFDTRLFVGTIFFFSFVCPTLMIIYYYSQIVGHVFSHEKALREQAKKMNVESLRSNVDKSKDTAEIRIAKAAITICFLFFVSWTPYGVMSLIGAFGDKSLLTPGATMIPACTCKLVACIDPFVYAISHPRYRMELQKRCPWLAIDEKAPESSSAASTTTTQEQQQTTAA

Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal. Phosphorylated on some or all of the serine and threonine residues present in the C-terminal region. Each Drosophila eye is composed of 800 facets or ommatidia. Each ommatidium contains 8 photoreceptor cells (R1-R8), the R1 to R6 cells are outer cells, while R7 and R8 are inner cells. Opsin Rh4 is sensitive to UV light. Belongs to the G-protein coupled receptor 1 family. Opsin subfamily.

A5V9W7

MTRLAETFARTRAEGRAALVTFVTGGDPTPGDMGPILDALVAGGADVIELGMPFTDPMADGPAIQRANLRALGAGTTTADLLAIAAAFRQRHPSVPLVLMGYANPMVRRGPEWFAAEAAKAGVDGVICVDIPPEQDGALGPALRAAGVAPIRLATPTTDAARLPAVLEGASGFLYYVSVAGITGMQQAGQASIEAAVARFKAATDLPVAVGFGVRGPEQAEAIGRVADGVVVGSAIVDLIGEHGAAAAGPVRDFTATLSAALRRAAQEKAA

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.

A3NEG8

MNKIRKGDEVIVITGKDKGKRGVVLAVGAEHVTVEGINLVKKHVKPNPMKGTTGGVEAKTMPLHISNVALVDANGKASRVGIKVEDGKKVRFLKTTGAVLSA

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.

Q3IFD2

MTLRIAITPGEPAGIGPDLLLKLAQQTWDAQLVAIADANMLKQRAKHLGLSIKLIEFDQHAAATPAPAGSLYLHQVDVAEPVELGVLNDANGQYVLDTLRIASEKNMDGTFAAVVTGPVHKGIINKAGISFSGHTEYFAQQSNTADVVMMLATQGLRVALVTTHIPLAYVSRAITEDRLIKVASILNHDLQTKFGIEKPRILVCGLNPHAGEDGHLGREEIDTIIPTLEILNNQGMNLIGPLPADTLFQDKYLNEADAVLAMYHDQGLPVLKYKGFGNSVNITLGLPFIRTSVDHGTALDLAGKGTADVGSFELAIREAIKLAQEKAQNQ

Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP). 4-(phosphooxy)-L-threonine + NAD(+) = 3-amino-2-oxopropyl phosphate + CO2 + NADH Binds 1 divalent metal cation per subunit. Can use ions such as Zn(2+), Mg(2+) or Co(2+). Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 4/5. Homodimer. The active site is located at the dimer interface. Belongs to the PdxA family.

P21564

MSHEKNEASGYPEAQSWKSQEAMLGARTEVSRWRAVKNCLYRHLVKVLGEDWIFLLLLGALMALVSWAMDFIGSRGLRFYKYLFALVEGNIGLQYLVWVCYPLALILFSSLFCQIVSPQAVGSGIPELKTIIRGAVLHEYLTLRTFVAKTVGLTVALSAGFPLGKEGPFVHIASICATLLNQLLCFISGRREEPYYLRADILTVGCALGISCCFGTPLAGVLFSIEVTCSHFGVRSYWRGFLGGAFSAFIFRVLSVWVKDTVTLTALFKTNFRGDIPFDLQEMPAFAIIGIASGFFGALFVYLNRQIIVFMRKKNFVTKILKKQRLIYPAVVTFVLATLRFPPGVGQFFGAGLMPRETINSLFDNYTWTKTIDPRGLGNSAQWFIPHLNIFIVMALYFVMHFWMAALAVTMPVPCGAFVPVFNLGAVLGRFVGELMALLFPDGLVSNGNLYHILPGEYAVIGAAAMTGAVTHAVSTAVICFELTGQISHVLPMMVAVILANMVAQGLQPSLYDSIIQIKKLPYLPELSWSSANKYNIQVGDIMVRDVTSIASTSTYGDLLHVLRQTKLKFFPFVDTPDTNTLLGSIDRTEVEGLLQRRISAYRRQPAAAAEADEEGRNGETGASFTGEAESSFAYIDQEDAEGQQREGLEAVKVQTEDPRPPSPVPAEEPTQTSGIYQKKQKGTGQVASRFEEMLTLEEIYRWEQREKNVVVNFETCRIDQSPFQLVEGTSLQKTHTLFSLLGLDRAYVTSMGKLVGVVALAEIQAAIEGSYQKGFRLPPPLASFRDVKHARNSGRTATSNSSGK

Voltage-gated chloride channel. This channel is thought to ensure the high conductance of the non-innervated membrane of the electrocyte necessary for efficient current generation caused by sodium influx through the acetylcholine receptor at the innervated membrane. Homodimer. Each subunit contains a channel ('Double barreled channel'). The CLC channel family contains both chloride channels and proton-coupled anion transporters that exchange chloride or another anion for protons. The absence of conserved gating glutamate residues is typical for family members that function as channels (By similarity). Belongs to the chloride channel (TC 2.A.49) family. ClC-0 subfamily.

B1XHI3

MSKSRLTVFSFVRRFLLRLMVVLAVFWGGGIALFSVAPVPFSAVMVERQVSAWLHGNFRYVAHSDWVSMDQISPWMGLAVIAAEDQKFPEHWGFDVASIEKALAHNERNENRIRGASTISQQTAKNLFLWDGRSWVRKGLEAGLTLGIETVWSKKRILTVYLNIAEFGDGVFGVEAAAQRYFHKPASKLTRSEAALLAAVLPNPLRFKVSSPSGYVRSRQAWILRQMYQLGGEPFMQQHQLD

Peptidoglycan polymerase that catalyzes glycan chain elongation from lipid-linked precursors. [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+) Cell wall biogenesis; peptidoglycan biosynthesis. Belongs to the glycosyltransferase 51 family.

Q3AQ40

MVSVQINDNETIDKMLKRFKKKYERAGVLKEYRANAYFVKPSIDNRLKRSRSRRRAQRANEERNS

Belongs to the bacterial ribosomal protein bS21 family.

Q6HBD4

MTENNDIKMVIITGMSGAGKTVALQSFEDLGYFCVDNLPPMLLPKFIELMADSKGKMNKVALGVDLRGREFFEHLWGALDDLSERTWIIPHILFLDAKDSTLVTRYKETRRSHPLAPTGLPLKGIEIERSLLTDMKARANIVLDTSDLKPKELREKIVHLFSTETEQAFRVNVMSFGFKYGIPIDADLVFDVRFLPNPYYIPHMKPLTGLDEEVSSYVLKFNETHKFLEKLTDLITFMLPHYKREGKSQLVIAIGCTGGQHRSVTLTEYLGKHLKPEYSVHVSHRDVEKRKGH

Displays ATPase and GTPase activities. Belongs to the RapZ-like family.

B2K7E7

MSAIALTVSMLALVAVLGLWIGNWKIYGVGLGIGGVLFGGIIVGHFAQTYQIVLNGDMLHFIQEFGLILFVYTIGIQVGPGFFSSLRVSGLRLNCFAILMVVVGGLVTAIIHKLFAVPLPIILGVFSGAVTNTPALGAAQQILTDLGSPPQLVSQMGMGYAMAYPFGICGILLVMWLIRLFFKINIDREAKAFDSSYGQNRELLQTMNVAVRNPNLHGLSVQDVPLLNSDEVVCSRLKRGDLLMVPMPATVIEIGDYLHLVGQRDALEKVRLVVGEEVDVTLSTAGTALQTARVVVTNEAVLGKKIRDLNLKQKYDVVITRLNRAGIELVASNSANLQFGDILNLVGRPEAIEAVSAIVGNAQQKLQQVQMLPVFIGVGLGVLLGSIPLFVPGFPAALRLGLAGGPLVVALILGRIGSIGKLYWFMPPSANLALRELGIVLFLSVVGLKSGGDFINTLVNGDGLAWIGYGAMITGIPLLTVGILARMLVKMNYLTLCGMLAGSMTDPPALAFANGLHPTSGAAALSYATVYPLAMFLRIMSPQILAVLFWTL

Belongs to the AAE transporter (TC 2.A.81) family. YidE subfamily.

Q6R5A6

MSKKLKPFEILEDSCASVCIWLNGEPTAISNRAENLWNKAKYRVATDGAVNEILKRKSFVEWPHIICGDFDSINKQIDTKNAKVVHLPDQDYTDLSKSVQWCLEQKTLTSWEFENIVVLGGLNGRFDHTMSTLSSLIRFVDSQTPVIVLDSRNLVLAVPTGDSNLDVNLEMTTKMCGIIPIVQKETIVSSIGLKYEMENLALEFGKLISTSNEVTTSQVFLKSSSSLIFSIELENWVYKLDSL

Catalyzes the phosphorylation of thiamine to thiamine pyrophosphate. Functions cell non-autonomously. ATP + thiamine = AMP + H(+) + thiamine diphosphate Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine diphosphate from thiamine: step 1/1. Belongs to the thiamine pyrophosphokinase family.

A1WZG0

MGVTAIYPGTFDPITHGHTDLIQRGARLFDRLIVGVAANPSPSKAPAFAVEERLELARTALAGIDNVEVEAFTSLLVDFVAHHEAQVIVRGLRAVSDFEYEFQLASMNRQLRADVETVFLTPAEQYAFISSSLVREVAALGGDVSRFVHPAVAEALRNRVRRVP

Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. (R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5. Homohexamer. Belongs to the bacterial CoaD family.

A6VFI6

MFKTEPFIEESIEEIRKQIDNRRTIIALSGGVDSSVAAVLADRAIGDKLLAVYVDTGLMRKNESEEIWKIFKEQMGLNLKIVEAKDIFLKELEGVIDPEEKRKIIGRLFIEVFEKVAEEQGEEVLVQGTIAPDWIESEGQIKTHHNIALPGGMVLDVVEPLRELYKDEVRLLAEALGLPDQIAHRQPFPGPGLAVRILGEITDEKLAICKEANFIVSEEIEKTELKNELWQYFAAVLDTKATGVKGDIRDYNWVVALRFVSSLDAMTAHTPEIPFDLIKRISKRITSEIPNVTRVVLDVTDKPPATIEFE

Catalyzes the synthesis of GMP from XMP. ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 H(+) + L-glutamate Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1. Heterodimer composed of a glutamine amidotransferase subunit (A) and a GMP-binding subunit (B).

D6VPZ6

MESQQLSQHSPIFHGSACASVTSKEVQTTQDPLDISASKTEECEKVSTQANSQQPTTPPSSAVPENHHHASPQAAQVPLPQNGPYPQQRMMNTQQANISGWPVYGHPSLMPYPPYQMSPMYAPPGAQSQFTQYPQYVGTHLNTPSPESGNSFPDSSSAKSNMTSTNQHVRPPPILTSPNDFLNWVKIYIKFLQNSNLGDIIPTATRKAVRQMTDDELTFLCHTFQLFAPSQFLPPWVKDILSVDYTDIMKILSKSINKMQSDTQEVNDITTLATLHYNGSTPADAFEAEVTNILDRLNNNGIPINNKVACQFIMRGLSGEYKFLPYARHRCIHMTVADLFSDIHSMYEEQQESKRNKSTYRRSPSDEKKDSRTYTNTTKPKSITRNSQKPNNSQSRTARAHNVSTFNNSPGPDNDLIRGSTTEPIQLKNTHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVKYGDFYWVSKKYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPKSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYQSFIASNEIQQSNDLNIESDHDFQSDIELYPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISDIESTDSGGMHRLDVPLLAPMSQSNTHESSYASKSKDFRHSDSYSDNETNHTNVPISSTGGTNNKTVPQTSEQETEKRIIHRSPSIDTSSSESNSLHHVVPIKTSDTCPKENTEESIIADLPLPDLPPEPPTELSDSFKELPPINSRQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMKTWDTDKYYDRKEIDPKRVINSMFIFNRKRDGTHKARFVARGDIQHPDTYDSGMQSNTVHHYALMTSLSLALDNNYHITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMVLFSKNLNSNKRIIDKLKMQYDTKIINLGESDEEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQQELELEEDDYKMKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSKQVLDMTYELIQFIWNTRDKQLIWHKSKPVKPTNKLVVISDASYGNQPYYKSQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSYLIQELDKKPITKGLLTDSKSTISIIISNNEEKFRNRFFGTKAMRLRDEVSGNHLHVCYIETKKNIADVMTKPLPIKTFKLLTNKWIH

Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity). The aspartyl protease (PR) mediates the proteolytic cleavages of the Gag and Gag-Pol polyproteins after assembly of the VLP. Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that catalyzes the conversion of the retro-elements RNA genome into dsDNA within the VLP. The enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes during plus-strand synthesis and hydrolyzes RNA primers. The conversion leads to a linear dsDNA copy of the retrotransposon that includes long terminal repeats (LTRs) at both ends (By similarity). Integrase (IN) targets the VLP to the nucleus, where a subparticle preintegration complex (PIC) containing at least integrase and the newly synthesized dsDNA copy of the retrotransposon must transit the nuclear membrane. Once in the nucleus, integrase performs the integration of the dsDNA into the host genome (By similarity). a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1) a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1) Endonucleolytic cleavage to 5'-phosphomonoester. The capsid protein forms a homotrimer, from which the VLPs are assembled. The protease is a homodimer, whose active site consists of two apposed aspartic acid residues (By similarity). The Gag-Pol polyprotein is generated by a +1 ribosomal frameshift. The ratio of Gag:Gag-Pol varies between 20:1 and 5:1 (By similarity). The C-terminal RNA-binding region of CA is sufficient for all its nucleocapsid-like chaperone activities. Integrase core domain contains the D-x(n)-D-x(35)-E motif, named for the phylogenetically conserved glutamic acid and aspartic acid residues and the invariant 35 amino acid spacing between the second and third acidic residues. Each acidic residue of the D,D(35)E motif is independently essential for the 3'-processing and strand transfer activities of purified integrase protein (By similarity). Initially, virus-like particles (VLPs) are composed of the structural unprocessed proteins Gag and Gag-Pol, and also contain the host initiator methionine tRNA (tRNA(i)-Met) which serves as a primer for minus-strand DNA synthesis, and a dimer of genomic Ty RNA. Processing of the polyproteins occurs within the particle and proceeds by an ordered pathway, called maturation. First, the protease (PR) is released by autocatalytic cleavage of the Gag-Pol polyprotein yielding capsid protein p45 and a Pol-p154 precursor protein. This cleavage is a prerequisite for subsequent processing of Pol-p154 at the remaining sites to release the mature structural and catalytic proteins. Maturation takes place prior to the RT reaction and is required to produce transposition-competent VLPs (By similarity). Retrotransposons are mobile genetic entities that are able to replicate via an RNA intermediate and a reverse transcription step. In contrast to retroviruses, retrotransposons are non-infectious, lack an envelope and remain intracellular. Ty1 retrotransposons belong to the copia elements (pseudoviridae). Produced by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the YBL005W-A ORF.

Q9H642

MSLMVSAGRGLGAVWSPTHVQVTVLQARGLRAKGPGGTSDAYAVIQVGKEKYATSVSERSLGAPVWREEATFELPSLLSSGPAAAATLQLTVLHRALLGLDKFLGRAEVDLRDLHRDQGRRKTQWYKLKSKPGKKDKERGEIEVDIQFMRNNMTASMFDLSMKDKSRNPFGKLKDKIKGKNKDSGSDTASAIIPSTTPSVDSDDESVVKDKKKKSKIKTLLSKSNLQKTPLSQSMSVLPTSKPEKVLLRPGDFQSQWDEDDNEDESSSASDVMSHKRTASTDLKQLNQVNFTLPKKEGLSFLGGLRSKNDVLSRSNVCINGNHVYLEQPEAKGEIKDSSPSSSPSPKGFRKKHLFSSTENLAAGSWKEPAEGGGLSSDRQLSESSTKDSLKSMTLPSYRPAPLVSGDLRENMAPANSEATKEAKESKKPESRRSSLLSLMTGKKDVAKGSEGENPLTVPGREKEGMLMGVKPGEDASGPAEDLVRRSEKDTAAVVSRQGSSLNLFEDVQITEPEAEPESKSEPRPPISSPRAPQTRAVKPRLEVSPEAQPTARLPSPTDSPSSLPPLPSSSGQASVPSELGHGADTQSSESPSVFSSLSSPIAAPISTSTPIESWPLVDRGQAKSEGPPLLPKAELQTESLTPVPNSGSSALGSLFKQPSFPANKGTEDSLMGRTRETGTEKNTSSLELEESLPEQPETGRQEEELPRFPCKKQDYSPSSGEAQEVPFALSLSSDGAVSPVGELAAGGDRDLESQAGSLVESKARDAAEEVAPPLPMGASVPSIDSMMRKLEEMGLNLRKDQKKTKKRVSFSEQLFTEEAVAGAALLVEGHSSCPQELNPAWSVAGNASDGEPPESPHAEDSERESVTTPGPATCGAPASPADHLLLPSQEESFSEVPMSEASSAKDTPLFRMEGEDALVTQYQSKASDHEGLLSDPLSDLQLVSDFKSPIMADLNLSLPSIPEVASDDERIDQVEDDGDQVEDDGETAKSSTLDIGALSLGLVVPCPERGKGPSGEADRLVLGEGLCDFRLQAPQASVTAPSEQTTEFGIHKPHLGKSSSLDKQLPGPSGGEEEKPMGNGSPSPPPGTSLDNPVPSPSPSEIFPVTHSFPSSAHSDTHHTSTAESQKKATAEGSAGRVENFGKRKPLLQAWVSPSETHPVSAQPGAGTGSAKHRLHPVKPMNAMATKVANCSLGTATIISENLNNEVMMKKYSPSDPAFAYAQLTHDELIQLVLKQKETISKKEFQVRELEDYIDNLLVRVMEETPNILRIPTQVGKKAGKM

A Rab11 effector protein involved in the endosomal recycling process. Also involved in controlling membrane trafficking along the phagocytic pathway and in phagocytosis. Homooligomer (isoform 2). Isoform 2 interacts with RAB4A, RAB11A, RAB11B and RAB25. According to PubMed:15280022, RAB4A binding to RAB11FIP1 is of very low affinity in vitro and in vivo. Rab11A rather than Rab4A mediates localization in the endocytic recycling compartment (ERC). Membrane-bound (isoform 2). Colocalizes with Rab11A at phagosomes (isoform 2). Isoform 2 is expressed in brain, heart, testis, lung, spleen, ovary and small intestine.

Q8NGJ4

MFLPNDTQFHPSSFLLLGIPGLETLHIWIGFPFCAVYMIALIGNFTILLVIKTDSSLHQPMFYFLAMLATTDVGLSTATIPKMLGIFWINLRGIIFEACLTQMFFIHNFTLMESAVLVAMAYDSYVAICNPLQYSAILTNKVVSVIGLGVFVRALIFVIPSILLILRLPFCGNHVIPHTYCEHMGLAHLSCASIKINIIYGLCAICNLVFDITVIALSYVHILCAVFRLPTHEARLKSLSTCGSHVCVILAFYTPALFSFMTHRFGRNVPRYIHILLANLYVVVPPMLNPVIYGVRTKQIYKCVKKILLQEQGMEKEEYLIHTRF

Odorant receptor. Belongs to the G-protein coupled receptor 1 family.

C4ZVQ3

MENAKMNSLIAQYPLVKDLVALKETTWFNPGTTSLAEGLPYVGLTEQDVQDAHARLSRFAPYLAKAFPETAATGGIIESELVAIPAMQKRLEKEYQQPISGQLLLKKDSHLPISGSIKARGGIYEVLAHAEKLALEAGLLTLDDDYSKLLSPEFKQFFSQYSIAVGSTGNLGLSIGIMSARIGFKVTVHMSADARAWKKAKLRSHGVTVVEYEQDYGVAVEEGRKAAQSDPNCFFIDDENSRTLFLGYSVAGQRLKAQFAQQGRIVDADNPLFVYLPCGVGGGPGGVAFGLKLAFGDHVHCFFAEPTHSPCMLLGVHTGLHDQISVQDIGIDNLTAADGLAVGRASGFVGRAMERLLDGFYTLSDQTMYDMLGWLAQEEGIRLEPSALAGMAGPQRVCASVSYQQMHGFSAEQLRNTTHLVWATGGGMVPEEEMNQYLAKGR

D-serine = NH4(+) + pyruvate Monomer. Belongs to the serine/threonine dehydratase family. DsdA subfamily.

B2RLG7

MNRSSFDLLSTVEYGGCSAKLDPAKLSELLHDIPLPVDSRIMVDVSTHDDAGVYRLNDDTALIVTTDFFPPVCSDPYTFGRIAAANALSDVYAMGGRPLLVLNLTMFPSEGIPVEVLADILRGGQQTIDESGAFTMGGHTIDDPIPKYGLAVTGIVHPEHLVTNAGVRAGQCLVLTKPLGIGVAMAAHRLGLIGSEVYEAAIGQMCLLNRAGAELMQKYGIRGATDITGFGLLGHAKELAEASDVCLHIDSRSVPVLPECLSLLRDGCIPGATFRNLRFVGDMLRADCPTEYKMLLADAQTSGGLLMAVDADRAEDLVADLHRTGLHPFAAIIGYATDAEDAAKLIVT

Synthesizes selenophosphate from selenide and ATP. ATP + H2O + hydrogenselenide = AMP + 2 H(+) + phosphate + selenophosphate Binds 1 Mg(2+) ion per monomer. Homodimer. Belongs to the selenophosphate synthase 1 family. Class I subfamily.

Q6AQ16

MKGNEIRSRFLEYFKGNGHTVAESSSLVPKDDPTLLFTNAGMVQFKRVFMGDDKRGYVRAVTSQKCVRAGGKHNDLENVGYTARHHTFFEMLGNFSFGDYFKEEAIRLAWNFLTVELGLPAEKMWVSVFEDDDEAFALWEKVEDLPKGRIVRLGEKDNFWAMGDTGPCGPCSEIHIDQGVGSSPCDNPNCAVGCDCDRFLELWNLVFMQFNRAEDGSLTALPRPSIDTGMGLERVAAVLQGKFNNYDSDLFAPIIAVLEDISGVKYGAAADTDTAIRVIADHARATSFLVADGVLPSNEGRGYVLRRIMRRAVRYGKKLGLEKPFMDRVTKAVCAEMQNAYPQLVATAALLEKVVNNEEERFRETLEHGLVQLDEKISQLLTSGGDAVIDGPFIFKLYDTFGFPFDIVRDIALERGVGFDEAGFATAMAEQRAKSRASRKGEGVKLHDEGVKALADAGKKAEFLGYEGLEADSVVEGLLSEQGSGVEKLVAGEKGRVFVAATPFYAEAGGQMGDRGSVRWQGGQASVYATQAEGTGLILHDLLVEEGELSLGLEVTLQVDDEERKATASNHSATHLLQAALISVLGDHVKQSGSLVGPERLRFDFTNFSQLTAAEIAQVETLVNEQIRNNAVIATDVLSKQEAIAGGATALFGEKYDDDVRVVSMGDYSRELCGGTHVGATGEIGLFVILSESGIAAGVRRIEALTGRAALAYVQGRLSTGNELADLLSCKSGDLVPKVESLLTAVKEGEKRVAQLAGQLASSGLDDLLNNALTVAGIKVVVAEVPLENAKALRELGDKVRDNLESGIAVIGGAVGGKVALLAIVTKDLVDRIQAGRIVSEVSGIVGGKGGGRPDMAQAGGTMPDKLSEAIASVPAIIEAML

Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala) Binds 1 zinc ion per subunit. Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs. Belongs to the class-II aminoacyl-tRNA synthetase family.

O35023

MKRESYQAEMFNWCEALKDQIQKRGQLDQFEDQIDKMIEALEDDQTTEEDWYKQAAALYRDITESDDTSERRAYVPIGKHVLPKLPYKYSALEPYISRDIMILHHTKHHQSYVDGLNKAESELKKARATKNYDLITHWERELAFHGAGHYLHSIFWFSMHPNGKRRPTGALFQMIDLSFGSYSAFKEHFTQASKKVEGVGWAILVWAPRSGRLEILTAEKHQLFSQWDVIPLLPLDVWEHAYYLQYKNDRASYVDHWWNVVDWREAEKRFEQAKEVVWKLY

Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. 2 H(+) + 2 superoxide = H2O2 + O2 Binds 1 Fe cation per subunit. Belongs to the iron/manganese superoxide dismutase family.

A1WVB2

MIQMESLLKAADNSGARQVQCIKVLGGSKRRYAGIGDIVKVSVKDAIPRGRVKKGEVYNAVVVRSKRGVRRADGSQIRFDGNAAVLLNNNLQPIGTRVFGPVTRELRNERFMRIISLAPEVL

Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome. Part of the 50S ribosomal subunit. Forms a cluster with proteins L3 and L19. In the 70S ribosome, L14 and L19 interact and together make contacts with the 16S rRNA in bridges B5 and B8. Belongs to the universal ribosomal protein uL14 family.

P22456

MDFVLTRLILLFLAATIIYSSEDESRLINDLFKSYNKVVRPVKAFKDKVVVTVGLQLIQLINVNEVNQIVTTNVRLKQQWEDVHLKWDPEDYGGIKKVRIPSSDIWRPDIVLYNNADGDFAIVQETKVLLDYTGKIIWLPPAIFKSYCEMIVTYFPFDLQNCSMKLGTWTYDGTLVVINPENDRPDLSNFMESGEWYMKDYRCWKHWVYYDCCPETPYLDITYHFLLQRLPLYFIVNVVIPCLLFSFLTGLVFYLPTDSGEKITLSVSVLLSLVVFLLVIVELIPSTSSAVPLIGKYMLFTMVFVIASIVITVIVINTHHRSPSTHIMPQWLKKIFIETIPRVMFFSTMKRPAQDQHKKKIFTEDIDISDISGKLGPTAVKYQSPILKNPDVKSAIEGAKYVAETMKSDQESTKASEEWKFVAMVLDHLLLAVFMIVCIIGTLAIFAGRLIELHMQG

Upon acetylcholine binding, 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. One of the alpha chains that assemble within the acetylcholine receptor, a pentamer of two alpha chains, a beta, a delta, and a gamma or epsilon chains. Oocytes. Belongs to the ligand-gated ion channel (TC 1.A.9) family. Acetylcholine receptor (TC 1.A.9.1) subfamily. Alpha-1/CHRNA1 sub-subfamily.

Q4WR62

MHSNVGLAGLAGLLATASVCLSAPADQNITSDTYFYGQSPPVYPSPEGTGTGSWAAAYAKAKKFVAQLTPEEKVNLTAGTDANNGCSGNIAAIPRLNFPGLCVSDAGNGLRGTDYVSSWPSGLHVGASWNKALARQRAVQMATEFRKKGVNVLLGPVVGPLGRVAEAGRNWEGFSNDPYLSGALVYETVDGAQSVGVATCTKHYILNEQETNRNPGMEDGVEVAAVSSNIDDKTMHELYLWPFQDAVLAGSASIMCSYNRVNNSYGCQNSKTLNGLLKTELGFQGYVMTDWGAQHAGIAGANAGLDMVMPSTETWGANLTTAISNGTMDASRLDDMATRIIASWYQMNQDSDFPSPGAGMPSDMYAPHQRVIGRDASSKQTLLRGAIEGHVLVKNNHSALPLKSPQLLSVFGYDAKGPNALKQNFNWLSYSPAIQENHTLWVGGGSGANNAAYIDAPIDAIQRQAYEDGTSVLYDISSEDPEVDPTTDACLVFINSYATEGWDRPGLADNSSDTLVKNVARKCANTIVTIHNAGIRVVGEWIDHENVTAVIFAHLPGQDSGRALVELLYGRANPSGKLPYTVAKKVEDYGSLLHPSLPETPYGLFPQSDFDEGVYIDYRAFDRANITAQFEFGFGLSYTSFDYSGLQISNPKQSPQYPPSAAIQQGGNPHLWDNIVTVSAEIKNTGRVAGAEVAQLYIGIPNGPVRQLRGFEKVDVSAGETTQVQFALNRRDLSTWDVEAQQWSLQRGTYRVYVGRSSRDLPLTGSFTL

Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose (By similarity). Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose. Glycan metabolism; cellulose degradation. Belongs to the glycosyl hydrolase 3 family.

Q08372

MKKIITLKNLFLIILVYIFSEKKDLRCNVIKGNNIKDDEDKRFHLFYYSHNLFKTPETKEKKNKKECFYKNGGIYNLSKEIRMRKDTSVKIKQRTCPFHKEGSSFEMGSKNITCFYPIVGKKERKTLDTIIIKKNVTNDHVVSSDMHSNVQEKNMILIRNIDKENKNDIQNVEEKIQRDTYENKDYESDDTLIEWFDDNTNEENFLLTFLKRCLMKIFSSPKRKKTVVQKKHKSNFFINSSLKYIYMYLTPSDSFNLVRRNRNLDEEDMSPRDNFVIDDEEEEEEEEEEEEEEEEEEEEEEEEEYDDYVYEESGDETEEQLQEEHQEEVGAESSEESFNDEDEDSVEARDGDMIRVDEYYEDQDGDTYDSTIKNEDVDEEVGEEVGEEVGEEVGEEVGEEVGEEVGEEVGEEVGEEEGEEVGEGVGEEVGEEEGEEVGEEEGEYVDEKERQGEIYPFGDEEEKDEGGESFTYEKSEVDKTDLFKFIEGGEGDDVYKVDGSKVLLDDDTISRVSKKHTARDGEYGEYGEAVEDGENVIKIIRSVLQSGALPSVGVDELDKIDLSYETTESGDTAVSEDSYDKYASNNTNKEYVCDFTDQLKPTESGPKVKKCEVKVNEPLIKVKIICPLKGSVEKLYDNIEYVPKKSPYVVLTKEETKLKEKLLSKLIYGLLISPTVNEKENNFKEGVIEFTLPPVVHKATVFYFICDNSKTEDDNKKGNRGIVEVYVEPYGNKINGCAFLDEDEEEEKYGNQIEEDEHNEKIKMKTFFTQNIYKKNNIYPCYMKLYSGDIGGILFPKNIKSTTCFEEMIPYNKEIKWNKENKSLGNLVNNSVVYNKEMNAKYFNVQYVHIPTSYKDTLNLFCSIILKEEESNLISTSYLVYVSINEELNFSLFDFYESFVPIKKTIQVAQKNVNNKEHDYTCDFTDKLDKTVPSTANGKKLFICRKHLKEFDTFTLKCNVNKTQYPNIEIFPKTLKDKKEVLKLDLDIQYQMFSKFFKFNTQNAKYLNLYPYYLIFPFNHIGKKELKNNPTYKNHKDVKYFEQSSVLSPLSSADSLGKLLNFLDTQETVCLTEKIRYLNLSINELGSDNNTFSVTFQVPPYIDIKEPFYFMFGCNNNKGEGNIGIVELLISKQEEKIKGCNFHESKLDYFNENISSDTHECTLHAYENDIIGFNCLETTHPNEVEVEVEDAEIYLQPENCFNNVYKGLNSVDITTILKNAQTYNINNKKTPTFLKIPPYNLLEDVEISCQCTIKQVVKKIKVIITKNDTVLLKREVQSESTLDDKIYKCEHENFINPRVNKTFDENVEYTCNIKIENFFNYIQIFCPAKDLGIYKNIQMYYDIVKPTRVPQFKKFNNEELHKLIPNSEMLHKTKEMLILYNEEKVDLLHFYVFLPIYIKDIYEFNIVCDNSKTMWKNQLGGKVIYHITVSKREQKVKGCSFDNEHAHMFSYNKTNVKNCIIDAKPKDLIGFVCPSGTLKLTNCFKDAIVHTNLTNINGILYLKNNLANFTYKHQFNYMEIPALMDNDISFKCICVDLKKKKYNVKSPLGPKVLRALYKKLNIKFDNYVTGTDQNKYLMTYMDLHLSHKRNYLKELFHDLGKKKPADTDANPESIIESLSINESNESGPFPTGDVDAEHLILEGYDTWESLYDEQLEEVIYNDIESLELKDIEQYVLQVNLKAPKLMMSAQIHNNRHVCDFSKNNLIVPESLKKKEELGGNPVNIHCYALLKPLDTLYVKCPTSKDNYEAAKVNISENDNEYELQVISLIEKRFHNFETLESKKPGNGDVVVHNGVVDTGPVLDNSTFEKYFKNIKIKPDKFFEKVINEYDDTEEEKDLESILPGAIVSPMKVLKKKDPFTSYAAFVVPPIVPKDLHFKVECNNTEYKDENQYISGYNGIIHIDISNSNRKINGCDFSTNNSSILTSSVKLVNGETKNCEININNNEVFGIICDNETNLDPEKCFHEIYSKDNKTVKKFREVIPNIDIFSLHNSNKKKVAYAKVPLDYINKLLFSCSCKTSHTNTIGTMKVTLNKDEKEEEDFKTAQGIKHNNVHLCNFFDNPELTFDNNKIVLCKIDAELFSEVIIQLPIFGTKNVEEGVQNEEYKKFSLKPSLVFDDNNNDIKVIGKEKNEVSISLALKGVYGNRIFTFDKNGKKGEGISFFIPPIKQDTDLKFIINETIDNSNIKQRGLIYIFVRKNVSENSFKLCDFTTGSTSLMELNSQVKEKKCTVKIKKGDIFGLKCPKGFAIFPQACFSNVLLEYYKSDYEDSEHINYYIHKDKKYNLKPKDVIELMDENFRELQNIQQYTGISNITDVLHFKNFNLGNLPLNFKNHYSTAYAKVPDTFNSIINFSCNCYNPEKHVYGTMQVESDNRNFDNIKKNENVIKNFLLPNIEKYALLLDDEERQKKIKQQQEEEQQEQILKDQDDRLSRHDDYNKNHTYILYDSNEHICDYEKNESLISTLPNDTKKIQKSICKINAKALDVVTIKCPHTKNFTPKDYFPNSSLITNDKKIVITFDKKNFVTYIDPTKKTFSLKDIYIQSFYGVSLDHLNQIKKIHEEWDDVHLFYPPHNVLHNVVLNNHIVNLSSALEGVLFMKSKVTGDETATKKNTTLPTDGVSSILIPPYVKEDITFHLFCGKSTTKKPNKKNTSLALIHIHISSNRNIIHGCDFLYLENQTNDAISNNNNNSYSIFTHNKNTENNLICDISLIPKTVIGIKCPNKKLNPQTCFDEVYYVKQEDVPSKTITADKYNTFSKDKIGNILKNAISINNPDEKDNTYTYLILPEKFEEELIDTKKVLACTCDNKYIIHMKIEKSTMDKIKIDEKKTIGKDICKYDVTTKVATCEIIDTIDSSVLKEHHTVHYSITLSRWDKLIIKYPTNEKTHFENFFVNPFNLKDKVLYNYNKPINIEHILPGAITTDIYDTRTKIKQYILRIPPYVHKDIHFSLEFNNSLSLTKQNQNIIYGNVAKIFIHINQGYKEIHGCDFTGKYSHLFTYSKKPLPNDDDICNVTIGNNTFSGFACLSHFELKPNNCFSSVYDYNEANKVKKLFDLSTKVELDHIKQNTSGYTLSYIIFNKESTKLKFSCTCSSNYSNYTIRITFDPNYIIPEPQSRAIIKYVDLQDKNFAKYLRKL

Gametocyte surface protein required for male/female gamete fusion. Also required for male gamete exflagellation and interaction with host erythrocytes. Heterodimer; heterodimerizes with PF45/48. Specifically expressed in gametocytes and gametes (at protein level). May be processed into a 310 kDa form as the parasite emerges from the host erythrocytes. Promising transmission-blocking vaccine candidate: targeting the protein would prevents transmission of the parasite decreasing the malaria burden (PubMed:32709983, PubMed:33741942). The LMIV230-01 transmission-blocking antibody against the 6-Cys domain 1 also binds to the heterologous P.falciparum Malian isolate 20-2217-0 which carries a 'Ser-605' polymorphism and to the heterologous St Lucia strain which carries 'Ser-605' and 'Asn-661' polymorphisms (PubMed:33741942).

Q899G5

MNKDFNEFKKFIYNKKVAIIGLGISNMPLVEFLSNLGARVTGFDKKNENELENNINELKAKGVNFELGENYLDKLSNFDVVFRTPSMRTDHPILIKAKSEGAYITSEMEEFIKYCPAKLFCITGSDGKTTTTTLIYNILKTEGYTVWVGGNIGNPLFTKIEEIKKDDKVVLELSSFQLMSIKEPIEVALVTNVSPNHLDIHKDMEEYIKAKKNIFKYQRENDLLVINEDNKITKSMEEECRGRLLKFSMKEKLKEGSFYYNEDLYINEKKVCNVSEVKLKGMHNVENLLAAFSCVSEDSSIDSMREVAKNFNGVEHRLEFVKEIQEVKYFNDSIASSPTRTLAALQSFDRPVILIAGGYDKKISFEVLAKEGISHIKHLILLGDTKYKIEEAFKKVMRDSSEDLPISICNSIEEAINIAKENGESGDVVTLSPACASFDMFKNFEERGNKFKSIIRNL

Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate Cell wall biogenesis; peptidoglycan biosynthesis. Belongs to the MurCDEF family.

B0S8V2

MDELTKRVIPCLDIKGGRVVKGVQFVNLIDAGDPVSCAVAYEENKADELCFLDITASSDKRDILLHLVEEVANKLFIPFTVGGGIRTIEDVKAVLNKGADKVSINTSAFQNPKLLKDASEIYGSQCIVCAIDVKFHPERKRYEVYLNGGRAETGREALDWGKEAHEMGAGEILLTSMDKDGTKDGFDINLMKSFTSNLTIPIIASGGAGNPEHMAEVILRGGADAVLAASIFHFGEFSIQETKQTMKEMGIKVRL

IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit. 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 Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9. Heterodimer of HisH and HisF. Belongs to the HisA/HisF family.

C5DGZ5

MLSRFKCSRLQLQKRAISVTKATTTTASQPKRRRTTTFSDALNKGPSFEDFVSGKAAKFTLDPLQQARSNIEEAKRLPRWLKVPIPKGTNYHKLKKDVRELKLSTVCEEAKCPNISECWGGGDSSKATATIMLLGDTCTRGCRFCSVKTNRAPSKPDPAEPENTAEAISRWGLGYVVLTTVDRDDLADGGAHHLAETVCRIKQKAPKTLVETLSGDFRGDLEMVKVMAQSGLDVYAHNLETVKDLTPHVRDRRATYEQSLSVLNQAKKTVPTLITKTSLMLGLGETDEQVLQTLQDLRAIGCDVVTFGQYMRPTKRHMKVVEYVKPEKFDYWRDKALELGFLYCASGPLVRSSYKAGEAFIENVLRKRANN

Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. [[Fe-S] cluster scaffold protein carrying a second [4Fe-4S](2+) cluster] + 4 H(+) + N(6)-octanoyl-L-lysyl-[protein] + 2 oxidized [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + 2 5'-deoxyadenosine + [[Fe-S] cluster scaffold protein] + 4 Fe(3+) + 2 hydrogen sulfide + 2 L-methionine + 2 reduced [2Fe-2S]-[ferredoxin] Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 2/2. Belongs to the radical SAM superfamily. Lipoyl synthase family.

Q4UMS5

MARSIWKGPFVDGYLIKKVQKLMESGKSEMIKTWSRRSTILPIFVGFTFSVHNGNKFIPVSVNEEMVGRKLGEFAPTRTFHGHGADKKVKRK

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

Q5FVN5

MELPTPQKVQEPPKSFEEFLKSQNWDYWPRDVHIRDGDIWENTLRKLEEAVSYNSVYSYLWTNVPRLYEIVDSMESKLKECSHLLQQHASRLFESDRLISKKRTYTNLDRYKAFLKEHYRRKKIVLSDQMETEKNIEGCTFLLKQNELTQLPRHLDAKQIYLYVLRTHNLEEKVFKVWKTHILSDCSIALLHDCFWWWFLHKFKPDKRDQDWLFDRIAESYVTLFMRIPLRRKDIFFQMYPDWLAQAVYTTFQESFPESCSLFNDNFKEDLGNTIFLWLSGLKPAPGFWTHWKLQDLCTTTIHGCRRVPVKLRRGIMSSQEHTSATVGLKIEDILKNPRALPVLKEESAASKVTTKSHYRSLGPEFYKVLFDFGGQSPLILYYLKMHELGGISVTYNPKGSKFTKILREPPPAPTYCEIIKDAKRKFADNKKDFKRVKQRIKDDIKFLKEQQEQIDKELDRLQAKASKNLQEVKNDFENFLHKLRVEAKLKEEYRGSASPSESLQSLQSPNSSLSSPAMSEDFNSVEEGGLKEARSDHYLRTTHSSFSSINLIGGECTTKSTFCCSSLKSSHQ

Belongs to the FAM227 family. Extended N-terminus.

C8WJW0

MYDDLKGKTVVVTGSSKGLGAAMARRFGAEGMNVVANYRSDEEGARETVRAIEEAGGAAAAVQADVSKNECVDALFDAAMFSFGGVDIWVNNAGIEVASPSDRKSIEEWQRVIDVNLTGVFAGCRRAIDHFLDRKMPGVIINLSSVHEIIPWPHFADYAASKAGVGMLTKTLALEYADRGIRVNAIAPGAMNTPINAEKFADPEARAATERLIPMGYVGAPEDVAAAAAWLASDQASYVTGTTLFVDGGMTLYPGFQFGQG

Involved in the modification of secondary bile acids into iso-bile acids (3beta-bile acids) via epimerization of the 3-OH group through a 3-oxo-intermediate. Catalyzes the reduction of 12-alpha-hydroxy-3-oxo-5-beta-cholan-24-oate (3-oxo-DCA) and 3-oxo-5-beta-cholan-24-oate (3-oxo-LCA) to yield isodeoxycholate (isoDCA) and isolithocholate (isoLCA), respectively. Is also able to catalyze the reduction of 3-dehydrocholate (3-oxo-CA or 7alpha,12alpha-dihydroxy-3-oxo-5beta-cholan-24-oate) and 7-alpha-hydroxy-3-oxo-5-beta-cholan-24-oate (3-oxo-CDCA), into isocholate (isoCA) and isochenodeoxycholate (isoCDCA), respectively. Prefers NADH to NADPH as cosubstrate. The conversion of the abundant bile acid deoxycholate (DCA) into isoDCA by the gut bacterium E.lenta favors the growth of the keystone commensal genus Bacteroides, since isoDCA is less cytotoxic than its parent compound, DCA; iso-bile acids have thus a potential role in modulating gut community composition. 3-oxo-5beta-cholan-24-oate + H(+) + NADH = isolithocholate + NAD(+) 12alpha-hydroxy-3-oxo-5beta-cholan-24-oate + H(+) + NADH = isodeoxycholate + NAD(+) 7alpha,12alpha-dihydroxy-3-oxo-5beta-cholan-24-oate + H(+) + NADH = isocholate + NAD(+) 7alpha-hydroxy-3-oxo-5beta-cholan-24-oate + H(+) + NADH = isochenodeoxycholate + NAD(+) kcat is 584 min(-1) with 12alpha-hydroxy-3-oxo-5beta-cholan-24-oate as substrate. Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Q9N421

MSSATSGEYWLISVPGEKGANDAWDKLNRSTGNTSTNSKYLIPDLKVGTLDQLVGLSDDLSKLDTSAEAVIRKLVQYFTEVLEEDKSKIAENLVIGNKDMKTYVTKFQWEGAKYPLKQSLKVLSEIIGKQISQIDNDLKVKSLTYNNLKNALASMDRKTVGSLLTKDLADLVKADDFVLNSEYLQTVIVVVPKISVKEWEQKYATLSSMVVPGSSKLLTEEGEHALYTVTLFKKVIDEFKNTARENKFIVRDFVYDEETLKAGRTERDKLMAEKQRQYAPLIRWLKINFGEIFAAYIHIKALRVFVESVLRYGLPVNFQAAVIEPAKGQQKKLRQELHKLYIHLDGSAAGPIDTLEDSPALMSLGVNEYYPYVFFKLNIDFLNK

Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (Probable). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity). Subunit C is necessary for the assembly of the catalytic sector of the enzyme and is likely to have a specific function in its catalytic activity (By similarity). Has roles in embryogenesis and ovulation (PubMed:10846178). V-ATPase is a heteromultimeric enzyme made up of two complexes: the ATP-hydrolytic V1 complex and the proton translocation V0 complex (By similarity). The V1 complex consists of three catalytic AB heterodimers that form a heterohexamer, three peripheral stalks each consisting of EG heterodimers, one central rotor including subunits D and F, and the regulatory subunits C and H (By similarity). The proton translocation complex V0 consists of the proton transport subunit a, a ring of proteolipid subunits c9c'', rotary subunit d, subunits e and f, and the accessory subunits vah-19/Ac45 and vah-20/PRR (By similarity). Interacts with V-type proton ATPase subunits a1 unc-32, a2 vha-5 and a3 vha-6 (PubMed:11441002). In embryonic cells, detected in dot-like structures in the cytoplasm around the nuclei. Expressed ubiquitously; higher levels are found in gastrointestinal and hypodermal cells, as well as H-shaped excretory cell. Worms display embryonic lethality. When vha-11 is silenced in adults, they are able to produce eggs but egg numbers gradually decrease and worms become sterile after 24 hours. This sterility continues for about 4 days and then viable eggs are produced again. Vha-11 and vha-3 are transcribed on a dicistronic transcript where vha-3 is the upstream transcript and vha-11 the downstream. Belongs to the V-ATPase C subunit family.

A2SCX6

MAEIVFQGASALALDAKGRLAVPARHRDVLGALAQGRLTLTKHPVGCLLVFPRPAWEGFRDKVAALPLRAEGWKRIFLGNAMDVEIDASSRVLVSPELRQAAGLVKDVMLLGMGSHFELWDVQRYQAHEAEVMQQGLPESLGDFSF

Forms oligomers. Belongs to the MraZ family.

P77435

MERLLIVNADDFGLSKGQNYGIIEACRNGIVTSTTALVNGQAIDHAVQLSRDEPSLAIGMHFVLTMGKPLTAMPGLTRDGVLGKWIWQLAEEDALPLEEITQELVSQYLRFIELFGRKPTHLDSHHHVHMFPQIFPIVARFAAEQGIALRADRQMAFDLPVNLRTTQGFSSAFYGEEISESLFLQVLDDAGHRGDRSLEVMCHPAFIDNTIRQSAYCFPRLTELDVLTSASLKGAIAQRGYRLGSYRDV

ChbG is essential for growth on the acetylated chitooligosaccharides chitobiose and chitotriose but is dispensable for growth on cellobiose and chitosan dimer, the deacetylated form of chitobiose. Deacetylation of chitobiose-6-P and chitotriose-6-P is necessary for both the activation of the chb promoter by the regulatory protein ChbR and the hydrolysis of phosphorylated beta-glucosides by the phospho-beta-glucosidase ChbF. Catalyzes the removal of only one acetyl group from chitobiose-6-P to yield monoacetylchitobiose-6-P, the inducer of ChbR and the substrate of ChbF. It can also use chitobiose and chitotriose as substrates. H2O + N,N'-diacetylchitobiose = acetate + N-acetyl-beta-D-glucosaminyl-(1->4)-D-glucosamine diacetylchitobiose-6'-phosphate + H2O = acetate + N'-monoacetylchitobiose-6'-phosphate Glycan degradation; chitin degradation. Homodimer. By N,N'-diacetylchitobiose. Cells lacking this gene are unable to grow on chitobiose and chitotriose. Belongs to the YdjC deacetylase family. ChbG subfamily. Was originally (PubMed:8121401 and PubMed:2179047) characterized as part of a cryptic cel operon for a cellobiose degradation system. The Cel+ phenotype is due to mutations making expression chitobiose-independent and altering the substrate specificity.