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Full Name
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taxon
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sequence
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2.75k
function
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5.51k
AlphaFoldDB
stringlengths
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Q3AGB7
MOAA_SYNSC
Molybdenum cofactor biosynthesis protein A
unclassified Synechococcus
MSTSLPLADRLNRPIGVLRLSLTARCNLACPYCCPDVEEPPGLLTLEQQIRVIRVATRLGVQTLRLTGGEPLLSRRLLPLLEAVAQARRDRSDPMAGLQAVALTSNGVLLSEPMGRALRAAGLDRITISLDAAEGEAAARMAGLQGGAVAGERLVRQVQDGIAAAFAAGFDPSRGELKLNAVIQRGINDDQLLPLAALARQRGMELRLIEYMDVGNRNQWTLDQVLPAAQMVERINARWPLEPLGRPRGGTARRWRYGDGAGSIGVISSISEPFCGDCNRLRVTADGQAFTCLFSAEGTDLKPALASDLQLEQAMRQLWQRRQDRYSEERDPAAAASTHAEMAYLGG
Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate.
Q3AGB7
A7NL05
NUOB2_ROSCS
NDH-1 subunit B 2
Roseiflexus
MSDDRDIQLEAEKQGVFLTTMQRFYNWGRRSSVWPLSFGLACCAIEMMATGLARFDLARFGAEMFRASPRQADLMIVAGTVTKKMAPQVVRLYNQMPEPRYVISMGACATSGGPFRDGYNVLRGIDLLIPVDVYIPGCPPRPEALLHALMTLQKQIDAQRLNRVRWYGKREAKEYPVPAFGKHGLEIDGKLVDPVGGLPLISPYTSPTHGEMRSGEIEHPELVRHFPIMDETVELESPNKAKGVAPEIRHNDLKRPAVEVDHARDEQR
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
A7NL05
A5IJD4
MIAB_THEP1
tRNA-i(6)A37 methylthiotransferase
Thermotoga
MRFYIKTFGCQMNENDSETMAGLLMKEGFTPASAPEEADVVIINTCAVRRKSEEKAYSELGQMLKIKRKRKLVVGVAGCVAEKEREKLLERGADFVLGTRAVLKVTEAVKRALQGEKVALFEDHLDEYTHELPRIRSSKHHAWVTIIFGCDRFCTYCIVPYTRGREKSRPMEDILEEVRELAKQGYREVTFLGQNVDAYGKDLKDGSSLAKLLEEASKIEGIERIWFLTSYPTDFSDELIEVIARNPKVAKSVHLPVQSGSNRILKLMNRSYTKEEYLALLERIRSKVPDVAISSDIIVGFPTETEEDFMETIDLVEKAQFERLNLAIYSPRKGTVAWKHYKDEVPYEEKVRRMQFLMNLQKRINRKLNERYKGKTVRVIVEAQAKNGLFYGRDIRNKIIAFEGEEWMIGRFADVKIEKITAGPLYGKVVWIEETPSPVSTDK
Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
A5IJD4
Q55G31
EXPL1_DICDI
Expansin-like protein 1
Dictyostelium
MKTFVLFVILLCLTFLSISKSETCPFSQSLVSGASATYYTDPNAGNCGYENLMGPLGPGNLFIAALGPNLYNNGKNCGQCFNISSPYTNRSVVIMATDSCPDSGYCQRSSHFDLSTQAFDVLGAQSIGVLEGLTYYKVPCGVNGNVKIMMKDGSNDYWTAFLIYNSKVTIKDVSVKITGKSTYTSLTQSSYNYWISPNMVPGSFDVRIESVGGEFIYITIPKVESRKQYETSSQFSVDGCVGTPSGPSGGLGSPSTGASIGTPSDASSLTLYALFSLTILFLVMLN
May serve to lubricate the movement of the cellulose microfibrils during cell growth and wall extension and/or they may serve to maintain the fluid state of the slug cell wall.
Q55G31
A5FYN8
RS6_ACICJ
30S ribosomal protein S6
Acidiphilium
MPLYECVLIARSEITQQQVDTIADAVTAQVESESGAVKKREYWGLRNLAYRIKKNRKGHYVLLGLDAEPATISEMERQLGLNEDVLRFMTVRVEDIDEAPSAPLARRGEDRDRDRGFRGPKPAGRFDSGRRRGADDREEYRARDEYRSDRDEDQNEEN
Binds together with S18 to 16S ribosomal RNA.
A5FYN8
O83857
RS15_TREPA
30S ribosomal protein S15
Treponema
MALTKERTASVVQQYGSGEKDTGSSSVQIALLTERIRQLTDHCKVHPKDKSSNRGLLVLVGRRRRLLRYSRRVSMGAYRSLVKSLGLRK
Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome.
O83857
B6EGX8
HSCB_ALISL
Co-chaperone protein HscB homolog
Aliivibrio
MNHFELFGLPNQFELDGGLLSAQFLELQKRFHPDNFATSSERDRLLSVQKAAQINDAYQTLKNPVTRAEYILSEQGHDIRGEQTTMQDPMFLMQQMELREDLEDLLSSSDPESALFDFSENVSAMRKTQLAELKQQLESELWQEAAQSVRKLKFIDKLNQEVEKLEDKLLG
Co-chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Seems to help targeting proteins to be folded toward HscA.
B6EGX8
B0S1S2
NADE_FINM2
NH(3)-dependent NAD(+) synthetase
Finegoldia
MNYAKLCEDLTKWIKEEVESANLKGAVFGISGGIDSAVLACLCKKAFGDNALGLIMPIKSNPKDEEDARILAKSIGLRFTKVDLNESYDALIGTFEKNSVEMAASNIKPRLRMITLYYYAQNNGYMVLSGSNRSEFMTGYFTKYGDSGADLMPLLNLYKTDIFEMAKVLGVPDVIINKKPSAGLWEGQTDEDEFGFTYEELDDYLMNNSNTKSKDLIDKKIKQSEHKRKFAKSFEFDRRNY
Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
B0S1S2
Q1IDV2
CAPP_PSEE4
Phosphoenolpyruvate carboxylase
Pseudomonas
MSDIDQRLREDVHLLGELLGETIRQQHGEAFLQKIEDIRHSAKADRRGEGEQLSSTLGDLAEEDLLPVARAFNQFLNLANIAEQYQLIHRRDTDQPEPFEARVLPELLARLKAAGHGNDALARQLARLDIQLVLTAHPTEVARRTLIQKYDAIAAQLAAQDHRDLIPAERQQVRERLRRLIAEAWHTEEIRRTRPTPVDEAKWGFAVIEHSLWQAVPNHLRKVDKALFEATGLRLPLESAPVRFASWMGGDRDGNPNVTAAVTREVLLLARWMAADLFLRDIDYLAAELSMQQASGALREQVGDSAEPYRALLKQLRDRLRATRAWAHASLAGPQPASAAVLVDNRDLIAPLELCYQSLHACGMGVIADGPLLDSLRRAVTFGLFLVRLDVRQDAARHRDALSEITDYLGLGRYADWDEERRIEFLQHELKNRRPLLPAHFKPAAETAEVLATCREIAAAPAASLGSYVISMAGAASDVLAVQLLLKEAGLTRPMRVVPLFETLADLDNAGPVMERLLGLPGYRAGLHGPQEVMIGYSDSAKDAGTTAAAWAQYRAQENLVRICREHQVELLLFHGRGGTVGRGGGPAHAAILSQPPGSVGGRFRTTEQGEMIRFKFGLPGIAEQNLNLYLAAVLEATLLPPPPPEPAWRALMDQLAADGVKAYRGVVRDNPEFVEYFRQSTPEQELGRLPLGSRPAKRRAGGIESLRAIPWIFGWTQTRLMLPAWLGWETALSNALARGQADLLAQMREQWPFFRTRIDMLEMVLAKADAQIAEAYDQRLVQPRLLPLGAHLRDLLSQSCQVVLGLTGQQVLLAHSPETLEFIRLRNTYLDPLHRLQAELLARSRSREAALDSPLEQALLVTVAGIAAGLRNTG
Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.
Q1IDV2
C3P7P7
RIBBA_BACAA
GTP cyclohydrolase II
Bacillus cereus group
MFHRIEEALEDLKQGKVVIVCDDENRENEGDFIALAEYITPETINFMITHGRGLVCVPITEGYAERLQLEPMVSHNTDSHHTAFTVSIDHVSTTTGISAHERATTIQQLLNPASKGADFNRPGHIFPLIAKEGGVLRRAGHTEAAVDLAQLCGAEPAGVICEIINEDGTMARVPDLLQCAKQFDIKMITIEDLIAYRRHHETLVTREVEITLPTDFGTFQAIGYSNSLDTKEHIALVKGDISTGEPVLVRVHSECLTGDVFGSCRCDCGPQLHAALAQIEREGKGVLLYMRQEGRGIGLLNKLRAYKLQEEGFDTVEANEKLGFPADLRDYGIGAQILKDLGLQHLRLLTNNPRKIAGLQGYDLTVTERVPLQMPAKEENKTYLQTKVNKLGHLLNL
Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate.
C3P7P7
Q5ZU79
PSUG_LEGPH
Pseudouridine-5'-phosphate glycosidase
Legionella
MFHDLLEFNEEVLDAINDKNPIVALESTIISHGMPYPDNLTTAIEVENIIRRQGAIPATIAMHQGKIRVGLTQEVMEHLALQKEVIKASRRDISFVLSRKVTASTTVAATMFCAHMAKLPLFVTGGIGGVHQDVTMSFDISADLIELSNTPVTVVCSGAKSILDLPKTLEVLETFGVPVIGYATDEFPAFYSRSSGIPVPQRLNSAEEVANLMSIQQKLNMKNGIVVANPIPVSAELSDEEISPYIKQAHDEAKHMSGKSLTPFLLKRIAELTAGKSLEANIELIKNNAFLGAEIAIAYQKKLFSKKT
Catalyzes the reversible cleavage of pseudouridine 5'-phosphate (PsiMP) to ribose 5-phosphate and uracil. Functions biologically in the cleavage direction, as part of a pseudouridine degradation pathway.
Q5ZU79
Q97CX4
RS18_CLOAB
30S ribosomal protein S18
Clostridium
MARDNGNKDRDGKRPNGGRNRKMKRKICSFCMEKSESIDYKDINKLRKYVTERGKILPRRISGNCAKHQRELTIAIKRARNIALLPFTTE
Binds as a heterodimer with protein S6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit.
Q97CX4
P50895
BCAM_HUMAN
Lutheran blood group glycoprotein
Homo
MEPPDAPAQARGAPRLLLLAVLLAAHPDAQAEVRLSVPPLVEVMRGKSVILDCTPTGTHDHYMLEWFLTDRSGARPRLASAEMQGSELQVTMHDTRGRSPPYQLDSQGRLVLAEAQVGDERDYVCVVRAGAAGTAEATARLNVFAKPEATEVSPNKGTLSVMEDSAQEIATCNSRNGNPAPKITWYRNGQRLEVPVEMNPEGYMTSRTVREASGLLSLTSTLYLRLRKDDRDASFHCAAHYSLPEGRHGRLDSPTFHLTLHYPTEHVQFWVGSPSTPAGWVREGDTVQLLCRGDGSPSPEYTLFRLQDEQEEVLNVNLEGNLTLEGVTRGQSGTYGCRVEDYDAADDVQLSKTLELRVAYLDPLELSEGKVLSLPLNSSAVVNCSVHGLPTPALRWTKDSTPLGDGPMLSLSSITFDSNGTYVCEASLPTVPVLSRTQNFTLLVQGSPELKTAEIEPKADGSWREGDEVTLICSARGHPDPKLSWSQLGGSPAEPIPGRQGWVSSSLTLKVTSALSRDGISCEASNPHGNKRHVFHFGTVSPQTSQAGVAVMAVAVSVGLLLLVVAVFYCVRRKGGPCCRQRREKGAPPPGEPGLSHSGSEQPEQTGLLMGGASGGARGGSGGFGDEC
Laminin alpha-5 receptor. May mediate intracellular signaling.
P50895
P59752
RS13_CHLCV
30S ribosomal protein S13
Chlamydia
MPRIIGIDIPAKKKLKISLTYIYGIGPALSEEIIAKLQLNPEARAVELTEEEIGRLNSLLQSEYVVEGDLRRRVQSDIKRLISIHAYRGQRHRLSLPVRGQRTKTNSRTRKGKRKTVAGKKK
Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites.
P59752
Q8ZZX3
KHSE_PYRAE
Homoserine kinase
Pyrobaculum
MKAPSTSANLGAGFDIVAVAHDAYFAEAYTAVGSGCGVHVKFKGYDPGPENTVTRSFKKFFELTGICRGVEVEVENNIPIARGLGSSGAAAVAALAAFIREAGIKTDPRAVIEAAGYGETAAAGSPHFDNVAGAALGGAVVLTSLSPIDYVKFSPRLIFVVGVPEVPPMPNKTKVMREVLPKSVEFKTYVRQTARVASLIAGLALSDPRLVARGMEDEVVEAARAPYVPGYARVRKYAFEAGALGVSLSGAGPSVIALVNEKEAEAVRDAVLRAYAEEGLRAEVKIASITEGALASL
Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
Q8ZZX3
Q9K8L9
CRCB2_HALH5
Putative fluoride ion transporter CrcB 2
Halalkalibacterium (ex Joshi et al. 2022)
MRQTVKEIVAIGIGGAIGTSFRFLLNTWTLTTGYPYGTLIENIVGSFLLGFLTSWFLVIVPKEWLKKGLGVGLCGGFTTMSTLAADSVLLYSHHPFSSLIYVAASLFGGIGFALLGYLLASKIATRRKREVAGS
Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Q9K8L9
Q12KJ6
RL19_SHEDO
50S ribosomal protein L19
Shewanella
MNNIIKMLNDEQMKTDVPDFGAGDTVVVQVRVKEGEKERLQAFEGLVIAKRNRGLHSAFTVRKISNGEGVERAFQTHSPLIASIEVKRRGRVRRAKLYYLRERSGKSARIREKLGTK
This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site.
Q12KJ6
Q2YAQ4
MDH_NITMU
Malate dehydrogenase
Nitrosospira
MKTPIRVAVTGAAGQIAYSLLFRIAAGDMLGEDQPVILQLLDIPQSLPSLKGVVMELDDCAFPLLRDITITDDPKTAFRDINIAMLVGARPRTKGMERKDLLEANGTIFRAQGKALDEVAGRDVKVLVVGNPANTNAYITMKNAPSLKPTSFSSMMRLDHNRAVFQLAVKVGQPVSSVRKMIVWGNHSSAQYPDLSHAEVDGHNAADLVNDMAWIETGFIPVIQKRGMEVIEARGSSSAASAANAAICHMRDWVSGTPEGDWVSMGIPSDGSYGIPEGVIYGYPVTCQGGEYKIVPDLEISEFSRMKMQASYRELMGERESIKHLLG
Catalyzes the reversible oxidation of malate to oxaloacetate.
Q2YAQ4
B8E879
HEM3_SHEB2
Pre-uroporphyrinogen synthase
Shewanella
MSENRIRIATRKSPLAMWQAEFVKAELERIHPGIVVELLPMSTKGDVILDTPLAKVGGKGLFVKELEVAMLDDLADIAVHSMKDVPVDFPEGLGLEVICEREDPRDAFVSNLYKSISELPLGATVGTSSLRRQCQIRASRPDLIIKDLRGNVGTRLAKLDNGEYDAIILAAAGLIRLKLSERIASFISAEESLPANGQGAVGIECRINDERVKALLAPLEHLETRYRVLAERAMNTRLEGGCQVPIGAFAEIDGDEMTLRGLVGNPDGSEIIEGVITGPKTEATQLGVALAEELLSKGAKSILDAVYAKA
Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
B8E879
Q41510
PALAD_THUAT
Palmitoyl-acyl carrier protein desaturase
Thunbergia
MALVFKSIGAHKTPPCTLNLASPALYHTRVTMASTITHPPPLKDRKISSTRRVRTYPLAPEKAEIFNSMHGWVEDTILPFLKPVEESWQPTDFLPDSTSDGFHEQVEELRKRTADLPDDYLVALVGAMVTEEALPTYQTMLNTTDVIYDESGASPVPWAVWTRAWTAEENRHGDIVNKYLYLSGRVDMKQIEKTIQYLIGSGMDPGADNNPYLAYIYTSYQERATAISHGSLGRLARQKGEMKLAQICGTISADEKRHEAAYSKIVEKLFELDPEGTMLALAYMMKMKIVMPARLMHDGKDPDMFQHFSAVSQRLGIYTAKEYTDILEHMIARWGVDKLTGLSGEGRRAQDYVCGLPMRFRKVEERAQAWAENISHVPFSWIFGRRV
Delta(6) fatty acid desaturase introducing a cis double bond at carbon 6 of palmitoyl-[acyl-carrier protein](16:0-ACP), producing 16:1(6Z)-ACP . No activity with the coenzyme A ester of the fatty acid . The position of the double bond is determined by its distance from the carboxyl end of the fatty acid . Low activity with several saturated acyl-[acyl-carrier protein]s, including 14:0-ACP and 18:0-ACP . Requires reduced ferredoxin for detectable in vitro activity .
Q41510
P03916
NU5M_PANPA
NADH dehydrogenase subunit 5
Pan
MTMYTTMTTLTLTPLILPILTTLINPNKKNSYPHYVKSIIASTFIISLFPTTMFMCLDQEAIISNWHWATTQTTQLSLSFKLDYFSMTFIPVALFVTWAIMEFSLWYMNSDPNINQFFKYLLIFLITMLILVTANNLFQLFIGWEGVGIMSFLLISWWYARTDANTAAIQAILYNRIGDIGFILALAWFLLHSNSWDPQQMVLLSTNPSLTPLLGFLLAAAGKSAQLGLHPWLPSAMEGPTPVSALLHSSTMVVAGVFLLIRFHPLAENNPLIQTLTLCLGAITTLFAAICALTQNDIKKIVAFSTSSQLGLMMVTIGINQPHLAFLHICTHAFFKAMLFMCSGSIIHNLNNEQDIRKMGGLLKTMPLTSTSLIIGSLALAGMPFLTGFYSKDLIIETANMSYMNAWALSITLIATSLTSAYSTRMILLTLMGQPRFPTLTNINENNPTLLNPIKRLTIGSLFAGFFITNNILPMSTSQMTIPLYLKLTALSVTFLGLLTALDLNYLTNKLKMKSPPYTFYFSNMLGFYPNIMHRSIPYLGLLTSQNLPLLLLDLTWLEKLLPKTISQYQVSASITTSTQKGMIKLYFLSFLFPLILTLLLIM
Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I.
P03916
Q3TDD9
PPR21_MOUSE
KLRAQ motif-containing protein 1
Mus
MASAELQGKYQKLAQEYSKLRAQNQVLKKGVVDEQASSAALKEQLKMKDQSLRKLQQEMDSLTFRNLQLAKRVELLQDELALSEPRGKKNKKSGESSSQLSQEQKSVFDEDLQKKIEENERLHIQFFEADEHHRHVEAELRSRLATLETEAAQHQAVIDGLTRKYMETIEKLQSDKAKLEVKSQTLEKEAKECRLRTEECQLQLKNLHEDLSGRLEESLSIINEKVPFNDTKCHLYNALNVPLHNRRHQLKMRDIAGQALAFVQDLVPALLNFHTYTEQRIQIFPVDSAIDTISPLNQKFSQYLHENASYVRPLEEGMLHLFESITEDTVTVLETTVKLKMFSDHLTSYVRFLRKILPYQLKSLEEECESSLCTPALRARNLELSQDMKTMTAVFEKLQTYVTLLALPSTEPDGLLRTNYTSVLTNVGAALHGFHDVMKDISKHYSQKASIEHEIPTATQKLVTTNDCILSSAVTLTNGAGKIASFFGNNVDYFIASLSYGPKTASGFISPLSAECMLQYKKKAAAYMKSLRTPLAESVPYGEAVANRRVLLSSTESREGLAQQVQQSLEKISKLEQEKEHWMLEAQLAKIKLEKENQRIADRLRGTTSAQLPGLAQENATVPIASSQEEAAAKVLTEPVQSTSLVGMLTRTPDSEAPDVESREDLIKSHYMARIAELTSQLQLADSKSVHFYAECRALSKRLALAEKSKETLTEEMRLASQNISRLQDELMTTKRSYEDQLSMMSDHLCSMNETLSKQREEIDTLKMASKGNSKKTRNR
Putative regulator of protein phosphatase 1 (PP1) activity. May play a role in the endosomal sorting process or in endosome maturation pathway.
Q3TDD9
A5CX55
COAD_VESOH
Pantetheine-phosphate adenylyltransferase
Candidatus Vesicomyosocius
MKKIAIYPGSFDPITNGHVDLIKRASKLFDEIIIGISQNSKKKAFLSINDRIDTINTALKDINNIRILSFDTLLVDFASLKNAQVILRGLRAISDFEYEYQLSGINKHLNPNIETLFMTPTEQYANISSSLIKEIIALGGDISVFVPASVKTLLKHRL
Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
A5CX55
P35896
O1174_RAT
Putative gustatory receptor PTE33
Rattus
MKMENHTLISEFFLLDLSDDPKLQPFLFGLFLSMYLVTMLGNLLIILAVSSNSQLHNPMYFFLSNLSFVDICFISTTVPKMLVNMQSQTKDISYIECLTQVYFFNTFVGMDDVLLTLMAYDCFVAICNPLKYTIIMNPRVCTLLVLMFWIIMFCISLIHVLLMNELNFSRGTKIPHFFCELAQVLKVSNSDTHINNIFMYVLSSLLGVIPMTGILMSYSQIVSSLLRMSSTVSKYKAFSTCGSHLCVVCLFYGSVIGVYFSSSVVLSTQRIMVASLMYTVISPMLNPFIYSLRNKDVKVALGELFIRVAPCPSWINDIITKFILKNIRQNL
Possible taste receptor.
P35896
Q8BL99
DOP1_MOUSE
Protein dopey-1
Mus
MNTEELELLSDSKYRNYVAAIDKALKNFEYSSEWADLISALGKLNKVLQNNAKYQVVPKKLTIGKRLAQCLHPALPGGVHRKALETYEIIFKIIGPKRLAKDLFLYSSGLFPLLANAAMSVKPALLGLYEMYYLPLGKTLKPGLQGLLTGILPGLEEGSEYYERTNTLLEKVAAAVEQSAFYSALWGSLLTSPAVRLPGITYVLAHLNRKLSMEDQLYIIGSDIELMVEAVSTSVQDSSVLVQRSTLDLILFCFPFHMSQATRPDMIRILSAALHVVLRRDMSLNRRLYAWLLGFDNNGAIIGPRSTRHSNPEEHATYYFTTFSKELLVQAMVGILQVNGFGEESTLMQDLKPFRILISLLDKPELGPVILEDVLIEVFRTLYSQCKAELDLQMEPPFSKDHAQLSSKLRENKKTAELIKTANLLFNSFEPYYMWDYIARWFEECCRQSFFLSRRTLHARLQVGPGDSSDSSELQLTNFCLLVDFLLDIVSLETYIEIQTEHLPQLLLRMISALTSHLQTLRLSELTDSLRLCSKILSKVQPPLLSAGNGGVVQFPSGQNSTVKEWEDKKQVSSVSMENPAEVFEDGENPPSSRSSESGFTEFIQYQADRPDDLDRELNGQGAATIPIGSTSSETETASTVGSEETVIQPPSTFTQGAAGRSGKAVQKTAMQCCLEYVQQFLSRLINLYIIHSDSFPQALAADHQGDFSRIQRETSKWDRDSQGDAKERNIHTPKTSKEYLSAFLAACQLFLECSSFPVYIAEGNHTSESHSEKPDTDCEHAHPPQWLRTLMSACSQARDFRVQSAAVSLVMDLVGLTQSVAMVTGENINSMEPAQPLSPNQGRVAVVIRPPLTQGNLKYIAEKTEFFKHVALTLWDQLGDGTPQHHQKSVELFYQLHNLVPSSSICEDVVSQQLTHKDKKIRMEAHAKFAVLWHLTRDLHINKSSFARSFDRSLFIMLDSLTSLDGSTSSVGQAWLNQVLQRHDIARVLEPLLLLLLHPKTQRVSVQRVQAERYWSKTSCYPGEENDKHFMQNFTCNNVSQVHLIASKGNGEKPLTMDEMENFSLTVNPLSDRLSLLSTSSETIPMVVSDFDLPDQQMEILQSSDSGCSQSSAGDNFSYEVDPENANAHEDSHMAKASSPDDDVQQVVFDLICKVVSGLEAESESVTSELEIESLQTKSSDLDPGKEATKIEDQAPQHSQHVLLSDDSPRFLSVSTEEGCECLANGISRNSSSPCISGTAQTLNDSSVPSETKSRQRSHSSIQFSFKEKLSEKVSEKETIVKESGKQPGAKPKVKLARKKDEDKKKAASEKLKQANVFFSEGLDLENWYSCGEGEISEIESDMGSPGSRKSPNFNIHPLYQHVLLYLQLYDSSRTLYAFSAIKSILKTNPIAFVNAISTTSVNNAYTPQLSLLQNLLARHRISVMGKDFYSHIPVDSNHNFRSSMYIEILISLCLYYMRSHYPTHVKVTTQDLIGNRNMQMMSIEILTLLFTELAKVIESSAKGFPSFISDMLSKCKVQKVILHCLLSSIFSVQKWHSEKTAGKSMVAVEEGFSEDSLINFSEDELDNGSTLQSQLLRVLQRLIVLEHHVMTIPEENEAGFDFVVSDLEHISPHQPMTSLQYLHAQPITCQGMFLCAVIRALHQHCACKMHPQWIGLITSTLPYMGKVLQRVVVSVTLQLCRNLDNLIQQYKYETGLSDSRPLWVASIIPPDMILTLLEGITAIIHYCLLDPTTQYHQLLVNVDQKHLVEARSGILSILHMIMSSVTLLWSILHQADASEKMAVAASASVTTINLGATKVIPAASEEQLLLVELVRSISVMRAETVIQTVKEVLKQPPAIAKDKVRKLCFCRKFSFRTGADRIPVPNIVDSWTSLLVLLKDSIQLSLPAPGQFLILGVLNEFIMKNPSLENKKDQRDLQDVTHKIVDAIGAIAGSSLEQTTWLRRNLEVKPSPKIMVDGTNLESDVEDMLSPAMETSNITPSVYSVHALTLLSEVLAHLLDMVFYSDEKERVIPLLVNIMHYVVPYLRNHSAHNAPSYRACVQLLSSLSGYQYTRRAWKKEAFDLFMDPSFFQMDASCVSHWRAIMDNLMTHDKTTFRDLMTRVAVAQSSSLNLFANRDVELEQRAMLLKRLAFAVLSSESDQYQKYLPDIQERLVESLRLPQVQVFLLMEQELTADEDISRTSGPSAAGLETTYTGGNGFSTSYNSQRWLNLYLSACKFLDLALALPSENLPQFQMYRWAFIPEASDDSGLEVRRQGIHQREFKPYVVRLAKLLRKRAKDEEDFKILEGLEMAKHQKNPEEDCSGRTLGWEPGHLLLTLCTMRNMEQLLPFFNVLSQVFNSKVTSRCGGHSGSPVLYPNSFPNKDMKLENHKAFSSKARQKIEEMIEKDFLEGVIKT
May be involved in protein traffic between late Golgi and early endosomes.
Q8BL99
Q61QN4
CLAP3_CAEBR
Protein CLASP-3
Caenorhabditis
MTSRIQPKSGGYLLSKSDFTKVFEDVPKIAITSSVDLRNKFDNVKTILSNTSEDWNKRQTQLKTIRSLIINGEKLVDRPTMIAHILQLLGCFELAVKDLRSQILREAAITCSFIVSKYGIETHSIGEDILIPAMGQVAVSTKIMATSASTLTEFIVEYIQTRQVFTILSSFSTSKDKNQRRQLAVLLEIIIGKWSDRLKKQIIRQICELVKSAINDADSETRAAGRRAFAKLEEFHSEEADALFLELENSKQKMLRGGDAASSWASINSDKGSIPIRSKLSAGAKGYSNISAKFLAQRSASAIDPKALKVTGPSRLARPLSTKAMVRQDTSPAGSKIPYPNRPGSRTRTSSITSNDSRDTSPTRRHSPLPPDTQKARVKYGNGSFFAKLGMSDNTDDDEFLLPIRVRSPQKPNLGDSPADNVSRVLKECCSSSVTEKKDGIKKLLPIVSDTTLSSTEIKNIGNCLNRLLSDASNTKLILQMVLEVYAVFIRTHSSRLSEWLRLALAKLFARKATETLPNTKKQINHTLNVILECFNAHHQLVTVCELMCDPIHLMVPKARVALLEYMTSLLDEYTEPGASINHKELKAALRKMFTWIGDQRQSILLTPYIEKAICSMFCVNVADFSALISEFDSDQKAWLHQTLQLNGLENGISSGSGGSGNNHPKATPLRETPHKNDSVVLPEFGSAQKRTAINLGSFNTSTNAALSKLEEQSTSRLMEKMNLNSTVTLPPDTLEKIQNVQDLLHKMRVSKDPDEQENAISQVYMKICDGGFGIWEQCYAKLLLNLFEILSTSRSENNKKMCLRILGKMCTAQAAKLFDSTEMAVCKVLDAAVNTNDATTALAVDDCLRTLATHLPLANIINIAKVILIQEPIDDERASLVLKMVTRLFEELPADELKNVVDDITPCVIKAYQSTSSSVRKTVVYCLVAMVNRVGEQRMAPHFTKLPKAMTNLIQVYVNRAISTSLPRL
Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules.
Q61QN4
B7NNT3
ARNC_ECO7I
Undecaprenyl-phosphate Ara4FN transferase
null
MFEIHPVKKVSVVIPVYNEQESLPELIRRTTKACESLGKEYEILLIDDGSSDNSAHMLVDASQAEGSHIVSILLNRNYGQHSAIMAGFSHVTGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQNRQDSWFRKTASKMINRLIQRTTGKAMGDYGCMLRAYRRHIVDAMLHCHERSTFIPILANIFARRAIEIPVHHAEREFGESKYSFMRLINLMYDLVTCLTTTPLRMLSLLGSIIAIGGFSIAVLLVILRLTFGPQWAAEGVFMLFAVLFTFIGAQFIGMGLLGEYIGRIYTDVRARPRYFVQQVIRPSSKENE
Catalyzes the transfer of 4-deoxy-4-formamido-L-arabinose from UDP to undecaprenyl phosphate. The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides.
B7NNT3
Q85G16
CYB6_CYAM1
Cytochrome b6
Cyanidioschyzon
MSKVYDWFQERLSIQDIADDITSKYVPPHVNIFYCLGGMTLTCFLVQVATGFAMTFYYRPTVAEAFSSVEYMMTQVNFGWLIRSLHRWSASMMVLMMILHIFRVYLTGGFKKPRELTWITGVILGVLTVSFGVTGYSLPWDQVGYWACKIVTGVPEAIPVVGSSLVELLRGDVSVGQATLTRFYSLHTLVLPVLSLVFMLAHFLMIRKQGISGPL
Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Q85G16
Q7U2S5
HTDZ_MYCBO
Enoyl-CoA hydratase 2
Mycobacterium tuberculosis complex
MRTFESVADLAAAAGEKVGQSDWVTITQEEVNLFADATGDHQWIHVDPERAAAGPFGTTIAHGFMTLALLPRLQHQMYTVKGVKLAINYGLNKVRFPAPVPVGSRVRATSSLVGVEDLGNGTVQATVSTTVEVEGSAKPACVAESIVRYVA
Shows trans-enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydratase activity.
Q7U2S5
A0QWT1
RPOZ_MYCS2
Transcriptase subunit omega
Mycolicibacterium
MSTPHADAQLNAADDLGIDSSAASAYDTPLGITNPPIDELLSRASSKYALVIYAAKRARQINDYYNQLGDGILEYVGPLVEPGLQEKPLSIALREIHGDLLEHTEGE
Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
A0QWT1
Q4UTQ7
MIAA_XANC8
Isopentenyl-diphosphate:tRNA isopentenyltransferase
Xanthomonas
MAADQRPLAIAVMGPTASGKTALAIEAAQRWGGEIVSVDSALVYRGLDIGAAKPDAAMRAAVPHHLLDLRDPWQVYSAAEFAADARTAMAQIVARGKIPILAGGTGLYFRAALEGLAQMPEADPAVRLAIAAEAEQVGWGALHAQLARIDPVAAARIHATDRQRIQRALEVYRISGKPISYWQTRPAGPRAPVRVLKLVLAPRQRAVLHARIAMRLDVMLADGFLTEVEQLRALPQMRAVAAPLDLPAVRAVGYRQAWEYLDGAGSLAEFRDKAVQATRQLAKRQLTWLRGELDARWFDPERDRGQLEQAVAGFLGQRRTMQQPSAV
Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Q4UTQ7
P82804
PYM_DROME
Protein within the bgcn gene intron
Sophophora
MSTYLQSSEGKFIPATKRPDGTWRKARRVKDGYVPQEEVPLYESKGKQFVAQRQAGVPPGMCPLLAAESKKEREKQERTRAKKQEKESGRQPKAPAPGVLVMPPSTCPPPKVSQQQQQQQQQPSGSRDINSISKTLEDTLKLDAAQEVVDPAKQLKKLRKKIREIEQIESRIQAGEQKKLDKDQLDKVKKKSEILRQIKDLESTPRS
Regulator of the exon junction complex (EJC), a multiprotein complex that associates immediately upstream of the exon-exon junction on mRNAs and serves as a positional landmark for the intron exon structure of genes and directs post-transcriptional processes in the cytoplasm such as mRNA export, nonsense-mediated mRNA decay (NMD) or translation. Acts as an EJC disassembly factor by disrupting mature EJC from spliced mRNAs. Required for normal localization of osk mRNA to the posterior pole of the developing oocyte. Does not interact with the small ribosomal unit or components of the translation initiation complex. May not function in cap-dependent translation regulation.
P82804
Q54TC5
NTPPB_DICDI
Maf-like protein DDB_G0281937
Dictyostelium
MTSRPLILGSSSIWRKQVLIDMGYIFKTMSPDIDEKAIRDSDPKTLTLLISRAKAQALLKRIKESDDELDKKSIMICSDQVIVHNGVIREKPETEQQCREYLQSYEFHPAVAVVSVVVVNIETGKIVEGTDIATQHFKKISDEFIDKLIKQGDVMHCAGGFTVEHMADFTLQLEGEVETILGLPKTLTKNLISQVSQ
Nucleoside triphosphate pyrophosphatase that hydrolyzes 7-methyl-GTP (m(7)GTP). May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Q54TC5
Q720K2
UNG2_LISMF
Uracil-DNA glycosylase 2
Listeria
MIKLGNDWDELLKDEFNQPYYLTLRQFLKKEYQTKKVFPDMYDIFNALKYTACKDVKVVILGQDPYHGPGQAHGLSFSVQQGVQIPPSLQNIYLELHNDLNCEIPNNGYLIRWADQGVLLLNTVLTVRAGQANSHRGQGWEILTNRIIEIINQKEEPVVFLLWGNNAKEKLQLLTNPKHTAFTSVHPSPLSASRGFMGCKHFSKTNQFLEQNGVKPIDWQIPSI
Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
Q720K2
Q64ZA7
NRFA_BACFR
Ammonia-forming cytochrome c nitrite reductase
Bacteroides
MEKKLKSWQGWLLFCGAMAVVFVLGLVVSSLMERRAETVSVFNNKRVEITGIEARNEVFGENYPRQYETWKETAKTDFKSEFNGNEAVDVLEQRPEMVVLWAGYAFSKDYSTPRGHMHAIEDITHSLRTGAPMDDKSGPQPSTCWTCKSPDVPRMMEAIGVDSFYNNKWGAFGSEIVNPIGCADCHEPTNMKLHISRPALREAFARQGKDIDKATPQEMRSLVCAQCHVEYYFKGDGKYLTFPWDKGFSVEDMEAYYDEADFADYTHALSKARILKAQHPDYEISQMGIHAQRGVSCADCHMPYKSEGGMKFSDHHIQSPLAMIDRTCQVCHRESEETLRNNVYDRQRKANEIRGRLEQELAKAHIEAEFAWDKGATDVQMAEALKLIRQAQWRWDFGVASHGGAFHAPQEIQRILGHGLDKALQARLAISKVLAQHGYTADVPMPDISTKEKAQEYIGLDMEKERKAKGKFLKTIVPEWLEKARANGRLAKL
Catalyzes the reduction of nitrite to ammonia, consuming six electrons in the process.
Q64ZA7
B5ZY09
CLPX_RHILW
ATP-dependent Clp protease ATP-binding subunit ClpX
Rhizobium
MSKVSGSNGGDSKNTLYCSFCGKSQHEVRKLIAGPTVFICDECVELCMDIIREENKSSMVKSRDGVPTPQDIIKVLDEYVIGQRQAKKILSVAVHNHYKRLAHASKNGEVELAKSNIMLVGPTGCGKTYLAQTLARIIDVPFTMADATTLTEAGYVGEDVENIILKLLQSADYNVERAQRGIVYIDEVDKISRKSDNPSITRDVSGEGVQQALLKIMEGTVASVPPQGGRKHPQQEFLQVDTTNILFICGGAFAGLDKIISARGEKTSIGFGATVKAQDDRRVGEVLRELEPEDLVKFGLIPEFIGRLPVLATLEDLDEDALIQILSEPKNALIKQYQRLFEMEDVELTFHEDALREIARKAIVRKTGARGLRSIMEKILLDTMFELPTLEGVREVVISEEVVRGSARPLYIYADRQEEKANASA
ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.
B5ZY09
P13189
GLUC_CALMI
Glucagon
Callorhinchus
HSEGTFSSDYSKYLDSRRAKDFVQWLMST
Glucagon plays a key role in glucose metabolism and homeostasis. Regulates blood glucose by increasing gluconeogenesis and decreasing glycolysis.
P13189
B5FAW4
HSCA_ALIFM
Chaperone protein HscA homolog
Aliivibrio
MLLQIAEPGQSAVPHQHKLAVGIDLGTTNSLVASVRSGEAKTLPDMKGNVILPSVVQYQEDKICVGMNAYQSAAMDPQNTIISVKRLMGRSLKDIQARYPELPYQFSESENGLPVIQTAQGEVNPIQVSSEILKSLSRRAQDTLGGELEGVVITVPAYFDDAQRAGTKDAATLAGLNVLRLLNEPTAAAIAYGLDSGQEGVIAVYDLGGGTFDISILRLSKGVFEVLATGGDSALGGDDFDHVLAQWIKEQAGITSSLSSQEQRELLTLATQTKVALSDSDNVKISFKDWSGEISVELFNSLIQPLIKKTLMACRRALKDADITSEEVMEVVMVGGSTRTPFVRTSVGDYFGQTPLTSIDPDQVVAIGAAIQADILVGNKPDSEMLLLDVIPLSLGIETMGGLVEKIIPRNTTIPVAKAQEFTTFKDGQTGMMVHVVQGEREMVEDGRSLARFSLKGIPPMAAGAAHIRVTYQVDADGLLSVTAMEKSTGVQSHIQVKPSYGLSDNEVANMLKDSMTYAKEDMQARALAEQQVEADRVIEGLVVALNNDGDALLSKEEQAEILQAIEALITLRQGTDAQAIEDGIKKADEASQEFAARRMDASIRAALAGQSIDEV
Chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB.
B5FAW4
A7HM42
RL14_FERNB
null
Fervidobacterium
MIQNESYLVAADNSGAKVLRVIRVLGGSHKQFGTIGDIVVCSVREAVPNTDIKKGDVVKAVVVRTKKEIRRPDGSYIRFDDNAAVVLDKFNQPKGTRVFGPVARELREKGFMKIVSLAPEVW
Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome.
A7HM42
Q6DKI2
LEG9C_HUMAN
Galectin-9-like protein B
Homo
MAFSGCQAPYLSPAVPFSGTIQGGLQDGFQITVNGAVLSCSGTRFAVDFQTGFSGNDIAFHFNPRFEDGGYVVCNTRQKGTWGPEERKMHMPFQKGMPFDLCFLVQSSDFKVMVNGSLFVQYFHRVPFHRVDTISVNGSVQLSYISFQNPRAVPVQPAFSTVPFSQPVCFPPRPRGRRQKPPSVRPANPAPITQTVIHTVQSASGQMFSQTPAIPPMMYPHPAYPMPFITTIPGGLYPSKSIILSGTVLPSAQRFHINLCSGSHIAFHMNPRFDENAVVRNTQINNSWGSEERSLPRKMPFVRGQSFSVWILCEAHCLKVAVDGQHVFEYYHRLRNLPTINKLEVGGDIQLTHVQT
Binds galactosides.
Q6DKI2
Q4UYZ4
HEM3_XANC8
Pre-uroporphyrinogen synthase
Xanthomonas
MTTLRIATRKSPLALWQSEHVATALRQHHPGLEVVLVPMSTRGDEVLDRSLAAIGGKGLFLKELELAMLRGEADCAVHSLKDVPMELDAPFVLPAILERGDPADALVSNLYATLQALPLGARVGTSSLRRQAQLRAARPDLELIDLRGNVNTRLAKLDNGGYDAIVLACAGLQRLGLEARITARLDAPEWLPAPAQGAVAVECRGDDARIHDLLAVLDAGRTRACVEAERAMNRALHGSCHVPVAAFARWEGEDLFLQGMVGSASDGRLIHAEAHGSPDATEDLGRLVADGLFEKGAAQLLAEL
Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Q4UYZ4
Q9A2B4
RIMM_CAUVC
Ribosome maturation factor RimM
Caulobacter
MAVSPDDPLILVGRVAGGFGVRGEVRITTYTEDPLSIAGFKALKRQDGSPALTIASARKTKDGVVCRCPGVETKEAADALRGLRLYVPRSALPEPDDDEFYLTDLVGLTVRHIQTDQLLGRVKSVQNFGAGDILEITPDLGGPTWYLPFTRAAVPEVRVSEGLILADPPALVGDHEGPEEKGLDENEELGDRD
An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Probably interacts with S19. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Q9A2B4
Q11U60
RS15_CYTH3
30S ribosomal protein S15
Cytophaga
MYLTSEIKKEIFKTNGTAKSATDTGSPESQIALFSHRIAHLTEHLKVNKKDYSTQLGLMKLVGKRRRLLNYLQKTEISRYRAIIAQLNLRK
Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome.
Q11U60
Q9CQN1
TRAP1_MOUSE
Tumor necrosis factor type 1 receptor-associated protein
Mus
MACELRAVLLWGRGLQTVLRAPALAGVRRGKPVLHLQKTTVQFRGPTQSLASGISAGQLYSTQAAEDKEEESLHSIISNTEAVRGSVSKHEFQAETKKLLDIVARSLYSEKEVFIRELISNASDALEKLRHKLVCEGQVLPEMEIHLQTDAKKGTITIQDTGIGMTQEELVSNLGTIARSGSKAFLEALQNQAETSSKIIGQFGVGFYSAFMVADKVEVYSRSAAPESPGYQWLSDGSGVFEIAEASGVRPGTKIIIHLKSDCKDFASESRVQDVVTKYSNFVSFPLYLNGKRINTLQAIWMMDPKDISEFQHEEFYRYIAQAYDKPRFTLHYKTDAPLNIRSIFYVPEMKPSMFDVSRELGSSVALYSRKVLIQTKAADILPKWLRFIRGVVDSEDIPLNLSRELLQESALIRKLRDVLQQRLIKFFIDQSKKDAEKYAKFFEDYGLFMREGIVTTAEQDIKEDIAKLLRYESSALPAGQLTSLPDYASRMQAGTRNIYYLCAPNRHLAEHSPYYEAMKQKHTEVLFCYEQFDELTLLHLREFDKKKLISVETDIVVDHYKEEKFEDTSPADERLSEKETEDLMAWMRNALGSRVTNVKVTFRLDTHPAMVTVLEMGAARHFLRMQQLAKTQEERAQLLQPTLEINPRHTLIKKLCQLRESEPELAQLLVDQIYENAMIAAGLVDDPRAMVGRLNDLLVKVLEKH
Chaperone that expresses an ATPase activity. Involved in maintaining mitochondrial function and polarization, downstream of PINK1 and mitochondrial complex I. Is a negative regulator of mitochondrial respiration able to modulate the balance between oxidative phosphorylation and aerobic glycolysis. The impact of TRAP1 on mitochondrial respiration is probably mediated by modulation of mitochondrial SRC and inhibition of SDHA.
Q9CQN1
B3QZT4
RL21_PHYMT
50S ribosomal protein L21
16SrX (Apple proliferation group)
MFAIIKNGSKQFRVFEGQEIFVEKISLMEKSNYEFKEILAIGGKNNILGQPFVSGAKVQAQIIKHGRAKKIIVFKYKSKKKYRCKQGHRQNYTKLLITKIIA
This protein binds to 23S rRNA in the presence of protein L20.
B3QZT4
Q8G514
RPOB_BIFLO
Transcriptase subunit beta
Bifidobacterium
MATESTTNTTTIIARADQHDIDLHKASDRVNFGSIKEPIDVPYLLGVQTDSFDWLIGNERWKARVEEDEKNGTNTVAHTSGLDEVFNEISPIENFAQTMSLTFSDPYFEEPRHTVQECKEKDYTYSAPLYVNAEFENGDTGEIKSQTVFMGDFPLQTPHGTFIIGGTERVIVSQLVRSPGVYFDRQQDRTSDKEVFGAKIIPSRGAWLEFEIDKKDQPQVRVDRKRKQSAIVFLMAIGMTKSEIAQAFKDYPLVLDALEKETLETQDEALVDLYRKIRPADTPTPEAGKNLLDSFYFNTKRYDLARVGRYKINRKLGVEADFNDRSLHQEDIIATIKYLVALHDGAATFPGKRNGEDVDLRVDVDDIDHFGNRRIRQVGELIQNQLRTGLSRMERVVRERMTTQDAEAITPQSLINIRPVNATIKEFFGTSQLSQFMDQNNPLSGVTNKRRLSALGPGGLSRDRASMEVRDVHPSHFGRMCPIESPEGPNIGLIGSLATFGRVNPFGFIETPYRKVVNGHVTDEVEYMTADRDLDHVIAQANQELDENGNFVQKSALARVGEEEAVDVPVSSVDYMDVSPRQMVSLGASLIPFLEHDEGHRALMGTNMQRQAVPLIESERPLVGTGSEWRAANDSGDVIKSEKDGVVTYVSADLIRVMNDDGTTSSYKLAKFQRSNQTTCYNQRPIVHDGERVEAGSVMADGPAIQNGDLALGKNLLIAFMPWNGYNYEDAVIISQRLVQDDTLSSIHIEEYEIDARETKLGAEEITRDLPNVGEDAVANLDERGIIRIGAEVEAGDILVGKVTPKGETELTPEERLLRAIFGEKSREVRDTSLRVPHGETGTVIGVKEITREDAEEDGDELPNGVNQMIRVYIAQHRKITVGDKLSGRHGNKGCISRILPEEDMPFLADGTPVDIMLNPLGVPSRMNLGQVLELHLGWIAHSGWDISLDPNLEAEWKKLIPSGAEKAEPNTPVATPVFDGVKPEVLKGLLSTTLPNRDGDRLVGPDGKATLFDGRTGEPYTKPISVGYMYMLKLHHLVDDKIHARSTGPYSMITQQPLGGKAQFGGQRFGEMEVWALEAYGAAYTLHEMMTTKSDDVDGRVRVYGAIVKGDNLPPAGIPESFKVLLKEMQSLSLNVEVLNAEGVAIDMKDEDDDPASSADDLGFNIGARPDAAAKEDQKAEEPEYQ
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Q8G514
Q83PC7
MURB_SHIFL
UDP-N-acetylmuramate dehydrogenase
Shigella
MNHSLKPWNTFGIDHNAQHIVCAEDEQQLLNAWQHATAEGQPVLILGEGSNVLFLEDYRGTVIINRIKGIEIHDEPDAWYLHVGAGENWHRLVKYTLQEGMPGLENLALIPGCVGSSPIQNIGAYGVELQRVCAYVDCVELATGKQVRLTAKECRFGYRDSIFKHEYQDRFAIVAVGLRLPKEWQPVLTYGDLTRLDPTTVTPQQVFNAVCHMRTTKLPDPKVNGNAGSFFKNPVVSAETAKALLAQFPTAPNYPQAGGSVKLAAGWLIDQCQLKGMQMGGAAVHRQQALVLINEDNAKSEDVVQLAHHVRQKVGEKFNVWLEPEVRFIGASGEVSAVETIS
Cell wall formation.
Q83PC7
Q66IW8
BRF2_XENLA
B-related factor 2
Xenopus
MSGAKRCPDCGSSEIVEDAHYSQDQLVCADCGCILSEGLITTTVSEETSLQAVRYSDSTGENDSVTYCMKRGIIRVRDLCRVLRLPDGFVDTALSYYKQAVGLPLYRLVSIEKKEIIVGCCVYITCRQQQWPITMGTICSLIYAKKELFASLFMDIVQVLKVDVPSISLQNLVKSHCRSFKLFKDSSEVPPQYAEKLDTVSERTVQTVELAYETWLVTGRHPIPMITAAAYISWQSFQPSRRLSCSLSRFCKLSDVDMPPPSTIRLKELQETLIKLAYHLPWLKILSLNRKNIVQHLGDLLKHRALLLRRALAVTEAELSKGTEASSSTDQLNSTLVFLPPCVSNPKKRSRSIAFPCGDLDITGDEEISDSEIEQYLRTPAEMKDYQQVQSCISSV
General activator of RNA polymerase III transcription. Factor exclusively required for RNA polymerase III transcription of genes with promoter elements upstream of the initiation sites. Contributes to the regulation of gene expression; functions as activator in the absence of oxidative stress. Down-regulates expression of target genes in response to oxidative stress. Overexpression protects cells against apoptosis in response to oxidative stress.
Q66IW8
Q9FRL5
ZHD5_ARATH
Homeobox protein 33
Arabidopsis
MDMRSHEMIERRREDNGNNNGGVVISNIISTNIDDNCNGNNNNTRVSCNSQTLDHHQSKSPSSFSISAAAKPTVRYRECLKNHAASVGGSVHDGCGEFMPSGEEGTIEALRCAACDCHRNFHRKEMDGVGSSDLISHHRHHHYHHNQYGGGGGRRPPPPNMMLNPLMLPPPPNYQPIHHHKYGMSPPGGGGMVTPMSVAYGGGGGGAESSSEDLNLYGQSSGEGAGAAAGQMAFSMSSSKKRFRTKFTTDQKERMMDFAEKLGWRMNKQDEEELKRFCGEIGVKRQVFKVWMHNNKNNAKKPPTPTTTL
Putative transcription factor. Binds DNA at 5'-ATTA-3' consensus promoter regions. Regulates floral architecture and leaf development. Regulators in the abscisic acid (ABA) signal pathway that confers sensitivity to ABA in an ARF2-dependent manner.
Q9FRL5
Q3B1I3
ACCA_CHLL3
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha
Pelodictyon
MATNVVLDFERPVVELEAKLNEMRECLRSSSREQAPVESDALSKEIETLEKKVDALRRSIYKNLTRWQKVQLARHPERPYTLDYIYMMTCDFVELAGDRHFSDDKAIVGGFARLEDRASGYSQPVMVIGHQKGRDTKSNLYRNFGMAQPEGYRKALRLMKLAEKFRKPVITLIDTPGAFPGIEAEERGQAEAIARNLYEMAKLTVPVIVVIIGEGASGGAIGLGVGDRILMAENSWYSVISPESCSSILWRSWNYKEQAAEALQLTAEDLLKQGIIDRIIPEPMGGAHTDPEAMASTLKGMLIEELKALMPVPEKELVNNRIEKFSAMGVWNDEG
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.
Q3B1I3
P55965
BYN_DROME
Protein brachyenteron
Sophophora
MTTSHILSAVDPTTGLSGNVSGGGGGGGAGGGAGSGSPQHVTHNGHGHGHGLGGVAAVSGGGASVSGNGGHRVVGGAGSPNELDRNLRISLDDRELWLRFQNLTNEMIVTKNGRRMFPVVKISASGLDPAAMYTVLLEFVQIDSHRWKYVNGEWVPGGKAEVPPSNPIYVHPESPNFGAHWMKEPISFAKVKLTNKTNGNGQIMLNSLHKYEPRVHLVRVGSEQRHVVTYPFPETQFIAVTAYQNEEVTSLKIKYNPFAKAFLDAKERPDTLYPHDTHYGWLIPPPTHYTAAAAAVAAPPPLSIAQSHGLVASCPSVSSAESVGPSSGGSCDRYGRSLSSRSVAPTRTTPYSRPRVVSGSGSNGSAGNASSTSPQPPSAPQTPTSLHSTSTGSVSTSVSSSSGGGIGSAPSTGCFSSSYAQSGFMSVDASPTASVFSYPSSWQSNGNYWNATSVPGPMPMNVCSGRNISSHNSPSPTNGSPSYTTSSPSYTIHHLTPHSHQYNMAQTDIYGTGVGVGGGAGTTGSPQAAYGAAAHQVYHPTPTSPTHQLYTNAVLNAPSALSYSASGWHNGSGAEYGLYQNAAAAYYQPEYIPLEIGYATHPLEPVDVSKTLDDPQAAMYKPSDEQGSVITLECASSSLKSSHDIKIESSSLEHAGERGTVGGGAAVVSVPTAVVNGAPAVAADTWTPLTPPQSTLQ
Required for the specification of the hindgut and anal pads.
P55965
Q12R42
NADD_SHEDO
Nicotinate mononucleotide adenylyltransferase
Shewanella
MRIGILGGTFDPIHYGHIRPALEVKNALNLDSIWLMPNHIPPHKAGPKTGTAHRLAMVQLVCSQHNEFELCDIEINRDTPSFTVTSLQQLTQAYPEHEFYFIMGMDSFIQLDRWYQWQTLFELCHIVVCQRPGWQLEYTSPMATLMQIKVQQQAIKGNSIKETKVGSIFPVNITAQDISSTEIRAQISAQSMNNQALSPLLPANIIDYIKQHQLYR
Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Q12R42
P05004
IFNA2_HORSE
Interferon alpha-2
Equus
MALPFSLLMALVVLSCHSSCSLGCDLPHTHSLGNTRVLMLLGQMRRISPFSCLKDRNDFGFPQEVFDGNQFRKPQAISAVHETIQQIFHLFSTDGSSAAWDESLLDKLYTGLYQQLTELEACLSQEVGVEETPLMNEDSLLAVRRYFQRIALYLQEKKYSPCAWEIVRAEIMRCFSSSTNLQQS
Produced by macrophages, IFN-alpha have antiviral activities.
P05004
P06834
DAS_PICAN
Glycerone synthase
Ogataea
MSMRIPKAASVNDEQHQRIIKYGRALVLDIVEQYGGGHPGSAMGAMAIGIALWKYTLKYAPNDPNYFNRDRFVLSNGHVCLFQYIFQHLYGLKSMTMAQLKSYHSNDFHSLCPGHPEIEHDAVEVTTGPLGQGISNSVGLAIATKNLAATYNKPGFDIITNKVYCMVGDACLQEGPALESISLAGHMGLDNLIVLYDNNQVCCDGSVDIANTEDISAKFKACNWNVIEVENASEDVATIVKALEYAQAEKHRPTLINCRTVIGSGAAFENHCAAHGNALGEDGVRELKIKYGMNPAQKFYIPQDVYDFFKEKPAEGDKLVAEWKSLVAKYVKAYPEEGQEFLARMRGELPKNWKSFLPQQEFTGDAPTRAAARELVRALGQNCKSVIAGCADLSVSVNLQWPGVKYFMDPSLSTQCGLSGDYSGRYIEYGIREHAMCAIANGLAAYNKGTFLPITSTFFMFYLYAAPAIRMAGLQELKAIHIGTHDSINEGENGPTHQPVESPALFRAMPNIYYMRPVDSAEVFGLFQKAVELPFSSILSLSRNEVLQYPGKSSAEKAQRGGYILEDAENAEVQIIGVGAEMEFAYKAAKILGRKFRTRVLSIPCTRLFDEQSIGYRRSVLRKDGRQVPTVVVDGHVAFGWERYATASYCMNTYGKSLPPEVIYEYFGYNPATIAKKVEAYVRACQRDPLLLHDFLDLKEKPNHDKVNKL
This is the major methanol assimilatory enzyme from the methylotrophic Hansenula polymorpha.
P06834
A7GJZ7
ISPD_BACCN
MEP cytidylyltransferase
Bacillus cereus group
MYTLIIPAAGQGKRMGAGKNKLFLLINEVPIIVHTLRAFEKDEACEKIIMAINEQERSDFEALIQKYGIRKNVQFIQGGAERQDSVYHALQYVKETEYVLVHDGARPFVTNKMIHEVLIVAKEKGASICAVPVKDTIKKVVNDAVFETVERSQLRAVQTPQGFSVALLLEAHQSAKQSGFLGTDDASLVERIGKEVGVVEGSYYNIKVTTPEDLLIAESFLHVQRR
Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
A7GJZ7
Q9HEG2
LOC1_NEUCR
60S ribosomal subunit assembly/export protein loc-1
Neurospora
MAPTKTIKNKHAANKSGIKGSKDAERSRNDGVLKSKGKPKGKAHTLVTASKGRPNIQELIARKKKKKTYSEKELAIPELNMITPVGVTKPKGKKKGKVFVDDKESMATILAIVQAEKEGQIESKMIKARQMEEIREARRAEAEKKEAERKARLEETKDSLRKKRKRSKQSGGSKGDDDDDSRDVKEFSSAGTKAVKSKKKKSVSFAAPE
Required for efficient assembly and nuclear export of the 60S ribosomal subunit.
Q9HEG2
Q9LFV0
RRP32_ARATH
Plastid-specific 30S ribosomal protein 3-2
Arabidopsis
MAVQANQSASFGFRTASPSQKLSSKPIAHISLSTKLKPSSRPSLSCSTWNQGQIPARHSCINPGIFAYPPSNLTFSHELPESESPPLGKKKMRVLVKPLEKPKVVLKFVWMQKDIGVALDHMIPGFGTIPLSPYYFWPRKDAWEELKTLLESKPWISELHRVFLLNQATDIINLWQSSGGDLS
Probably a ribosomal protein or a ribosome-associated protein.
Q9LFV0
Q10287
BGS1_SCHPO
1,3-beta-D-glucan-UDP glucosyltransferase
Schizosaccharomyces
MDQYWREQEGRGLFEDDANSYVSDDDTMSSLTRMIYDKNSSRDALHSDYDSSSFNVDSSSVAYPAWNQAGEEAPVTMEGVQEILLDLTNKLGFQKDNMRNIFDYVMVLLDSRASRMSPSSALLTIHADVIGGEHANFSKWYFASHFNDGHAIGFHDMSSPIVETMTLKEAEQAWRDQMAAFSPHRMMVQVCLYFLCWGEANNVRFVPECLCFIFECAYDYYISSEAKDVDAALPKEFYLDSVITPIYRFIHAQLFEILDGKYVRRERDHSQIIGYDDINQLFWSYKGLQEIMCADKTPLLDLPPFMRYRHLSDVEWKSCFYKSYYEYRSWFHNVTNFSRIWVMHISAYWYYSAYNSPNLYTKNYHIRLNNKPPASCRWTACGLAGAIASFITLAAVVFEYIHVPRRYHSARRLWPSMLLLISTLLLNIAPVVFIFASSTKEQHYASRLVVGIVHFFFSLVCVVYYSITPLRNLVGFTTKRSGKNLANRFFTANFTPTSKTGAFVSWCLWITVLVAKFLESYFFLTLNLADSIRFLGAMRPYDCRDYILGAGLCKAQPKILLSLLYLTDLSLFFLDTYLWYILISTIYSLAYAFCLGISVWTPWRELFYRVPRRIYTKLLYTDDMEIVFKPKVLISQVWNAIIISMYREHLISRTQIQELLYHQVPSEKAGYHTLRAPNFFYSQQVKHYKQDLFPANSEAARRISFFAQSLAESIPKTSSIDAMPTFTVLVPHYSEKILLSLREIIREEDQLSRVTLLEYLKQLYPVEWRNFVDDTKLLADENDSVIGSIDNEKNGVNKAYDLPFYCVGFKSATPEYTLRTRIWASLRTQTLYRTINGFSNYSRAIKLLYRTETPELVEWTNGDPVRLDEELDLMANRKFRFCVSMQRYAKFTKEEAENAEFLLRAYPDLQIAYMDEDPQSRHNDERHLYSVLIDGHCPIMENGKRRPKYRIRLSGNPILGDGKSDNQNMSIPYIRGEYVQMIDANQDNYLEECLKIRSILAEFEQLTPPLHSPYSVNAKAADNHPVAILGAREYIFSENTGMLGDVAAGKEQTFGTLFARILSLIGGKLHYGHPDFINVLFMITRGGVSKAQKGLHVNEDIYAGMIALQRGGRIKHCDYYQCGKGRDLGFGSILNFTTKIGTGMAEQMLSREYFNLGTQLPFDRFLSFFYAHAGFHVNNMVIMFSLQLLMLVIINLGAMYTVVPVCRYRQFDSLTASLYPEGCYQLKPVLEWLKRCILSIFIVFGIAFVPLAVCELGERGAIRMVIRLAKQIFSLSPIFEIFTCQIYAQSLIANLTFGGARYIGTSRGFATVRVPFSLLYSRFSGPSLYFGSRLMYMLLFGSITAWLPHYIYFWITLTALCISPFLYNPHQFAWTDFFVDYREFMRWLFRENSRNQANSWIGNCQLCRTRVTGYKRKIYGKKADKIAMDSPRARITTMFYGEILGPLGTLFFTCIPFLFINSQPGNDDETQSTNAFIRLIIMSVAPLVLSAIIAFFFFCLGIMLRPILGDRSKTYGVYLAGVAHFLFVCVDVVVFEVLGYLEGWSFSKTLLGFVAIISIHRFAHKFFIICFLSREFRHDGANLAWWSGRWNGQGFGYMVLTQPWREFVCKTTELNMFAGDFLLSHLLLFLQAPVILIPYIDKLHSIILFWLVPSRQIRPPIYTIRQNKLRRQIVLRYATLYFSLFIAFFVLLILPFVFGKSAAGTSMDKFNLIQPATKIVYSSTKNSSV
Required for the assembly of the division septum and maintenance of cell polarity.
Q10287
O94534
ALP14_SCHPO
Altered polarity protein 14
Schizosaccharomyces
MSQDQEEDYSKLPLESRIVHKVWKVRLSAYEECSKSFSLSADGSDNCFELWNNQSELWKSVLTDSNVAAQEAGTAAFVAYCRFSDPSHLLKAREISVLSISEKCLTSPRAGTRENALEALMLLVEADSAAPVIESIIPSLSARSPKVIASNVAAIASLVEQFGAKVIPSKMIIPHISNLFGHADKNVRKEASRLTVNIYRWTGDPLKDLLFKDLRPVQTKELESLFAELPTEPPKQTRFLKSQQPTSEPNVETQVEEQPALENEESEPEPSDDQFDLVEEVDVLPNVDPNLETLMASSKWKDRKEALDKLLPVLSQPKIKDNDFFNLVAILTKSVSKDANIMVVINAAHCIQAMAKGLRSNFSKYASTSINALLERSKEKKANVIESLSSAMDAVLATSSLDDLAELIASFAGNKNPQIKSSCFSLFSRSFSNMTSLPSKFTVDTCAKACVPGVSDTFEPVRSAAAEALGVLMKLVGERAINQYLSPLDDIRKSKIRSFYETATVKAKAPTKKSKVKPSKQEESKVVVPSNAKAVKKSVVPSSPVVPSPRKATNKSLSMDVSKGNAFENGPLLPRPTTRPVSRGLSRGTSSSLQQKVKASTPLNSGALNETVQNLKNMELDDPAPQPAKHSRVDRYEHPKVLEDNDSTISSLESLKRENEELREQLKVEHEENISMQKQLSELKGELNTLRSARKASPIGDRKPAFMRRANTDFLELSTSPSFQRSVREFEPTRPKLYSSIDVNQRSPLASAKTNGNFTFHAELPRSPFSSRANNINPDWTKAIDLAAKLKQKITEMKQTDQRHQGLIH
Required for bipolar spindle formation and proper chromosome segregation. Has a role in connecting the kinetochores and the plus end of pole to chromosome microtubules. Also required for the activation of the spindle checkpoint pathway.
O94534
Q8UIN7
RL20_AGRFC
50S ribosomal protein L20
Agrobacterium tumefaciens complex
MARVKRGVTSRAKHTKTLKAAKGFYGRRKNTIRAAKAAVDRSKQYAYRDRKVNKRNFRALWIQRINAAVRESGLTYGRFIDGLNKAGIEVDRKVLSDMAIHEPAAFGALVEAAKKALEYLKDAGTTNEFETAVK
Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit.
Q8UIN7
A1R863
MNMA_PAEAT
tRNA-specific 2-thiouridylase MnmA
Paenarthrobacter
MRVLAAMSGGVDSAVAAARAVEAGHDVVGVHLALSRMPGTLRTGSRGCCTIEDSRDAWRACDVLGIPYYVWDFSERFKEDVVQDFIDEYAAGRTPNPCMRCNERIKFAALLEKAIALGFDAVCTGHYAKVIEDADGNRELHRAADWAKDQSYVLGVLTHEQLKHSMFPLADTPSKAEVRAEAERRGLSVANKPDSHDICFISDGDTRGWLAEKIDMTTGDIVDETGAKVGEHPGANAFTVGQRRGLKLGTPAADGKPRFVLEIRPKENKVVVGPEALLAIDEIRGIKVSWAGLPISEVATGAEFDCHAQVRAHGDPVPAIARVEAVTDESGVERAQLVVTLTDPLRGVAPGQTVVLYQGSRVLGQATIDAARSLQRQVL
Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
A1R863
A3CW56
RNP2_METMJ
Pop5
Methanoculleus
MRPRPPAMRTKRRYILARILPYRARVDQKQMYFAVIEAATSLLGDAAAGLAQPAVVFCEGGYVVVRCRRGTEKDVAVALSTVTAVADERIALRTVATSGTIHALRRRMRSIRQLPGDEEVKIGETYFAVYRYPRQKVDLVEKGIKHQKSLFFTEADLEER
Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.
A3CW56
O06928
MADH_MALRU
[Acyl-carrier protein]:acetate ligase
Malonomonas
MAEQLKELAEMVESFGTAPTMGEMPCRTLATKGINGPTAAHVIEEIHTPFNLAYVTFTTGSTAFQNVVGVTHSEIDGRVRASLAAFDMANVERHGKFLVTYAPLVNVFSAEALKIHGLDWFFLQRSSRDAFLLSLCQEKPNVLIGESTFIRSALEDASVLGLSHSIPQGVIAFTAGTPLDLDLLQVAEKHNWKIHDLYGCQEFGWLTLDGVPLRADITLIPSPKGSDFREFVVGGLPMADSFPYAESGHVCNPEGKIITYRRARTNPEYEVIVRETKLSSKETTERVARTILRIKGRVVKVDPALKVSSTKTVLDLVPSVSAEGKSTSESYRIEGDDKTFLFETLIEAQLALQQTAKTDQVWKKTR
Acyl-carrier protein (ACP) acetate ligase of the biotin-dependent malonate decarboxylase multienzyme complex (EC 7.2.4.4). Involved in the conversion of the thiol group of the ACP-bound 2'-(5-phosphoribosyl)-3'-dephospho-CoA prosthetic group into its acetyl thioester using the energy from the hydrolysis of ATP.
O06928
P85084
CHIT_CARPA
Endochitinase
Carica
GIEKIISRSMFDQMLKHRNNPACPAKGFYTYDAFLAAAKSFPSFGTTGSTDVRKRELAAFLGQTSHETTGGWPSAPDGPYAWGYCFLKERNPSSNYCAPSPRYPCAPGKSYYGRGPLQLSWNYNYGPCGEALRVNLLGNPDLVATDRVLSFKTALWFWMTPQAPKPSCHDVLTGRWQPSAADTAAGRLPGYGVLTNLLNGGLECGKGPNPQVADRLGFFRRYCGLLGVGTGNNLDCYNQRPFG
Defense against chitin-containing fungal pathogens. Shows activity on chitin, tetra-N-acetylglucosamine and chitosan.
P85084
Q8TXJ2
RS12_METKA
30S ribosomal protein S12
Methanopyrus
MPGKKSPAGEFAARKLREKRKKFRWKDERYKRRMLKLDEKADPLEGAPQARGIVLEKVGVEAKQPNSAIRKCVRVQLIKNGKQVTAFCPGDGAIDYIDEHDEVVIEGIGGPKGRAKGDIPGVRYKVVKVNDVALSELLKGKIEKPMR
With S4 and S5 plays an important role in translational accuracy. Located at the interface of the 30S and 50S subunits.
Q8TXJ2
Q3JEJ6
RS6_NITOC
30S ribosomal protein S6
Nitrosococcus
MRHYEVVFLVHPDQSEQLSAMMDRYRQIIETDGGCIHRLEDWGRRQLAYPIQKLYKAHYVLMNIECTPRTIEELTSAFRFNDAVLRDMVIRREEAITETSPLAKGEESGGRGYDSARSGRDRDESGGRGYDGARPGRDEDESKENTDRDEQSEDSE
Binds together with S18 to 16S ribosomal RNA.
Q3JEJ6
A3P0Z1
ATPG_BURP0
F-ATPase gamma subunit
pseudomallei group
MAGMKEIRGKIKSVQNTRKITKAMEMVAASKMRRAQERMRAARPYAEKVRAIAAHMSRANPEYRHPFMVANDGVKTAGMILVTTDKGLCGGLNTNVLRASLQKFKELEEQGQKVEATAIGGKGLGFLNRFGAKVISQVVHLGDTPHLDKLIGAVKTQLDLYSEGKLSAVYLAYTRFVNTMKQETVIEQLLPLSSEHFDTNDGTPATSWDYIYEPDAQAVVDELLVRYVEALVYQAVAENMASEQSARMVAMKAASDNAKTVISELQLSYNKSRQAAITKELSEIVGGAAAV
Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
A3P0Z1
Q57QS3
RLMI_SALCH
rRNA (cytosine-C(5)-)-methyltransferase RlmI
Salmonella
MTESTFPQYPRLVLSKGREKSLLRRHPWVFSGAVSRLEGKANLGETIDIVDHQGKWLARGAWSPASQIRARVWTFDKAESIDIAFFTRRLRQAQQWRDWLAKKDGLDSYRLIAGESDGLPGVTIDRFGHFLVLQLLSAGAEYQRAALISALQTCYPDCAIYDRSDVAVRKKEGMALTQGPVTGELPPALLPIEEYGMKLLVDIQGGHKTGYYLDQRDSRLATRRYVENQRVLNCFSYTGGFAVSALMGGCRQVVSVDTSQDALDIARQNVELNQLDLSKAEFVRDDVFKLLRAYREHGEKFDVIIMDPPKFVENKSQLMGACRGYKDINMLAIQLLNPGGILLTFSCSGLMTSDLFQKIIADAAIDAGRDVQFIEQFRQAADHPVIATYPEGLYLKGFACRVM
Specifically methylates the cytosine at position 1962 (m5C1962) of 23S rRNA.
Q57QS3
Q9BSK1
ZN577_HUMAN
Zinc finger protein 577
Homo
MKNATIVMSVRREQGSSSGEGSLSFEDVAVGFTREEWQFLDQSQKVLYKEVMLENYINLVSIGYRGTKPDSLFKLEQGEPPGIAEGAAHSQICPGFVIQSRRYAGKDSDAFGGYGRSCLHIKRDKTLTGVKYHRCVKPSSPKSQLNDLQKICAGGKPHECSVCGRAFSRKAQLIQHQRTERGEKPHGCGECGKTFMRKIQLTEHQRTHTGEKPHECSECGKAFSRKSQLMVHQRTHTGEKPYRCSKCGKAFSRKCRLNRHQRSHTGEKLYGCSVCGKAFSQKAYLTAHQRLHTGDKPYKCSDCGRTFYFKSDLTRHQRIHTGEKPYECSECEKAFRSKSKLIQHQRTHTGERPYSCRECGKAFAHMSVLIKHEKTHIRETAINSLTVEKPSSRSHTSLYMSELIQEQKTVNTVPIEMPSSGTPPLLNKSERLVGRNVVIVEQPFPRNQAFVVNQEFEQRISLTNEVNVAPSVINYILYLTDIVSE
May be involved in transcriptional regulation.
Q9BSK1
P57762
PCNA1_SULOH
Proliferating cell nuclear antigen homolog 1
Sulfurisphaera
MRIVYDDVRDLKAIVQALLKLVDEALFDIKPEGIQLVAIDKAHISLIKIELPKEMFKEYDVPEEFKFGFNTQYMSKLLKAAKRKEEIIIEADSPEVVKLTLSGALNRVFNVNNIEVLPPEVPEVNLEFDIKATINASGFKNAIGEIAEVADTLLISANEEKVIVKGEGENKVEVEFSKDTGSLADIEFNKESSSAYDVEYLNDIISLTKLSDYVKVAFAEQKPMQLEFNMEGGGKVTYLLAPKLS
Sliding clamp subunit that acts as a moving platform for DNA processing. Responsible for tethering the catalytic subunit of DNA polymerase and other proteins to DNA during high-speed replication.
P57762
B7H673
PROA_BACC4
Glutamyl-gamma-semialdehyde dehydrogenase
Bacillus cereus group
MNEVLAKGIKAKEVARELVLKSTEQKNEALSAIADQLILETAYILEENKRDIEEGKAKGFSDSLLDRLLLTENRIIDMTEGIKQLIELRDPVGECVSAWERPNGLSIQEMRVPLGVIGMIYEARPNVTVDAATICLKTGNAVILRGSSSAIHSNKAIVAVIHRALKLTSLPQESVQLIEDTTRNSAKQLFTMKDYLDVLIPRGGKQLIDTVVREASVPVLETGAGNCHIFIDETADKQMAFNIIINAKTQRPSVCNAIETIVLHENWAEQYGSELFSSLKERGVELRGDNKAVAIDSSILLATEEDWETEFLSLTLAVKVVSTVEEAIHHINTYGSMHSEAIITENEENVSKFFTSVDAAALYHNASTRFTDGSEFGFGAEIGISTQKLHVRGPMGLPALTSTKYVIRGNGQIRK
Catalyzes the NADPH-dependent reduction of L-glutamate 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate.
B7H673
D2S9Y8
DAPD_GEOOG
Tetrahydropicolinate succinylase
Geodermatophilus
MTDSAPHSAVAAGLATVTPAGTVLDTWYPEPRLGVPAGARPGTTRLGALEISGELGPDYGGLVRRDESRGVEVIAVRTVIPDLAAAPVDTHDVWLRLHLLSHRLVSPRSISMDGVFGLLTNVAWTSAGPVEAATFNVHRLRAALGHVTVFGVDKFPRMVDYVIPSGVRVADGDRVRLGAHLAEGTTVMHEGFVNYNAGTLGPSMVEGRISAGVVVGPNSDIGGGASIMGTLSGGGKQVVSIGSGCLLGANAGIGISLGDNCVVEAGCYVTAGSRVTLPDGSVVKAAELSGRDGLLFRRNSVSGALEALPRTGTWGELNAQLHAN
Catalyzes the conversion of the cyclic tetrahydrodipicolinate (THDP) into the acyclic N-succinyl-L-2-amino-6-oxopimelate using succinyl-CoA.
D2S9Y8
P37921
FIMA1_SALTY
Type-1A pilin
Salmonella
MKHKLMTSTIASLMFVAGAAVAADPTPVSVSGGTIHFEGKLVNAACAVSTKSADQTVTLGQYRTASFTAIGNTTAQVPFSIVLNDCDPKVAANAAVAFSGQADNTNPNLLAVSSADNSTTATGVGIEILDNTSSPLKPDGATFSAKQSLVEGTNTLRFTARYKATAAATTPGQANADATFIMKYE
Fimbriae (also called pili), polar filaments radiating from the surface of the bacterium to a length of 0.5-1.5 micrometers and numbering 100-300 per cell, enable bacteria to colonize the epithelium of specific host organs.
P37921
Q8LWN4
NU4LM_TAMTE
NADH dehydrogenase subunit 4L
Tamandua
MSSIYMNILLAFTMALLGLLMYRSHLMSSLLCLEGMMLSLFILSTVTMLNTSFTLSSMMPVMLMVFAACEAAVGLALLVTVSNTYGLDYVQNLNLLQC
Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor.
Q8LWN4
Q96Y90
AROD_SULTO
Type I dehydroquinase
Sulfurisphaera
MTFVVASLPIRSEKDLDKIPRLLDADFVELRLDYSTSLPEIQVIEKYKDRIIVTIRDVDEGGINKIDPEIKAEYLIELNKKNILYDVEAKFAKKYNIPTSNKIVSIHYLDRVPSYSEVFESLRDFIKESFLLKVAVIGKDGYKELLSKLLELEKIAVMPIGVNPLERIAFSILGSKLIYGHAGEETAKGQFHYKVAKQILDYLTSISISSPSILTG
Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.
Q96Y90
Q313S6
MNMA_OLEA2
tRNA-specific 2-thiouridylase MnmA
Oleidesulfovibrio
MHIAVAVSGGTDSLFALLQVLEAGHQVTALHAHFLSPHDTPETTAHNTQAIEKACRALGADFHVEDLSAAFRKHVIEPFIDAYRQGRTPNPCARCNASMKFGLLADTARKLGAQAIATGHYARLQPDLPRPGNTVSLWRGDDPAKDQSYFLSLVPQHRLACAVFPLGGWRKQDVRAHLKQRGIVPPLPSESQEICFIPGDDYRAYLTAHAAGLPGAGPMVLRDGHVVGHHNGLWQYTEGQRRGLGIAWSEPLYVLEKDVSRNALVVGTRKQLTARGCRCVGVNTLVPPDQWPDAVYVKTRYRQTMIAAQVTPDADGADTMRVIFAASHTPPAAGQVAAVYDAAGRVLAGGIIASVF
Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Q313S6
A4QGT5
NADE_CORGB
NH(3)-dependent NAD(+) synthetase
Corynebacterium
MTNTQTEIINELKVSPAIDVAKEVEFRVQFLVDYLRASHAKGFVLGISGGQDSTLAGRLAQLAVERIRAEENSTDYVFYAVRLPYAIQADEDDAQVALEFIAPDKSVTVNVKDATDATEATVAAALELPELTDFNRGNIKARQRMVAQYAIAGQYGLLVIGTDHAAENVTGFFTKFGDGAADLLPLAGLSKRQGAAILEHLGAPSSTWTKIPTADLEEDRPALPDEEALGVSYADIDNYLENKPDVSEGAQQRIEHLWKVGQHKRHLPVTPQEDWWR
Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
A4QGT5
A6VGF5
COBQ_METM7
Probable cobyric acid synthase
Methanococcus
MAKFIMVVGTSSNSGKTVLVSGICRMLSNKGYKVAPFKSQNMSLNSRVSIEDGEIAVAQYTQAMAARAEPSVHFNPILLKPKGNFISQVIVHGTPYEDRDYNEYRSNKDDMLEKIKESIDYLDTNYDYVVIEGAGSCCEINLLKDDIANLRIAEISGADAILVSDIDRGGVFAAIYGTVQLLPENWRKLLKGFVINKFRGNIDVLKDGFEKIEELTNIPVIGTIPYDETLILPEEDSQALEGKRVFGNLKSPIEVNIVKFSKIANFTDVDPLSSDCLMRYLDFNDDITGDILILPGTRCSTVEMDLMKKHGMDKKIMEFIERGGIILGICGGYQTLGKMLIDENFSEGDVGTISGLGLFDMETTFGNKKAIKNSTGKISIFDQNFDVAGYELHEGYSVSNETPLISLSRGFGNCGNSYDGSFKVVGNSYIFGTYFHGILENFEFRNYLVNIVNNRKNLSKIENDNYAEIFNKNMDKLSKLIEESLDLSKIIK
Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation.
A6VGF5
Q7YNV4
PSBM_ARAEL
Photosystem II reaction center protein M
Aralia
MEVNILAFIATALFILVPTAFLLIIYVKTESQNKK
One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. This subunit is found at the monomer-monomer interface.
Q7YNV4
C6Y4A7
EMC5_SCHPO
ER membrane protein complex subunit 5
Schizosaccharomyces
MESSTINAKKISVLLTLFSIIGYTAYSAHESILEIRQDGKLPLDIKCEVILVTLLFTFTTVIIASPLRSIQLNKWSHQRSDLAFLNSRTNFLRIKELKEKIEKVKN
The EMC seems to be required for efficient folding of proteins in the endoplasmic reticulum (ER).
C6Y4A7
P45790
GSPC_AERHY
General secretion pathway protein C
Aeromonas
MTLPFRNDLLSSLLARCKTVPLSRFSQPLFWLLLLLLAHQCAGLTWRLLDLGSQQASQPWQPAMVASQGQGSARLDLSGISRLSLFGKAKQQAQAADAVAADAPKTQLNAQLNGVLASSDPAKSIAIIAHNGVQNSYGIGDFIDGTQAKIRQVFADRVIIERDGRDETLMLDGEEYGKPLPKPGNQDDKLSSVRSELLGNPGKITDYLNISPVRVDGRMVGYRLNPGSNPELFNQLGLVANDMAVSINGLDLRDNAQAMQAMQQVAGATEMTVTVERQGQLYDVYVGLSE
Involved in a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of proteins.
P45790
B7FTW3
TRM51_PHATC
tRNA methyltransferase 5 homolog 1
Phaeodactylum
MLDPVEASSVPVVDDSTIRSLSDFPDRNVFRREDRYPALNIPVRRTAELRKTLKHVLWRRPKTKNVYDDETDPQRRILVLANIDEDAFRDETVQRLIQHEDCRKASYTVTTAYENYTVEEILKQLLPNESEIPSAFEMVGHLAHVNLRSSQLPFKYWIGKVMLDKNQPRIRTVVNKLGTIETEYRTFGMEVIAGYQGENWSVVTVKEERCTFRLDFTKVYWNSRLAGEHRRLVQQILKESQTKPLVVADLMAGVGPFAVPLTASHGRRNQVTVYANDLNPESYKYLLQNVQSNKCTNIHCYNQCGRAMVHQLQAENIEVDHVIMNLPASAPEFLDAFRGYEGVKRPCIHVHCFAPKASEATDYQDALDRCSSALGCTLDRISNDVHVHVVRDVSPNKNMLSVSFLLPVETQSLVKMKLQPLRTETSEPGAKRIKSN
Specifically methylates the N1 position of guanosine-37 in various cytoplasmic and mitochondrial tRNAs. Methylation is not dependent on the nature of the nucleoside 5' of the target nucleoside. This is the first step in the biosynthesis of wybutosine (yW), a modified base adjacent to the anticodon of tRNAs and required for accurate decoding.
B7FTW3
B4RD45
ATPA_PHEZH
F-ATPase subunit alpha
Phenylobacterium
MDIRAAEISAILKSQIANFGEEADVSDVGSVLSVGDGIARVYGLDNVQAGEMVEFPSAGVKGMALNLERDNVGIVIFGEDRAIREGDEVRRLGEIVDVPVGKGLLGRVVNPLGEPIDGKGPIQNVAERRRVDVKAPGIIPRKSVHEPVQTGLKAIDTLIPVGRGQRELIIGDRQTGKTAVAVDTILNQKQVNAGGDESQKLYCIYVAIGQKRSTVAQIVKTLEERGALDYTIVVSATASEPAPLQFLAPFAGCAMGEWFRDNGMHAVIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLNEDNGLGSLTALPIIETQANDVSAYIPTNVISITDGQIFLETDLFFQGIRPAVNVGISVSRVGSSAQIKAMKTAAGPIKGELAQYREMAAFAKFGSDLDVATQRQLARGERLTELLKQPQYSPLAVEEQVVSVYAGTRGYLDKIPTAQVGRFESELLSYMHAKHQDILDEIRTKKDLGPVEDRLKSALAAFADSFA
Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
B4RD45
A4VIT1
PURT_PSEU5
Phosphoribosylglycinamide formyltransferase 2
Pseudomonas
MPRIGTPLSPSATRILLCGCGELGKELVIELQRFGVEVIAVDRYANAPAMQVAHRSHVLDMLDGAALRAVIEQERPHYIVPEIEAIATATLVELEREGYTVIPTARAAQLTMNREGIRRLAAEELGLPTSPYRFADTLDECRAAAMALGFPCLVKPVMSSSGKGQSVLRSDADIDAAWEYAQAGGRAGRGRVIVEGFIDFDYEITLLTVRHAGGTSFCEPVGHRQEKGDYQESWQPQPMAPAALAEAKRIALAVTDALGGRGIFGVELFVKGEQVWFCEISPRPHDTGLVTLVSQDLSEFALHARAILGLPIPVIRQLGPAASAVVLVEGESTQVSFGNLAEVLAEPDTALRLFGKPGVSGQRRMGVALARDTSIDAARQKALRAAAAVKIEL
Involved in the de novo purine biosynthesis. Catalyzes the transfer of formate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR). Formate is provided by PurU via hydrolysis of 10-formyl-tetrahydrofolate.
A4VIT1
B8H9Q1
SYS_PSECP
Seryl-tRNA(Ser/Sec) synthetase
Pseudarthrobacter
MIDVKDLSENPDKFRASQRARGADESVVDAIISADSARRAALIRYENLRAEQNVFGKKVAQAKGEEKQALLAEVKELANSVKAASAEADAAQTKQEELLRTVPNLVEDGVPEGGEDDYVVVKTVGTPREFPDFEPKDHLEIGELIGAIDMERGAKVSGSRFYFLRGVGARLEMALLQMAMEQAIEAGFIPMITPTLVRPETMQGTGFDVKHDAEIYRLAEDDLYLVGTSEVALAGYHADEILDFSAGPIRYAGQSSCYRREAGSHGKDTRGIIRVHQFNKVEMFIYTTVEEAAAEHQRLLAWEEEMLAKCELPYRVIDTAAGDLGNSAARKYDCEAWVPTQGAYRELTSTSNCTTFQARRLNIRERAVNAEGVAKGTRAVATLNGTLATTRWIVALLEHHQNADGSVNVPKALQKYLGGLEVLPVL
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).
B8H9Q1
Q8VIJ5
OGA_RAT
N-acetyl-beta-glucosaminidase
Rattus
MVQKESQAALEERESERNANPASVSGASLEPSAAPAPGEDNPSGAGAAAGTGAAGGARRFLCGVVEGFYGRPWVMEQRKELFRRLQKWELNTYLYAPKDDYKHRMFWREMYSVEEAEQLMTLISAAREYEIEFIYAISPGLDITFSNPKEVSTLKRKLDQVSQFGCRSFALLFDDIDHNMCAADKEVFSSFAHAQVSITNEIYQYLGEPETFLFCPTEYCGTFCYPSVSQSPYLRTVGEKLLPGIEVLWTGPKVVSKEIPVESIEEVSKIIKRAPVIWDNIHANDYDQKRLFLGPYKGRSTELIPRLKGVLTNPNCEFEANYVAIHTLATWYKSNMNGVRKDVVMTDSEDSTVSIQIKLENEGSDEDIETDVLYSPQMALKLALTEWLQEFGVPHQYSSRQVAHSGAKTSVVDGTPLVAAPSLNATTVVTTVYQEPIMSQGAALSGEPSALTKEEEKKQPDEEPMDMVVEKQEESEHKSDNQILTEIVEAKMAEELKPMDTDKESIAESKSPEMSMQEDCINDIAPMQTDEQANKEQFVPGPNEKPLYAAEPVTLEDLQLLADLFYLPYEHGPKGAQMLREFQWLRANSSVVSVNCKGKDSEKIEEWRSRAAKFEEMCALVMGMFTRLSNCANRTILYDMYSYVWDIKSIMSMVKSFVQWLGCRSHSSAQFLIGDQEPWAFRGGLAGEFQRLLPIDGANDLFFQPPPLTPTSKVYTIRPYFPKDEASVYKICREMYDDGVGLPFQSQPDLIGDKLVGGLLSLSLDYCFVLEDEDGICGYALGTVDVTPFIKKCKISWIPFMQEKYTKPNGDKELSEAEKIMLSFHEEQEVLPETFLANFPSLIKMDIHKKVTDPSVAKSMMACLLSSLKANGSRGAFCEVRPDDKRILEFYSKLGCFEIAKMEGFPKDVVILGRSL
Lacks enzyme activity.
Q8VIJ5
Q92GY1
RL6_RICCN
50S ribosomal protein L6
spotted fever group
MSRVGKLPITIPEGVKIGLNDLEVKISGPKGELSKTFKGNIAISLAENKLLVKPLAANKNARAMWGTARSIISNMVTGVKEGFKLKLEINGVGYRAMVKGKYLNLMLAKSHNTKIEIPSDIKIEMPKQNIIILEGTDKEKLGQFASIIIKQRPPEPYKGKGIKFENQCIPRKEGKKN
This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center.
Q92GY1
B8D8P9
AROC_BUCA5
5-enolpyruvylshikimate-3-phosphate phospholyase
Buchnera
MSGNTIGKIFCVTTFGESHGEALGCIIDGTPPGLELSCKDLQYDLNRRRPGTSRYTTLRREPDEVNILSGIFNGVTTGTSIGLIIYNHDHRSQDYSDIKNLFRPGHADYTYEKKYGIRDYRGGGRSSARETAMRVAAGAIAKKYLNEKYGITIRAYLSAMGNIKCPFKSWQEVENNPFFCSDPEKILALENLIKYLKKIGDSIGAEITIIAENIPVGLGEPVFDRLDADLSHALMSINAAKGVEIGDGFSVINQRGSEHRDEITPQGFLTNHSGGILGGISNGREIVLKVAFKPTSSIRKAGNTINKNNEKVQIVTKGRHDPCVGLRAVPITEAMVAIVLMDHLLRFRAQCSGK
Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.
B8D8P9
O67080
GCSH3_AQUAE
Glycine cleavage system H protein 3
Aquifex
MGKQEKDLGTAWEYQGCLIPKDLYYDIENQVWVRVNEDGTVTLGLTDVGQTRAGRLLHIRVKPVGTKVKKGKPVATLESGKWAGPVPALVEGEIVEVNPKVVEDPNYINIDPYGDAWIVKIKPTSEETLKRDLSELAHGEKAHEEMKKHIDEWDIVCMRCV
The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein.
O67080
P72205
CYSZ_MANHA
Sulfate transporter CysZ
Mannheimia
LNFTFGALVSLFTMIPFVNLVVMPVAVCGATALWVKEYRNFFLNNQTGEFSKADYTFTKVNSTSLSTETRTGEVSPNVRNGDIRKQ
High affinity, high specificity proton-dependent sulfate transporter, which mediates sulfate uptake. Provides the sulfur source for the cysteine synthesis pathway.
P72205
Q221N8
GLGC_ALBFT
ADP-glucose synthase
Rhodoferax
MKDGAHHRPVRRTISLVLAGGRGSRLQDLTENCAKPAVHFGGKFRIIDFVLSNCVNSGLHRIGVLTQYKSHSLLRHLQHGWSFLRNEVNEFIDLLPAQQRVDEASWYRGTADAVYQNIDILREHDPKYILVLAGDHVYKMNYASLIEDHVALGAPCTVACIEVPLAEASAFGVMTVDAMRHITRFDEKPAHPQPMLDQPEQALVSMGVYVFDADYLFAALQTDIEDAASHHDFGKDLIPAIVSRGEAMAHPFDLSCVKSSPESPSYWRDVGTVDAYWAANIDLTATIPQLDLYDKDWPIWTYQPTSPPAKFVFDDEGRRGMAVDSLVSGGCIVSGALVRRSVLFTGVHLHSYSSVEESVLLPEADVGRHCRLRKVVVDEGCRIPAGMTIGFDAEDDARRFHVSADGVVLVTVAMLEALRVSQA
Involved in the biosynthesis of ADP-glucose, a building block required for the elongation reactions to produce glycogen. Catalyzes the reaction between ATP and alpha-D-glucose 1-phosphate (G1P) to produce pyrophosphate and ADP-Glc.
Q221N8
Q05865
FOLC_BACSU
Tetrahydrofolylpolyglutamate synthase
Bacillus
MFTAYQDARSWIHGRLKFGVKPGLGRMKQLMARLGHPEKKIRAFHVAGTNGKGSTVAFIRSMLQEAGYTVGTFTSPYIITFNERISVNGIPISDEEWTALVNQMKPHVEALDQTEYGQPTEFEIMTACAFLYFAEFHKVDFVIFETGLGGRFDSTNVVEPLLTVITSIGHDHMNILGNTIEEIAGEKAGIIKEGIPIVTAVTQPEALQVIRHEAERHAAPFQSLHDACVIFNEEALPAGEQFSFKTEEKCYEDIRTSLIGTHQRQNAALSILAAEWLNKENIAHISDEALRSGLVKAAWPGRLELVQEHPPVYLDGAHNEEGVEKLAETMKQRFANSRISVVFSALKDKPYQNMIKRLETIAHAIHFASFDFPRASLAKDLYDASEISNKSWSEDPDDVIKFIESKKGSNEIVLITGSLYFISDIRKRLK
Functions in two distinct reactions of the de novo folate biosynthetic pathway. Catalyzes the addition of a glutamate residue to dihydropteroate (7,8-dihydropteroate or H2Pte) to form dihydrofolate (7,8-dihydrofolate monoglutamate or H2Pte-Glu). Also catalyzes successive additions of L-glutamate to tetrahydrofolate, leading to folylpolyglutamate derivatives.
Q05865
P57034
CTRB_NEIMA
Capsule polysaccharide export inner-membrane protein CtrB
Neisseria
MSEQLPVAVATETKAERKKPKKKSWIKKLSPLFWVTVIIPTVISLVYFGFFASDRFTSQSSFVVRSPKSQSSLNGLGAILQGTGFARAQDDIYTVQEYMQSRSALDALRKKMPIRDFYEKEGDIFSRFNGFGLRGEDEAFYQYYRDKVSIHFDSVSGISNLSVTSFNAGESQKINDALLKQGEVLINQLNERARQDTIRYAQEVVNSAEEQVKEASVQLTKFRVSNGIFDLKAQSDVQMGLVSKLQDELIVIQTQLDQVKAVTPENPQIPGLIAREKSLRKEISQQMKAISGGGEGSLSNQAAEYQRVYLENELAEKQLAAAMTSLESAKAEADRQQLYLEVISQPNKPDLAYEPNRLYNIVATFVIGLIVYGIVVLLSASIREHKN
May form an ATP-driven capsule polysaccharide export apparatus, in association with the CtrC and CtrD proteins.
P57034
A4WG90
RHAR_ENT38
L-rhamnose operon transcriptional activator RhaR
Enterobacter
MGVPLILRKTDFFANAGQAVAVADRYPQNVFAEHTHEFCELVLVWRGNGLHVLNDRPYRITRGDLFYIRAEDKHSYASVNDLVLQNVIYCPDRLKLNVDWASNIPGFNDARGAPHWRLSSNGMGQVRPVITQLEQESLKADQSANEMAELLFAQLVMTLKRFRYATDNPSANEQEALLDKLITALAGSLNRSFVLEKFCEQEQCSERALRQQFRTQTGMTVNHYLRQLRICHAQYLLQHTELMVSEVAMRCGFEDSNYFSVVFNREVGMTPVQWRHRSRKAA
Activates expression of the rhaSR operon in response to L-rhamnose.
A4WG90
P0C7J0
RMLB_XANCP
dTDP-glucose 4,6-dehydratase
Xanthomonas
MATWLVTGRAGFIGGNFVLEAVSRGIRVVNLDALTYAGNLNTLASLEGNADHIFVKGDIGDGALVTRLLQEHQPDAVLNFAAESHVDRSIEGPGAFIQTNVVGTLALLEAVRDYWKALPDTRRDAFRFLHVSTDEVYGTLGETGKFTETTPYAPNSPYSASKAASDHLVRAFHHTYGLPVLTTNCSNNYGPYHFPEKLIPLVIAKALAGEPLPVYGDGKQVRDWLFVSDHCEAIRTVLAKGRVGETYNVGGNSERQNIEVVQAICALLDQHRPREDGKPRESQIAYVTDRPGHDRRYAIDASKLKDELGWEPAYTFEQGIAQTVDWYLTNQTWVQGVLDGSYRLERIGATV
Catalyzes the dehydration of dTDP-D-glucose to form dTDP-6-deoxy-D-xylo-4-hexulose via a three-step process involving oxidation, dehydration and reduction.
P0C7J0
P22324
A1AF_CAVPO
Alpha-1-proteinase inhibitor
Cavia
SAIPRGLLLLAGLCCLVFGIMAEDAQVAQGPSQQIPRSLAHFAHSMYRVLTQQSNTSNIFFSPVSIATALAMVSLGAKGDTHTQILWGLEFNLTEIAEADIHDGFQNLLHTLNRPHSEHELTTGNGLFLDQKLKLKEKFSEDVKTLYHAEAFPTNFSNPKEAEKQINAYVEKGTQGKIVDLVKDLSADTVLALVNYIFFRGKWEKPFDVKHTTQEDFLVDMNTTVNVPMMKRQGMYKAFHCSTIQSWVLLLDYEGNVTTLFLLPDKGKMQHLEETLTPELIFKFARKTERMFANVHLPKLSISGTYDLKEVLGHLGITNVFSGAADLSGITEDMPLKISKGLHKALLTIDEKGTEAAGATELEITPHSVPQDLFFNKPFLFLIIDHSTDTPLFVGKVMDPTKK
Inhibits elastase, chymotrypsin, cathepsin G, plasmin, and trypsin.
P22324
Q2RRT3
MSRA_RHORT
Peptide-methionine (S)-S-oxide reductase
Rhodospirillum
MATATFAAGCFWGVEETFRKIPGVTGTTVGYTGGHFKEPTYRQVCAGDTGHAEAVRVDYDPDKVTYEQLLDVFWAAHDPTQVDRQGPDIGDQYRSAIFYHDAGQEAAAGASRARLEQSGALSRAIATRIEPAGPFWPAEEYHQRYIDKQRARTGVAPACH
Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
Q2RRT3
B1VDL1
SYDND_CORU7
Non-discriminating aspartyl-tRNA synthetase
Corynebacterium
MLRTHLAGELRPGDIDSEVTLTGWVGRRRDHGGVIFIDLRDRSGVAQVVFRESEVAERAHALRSEYCVRVRGRVEARPEGSENPNLPSGAVEVNVSELEVLNESAALPFQIDDPSSAGEVGEETRLKYRYLDLRRASQGDALRLRSKANAAARKVLERHDFTEIETPTLTRSTPEGARDFLVPARLKPGTFYALPQSPQLFKQLLMVAGMERYYQIARCYRDEDFRADRQPEFTQLDVEMSFVDQEDVIALAEEILTEVWSTAGYEVQTPFPRMTYADAMRLYGSDKPDLRFDIQITECTEFFKDTTFRVFQNEYVGAVVMDGGASQPRRQLDAWQEWAKQRGAKGLAYILVGEDGELSGPVAKNITDDERAGIADHVGAKPGDCIFFAAGDTKSSRALLGAARGEIAQKLGLIDDSKWAFTWVVDAPMFEPAADARAEGDVALGNSAWTAVHHAFTSPKPEFLDSFDQDPGSALAYAYDIVCNGNEIGGGSIRIHQRDVQERVFQVMGISQEEAREKFGFLLDAFAFGAPPHGGIAFGWDRIVSLLGGFDSIRDVIAFPKSGGGVDPLTDAPSEITPEQRKESGIDAKPKRAAAAQAGAAKASSK
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
B1VDL1
Q815S0
SYY2_BACCR
Tyrosyl-tRNA synthetase 2
Bacillus cereus group
MNIIDELEWRGAVNQQTDEEGLRKLVEEKKISLYCGVDPTGDSMHIGHLIPFMMMKRFQLAGHHPVILIGGATGTIGDPSGRQSERQLQTLEVVQHNVDALTAQMKKLFDFGGNSEVKMVNNYDWTHEINIIEFLRDYGKNFSINSMLAKDIVASRLDTGISFTEFTYQILQAMDFHHLYTKEDVQLQIGGSDQWGNITSGLDLIRKLEGHEAKVFGLTIPLLLKSDGTKFGKSAGGAVWLDPEKTTPFEFYQFWVNTDDRDVIKYLKYFTFLTKERIDELATKVEVEPHKREAQKVLAEEMTKFVHGEEAFLQAEKITAALFSGDIKSLTADEIEQGFKEMPTFQSSKETKNIVEWLVDLGIEPSRRQAREDINNGAISMNGEKVTDVGTDVTVENSFDGRFIIIRKGKKNYSLVKLGE
Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
Q815S0
P56637
SIXE_HOTJU
Beta-insect excitatory toxin Bj-xtrIT
Hottentotta
MKFFLMCLIIFPIMGVLGKKNGYPLDRNGKTTECSGVNAIAPHYCNSECTKVYYAESGYCCWGACYCFGLEDDKPIGPMKDITKKYCDVQIIPS
Excitatory insect toxins induce a spastic paralysis. They bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing. This toxin is active only on insects.
P56637