Datasets:
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Full Name
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147
⌀
taxon
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46
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sequence
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2.75k
function
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5.51k
AlphaFoldDB
stringlengths
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10
P55470
Y4GN_SINFN
Uncharacterized protein y4gN
Sinorhizobium
MDQTLSRRLFLWHNPQTDNQCRNERHMIHTSKIYREINRIGVQIKGLPDYWMGQARRISYDRVGSAGNTITEGRKPVSADMAILLIYQPRGLLESLFLQLEHLLSKGLGVVIVSNRKVLEHDRNRLSEYCHLIIERKNIGYDFGGYRDGILALHKRSIHPKSLFVMNDSVWFPIRKDCDLIDRCRESRSDIVGVFYNNKSKFPKNHHLQSYFYRFGEKVVSDSRFLAYWRKIPMYNDKRNVIRNLEIKLTKNFQLMGFGISSLYAPEDILKAFKNIEVRNIRPVLDYYISALGYDQNTFWSAYKNESPKGGDTHALPIDVPNSRVFFHFLDAHPEILIRKLNSPIIKKNRDKRFVAQRKAIIEGGFLKEIDAVIQKELINWDR
Could have an enzymatic function.
P55470
Q5WZ61
TRMB_LEGPL
tRNA(m7G46)-methyltransferase
Legionella
MQRKIKSYVLRAGRISNRQQQGLDLWLEDYELKFDSPSPWNFAKEFGRHDADTIVEIGFGMGTSLFAMAMNNPQCNYLGIEVHKAGVGSLVADLHEYQISNVRVVAHDAVEVLQTKIPENSLAGVQIFFPDPWHKKRHHKRRLIQSEFIQMLVKKIRPSGFIHCATDWEDYAEHILNVLSSESALFNQQKEGGYSPRPDSRPLTKFELRGERLGHGVWDLVFIKK
Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Q5WZ61
C1A8T0
UVRC_GEMAT
Excinuclease ABC subunit C
Gemmatimonas
MPVAQKLPHLPESPGVYLWKDVEGQVLYVGKAKRLRSRVRSYWAQEHESSPKTRAMVRKVRDLETIVVPSEAHALILEATLIKEYHPRFNIALRDDKSYPYIRVTVNEPFPRVMVTRRLLDDGARYFGPYTDVGAMRRALNVVKRIFTVRSCHYALPGEAPERPCLDYSIKRCKAPCVGYQSREDYRAMIDEVVWFLDGRTSDVMHHVRERMLDASERLDFERAAELRDALAHLEKMESPSVVLEVEGGDRDVVGYARDGEDACVAVMRIRGGKLLARDHRLLEHAEDEEDGAVLGACLAQWYRTAEARAGELLVPFDFEDRESLEASLDGTHIRVPQRGPRRALVDLADQNARHLLEEFKLAALEADERAVDPVYELQRELGLPRLPRSLVCFDISHAQGTDVVASAVFFENGRPKRSEYRKFKIKVFEGNDDFRSMHEVVTRYFRRRLDEEKPLPDLAVIDGGKGQLGAARAALDELGAPQIGLISLAKREEEIFQYGRPDPVRLPRRSPALRMLQQARDEAHRFAITFQRQKRAARTITSELLKIPGVGPTKRRALLHTFGSVQGVREASVEQIAAIPGFGAASARRLLEALGVAVPDVSAPTIDSPSDPPLS
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision.
C1A8T0
A3M4W0
TRMA_ACIBT
tmRNA (uracil(341)-C(5))-methyltransferase
Acinetobacter calcoaceticus/baumannii complex
MTSSYRQQLQAKIDRITTQFSEFTPPTLEVFESPEQHFRMRAEFRIWHTENDMFYAMFERNDDGKQKTVVRIDEFPIADKSINDLMPLLLAELKANSLLSQRLFEVDFLATLSGEMLVTLIYHRKLNQEWEQAAKALAEKLNIKIMGRSRGQKIVIGDDFVVEEFELLNRSFKYKQIESSFTQPNAQVCKKMLQWACDAAEGSKKHLLELYCGNGNFTLPLSLKFERVLATELAKSSVYAAQWNIEQNQIDNIQVARLSAEEFTQAYQGEREFRRLQEAYIDIQSYDFGTVFVDPPRAGIDDETLKLLQGFERIIYISCNPDTLYENLKTLTQTHRVTKFALFDQFPYTHHVESGVLLEKI
Dual-specificity methyltransferase that catalyzes the formation of 5-methyluridine at position 54 (m5U54) in all tRNAs, and that of position 341 (m5U341) in tmRNA (transfer-mRNA).
A3M4W0
O67108
TOP4A_AQUAE
DNA gyrase subunit A
Aquifex
MENRENLVEIPIEEEVKQAYIDYAMSVIVGRAIPDVRDGLKPVQRRILYSMYEMGLLPDKPFKKSARIVGETLGKYHPHGDQAVYEALVRMAQDFTMRYPLIIGQGNFGSIDGDPAAQMRYTEAKLSPLAVEMLTDIDKDTVDFQPNFDDTLMEPEVLPSKFPNLLCNGTSGIAVGLATSIPPHNLTEVGNALVKLAQNPQISVDEIMEILKGPDFPTGGVIENFAQVKEIYKTGRGIIKVKGKAHVEKVQGGRERIVITEIPYQVNKAELIKKIADNVRNGKIKEISDIRDETDKEGIRIVVELKRDAKGEEVLKKLYKYTPLEKGFPVNLVVLIDKEPKLVDIKTLLREFIKHRLEVILRRSKYFLKKVQDRLHIVEGLLKAINFIDDIIERIRRSKDASEARNYLMEEFGLSEKQAQAVLDLRLQRLTSLEREKLLEEEKELREKIEYYKKLVASEGERIKVFIEETEELVKKYGDKRRTFIGGVKEVKEGSITVAVLQDGSIIPVEELPLEKAPVVNILRVPFTEGLFLVSNRGRVYWIAGSQALQGSKVSLKSREEKIVGAFIREKFGNRLLLATKKGYVKKIPLAEFEYKAQGMPIIKLTEGDEVVSIASSVDETHILLFTKKGRVARFSVREVPPSTPGARGVQGIKLEKNDETSGLRIWNGEPYLLVITAKGRVKKISHEEIPKTNRGVKGTEVSGTKDTLVDLIPIKEEVELLITTKNGKAFYDKINQKDIPLSTKKSIPRTRWKLEDDEIIKVVIKKSE
A type II topoisomerase. Despite its similarity to DNA gyrase, this enzyme is not able to supercoil DNA, and instead acts like topoisomerase IV. Relaxes both positively and negatively supercoiled DNA in an ATP-dependent fashion, decatenates interlocked circles. This the first bacteria shown to not contain DNA gyrase, although it has 2 copies of a reverse gyrase that introduces positive supercoils. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner .
O67108
Q7XKF4
YSL13_ORYSJ
Protein YELLOW STRIPE LIKE 13
Oryza sativa
MATVPTPSEAHGGATPTAADVEMVEASELRRRGKPSGDRATGPSRDGAAAAAEEAAAPSVERVFADRPVPSWREQLTVRAFVVSFFLVIMFSVIVMKLNLTTGIIPSLNVSAGLLGFFFVRLWTAAIERVGLLRQPFTRQENTVIQTCVVAGYDIAFSGGFGNYILSMSERIAGLGTEANNAQNIKNPHLGWIIGFLFLVSFIGLFGLVPLRKVMIIDYKLTYPSGTATAFLINGFHTPHGAKIAAKQVKKLGIFFILSFFWGFFQWFYTATDDCGFHKFPSLGLQAFQHKFFFDFSPTYVGVGMICPHIVNVSVLLGGILSWGIMWPLIAKKRGDWFSADLPDGSLHGMQGYRVFIAIALILGDGLYNFLKMIILTAFSLRSQIKKKNASTLPVSDDGMVTTTAAVSYDEERRNELFVKDQIPWYVAYGGYAVVAAISIGTVPQIIPQLKWYQILVAYIVAPILAFCNAYGTGLTDWSLVTTYGKLAIFAFGAWTGASHGGVLAGLAACGVMMNIVSTAADLMQDFKTGYLTLASPRSMFVSQVIGTAMGCVIAPCVFWLFYKAFDNIGISGSDYPAPNAAVFRSIAILGVDGFSSLPKNCLNLCYAFFAAAIVVNLIRDLVPKVSRFIPIPMAMAIPFYIGSYFAIDMFIGTVILFVWQRVDRAKADTYGPAVASGMICGDGIWVLPQSVLALAKVKPPICMKFLSRRTNDKVDAFLTTLGK
May be involved in the transport of nicotianamine-chelated metals.
Q7XKF4
P08562
TBB_TRYCR
Beta-tubulin
Schizotrypanum
MREIVCVQAGQCGNQIGSKFWEVISDEHGVDPTGTYQGDSDLQLERINVYFDEATGGRYVPRAVLIDLEPGTMDSVRAGPYGQIFRPDNFIFGQSGAGNNWAKGHYTEGAELIDSVLDVCRKEAESCDCLQGFQICHSLGGGTGSGMGTLLISKLREEYPDRIMMTFSIIPSPKVSDTVVEPYNTTLSVHQLVENSDESMCIDNEALYDICFRTLKLTTPTFGDLNHLVSAVVSGVTCCLRFPGQLNSDLRKLAVNLVPFPRLHFFMMGFAPLSSRGSQQYRGLSVPDVTQQMFDAKNMMQAADPAHGRYLTASALFRGRMSTKEVDEQMLNVQNKNSSYFIEWIPNNIKSSICDIPPKGLKMAVTFVGNNTCIQEMFRRVGEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATIEEEGEFDEEEQY
Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
P08562
Q8U192
THIE_PYRFU
Thiamine-phosphate pyrophosphorylase
Pyrococcus
MNLRNKLKLYVITDRRLKPEVESVREALEGGATAIQMRIKNAPTREMYEIGKTLRQLTREYDALFFVDDRVDVALAVDADGVQLGPEDMPIEVAKEIAPNLIIGASVYSLEEALEAEKKGADYLGAGSVFPTKTKEDARVIGLEGLRKIVESVKIPVVAIGGINKDNAREVLKTGVDGIAVISAVMGAEDVRKATEELRKIVEEVLG
Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
Q8U192
C3PBW1
THIE_BACAA
Thiamine-phosphate pyrophosphorylase
Bacillus cereus group
MSRISKAEMSKLLSVYFIMGSNNCTKDPLQVLREALEGFITIFQFREKGEGALTGEERICFAKELQAICKEYGVPFIVNDDVELALELDADGVHVGQDDEGITSVREKMGDKIVGVSTHTIEEARWVIENGADYLGVGPIFPTSTKKDTKAVQGTKGLAHFREQGITIPIVGIGGISIENTASVIEAGADGVSVISAISLAESAYESTKKLVEEVSRSL
Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
C3PBW1
P16559
TCMN_STRGA
Multifunctional cyclase-dehydratase-3-O-methyl transferase TcmN
Streptomyces
MAARTDNSIVVNAPFELVWDVTNDIEAWPELFSEYAEAEILRQDGDGFDFRLKTRPDANGRVWEWVSHRVPDKGSRTVRAHRVETGPFAYMNLHWTYRAVAGGTEMRWVQEFDMKPGAPFDNAHMTAHLNTTTRANMERIKKIIEDRHREGQRTPASVLPTELHAQQLLLLAASGRLARIVHVLTELRIADLLADGPRHVAELAKETDTHELSLYRVLRSAASVGVFAEGPVRTFSATPLSDGLRTGNPDGVLPLVKYNNMELTRRPYDEIMHSVRTGEPAFRRVFGSSFFEHLEANPEAGEFFERFMAHWSRRLVLDGLADQGMERFSRIADLGGGDGWFLAQILRRHPHATGLLMDLPRVAASAGPVLEEAKVADRVTVLPGDFFTDPVPTGYDAYLFKGVLHNWSDERAVTVLRRVREAIGDDDARLLIFDQVMAPENEWDHAKLLDIDMLVLFGGRERVLAEWRQLLLEADFDIVNTPSHTWTTLECRPV
The N-terminal domain enhances the formation of an early, partially cyclized intermediate, while the C-terminal domain catalyzes the 3-O-methylation of one or more later intermediates in the biosynthetic pathway. Catalyzes the methylation of tetracenomycin D3 (Tcm D3) to yield Tcm B3. Catalyzes as well the following side reactions: methylation of 8-O-methyl-Tcm D3 to yield Tcm E; and of 9-carboxymethyl-Tcm B3 to yield Tcm A2.
P16559
P0C7B1
VM3BG_BOTAL
Snake venom metalloproteinase
Bothrops
SISACNGLKGHFLIEPLKLSDSEKTDLLNRSHDNAQLSPINLVVAVIMAHEMGHGMVLPGTK
Snake venom Zinc metalloproteinase that inhibits ADP-induced platelet aggregation and inhibits the alpha-5/beta-1 (ITGA5/ITGB1) integrin, a fibronectin receptor. Has caseinolytic activity. Induces the detachment of cells that are bound to fibronectin.
P0C7B1
Q14593
ZN273_HUMAN
Zinc finger protein HZF9
Homo
MSSAPRGPPSVAPLPAGIGRSTAKTPGLPGSLEMGPLTFRDVAIEFSLEEWQCLDTSQQNLYRNVMLDNYRNLVFLGIAVSKPDLITCLEQGKEPCNMKRHAMVAKPPVVCSHFAQDLWPKQGLKDSFQKVILRRYGKYGHENLQLRKGCKSADEHKVHKRGYNGLNQCLTTTQSKIFQCDKYVKVLHKFSNSNIHKKRQTGKKPFKCKECGKSCCILSQLTQHKKTATRVNFYKCKTCGKAFNQFSNLTKHKIIHPEVNPYKCEECGKAFNQSLTLTKHKKIHTEEKPYKCEDCGKVFSVFSVLTKHKIIHTGTKPYNCEECGKGFSIFSTLTKHKIIHTGEKPYKCNECGKAFNWSSTLTKHKRIHTGEKPYKCEECGKAFNQSSTLTRHKIVHTGEKPYKCEECGKAFKRSTTLTKHKRIYTKEKPYKCEECGKAFSVFSTLTKHKIIHTGAKPYKCEECGSAFRAFSTLTEHKRVHTGEKPYKCNECGKAFNWSSTLTKHKRIHTGEKPYKCEECGKAFNRSSNLTRHKKIHTGEKPYKPKRCDSAFDNTPNFSRHKRNHMGEKS
May be involved in transcriptional regulation.
Q14593
B4R1P9
TOTX_DROSI
Protein Turandot X
Sophophora
MGLHIGSLLICVFLGILPFATANTNRSGYEEQRNYLLNIFHNPLVNDSIKEKNIPELIAFYQRYPTDVPLSDADRQQFERFIHDYREYREVLVDGVPPQGGSFGNIFGHFLGRVGTRYISSLFNKKREEGQSNHANSPTTLPSRIQKMTK
A humoral factor that may play a role in stress tolerance.
B4R1P9
Q7M9S1
TRPB1_WOLSU
Tryptophan synthase beta chain 1
Wolinella
MMHKPYLKSFPNKEGYFGKYGGAYLPPLLIEHFKEIGEAYLKISQSFDFIQELKSIRKHYQGRPTPLYYARRLSQKAGGAAIYLKREDLNHTGAHKLNHCMAEALLAKHLGKKKLIAETGAGQHGVALATAAAYFGMECEIHMGEVDIAKEHPNVIRMKMLGAKVVPVSFGERTLKEAVDSAFEAYLKDPANAIYAIGSVVGPHPFPKMVRDFQSVVGAEAKEQFLEMTGELPDHIVACVGGGSNAMGIFSAFIDDPVELWGVEPLGKGKSLGEHAASLSYGKEGVMHGFNSIMLQNEDGSPASVHSVASGLDYPSVGPEHAYLHEIGRTHSVGVSDEEAIKNFFALSRLEGIIPAIESAHAIAYGMKLAKERLGEKILINLSGRGDKDIDYVSETFGFGGEE
The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
Q7M9S1
A9AGE2
UBIA_BURM1
4-HB polyprenyltransferase
Burkholderia cepacia complex
MLARFPLYLRLVRMDKPIGSLLLLWPTLNALWIASDGHPRWPLIVIFALGTLLMRSAGCAMNDYADRDFDRHVKRTADRPLTSGKIRAWEAVAIAVGLSFVAFLLILPLNTLTKELSVVALFVAGTYPFMKRFFAIPQAYLGIAFGFGIPMAFAAVQNTVPPLAWVMLIANVFWSIAYDTEYAMVDRDDDIKIGIRTSALTFGRFDVAAVMACYAVTLGIYVWIGIALGFGAAYWVGWAAAAGCAVYHYTLIKGRERMPCFAAFRHNNWLGGVLFAGIAAHYLMAGS
Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 3-octaprenyl-4-hydroxybenzoate.
A9AGE2
Q8ECV0
TRPB_SHEON
Tryptophan synthase beta chain
Shewanella
MSQLKLNPYFGEYGGMYVPQILVPALKQLESAFVEAQTDESFQAEFTDLLKNYAGRPTALTLTRNLSPNPMVKIYLKREDLLHGGAHKTNQVLGQALLAKRMGKKEIIAETGAGQHGVATALACALLGLKCKVYMGAKDVARQSPNVFRMRLMGAEVIPVTSGSATLKDACNEAMRDWSGSYEKAHYLLGTAAGPHPFPTIVREFQRIIGEETKKQILEREGRLPDAVIACVGGGSNAIGMFADFIDETNVELIGVEPAGKGIDTHMHGAPLKHGKTGIFFGMKAPLMQDSEGQIEESYSISAGLDFPSVGPQHAHLNAIGRARYESATDDEALEAFQLLARCEGIIPALESAHALAYALRLAKECTKETILVVNLSGRGDKDIFTVSDILNGKEE
The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
Q8ECV0
P47750
TSHR_MOUSE
Thyroid-stimulating hormone receptor
Mus
MRPGSLLLLVLLLALSRSLRGKECASPPCECHQEDDFRVTCKELHRIPSLPPSTQTLKLIETHLKTIPSLAFSSLPNISRIYLSIDATLQRLEPHSFYNLSKMTHIEIRNTRSLTYIDPDALTELPLLKFLGIFNTGLRIFPDLTKIYSTDIFFILEITDNPYMTSVPENAFQGLCNETLTLKLYNNGFTSVQGHAFNGTKLDAVYLNKNKYLTAIDNDAFGGVYSGPTLLDVSSTSVTALPSKGLEHLKELIAKDTWTLKKLPLSLSFLHLTRADLSYPSHCCAFKNQKKIRGILESLMCNESSIRNLRQRKSVNILRGPIYQEYEEDPGDNSVGYKQNSKFQESPSNSHYYVFFEEQEDEVVGFGQELKNPQEETLQAFESHYDYTVCGDNEDMVCTPKSDEFNPCEDIMGYRFLRIVVWFVSLLALLGNIFVLLILLTSHYKLTVPRFLMCNLAFADFCMGVYLLLIASVDLYTHSEYYNHAIDWQTGPGCNTAGFFTVFASELSVYTLTVITLERWYAITFAMRLDRKIRLRHAYTIMAGGWVSCFLLALLPMVGISSYAKVSICLPMDTDTPLALAYIVLVLLLNVVAFVVVCSCYVKIYITVRNPQYNPRDKDTKIAKRMAVLIFTDFMCMAPISFYALSALMNKPLITVTNSKILLVLFYPLNSCANPFLYAIFTKAFQRDVFILLSKFGICKRQAQAYQGQRVCPNNSTGIQIQKIPQDTRQSLPNMQDTYELLGNSQLAPKLQGQISEEYKQTAL
Receptor for the thyroid-stimulating hormone (TSH) or thyrotropin. Also acts as a receptor for the heterodimeric glycoprotein hormone (GPHA2:GPHB5) or thyrostimulin. The activity of this receptor is mediated by G proteins which activate adenylate cyclase. Plays a central role in controlling thyroid cell metabolism.
P47750
Q06J27
YCF3_BIGNA
Photosystem I assembly protein Ycf3
Bigelowiella
MPRSQKNDNFIDKTFTVVADILLKVLPTSIDEKRAFTYYRNGMSAQSEGEYAEALQNYYQALRYEIDAYDRSYMLYNIGLIHSSNGQQSKALEYYYQALDRNPRLSQALNNIATIYHYRGEQALINNQDEISKIFFDKAADYWKEAIRLSPTSYTKAKNWLSVRNK
Essential for the assembly of the photosystem I (PSI) complex. May act as a chaperone-like factor to guide the assembly of the PSI subunits.
Q06J27
Q8PEW6
TTCA_XANAC
tRNA 2-thiocytidine biosynthesis protein TtcA
Xanthomonas
MTAVLPLPQPLADPAPRDPRQRLQREQLRLGKRLQRQVGQAIADFGMIAPGDKIMVCLSGGKDSYTLLDMLLQLQRKAPVPFSLVAVNLDQKQPDFPAHVLPAYLRGLGVPFAIVEQDTYSVVSRVIPAGKTMCSLCSRLRRGALYAYAQTHGVTKIALGHHRDDIVATFFMNLFHHARLAAMAPKLRSDDGAHVVIRPLAYVREADIAAYAQARQFPIIPCNLCGSQENLQRQQVGKLLQQWDRESPGRVEQIARALGDVRPEQLADRTLFDFLALGRSGDAPSGLDPDPRAWLSAGHATHDSD
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.
Q8PEW6
Q4JG17
VASAL_PENVA
Vasa-like protein
Penaeus
MSDDWDETDAAPASDWNIESFGLPTSFGSTKKTCNTGNAFNDGEGGFDEGSQSNFDDPFRSGGGGFGGRGRGGPRACFKCGDEGHMARDCPSASDSRGNRTNNRRQDNWGGGSSSKPANGEPFGFGSAFGDNQESDPFGATESSGFGFGSGSGSRGGRRNDGGRGCFKCGEEGHMSRDCPSGGGRNKGCFKCGQEGHNARDCPNPGEGSEEKKPRAPLYIPADVNEDELFVMGIEAGSNFDAYANVPANVSGAEPIQPAAESFQSMNLRPLLLENIVKAGYGCPTPVQKYTIPNVMNGRDIMACAQTGSGKTAAFLLPMLHYILDNNCPSNAFEEPAQPTGLVICPTRELAIQIMREARKFSHSSVAKCCVAYGGAAGFHQLKTIHSGCHILVATPGRLLDFLEKGKIVFSSLKYLVLDEADRMLDMGFLSSIKTVINHKTMTPTAERITLMFSATFPHEIQELASAFLNNYLFVVVGTVGAANTDVKQEVLCVPKFEKKAKLVEMCEEILISADDEKILVFVEQKRVADFVGTYLCEKKFRATTMHGDRYQAQREQALSEFRTGVHNILVATAVTARGLDIKGIGVVVNYDLPKDIDEYVHRIGRTGRLGNRGLSISFYDDETDACLTKDLVKVLSEANQTIPDWLTQKANASGHAQTYHGSGLFASSDIRSKNGGGRGWEKNQASSFLGGPSESNVDEEWD
Involved in translational control mechanisms operating in early stages of oogenesis. Required maternally in many stages of oogenesis, including cystocyte differentiation, oocyte differentiation, and specification of anterior-posterior polarity in the developing cysts. Essential for the formation and/or structural integrity of perinuclear nuage particles during germ cell formation.
Q4JG17
B2SDE3
UVRC_FRATM
Excinuclease ABC subunit C
Francisella
MIVDNSKDFDLKSFLANLTTHSGVYRMLDKHGEIIYVGKAKNLKNRVNSYFSKGAKDSKTLMMVEQIARIEITITPSDYEAYLLENNLIKQHRPKYNILFKDDKSYPYLVISRDKFPRVSFYRGKSAYKKGQCFGPYVSISSVKNTLNTIQKIFPIRQCENSYYKSRVRPCLQYQIKRCLAPCVGLVSQQQYDEQLAILKKFLAGKFSSVLEEISAKMYQASEDMEYEKAQVYRDQLVVLRKLQQQQIVDIQEDKTFDVIGIYMQDSYASIALLQIQNGDVVADRHWSIDAKGQDKTSIMHAFLSHFYLGDEIRNIWPKNIILSKVEFADITDLMNSISQKIGQAINWIIAPAADNLKWLKLAEVNARQKLNIYTSSKSQYQKRLESLKEFLELEKDIKRIECFDISHFQGEATIASCVVYTDDGEDRKSHRRYNIKGIKSGDDYAAIHQAVSRRVSSGLEADNLPDVMIIDGGKGQIHQAEAVFREYGIQDKVQLVSLGKGVERISGKEKIYKGFDDTEYTLDEHNPGFLLLRQVRDSAHDHAIKGQRKKVSANRQSSIIEEIEGVGSKRRKALLRYFGGWQELSRASVDEIAKVKGISKKLAQEIWECFH
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision.
B2SDE3
B5YKY0
Y1069_THEYD
Nucleoid-associated protein THEYE_A1069
Thermodesulfovibrio
MSKKMFGEIMRQAQKIQEEIQKKQEEVKKMTVEATSGGGMVTVQANGAGEIVSIKIDREVVNPDDIEMLEDLVLAAVNEAIKRAHELAQSEMAKVSMPFNLPGMPDLSSLFGKL
Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection.
B5YKY0
Q9VMR8
TOTM_DROME
Protein Turandot M
Sophophora
MNPTIYLSCLMVFSVFLLGKVNAENEDEFVTEKQRLFSVYGDSSVDEATKYRNIDSLVTFYDKYFTRLQLKPDLNTRAHDLLRRYKEENARVVLVDGTPAQGGFWLPLVKLLIVQLGVEIASEGVKRAIES
A humoral factor that may play a role in stress tolerance. Requires Mekk1 expression in the fat body to regulate response to septic injury and consequent immune response.
Q9VMR8
P37806
UNC87_CAEEL
Uncoordinated protein 87
Caenorhabditis
MLSFNNTTSASSFQSASSRYLMSSSSSIGPPQQQSAKLFPEHFYPSGLSPRQSEALERLRPNTASRERNIPIQFTGKNPTTNSALEEYKPVPHVQVTSPKSSIVPNFVSEQRGLQPQPTSQAPTNYRQFVAAPRSPRGYGDYPEMTGKASAAGDSEPVQIPIKTQTPITQARAQETKIPTIVSPHPVYYYDNQEQPIQQIREEQPNATMETKVTGQGQPKRVGRWTLAQLRQTDGIIPSQAGWNKGDSQKLMTNFGTPRNTNTRVKSENLQEIPEDIANRTHGEVRLQSGTNKYCSQRGMTGFGSGRDVCREGVRVAQNPADLAELPEEKIRMSEGIVRLQAGTNKYDSQKGMTGFGTGRRETTKMVDSKHPEYDHEKPDQSEIPLQSGTNKFASQKGMTGFGTARRETTKMVDSNHPDYSHECSIDQTTIPSQMGSNQYASQKGMTGFGQPRWEVLDPSISWQNRKSQGMVRLQSGTNRFASQAGMIGFGTCRNTTFEAEGGELPYEAMKVSETIIPSQAGWNKGDSQKKMTSFGAPRDVKGKHLKRIWELEYPEEAEISLDRL
Acts as a negative regulator of myosin-dependent contractility of smooth muscle-like cells in the somatic gonad.
P37806
C3N1X1
Y365_SULIA
Putative antitoxin M1627_0365
Sulfolobus
MAKTITISEEAYKLLLKEKRDGESFSDVIVRLIKGNRREVMDYAGIWSDMNDEESNKLFKDLEKMWERWNVNA
Possibly the antitoxin component of a type II toxin-antitoxin (TA) system.
C3N1X1
E9L011
UGTB1_STABO
UDP-glucosyltransferase B1
Starmerella
MAIEKPVIVACACPLAGHVGPVLSLVRGLLNRGYEVTFVTGNAFKEKVIEAGCTFVPLQGRADYHEYNLPEIAPGLLTIPPGLEQTGYSMNEIFVKAIPEQYDALQTALKQVEAENKSAVVIGETMFLGVHPISLGAPGLKPQGVITLGTIPCMLKAEKAPGVPSLEPMIDTLVRQQVFQPGTDSEKEIMKTLGATKEPEFLLENIYSSPDRFLQLCPPSLEFHLTSPPPGFSFAGSAPHVKSAGLATPPHLPSWWPDVLSAKRLIVVTQGTAAINYEDLLIPALQAFADEEDTLVVGILGVKGASLPDSVKVPANARIVDYFPYDELLPHASVFIYNGGYGGLQHSLSHGVPVIIGGGMLVDKPAVASRAVWAGVGYDLQTLQATSELVSTAVKEVLATPSYHEKAMAVKKELEKYKSLDILESAISELAS
Catalyzes the second glycosylation step of sophorolipid biosynthesis, the further glucosylation of the previoulsy formed glucolipid to give rise to an acidic sophorolipid.
E9L011
Q8QHK3
VSP1_CROAT
Catroxase I
Crotalus
MVLIRVLANLLILQLSYAQKSSEPIIGGDECNRNEHRFLALVSSDGNQCGGTLINEEWVLTAAHCEGNKMKIHLGVHSKKVPNKDKQTRVAKEKFFCVSSKNYTFWDKDIMLIRLDRPVSNSEHIAPLSLPSSPPSVGSVCRIMGWGTISPTKVILPDVPHCVNINLLNYSVCRAAYPEYGLPATSRTLCAGILEGGKDTCVGDSGGPLICNGQFQGIASWGSPNCGYVREPALYTKVFDHLDWIQSIIAGNTDATCPFVNF
Snake venom serine protease that may act in the hemostasis system of the prey.
Q8QHK3
P32819
YAMY_BACAD
Uncharacterized 39.9 kDa protein in amylase 3'region
Bacillus
MDPIALDERIGTLDYLRGFALLGIILVNILGLLTVKTPALHSVDAVYQRFLYFFVEARFYPIFSFLFGVGFYLFIARANTRGENGAILFLRRILVLFIFGFIHFLFQPGEALTVYASCGLLMLPFYKIKKEVNLFTGCILLLFVSIFAAKIFMPLPLILLGLSAGQYRIFEKLARYKTETAIFTFFMFILSVGGLLLQYCYVPEQPFNNLNGLEKNYQNMDQLKWFLHLGVATGPILSAFYAGFLLLLLQAPIARRLLSPLKSYGRMALTNYISQTALILLAGKLFHLFNRITYLQSLWLCLAIYVIQLIFSAMWLKYCKFGPLEWVWRMMTYNRKFPILLKKEAD
Involved in transport.
P32819
Q3ANX8
TAL_CHLCH
Probable transaldolase
Chlorobium
MQFFIDTANLDEIRAAAELGVLDGVTTNPSLIAKVAGSSKPFTWQAFKDHIAAICEIVDGPVSAEVTALDANGMIDQGEELADIDGKVVIKCPVTLEGLKAISYFDENDIMTNATLVFSPNQALLAAKAGATYVSPFVGRLDDVSTNGMELIRQIVTIYRNYDFITEVIVASVRHSQHVVEAAMIGADIATIPFNVIKQLISHPLTEAGLKKFTEDAAIIQM
Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
Q3ANX8
A9LYA2
YCF3_ACOAM
Photosystem I assembly protein Ycf3
Acorus
MPRSRINANFIDKTSTIVANILLRIIPTTSGEKEAFTYYRDGMSAQSEGNYAEALQNYYEATRPEIDPYDRSYILYNIGLIHTSNGEHTKALEYYFRALERNPFLPQAFNNMAVICHYRGEQAIRQGDSEIAEAWSDQAAEYWKQAIALTPGNYIEAQNWLKITRRFE
Essential for the assembly of the photosystem I (PSI) complex. May act as a chaperone-like factor to guide the assembly of the PSI subunits.
A9LYA2
A7Z4T7
TRUB_BACVZ
tRNA-uridine isomerase
Bacillus amyloliquefaciens group
MVNGVLLLHKPVGMTSHDCVMKIRKLLKTKKVGHTGTLDPEVSGVLPICVGRATKIVEYVTDKSKTYDAEITLGFSTSTEDQTGETVSVKPVKEPLKEADIKAVLDELKGPQEQVPPMYSAVKVNGKKLYEYARAGIEVERPKRNITIEDIALTSPVTYNEDTASFRFTVTCSKGTYVRTLAVTIGEKLGYPAHMSHLIRTASGDFSLDECFTFEELEQQVSDGTVAEHAVPIDRALNHLPKWVISDTLAKKAENGSVFDIPAEFSAMTADARIAVCTEDGECVAIYMPHPSKKGLLKPAKVLMQKSEQ
Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
A7Z4T7
Q07QT9
UREG_RHOP5
Urease accessory protein UreG
Rhodopseudomonas
MARYNGPLRVGIGGPVGSGKTALMDLLCKELRERYQIAAITNDIYTKWDAEFLVRSGSLTPDRIVGVETGGCPHTAIREDASMNLAAVADMRAKFPDLDLVLIESGGDNLAATFSPELADLTIYVIDVAAGDKIPSKGGPGITRSDLLVINKIDLAPYVGASLAKMEVDAKRMRGERPFVMTNLKQSAGLDRIIAFLEAKGGLQAEPVDA
Facilitates the functional incorporation of the urease nickel metallocenter. This process requires GTP hydrolysis, probably effectuated by UreG.
Q07QT9
P86176
TIGIT_MOUSE
V-set and transmembrane domain-containing protein 3
Mus
MHGWLLLVWVQGLIQAAFLATAIGATAGTIDTKRNISAEEGGSVILQCHFSSDTAEVTQVDWKQQDQLLAIYSVDLGWHVASVFSDRVVPGPSLGLTFQSLTMNDTGEYFCTYHTYPGGIYKGRIFLKVQESSDDRNGLAQFQTAPLGGTMAAVLGLICLMVTGVTVLARKDKSIRMHSIESGLGRTEAEPQEWNLRSLSSPGSPVQTQTAPAGPCGEQAEDDYADPQEYFNVLSYRSLESFIAVSKTG
Binds with high affinity to the poliovirus receptor (PVR) which causes increased secretion of IL10 and decreased secretion of IL12B and suppresses T-cell activation by promoting the generation of mature immunoregulatory dendritic cells.
P86176
Q7ZUK7
WAC_DANRE
WW domain-containing adapter protein with coiled-coil
Danio
MVMYARKQPRLGDGCTDRRDSQPYQTLKYSSKSHPDHRHEKMRDSNDATPPCKMLRRSDSPDNKHMDNTGHGRAKAIHPHRGREREGGTSISPQENSHNHSSLHSSNSHSNPNKSSDTPFEPADDWSEHISSSGKKYYYNCRTEVSQWEKPKEWLEREQRQKEATKTAAVVNSFPKDRDYRREAMQATPASYSSTKSSIATEKPSSLTPSSSSAAVSGLDVPNSASSASGSTVPVSPVMQSPAPPTLLQDPSLLRQLLLALQTALQLNNASVDMAKINEVLTAAVTQASLQSILHKILTAGPSAFNITTLLSQATQLSNQVAQQSSQSPMSLTSDASSPRSYVSPRISTPQTNTASLKPPLSTTPVSSQTKINAMTVKSSSLPPPSSQQPLSTEKHHDNGNSPRTLQRQSSQRSPSPGPNHMGSNSSSSSNNGGGGGGQGPGVVSGAMPPGSVPPGTAPGRATCSFTPTLAAHFNENLIKHVQGWPAEHVEKQASRLREEAHTMGSIYMSENCTELKNLRSLVRVCEIQATLREQRILFLRQQIKELEKLKNQNSFMV
Acts as a linker between gene transcription and histone H2B monoubiquitination at 'Lys-120' (H2BK120ub1). Positive regulator of amino acid starvation-induced autophagy. Positively regulates MTOR activity. May negatively regulate the ubiquitin proteasome pathway.
Q7ZUK7
Q929F3
YHAM_LISIN
3'-5' exoribonuclease YhaM
Listeria
MEKRLLDYEVGETVELFLLIKSSVKGTASNGKPFLSLVLQDKSGELEAKLWDVKESDEINYGVQQIVHLMGDIQNYRGRKQLKIRQIRQASPLDGVSASEFMETAPINKDEMADEITQYIFEMKNANLQRITRALLKKYQDDFYDYPAAMRHHHEFVSGLSFHVVSMLRLAKSVADLYPTVNRDLLYAGVILHDLGKVIELSGPVSTTYTLEGNLIGHISIVVEEVSKIAEELSIDGEEVVVLKHVLLSHHGKGEWGSPKPPLVREAEILHQIDLMDASLNMMDKVLKHTKPGEFSERVFGLDNRSFYNPTFE
Shows a 3'-5' exoribonuclease activity.
Q929F3
Q822W3
TRPB2_CHLCV
Tryptophan synthase beta chain 2
Chlamydia
MKHPYPFGGQFMPEILMAPVQDLSNSWKSLQNHSDFKNELDSVLKNYAGRPTPLTEIKNFAKAIHGPRIFLKREDLLHTGAHKINNALGQCLLAKHLGKTRIIAETGAGQHGVATATACGCLGLECVIYMGAKDIERQKPNVDKMNLLGAEVISVNQGAQTLKDAVNEALRDWSKNYESTHYCLGSALGPSPYPEMVRNFQSVISLEVKSQLQEIGFSPDLLIACVGGGSNAIGFFHHFIPDTRVKLVGVEAGGLGIESGHHAARFATGRPGVLHGFYSYLLQDNEGQVLPTHSISAGLDYPAVGPDHAVLYESGRASYTVATDKAALEAFFLLSRLEGIIPALESSHALAELINIAPTLPKESVVVVNLSGRGDKDLEQITNLIKAGNNE
The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
Q822W3
Q91241
THAA_PAROL
Nuclear receptor subfamily 1 group A member 1-A
Paralichthys
MEPMSNKQDSNSSEGDEKGWPDVPKRKRKNSQCSMKSMSALSVSVPGYIPSYLEKDEPCVVCGDKATGYHYRCITCEGCKGFFRRTIQKNLHPSYSCKYEGCCIIDKITRNQCQLCRFKKCISVGMAMDLVLDDSKRVAKRRLIEENREKRKREEMVRTLQIRPEPDTAEWELIRMATDAHRHTNAQGSSWKQKRKFLSDDIGQSPMVPTSDGDKVDLEAFSEFTKIMTPAITRVVDFAKKLPMFSELPCEDQIILLKGCCMEIMSLRAAVRYDPDSETLTLNSEMAVKREQLKNGGLGVVSDAIFDLGKELGQFNLDDTEVALMQAVLLMSSDRSGHQCMEKIEQCQEAYLLAFEHYINYRKHNIPHFWPKLLMKVTDLRMIGACHASRFLHMKVECPSELFPPLFLEVFEDQEV
High affinity receptor for triiodothyronine.
Q91241
A0PVP6
Y4430_MYCUA
Putative S-adenosyl-L-methionine-dependent methyltransferase MUL_4430
Mycobacterium
MARTEGDSWDLANSVGATATMVAAARAAATRRSRPIIADPFAEPLVRAVGLDLFTRAASGEVDLDEVAAGLGFVRMVDTFAARALFFDKFFADAIAAGLRQVVIVASGLDARPYRLPWPTGMRVYEIDQPEVIEFKTTTLARLGASPTADHHPVGIDLRDDWPSALRAAGFDAARPTAWLAEGVRIGFLPPEAETRLLDNVIELSAVGSRLAADYGTINGSSAESQQLAQQMTEGWRAHGLDMDIAGLTYPGEHTDVAAYLRSHGWKTATADHGDLVLAAGLAELTAADRQSPASTIGFVTAVRSTD
Exhibits S-adenosyl-L-methionine-dependent methyltransferase activity.
A0PVP6
D1GY43
UBA5_DROAN
Ubiquitin-like modifier-activating enzyme 5
Sophophora
MSHAIDELQAIIAELKVELEEQKTSNRQARSRIDRMSAEVVDSNPYSRLMALQRMNIVKEYERIRDKAVAVVGVGGVGSVTADMLTRCGIGKLILFDYDKVELANMNRLFFTPDQAGLSKVEAAARTLNFINPDVQIETHNYNITTVDNFDRFLATITESGKELGQPVDLVLSCVDNFEARMAINAACNERNLNWFESGVSENAVSGHIQFIRPGDTACFACAPPLVVAENIDEKTLKREGVCAASLPTTMGITAGFLVQNALKYLLNFGEVSDYLGYNALNDFFPRMTLKPNPQCDDRNCLLRQKEFQARPKPIEVKEDVSSSDEPLHATNEWGIELVADDEPVNCPEPAKSSAVVQGLKLAYEAPEKEKVEEENVATVSDETSLEDLMAQMKSM
E1-like enzyme which activates UFM1.
D1GY43
P19123
TNNC1_MOUSE
Troponin C, slow skeletal and cardiac muscles
Mus
MDDIYKAAVEQLTEEQKNEFKAAFDIFVLGAEDGCISTKELGKVMRMLGQNPTPEELQEMIDEVDEDGSGTVDFDEFLVMMVRCMKDDSKGKSEEELSDLFRMFDKNADGYIDLDELKMMLQATGETITEDDIEELMKDGDKNNDGRIDYDEFLEFMKGVE
Troponin is the central regulatory protein of striated muscle contraction. Tn consists of three components: Tn-I which is the inhibitor of actomyosin ATPase, Tn-T which contains the binding site for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the inhibitory action of Tn on actin filaments.
P19123
A4QJQ8
TI214_AETGR
Translocon at the inner envelope membrane of chloroplasts 214
Aethionema
MMVFQSFILGNLVSLCMKIINSVVVVGLYYGFLTTFSIGPSYLFLLRARVMDEGEEGTEKKVSATTGFIAGQLMMFISIYYAPLHLALGRPHTITVLALPYLLFHFFWNNHKHFFDYGSTTRNEMRNLRIQCVFLNNLIFQLFNHFILPSSMLARLVNIYMFRCNNKMLFVTSSFVGWLIGHILFMKWVGLVLVWIQQNHSIRSNRSNVLIRSNKYKFLVSELRNSMARIFSILLFITCVYYLGRIPSPILTKKLKGTSETEERGGTKQDQEVSTEEAPFPSLFSEEREDLDQIDEIDEIRVNAKEQINKDDEFHIRTYYNYNKISENIDGNKENSNLEFLKIKKKEDSVLWFEKPLVTLIFDYKRWNRPNRYIKNDQIENAVRNEMSQYFFSACQSDGKDRISFSYPRNLSTFSEMIQKKIPSFRREKNPSDQFSTCWSLINEEKKENLKKEFLNRIEALDKEWSVEHILEKTTRFCHNETKKEYLPKIYDPFLHGISRGRTQRLFPFQIITKTYLKNPIGGSWINKIHGILLNINYQKFEQTIEKFNRKSSAIKKNLSFFSDPQEEKYKSEEESKIFKFLFDVVIADSNDQTLIKNFMDFHEIHKKVPRWSYKLRSDLEELEGENEETIPLEEPGIRARKAKRVVIFTDTEPHNEIYTNLKNNKNYDQNDEMVLIRYSQQSDFRREIIQGSMRPQRRKTVIWEFFQANMHSPLFFDRIDKFFFFSFDIRGLTKQILRNFMRKNEKKKLDKKDAERSKRKEKGRLKIAEVWDSFFFAQILRGFLLVTQSILRKYILLPLLIIIKNSVRMLLFQIPEWSEDLKDWKREMHVKCTYNRVPLSETEFPRNWLTDGIQIKILFPFYLKPWHKSKFHSSQKGRLKKTKDKGKKKDFCFLTVWGMETELPFGSAHKQPSFFGPISKELKKKMKKYKTKSFQVLRFFKERDKIFLKGAKEIKNWIMKNFVFIKGKRNDLSKGNRIPLLGLREIDELTETKNDSITSNPIIHELSVQNRSMEWKNSSFSENKIKNSIDRINTIRNQIEAISKEKKKITNSCNKPPYDSKIIESSKKKWQIVKSKNTRLIRKTFYFVKFCIEQLSLGIFGGIINIPRIITQLLFESTKQIRDKSIYKNEETQEKINKKKNTIYLISTIKKFKSNKKKISYDLCSLSQAYVFYKLSQLQVSNFSKLRAVLEYNICVTSLFVKNQIKDFFQEHGIFHYKLKEKTFLNSESNQWKNWLRSHYQYNLPEIVWARLVTEKWKNKINQDSLVLNQSLNKEDSYEKNQFDNYKKLNSFEADSLLNPKQNLKKDYIYNLFCYNSINSKETIFDMPLDIIIDNFLVSSFRGKSNIRGIGKFRTRKFLDWRILTFWFIKKVNIESAVDTTSKKKNIQTQAQNSERIHKITKTGLANQKKDFFDWMGMNEEILNYPIANFDFLFFPEFVLFSSTYKIKPWVIPIKLLLFNFNEKKTVNKKITRNQNVFIPSNETKNLRFYNLTKESADQGELESDNEKQRNPELALPNQEKNIEENYAESKIKKPENKKQYKPNTEVELDLFLTRYSRFQLRWNFFLNTKILNNIKIYCLLVRLKNPNEIAISSIERAEMNLDLLMIEKNFTFAKLMKKGILIIEPLRLSVKNDGQLIIYRTIGISLVHKNNHQISQREKKKIEKAITKYKKKTVNRKKKNSDFFAPENLLSPKRRREFRILICSKFKTKSTRYRNSRFDKNIQNCGQVLNQKKDLDKDKTNLMKLKFFLWPNFRLEDLACMNRYWFNTNNGNHFSMIRIHMYTRLKINS
Involved in protein precursor import into chloroplasts. May be part of an intermediate translocation complex acting as a protein-conducting channel at the inner envelope.
A4QJQ8
Q5V4R4
TOP6A_HALMA
Type II DNA topoisomerase VI subunit A
Haloarcula
MSTDSDTTPDTEEAREQLIDLAADFYDQFADGEVPTMTIPTRTKSNIVFDEDEQVWVYGDRNSTRSAKTISGAEKILKAVYTIDFLSQQLEEDRSSTLRELYYLSESWDLDEAQFNTQDESNNLIEDLEIVSDVKREDFHMRPEESGAKVMGPLLLREQTNRGDREIHCQDDVGQGGYQIPNNPDTIEFLDNDAKFVLCVETGGMRDRLVENGFDDEYDALVVHLGGQPARATRRLIKRLHDELDLPVTVFTDGDPWSYRIFGSVSYGSIKSAHLSEYLATPEAQFIGIRPEDIVEYELPTDPLSDSDVNALESELEDPRFQTDFWEEQIELQLDINKKAEQQALASRGLDFVTETYLPERLDEMGIL
Relaxes both positive and negative superturns and exhibits a strong decatenase activity.
Q5V4R4
A9VUC4
TGL_BACMK
Transglutaminase
Bacillus cereus group
MIVIGRSIVHPYITNEYEPFAAEKQQILSIMAGNQEVYSFRTADELSFDLNLRVNIITSALELFQSGFQFRTFQQSFCNPQFWERTSLGGFQLLPNIAPSIAIQDIFKNGKLYGTECATAMIIIFYKALLSLYEEKTFNRLFANLLLYTWDYDRDLKLITKTSGDIVPGDLVYFKNPQVNPATIEWQGENAIYLGNFFFYGHGVGVKTKEEIIYSLNERRIPYAFISAYLTDFITRIDSRMMSQYAPPNTPQTSIGFIPIRDDAIVATVGHTTTIY
Probably plays a role in the assembly of the spore coat proteins by catalyzing epsilon-(gamma-glutamyl)lysine cross-links.
A9VUC4
Q8Y4D5
Y2514_LISMO
DegV domain-containing protein lmo2514
Listeria
MNEKIAVVTDSTTYLPDEVKEQLRINVVPLSVIIDGKSYREGEELSATDFYRKVKEAENFPTSSQPAPGEFIHLFENLKEQGFDTVISIHLSSGISGTFQNAASAGELIEGLNVVAYDSELSCMAQGMFAVKAAEMALANEPLDQIIQKLDKIKQAQDAYFMVDDLNNLQRGGRLNGAQALVGSLLQIKPILHFNDKQIVLFEKVRTQKKALKRIEDILQKAVQNKTAEKAYVIHGNDLAKGEAWLAQLEAKFPEVTFELSYFGPVIGTHLGEGALGLTWSIK
May bind long-chain fatty acids, such as palmitate, and may play a role in lipid transport or fatty acid metabolism.
Q8Y4D5
A6WZV4
TYSY_BRUA4
Thymidylate synthase
Brucella
MRTYLDLLQHVLDNGTDRGDRTGTGTRSVFGYQMRFNLEEGFPVLTTKKLHLRSIIHELLWFLKGDTNIAYLKENGVSIWDEWADKNGDLGPVYGYQWRSWPAPDGRHIDQIANLLKMLHGNPNSRRLIVSAWNPALVDEMALPPCHCLFQFYVADGKLSCQLYQRSADIFLGVPFNIASYALLTMMIAQVAGLKPGEFIHTLGDAHIYANHFDQARLQLTRIPKKLPTMWINPDVKDLFAFRFEDFQLEGYEADPTIKAPIAV
Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis.
A6WZV4
Q829Y6
UVRB_STRAW
Excinuclease ABC subunit B
Streptomyces
MRPVSKIERTVAPFEVVSPYQPSGDQPAAIAELDRRIRAGEKDVVLLGATGTGKSATTAWMIEKLQRPTLVMAPNKTLAAQLANEFRELLPNNAVEYFVSYYDYYQPEAYVPQSDTYIEKDSSINEEVERLRHSATNSLLTRRDVVVVASVSCIYGLGTPQEYVDRMVPLRVGDEVDRDDLLRRFVDIQYTRNDLAFTRGTFRVRGDTIEIFPVYEELAVRIEMFGDEIEALSTLHPLTGEIISDDQHLYVFPASHYVAGPERLERAANDIEKELGERLTELEKQGKLLEAQRLRMRTTYDLEMLRQIGSCSGVENYSMHFDGREPGSPPNTLLDYFPDDFLLVIDESHVTVPQIGAMYEGDASRKRTLVDHGFRLPSALDNRPLKWEEFQERIGQAVYLSATPGKYELSRGDGFVEQIIRPTGLIDPEVVVKPTEGQIDDLVHEIRKRTEKDERVLVTTLTKKMAEDLTDYFLELGIQVRYLHSDVDTLRRVELLRELRAGEYDVLVGINLLREGLDLPEVSLVAILDADKEGFLRSGTSLIQTIGRAARNVSGQVHMYADKITPAMEKAIDETNRRREKQVAYNKEKGIDPQPLRKKINDIVAQIAREDIDTEQLLGSGYRQAKDGKGAKAPVPSLGGKAAAKGAKSAKGKAKETVPTDRPAAKLAEEIEELTNRMRAAAADLQFEIAARLRDEVSEMKKELRQMKEAGLA
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage.
Q829Y6
B3LGB9
TRM82_YEAS1
Transfer RNA methyltransferase 82
Saccharomyces
MSVIHPLQNLLTSRDGSLVFAIIKNCILSFKYQSPNHWEFAGKWSDDFDKIQESRNTTAKEQQGQSSENENENKKLKSNKGDSIKRTAAKVPSPGLGAPPIYSYIRNLRLTSDESRLIACADSDKSLLVFDVDKTSKNVLKLRKRFCFSKRPNAISIAEDDTTVIIADKFGDVYSIDINSIPEEKFTQEPILGHVSMLTDVHLIKDSDGHQFIITSDRDEHIKISHYPQCFIVDKWLFGHKHFVSSICCGKDYLLLSAGGDDKIFAWDWKTGKNLSTFDYSSLIKPYLNDQHLAPPRFQNENNDIIEFAVSKIIKSKNLPFVAFFVEATKCIIILEMSEKQKGDLALKQIITFPYNVISLSAHNDEFQVTLDNKESSGVQKNFAKFIEYNLNENSFVVNNEKSNEFDSAIIQSVQGDSNLVTKKEEIYPLYNVSSLRKHGEHYS
Required for the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA, a modification required to maintain stability of tRNAs; its absence resulting in tRNA decay. In the complex, it is required to stabilize and induce conformational changes of the catalytic subunit.
B3LGB9
Q11DE1
TAL_CHESB
Probable transaldolase
unclassified Chelativorans
MKFFVDTADVNEIRELSETGLLDGVTTNPSLIMKSGRPILEVTREICEIVDGPVSAEVTAVDFKEMMREADILSKIADNIAIKVPLTMDGLKACKALTSSGRMVNVTLCFSANQALLAAKAGATFISPFIGRIDDMGIDGMELIAEIRTIYDNYDFDTEILAASIRSVNHVKQAAIIGADVATVPPAVLKSLVKHPLTDKGLEAFLADWAKTGQKIG
Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
Q11DE1
Q01QT2
TILS_SOLUE
tRNA(Ile)-lysidine synthetase
Candidatus Solibacter
MFASGARVAVGVSGGADSVCLLHALVELGGLKLSVLHVDHGLRGAESRADAEFVGELAARMGLPFCLREVTLGPGNVEQEGRRARLRFFHEQLAAGNCDRVALGHTRSDQAETVLFRFLRGSGTAGLAGIRPVTAEGIVRPLIELERAEIEEYLRERQIPWREDATNAGEEFARNRIRHGLLPQLAAEWNPALVETLAHTAEFARAEEAYWAGEIDRLSAESLTAGDGCVLIRTESLKALSLAVARRLVRRAIQMAKGDLRGVDFGHVERVVELASAPTGRGRTQVPGLDVRRSFEWLRLGVPFTRKPYSLKPLVPGTTQIPGTRNGISLELIEKSETSVLPWNVYNTEMGCLDWKRLAGSLELRNWRFGDQYQPMGLTGSEKIKTLFQLQRIPVWERAQWPVLTDGESIVWTRRFGPAAGFAAGPESGVVLKLGEVTIR
Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Q01QT2
Q97QD1
Y1288_STRPN
UPF0122 protein SP_1288
Streptococcus
MEIEKTNRMNALFEFYAALLTDKQMNYIELYYADDYSLAEIAEEFGVSRQAVYDNIKRTEKILEDYEMKLHMYSDYIVRSQIFDQILERYPKDDFLQEQIEILTSIDNRE
Might take part in the signal recognition particle (SRP) pathway. This is inferred from the conservation of its genetic proximity to ftsY/ffh. May be a regulatory protein.
Q97QD1
Q316N1
YQGF_OLEA2
Putative pre-16S rRNA nuclease
Oleidesulfovibrio
MKYLGIDYGTRRTGIAVTDGAGMMAFPRRTIVMSTRDAFFAELLSVVEEERPAGVVVGLPLLAGGEETLITRQVRNFVARLRRRSSLPVYLVAEELSSFEAGEDLREAGLSFREREAVVDQQAAVRILESFLNLPEDRRIPLEG
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
Q316N1
B9MKC1
TRUA_CALBD
tRNA-uridine isomerase I
Caldicellulosiruptor
MRNILLTIEYDGTGYFGWQKQPNKKTIQGTIEEAIKKLTGEEVNLIGSGRTDRGVHALNQKANFKTSSKIPTDKFPLALNSVLPGDISIKDAVEAPLDFSARYSARQKTYKYLIYNKKSRPALLRNYAYYYPYQLDVDAMQRACEYFIGEYDFKSFCSADSEAKTTIRRVYNAYLTFENECIAIYITANGFLYNMARIIAGTILDVGAGKLKPMDIPLIIESKDRTKAGKTLPPWGLYLVDVVY
Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
B9MKC1
Q1MBA9
UBIG_RHIL3
3-demethylubiquinone 3-O-methyltransferase
Rhizobium
MTEGAKSTIDQGEVDRFSAMAAEWWSPTGKFKPLHKFNPVRLAYIRDKACENFSRDPKSARPLEGLRVLDIGCGGGLLSEPVARMGASVVGADPSEKNIGIASTHAKASGVSVDYRAVTAEGLAEAGETFDIVLNMEVVEHVADVEFFMTTCAKMVRPGGLIFVATINRTMKAAALAIFAAENILRWLPRGTHQYEKLVRPEELEEPLVASGLEITDRTGVSFNPLSNQWNLSKDMDVNYMLLAKRPT
O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.
Q1MBA9
Q18HD7
TRM56_HALWD
tRNA ribose 2'-O-methyltransferase aTrm56
Haloquadratum
MKRSCENDVSVLRYGHRPGRDDRMTTHVGLTARALGADQVIFPDNATQSAETVSDIVSRFGGPFDVERTDGLNATIREWSGTVIHLTMYGERVQDVTEVIRETCLHHQPLLIIIGGEKVPSDVYEWADWNIAVTNQPHSEVAGLAVFLDRLFMGQELEQEWAGAEHVVVPQACGKRVVDAELTTEADEMNAEK
Specifically catalyzes the AdoMet-dependent 2'-O-ribose methylation of cytidine at position 56 in tRNAs.
Q18HD7
O59412
TYW1_PYRHO
tRNA wyosine derivatives biosynthesis protein Taw1
Pyrococcus
MMEMITIKPGKITVQANPNMPKEVAELFRKQHYEIVGRHSGVKLCHWLKKSLTEGRFCYKQKFYGIHSHRCLQMTPVLAWCTHNCIFCWRPMENFLGTELPQPWDDPAFIVEESIKAQRKLLIGYKGNPKVDKKKFEEAWNPTHAAISLSGEPMLYPYMGDLVEEFHKRGFTTFIVTNGTIPERLEEMIKEDKLPTQLYVSITAPDIETYNSVNIPMIPDGWERILRFLELMRDLPTRTVVRLTLVKGENMHSPEKYAKLILKARPMFVEAKAYMFVGYSRNRLTINNMPSHQDIREFAEALVKHLPGYHIEDEYEPSRVVLIMRDDVDPQGTGVEGRFIKH
Component of the wyosine derivatives biosynthesis pathway that catalyzes the condensation of N-methylguanine with 2 carbon atoms from pyruvate to form the tricyclic 4-demethylwyosine (imG-14) on guanosine-37 of tRNA(Phe).
O59412
Q0APU5
TRPD_MARMM
Anthranilate phosphoribosyltransferase
Maricaulis
MQNIYLCLTAFARGTYPDDAAIAGAFDELMSGDAPDAAIGGFLVGLAALGERPSDIAAGARALRSRMTRIEAPVGAIDTCGTGGDGKGAWNISTTAAIIAAGAGATVAKHGNRAASSKSGSSDVLAQLGVKLDCPPAAVERSLAEARVGFLFAPAHHAAVRHVGPARQALKVRTVFNLLGPLSNPAGVKRQLLGVYDRRWLVPIAEALRDLGCEHALVICGQDGMDELTTTTGSDIAELRDGDIREYSFHPEEAGLALVREADLQGGTPADNAAAIRALLDGQQGAFRDIAILNAGAALVLAGLATTIPEGTSLAAAAIDDGRAKAALMRMVAISNGEA
Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
Q0APU5
Q8Z172
ULAA_SALTI
Ascorbate-specific permease IIC component UlaA
Salmonella
MEILYNIFTIFFNQVMTNAPLLLGIVTCLGYILLRKSVSVIIKGTIKTIIGFMLLQAGSGILTSTFKPVVAKMSEVYGINGAISDTYASMMATIERMGDAYSWVGYAVLLALALNICYVLLRRITGIRTIMLTGHIMFQQAGLIAVSFYIFGYSMWTTIICTAILVSLYWGITSNMMYKPTQEVTDGCGFSIGHQQQFASWIAYKVAPFLGKKEESVEDLKLPGWLNIFHDNIVSTAIVMTIFFGAILLSFGIDTVQAMAGKVHWTVYILQTGFSFAVAIFIITQGVRMFVAELSEAFNGISQRLIPGAVLAIDCAAIYSFAPNAVVWGFMWGTIGQLIAVGILVACGSSILIIPGFIPMFFSNATIGVFANHFGGWRAALKICLVMGMIEIFGCVWAVKLTGMSAWMGMADWSILAPPMMQGFFSIGIAFMAVIIVIALAYMFFAGRALRAEEDAEKQLAEQSA
The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II UlaABC PTS system is involved in ascorbate transport.
Q8Z172
A7H426
TRUA_CAMJD
tRNA-uridine isomerase I
Campylobacter
MMKIKIIFSYDGSAFLGSATQPHKKGVQDVLSEALSHLGIFSPLLMASRTDKGVHASYAVASVECGDHFVNLEYLQKQLNKFSHPFIHIKKIEKVKDDFEVRFDVKSREYRYIFSHSSYSPFMASYVYFYPKFDLGKANELLGFFVGKKDLKFFCKSGGDNKTTLREIFIARAYAYKDFSIFHFKANGFLRGQIRLSVASVLKVLEGKMSEKELKEQIEAKKQCNHFLAPPNGLYLSRICY
Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
A7H426
Q1Q8B0
UVRC_PSYCK
Excinuclease ABC subunit C
Psychrobacter
MVNVSESSPIDDKKARLKHLIQRLPNLPGVYKMLGKNGDILYVGKAKSLKSRVNSYFAKTIDHPKTRALVARIHNIETIITRSETEALLLEQNLIKEYRPPYNVLLRDDKSYLYVFISADKPYPRLAYGRGKGNHQKGRFFGPFPSAHAAKETLVLMQKMFQMRQCTNTFFKQRKRPCLEYQIKRCRAPCVGLVSPEEYSEDVNNTIRFLKGDSSDIHTALIEKMEASAEELDFEKAVFYRDQLSMLREVQAKQAVYTVQGEADVIAIASQGGMTCVNVLTVRGGRVLGGKNYFPDVDSSEPLADNLSAFITSFYFQVTDDLPAEIILSDELPDQLAVSEALATHFGSKVVIKTSVREHRAEWLDLAKLNTNNALKTKLGDYLELHARFGALKDVLTEVTDRTIDRIECFDISHTMGEATIGSCVVFDQGGSRRRDYRQYAIHDIVGGDDYAAMKQVLTRRYKKQPLPDLLLIDGGKGQLGIAKEVLTELGILGDTLLISVAKGEGRKAGLEVLHFIDHEPLDLPMDSKALHLLMHIRDEAHRFAITAHRKKRDKRRSSSVLEVIPGLGEKRRRDLLNHFGGMQQLLGASQQELAGVQGIGPVLAKTVYKVLHE
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision.
Q1Q8B0
A2QWA2
VPS27_ASPNC
Vacuolar protein sorting-associated protein 27
Aspergillus subgen. Circumdati
MAGWFSSTSTIEDQVEKATASSLEDIALNLEISDLIRSKGVQPKDAMRCLKRRLENKNPNIQLATLKLTDTCVKNGGTHFLAEIASREFMDNLVSLLKTEGAPLNSDVKAKMLELIQDWAMAAQGRMDLSYVGETYRRLQDEGFRFPPKTQISGSMLESSAPPEWIDSDVCMRCRTPFSFMNRKHHCRNCGSVFDAQCSSKSLPLPHLGILQPVRVDDGCYAKLTSKALAPSGLSDRASFKNNSITKSSVMEPRGGRAEGGFDDDLRRALQMSLEEAQNKGSSGYVPQSTAVQQPPRAPAQPAIEEEEDADLKAAIEASLRDMEEHKQKHAAALKNTSSADIPSRQTPSATPLPKNSYELSPVEVENIHLFAALVDRLQHQPPGTILREPQIQELYESIGALRPKLARSYGETMSKHDTLLDLHAKLSTVVRYYDRMLEERLSSAYAQHSLGYSPVPGGSPYPNIYPPMPAHAPDGKTGTESFYYGNAIAESHQAPTTPYPQPQPERELHERVGTRSGTMSPGVYAHPSQPISPTVPWNGSAHAVASPQPSSASMAYPSNPSAYAGPAAPTQFYTSPPHVEPDSKPAQHARPMEPDMPYQGSPVMQRETPYQPTAPSAPDLPADQGPASGYGLQRQPTDPSAALYYAPQPPQGTPYPAYPQGAPVHPGQAVGDVSPVGVTPAHAPYQQPTPSRPPVEESLIEL
Component of the ESCRT-0 complex which is the sorting receptor for ubiquitinated cargo proteins at the multivesicular body (MVB) and recruits ESCRT-I to the MVB outer membrane.
A2QWA2
Q885T9
UBIG_PSESM
3-demethylubiquinone 3-O-methyltransferase
Pseudomonas
MSNVDRAEIAKFEALAHRWWDRESEFKPLHDINPLRVNWIDERANLAGKKVLDVGCGGGILSEAMALRGATVTGIDMGEAPLAVAQLHQLESGVSVEYRQITAEDLAEEMPEQFDVVTCLEMLEHVPDPSSVIRACHRMVKPGGQVFFSTINRNPKAYLFAVVGAEYILNLLPRGTHDFKKFIRPSELGAWSRDAGLQVKDIIGLTYNPLTKHYKLASDVDVNYMIQTLREA
O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.
Q885T9
P44401
XYLB_HAEIN
Xylulose kinase
Haemophilus
MYIGIDCGTQGTKAIVLDSVQKKVIGVGYAKHELITQSNGRREQQPNWWIEALQQALQIALKQAKNSPHFSPNLVKGIGISGQQHGLVMLDKNDRPLYKAKLWCDTETATENDILIEKLGGQTAVFEKLGIICQTGYTASKLSWFRQNYPDKFANIRKIMLPHDYLNYWLTGKFCTEFGDASGSGYFDVVKREWKREVFKYLAPELNMDEVLPKLLSAEQKIGVIKPEIATLFGFNENVIVSTGGGDNMMGAIGTGNIREGIATMSLGTSGTLYAYTQKPLLNLPPMIANFCSSNNGWLPLVCVMNITSSNKQLMNLLNIDIEELNQLAQQAPIGANGITILPFFNGERVPPLPNTKASILGLDSSNFTRENLCRAMMESATFTLRYGLDLFRQAGLKTSQIRLIGGGAKSSFWRQMIADVMNSEVVCLQEEEAAALGGAIQAMWANGEGELEFLCETFIHLDENSKAYPNLSQVKNYQNAYERYLTHLSQLY
Catalyzes the phosphorylation of D-xylulose to D-xylulose 5-phosphate.
P44401
Q8EQG0
TYSY_OCEIH
Thymidylate synthase
Oceanobacillus
MLGEQAYLDLCKQIFKTGEQRGDRTNTGTHSIFGHQIRFDLNKGFPLLTTKRVPFRLVASELLWFIKGDTNIRYLLKHNNNIWNEWAFEKWVNSADYQGPDMANFGLRSQKDENFNKQYQEQMELFKTRILEDDSFADKYGDLGSVYGKQWRNWKTTQNETIDQLKDVIHSIKTNPNSRRHIVSAWNPEDIPTMALPPCHTLFQFYVSNGKLSCQLYQRSADVFLGVPFNIASYALLTHLIAHECGLEVGDFVHTFGDAHIYSNHVEQVETQLEREIRDFPQLIINKDKNSIFEMDLDDLVIENYNPHPSIKAPIAV
Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis.
Q8EQG0
G5EFD5
UNC71_CAEEL
Uncoordinated protein 71
Caenorhabditis
MICASKITMLGLLVMCTLGGVLGKVDIRQTTANKAFMETMRADGYEVVHPFQIRDKNERIGIDTRNYFLKAQEHYSHVTIVIRSNQLGRLKLVLERNNFIFLNQTAFHKLDADGERVIQNRVENCYYQGTVGGEESSFVALSSCNGLRGVISFANGTTFGIWPLDGGDRNSRRHPHILYKSEWSQEAKCGSSMAHAVGQRRMKKHVHKHRSHHHEHNKKRDVSKRTKYVEVALIADYEFMKARGLHDLDAISYMLESLNIADSMLSRDLNIRLSAVYVELWTDVQRIDLWEDIERTLSGVVDYASGHIYHIQKDASILFTAGSFANQEVSNAAIRSICTARSAVIVKGVEQFATHWNGELLAQSIGHLLGLEHDTTACSCEPSPECVMRQQPGRVGGGGGSPFSWQFSKCSVARMHGIWQDGNIQCLLNKPFQVSELRECGNGVVDGSEECDCGSRENCQDPCCDPLTCTLRPHAQCAAHHKCCHRCELRKAGDTCRSSKSPCDVAEQCDGKSGDCPPDGHLIDGTVCGTDGQCWRGNCSDSHQQCQKLWGREARVAEPVCFEQNTKGAEYANCGQRQADGTYHPCQIEDTRCGTLHCHSGSITPIDSSLKAFTFHFTENSHQIQCKSIASAAVGLTSDGTNCASGRVCVAGSCVEMSSVSSATACPTNNLALLCSGHGHCTTTARCVCFNGWSGVACDIRSNSSTYQGSMGFGEEGSGGSSQKSSERKTIMIPHLNIGTTLETATLFAILLGFGVFLLLCLVCLMLCYRRRSVVEIPKPSDEKDEESPDRQIKFGNMPSYREEKRKRKSNKKIYGALNRITEADERDSTSLRSRDSAGGSQQLVDRRNGAPVVVGGIRDPYAGEHIYAESSSNHLTRQFRGINSDGSYPLRSFGSWRSSAPISPASSSGQLTDVSTATTPLRLNKIGKFLKTLQSDDESPSPFSDHQSFTTGIGIGARLEQMQFGGGGDEELSAVEADHDVGSNTESSRGCEEPMDPGSWDSPTLVNGASSSSTSNNYNFRQSPSLFSDPFKLEMTNSMHN
Involved in the migration of sex myoblasts (progenitors of egg-laying muscles), Q neuroblasts and BDU interneurons during development . Involved in axon branching and guidance of neurons including GABAergic type D motor neurons . Promotes sex myoblast migration and positioning independently of gonad attraction cues . May act downstream of mig-13 in order to promote the guidance, migration and positioning of Q neuroblasts and their descendants along the anteroposterior body axis . Required for coordinated movements .
G5EFD5
P21875
VLP21_BORHE
Variable major outer membrane lipoprotein 21
Borrelia
MRKRISAIINKLNISIMMMIVVLMIGCGQQPEAGKTGAAGGEKQGAGSLSEVLMEVGKSAENAFYSFLELVSDTLGFTAKSTTKKEDVGGYFNSLGGKLGEASNELEQVAKNSEAGIEKNDASKNPIRSAVNAAKKTLEALKGYLDSLGTVGDSNPVGWASNNAQGAAVDEAELKKAYKALKGIMDTAEGAGVARPEVGNIAVKVGNGTDNKDGAKILATDGAAAVGDAGKAAAILTTVSGKEMLASIVNSTEDKAVKITGNVTVETTPLEFAVGGNGAHLSQNANSKAAAVAGGIALRSLVKGGKLAADNNDDDKASQGVGITAANKLLVAVEDIIKKTVKNVLEKAKGEIDKARDPKPAGQQ
The Vlp and Vsp proteins are antigenically distinct proteins, only one vlp or vsp gene is transcriptionally active at any one time. Switching between these genes is a mechanism of host immune response evasion.
P21875
Q31EL5
UPPP_HYDCU
Undecaprenyl pyrophosphate phosphatase
Hydrogenovibrio
MEIFQAAILGIIEGLTEFLPISSTGHLIVVSDWLGIEQTKQNTAFEVIIQVAAILAIFSHYKEKFSLQHLRLWNNVLIAFLPIAIIGFIFQDTVKAFFTIETVAWFFIIGGLIFLIMEKLYVDGKHRTQDIEDLTMRQAFWIGIIQVFALIPGTSRAGASIVGGVMMGLDRKTAAEFSFLLALPVLMAASGLDLLKHYEDFNNTSWTPLMVGFLMAFLAAWLTIKVFIKFLQTFTFNAFGVYRIVFGIVLLIWFV
Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Q31EL5
Q32KS7
ZN821_BOVIN
Zinc finger protein 821
Bos
MSRRKQTNPNKVHWDQVFAGLEEQARQAMMKTDFPGDLGSQRQAIQQLRDQDSSSSDSEGDEEETTQDEVSSHTSEEDGGVVKVEKELENAEQPVGGKKVVEHEVTENLHSDPLLGLCQCPLCQLDCGSREQLIAHVYQHTAAVVSAKSYMCPVCGRALSSPGSLGRHLLIHSEDQRSNCAVCGARFTSHATFNSEKLPEVLNVESLPPAHSEGPSSAEGKDIAFTPPVYPAGILLVCNNCAAYRKLLEAQTPSVRKWALRRQNEPLEVRLQRLERERTAKKSRRDNETPEEREVRRMRDREAKRLQRMQETDEQRARRLQRDREAMRLKRANETPEKRQARLIREREAKRLKRRLEKMDMMLRAQFGQDPSAMAALAAEMNFFQLPVSGVELDSQLLGKMAFEEQNSSSLH
May be involved in transcriptional regulation.
Q32KS7
Q17134
TBXT1_BRAFL
Brachyury protein homolog 1
Branchiostoma
MSSAETMKQPTAASPDQFSVSHLLSAVESEISAGSEKGDPTERDLKITLEEKPLWDKFNALTNEMIVTKNGRRMFPVLKVNVSGLDPNAMYSFLLDFTAADNHRWKYVNGEWVPGGKPEPSVPSCVYIHPDSPNFGAHWMKSPVSFSKVKLTNKLNGGGQIMLNSLHKYEPRLHIIKVGGPDNQRMVSTHTFPETQFIAVTAYQNEEITALKIKYNPFAKAFLDAKERSDGKDGMEDLQDQPQYSQLGGWFLPGTGPICPPPNPHQFAPSLGLPSHGCDRYSTLRNHRSAPYPHPYQRSSPPTNYGHDTAASLPMMPTHDNWSGLPVSTHNMLSMSAMPHTTTSTHAQYPNLWSVSNNNLTPTTHAQTHMSGTMGTGLPHQFLRTTAPAPYHSIPTCTVPTTASSSPVYHDSHEVSSTDSGYGHSTTPPAPQTRITSNNWSPMTPPSL
Involved in the transcriptional regulation of genes required for mesoderm formation and differentiation.
Q17134
Q5P7U3
UBIG_AROAE
3-demethylubiquinone 3-O-methyltransferase
Aromatoleum
MNMNADPAELQKFSELAHRWWDTTSEFKPLHEINPLRLDWIDRNAGLAGKRVLDIGCGGGILSESMAAAGAHVTGIDLSEKALGVARLHLFESGQKVDYHHASAEEFAAQHAGEFDIVTCMEMLEHVPDPASTVAACAQLVRPGGQVFFSTINRNFKAYLFAVLGAEYILKLLPRGTHDYVKFIRPSELARYCRQAGLETAELLGMSYNPLTQVYSLGNDTDVNYLVHAKQAVS
O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.
Q5P7U3
A6MM37
YCF3_BUXMI
Photosystem I assembly protein Ycf3
Buxus
MSRSRINGNFIDKTFSIVANILLRIIPTTSGEKEAFTYYRDGMSAQSEGNYAEALQNYYEATRLEIDPYDRSYILYNIGLIHTSNGEHTKALEYYSRALERNPFLPQAFNNMAVICHYRGEQAIRQGDSEIAEAWSDQAAEYWKQAIALTPGNYIEAHNWLKITGRFE
Essential for the assembly of the photosystem I (PSI) complex. May act as a chaperone-like factor to guide the assembly of the PSI subunits.
A6MM37
Q747I7
UVRC_GEOSL
Excinuclease ABC subunit C
Geobacter
MFDTKRLTTLPDAPGVYLMKGNGGDILYVGKAKSLRKRVRSYFSKGGESRYHIRFLVGRVADIDVIVTDTEKEALLLENTLIKEHRPRYNLDLRDDKTYFSLRLDMNEEFPRLTIVRRPGRDGARYFGPYSSASAAREVLKQLYKLFPLRHYPLESCRRRRRPCLFYQLRQCAAPCHGLISGEDYQSLAEGAALFLAGKNSDLTRLYRQRMAAAAADERYEDAARYRDLIRAIEVTVEKQKMVAGDGDTDVVGFFRDATDLSVSILFYRGGRLMGSRNYLLDWEMDDAEGLSSFLSGYYNRDVVIPDEILIPFTVDDTDPLGELLTERRGKKTVLRHPVRGTKAELVRLAARNAEAYLHEKREKDSGMEQVLGELKEKLHLTNLPRRIECYDISTIQGRYSVGSRVRFQNGAPDKAGYRRYRIRTVPGTDDFAMMHEVLSRRFRDGHGGDGRPDLIVIDGGMGQLNVLTAILEELGLHGIDAVSLAKSRVERNMSDNEVVRSDERVFLPGRRNPVVLRQNGAPLLLLARIRDEAHRFAITYHQKLRGKGSIRSSLEGIPGIGEKRKRELLKRFGSIRALRQADREQLAAVPSVSPALADAIWKALHGEEPEAP
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision.
Q747I7
Q9UKP6
UR2R_HUMAN
Urotensin II receptor
Homo
MALTPESPSSFPGLAATGSSVPEPPGGPNATLNSSWASPTEPSSLEDLVATGTIGTLLSAMGVVGVVGNAYTLVVTCRSLRAVASMYVYVVNLALADLLYLLSIPFIVATYVTKEWHFGDVGCRVLFGLDFLTMHASIFTLTVMSSERYAAVLRPLDTVQRPKGYRKLLALGTWLLALLLTLPVMLAMRLVRRGPKSLCLPAWGPRAHRAYLTLLFATSIAGPGLLIGLLYARLARAYRRSQRASFKRARRPGARALRLVLGIVLLFWACFLPFWLWQLLAQYHQAPLAPRTARIVNYLTTCLTYGNSCANPFLYTLLTRNYRDHLRGRVRGPGSGGGRGPVPSLQPRARFQRCSGRSLSSCSPQPTDSLVLAPAAPARPAPEGPRAPA
High affinity receptor for urotensin-2 and urotensin-2B. The activity of this receptor is mediated by a G-protein that activate a phosphatidylinositol-calcium second messenger system.
Q9UKP6
Q9UL33
TPC2L_HUMAN
Trafficking protein particle complex subunit 2-like protein
Homo
MAVCIAVIAKENYPLYIRSTPTENELKFHYMVHTSLDVVDEKISAMGKALVDQRELYLGLLYPTEDYKVYGYVTNSKVKFVMVVDSSNTALRDNEIRSMFRKLHNSYTDVMCNPFYNPGDRIQSSRAFDNMVTSMMIQVC
Plays a role in vesicular transport from endoplasmic reticulum to Golgi.
Q9UL33
Q9GKZ4
TRAM1_BOVIN
Translocating chain-associated membrane protein 1
Bos
MAIRKKSSKNPPVLSHEFVLQNHADIVSCVAMVFLLGLMFEITAKVSIIFVTLQYNVTLPATEEQATESAFLYYYGIKDLATVFFYMLVAIIIHAIIQEYVLDKINRRMHFSKTKHSKFNESGQLSAFYLFSCIWGTFILISENYISDPTILWRAYPHNLMTFQMKFFYISQLAYWFHAFPELYFQKTKKEDIPRQLVYIGLYLFHIAGAYLLNLNHLGLVLLVLHYFVEFLFHISRLFYFSDEKYQKGFSLWAVLFVLGRLLTLILSVLTVGFGLARAENQKLDFSTGNFNVLAVRIAVLASICITQAFMMWKFINFQLRRWREHSAFQAPAVKKKPPVTKGRSSRKGTENGVNGTVTSNGADSPRNRKEKSS
Involved in the translocation of nascent protein chains into or through the endoplasmic reticulum (ER) membrane by facilitating the proper chain positioning at the SEC61 channel. Regulates the exposure of nascent secretory protein chain to the cytosol during translocation into the ER. May affect the phospholipid bilayer in the vicinity of the lateral gate of the SEC61 channel, thereby facilitating ER protein transport. Intimately associates with transmembrane (TM) domain of nascent membrane proteins during the entire integration process into the ER membrane. Associates with the second TM domain of G-protein-coupled receptor opsin/OPSD nascent chain in the ER membrane, which may facilitate its integration into the membrane. Under conditions of ER stress, participates in the disposal of misfolded ER membrane proteins during the unfolded protein response (UPR), an integrated stress response (ISR) pathway, by selectively retrotranslocating misfolded ER-membrane proteins from the ER into the cytosol where they are ubiquitinated and degraded by the proteasome.
Q9GKZ4
Q5XI41
TRAM1_RAT
Translocating chain-associated membrane protein 1
Rattus
MAIRKKSNKNPPVLSHEFVLQNHADIVSCLAMLFLLGLMFEITAKGAIIFVALQYNVTRPATEEQAAESASLYYYGIKDLATVFFYMLVAIIVHAIIQEYVLDKINRRMHFSKTKHSKFNESGQLSAFYLFACVWGTFILVSENYISDPTILWRAYPHNLMTFQMKFFYISQLAYWLHAFPELYFQKTKKEDIPRQLVYIGLYLFHIAGAYLLNLNHLGLVLLVLHYFVEFLFHISRLFYFSDEKYQKGFSLWAVLFVLGRLLTLILSVLTVGFGLARAENQKLDFSTGNFNVLAVRIAVLASICITQAFMMWKFINFQLRRWREHSAFQAPPVKRKPAVTKGRSSRKGTENGVNGTVTSNGADSPRSRKEKSS
Involved in the translocation of nascent protein chains into or through the endoplasmic reticulum (ER) membrane by facilitating the proper chain positioning at the SEC61 channel. Regulates the exposure of nascent secretory protein chain to the cytosol during translocation into the ER. May affect the phospholipid bilayer in the vicinity of the lateral gate of the SEC61 channel, thereby facilitating ER protein transport. Intimately associates with transmembrane (TM) domain of nascent membrane proteins during the entire integration process into the ER membrane. Associates with the second TM domain of G-protein-coupled receptor opsin/OPSD nascent chain in the ER membrane, which may facilitate its integration into the membrane. Under conditions of ER stress, participates in the disposal of misfolded ER membrane proteins during the unfolded protein response (UPR), an integrated stress response (ISR) pathway, by selectively retrotranslocating misfolded ER-membrane proteins from the ER into the cytosol where they are ubiquitinated and degraded by the proteasome.
Q5XI41
O75541
ZN821_HUMAN
Zinc finger protein 821
Homo
MSRRKQTNPNKVHWDQVFAGLEEQARQAMMKTDFPGDLGSQRQAIQQLRDQDSSSSDSEGDEEETTQDEVSSHTSEEDGGVVKVEKELENTEQPVGGNEVVEHEVTGNLNSDPLLELCQCPLCQLDCGSREQLIAHVYQHTAAVVSAKSYMCPVCGRALSSPGSLGRHLLIHSEDQRSNCAVCGARFTSHATFNSEKLPEVLNMESLPTVHNEGPSSAEGKDIAFSPPVYPAGILLVCNNCAAYRKLLEAQTPSVRKWALRRQNEPLEVRLQRLERERTAKKSRRDNETPEEREVRRMRDREAKRLQRMQETDEQRARRLQRDREAMRLKRANETPEKRQARLIREREAKRLKRRLEKMDMMLRAQFGQDPSAMAALAAEMNFFQLPVSGVELDSQLLGKMAFEEQNSSSLH
May be involved in transcriptional regulation.
O75541
Q9I748
TSSC1_PSEAE
Sheath protein HsiC1
Pseudomonas
MAELSTENLAQGQTTTEQTSEFASLLLQEFKPKTERAREAVETAVRTLAEHALEQTSLISNDAIKSIESIIAALDAKLTAQVNLIMHHADFQQLESAWRGLHYLVNNTETDEQLKIRVLNISKPELHKTLKKFKGTTWDQSPIFKKLYEEEYGQFGGEPYGCLVGDYYFDQSPPDVELLGEMAKISAAMHAPFISAASPTVMGMGSWQELSNPRDLTKIFTTPEYAGWRSLRESEDSRYIGLTMPRFLARLPYGAKTDPVEEFAFEEETDGADSSKYAWANSAYAMAVNINRSFKLYGWCSRIRGVESGGEVQGLPAHTFPTDDGGVDMKCPTEIAISDRREAELAKNGFMPLLHKKNTDFAAFIGAQSLQKPAEYDDPDATANANLAARLPYLFATCRFAHYLKCIVRDKIGSFKEKDEMQRWLQDWILNYVDGDPAHSTETTKAQHPLAAAEVVVEEVEGNPGYYNSKFFLRPHYQLEGLTVSLRLVSKLPSAKEA
Core component of the H1 type VI (H1-T6SS) secretion system that plays a role in the release of toxins targeting both eukaryotic and prokaryotic species. Forms the sheath of the structure by assembling into tubules together with TssB1 resulting in the stacking of cogwheel-like structures showing predominantly a 12-fold symmetry . The sheath contracts to provide the energy needed for effector delivery .
Q9I748
P37617
ZNTA_ECOLI
Zn(2+)/Cd(2+)/Pb(2+) export ATPase
Escherichia
MSTPDNHGKKAPQFAAFKPLTTVQNANDCCCDGACSSTPTLSENVSGTRYSWKVSGMDCAACARKVENAVRQLAGVNQVQVLFATEKLVVDADNDIRAQVESALQKAGYSLRDEQAAEEPQASRLKENLPLITLIVMMAISWGLEQFNHPFGQLAFIATTLVGLYPIARQALRLIKSGSYFAIETLMSVAAIGALFIGATAEAAMVLLLFLIGERLEGWAASRARQGVSALMALKPETATRLRKGEREEVAINSLRPGDVIEVAAGGRLPADGKLLSPFASFDESALTGESIPVERATGDKVPAGATSVDRLVTLEVLSEPGASAIDRILKLIEEAEERRAPIERFIDRFSRIYTPAIMAVALLVTLVPPLLFAASWQEWIYKGLTLLLIGCPCALVISTPAAITSGLAAAARRGALIKGGAALEQLGRVTQVAFDKTGTLTVGKPRVTAIHPATGISESELLTLAAAVEQGATHPLAQAIVREAQVAELAIPTAESQRALVGSGIEAQVNGERVLICAAGKHPADAFTGLINELESAGQTVVLVVRNDDVLGVIALQDTLRADAATAISELNALGVKGVILTGDNPRAAAAIAGELGLEFKAGLLPEDKVKAVTELNQHAPLAMVGDGINDAPAMKAAAIGIAMGSGTDVALETADAALTHNHLRGLVQMIELARATHANIRQNITIALGLKGIFLVTTLLGMTGLWLAVLADTGATVLVTANALRLLRRR
Confers resistance to zinc, cadmium and lead . Couples the hydrolysis of ATP with the export of zinc, cadmium or lead, with highest activity when the metals are present as metal-thiolate complexes . Can also bind nickel, copper, cobalt and mercury .
P37617
Q89UZ9
YACG_BRADU
DNA gyrase inhibitor YacG
Bradyrhizobium
MDDQVKMPTGPLKTCPICGKPAVQATHPFCSSRCRDVDLNRWLKGSYVIPGRDDEVDDVE
Inhibits all the catalytic activities of DNA gyrase by preventing its interaction with DNA. Acts by binding directly to the C-terminal domain of GyrB, which probably disrupts DNA binding by the gyrase.
Q89UZ9
P36987
TX22E_PLETR
Plectoxin-13
Plectreurys
ALKCQGWVDYCNGNVECCNECVMY
Potent toxin that may paralyze and/or kill insect pests such as H.virescens (lepidoptera), S.exigua (beet armyworm) and M.sexta (tobacco hornworm).
P36987
B0TJ18
UBIB_SHEHH
Ubiquinone biosynthesis protein UbiB
Shewanella
MTAKNIRRAYHVIRTALHYGLDDLIPSKLTPWYFKLFRYSFFWLRNQHKDKVGGERLKLAMQELGPVYIKFGQMLSTRRDLLSDEWAEELAMLQDRVPPFDSAIARASIETELNAPIESYFNDFDDIPLASASISQVHTATLKSNGAAVVLKILRPDVEQKVHADLLLMSQAADFLETLLGTNNRLRPAEVVEDYRTTIEGELNLKLEALNAIKLRNNFIDSNALYIPYMYEELCFTRLIVMERIDGIPVSDKVALEAQGTNLKLLAERGVELFFTQVFRDNFFHADMHPGNIFVSREHPNDPLYIGLDCGIMGTLTEEDKRYLAENFLAFFNRDYRRIAQLYIESGWVSPDTDVAAFEQAVKVVCEPMFNKPLDEISFGHVLLELFRTARRFDMVVQPQLVLLEKTLLYIEGLGRQLYPQLDLWQTAKPFLEQWMAEQVGPKVMAAKVKQKLPYWAEHLPELPELIYDNLKMGRNLSKNQNNLLDRYLKHQQKAHKSNYLLITSAILVICGTILINQDATLWPSYGSIGTGIALWVLGWRSRPKNRKI
Is probably a protein kinase regulator of UbiI activity which is involved in aerobic coenzyme Q (ubiquinone) biosynthesis.
B0TJ18
O31617
THIS_BACSU
Thiamine biosynthesis protein ThiS
Bacillus
MLQLNGKDVKWKKDTGTIQDLLASYQLENKIVIVERNKEIIGKERYHEVELCDRDVIEIVHFVGGG
Is the sulfur donor in the synthesis of the thiazole phosphate moiety of thiamine phosphate.
O31617
Q8N554
ZN276_HUMAN
Zinc finger protein 477
Homo
MKRDRLGRFLSPGSSRQCGASDGGGGVSRTRGRPSLSGGPRVDGATARRAWGPVGSCGDAGEDGADEAGAGRALAMGHCRLCHGKFSSRSLRSISERAPGASMERPSAEERVLVRDFQRLLGVAVRQDPTLSPFVCKSCHAQFYQCHSLLKSFLQRVNASPAGRRKPCAKVGAQPPTGAEEGACLVDLITSSPQCLHGLVGWVHGHAASCGALPHLQRTLSSEYCGVIQVVWGCDQGHDYTMDTSSSCKAFLLDSALAVKWPWDKETAPRLPQHRGWNPGDAPQTSQGRGTGTPVGAETKTLPSTDVAQPPSDSDAVGPRSGFPPQPSLPLCRAPGQLGEKQLPSSTSDDRVKDEFSDLSEGDVLSEDENDKKQNAQSSDESFEPYPERKVSGKKSESKEAKKSEEPRIRKKPGPKPGWKKKLRCEREELPTIYKCPYQGCTAVYRGADGMKKHIKEHHEEVRERPCPHPGCNKVFMIDRYLQRHVKLIHTEVRNYICDECGQTFKQRKHLLVHQMRHSGAKPLQCEVCGFQCRQRASLKYHMTKHKAETELDFACDQCGRRFEKAHNLNVHMSMVHPLTQTQDKALPLEAEPPPGPPSPSVTTEGQAVKPEPT
May be involved in transcriptional regulation.
Q8N554
Q8EV76
TIG_MALP2
PPIase
Malacoplasma
MKITSVKNEKELVSFEIDLSEKKWNEFLDKEILKASKNLKMPGYRPGKVPLEIAKKNINMPVCFVNALSSARERIEDWIIDQDEFKKMADEICDFDPVTSKPNNSNNVLNKTVSFTMSFGKYPEFKVKNVKDIKIEKIESKVNKQMVDQAIEKELAKNETMSVKERAAKLNDIVIIDFKGYVDNVAFEGGEAKNYELKLGSKSFIDNFEEQLVGLKAGDKKDVNVTFPKDYHVANLKGKKAKFEVTVHVVNEVETPKLDDEFVKSLNLKNVNTVAEYKKHLEAELQKQLDGTVDNQIQSALYTELNKMVPSDLKIHEGLVNNVAEIFISRLMISLIGKVVNIDEFVKMIDGGRGALTKEKLIEEEKNQAREYLKVKFALKQYSKVEKISVSNEDIEKEIKEIAANSNTKEKEIKEDFAVYSSIKREALDKKVFEYLKNQVAKAAK
Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Q8EV76
Q6FYW7
VIRB4_BARQU
Type IV secretion system protein virB4
Bartonella
MSIMKRESLPEEYIPYIRHVNQHVIALNSRCLMTVMAVEGVNFDTADINHLNSLHNQLNTLLRNIADERVALYSHIIRRRETIYPESRFFSSFAATLDEKYKKKMVSQELYRNDLFVSLLWNPTSGKTEQLASFFQRLTKAKKTQSEPDMEAIRKIEELSQDLIQGLESYEARLLSVYAHEGILFSEQSEFLHQLVGGRRERIPLTFGTIASTIYSDRVIFGKEMIEIRHESNERFVGMFGWKEYPSKTRPGMTDGLLTAPFEFILTQSFVFKSKAAARVIMGRKQNQMINAADRASSQIDALDEALDDLESNRFVLGEHHLSLAVFADQPKTLVEYLSKARAHLTNGGAVIAREDLGLEAAWWAQLPGNFSYRARSGAITSRNFAALSPFHSFPIGKLEGNVWGAAVALLKTQAGSPYYFNFHYGDLGNTFVCGPSGSGKTVIVNFLLAQLQKHNPTMVFFDKDQGAEIFVRAGGGKYKPLKNGQPTGIAPLKGMEYTEKNKIFLRSWVLKLVTTEGQTVTEQERQDIAKAINSLESLPHAQRSLGALQLFFDNTSKEGIAIRLQRWIKGNDLGWVFDNDQDDLNLDSQFIGYDMTDFLDNEEIRRPLMMYLFNRILDLIDGRRIIIVIDEFWKALEDDSFKAFAQDRLKTIRKQNGMMLFATQSPKDALNSTIAHTIIEQCPTQIFFPNQKANYKDYVEDFKLTEREFELIQSELSRESRRFLIKQGQNSVVAELNLRGMNDEIAILSGTTKNIELVNQIINDYGADPDTWLPIFHQRRENQ
Component of the type IV secretion system VirB/VirD4 which could be a major virulence determinant for subversion of human endothelial cell (HEC) function. Altogether with virB11, may be implicated in providing the energy, via hydrolysis of ATP, for the assembly of secretion system and substrate transport.
Q6FYW7
A4JCZ0
THIC_BURVG
Thiamine biosynthesis protein ThiC
Burkholderia cepacia complex
MNANPKFLSADAHVDAAAVAPLPNSRKVYVTGSQPDIRVPMREITQADTPTGFGGEKNPPIYVYDTSGPYTDPDAKIDIRAGLPALRQRWIEARGDTEVLDGLSSGYGRERAADPATADLRFPGLHRNPRRAQAGKNVTQMHYARQGIITPEMEYIAIRENQRRAEYLENLKASGPNGAKLAAMMGRQHPGQAFGAAAFGANALAEITPEFVRDEVARGRAIIPANINHPESEPMIIGRNFLVKINANIGNSAVTSSIGEEVDKMTWAIRWGGDTVMDLSTGKHIHETREWIIRNSPVPIGTVPIYQALEKVNGKAEDLTWEIFRDTLIEQAEQGVDYFTIHAGVRLQYVPLTANRMTGIVSRGGSIMAKWCLAHHKESFLYEHFEEICEIMKAYDVSFSLGDGLRPGSIYDANDEAQLGELKTLGELTQIAWKHDVQVMIEGPGHVPMQLIKENMDLQLDWCKEAPFYTLGPLTTDIAPGYDHITSGIGAAMIGWFGTAMLCYVTPKEHLGLPNKDDVKEGIITYKLAAHAADLAKGHPGAQVRDNALSKARFEFRWEDQFNIGLDPDKAREFHDETLPKDSAKVAHFCSMCGPHFCSMKITQDVREFAAQQGVSETEALQKGMEVKAVEFVKTGAEIYHRQ
Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction.
A4JCZ0
Q1C570
UNG_YERPA
Uracil-DNA glycosylase
Yersinia
MSPSLTWHDVIGQEKEQPYFKDTLAYVAAERRAGKTIYPPQKDIFNAFRLTELDQVKVVILGQDPYHGPNQAHGLSFSVLPGVPAPPSLGNIYKELVTDIPGFQRPNHGFLQSWAEQGVLLLNTVLTVEAGKAHSHANLGWETFTDKVIAALNEHREGVIFMLWGSHAQKKGRIINTERHYILKAPHPSPLSAHRGFLGCKHFSQANQLLQQQNQQPIDWQPKLPAVE
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.
Q1C570
Q479P4
ZAPD_DECAR
Z ring-associated protein D
Dechloromonas
MITYEYPFNERIRTLLRLEDLFEKTAYFTQEDGALEHHAALVSMFEILEVAGRADLKMDLIQELERQRQTLLAFRNNPDISEEALSGALYEIEQSSAALLGMAGKIGQYLRENDWLMSIKSRAAIPGGVCEFDLPSYHWWLHRSPETRRDALEGWLKPMLPLRDAAAIVLRLLRSSGRPKNYTATNGQFQLNLGGSAAQMVRVTVHVDEQAIPEVSANKYFLNIRFTKPPAGEIKARGCERDVAFDLTFCNL
Cell division factor that enhances FtsZ-ring assembly. Directly interacts with FtsZ and promotes bundling of FtsZ protofilaments, with a reduction in FtsZ GTPase activity.
Q479P4
O27520
TRPB2_METTH
Tryptophan synthase beta chain 2
Methanothermobacter
MMNKIVLDENEIPKKWYNINPDLPSPLPEPKNPEGGKNIENLPRVFSRGVLEQEMSMERWIKIPREVMDVYKMIGRPTPLFRAKGLEEMLDTPARIYYKREDYSPTGSHKLNTAIAQAYYARKDGAERLTTETGAGQWGTALSLACSLMDLQCKVYMVRVSFNQKPFRKTIMQLYGGEVVPSPSNHTEFGRRMLKEDPEHPGSLGIAISEAMEEALQEENVYYSLGSVLNHVLLHQTVIGLETKKQLEIAGETPDIMIGCVGGGSNFGGAIFPFVKDKLDGKLDCEFIAAEPKSCPTLTAGEYRYDFGDTAGMTPLLKMYTLGHDFVPPSVHAGGLRYHGMSPQVALLVREGVINARAVPQHTIFESGVKFAKAEGVVPAPETCHAISVAIDEARKCRETGEEKTIVISFSGHGLLDLKGYGDYLEGKI
The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
O27520
Q9UK55
ZPI_HUMAN
Serpin A10
Homo
MKVVPSLLLSVLLAQVWLVPGLAPSPQSPETPAPQNQTSRVVQAPKEEEEDEQEASEEKASEEEKAWLMASRQQLAKETSNFGFSLLRKISMRHDGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLQALKPTKPGLLPSLFKGLRETLSRNLELGLTQGSFAFIHKDFDVKETFFNLSKRYFDTECVPMNFRNASQAKRLMNHYINKETRGKIPKLFDEINPETKLILVDYILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNFRCHVLKLPYQGNATMLVVLMEKMGDHLALEDYLTTDLVETWLRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPFADLSELSATGRNLQVSRVLQRTVIEVDERGTEAVAGILSEITAYSMPPVIKVDRPFHFMIYEETSGMLLFLGRVVNPTLL
Inhibits activity of the coagulation protease factor Xa in the presence of PROZ, calcium and phospholipids. Also inhibits factor XIa in the absence of cofactors.
Q9UK55
A0B5H8
TBP_METTP
TATA-box factor
Methanothrix
MESTINIENVVASTKLADEFDLVKIESELEGAEYNKEKFPGLVYRVKSPKAAFLIFTSGKVVCTGAKNVEDVRTVITNMARTLKSIGFDNINLEPEIHVQNIVASADLKTDLNLNAIALGLGLENIEYEPEQFPGLVYRIKQPKVVVLIFSSGKLVVTGGKSPEECEEGVRIVRQQLENLGLL
General factor that plays a role in the activation of archaeal genes transcribed by RNA polymerase. Binds specifically to the TATA box promoter element which lies close to the position of transcription initiation.
A0B5H8
Q8YVT9
TGT_NOSS1
tRNA-guanine transglycosylase
Nostoc
MSAIFSFQSLARCSQTKARSGIFLTPHGIVETPRFMPVGTLANVKTVTPAQLKETGAQMVLSNTYHLHLQPGEAIVAGGGGLHKFMGWNGPMLTDSGGFQVFSLSEMRKITEEGVTFRSPRDGQIIKLTPERSIEIQNILGADVIMAFDECPPYPANRQEVEAATERTYRWLERCITAHQRQDQALFGIVQGGVYLDLRAKAANTLTELDLPGYAIGGVSVGEPPEMMAQIVQATAPLLPAHKPRYLMGVGTYREMVIAIASGIDLFDCVIPTRWARHGTAMVKGERWNLKNAKFREDFAPIDETCPCYACQNFSRAYISHLVRSQEILAYTLLSIHNITELIRFTQKIREAILSDRFLEEFGHWLNSAETDNR
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Q8YVT9
Q6D855
TGT_PECAS
tRNA-guanine transglycosylase
Pectobacterium
MKYELQTTDGRARRGRLIFERGVVETPAFMPVGTYGTVKGMTPEEVKETGAQILLGNTFHLWLRPGQEIMKLHGDLHDFMNWHGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDSIFLSPEKSMEIQNDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRQRFDELENKNALFGIIQGSVYEDLRDVSVKGLVDIGFDGYAVGGLAVGEPKEDMHRILEHVCPQIPEDKPRYLMGVGKPEDLVEGVRRGVDMFDCVMPTRNARNGHLFVTDGVVKIRNAKHKDDVSSLDEHCDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRQAIEEGKLELFVVDFYQRIGKPIPPLAEKDVAASN
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Q6D855
Q88DP1
THIE_PSEPK
Thiamine-phosphate pyrophosphorylase
Pseudomonas
MKLRGLYAITDSQLLAGRFLSHVEAALEGGVCLLQYRDKTDDAARRLREAEGLMKLCERYGTQLLINDDAELAARLGVGVHLGQTDGPLTPARALLGRQAIIGSTCHASLELAAQAASEGASYVAFGRFFNSVTKPGAPAANVGLLEQARAQVKLPIAVIGGITLDNAAPLVAHGADLLAVIHGLFGADSAQEVTRRARAFNALFAS
Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
Q88DP1
P18729
ZG57_XENLA
Gastrula zinc finger protein XlCGF57.1
Xenopus
TGGKSYTCTECGKGFIKKSRLVTHMKIHTGETHFICTECGKGFSQKGILQTHMKTHTGEKPFTCTECGKNFAQITTLLRHLTIHTGEKPFSCTECGKHFAHKGHLVSHMKTHTGEKPFTCTECGKHFAQKGHLVSHMKTHTGEKPFTCTECGKNFAQKTNLLCHLKIHTGEKPFTCTECGDKFAKKNNLLRHLKIHTGEKPFTCTECGKAFTLKGSLVGHMKIHTGEKPFSCTQCGKNFTQKNSLLCHLTMHTGEKPFTCTECGKGFALKGNLVLHTKIHTGEKPFSCTQCGKNFAQKNSLLRHLKIHTREKPFTYSECGKKYSQIVNLASHMKIH
May be involved in transcriptional regulation.
P18729
Q6ND54
TSAD_RHOPA
tRNA threonylcarbamoyladenosine biosynthesis protein TsaD
Rhodopseudomonas
MTSEQALLVLGIETTCDETAAAVVERRADGSGRLLSNIVRSQTDEHAPFGGVVPEIAARAHVDVLDGIIAAAMNEAGVAFASLSGVAAAAGPGLIGGVIVGLTTAKAIALVHGTPLIAVNHLEAHALTPRLTDSVEFPYCLFLASGGHTQIVAVLGVGNYVRLGTTVDDAIGEAFDKIAKMLGLPYPGGPQVERAAEAGDPNRFAFPRPMLGRQDANFSLSGLKTAVRNEAGKLTPLDPQDINDLCAGFQAAVLESVADRLGAGLRLFKERFGPPKALVAAGGAAANQAIRRMLREVAAKVQTTLIVPPPALCTDNGAMIAWAGAERLALGLTDTMDTAPRARWLLDANATAPAKFANTRAGF
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
Q6ND54
Q4I1B1
VAC8_GIBZE
Vacuolar protein 8
Fusarium
MGICSSTCCGGRARDGLYEPVLADSEREAVADLLQYLENRGETDFFSGEPLRALSTLVFSENIDLQRSASLTFAEITERDVREVDRDTLEPILFLLQSPDIEVQRAASAALGNLAVDTENKVLIVQLGGLTPLIRQMMSPNVEVQCNAVGCITNLATHEENKAKIARSGALGPLTRLAKSRDMRVQRNATGALLNMTHSDENRQQLVNAGAIPVLVQLLSSPDVDVQYYCTTALSNIAVDASNRRKLAQSEPKLVQSLVNLMDSTSPKVQCQAALALRNLASDEKYQLDIVRANGLHPLLRLLQSSYLPLILSAVACIRNISIHPMNESPIIETNFLKPLVDLLGSTDNEEIQCHAISTLRNLAASSDRNKALVLDAGAVQKCKQLVLDVPITVQSEMTAAIAVLALSDDLKSHLLNLGVCGVLIPLTHSPSIEVQGNSAAALGNLSSKVGDYSIFVQNWTEPQGGIHGYLCRFLQSGDATFQHIAVWTLLQLFESEDKTLIGLIGKAEDIIEHIRSIANRQIEPDNEFEDEDEGEVVNLAQRCLELLGQSMSKAHIEG
Functions in both vacuole inheritance and protein targeting from the cytoplasm to vacuole.
Q4I1B1
Q9RCA5
YIDC1_HALH5
Membrane protein YidC 1
Halalkalibacterium (ex Joshi et al. 2022)
MYRKFGMAAMLVSILLLMTGCFNVNEPINAQSEGIWDSYFVYPLSWLMIYFANAFNGSFGLAIIVVTLLIRLLILPLMIKQLKSTRAMQALQPEMQALREKYSAKDQRTQQKLQQETMALFQKHGVNPLAGCFPVLIQMPILLAFYHAIMRTREIGDEHFLWFVLNQPDPILLPIIAGITTFLQQKMMMVTDNPQMKVLLYVMPVMILVFAMFLPSSLALYWVIGNLFMILQTYFITGPNVGAKKVAADVKVGGKKK
Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins.
Q9RCA5
Q9V150
TRPB2_PYRAB
Tryptophan synthase beta chain 2
Pyrococcus
MKVVLPDGRIPRRWYNILPDLPEPLDPPLDPETEEPIDIEKLKRIFAEELVKQEISRERYIEIPGELRKLYSKIGRPTPLFRATNLEKLLGTPARIYFKYEGATVTGSHKINTALAQAYYAKKQGIERLVTETGAGQWGTALSLAGALLGLKVRVYMARASYQQKPYRKTLMRIYGAEVFPSPSENTEVGKRFLKEDPNHPGSLGIAISEAIEDVLKDEKARYSLGSVLNHVLMHQTVIGLEAKEQMEEFEEPDVIIGCVGGGSNFAGLAYPFVKDVLDGKSEYEFIAVEPKAAPTMTRGVYTYDYGDSAGLTPKLKMHTLGHRYYVPPIHAGGLRYHGLAPTLSVLINHGIVKPIAYHQTEVFEAAVLFAKAEGIVPAPESAHAVKAVIDKALEARREGKEMVILFNLSGHGLLDLKGYEDYLDGKLEDYEPRDLPVKS
The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
Q9V150
O05960
YBEY_RICPR
Endoribonuclease YbeY
typhus group
MINVEIIRNYNKWREHRKINKGLIKKITQNVLVRFDNFSKIKQFELSILLTNTAEILTLNQQFRSIEKATNVLSFPNNELNWHNLYSKLEFLYYSDYMHLGDIAFCYEVIYNESCEQQKTFENHFIHMLIHSILHLIGFDHQNDTDANIMESLEIEILSYFGIPSPY
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
O05960