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sequence
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2.75k
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5.51k
AlphaFoldDB
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10
Q0JXE7
BPE_ARATH
bHLH transcription factor bHLH031
Arabidopsis
MDPSGMMNEGGPFNLAEIWQFPLNGVSTAGDSSRRSFVGPNQFGDADLTTAANGDPARMSHALSQAVIEGISGAWKRREDESKSAKIVSTIGASEGENKRQKIDEVCDGKAEAESLGTETEQKKQQMEPTKDYIHVRARRGQATDSHSLAERARREKISERMKILQDLVPGCNKVIGKALVLDEIINYIQSLQRQVEFLSMKLEAVNSRMNPGIEVFPPKEVMILMIINSIFSIFFTKQYMFLSRYSRGRSLDVYAVRSFKHCNKRSDLCFCSCSPKTELKTTIFSQNMTCFCRYSRVGVAISSSKHCNEPVTLCFYSYCLRKIYHFLLWNLKYKIQKSVLFS
Involved in the control of petal size, by interfering with postmitotic cell expansion to limit final petal cell size.
Q0JXE7
Q8NHV4
NEDD1_HUMAN
Neural precursor cell expressed developmentally down-regulated protein 1
Homo
MQENLRFASSGDDIKIWDASSMTLVDKFNPHTSPHGISSICWSSNNNFLVTASSSGDKIVVSSCKCKPVPLLELAEGQKQTCVNLNSTSMYLVSGGLNNTVNIWDLKSKRVHRSLKDHKDQVTCVTYNWNDCYIASGSLSGEIILHSVTTNLSSTPFGHGSNQSVRHLKYSLFKKSLLGSVSDNGIVTLWDVNSQSPYHNFDSVHKAPASGICFSPVNELLFVTIGLDKRIILYDTSSKKLVKTLVADTPLTAVDFMPDGATLAIGSSRGKIYQYDLRMLKSPVKTISAHKTSVQCIAFQYSTVLTKSSLNKGCSNKPTTVNKRSVNVNAASGGVQNSGIVREAPATSIATVLPQPMTSAMGKGTVAVQEKAGLPRSINTDTLSKETDSGKNQDFSSFDDTGKSSLGDMFSPIRDDAVVNKGSDESIGKGDGFDFLPQLNSVFPPRKNPVTSSTSVLHSSPLNVFMGSPGKEENENRDLTAESKKIYMGKQESKDSFKQLAKLVTSGAESGNLNTSPSSNQTRNSEKFEKPENEIEAQLICEPPINGSSTPNPKIASSVTAGVASSLSEKIADSIGNNRQNAPLTSIQIRFIQNMIQETLDDFREACHRDIVNLQVEMIKQFHMQLNEMHSLLERYSVNEGLVAEIERLREENKRLRAHF
Required for mitosis progression. Promotes the nucleation of microtubules from the spindle.
Q8NHV4
Q81MB0
BIOF_BACAN
8-amino-7-ketopelargonate synthase
Bacillus cereus group
MNQPWRTHLQTKLKQLHEQGQYRNLHVTEQAEETWLIRDEKRMLNLASNNYLGLAGDERLKEAAIVCTRKYGTGATASRLVVGNYSLYEEVERSICNWKGTEKALVVNSGFTANVGAISSLACRHDIVFSDKLNHASIVDGIILSGAEHKRYRHNDLNHLEALLKTASPEKRKLIVTDTVFSMDGDTAHLRELVQLKEKYGAIIIVDEAHASGIYGIGGAGLSHIEKDLAQKIDIHMGTFSKALGCYGAYLTGDAIYIEYLQNMMRSFIFTTALPPSTLGAVQKAIEIVQEDHKRRENLIANGEYFRSKLREAGFNIGNSSTHIVPIVVGSNENTLRFSKRLQEAGIAAIAIRPPTVPVHSSRIRFAVTSQHTIADLKWAIDRITHIAKEEELFV
Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide.
Q81MB0
Q7JVI3
EIF3M_DROME
Transport and Golgi organization protein 7
Sophophora
MTSHPVFIDLSLDEQVQELRKYFKKLGAEISSEKSNKGVEDDLHKIIGVCDVCFKDGEPSQIDGILNSIVSIMITIPLDRGENIVLAYCEKMTKAPNLPLGKVCLQSLWRLFNNLDTASPLRYHVYYHLVQVAKQCEQVLEVFSGVDQLKSQFANCPPSSEQMQKLYRLLHDVTKDTNLELSSKVMIELLGTYTADNACVAREDAMKCIVTALADPNTFLLDPLLSLKPVRFLEGDLIHDLLSIFVSEKLPAYVQFYEDHREFVNSQGLNHEQNMKKMRLLTFMQLAESSPEMTFETLTKELQINEDEVEPFVIEVLKTKLVRARLDQANQKVHISSTMHRTFGAPQWEQLRDLLQAWKENLSTVREGLTSVSSAQLDLARSQKLIH
Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation (Potential).
Q7JVI3
Q6FR35
UBA4_CANGA
Sulfurtransferase UBA4
Nakaseomyces/Candida clade
MTDQDLLAQIELLKKENAQLKEKLKSQDDEQLSLEEYSRYGRQMIVEGTGGVVGQLRLKKAKVLVVGAGGLGSPSLPYLVGAGVGTIGIVDNDIVDTSNLHRQTIHNTAKVGMLKCESAKQVLKDLNPHVNINTYPVRLGPENAFSIFADYDIVMDCTDTPLTRYLISDVAVNLGKTVVSASGLGTEGQLTILNFNNIGPCYRCFYPVSPNPYAVSSCQEGGVIGPCIGLVGTMMAVETLKIIMGVYNNENFEPFLLSYSGFPIQSLRRFKMRGRQSKCQTCGDAPVITKEAIESGIIDYNIFCGSRNYNVCAEGERLTAKEFDENYGPEFSGNNKVLLDVRPSHHFDISHFNNAVNIPLKELRDMDGDISTLQSRIPNINKNSEVVVLCRYGNDSQLATRMLKDEFGITNVKDVAGGFFKYIDDVDQSIPKY
Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Acts by mediating the C-terminal thiocarboxylation of sulfur carrier URM1. Its N-terminus first activates URM1 as acyl-adenylate (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to URM1 to form thiocarboxylation (-COSH) of its C-terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as nucleophile towards URM1. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; NFS1 probably acting as a sulfur donor for thiocarboxylation reactions. Prior mcm(5) tRNA modification by the elongator complex is required for 2-thiolation. May also be involved in protein urmylation.
Q6FR35
Q0I8N1
ACCA_SYNS3
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha
unclassified Synechococcus
MARRPLLEFEKPLIELEQQIEQIRQLARDSEVDVSQQLLQLETLAARRREEIFQNLTPAQKIQVARHPHRPSTLDFIQMFCDDWVELHGDRRGSDDQALVGGLGRIGDRSVVLLGHQKGRDTKENVARNFGMATPGGYRKALRLMEHADRFGLPIFAFIDTPGAYAGLLAEEQGQGEAIAVNLREMFRLRVPIIATVIGEGGSGGALGIGVADRLLMFEHSVYTVASPEACASILWRDAAKAPEAAAALRITGKDLLSLGVVDEVLAEPSGGNNWAPLEAGATLREALERNLSELLALPPQELRDQRYRKFRAMGRFIDQASSDADSAS
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.
Q0I8N1
C0MBD4
DLTC_STRE4
D-alanine--poly(phosphoribitol) ligase subunit 2
Streptococcus
MSTKETVIDLFDRLFMEDVSDMMDEDLFDAGVLDSLGTVELIVEIESIFNIKVPISEFGREDWNTANKIIQGIEELQHA
Carrier protein involved in the D-alanylation of lipoteichoic acid (LTA). The loading of thioester-linked D-alanine onto DltC is catalyzed by D-alanine--D-alanyl carrier protein ligase DltA. The DltC-carried D-alanyl group is further transferred to cell membrane phosphatidylglycerol (PG) by forming an ester bond, probably catalyzed by DltD. D-alanylation of LTA plays an important role in modulating the properties of the cell wall in Gram-positive bacteria, influencing the net charge of the cell wall.
C0MBD4
P16172
MERB_BACCE
Organomercurial lyase
Bacillus cereus group
MKTEIQEIVTRLDQQSNKGEGGESMKWLFRPLLQMLAGGESVTIEDMATTTGKPVEEVKKVLQSLPSVEIDEQGRVVGLGLTLIPTPHHFTVDGKQLYAWCALDTLIFPALIGRSVNIESPCHSTGEPIRLNVEPDHIVSVEPSTAVVSIVTPDDMSSIRTAFCNEVHFFSSPNAAEDWLDQHPGGKVLSVEDAFELGRLMGTRYEESRPANGSCCDI
Cleaves the carbon-mercury bond of organomercurials such as phenylmercuric acetate. One product is Hg(2+), which is subsequently detoxified by the mercuric reductase.
P16172
A4VII0
DDL_PSEU5
D-alanylalanine synthetase
Pseudomonas
MMALQSTRDPKEFGRVAVLFGGKSAEREVSLKSGAAVLAALQAAGVDAFGIDAGDDLLQRLSSERIDRAFIVLHGRGGEDGSMQGLLECAGIPYTGSGILASALAMDKLRTKQVWQSLGLPTPRHAVLASEVDCQAAAQMLGFPLIVKPAHEGSSIGMAKVGDVAELIAAWRAASAYDAQVLVEQWIQGPEFTVAVLHGEVLPPIGLGTPHTFYDYDAKYLASDTQYRIPCGLDAAREEALKVLSARACEAVGIRGWARVDVMQDAEGNFWLLEVNTVPGMTDHSLVPMAARAAGLDFQQLVLSILDDSLEAGN
Cell wall formation.
A4VII0
Q9LIN3
RZ1A_ARATH
null
Arabidopsis
MSEDPEYRCFIGGLAWTTSDRGLRDAFEKYGHLVEAKVVLDKFSGRSRGFGFITFDEKKAMDEAIAAMNGMDLDGRTITVDKAQPHQGGAGRDNDGDRGRDRGYDRDRSRPSGGRGGGDCFKCGKPGHFARECPSESSRDGGGRFSSKDDRYSSKDDRYGAKDDRYGAKEDRYGAKDDRYSSKDDRYSSKDDRYGSRDGGGSRYGPDRSGERAGGRSRDGGSRGAPGGERHSRAPYDRPRAGGFH
Binds RNA and DNA sequences with a preference to single-stranded nucleic acids. Displays strong affinity to poly(G) and poly(U) sequences. May be involved in tolerance to cold stress.
Q9LIN3
A1JPI0
PSRP_YERE8
Pyruvate, water dikinase regulatory protein
Yersinia
MERSVFYISDGTAITAEVLGHAVLSQFPVKATTFTLPFVESATRAQEVCEKINEIYRETGVRPLVFYSIISPEVRELIQHSEGFCQDIVQALVAPLQGELGVSPQPVLNRTHGLTESNLGKYDARIAAIDYALAHDDGISLRNLDQAQVILLGVSRCGKTPTSLYLAMQFGIRAANYPFIADDMDNLQLPAALKPFQHKLFGLTINPERLAAIREERRENSRYASLRQCRMEVGEVEALFRKNQIRYLNSTNYSVEEISTKILDILGMSRRMF
Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the phosphoenolpyruvate synthase (PEPS) by catalyzing its phosphorylation/dephosphorylation.
A1JPI0
C5CC59
RL2_MICLC
50S ribosomal protein L2
Micrococcus
MAIRKYKPTTPGLRGSSVADFAEITRSTPEKSLLRPLHKTGGRNNTGRITTRHKGGGHKRQYRLVDFRRHDKDGVPATVAHIEYDPNRTARIALLHYADGAKRYILAPAKLKQGDVVEAGPNADIKPGNNLPMRNIPVGTTIHAVELRPGGGAKMARSAGASVQLVAREGKYAQLRLPSGEIRNVDVRCRATIGEVGNAEQSNINWGKAGRMRWKGVRPTVRGVVMNPVDHPHGGGEGKTSGGRHPVNRNGKPEGRTRRPNKESDKLIVRRRRTGKNKR
One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome.
C5CC59
Q3SJQ0
NUOH_THIDA
NDH-1 subunit H
Thiobacillus
MEAGIVEAAGMDWEAFQTVAWTLVKIMALVVPLMLGVAYLTYAERKIIGWMQVRIGPNRVGFQGLLQPIADAVKLLMKEIIIPSGASRALFILGPILAIAPALAAWAVIPFSDGLVLADINAGLLYVMAITSMGVYGVIIAGWASNSKYAFLGAMRSAAQIVSYEIAMGFALVGVLMASQSLNLSAIVQGQAGGIQQWYLWPLFPLFVVYLVAGVAETNRAPFDVAEGESEIVAGFHVEYSGMAFAVFFLAEYANMILVAALTTLMFLGGWLSPVAFLPDGIVWWLLKTGFVLFLFLWFRATFPRYRYDQIMRLGWKVFIPITIVWIVFVGGMMQTPYGHLFH
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. This subunit may bind ubiquinone.
Q3SJQ0
P57432
FABG_BUCAI
Beta-ketoacyl-ACP reductase
Buchnera
MNINRQTAFITGANQGIGKAIAKKLIKKGIQVIGTSTTEDGVKRINDYLEGNGFGFVLNLKNIDSITEKIQEIYKKKHSIDILINNAGIKEDNLLVNMKSTEWDDVIKTNLSSVFHLVKSVIRSMIKKRQGRIITIGSVIAYTGNKGQVNYSASKSGLIGFHKSLALEVASKGITVNIVSPGLIKTNFTEKLNSIQYQKYLSNIPMKRFGQKEEVADAVIFLASKKASYITGHTLHVNGGMYMI
Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis.
P57432
Q96H20
SNF8_HUMAN
ESCRT-II complex subunit VPS22
Homo
MHRRGVGAGAIAKKKLAEAKYKERGTVLAEDQLAQMSKQLDMFKTNLEEFASKHKQEIRKNPEFRVQFQDMCATIGVDPLASGKGFWSEMLGVGDFYYELGVQIIEVCLALKHRNGGLITLEELHQQVLKGRGKFAQDVSQDDLIRAIKKLKALGTGFGIIPVGGTYLIQSVPAELNMDHTVVLQLAEKNGYVTVSEIKASLKWETERARQVLEHLLKEGLAWLDLQAPGEAHYWLPALFTDLYSQEITAEEAREALP
Component of the endosomal sorting complex required for transport II (ESCRT-II), which is required for multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs. The MVB pathway mediates delivery of transmembrane proteins into the lumen of the lysosome for degradation. The ESCRT-II complex is probably involved in the recruitment of the ESCRT-III complex. The ESCRT-II complex may also play a role in transcription regulation by participating in derepression of transcription by RNA polymerase II, possibly via its interaction with ELL. Required for degradation of both endocytosed EGF and EGFR, but not for the EGFR ligand-mediated internalization. It is also required for the degradation of CXCR4. Required for the exosomal release of SDCBP, CD63 and syndecan .
Q96H20
Q2Y5Z0
DAPF_NITMU
PLP-independent amino acid racemase
Nitrosospira
MKLKFTKMHGLGNDFIVIDAVNQQISLSPEQLRRLADRHLGVGCDQILLIEKAEGDADFRYRIFNADGGEVEQCGNGARCFVRYVHDHGMTDKQQVRIETLSGVVIPELEADGEVTVNMGVPKFDPVEIPFIAEQRAPTYSLSLDDRQVEISSVSMGNPHAVQVVSDLDNAPVLTEGPVIEKHSRFPQRVNAGYMQVVDPHHIRLRVYERGAGETLACGTGACAAAVAGIQRGLLESPVRVSFSTGDLFIRWEGENQPVWMTGPAVAVFDGEIELQF
Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan.
Q2Y5Z0
Q9UTG8
DAD2_SCHPO
Outer kinetochore protein dad2
Schizosaccharomyces
MLQARIEEKQKEYELICKLRDSSNDMVQQIETLAAKLETLTDGSEAVATVLNNWPSIFESIQIASQHSGALVRIPPSTSNTNASATEQGDVEEV
Component of the DASH complex, a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. The DASH complex mediates the formation and maintenance of bipolar kinetochore-microtubule attachments by forming closed rings around spindle microtubules and establishing interactions with proteins from the central kinetochore. May be necessary for growth under high osmotic stress.
Q9UTG8
Q5LHY8
ARGR_BACFN
Arginine repressor
Bacteroides
MKKKANRLDAIKMIISSKEVGSQEELLQELGQEGFELTQATLSRDLKQLKVAKAASMNGRYVYVLPNDIMYKRVGDQSASEMLMNNGFISLQFSGNIAVIKTRPGYASSMAYDIDNRESDTILGTIAGDDTIMLVLREGATPTAVRHFLSLIIPNIN
Regulates arginine biosynthesis genes.
Q5LHY8
B6HZI2
IRAP_ECOSE
Anti-adapter protein IraP
Escherichia
MKNLIAELLFKLAQKEEESKELCAQVEALEIIVTAMLRNMAQNDQQRVIDQVEGALYEVKPDASIPDDDTELLRDYVKKLLKHPRQ
Inhibits RpoS proteolysis by regulating RssB activity, thereby increasing the stability of the sigma stress factor RpoS especially during phosphate starvation, but also in stationary phase and during nitrogen starvation. Its effect on RpoS stability is due to its interaction with RssB, which probably blocks the interaction of RssB with RpoS, and the consequent delivery of the RssB-RpoS complex to the ClpXP protein degradation pathway.
B6HZI2
B4XSZ4
SLA4_MACLB
C-type lectin A4
Macrovipera
MGRSISVSFGLLVVFLSLSGTGADQDCLPGWSSHEGHCYKVFNLNKTWEDAKKFCTEQANSGHLVSIDSKKEANFVAELVSQNIKETRRTDFVWIGLRAEDKRQHCSSEWSDGSSINYQNWIEAESKKCLGLEKQTRYRKWVNLNCGQPYRFTCEI
Interferes with one step of hemostasis (modulation of platelet aggregation, or coagulation cascade, for example).
B4XSZ4
Q746Y7
GATA_GEOSL
Glutamyl-tRNA(Gln) amidotransferase subunit A
Geobacter
MELFELTLHELHDKLAKREVSSVEATRALLARIEATDSRVNAYITVTPDEALAAAEAADRRIAAGGLTPLTGVPVALKDIFVTRGIRTTCGSKILGNFIPPYDGTVVAKLREAGAVIVGKLNQDEFAMGSSGESSAFGATKNPWNLACIPGGSSSGSAAAIAARSATATLGTDTGGSIRQPASHCGCVGLRPTYGRVSRYGVIAYASSLDQVGPVTRDVTDCALMLGAVAGHDPLDSTSIDLPVPDYAAALTGQVKGLRLGLPKEYYLEGLDPDVKRALDAAIETYRGLGAEFVEVSLPHTDYAVATYYLIATAEASSNLARYDGVRFGHRAAGAANLIDMFRRSRAEGFGAEVKRRIMIGTYALSSGYYDAYYLKAQKVRTLIMQDFMKAFEQVDALLTPVAPTPAFKIGEKVDDPLQMYLSDIFTIPVNLAGTCAISVPAGMSAAGLPIGLQLIGRPFGEETILRAAHAFEQATEWHRHTAQL
Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
Q746Y7
A9B536
ACCD_HERA2
Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta
Herpetosiphon
MKDFFRRAPLPFTSSRREQQIPDNVWAKCANCGELTYQKQFNDALKVCPKCSYHSRISSREWIEVLADADSFVEYDADLQGIDILGFVSPKDNYEAKLAATSERTGTNDVVMSGSASIEGLPFEIAACNFEFMGGSMGSVFGEKVARAVERAADRGVPVLTINASGGARMHEGIFALMQMAKVSVALTRLARVRQPHISLLVDPCYGGVSASYASVADIILAEPGANIGFAGRRVIEQTIRQKLPPNFQTAEFFLEHGMIDAVVPRSDMRATIGRLLRLYQRPTSSADHREHVVAGHQ
Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.
A9B536
Q8VED2
BL1S4_MOUSE
Protein cappuccino homolog
Mus
MEEGPAVGTLSREVSTEEAEPLGAAWSGDSGHVSQSHSSASGPWDDDGPEDAPGRDLPLLRRAASGYASSLLPSAGPRPEVEALDASLEELLAKVDEFVGMLDMIRGDSSHVVGEGVPRIHAKAAEMRRIYGRIDKLEAFVRMIGSSVARMEEQVAKAEAELGTFPRAFRRLLHTISVPALFRSAPSGPQRAAYEPPVLFRTEDHFPGCGDRPQL
Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. Plays a role in intracellular vesicle trafficking.
Q8VED2
P85110
SLAP2_BACHU
55 KDa parasporal endotoxin
Bacillus cereus group
LDTDLQGTMPEVYASERAAFL
The S-layer is a paracrystalline mono-layered assembly of proteins which coat the surface of bacteria.
P85110
Q8PLS0
ENO_XANAC
2-phosphoglycerate dehydratase
Xanthomonas
MTTIAKILAREILDSRGNPTLEAEVTLDDGSFGRAAVPSGASTGTKEAVELRDGDKTRYLGKGVRHAVDNVNGTIAETLKNFDAADQQGLDRRLIDLDGTENKGRLGANALLGVSLAAAHAVAASRKQPLWQYLSTITEADVALPVPMMNIINGGAHADNNVDFQEFMVLPVGCSSFSEALRAGTEIFHSLKSVLKGHGLSTAVGDEGGFAPDFRSNVEALDTILEAIGKAGYTAGEDILLGLDVASSEFYDNGKYNLVGENKRLTSEQFVDFLADWVAQYPIISIEDGLAEDDWAGWKLLTDRVGKKVQLVGDDLFVTNPKIFKQGIDSGTANAILIKVNQIGTLTETLEAIAMAHAANYASIVSHRSGETEDTTIADIAVATTATQIKTGSLCRSDRVAKYNQLLRIEQALGSGARYAGRDAFVSIKR
Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
Q8PLS0
B8N7S7
EGLX_ASPFN
Mixed-linked glucanase AFLA_105200
Aspergillus subgen. Circumdati
MSSSSFVWTVGSIALSSLITPTIADGSGSRYQLTEAWQGEKFLDHFKFFSGSDPTNGFVTYANQSYAESSGLIEVTESGSFYMGVDYKTKLSPNGPGRDSVRIESKEYYDEGLYIIDLQHMPGSVCGTWPAFWSVGPNWPYDGEIDIIEGVNKHEANEIVLHTSGSCSLSSENDMSGTMSSSECGESSGTIGCVVKGQTGTSGAPFNEKNGGVYAMEWTSSFVKIWYFARSEIPQSITEGNPDTTAFGTPMAHLQGTCDFGERFKSQKFILDTTFCGDWAGGVFGDSGCPVSDPSNPIQSCVNYVAENPAAFKEAYWEINYIKLFQTGTGHSTASIASQAETATAVVSKTVDSVPSVTSTPILETTAPAPETVSAEAPATSSAVPEPANPQTSVAGAETTAAPAPSPETTAAPASPSSDDSEGADAVSETTIYVTETTTICGASTQKGTIQTIGGGETEVSPASSTVESAATPAAPTPTSQEPVASLPGTTVNDGTPVPTDVSPETPAEETAGESGAPTPSAEQPEKPQPAATSIETGIVPPPVSNPAPTEQGTPEGASPVDATESRHVPDEPAPTSAAPIRSPSPSSWTISSSSRVALSSSFASTTSSASRTTSATKEATAPTETDSGASTGTNPESPVFTAGASKSVGISGLAGIVCGIAMAMLA
Mixed-linked glucanase involved in the degradation of complex natural cellulosic substrates.
B8N7S7
Q5PPG4
ZN639_RAT
Zinc finger protein 639
Rattus
MSEYPKKRKRKTLHPSRYSDSSGISRIADGVSGIFSDHCYSVCSMRQPDLKYFDNKDDDSDPETANDLPKFTDGTKARSRSQSCLVPSPVLRILEHTVFSTEKPADVEICDEECGSPESGHQHTHEESPIEVHTSEDVPIAVEVHAISEDYDIEAENNSSESLLDQTDEEPPAKLCKILDKSQASNVTAQQKWPLLRANSSGLYKCELCEFNSKYFSDLKQHVILKHKRTDSNVCRVCKESFSTNMLLIEHAKLHEEDPYICKYCDYKTVIFENLSQHIADTHFSDHLYWCEQCDVQFSSSSELYLHFQEHSRDEQYLCQFCEHETGDPEDLHSHVVNEHARRLIELSDKCGSGGHGQCSLLSKITFDKCKNFFVCQVCGFRSRLHTNVNRHVAIEHTKIFPHVCDDCGKGFSSMLEYCKHLNSHLSEGIYLCQYCEYSTGQIEDLKIHLDFKHSADLPHKCSDCLMRFGNERELISHLPVHETT
Binds DNA and may function as a transcriptional repressor.
Q5PPG4
Q3Z8D9
KTHY_DEHM1
dTMP kinase
Dehalococcoides
MSLFITFEGGEGCGKSTQSKALYRYLKKLGLGCVLTHEPGGTRSGDKITRLLKWSEEENISPLAELFLFNASRSILIDNVIKPALLDGNIVICDRYTDSTLAYQGYGRGLELDTVKCINSLASGGLVPDLTIWLDMDDKAALLRKGKLPPDRFESENNGFHQRVRDGFGVIAAAEPNRFLKLDASLSQSELTKCIKQRVNALLKLPQ
Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Q3Z8D9
Q867Z4
LOLA4_DROME
Longitudinals lacking protein, isoforms F/I/K/T
Sophophora
MDDDQQFCLRWNNHQSTLISVFDTLLENETLVDCTLAAEGKFLKAHKVVLSACSPYFATLLQEQYDKHPIFILKDVKYQELRAMMDYMYRGEVNISQDQLAALLKAAESLQIKGLSDNRTGGGVAPKPESSGHHRGGKLSGAYTLEQTKRARLATGGAMDTSGDVSGSREGSSSPSRRRRKVRRRSMENDAHDNSNSSVLQAAASNQSILQQTGAGLAVSALVTTQLSSGPAAGTSSQASSTQQQQPLTSTNVTKKTESAKLTSSTAAPASGASASAAVQQAHLHQQQAQTTSDAINTENVQAQSQGGAQGVQGDDEDIDEGSAVGGPNSATGPNPASASASAVHAGVVVKQLASVVDKSSSNHKHKIKDNSVSSVGSEMVIEPKAEYDDDAHDENVEDLTLDEEDMTMEELDQTAGTSQGGEGSSQTYATWQHDRSQDELGLMAQDAQQRDPQASKQDKGEQTEGAQDEFELDDCLLESNDIVITQNKDGFVLHVKKLGNITAAKLEENQAVAQQQGQAAVTVTGPAGQPTPTITELLNAAAASHSEPKPTLTTLTSTPIKLPSSECELINIKKIIPATTTIATHHPHTSSTIIHPHHIIQHVSQEPHHQEHHQQHQTIHIEEVPQTSQQHHQQQHHHQLQTVQPTHTQVQSIITAHPGQTINLVGLRNVQLADSKPIASRIRYSRGKIIGPTVQNLQIVETHEPIQHQHHELSDGTKYEISEIDLNNPNASAAIISDLVKYAEIDDIELPDGTKIGIGFAPSEITEHMQTSGGETHITTIEHEPQELQTVHQHEQTQQTHHIHAGQLQTHHIQTVVQSSSGQQQHDQQQHHQHHSIELQDDDGVETITPEELGMHDSSKSYTILTTRPMKEESEHDPSGMTYELSLSDSSLGPCDDPESRYVCRHCGKKYRWKSTLRRHENVECGGKEPCHPCPYCSYKAKQRGNLGVHVRKHHPEKPQLESKRGRKV
Putative transcription factor required for axon growth and guidance in the central and peripheral nervous systems. Repels CNS axons away from the midline by promoting the expression of the midline repellent sli and its receptor robo.
Q867Z4
Q15WH0
HSCA_PSEA6
Chaperone protein HscA homolog
Pseudoalteromonas
MALLQIAEPGLSAAPHQRKLAVGIDLGTTNSLVATVRSGQAETLGDNNNQHLLPSVVSYTAEQVVVGEQAKHDASLDPANTIVSVKRFLGRSLNDIRRSYPDLPYDFDESNPNSPLLNVTGRQVNPVEVSSEILTTLRLRAEQSLGEELSGAVVTVPAYFDDAQRQGTKDAAQLAGLKVLRLLNEPTAAAIAYGLDTAQEGVIAVYDLGGGTFDISILRLSKGVFEVLATGGDSALGGDDFDHMIVKHFRQQLGLEGALSKRLHRVLLDKAKFAKESLSDNDTVTVDFADDEQKLLSLSISRETFQGLIADLTKSTLRACRRALKDAELEKDEVLEVVMVGGSTRVPYVREQVGEFFGRTPLTSIDPDKVVAIGASIQADILVGNKPDGEMLLLDVLPLSLGLETMGGLVEKVIHRNTTIPVAKAQEFTTFKDGQTAMMIHVLQGERELVDDCRSLAKFTLHGIPPMAAGAAHIRVTFQVDADGLLNVMAMEKSSGVQAEIQVKPSYGLDESQISDMLKASMQNATGDMQARMLKEQQVEAARVHEALQAALNADGAELLSAAEIGTIQASLEVLDIAGKNDDIDAIKQAISAADAASQIFAEKRMDHSIKKALAGHTVDSI
Chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB.
Q15WH0
P0C1B8
IKIT_PARTR
Ikitoxin
Parabuthus
ADVPGNYPLDKDGNTYKCFLLGENEECLNVCKLHGVQYGYCYASKCWCEYLEDDKDSV
Beta toxins 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. Does not produce effect when administered to blowfly and cabbage looper larvae. In mice, does not produce convulsions, tremors, increased ventilation nor death.
P0C1B8
Q47UT5
TRHO_COLP3
tRNA hydroxylation protein O
Colwellia
MSSSEKQLSTPATIQTASTITICALYKFVRLDAYEALREPLSNKMASVDVKGTLLLAAEGINGTIAGPQTGIDTVLAFLGEQPGLDNISHKESYSEENPFHRTKVKLKKEIVTMGIEGIDPNQVVGTYVKPKDWNALISDPEVVLVDTRNDYEIEIGTFKNAINPNTETFREFPDYVAKNLDKNKHKKVAMYCTGGIRCEKSTAYLKEQGFEEVYHLEGGILKYLEEVPSTETMWEGECFVFDGRVAVNHELEQGQYDQCFACRFPLTDVEKESEHYVKGVSCHRCHDKVSEQQRSRYAERQRQISLAEERGESHIGGDIQNIIEERRQEKNDKKAKQANK
Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs.
Q47UT5
B2SDI5
KATG_FRATM
Peroxidase/catalase
Francisella
MLKKIVTALGMSGMLLASSNAIAEDTTTKNDNLSPQSVDLSPLRNLNKLDSPMDKDYNYHQAFKKLDTEQLKKDMQDLLTQSQDWWPADFGNYGPFFIRLSWHDAGTYRIYDGRGGANRGQQRFSPLNSWPDNVNLDKARQLLWPIKQKYGDAVSWSDLIVLAGTVSLESMGMKPIGFAFGREDDWQGDDTNWGLSPEEIMSSNVRDGKLAPAYAATQMGLIYVNPEGPDGKPDIKGAASEIRQAFRAMGMTDKETVALIAGGHTFGKTHGAVPEDKVKQAIGPAPDKAPIEQQGLGWHNSYGTGNGDDTMGSGLEGSWTSTPTFWNHDFLHNLYNLDWKKTLSPAGAHQWTPTNAKPENMVPDAHKPGVKHKPIMFTTDLALKEDDGFNKYTQEFYNNPEEFKEEFAKAWFKLTHRDMGPKSRYIGPWIPEQNFIWQDPVPAADYKQVSTQDIAQLEQDIINSGLTNQQLIKTAWDSASTYRKTDYRGGSNGARIALAPEKDWQMNEPAKLEVVLTKLKEIQTNFNNSKADGTKVSLADLIVLGGNVGVEQAAKQAGYNIQMPFVPGRTDATQAQTDIESFNYLKTKSDGFINYTDGSVSADKLPQTLVEKASMLDLNIPEMTVLVGGMRALDVNYDNSQKGVLTTTPGQLNNSFFVNLLDMSTQWKKSDKKDGEYIGIDRKTGKQKWTASPVDLIFGSNSELKAVAQVYAENGNEQKFVNDFAKAWHKVMMLGRFDVQQ
Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity.
B2SDI5
O29238
RGYR_ARCFU
Topoisomerase
Archaeoglobus
MIPVVYSNLCPVCGGDLESKEIEKHVCFRKKRSLCLFPEDFLLKEFVEFFRKCVGEPRAIQKMWAKRILRKESFAATAPTGVGKTSFGLAMSLFLALKGKRCYVIFPTSLLVIQAAETIRKYAEKAGVGTENLIGYYHGRIPKREKENFMQNLRNFKIVITTTQFLSKHYRELGHFDFIFVDDVDAILKASKNVDKLLHLLGFHYDLKTKSWVGEARGCLMVSTATAKKGKKAELFRQLLNFDIGSSRITVRNVEDVAVNDESISTLSSILEKLGTGGIIYARTGEEAEEIYESLKNKFRIGIVTATKKGDYEKFVEGEIDHLIGTAHYYGTLVRGLDLPERIRFAVFVGCPSFRVTIEDIDSLSPQMVKLLAYLYRNVDEIERLLPAVERHIDEVREILKKVMGKERPQAKDVVVREGEVIFPDLRTYIQGSGRTSRLFAGGLTKGASFLLEDDSELLSAFIERAKLYDIEFKSIDEVDFEKLSRELDESRDRYRRRQEFDLIKPALFIVESPTKARQISRFFGKPSVKVLDGAVVYEIPMQKYVLMVTASIGHVVDLITNRGFHGVLVNGRFVPVYASIKRCRDCGYQFTEDRESCPKCGSENVDNSRSRIEALRKLAHDAEFVIVGTDPDTEGEKIAWDLKNLLSGCGAVKRAEFHEVTRRAILEALESLRDVDENLVKAQVVRRIEDRWIGFVLSQKLWERFNNRNLSAGRAQTPVLGWIIDRFQESRERRKIAIVRDFDLVLEHDEEEFDLTIKLVEEREELRTPLPPYTTETMLSDANRILKFSVKQTMQIAQELFENGLITYHRTDSTRVSDVGQRIAKEYLGDDFVGREWGESGAHECIRPTRPLTRDDVQRLIQEGVLVVEGLRWEHFALYDLIFRRFMASQCRPFKVVVKKYSIEFDGKTAEEERIVRAEGRAYELYRAVWVKNELPTGTFRVKAEVKSVPKVLPFTQSEIIQMMKERGIGRPSTYATIVDRLFMRNYVVEKYGRMIPTKLGIDVFRFLVRRYAKFVSEDRTRDLESRMDAIERGELDYLKALEDLYAEIKSID
Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. It cleaves transiently a single DNA strand and remains covalently bound to the 5' DNA end through a tyrosine residue. May be involved in rewinding the DNA strands in the regions of the chromosome that have opened up to allow transcription or replication.
O29238
Q9CMC7
MIAA_PASMU
Isopentenyl-diphosphate:tRNA isopentenyltransferase
Pasteurella
MPLTTPTAIFLMGPTASGKTDLAIQLRQTLPVEVISVDSALIYRGMDIGTAKPSAEELALAPHRLIDICDPAESYSAANFRQDALREMADIIAAGKIPLLVGGTMLYYKALLEGLSPLPSADEKVRSEIEEKAQLQGWAALHQELAKIDPLAAQRINPNDSQRINRALEVFYLTGKSLSELSQQKGDSLPYQILQFAIAPKDRSILHDRIALRFQKMIEQGFQQEVEKLYQREDLHLDLPAMRCVGYRQMWEYLRGDYDHDEMIFRGICATRQLAKRQITWLRGWKYPIEWLDSLAIESAKQTIIHAVTKISHSNS
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).
Q9CMC7
B6JBS5
FBID_AFIC5
3-phospho-D-glycerate guanylyltransferase
Afipia
MARSDAFVILPVKAFVGAKSRLAPLLSVGERTMLARVMLNDVLDAAIAAVGPQSVSVVTSADDVADHARRAGVGVIDDEGARGTNAAVKVGFARIAARRRGAVLTLSSDIPGLIPSDIVALISAAERSRVALAPACDDGGTNALACDVVGRIPLCFGPGSFARHIAAANAADVRPAVLLNQRLGLDLDEPHHLMQFLDRGTSTQTDAYLRVLRLKERKGHSFVVAAQQATGARRLAV
Guanylyltransferase that catalyzes the activation of (2R)-3-phosphoglycerate (3PG) as 3-[(R)-glyceryl]-diphospho-5'-guanosine, via the condensation of 3PG with GTP. It is involved in the biosynthesis of a derivative of the hydride carrier cofactor coenzyme F420, 3PG-F420.
B6JBS5
P15935
BCNA_CLOPF
Bacteriocin UviA
Clostridium
MSELYKNIVLCQNGDKKAIEYIINRFEILINKYKMSFLKEIHFNSYDIEDNKQDLIVSLINIVNKIPIDNPQFENEGCLVNYIYKSILNSRKDMYINKNIKRYFIESQSLSSMVEFKDKPLVKYIESNIEIEDMLKCLTEKEQKVIKYKFLNDKSEVEIAEIMGTSRQWINRIKNTALKKLKENI
May have a role in bacteriocin secretion or immunity.
P15935
B7LF12
LPLT_ECO55
Lysophospholipid transporter LplT
Escherichia
MSESVHTNTSLWSKGMKAVIVAQFLSAFGDNALLFATLALLKAQFYPEWSQPILQMVFVGAYILFAPFVGQVADSFAKGRVMMFANGLKLLGAASICFGINPFLGYTLVGVGAAAYSPAKYGILGELTTGSKLVKANGLMEASTIAAILLGSVAGGVLADWHVLVALAACALAYGGAVVANIYIPKLAAARPGQSWNLINMTRSFLNACTSLWRNGETRFSLVGTSLFWGAGVTLRFLLVLWVPVALGITDNATPTYLNAMVAIGIVVGAGAAAKLVTLETVSRCMPAGILIGVVVLIFSLQHELLPAYALLMLIGVMGGFFVVPLNALLQERGKKSVGAGNAIAVQNLGENSAMLLMLGIYSLAVMIGIPVVPIGIGFGALFALAITALWIWQRRH
Catalyzes the facilitated diffusion of 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) into the cell.
B7LF12
Q6G070
PSD_BARQU
Phosphatidylserine decarboxylase beta chain
Bartonella
MSILQSVHNSFTPVHKEGYPFIIAFFVLSLIFGWVWSPLFWCGLVLTVWCIYFFRDPNRVIPVNSNWIISPADGRISFVEPCIPPEELGLGNEEMIRISVFMDIFSCHINRIPISGKVESIVYRPGQFANAELDKASQFNERNGMVIDSKHGKIGVVQIAGAIARRIVCWSKENDSVITGQRFGLIRFGSRLDIYIPTEVKLRVAVGQTAIAGETVLGSFDDKSSATIDFRFD
Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
Q6G070
A7GX26
SYI_CAMC5
Isoleucyl-tRNA synthetase
Campylobacter
MDYKDTLLLPATDFPMRGDLPKNEPIRLKSWYEERKIYEKMKSKRAGAAKNFAIHDGPPYANGHLHIGHALNKILKDIITKTHYFFGENVRYVPGWDCHGLPIEQQVEVKLGDKKKELSKTQIRELCRAHAREFIDIQREEFKALGIIGDFENPYMTMKFEFEADIYRSLCEIAKKGLLIERSKPVYWSWAAKSALAEAEVEYEDKEDYSIYVAFELDSDALAKLGVKLAKAVIWTTTPWTLPANQAISLKPDEIYVLTSENLIFAKPLLESLVNLGLTKGEILKEFVSNELENTHAINPLNDRKSRFLLGDHVLMDGGTGLVHTAPGHGEDDYYICLRYGFKEILMPVDDGGLYDETLKAHSLLRADVVDSFVGMHIFKANEKIIELLGENLLHVSKFTHSYPFCWRTHKPVIYRATKQWFIAMDEPKLGGKTLREVARGELENVKFYPSVGIKRIGSMIENRPDWCISRQRDWGVPIAFFRRKDTKEPIFEPKILEHIAKIFEQKGADAWWDMSVEELLAPDSGFEAKNLEKVMDILDVWFDSGSTWHAVLNSKNYDAGSYPADMYLEGSDQHRGWFQSSLLVSTAINSHAPYKNILTHGFTVDENGQKMSKSKGNVVAPQDVAKSYGVEILRLWVGLSDYSSDLKISENILKQVSEQYRKIRNTIRFLLANVNDLETIGTDFGFLDQWILGRAKRVFDEASKCFRAYDFSKGFNLLLNFLSADLSGIYLDICKDRLYCDAKDSPRRRSAQSAMAIITKSLLPLIAPTLTYTVDEVMDYAPAIIKGDAKDAFDLVYEPINFDFDVEDELLFASREKFFELIDALKKDKKIKSTLELVLETTSSKILDYDSVERADIYMVSDVHRYSGNEGLGEFEIDGEKFKIVLSDASKCPRCWKFNAIIDGSTCERCSEVLNSVC
Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile).
A7GX26
Q3AUJ5
RL11_SYNS9
50S ribosomal protein L11
unclassified Synechococcus
MAKKVVAVIKLALQAGKANPAPPVGPALGQHGVNIMMFCKEYNARTQDKAGLVIPVEISVFEDRSFTFITKTPPASVLITKAAGIEKGSGDSAKGSVGSISRAQLEEIAKTKLPDLNCSSVDSAMRIIEGTARNMGVAVSD
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
Q3AUJ5
A9M642
PDXJ_BRUC2
Pyridoxine 5'-phosphate synthase
Brucella
MPAKLSVNLNAIAMLRNRRDLPWPSVTGLGRAALAAGAAGLTVHPRPDQRHIRFSDLGDIRALIDDEYPQAEFNIEGFPSEAFLDLVEKHEPEQVTLVPDDPMQATSDHGWDFMSKADFLAPIVARLKGRGMRVSLFADPDSLGYERAKAIGADHVELYTGPYGATHDDPAAAARELDRLEKAARAATALGLAVNAGHDLTVDNLPALVKRIPQLAEVSIGHGLTADALMYGIPVTVSRYITALAG
Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
A9M642
P25019
6B2_AGRVI
Protein 6b
Agrobacterium
MTVANWQVRDFTRILNAGELQGRLEQARTDFGALLAEIVYFHPPGATPEEGDDEYILTGQGLVYVYLSEQTARQCALNRLLPSNSSNFGTVVTAIPPWLMDTQTLNLTLQERCDQGGIVNYYHGSRTNEFFLAIMLSNCFVRFGTDEINGASYGFYARRGNYTEEGEDDDNEIGDEGEAGGAEIRDYQFGDLVNYPIVALGSSRLSA
Involved in tumor formation and increases auxin and cytokinin effects in host plants.
P25019
A1SE40
NUON_NOCSJ
NDH-1 subunit N
Nocardioides
MDFIKPTIEYGDVWPLLVVFGVAAVGVLVEGFVPRAQRYLVQAALAIAGVVVALVGTILVARDLDVLGDGAARGAIDVEGTIAVDGPALFIWGMLLVFALGGALLFAERRLEGGVSAFAGQAAALPGTEAERQASTRGLEHTEVYPLMMFALGGMMLFAAANDLLTLFVALEVLSLPLYLLSGLARRRRLLSQEAALKYFMLGAFSSGFFLYGAALVYGFSGSMGFAEINEAVRDDVGNQTLLLIGIGMLSVGLLFKVGAVPFHSWTPDVYQGAPTAVTAFMAAGTKIAAFGAMLRLFYVAFGSDRWSWQPMLWIIAILTMLVGALIAIVQTDMKRMLAYSSVAHTGFLLTGVLGVQQASELADGEVTSLQAVLFYLVTYGFAVVGAFAVVTLVRDAGGEAGQFVRWRGIGRRSPLVAGVFAFFLLSMAGIPLTAGFVGKWAVFTVALAAGAWPVVIAAVLCSIIAVFFYVRVILLMFFEDDDVSAQGEVASVTKPSVLTSATIFVGVAATLVLGVVPGPVLDLAANAGQFVR
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
A1SE40
B7IUJ1
TRMFO_BACC2
Folate-dependent tRNA(M-5-U54)-methyltransferase
Bacillus cereus group
MTTQVVNVIGAGLAGSEAAYQIAKRGVQVRLYEMRPVRQTPAHHTDKFAELVCSNSLRANTLTNAVGVIKEEMRLMDSVIIRAADECSVPAGGALAVDRHEFAAKVTEYVKNHPNVTVVNEELTEIPEGPTIIATGPLTSPDLAAQLKELTGEDYFYFYDAAAPIVEKDSIDMNKVYLKSRYDKGEAAYLNCPMTEEEFDRFYEALIAAETVPLKEFEKEIFFEGCMPVEVMASRGRQTLVFGPMKPVGLEDPKTGKTPYAVVQLRQDDAAGTLYNIVGFQTHLKWGPQKEVLQLIPGLENAEIVRYGVMHRNTFINSPNLLRPTYQYKQRDDLFFAGQMTGVEGYVESAASGLLAGINAARLVQGEEPVVLPSVTAMGSMANYITATNAKNFQPMNANFGLFAPLEKKIKKKAERNEAYATRALETIQNFVNI
Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs.
B7IUJ1
P28173
PUR1_CHICK
Glutamine phosphoribosylpyrophosphate amidotransferase
Gallus
MELEELGIREECGVFGCIAAGVWPTELDVPHVITLGLVGLQHRGQESAGIVTSDGESSQAFKVHKGMGLINHVFNADSLKKLYVSNLGIGHTRYSTSGISELQNCQPFVVETLHGKIAVAHNGELTNAVRLRRKLMRHGVGLSTSSDSELITQLLAFTPPLENDDTADWVARIKNLMNETPTSYSLLIMHKDIIYAVRDPYGNRPLCIGRLIPVGDINGKGKDNSETEGWVVSSESCSFLSIGAEYYREVLPGEIVKISRYDVQTLDVVPRPEGDPSAFCIFEYVYFARPDSIFEGQMVYSVRRRCGQQLAIEAPVEADLVSTVPESATPAALGYAQKCGLPYVEVLCKNRYVGRTFIQPNMRLRQLGVAKKFGVLSDNFKGKRVVIIDDSIVRGNTISPIIKLLRESGAKEVHIRVASPPIRFPCYMGINIPTKEELIANRPEFHDLANYIGADSVVYLSVEGLVSSVQESIKARKENENSLKTQKSRVGKIGHCTACLTGDYPVELEW
Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine.
P28173
P46011
NRL4_ARATH
Nitrilase 4
Arabidopsis
MSMQQETSHMTAAPQTNGHQIFPEIDMSAGDSSSIVRATVVQASTVFYDTPATLDKAERLLSEAAENGSQLVVFPEAFIGGYPRGSTFELAIGSRTAKGRDDFRKYHASAIDVPGPEVERLALMAKKYKVYLVMGVIEREGYTLYCTVLFFDSQGLFLGKHRKLMPTALERCIWGFGDGSTIPVFDTPIGKIGAAICWENRMPSLRTAMYAKGIEIYCAPTADSRETWLASMTHIALEGGCFVLSANQFCRRKDYPSPPEYMFSGSEESLTPDSVVCAGGSSIISPLGIVLAGPNYRGEALITADLDLGDIARAKFDFDVVGHYSRPEVFSLNIREHPRKAVSFKTSKVMEDESV
Highly specific for beta-cyano-L-alanine (Ala(CN)). Low activity with 3-phenylpropionitrile (PPN) or allylcyanide and no activity with indole-3-acetonitrile. Not associated with auxin production but may be involved in cyanide detoxification.
P46011
Q3ICT8
HMUV_PSET1
Hemin import ATP-binding protein HmuV
Pseudoalteromonas
MLCANNVSAQIGQKKLLKHINFYVKPNELVVIIGPNGAGKSSLLKALCGDIKINNGDITLNDRLLSDYSIASLATLRAVLTQNYELDFPFSVAEVVDMAHFAHQADYSKQQLMHFSEQVMQALSVTHLKTHTFTQLSGGEKQRVQLARVLCQIQPSLVANKTPYLLIDEPTSSLDIFHQYDVMAQAKSIASQGAGVVAVIHDLSLAASFADRIYMLNNGEVAACGIPKEVLTPALLKRVYNINARLENNTSEAMPHIQMCY
Part of the ABC transporter complex HmuTUV involved in hemin import. Responsible for energy coupling to the transport system.
Q3ICT8
P18649
APOE_CANLF
Apolipoprotein E
Canis
MKVLWAALVVTLLAGCWADVQPEPELERELEPKVQQELEPEAGWQTGQPWEAALARFWDYLRWVQTLSDQVQEGVLNTQVTQELTALMDETMKEVKAYKAELDEQLGPMTSETQARVAKELQAAQARLRSDMEDVRNRLTQYRGELQAMLGQSSEELRARFASHMRKLRKRVLRDAEDLQRRLAVYKAGVREGAERSVSSIRERLWPLLEQARERNAKVGALATQPLLERADALGQQLRGQLEEMSSRARGHLEEMREQIQEVRVKMEEQADQIRQKAEAFQARLKSWFEPLLEDMQRQWDGLVEKVQAAVATIPTSKPVEEP
APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apoliproteins are amphipathic molecules that interact both with lipids of the lipoprotein particle core and the aqueous environment of the plasma. As such, APOE associates with chylomicrons, chylomicron remnants, very low density lipoproteins (VLDL) and intermediate density lipoproteins (IDL) but shows a preferential binding to high-density lipoproteins (HDL). It also binds a wide range of cellular receptors including the LDL receptor/LDLR and the very low-density lipoprotein receptor/VLDLR that mediate the cellular uptake of the APOE-containing lipoprotein particles. Finally, APOE has also a heparin-binding activity and binds heparan-sulfate proteoglycans on the surface of cells, a property that supports the capture and the receptor-mediated uptake of APOE-containing lipoproteins by cells.
P18649
Q2SBR1
LPXB_HAHCH
Lipid-A-disaccharide synthase
Hahella
MTPISERPIRIGIVAGEASGDLLGAGLMQEIKALYPQATFEGIGGERMLKEGFNTFFQMERLSIMGLVEVLGRLPELLAMRRRIVDHFTATPPDLFLGIDSPDFTIGIELKLRQAGIKTAHYVSPSVWAWRQNRVFKIAKAVDLMLTLLPFEARFYREHNVPVKFVGHPLAEIIPLHPDKVAMRHELGIDASGEVIAVLPGSRGGEVSRLGPTFIETIAWLHQRRPDVRFVIPAANQARKTQIEQQLQSHGGRLPVTLIDQHSRECMMAADAILLASGTATLEAMLVKRPMVVAYKLATLSYWIMRRLLKAKYISLPNLLADKALVPELIQNDATPAKLGEALLKELNVERRRSLEDEFEGLHKLIRQNASVAAAQAVAELIEKGRVATHDAREGH
Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Q2SBR1
Q2G662
ENO_NOVAD
2-phosphoglycerate dehydratase
Novosphingobium
MTAIIDIHAREILDSRGNPTVEVDVLLEDGSFGRAAVPSGASTGAHEAVELRDGDKARYLGKGVTKAVTAVNSDIAECILGLDAEDQRDIDLAMIELDGTENKSRLGANAILGTSLAVAKAAADARGLPLYSYVGGVSAHVLPVPMMNIINGGEHADNPIDFQEFMIMPVGAPSLAEAVRWGAEVFHTLKKGLHEKGLATAVGDEGGFAPNLASTRDALDFVMASIEKAGFKPGEDMMLALDCAATEFFKNGKYEISGEGLSLSPDAMADYLAALCDAYPIISIEDGMGEDDFEGWAALTAKVGKRVQLVGDDLFVTNPKRLEMGIGKGLANSLLVKVNQIGSLTETLEAVSIAQRNGYTAVMSHRSGETEDATIADLAVATNCGQIKTGSLARSDRLAKYNQLIRIEEELGVSARYAGKTAFGRLGA
Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
Q2G662
C6XAJ7
NUOK_METGS
NDH-1 subunit K
Methylovorus
MVGLSHYLILGSLLFAISVVGIFLNRKNVIVLLMAIELMLLAVNLNFIAFSHYLQDTAGQVFVFFILTVAAAESAIGLAILVVLFRNLKTINVDDINSLKG
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.
C6XAJ7
C5BQ65
RS19_TERTT
30S ribosomal protein S19
Teredinibacter
MPRSLKKGPFIDHHLLKKVEVAAEKNDRRPIKTWSRRSMILPEMVGLTIAVHNGRQHVPVLVSEEMVGHKLGEFAATRTYRGHVADKKAKR
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
C5BQ65
A9KKR4
PYRE_LACP7
Orotate phosphoribosyltransferase
Lachnospiraceae
MEQYKKEFIEFMVDCGVLKFGDFTTKSGRKTPFFVNTGFYRTGAQLRKLGEYYAKAIHDAYGLDFDVLFGPAYKGIPLSVATAMSISEHFDKDIKYCSNRKEVKDHGDTGILLGSPISDGDKVVIIEDVTTAGTSIGETMPILSAQGNVDVVGLVVSVDRMERGQGKKSALKEIEENYGIETTAIVTMKEVVEHLYGKPYNGKVVIDDQLKQAIDAYYEQYGVEA
Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
A9KKR4
A6U3J2
ATPF_STAA2
F-type ATPase subunit b
Staphylococcus
MTETANLFVLGAAGGVEWGTVIVQVLTFIVLLALLKKFAWGPLKDVMDKRERDINRDIDDAEQAKLNAQKLEEENKQKLKETQEEVQKILEDAKVQARQQQEQIIHEANVRANGMIETAQSEINSQKERAIADINNQVSELSVLIASKVLRKEISEQDQKALVDKYLKEAGDK
Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
A6U3J2
Q4ZQH9
ASTB_PSEU2
N-succinylarginine dihydrolase
Pseudomonas syringae
MKSCEVNFDGLVGPTHNYGGLSYGNVASQSNSQQSANPREAALQGLAKMKALMDLGFTQGVLAPQERPDVSGLRRLGFTGSDEQVIEKAARQDMPLLVASCSASSMWVANAATVSPSADTADGRVHFTAANLNCKYHRSIEHPTTTRVLGAMFADAKHFAHHPALPAVAQFGDEGAANHTRFCRDYGEAGVEFFVFGRSAFDTRYPAPQKYPARQTLEASRAVARLHGLSEAGVVYSQQNPAVIDQGVFHNDVIAVGNGEVLFYHQDAFLNTDPMLNELRDKLGRVGGQLRAICVPRAEVSVQDAVRSYLFNSQLLSRPDGSMLLIVPQECQANASVWAYLQRLIADDSPVAEVKVFDLKQSMQNGGGPACLRLRVALNDTELAAVNPGVIMTAPLYETLTQWVDRHYRDRMSESDLADPRLLSECRTALDELTQILKLGAVYPFQLN
Catalyzes the hydrolysis of N(2)-succinylarginine into N(2)-succinylornithine, ammonia and CO(2).
Q4ZQH9
B9WFW5
SLX4_CANDC
Structure-specific endonuclease subunit SLX4
Candida
MATETGDDDGGIYFHSTQIQSIHESLEQEKSQRLYLQASIKKLESFKHVSDESLNNLNPSPVSVVQIKKKAATRKRKLSARKPNLKKPKSSSEVVRQAFEKDKFAYFTNNQARIDEFLTNGSVSTENSTSNQGSLISSDEWNYIKQTYLQQQGESKTTLKGIRNKIKQSKNSGIGMWEITASNPDISLNDEDIQYLHDLDEQQMMSDGNSFTDDDIDPTQDDGLVLTLSQNCSSQHDICHHEKDHQEHILINSSIGEAVQHDRNLESRSQKYSDNGNTIPDQNSAIRTGEMESTDAHEVQEIFSTPSYVPSNQLNTDKDSSQESGSSIIMLAENIVSTQPDVIESISDSESEIEIIEKPRLQVLQSVYENDISTNQTRHESAILKYSENSKQSEHQDYESEVVESDSTPIITPNVTPKKKAHISPVNETHGIMNESPVPLASRNTPDRITNIVGRIPSSPSPIKLVLESPLKKQRKIEFSDTESIYSTAVSQFGTPKQTTSSPVEVLTSKVGSPQLGICSDSETISVVSSMAHKKSHAAKKLRTTTLEVSAALRVKTYTDPENNITVKKLGEEKKREFIDLDNEIPDSENSDDDTGFSIIEITRQVVERKEHNNDDYSEEQSTDLFQIGLKDKRDIANTSHLQVPSSLVMQLGNTGNTFLDSSLVEEDDEIAKLTATELRERFKDWGLKPVQGKDKMLEILQGISDFISPESLLALKGDDLQQRVFDKLELLIKQDQFWYDRILTFEPIRLEEMRQWLNSHNHYLELDMLRLYCDRNCITTTNT
Regulatory subunit of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA.
B9WFW5
P57730
CAR18_HUMAN
Caspase-1 inhibitor Iceberg
Homo
MADQLLRKKRRIFIHSVGAGTINALLDCLLEDEVISQEDMNKVRDENDTVMDKARVLIDLVTGKGPKSCCKFIKHLCEEDPQLASKMGLH
Inhibits generation of IL-1-beta by interacting with caspase-1 and preventing its association with RIP2. Down-regulates the release of IL1B.
P57730
P51782
LYSC_TRIVU
1,4-beta-N-acetylmuramidase C
Trichosurus
MKVLLLLGFIFCSMAAHGKRMERCEFARRIKQLHLDGYHQISLANWVCLAQWESGFDTKATNYNPGDQSTDYGILQINSHYWCDDGKTPHAANECKVRCSELQEDDLVKAVNCAKKIVDQQGIRAWVAWRNKCEGKDLSKYLEGCHL
Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents.
P51782
Q8FHB1
FOLM_ECOL6
Dihydrofolate reductase
Escherichia
MGKTQSLPILITGGGRRIGLALAWHFINQKQPVIVSYRTHYPAIDGLIKAGAQCIQADFSTNDGVMAFADEVLKSTHGLRAILHNASAWMAEKPGAPLTDVLACMMQIHVNTPYLLNHALERLLRGHGHAASDIIHFTDYVVERGSDKHIAYAASKAALDNMTRSFARKLAPEVKVNSIAPSLILFNEHDDAEYRQQALNKSLMKTAPGEKEVIDLVDYLLTSCFVTGRSLPLDGGRHLR
Catalyzes the reduction of dihydromonapterin to tetrahydromonapterin. Also has lower activity with dihydrofolate.
Q8FHB1
Q67NL0
MUTL_SYMTH
DNA mismatch repair protein MutL
Symbiobacterium
MARIRLLDERTANQIAAGEVVERPASVVKELVENALDAQAKRIVVEVSGGGRELVRVTDDGIGMVPEDARLALQRHATSKIRTAEDLNAITTLGFRGEALPSIAAVSQFELITRPHDQLAGYRILAEGGQIVAEGEHGCPAGTRVTVRDLFFNVPARLKYLKTNATELAQIGDILTRLALANPEVAFRFQSGQAQVFATPGTGDLTAAVAALLGREMAKELLPVDYRNDAARVHGFVGRPTIARAGRSHQYFFVNRRAVRTIAARYALEEAYAHLLPNGRYPVCILFIEVEPHEVDVNVHPTKAEVRFQRDREVRAAVYQAARHALGAALLIPGTEVTADGEVRVPDRAEEKAALQRGWVPPGAGRPGEGGGRAAPPPWRVSAGGPGGQTTAREPVQAYLPAGGLQAALAQRAAEEAAAAVPAVDLAEATLVPRSAEPGELIRALRPLGQVHRSYIACDGPEGLYLIDQHAAHERIFFERLYAAAQEQATAVQRLLFPLTLDLTPAQMAIWQENAAIFAESGFEAEPFGGNTLLIHGVPAGLGTDHVARLVCDFLDRLQEDQVAPGTPVTDRRRRVLAAMAACKAAIKARDPLQPEDIAALLSDLAACASPETCPHGRPTVICVSISELEKRFKR
This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex.
Q67NL0
P51165
AT1B1_ANGAN
Sodium/potassium-dependent ATPase subunit beta-1
Anguilla
MPAATKDSDGGWKKFLWNSEKKEFLGRTGGSWAKILLFYVIFYGCLAGIFIGTIQALLLTINDFKPVYQDRVAPPGLSHTPRSEKSEMSFKVGDPSTYQKYVKAMHDFLQAYNDSKQENMMKYEDCGDTPKSYINRGELDNNQGIKKACIFRRSWLDKCSGLEDPTFGFSEGKPCLIVKLNRIVNFRPRPPTSNDSIPEEAQSKVQPDVIPIYCTNKREEDAAKVREIKYYGIQEGFPLQYYPYYGKQLHPQYLQPLVAVHFTNLTMATELRIECRVYGQNIAYSDKDRYRGRFDVKFTINES
This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The beta subunit regulates, through assembly of alpha/beta heterodimers, the number of sodium pumps transported to the plasma membrane.
P51165
P9WFI8
Y293_MYCTO
Putative S-adenosyl-L-methionine-dependent methyltransferase MT0293
Mycobacterium tuberculosis complex
MRTEGDSWDITTSVGSTALFVATARALEAQKSDPLVVDPYAEAFCRAVGGSWADVLDGKLPDHKLKSTDFGEHFVNFQGARTKYFDEYFRRAAAAGARQVVILAAGLDSRAYRLPWPDGTTVFELDRPQVLDFKREVLASHGAQPRALRREIAVDLRDDWPQALRDSGFDAAAPSAWIAEGLLIYLPATAQERLFTGIDALAGRRSHVAVEDGAPMGPDEYAAKVEEERAAIAEGAEEHPFFQLVYNERCAPAAEWFGERGWTAVATLLNDYLEAVGRPVPGPESEAGPMFARNTLVSAARV
Exhibits S-adenosyl-L-methionine-dependent methyltransferase activity.
P9WFI8
Q0B092
WHIA_SYNWW
Probable cell division protein WhiA
Syntrophomonas
MSFSSDVRNELARIIPEKECCRKAELAALLAISGDLVVGEDGRRILKVQADNAATARKIITLLKENYQIPSTFKALEQKRFKRKRIYEVNVLLDGEDEALNKELEEILLLREKETTPVLNRSLLGRTCCKRAYLRGIFLSRGSINRPEGEYHLELVLNDSRMALAVQKMLDKFALEPGLVERKNYLVVYLKESEKIVDFLRVVEASRALLNFENVRIIKSVRNNVNRQVNCETANLSKTIDASLRQIELIKRLLEEQGLEILPGNLRDLAEMRMSYTDASLKELGDLLDPPLSKSGVAYRMRKLEESVKEILQED
Involved in cell division and chromosome segregation.
Q0B092
Q1LTI9
DXS_BAUCH
1-deoxyxylulose-5-phosphate synthase
Candidatus Baumannia
MSMQIKRYPTLDLADNPIKLRLLPKESLLTLCDELRQFLLTSVSGSSGHFASGLGTVELTVALHYVYNTPFDNVIWDVGHQAYPHKILTGRRECIATIRQRNGLHPFPWREESEYDILSVGHSSTSISAGLGMAVAATYEGIGRKTVCVIGDGAMTAGMAFEALNHAGDIKSDLLVILNDNKMSISRNVGALNNHLAQILSGKLYLRINESSKKALHGMPYLKELAKRTKEQIKNIIVPNCTLFEELGFNYIGPVDGHDVQGMVHILKNMRCMKGPQLLHIITQKGRGYAPAEKDPTTWHAVPKFDPAIGQLPYQNISNYPTYSDVFGDWLCNAATSNKKLIAITPAMREGSGMAKFANQFPQQYFDVAIAEQHAVTFAAGLAISGYKPVVAIYSTFLQRAYDQVIHDVAIQKLPVLFAIDRGGVVGADGQTHQGAFDLSYLRCVPNMVIMTPSDENECRLMLHTGYHYNNGPSAVRYPRGNGIGVEYSLLRILPLGKAIVCRQGTKIAILNFGTLLTQAKKVAKTFDATLVDMRFVKPLDIELINQLAISHQALVTLEENAVIGGAGSGVNEYLMRQRLLVPVLNIGLPDYFIPQGSQEEIRAELKLDSDGIMEQIKQWLAR
Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP).
Q1LTI9
Q7W5K6
AMPA_BORPA
Leucyl aminopeptidase
Bordetella
MEFSTQTTASLHQIKTAALAVGVFADGVLSAAAEVIDRASHGAVAAVVKSEFRGRTGGTLVLRSLAGVSAQRVVLVGLGKQAEYNARAHASAEQAFAAACVAAQVGEGVSTLAGVAIEGVPVRARARSAAIAAGAAAYHYDATFGKANRDARPRLKKIVQVVDRAASAQTQLGLREGAAIAHGMELTRTLGNLPGNVCTPAYLGNTAKKLAREFKSLKVEVLERKQVEALGMGSFLSVARGSEEPLRFIVLRHAGKPAKKDKAGPVVLVGKGITFDAGGISLKPAATMDEMKYDMCGAASVLGTFRALAELELPLDVVGLIAACENLPSGKANKPGDVVTSMSGQTIEILNTDAEGRLVLCDALTYAERFKPAAVIDIATLTGACVVALGNVNSGLFSKDDALADALLAASRQSLDPAWRLPLDDAYQDQLKSNFADIANIGGPPAGAVTAACFLSRFTKAYPWAHLDIAGTAWRGGKDKGATGRPVPLLMQYLLDQAG
Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
Q7W5K6
O93743
BACS_HALSD
Sensory rhodopsin
Halorubrum
MTGAVTSAYWLAAVAFLIGVGITAALYAKLEGSRARTRLAALAVIPGFAGLSYVGMALGIGTVTVNGAELVGLRYVDWVVTTPLLVGFIGYNAGASRRAIAGVMIADALMIVFGAAAVVSGGTLKWALFGVSALFHVSLFAYLYVIFPGGIPDDPMQRGLFSLLKNHVGLLWLAYPFVWLMGPAGIGFTGAVGAALTYAFLDVLAKVPYVYFFYARRQAFIDVTDSRAAAKGDGPAVGGEAPVATGDDAPTAAD
Involved in the control of phototaxis.
O93743
P32332
OAC1_YEAST
Mitochondrial carrier protein PMT
Saccharomyces
MSSDNSKQDKQIEKTAAQKISKFGSFVAGGLAACIAVTVTNPIELIKIRMQLQGEMSASAAKVYKNPIQGMAVIFKNEGIKGLQKGLNAAYIYQIGLNGSRLGFYEPIRSSLNQLFFPDQEPHKVQSVGVNVFSGAASGIIGAVIGSPLFLVKTRLQSYSEFIKIGEQTHYTGVWNGLVTIFKTEGVKGLFRGIDAAILRTGAGSSVQLPIYNTAKNILVKNDLMKDGPALHLTASTISGLGVAVVMNPWDVILTRIYNQKGDLYKGPIDCLVKTVRIEGVTALYKGFAAQVFRIAPHTIMCLTFMEQTMKLVYSIESRVLGHN
Transports oxaloacetate and sulfate.
P32332
O35949
ELOV3_MOUSE
Very long chain 3-oxoacyl-CoA synthase 3
Mus
MDTSMNFSRGLKMDLMQPYDFETFQDLRPFLEEYWVSSFLIVVVYLLLIVVGQTYMRTRKSFSLQRPLILWSFFLAIFSILGTLRMWKFMATVMFTVGLKQTVCFAIYTDDAVVRFWSFLFLLSKVVELGDTAFIILRKRPLIFVHWYHHSTVLLFTSFGYKNKVPSGGWFMTMNFGVHSVMYTYYTMKAAKLKHPNLLPMVITSLQILQMVLGTIFGILNYIWRQEKGCHTTTEHFFWSFMLYGTYFILFAHFFHRAYLRPKGKVASKSQ
Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme that exhibits activity toward saturated and unsaturated acyl-CoA substrates with higher activity toward C18 acyl-CoAs, especially C18:0 acyl-CoAs. May participate in the production of saturated and monounsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. Participates in the formation of certain VLCFA and triglycerides in certain cells of the hair follicles and the sebaceous glands, required for skin barrier function. Critical enzyme for lipid accumulation and metabolic activity in brown adipocytes during the early phase of the tissue recruitment. Plays a role in lipid storage and in resistance to diet-induced obesity.
O35949
A7ZCY8
YIDD_CAMC1
Putative membrane protein insertion efficiency factor
Campylobacter
MKKFAIKFIAFYQKYISILLPKSCRYYPTCSQYAIWEFQTNSFFSAFFATFMRILRCNQLFKGGINYPIIRKKFNSCFIFQKSDTKNVNFWFIPCQNSKFYVVKVLDKLKEKN
Could be involved in insertion of integral membrane proteins into the membrane.
A7ZCY8
O82056
CADH_SACOF
Probable cinnamyl alcohol dehydrogenase
Saccharum officinarum complex
MGSLASERKVVGWAARDATGHLAPYTYTLRSTGPEDVVVKVLYCGICHTDIHQAKNHLGASKYPMVPGHEVVGEVVEVGPEVTKYGVGDVVGVGVIVGCCRECKPCKANVEQYCNKKIWSYNDVYTDGRPTQGGFASTMVVDQKFVMKIPAGLAPEQAAPLLCAGVTVYSPLKAFGLTTPGLRGAILGLGGVGHMGVKVAKAMGHHVTVISSSSKKRAEAMDHLGADAYLVSSDAAAMAAAADSLDYIIDTVPVHHPLEPYLALLKLDGKHVLLGVIGEPLSFVSPMVMLGRKAITGSFIGSIDETAEVLQFCVDKGLTSQIEVVKMGYVNEALDRLERNDVRYRFVVDVAGSNVEEVAADAPSN
Involved in lignin biosynthesis. Catalyzes the final step specific for the production of lignin monomers. Catalyzes the NADPH-dependent reduction of coniferaldehyde, 5-hydroxyconiferaldehyde, sinapaldehyde, 4-coumaraldehyde and caffeyl aldehyde to their respective alcohols.
O82056
A3PCJ7
PROB_PROM0
Gamma-glutamyl kinase
Prochlorococcus
MKTWVIKIGTSILRGTEETSTEEVIENLSRSFTSFLSKGNKLILVTSGAVGLGCQKLNIKTRPNDLSTLQATAAVGQVNLMSLYDKVFNKLGLNIAQILITKADFNSRESFNNASKTLKRLIDLNVIPIVNENDTVANEELKYGDNDTLSALVALAINANKLILLTDIENLYSKDPRNNKDAQPIKEVHNSELKEIKDKNIQNSNNEWGTGGISTKLISAEIATKGGVEVQLVDGTNKKNLIEIFNDNKIGTLFYPVEKPIGNKKSWLSHAIQTVGKITLDDGASFAIKKKGASLLAVGVKNVEGNFTINQAVKIVNTNDKEVAKGLVSISSDKLRSILNNKENNNSSIIVVHRDVLALS
Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate.
A3PCJ7
Q6LR94
MATP_PHOPR
Macrodomain Ter protein
Photobacterium
MKYQQLENLEAGWKWTYLVKKWKEEEAITCHIDSSEAEAAIQSLLTIEHEPTKVIEWIDKHMSPALENKLKQAIRAKRKRHFNAEQVHTRKKSIDLDYRVWEKLAEKSQELGSTLSDTIEYLLSESNRTETVTKTVSDIRKDLSDLLD
Required for spatial organization of the terminus region of the chromosome (Ter macrodomain) during the cell cycle. Prevents early segregation of duplicated Ter macrodomains during cell division. Binds specifically to matS, which is a 13 bp signature motif repeated within the Ter macrodomain.
Q6LR94
Q057C7
RS11_BUCCC
30S ribosomal protein S11
Buchnera
MSKKKLNQPKKRIKRQILDGIAHIHASFNNTIVTITDRKGNTLGWATSGGSGFRGSRKSTPFAAQVAAEKCADRVKDYGIKNLEVMIKGPGPGRESTIRALNSSGFRITNIIDVTPIPHNGCRPSKKRRV
Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome.
Q057C7
B1KM68
LEXA_SHEWM
LexA repressor
Shewanella
MRPLTPRQAEILELIKCNIAETGMPPTRAEIAKRLGFKSANAAEEHLKALAKKGCIEIIPGTSRGIRLAQTEELEEQGLPLIGQVAAGEPILAQEHVEQHYQVDPNMFHPSADFLLRVRGDSMKDIGILEGDLLAVHKAEQARNGQVVVARVEDDVTVKRFEKKGSTVYLHAENEDYSPIVVDLTNQSLSIEGLAVGVIRNGDWQ
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
B1KM68
B7VGU7
TRPB_VIBA3
Tryptophan synthase beta chain
Vibrio
MAKLDAYFGEYGGQYVPQILVPALDQLEQAFIDAQADPEFRSEFMTLLQEYAGRPTALTLTRNLTKGTKTKLYLKREDLLHGGAHKTNQVLGQALLAKRMGKQEIIAETGAGQHGVATALACALLGLKCRVYMGAKDVERQSPNVFRMKLMGAEVIPVHSGSSTLKDACNEALRDWSATYEDAHYLLGTAAGPHPFPTIVRDFQRMIGEETKNQILAREGRLPDAVIACVGGGSNAIGMFADFIEEESVRLIGVEPAGKGIDTDQHGAPLKHGKTGIFFGMKAPLMQDENGQVEESYSVSAGLDFPSVGPQHAHLNAIGRAEYDNVTDDEALEAFQLIARKEGIIAALESSHALAHAVKMAHDDPEKEQLLVVNLSGRGDKDIFSVHDILKEKGAL
The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
B7VGU7
Q1GAX5
RF1_LACDA
Peptide chain release factor 1
Lactobacillus
MDNVMAQLESLEVRYEEIQEMMADPEVIADTKRYMEITKEEADMREVVQKFRKFKADKEEIAGNKEIIADGSDPELVEMAKMENSELEDEISQLEDEIKILMLPKDPNDDKDIIMEIRGAAGGDEASLFAGDLLRMYEKYAENQGWNVSIVDSEQTEVGGYKRAAIMITGNKVYSKLKYENGAHRVQRIPVTESAGRVHTSTATVAVMPEYEQVDIDLDPKEIRVDVYRSSGAGGQHINKTSSAVRMTHLPTGIVVAMQDQRSQQQNRAKAMEILKSRVYDYYESQNRDKYDAKRKNAVGTGDRSERIRTYNYPQNRVTDHRIGLTLNKLDRIMNGELDEVIDALTVYYQTKQLEELAENA
Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
Q1GAX5
Q9UMZ2
SYNRG_HUMAN
Gamma-synergin
Homo
MALRPGAGSGGGGAAGAGAGSAGGGGFMFPVAGGIRPPQAGLMPMQQQGFPMVSVMQPNMQGIMGMNYSSQMSQGPIAMQAGIPMGPMPAAGMPYLGQAPFLGMRPPGPQYTPDMQKQFAEEQQKRFEQQQKLLEEERKRRQFEEQKQKLRLLSSVKPKTGEKSRDDALEAIKGNLDGFSRDAKMHPTPASHPKKPGPSLEEKFLVSCDISTSGQEQIKLNTSEVGHKALGPGSSKKYPSLMASNGVAVDGCVSGTTTAEAENTSDQNLSIEESGVGVFPSQDPAQPRMPPWIYNESLVPDAYKKILETTMTPTGIDTAKLYPILMSSGLPRETLGQIWALANRTTPGKLTKEELYTVLAMIAVTQRGVPAMSPDALNQFPAAPIPTLSGFSMTLPTPVSQPTVIPSGPAGSMPLSLGQPVMGINLVGPVGGAAAQASSGFIPTYPANQVVKPEEDDFQDFQDASKSGSLDDSFSDFQELPASSKTSNSQHGNSAPSLLMPLPGTKALPSMDKYAVFKGIAADKSSENTVPPGDPGDKYSAFRELEQTAENKPLGESFAEFRSAGTDDGFTDFKTADSVSPLEPPTKDKTFPPSFPSGTIQQKQQTQVKNPLNLADLDMFSSVNCSSEKPLSFSAVFSTSKSVSTPQSTGSAATMTALAATKTSSLADDFGEFSLFGEYSGLAPVGEQDDFADFMAFSNSSISSEQKPDDKYDALKEEASPVPLTSNVGSTVKGGQNSTAASTKYDVFRQLSLEGSGLGVEDLKDNTPSGKSDDDFADFHSSKFSSINSDKSLGEKAVAFRHTKEDSASVKSLDLPSIGGSSVGKEDSEDALSVQFDMKLADVGGDLKHVMSDSSLDLPTVSGQHPPAADIEDLKYAAFGSYSSNFAVSTLTSYDWSDRDDATQGRKLSPFVLSAGSGSPSATSILQKKETSFGSSENITMTSLSKVTTFVSEDALPETTFPALASFKDTIPQTSEQKEYENRDYKDFTKQDLPTAERSQEATCPSPASSGASQETPNECSDDFGEFQSEKPKISKFDFLVATSQSKMKSSEEMIKSELATFDLSVQGSHKRSLSLGDKEISRSSPSPALEQPFRDRSNTLNEKPALPVIRDKYKDLTGEVEENERYAYEWQRCLGSALNVIKKANDTLNGISSSSVCTEVIQSAQGMEYLLGVVEVYRVTKRVELGIKATAVCSEKLQQLLKDIDKVWNNLIGFMSLATLTPDENSLDFSSCMLRPGIKNAQELACGVCLLNVDSRSRKEEKPAEEHPKKAFNSETDSFKLAYGGHQYHASCANFWINCVEPKPPGLVLPDLL
Plays a role in endocytosis and/or membrane trafficking at the trans-Golgi network (TGN) . May act by linking the adapter protein complex AP-1 to other proteins (Probable). Component of clathrin-coated vesicles . Component of the aftiphilin/p200/gamma-synergin complex, which plays roles in AP1G1/AP-1-mediated protein trafficking including the trafficking of transferrin from early to recycling endosomes, and the membrane trafficking of furin and the lysosomal enzyme cathepsin D between the trans-Golgi network (TGN) and endosomes .
Q9UMZ2
A8EVR4
HLDE_ALIB4
D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase
Aliarcobacter
MLSKKPNILVIGDLMIDHYLWGSCDRISPEAPVQVVNVKKESSVLGGAGNVINNLFTLGTTVDVISVIGDDNVANELKSLLEKIKISTSNLIVENNRKTSKKSRLIASQQQVLRYDMESIDDINEESHKKIISNLEKNIKKYSSIILSDYGKGVLTTKLTQDIINIANKNSVKVLVDPKGKDYSKYKGSYTLTPNKKEAQEATNIDIKDENSLINALKDLKEKCDLEVSLITLSEQGIAIFDENLTIKPTVAREVYDVTGAGDTVIASIAFALGNDLNINEAVSFANLAAGVVVGKLGSATTTLDEIYEYESSLHKSNSNSHIKTFEEIEKLAAKLHNLGKKIVFTNGCFDILHVGHVKYLEEARSYGDVLILGLNADSSVKKLKGESRPINNQDDRAYILASLESVDYVVIFEEETPYELIKLIKPHVLVKGGDYEGKDVVGQDIADELKLVKFVDGKSTTNTIKRIQENEKCNN
Catalyzes the ADP transfer from ATP to D-glycero-beta-D-manno-heptose 1-phosphate, yielding ADP-D-glycero-beta-D-manno-heptose.
A8EVR4
Q7LZS9
VM1A_DEIAC
Ac1-proteinase
Deinagkistrodon
STEFQRYMEIVIVVDHSMVKKYNGDSPKIKAWVYEMINTITEGYRDLYIDIILSGLEIWSEKDLINVEASAGNTLKSFGEWRAKDLIHRISHDNAQLLTATDFDGPTIGLAYVASMCEPKLSVGVIQDHSSVNRLVAITLAHEMAHNLGVRHDEKDCVGVVYLCIMRIPVVEDKRSYFSDCSYIQCREYISKENPPCILNKP
Snake venom metalloproteinase that impairs hemostasis in the envenomed animal.
Q7LZS9
B8CH52
SELU_SHEPW
tRNA 2-selenouridine synthase
Shewanella
MPVNMVSASEYRRILVSDHPIMDARAPVEFTKGAFPASRNHPLMEDEERRLVGTCYKQNGQQAAIDLGHSLVTGEIKQQRLDAWQRYFTKHPDAYLYCFRGGLRSKLTQQWLKEAGIDVPFIEGGYKAMRQFLIETIDNAASQNPMLILSGITGSGKTDFLLARNDSVDLEGIAHHRGSSFGRYHEPQPTQINFENALAVALLKHQDSQAKHLLLEDESFLIGRSALPQAFYKGMQQANVVVLEEPMEARLTRLLNEYVHKMHSGYIQRLGEEAGFAAFAEYLALSITGIKKRLGGKQHDEFQAIITNALNIQQSRGDTSAHIEWIELLLSKYYDPMYQYQIDKKAERILFKGDHLAMHQWLDAN
Involved in the post-transcriptional modification of the uridine at the wobble position (U34) of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Catalyzes the conversion of 2-thiouridine (S2U-RNA) to 2-selenouridine (Se2U-RNA). Acts in a two-step process involving geranylation of 2-thiouridine (S2U) to S-geranyl-2-thiouridine (geS2U) and subsequent selenation of the latter derivative to 2-selenouridine (Se2U) in the tRNA chain.
B8CH52
Q9M3A8
PP273_ARATH
Protein EMBRYO DEFECTIVE 1796
Arabidopsis
MSISKAAFLNHLQTLSRSYRHRVLPQPFLAVRYMSFATQEEAAAERRRRKRRLRMEPPVNSFNRSQQQQSQIPRPIQNPNIPKLPESVSALVGKRLDLHNHILKLIRENDLEEAALYTRHSVYSNCRPTIFTVNTVLAAQLRQAKYGALLQLHGFINQAGIAPNIITYNLIFQAYLDVRKPEIALEHYKLFIDNAPLNPSIATFRILVKGLVSNDNLEKAMEIKEDMAVKGFVVDPVVYSYLMMGCVKNSDADGVLKLYQELKEKLGGFVDDGVVYGQLMKGYFMKEMEKEAMECYEEAVGENSKVRMSAMAYNYVLEALSENGKFDEALKLFDAVKKEHNPPRHLAVNLGTFNVMVNGYCAGGKFEEAMEVFRQMGDFKCSPDTLSFNNLMNQLCDNELLAEAEKLYGEMEEKNVKPDEYTYGLLMDTCFKEGKIDEGAAYYKTMVESNLRPNLAVYNRLQDQLIKAGKLDDAKSFFDMMVSKLKMDDEAYKFIMRALSEAGRLDEMLKIVDEMLDDDTVRVSEELQEFVKEELRKGGREGDLEKLMEEKERLKAEAKAKELADAEEKKKAQSINIAALIPPKAVEEKKETAKLLWENEAGGVEEADVVEMAKGVEAGGSNGQDPPSC
May play a role in embryogenesis.
Q9M3A8
O27448
CFBA_METTH
Sirohydrochlorin nickelchelatase
Methanothermobacter
MDSNSNQKPKIGVLLVGHGSRLPYGEEVINGIADIYRQEADHPVAVGFMNMSRPSIPEAINELAAMGVEKIIVTPVFLAHGVHTKHDIPHILGLDNGAEGHHHHEHEHEHEEFEFDGEIVYTEPLGADPRIAEIIRDRVKSAI
Catalyzes the insertion of Co(2+) into sirohydrochlorin as part of the anaerobic pathway to cobalamin biosynthesis . Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation (Potential). Catalyzes the insertion of Ni(2+) into sirohydrochlorin to yield Ni-sirohydrochlorin (Potential).
O27448
Q2K0X8
THIM_RHIEC
4-methyl-5-beta-hydroxyethylthiazole kinase
Rhizobium
MLDAMREKPPLVHCITNYVAMNIAANVLLASGASPAMVHAPEEAGEFAGIASALTVNIGTLSTQWIDGMQAAAKAAASAGKPWVLDPVAHYATTFRRQAVADLLALKPTIIRGNASEIIALAGGESRGQGVDSRDPVEQAEDSARRLAERQQAIVAVTGAVDFVTDGERAVRIKGGSVLMPEVTALGCSLTCLIGAFAATAPEDLFGATVAALATFAVAGEDAALGAAGPGSFAWRFLDALAALDGEALDARARVSLA
Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ).
Q2K0X8
Q9FFH6
FLA13_ARATH
Fasciclin-like arabinogalactan protein 13
Arabidopsis
MATTPLLLLLLTAVFLSTEITAQRAAPAPGPAGPINITAILEKGGQFVTLIRLLNTTQIGNQINIQINSSSEGMTVLAPTDNAFQNLKPGTLNKLSPDDQVKLILYHVSPKFYTLEDLLSVSNPVRTQASGRDVGGVYGLNFTGQGNQVNVSTGVVETRLSTSLRQERPLAVYVVDMVLLPEEMFGERKISPMAPPPKSKSPDVSDDSESSKKAAAPSESEKSGSGEMNTGLGLGLGLVVLCLKFLL
May be a cell surface adhesion protein.
Q9FFH6
A3CQ45
SYS_STRSV
Seryl-tRNA(Ser/Sec) synthetase
Streptococcus
MLDLKRIRTDFDSVAEKLATRGVDAATLSQMKTIDKERRDLLVKVEELKAERNTVSAEIAQAKRNKENTDDKIAAMQKLSAEVKNLDASLAELDAKLTEFTTTLPNIPHDSVPVGADENENVEVRRWGTPHQFDFEAKAHWDLGEDLDILDWERGAKVTGARFLFYKGLGARLERAIYNFMLDEHGKEGYTEVITPYMVNHDSMFGTGQYPKFKEDTFELSDTNFVLIPTAEVPLTNYYRDEILDGKELPIYFTAMSPSFRSEAGSAGRDTRGLIRLHQFHKVEMVKFAKPEESYEELEKMTANAENILQKLNLPYRVVALCTGDMGFSAAKTYDLEVWIPAQNTYREISSCSNTEDFQARRAQIRYRDEADGKVKLLHTLNGSGLAVGRTVAAILENYQNEDGSVTIPEVLRPYMGGLEVIAPK
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).
A3CQ45
C5CNS8
SELO_VARPS
Protein adenylyltransferase SelO
Variovorax
MSLLAEDTAAADLGLRWKPGFRALGPAFLTELRPTPLPDPPYWVGHSEAAARLLGLPADWRQSEGTLAALTGNLPVAGTLPFATVYSGHQFGVWAGQLGDGRAIMLGETEGGLEVQLKGAGRTPYSRGADGRAVLRSSIREFLCSEAMHGLGIPTTRALCVTGSDARVYREMPETAAVVTRVAPSFIRFGHFEHFSASQRDAELRALADYVIDRYYPDCRSTSRFNGNAYAAFLEAVSERTAALLAQWQAVGFCHGVMNTDNMSILGLTIDYGPFQFLDGFDPRHICNHSDTSGRYAFNQQPNVAYWNLFCLAQALLPLIGDQEIAVAALESYKTVFPREFESRMRAKLGLAEPAEGDRALIEGVLKLMAAEKVDYTIFWRRLSQHMAGGNAEPVRDLFLDRAGFDAWLLSFSERHAQLPRAQAADLMLRSNPKYVLRNHLGQQAIEAASQKDFSAVATLLALLETPFEEHPGADAYAGFPPDWASTIEISCSS
Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation).
C5CNS8
D5AUZ7
CBIQ_RHOCB
Energy-coupling factor transporter transmembrane protein CbiQ
Rhodobacter
MSIASIDRVAAQGRWRNRPLAEKCLIGLGFLALAVTVPPFPGAVLVTVAILAFTFLGARVPLRFWAAVAVLPLGFLTTGAAVLLIQIGPDGIGLAPQGPAKAAALVMRASAATCCLLFLATTTPAADLLSGLRRWRVPAELIEIALLTYRFVFILAEEAAAMTTAQRARLGHATRRRWLRSTAQVIAALLPRALDRARRLETGLAARNWQGEMRVLSTRPAASPLVLGLILTLQAAILAAGVLL
Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import. The complex confers cobalt uptake upon expression in E.coli; can also transport nickel with a very low affinity.
D5AUZ7
D4B1G0
ADMB_ARTBC
Disintegrin and metalloproteinase domain-containing protein B
Trichophyton
MKAFSCLLSVIATAASLFQHVDARSHARDKLNNISRVERPVIHTPSRRVHAHSHFDLTFDLYPRSSRIKLQLEPNHDVLSHDARVTFLDTEGNVDRTERIERRDHSVFKGWAWTQAKSGAWERVGWARIILHRDGEDPLFEGVFTVMHDHHQVIAKSKYVRKRHQQDPPLDNTPGEYMLLFRGSDIAQTQSTGNVERSIMSSPSCDADTLAYDSNSNFMFPPLPEENNTSIWNYFMTSIGKRQMTDTGGVVPGSRDLKETIGSTSGCPNTRKVALIGVVADCTYTNTFASEMDARADIISVVNAASVVYEHSFNISLTLGEINILPKNCPATASSATPFNQQCDDRAGGGSFTLADRLNTFSAWRGKKTDDFAFWTLMTDCTTENQVGLAWAAQLCVKGVQGNPDSRNSSSQAVAGANVVSKTDNTWQVFAHEAGHIFGAVHDCDSMLCQNPANPDNSRCCPATASTCDARGRFMMNPTSGSQITDFSPCSIGQICSRMARRTILTSCLTTNRGVDTISGQQCGNGIVEDGEDCDCGDEESCKGNTCCDPKTCKYTSGSQCDDANEECCKGCKFASSSTICRTSSGPCDPEEKCSGNSGDCPHDIHSKDGETCGTDLQCASGQCTSRDLQCQMHLGNQVAGSRTVAFDSYGCEVACKDPDRPNVRYEGSLTFLDGTPCGGGGTCKNGQCSGSTFGNEVSDWVSRHKPIVIGVAVGAGCLLLLAIASCICGRSRRQRPRNRKMPPINMRPMAPVYNGWNGAPPNAQQSSPGGHPPYNNIPPPINAPPPAYPGHLPSTRYA
Probable zinc protease.
D4B1G0
Q92DS8
GLMS_LISIN
L-glutamine--D-fructose-6-phosphate amidotransferase
Listeria
MCGIVGYIGTNNAKGILLEGLEKLEYRGYDSAGIALQNKDLVTVVKEKGRIADLASLVPSDAFGTTGIGHTRWATHGKPNHENAHPHQSKSGRFTIVHNGVIENYTLLKEEYLKNHSFISDTDTEVIVQLIELFAEKLSTKEAFKKALSLLHGSYAICLIDQTDTETLYAAKNKSPLLIGKGENFNVIASDAMAVLKETDEFVEIMDKEIVIVTKDGFTLETLEGEEVSRASYTAELDASDIEKGTYPHYMLKEIDEQPAVTRKIIQAYQNEAGEINVDQTILDEILSSDRIHIVACGTSYHAGLVGKNLIEKMAKIPVEVHVSSEFGYNLPLMSKKPLFIFITQSGETADSRQCLVKVKELGYRTLTLTNVPGSTLDREADHSMYLYAGPEIAVASTKAYTAQISVLAVLAVSLGREIGDAEALSINLAAELGIVATAMEAMVSSKEVIEHIAGEYLATSRNAFFLGRNIDYFVAMEAALKLKEISYIQAEGFASGELKHGTIALIEDGTPVLALITQESINWNIRGNVNEVLARGAKTCVFAMENVAQPGDRFVIPQVHPLLTPLASVIPCQLLAYYAALHRDCDVDKPRNLAKSVTVE
Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
Q92DS8
Q2MI74
PSBT_SOLLC
Photosystem II reaction center protein T
Solanum subgen. Lycopersicon
MEALVYTFLLVSTLGIIFFAIFFREPPTIRTKKN
Seems to play a role in the dimerization of PSII.
Q2MI74
A6T2B6
PRMA_JANMA
Ribosomal protein L11 methyltransferase
Janthinobacterium
MSWTEIVIEVARTHAEALSDALMEAGALSVSVEDADFGTDAEQPLFGEPGMEPTEAAWEHSRVVALTPVEADQAAIVAEAAQAVGLAATDVAFTLRAVEEQDWVRLTQSQFEPIHIGKNIWVVPSWHDAPDPQALVLELDPGLAFGTGSHPTTRLCMEWLEAHPPVGLSVLDYGCGSGILAMVAAKLGSTDVIGIDIDPQAIKSALFNTERNHCEVAYYLPDEFASSGHAHTFDVVVANILANPLKVMAPMLSGRVKPGGKLILSGVLATQVEEVSAAYAPFIKLSVWAEHEGWVALAGQLPPGPESGQA
Methylates ribosomal protein L11.
A6T2B6
A5UG09
AROK_HAEIG
Shikimate kinase
Haemophilus
MAEKRNIFLVGPMGAGKSTIGRQLAQQLNMDFIDSDAVIEERTGADISWIFDLEGEDGFRKREERIINELTQMQGIVLSTGGGAVLSKENRNYLSARGIVIYLETTVEKQFQRTQRDKKRPLLQDAENPRQVLEDLAKIRNPLYEEIADITLPTDEQNAKIMVNQIVDLIDNMNGLNGAL
Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
A5UG09
Q47VU0
GMHA_COLP3
Sedoheptulose 7-phosphate isomerase
Colwellia
MLEQIKNNFTESIQTQIAASELLGPSIEHAGMMMVQCLLGGNKIISCGNGGSAGHAQHFCAQLLNKYETERPSLPAISLNSDISTITSIANDYQYDEVFSKQIRALGHNGDVLLAISTSGNSRNVVKAIESAVSRDIPIIALTGFDGGDISGLLGEGDVEIRVPSARTSRIQEVHLVVLHSLCEIIDTTLFPQGDS
Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate.
Q47VU0
Q8W4D0
CPY71_ARATH
Cyclophilin-71
Arabidopsis
MEEESKNGGTTIPTEELAVVAVPPVVEEEEPMVGPGPAPRGKRKRPLQFEQAYLDSLPSANMYEKSYMHRDVVTHVAVSAAEFFISGSMDGHLKFWKKKGVGIEFAKHFRSHLGPIEGLAVSIDGLLCCTISNDHAVKIYDVVNYDMMAMIRLPYIPGAVEWVYKQGDVKAKLAVSDRDSLFVHIYDPRSGSNEPIASKEIHMNPIKVMKYNPVSDTMISGDTKGIIEYWSATTLQFPEDEVNFKLKSDTNLFEIIKCKTTISAIEVSPDGKQFSITAPDRRIRVFWFRTGKLRRVYDESLVVAQDLQRSDAPLYRLEAIDFGRRMAVEKELEKTESAPQPNAVFDESSNFLIYATFLGIKVINLHTNTVARILGKVESNERYLRVALYQGDQGGKKVRKIPAAAANVNESKEPLTDPTILCCAFKKHRIYMFSRREPEEPEDASQGRDVFNEKPAADELMSVSDIGNSATTSLPENVIMHTTLGDIHMKLYPEECPKTVENFTTHCRNGYYDNHLFHRVIRGFMIQTGDPLGDGTGGQSIWGREFEDEFHKSLRHDRPFTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQGIEKVKTDKNDRPYQDVKILNVTVPKS
PPIases accelerate the folding of proteins (Probable). It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides . Histone proline isomerase that increases the rate of cis-trans isomerization of the synthetic histone H3 peptides H3P30 (RKSAP30F-p-nitroanilide) and H3P30K27me3 (RKme3-SAP30F-p-nitroanilide) in the histone H3 N-terminal tail, in vitro . Histone remodeling factor involved in chromatin-based gene silencing . Reinforces H3K27 methylation . Involved in fundamental processes of chromatin assembly and histone modification by mediating the targeting of FAS1 and LHP1 on the chromatin . Required for the formation and development of leaves, for normal phyllotaxy and for the formation, maintenance and activity of root and shoot apical meristems .
Q8W4D0
H9BFW7
NEUAB_DANRE
CMP-sialic acid synthetase 2
Danio
MEGGRCAQVSSVPASPSSGHRHRAALILARGGSKGIPLKNIKNLAGVPLIGWVLRAALDSDVDSVWVSTDHDEIERVAKLWGAKVHRRSPEVSKDSSSSLETIQEFIRLRPEVDVICHIQATSPCLHPHHINEALQKITHQGFSYVLSVVRRHQFRWEELQENEDRNPKSFNINVAQRPRRQDWPGELYENGSFYFSTRKAWESGLTELGRIAYYEMPPEFSVDIDVDIDWPVAEQRVLRFGYFGREENAAVRLFLCKVSGCLTNGQIYMSVSGEDLVTINARDVAGIQMLQKENIEVILISSVNEPLSRGVLEKVSQRAGCGLSFTEQRNALEMQKLMDKRKLHWDQVAFMGSESEDVEIMSQAGLNGVPSDAPVAELIAAKYTCQRAGGHGAVREFAEYILSMKRKSSREENHERIDKHNF
Catalyzes the activation of 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN) to cytidine 5'-monophosphate 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (CMP-KDN), a substrate required for the addition of sialic acid. Also has weak activity towards N-acetylneuraminic acid (NeuNAc) and N-glycolylneuraminic acid (Neu5Gc).
H9BFW7
B0K971
DTD_THEP3
Gly-tRNA(Ala) deacylase
Thermoanaerobacter
MRAVVQRVSRGEVSVGGEMVSSIGKGFVVLVGISIDDNENDVMYMADKIVNLRVFEDEEGKMNLSLLDIGGEVLLVSQFTLLGDVRKGRRPNFMMAQKPQEALKYFNLLVKEIEKRGVSVKTGIFQAMMKVLIENDGPVTILIDSKKVF
An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo and helps enforce protein L-homochirality.
B0K971
B3CT24
RL15_ORITI
50S ribosomal protein L15
Orientia
MKLNTLFNLNGAKKCSKRIGRGIGSGKGKTCGRGAKGQKSRAKVARGFEGGQTPLIKRLPKRGFKSMNKRNYNIINIITILRLVKANKIEYGAVIDKLLLLKLKMLKKSINKIKLLWANPSSLVLNSEDISLLTKLDLQFNLDEYSISARKNIIKLGMKVINN
Binds to the 23S rRNA.
B3CT24
Q87S29
ISCR_VIBPA
HTH-type transcriptional regulator IscR
Vibrio
MKLTSKGRYAVTAMLDVALHSQQNPVPLADISERQGISLSYLEQLFSKLRKAGLVASVRGPGGGYRLGADAHSIAIGTVIAAVDESVDATKCQGKGDCQGGTRCLTHTLWRDLSSRISDFLNNITLGELMTDNEVLEISDRQDIGLAVTHGLSNKNTTAAPIGVNVRS
Regulates the transcription of several operons and genes involved in the biogenesis of Fe-S clusters and Fe-S-containing proteins.
Q87S29
Q2GHF3
RS18_EHRCR
30S ribosomal protein S18
Ehrlichia
MLKKNKKANSNNSGATAYSPLAYLKRPYFKRSKACPLEQCPNEDIDYKNKGLLSKFTSEYGRILPSRITSVSSRKQRLLSTAVKRARYLALLPYC
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.
Q2GHF3