accession
stringlengths 6
10
| name
stringlengths 6
11
| Full Name
stringlengths 1
147
⌀ | taxon
stringlengths 3
46
⌀ | sequence
stringlengths 16
2.75k
| function
stringlengths 6
5.51k
| AlphaFoldDB
stringlengths 6
10
|
|---|---|---|---|---|---|---|
Q93DY8
|
MAMQ_MAGGM
|
Magnetosome protein MamQ
|
Magnetospirillum
|
MAVSDADASSVDKVESITLQRVKQSEELLAQLYVVEESPRRMGRGPVQLMLAISVLSLVAFITTLLMRYNAFVTMYEDAQAKRSNFEVMIQRRDNLFGNLVKLTLNHAALEHSIFSHTSDKRKESVEAGKGGPIGSAIEQLMKQGGIGKLLGDGGAGKALLGADGGFGNALGRLMAIVEQYPTVQSADTYKHMMTSLVDMEDRIASKREEFNASAATYNVAITKWPWDYLAMITGFKRVEYFHEKPAGDTPIITPQIFQELLPLTHSQESKN
|
Essential for magnetosome formation . Not essential for formation of magnetosome membrane vesicles. One of 7 genes (mamLQBIEMO) able to induce magnetosome membrane biogenesis; coexpression of mamLQRBIEMO in a deletion of the 17 gene mamAB operon restores magnetosome vesicle formation but not magnetite biosynthesis .
|
Q93DY8
|
A2BXA4
|
PSBY_PROM5
|
Photosystem II protein Y
|
Prochlorococcus
|
MLRTLVVFAPIIAALAWVIFNIQKPAREQFNRDFLGKKD
|
Manganese-binding polypeptide with L-arginine metabolizing enzyme activity. Component of the core of photosystem II.
|
A2BXA4
|
Q883N9
|
RLMKL_PSESM
|
rRNA (guanine-N(7)-)-methyltransferase RlmK
|
Pseudomonas
|
MSDRYELFLTCPKGLEGLLAEEATALGLQETREHTSAIRGSADMETAYRLCLWSRLANRVLLVLKRFPMKDAEDLYHGVLDVEWHDHLEPEGTIAVEFSGHGSGIDNTHFGALKVKDAIVDKLRTPEGERPSVDKINPDLRVHLRLDRGEAILSLDLSGHSLHQRGYRLQQGAAPLKENLAAAILIRAGWPRIAAEGGALADPMCGVGTFLVEAGMIAADIAPNIKRERWGFSAWLGHVPTLWRKLHDEALARAEAGLAKTPSWIRGYEADPRLIQPGRNNIERAGLSDWIKVYQGEVATFEPRPDQNQKGLVICNPPYGERLGDEASLLYLYQNLGERLRQACLNWEAAVFTGAPDLGKRMGIRSHKQYSFWNGALPCKLLLIKVTPDQFVTGERRTPEQRQVERENPVEVEVVERKLNKNGNPIKPEPVVVEQARLSEGGQMFANRLQKNLKLLGKWVRREGIDCYRVYDADMPEYSLAIDLYHDWVHVQEYAAPKSIDPEKASARLFDALAAIPQALNIDKSRVVIKRRERQSGTKQYERQSAQGQFLEVSEGGVKLLVNLTDYLDTGLFLDHRPMRMRIQREAAGKRFLNLYAYTATASVHAAKGGARSTTSVDLSRTYLDWARRNLSLNGFSDKNRLEQGDVMAWLQANRDEYDLIFIDPPTFSNSKRMEGIFDVQRDQVELIDLAMARLAPGGVLYFSNNFRKFVLDENLGQRYAVEDITAQTIDPDFARNGKIHRAWKITARA
|
Specifically methylates the guanine in position 2445 (m2G2445) and the guanine in position 2069 (m7G2069) of 23S rRNA.
|
Q883N9
|
A1R6X0
|
RS20_PAEAT
|
30S ribosomal protein S20
|
Paenarthrobacter
|
MANIKSQKKRILTNEKARLRNNAVKSELKTAIRAVNTAVESADKDAAGTALVAASRKLDKAVSKGVIHKNNAANRKSAISKKVNAL
|
Binds directly to 16S ribosomal RNA.
|
A1R6X0
|
Q9JKL5
|
CHP3_MOUSE
|
Tescalcin
|
Mus
|
MGAAHSASEEVRELEGKTGFSSDQIEQLHRRFKQLSGDQPTIRKENFNNVPDLELNPIRSKIVRAFFDNRNLRKGSSGLADEINFEDFLTIMSYFRPIDTTLGEEQVELSRKEKLKFLFHMYDSDSDGRITLEEYRNVVEELLSGNPHIEKESARSIADGAMMEAASVCVGQMEPDQVYEGITFEDFLKIWQGIDIETKMHIRFLNMETIALCH
|
Functions as an integral cofactor in cell pH regulation by controlling plasma membrane-type Na(+)/H(+) exchange activity. Promotes the maturation, transport, cell surface stability and exchange activity of SLC9A1/NHE1 at the plasma membrane. Promotes the induction of hematopoietic stem cell differentiation toward megakaryocytic lineage. Essential for the coupling of ERK cascade activation with the expression of ETS family genes in megakaryocytic differentiation. Also involved in granulocytic differentiation in a ERK-dependent manner. Inhibits the phosphatase activity of calcineurin.
|
Q9JKL5
|
O44572
|
TNNI4_CAEEL
|
Troponin I 4
|
Caenorhabditis
|
MSDVDADEARKMAERERKKEEVRKRLEEASRMKKAKKGFLTPERKKKLRKLLMMKAAEDLKQQQMLKEQERQRILQERIIPLPDLDNEDDLEAVYDEIRERLIDLESENYDVSYIVRQKDFEINELTIAVNDLRGKFVKPTLKKVSKTEGKFDKLKKKEATKVDFRAQLKVVDKNEFALDEEDTEKKEKAAWAK
|
Troponin I is the inhibitory subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to muscle actomyosin ATPase activity.
|
O44572
|
L7T720
|
C719A_PODPE
|
Cytochrome P450 family 719 subfamily A polypeptide 23
|
Podophyllum
|
MEMETSVLGLSSTLIIALAITVIFLLKAKSSSAIKWPPGPKTLPIIGNLHQLGGDELHIVLAKLARVHGAIMTIWMAKKPVIVVSDVNSVWEVLVSKSSDYAARDAAEISKIVSASSHSINTSDSGPYWQTLRRGLTHGPLGPLNISAQIPIQQRDMQRVIREMQQDAAANGGVIKPLDHLKRSSTRLVSRLIFGDTFDNDPYNDSMHEVVQDLNRFGGIALLEQAFSFAKYLPSYKRGVKEFHIHKRKIDDLVRPVVASSNPPSNSYLGFLQSQNYSEEIIIACIFELYLLAMDSSASTATWALAFMIRDQQVQEKLYQDIKRVIGDEVGLVKAEDLSKMHYLQAVVKETMRMKPIAPLAIPHKTAIDTSLMGTKVPKGTCVMVNLYALHHDESVWAKPYTFMPERFLQREDGKSVTEQAFLPFGAGMRICGGMEVGKLQFSLALANLVNAFKWTSAAEGKLPDMSDELQFITVMKTPLEARIVPRNP
|
Cytochrome P450 involved in the biosynthesis of etoposide, a chemotherapeutic compound of the topoisomerase inhibitor family . Catalyzes the conversion of matairesinol to pluviatolide .
|
L7T720
|
Q99PI5
|
LPIN2_MOUSE
|
Lipin-2
|
Mus
|
MNYVGQLAGQVLVTVKELYKGINQATLSGCIDVVVVRQQDGSYQCSPFHVRFGKLGVLRSKEKVIDIEINGSAVDLHMKLGDNGEAFFVEETEEEYEKLPAYLATSPIPTEDQFFKHIETPLVKSSGNERPAQSSDVSHTLESEAVFTQSSVKKKKRRRKKCKQDNRKEEQAASPVAEDVGDVGVSSDDEKRAQAARGSSNASLKEEDYKEPSLFHSGDNYPLSDGDWSPLETTYPQAVCPKSDSELEVKPSESLLRSEPHMEWTWGGFPESTKVTKRERYDYHPRTATITPSENTHFRVIPSEDSLIREVEKDATVEDTTCTIVKPKPRALCKQLSDAASTELPESPLEAPQISSLLDADPVPSPSAEAPSEPKPAAKDSPTKKKGVHKRSQHQGPDDIYLDDLKALEPEVAALYFPKSDTDPGSRQWPESDTFSGSQSPQSVGSAAADSGTECLSDSAMDLPDVTLSLCGGLSENGEISKEKFMEHIITYHEFAENPGLIDNPNLVIRIYNRYYNWALAAPMILSLQVFQKSLPKATVESWVKDKMPKKSGRWWFWRKKESMIKQLPETKEGKSEVPPANDLPSNAEEPTSARPAENDTSSDEGSQELEESIKVDPITVETLSHCGTASYKKSLRLSSDQIAKLKLHDGPNDVVFSITTQYQGTCRCAGTIYLWNWNDKVIISDIDGTITKSDALGQILPQLGKDWTHQGIARLYHSINENGYKFLYCSARAIGMADMTRGYLHWVNDKGTILPRGPLMLSPSSLFSAFHREVIEKKPEKFKIECLNDIKNLFAPSRQPFYAAFGNRPNDVYAYTQVGVPDCRIFTVNPKGELIQERTKGNKSSYHRLSELVEHVFPLLSKEQNSAFPCPEFSSFCYWRDPIPDLDLDDLA
|
Acts as a magnesium-dependent phosphatidate phosphatase enzyme which catalyzes the conversion of phosphatidic acid to diacylglycerol during triglyceride, phosphatidylcholine and phosphatidylethanolamine biosynthesis in the reticulum endoplasmic membrane . Plays important roles in controlling the metabolism of fatty acids at different levels. Acts also as a nuclear transcriptional coactivator for PPARGC1A to modulate lipid metabolism.
|
Q99PI5
|
A9G0D6
|
RS20_SORC5
|
30S ribosomal protein S20
|
Sorangium
|
MANHASADKRNRQRITRTARNRAIKSELRTTVKKARTALKGVPQESAAPVTAAVSALDRAASKGTIPAKRASRVKSRLALALHKASVAAKTAAS
|
Binds directly to 16S ribosomal RNA.
|
A9G0D6
|
O55235
|
GROA_CAVPO
|
C-X-C motif chemokine 1
|
Cavia
|
MAGAAPKTLRFAPLLLLLLLLVLGTSRRAAGAPAASELRCRCLRPVRGLHPKNIQSVAVTAPGPHCHQTEVLATLKDGREACLDPEAPMVQKVLQRMLKGSKAT
|
Has chemotactic activity for neutrophils.
|
O55235
|
B1KR25
|
AROQ_SHEWM
|
Type II DHQase
|
Shewanella
|
MSAKAKILLVNGPNLNLLGRREPGHYGHHTLDSIVQNMKNTANSADVELEHIQSNAEHELIDAIHSTDANFIIINPAAFTHTSVAIRDAILGVAIPFIEVHLSNVHAREPFRHHSYFSDKAVGVICGLGADGYQFALKSAINRLQGPSA
|
Catalyzes a trans-dehydration via an enolate intermediate.
|
B1KR25
|
Q8K952
|
RL23_BUCAP
|
50S ribosomal protein L23
|
Buchnera
|
MISQERFLKVLLSPHISEKSSISMEKFNTVVLKVSRNTTKNEIKFAVQNLFNIQVESVKTVYVKGKKKRQSNRIIYRSDWKKAYIKVKKGQNLDFMSNIE
|
One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome.
|
Q8K952
|
B0KD95
|
GCST_THEP3
|
Glycine cleavage system T protein
|
Thermoanaerobacter
|
MDNLKKTPLFDLYKKYNGKIIDFAGWALPVQFESIISEHEAVRNAAGLFDVSHMGEITVKGREAFNFLQNLITNDLSKLKDNQVFYTFMCNYNGGVVDDLLVYKYSDEHFLLVVNAANIEKDYKWMKDNKGVYEVEINNISDEISELAVQGPKAEEILQKLTYTDLSEIKFFYFKDNVKIAGIECLVSRTGYTGEDGFEIYMPNKYAVELWEKIIEVGKEYGLKPAGLGARDTLRFEAGLPLYGNELSEEITPLEAGFEFFVKFDKGNFIGKDALLKQKEEGLKRKIVGFEMIDNGIPRHGYEVRADNQKIGYVTTGYFSPTLKKNIGLALIDSKYAQLGNQIEIVIRNKPLKALIISKNFYKKNYKK
|
The glycine cleavage system catalyzes the degradation of glycine.
|
B0KD95
|
A9MNE8
|
PURT_SALAR
|
Phosphoribosylglycinamide formyltransferase 2
|
Salmonella
|
MTLLGTALRPAATRVMLLGSGELGKEVAIECQRLGIEVIAVDRYPDAPAMHVAHRSHVINMLDGEALRHVIAVEKPHYIVPEIEAIATDTLRDLEDEGLNVVPCARATQLTMNREGIRRLAAEELGLPTSTYRFADSEASFRDAVAAVGFPCIVKPVMSSSGKGQSFIRSPEQLAQAWKYAQQGGRAGAGRVIVEGVVKFDFEITLLTVSAVDGVYFCAPVGHRQQDGDYRESWQPQQMSELALKRAQEIARHVVLALGGHGLFGVELFVCGDEVIFSEVSPRPHDTGMVTLISQDLSEFALHVRAFLGLPVGAIRQYGPAASAVILPQLTSRNVTFDNVQAAVGAGLQVRFFGKPEIDGARRLGVALATGENVEEAVIRAKKAVSSVIVKE
|
Involved in the de novo purine biosynthesis. Catalyzes the transfer of formate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR). Formate is provided by PurU via hydrolysis of 10-formyl-tetrahydrofolate.
|
A9MNE8
|
P58445
|
HYPAA_POMPR
|
Cyclotide hypa-A
|
Pombalia
|
GIPCAESCVYIPCTITALLGCSCKNKVCYN
|
Probably participates in a plant defense mechanism.
|
P58445
|
B1WT39
|
RECF_CROS5
|
DNA replication and repair protein RecF
|
Crocosphaera subtropica
|
MYLKHIHLYGFRNYHEQTLDLQSQKTILLGNNAQGKSNLLEAVELLATLKSHRTNRDRDLILEGKKTGQILAMVERTYGESELGITFRSPGRRSLMLNHENLRRHLDFLGHINAVEFSCLDLDLVRGSPETRRSWLDTLLIQLEPVYASIIHQYYKILRQRNALLKVIRKTVEEQENSSNLSAELSQLKVWDQQLAEAGTRVTRRRYRVIERITPLAQKWHQEISSGTEILAINYLPNIKIENEDPQQVQQAFLDKIEQRRMAEQQLATTVVGPHRDDVEFNINHTPAKSYGSQGQQRTLVLAIKLAELQLIEEVIGEPPLLLLDDVLAELDPNRQNQLLEVIQGRFQTLITTTYLHSFDAQWLNSSQIMKVEGGKIAQL
|
The RecF protein is involved in DNA metabolism; it is required for DNA replication and normal SOS inducibility. RecF binds preferentially to single-stranded, linear DNA. It also seems to bind ATP.
|
B1WT39
|
P59143
|
RR4_HYPDI
|
30S ribosomal protein S4, chloroplastic
|
Hypopterygium
|
MSRYRGPRVRIIRRLGALPGLTNKTPQLKSSSINQSASNKKISQYRIRLEEKQKLRFHYGITERQLLNYVRIARKAKGSTGEILLQLLEMRLDNVIFRLGMTPTIPGARQLVNHRHILVNGYIVDIPSYRCKPQDFINIKNQRKSEAIISKNIEFYQKYKIPNHLTYNSLEKKGLVNQILNRESIGLKINELLVVEYYSRQA
|
With S5 and S12 plays an important role in translational accuracy.
|
P59143
|
Q1J626
|
METK_STRPF
|
Methionine adenosyltransferase
|
Streptococcus
|
MSERKLFTSESVSEGHPDKIADQISDAILDAILAEDPEAHVAAETCVYTGSVHVFGEISTTAYIDINRVVRDTIAEIGYTEAEYGFSAESVGVHPSLVEQSGDIAQGVNEALESREGDTDDLSHIGAGDQGLMFGFAINETPELMPLPISLSHQLVRRLAELRKSGEISYLRPDAKSQVTVEYDEHDKPVRVDTVVISTQHDPEATNDQIRQDVIEKVIKDVIPADYLDDDTKFFINPTGRFVIGGPQGDSGLTGRKIIVDTYGGYSRHGGGAFSGKDATKVDRSASYAARYIAKNLVAAGLATKAEVQLAYAIGVAQPVSVRVDTFGTSTVPEAVLEAAVRQVFDLRPAGIIQMLDLKRPIYKQTAAYGHMGRTDIDLPWERLNKVDALVEAVKTVL
|
Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme.
|
Q1J626
|
B0TT43
|
AROA_SHEHH
|
5-enolpyruvylshikimate-3-phosphate synthase
|
Shewanella
|
MNQLRLEPIKKVSGTINIPGSKSISNRALLLATLASGTTTLTNLLDSDDIRYMLASLKQLGVSYRLSNNNTVCELDGLAGPLNAGEPQTLFLGNAGTAMRPLCAALTLGQGQFTLTGEPRMEERPIGDLVDALRQLGAEVSYLKNEGFPPLNITSTGLNGGNVEIAGDLSSQFLTALLMVAPLAKGDVNIKIKGELVSKPYIDITLALMAQFGVEVQNNDYASFVIKAGQRYVSPGKVLVEGDASSASYFLAAGAIQGGEVKVTGVGKLSIQGDVKFADVLEQMGADIEWGDDYIIARQAKLKAVDLDMNHIPDAAMTIATAALFATGTTRIRNIYNWRIKETDRLAAMATELRKVGAIVDEGHDYISVTPPAKLNTAAIDTYNDHRMAMCFSMMAFADCGITINEPECTSKTFPDYFNQFNALAN
|
Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.
|
B0TT43
|
B7JVZ9
|
AROC_RIPO1
|
5-enolpyruvylshikimate-3-phosphate phospholyase
|
Rippkaea orientalis
|
MGNTFGHLFRITTFGESHGGGVGVVIDGCPPRLEISESDIQYDLDRRRPGQSKITTPRHESDTCEIISGVFEGKTLGTPIAILVRNKDQRSQDYDEMSVKLRPSHADATYEAKYGIRNWQGGGRSSARETIGRVAAGAIAKKILKQVANVEIIGYVKRIKDLEGMVDPSTVTLENVESNIVRCPDPEMAEKMIDLIDQTRRNKDSIGGVVECVARNIPKGLGQPVFDKLEADLAKGVMSLPASKGFEIGSGFAGTLLTGSEHNDEFYLDETGEIRTTTNRSGGIQGGISNGENIIIRVAFKPTATIGKEQKTVTNTGEETTLAAKGRHDPCVLPRAVPMVEAMVALVLCDHLLRQEGQCGLF
|
Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.
|
B7JVZ9
|
P56109
|
ALF_HELPY
|
Fructose-1,6-bisphosphate aldolase
|
Helicobacter
|
MLVKGNEILLKAHKEGYGVGAFNFVNFEMLNAIFEAGNEENSPLFIQTSEGAIKYMGIDMAVGMVKTMCERYPHIPVALHLDHGTTFESCEKAVKAGFTSVMIDASHHAFEENLELTSKVVKMAHNAGVSVEAELGRLMGIEDNISVDEKDAVLVNPKEAEQFVKESQVDYLAPAIGTSHGAFKFKGEPKLDFERLQEVKRLTNIPLVLHGASAIPDNVRKSYLDAGGDLKGSKGVPFEFLQESVKGGINKVNTDTDLRIAFIAEVRKVANEDKSQFDLRKFFSPAQLALKNVVKERMKLLGSANKI
|
Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis.
|
P56109
|
Q87DM0
|
MNMA_XYLFT
|
tRNA-specific 2-thiouridylase MnmA
|
Xylella
|
MNTPRIIVAMSGGVDSSVAAWRLNSQREAIAGLFMRNWTDDGNGQCHAEEDRRDAVAVCGILGIAFHFRDFSHEYWQEVFTHFLAEYANGRTPNPDVLCNREIKFKHFLETARELGADRIATGHYARIEHYRQRWHLLRGADRSKDQSYFLHQLGQEQLAATLFPIGDLEKQQLRQLAHQTGLPTHAKKDSTGICFIGERNFREFLKQYLPAQPGEIRDPQEQRIAEHPGVFYFTLGQRQGLNIGGVRNRPPSPWYVIGKDLATNVLYVDQHRDSPFLQSRWLRSEPAHWVSGSPPAPTFTCTAQTRYRQADEPCKVTVRNDGSLDVDFTRTQWAVTPGQSLVLYDGNECLGGAVIATTDAPLERKRARNLSKTENVLQ
|
Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
|
Q87DM0
|
P59530
|
TA2R7_MOUSE
|
mT2R42
|
Mus
|
MTYETDTTLMLVAVGEALVGILGNAFIALVNFMGWMKNRKIASIDLILSSVAMSRICLQCIILLDCIILVQYPDTYNRGKEMRTVDFFWTLTNHLSVWFATCLSIFYLFKIANFFHPLFLWIKWRIDKLILRTLLACVIISLCFSLPVTENLSDDFRRCVKTKERINSTLRCKVNKAGHASVKVNLNLVMLFPFSVSLVSFLLLILSLWRHTRQIQLSVTGYKDPSTTAHVKAMKAVISFLALFVVYCLAFLIATSSYFMPESELAVIWGELIALIYPSSHSFILILGSSKLKQASVRVLCRVKTMLKGKKY
|
Gustducin-coupled receptor implicated in the perception of bitter compounds in the oral cavity and the gastrointestinal tract. Signals through PLCB2 and the calcium-regulated cation channel TRPM5.
|
P59530
|
A0PGB2
|
TAP75_TETTS
|
Telomerase-associated protein of 75 kDa
|
Tetrahymena
|
MEIEEDLNLKILEDVKKLYLQSFDYIKNGISSSLPSDKKFLADDDIDLSRITFLYKFISVNPTLLLINEKTQAKRRIFQGEYLYGKKKIQFNIIAKNLEIERELIQFFKKPYQCYIMHNVQVFQMLNKNKNNNVVEFMDSEDLQSSVDCQLYYLIDESSHVLEDDSMDFISTLTRLSDSFNSNEFVFETNYSIQISQMPKPLNTTHFKLLQPKVVNSFEGVILQVQEGKNILQIEELIDQVYLNSRRDRFYILKVANGKNYMDFIEVYLVYDNEDQEAKQQLQFYLKPFQRILIFQSLKHFTKNLKLFMISFFYSSGVQPNNSNVKNFLVSHKGVEFFSRFDIQKNELLCKDLIKSYNKLPLSNISKLLEDEGVMIRSNMKFQVRVKKVKYFKIRLNCLNCKQEWTVGLKNCINCKGQQSYISYNIQVLVQDQHFLEQQAYIYLYDDLAAQFFNITESEKKELHLHLTKNETFIQLYYSFNKDYPLSIIKFKDKIFNKDITNCIVAYPFADIDNKIFNSQQQIIQDENLRIESEKFIQNFTEDNNLQESKLYYEKFKSKNKQQIFVNGTYISTNYSQGQKICLKPIPCLKVMYVFPQEDIKLSALKIIEEINQLKIQIDQLN
|
Component of a CST-like subcomplex of the holoenzyme telomerase ribonucleoprotein complex, which stimulates telomerase complementary-strand synthesis (Probable). Telomerase is an essential ribonucleoprotein enzyme that copies new telomeric repeats onto chromosome ends by repetitively synthesizing the short telomere-repeat sequence 5'-TTGGGG-3' using an RNA template component TER (Probable). The CST-like subcomplex (also named 7-4-1) binds telomeric single-stranded DNA and coordinates telomere G-strand and C-strand synthesis (Probable).
|
A0PGB2
|
Q9N5K3
|
SYP4_CAEEL
|
Synaptonemal complex protein 4
|
Caenorhabditis
|
MSFPTLQVRPNEKNPKVLRCHEFLRQSNQLVERNMINTEGRKMLAKLLTKMVSEAKGIYALDERRAELAKSGKLQEKLKSAYQTSLTVMEDRLHIAELSRQVQEKKLTVQQKYYECDDLRKSVQETNTEARRVQEINEQRLVDTTRATEELIVKSASILKNLENSSDVHKLRAMEEEKRILEEVVEGLRDQKKCLADDIRTKKATLKAESKKSFEKTVIECAKHYKLHQSLMPKLDKSKRSLETLKDEEENRRICGSLSLDETMQFDRSFILASMDKTNKPEKAVQQLTSKSSEVSITPQISETAKSSFSKEPIPTQHPMEVGEEPVIEHSAEESVHIEPPNVTEIREVVPQITIQPTRQDSVVQRDAEELDTSAVPSPQPESILDEPEEEEEELSNHENHADQSMDVMEVDQEVPEESPMEVGEQEEIEQPSVFKDILATEQAALSQEQEPEIVEKQADNDVQFVDDQQVGAQLDVEDEEEVMSENGSNKSNNFSFNFFGNSKGTSAGEGGGEGNFDFNFDGIGAGDDGSNNGGSTGDLDFLNYDGEDEGKGSGNTQSDPFGFASNGNAAGGGGDGSFNFNFDGDGEGGATSGAGGNSTSFFNF
|
Constitutes an element of the transverse filaments of the synaptonemal complex (SC), formed between homologous chromosomes during meiotic prophase I, and is required for the assembly of the central region of the SC . Required for chromosome synapsis and chiasma formation between homologous chromosomes during meiosis, mechanisms that are crucial for crossover formation and meiotic recombination .
|
Q9N5K3
|
A0AK63
|
SCPA_LISW6
|
Segregation and condensation protein A
|
Listeria
|
MVEMNFKVDAFEGPLDLLLHLIGQLEVDIYDIPMAEITDQYMEFVHTMQEMELDVASEYLVMAATLLAIKSKMLLPKQELEIDYDTLEEEEDPRDALVEKLMEYKRFKEAAKELKEKEAERSFYFSKPPMDLAEYDDGTKVAELDVSLNDMLSAFNKMLRRKKLNKPLHTRITTQEISIDDRMNSVLGKLNQQKNHRLRFDELFEEQTKEQLVVTFLALLELMKRKLVEVEQSESFADLYVQGKGEELS
|
Participates in chromosomal partition during cell division. May act via the formation of a condensin-like complex containing Smc and ScpB that pull DNA away from mid-cell into both cell halves.
|
A0AK63
|
P0AAZ6
|
RARA_ECO57
|
Replication-associated recombination protein A
|
Escherichia
|
MSNLSLDFSDNTFQPLAARMRPENLAQYIGQQHLLAAGKPLPRAIEAGHLHSMILWGPPGTGKTTLAEVIARYANADVERISAVTSGVKEIREAIERARQNRNAGRRTILFVDEVHRFNKSQQDAFLPHIEDGTITFIGATTENPSFELNSALLSRARVYLLKSLSTEDIEQVLTQAMEDKTRGYGGQDIVLPDETRRAIAELVNGDARRALNTLEMMADMAEVDDSGKRVLKPELLTEIAGERSARFDNKGDRFYDLISALHKSVRGSAPDAALYWYARIITAGGDPLYVARRCLAIASEDVGNADPRAMQVAIAAWDCFTRVGPAEGERAIAQAIVYLACAPKSNAVYTAFKAALADARERPDYDVPVHLRNAPTKLMKEMGYGQEYRYAHDEANAYAAGEVYFPPEIAQTRYYFPTNRGLEGKIGEKLAWLAEQDQNSPIKRYR
|
DNA-dependent ATPase that plays important roles in cellular responses to stalled DNA replication processes.
|
P0AAZ6
|
Q87ZB3
|
FADA_PSESM
|
Fatty acid oxidation complex subunit beta
|
Pseudomonas
|
MSLNPRDVVIVDFGRTPMGRSKGGMHRNTRAEDMSAHLISKLLERNNKVDPAEVEDVIWGCVNQTLEQGWNIARMASLLTQIPHTSAAQTVSRLCGSSMSALHTAAQAIMTNNGDVFVIGGVEHMGHVSMMHGVDPNPHMSLHAAKASGMMGLTAEMLGKMHGITREQQDAFGLRSHQLAHKATLEGKFKDEIIPMQGYDENGFLRVFDYDETIRPDTTLESLAALKPAFNPKGGTVTAGTSSQITDGASCMIVMSAQRAQDLGIQPLAVIRSMAVAGVDPAIMGYGPVPATQKALKRAGLSISDIDFFELNEAFAAQALPVLKDLKVLDKMNEKVNLHGGAIALGHPFGCSGARISGTLLNVMKQNGGTFGVSTMCIGLGQGIATVFERV
|
Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed.
|
Q87ZB3
|
P33684
|
PAHO_MACMU
|
Pancreatic polypeptide
|
Macaca
|
APLEPVYPGDNATPEQMAQYAADLRRYINMLTRPRY
|
Pancreatic hormone is synthesized in pancreatic islets of Langerhans and acts as a regulator of pancreatic and gastrointestinal functions.
|
P33684
|
Q7S2Y8
|
DML1_NEUCR
|
Protein dml-1
|
Neurospora
|
MHEIITLQLGQQSNYLATHFWNAQESYFTYSEDQEPAVNHDIHWRPGIGADGTETYMPRTVIYDLKGGFGSMAKTNALYNDLEEGQTPQALWNGPTVLQKQPAIPQSAYQQSLDAGLEPPPLTTDTVRYWSDFNRVFYHPRSVVQLNEYELNSSIMPFERYATGEDLFASLDKEHDLLDRDLRPFIEEADQMQGIQVMTGLDDAWGGFAAKYLERIRDEYGKTAMFVWGSEQESVMRAGGLSREKRLLRLANKARTMTEVYKYASVVVPFTVPATLPGSVVLDAGSQWHNTALSAAAIESVTLPSRLRDPANRDTMATLADSLNAMGKQNVASLGMSFAPEPTEEEDVVMEGTQDFRQRQLLNQKSSRHAAVMVKENPEGVFLDINFTPTDQLDYVRRRGGGDDDRPRVFSQMLTSRGYEIDEQVQEAKEAEEDERFRRRSSYETVMKSYHTPLRFPLLDSFPQIFRDDSGEPLKRGGAINVTSSLSTDASVHKRLKSLRTTVGRSIGLEDREQLGNELAEMADEYHEGWSSGSDDGDDD
|
Involved in the partitioning of the mitochondrial organelle and mitochondrial DNA (mtDNA) inheritance.
|
Q7S2Y8
|
Q9SIJ5
|
RADL2_ARATH
|
Protein RADIALIS-LIKE SANT/MYB 1
|
Arabidopsis
|
MASGSMSSYGSGSWTVKQNKAFERALAVYDQDTPDRWHNVARAVGGKTPEEAKRQYDLLVRDIESIENGHVPFPDYKTTTGNSNRGRLRDEEKRMRSMKLQ
|
Probable transcription factor. Required for female gametophyte development.
|
Q9SIJ5
|
Q9SYT0
|
ANXD1_ARATH
|
Annexin A1
|
Arabidopsis
|
MATLKVSDSVPAPSDDAEQLRTAFEGWGTNEDLIISILAHRSAEQRKVIRQAYHETYGEDLLKTLDKELSNDFERAILLWTLEPGERDALLANEATKRWTSSNQVLMEVACTRTSTQLLHARQAYHARYKKSLEEDVAHHTTGDFRKLLVSLVTSYRYEGDEVNMTLAKQEAKLVHEKIKDKHYNDEDVIRILSTRSKAQINATFNRYQDDHGEEILKSLEEGDDDDKFLALLRSTIQCLTRPELYFVDVLRSAINKTGTDEGALTRIVTTRAEIDLKVIGEEYQRRNSIPLEKAITKDTRGDYEKMLVALLGEDDA
|
Has a peroxidase activity. May act in counteracting oxidative stress. May also mediate regulated, targeted secretion of Golgi-derived vesicles during seedling development.
|
Q9SYT0
|
B4S5M5
|
RL23_PROA2
|
50S ribosomal protein L23
|
Prosthecochloris
|
MRNPLMQPWLTEKSTGLTEQKGQYVFKVKSAANKTEIKAAVEAKFGVDVASVRTVNCLGKTKRQFTRKGVLAGKKNDWKKAFITLKEGQAIDYYSGSTDQGEEKKSNKG
|
One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome.
|
B4S5M5
|
C0QT45
|
NUSB_PERMH
|
Antitermination factor NusB
|
Persephonella
|
MGKYRKKAREIVFRTLYTYDIKGGDLFEIMEDHIKDIRGKLSKKTVDYIYSILKGIDEHLPEIDDILRENLKNWRLERLGYPERALLRLGVYELLFSDIEDKGRVFMDILDLTKCYIDNPDTVKFINGVLSTVYKNRQKVNQ
|
Involved in transcription antitermination. Required for transcription of ribosomal RNA (rRNA) genes. Binds specifically to the boxA antiterminator sequence of the ribosomal RNA (rrn) operons.
|
C0QT45
|
Q2S0W8
|
DABA_SALRD
|
Probable inorganic carbon transporter subunit DabA
|
Salinibacter
|
MPIDRSVVRARIENAAEYVGPLWPLRTFNAANPLLGFEDQPFDRAVQKAGQLFGGRGYPGPTVFRQAWENGEIDADVLTRHLAEHGITERPEVLLDRMDADAAGRDAAPADQPLDRVLTKWLAAFLDQGQAAWPMPNREDGFYAAWRTVAPYDGDIPGVGRPSDLPGTVVEAFEAVLESYPEARWEPIFVHHLTALPGWTGFIKWRSRRADTAWQAAHPISLTEYLAVRLTLADRMGAAIAPDRTDELPANGTDQPVLPRIWLRAWEESYRTRLLDDLRQTQQTTPSGSDAGRPDAQLVFCIDTRSEVIRRHIEQQGPYETHGYAGFFGVPMQHQPYGTEERVKSCPPIVDPKHRIMERPAEPHRAQAERYDWWARLQKAGAALLKTLKKNVAAVFGFVEGSGGFFGAAMAARTLAPSGLSRLDEALDDWLPGPASFCEPTVDRAPPADADAEDGLPVGLADEAKVLYAEAAFRLMGWTDTFAPVVVFTGHGSQTPNNPYKASLDCGACAGNPGGPNARVLAAICNEDAVQEALRERGIAIPDDTVFLAGQHNTTTDEIALFVDEDDPPVAPDALDRLRRDLHAAQADAATERVRTLNTSVDEGRPAAAVRETERRAADWAETRPEWGLAGNAAFIVGPRALTRGLDLDGRCFLHSYDWATDDDGTALENIMTGPLVVGEWINTQYYFSTVDNAAYGSGSKVTQNVVGKLGVVQGNGGDLMSGLPLQSLKADDEHVHHRPLRLMALIQAPTDRVEAILDRHAAVAHLFDHEWMHLTVMDPEQDDAFVRYKPGGGWHARPAPDASTATKAPASAGVPS
|
Part of an energy-coupled inorganic carbon pump.
|
Q2S0W8
|
Q1D654
|
GLGB_MYXXD
|
Glycogen branching enzyme
|
Myxococcus
|
MRKPADKAQVDAELQRVVELRHPEPHAVLGIHPDGDGVVIRAFRPDAVAIHVLPESGGRVAMTHRPGGVYEARINGKDQTFNYLLEVEYPGKRVFTLRDPYSFLPTLGEMDLYYAGEGRHERLWERMGAHLLHHHGVRGTSFAVWAPTAAGVSVVGDFNGWDGRLHSMRRMGSSGIWELFVPEVGEGTRYKFEIRPGQGGPNVLKADPFAFRTEVPPATASVVHDLARYTWGDAAWLEQRAQRRDVHHQPWSVYEVHLGSWRRVVEDGDRPMTYRELAPALAEYIKFTGFTHIELLPVAEHPYGGSWGYQVGGYYAPTARFGHPDDLRFFIDHMHQEGIGVLVDWVPGHFPRDLHALGQFDGTALYEHADPRKGAQPDWGTLVFNFGRNEVRNFLIANALFWIEEYHIDGLRVDAVASMLYLDYSRKQGEWIPNRWGGRENEEAIHFLRELNETVHRKHPGVVVIAEESTAWPKVSAPVSEGGLGFDYKWNMGWMHDTLSYFSKDPIYRQYHHNQLTFGLLYAFSEQFMLPLSHDEVVHGKGSLYGRMPGDPWQKRANLRALFAWMWAHPGKKLVFMGGEFGQPAEWNHDKSLDWHLTHDPGHHGILQLVSDLNRIYRDMPALHDADGEPMGFQWLQPDSAAYNVFAFVRRARQPGRHVVCIANLSPTVRENYRVGFPFQGRYVELLNTDAEQYGGSNLGNMGQIHTEPTGWDGQPASATLTLPPLSVLWFTPG
|
Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position.
|
Q1D654
|
A4XL73
|
RIMP_CALS8
|
Ribosome maturation factor RimP
|
Caldicellulosiruptor
|
MSKVTKKVEELVKPILEKYGFDLVDIEFKKEGKKHFLRVYIDKPGGITIDDCQLVSEELSNKLDIVDPIPFSYYLEVSSPGVDRPLVNDRDFIRNKGRVVDVFLKQPIMNTTKLTGELVEKNEDVLIIMIDGENISIPFENVKKVKVAIRF
|
Required for maturation of 30S ribosomal subunits.
|
A4XL73
|
Q9VBZ5
|
YTHDF_DROME
|
YTH domain-containing family protein
|
Sophophora
|
MSGVDQMKIPGNTAKSVEERNIPWSQQVDEASYENLSSPTHDEVSGNDNSMQFQYPPFNFKENCNTPWNNMNKGRKANANHDSYRRHGHSIPNNTRRDEHQVNPWNSRKPAAQSFRNENDQPSTKLDNRTSDEAQNQEVVAAPKKTTWASIASQPAKLTSRAASTTSNSKKKGPGMPPPPMVPGKHNLDVNVWDLPNNKPPPVPSPPSPIDLGYSDLSSDFSISSNTAPPLGARAEKVHKDTENFLKYEHKGLGNNNNFSRAKVSPTGPVRRNLGPQQPVHHAAPRPATNAGPFGPPNARRHDGGPHPSRNSERSGNYSSFRGSEFESASKFEYRDENQSRPVEATSATEELPVDSQLVLDELKDKNNYNPKVLDLKKAGSARFFVIKSYSEDDIHRSIKYEIWCSTDHGNKRLDDAFKERHEEGGNIMLFFSVNGSGHFCGMAQMMTPVDYNSTSSVWSQDKWRGKFKVKWIYVKDVPNGTLRHIRLENNENKSVTNSRDTQEVPNDKGIEVLQILHSYNHSTSIFDDFFHYEKKQEEEVSSKRPPMHGPDGNNHAPAPLARSFNRQADDKDRDRDGRGGMSQKHFNSGGGAGFRNPGHRGGAGSGGSHNNYSEYRRGFDIHKSSSDYQFKDRDGPDFDRENDFGSHYGSNNRKNEYKHNNTNKARLKTRDRDFSTEQIKIGVRFKDTDKDKMRSNEYS
|
Specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs . M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in the efficiency of mRNA processing and stability . Together with Fmr1, regulates axonal growth in the mushroom bodies and neuromuscular junctions by repressing the translation of several mRNAs, such as those of chic and futsch .
|
Q9VBZ5
|
Q4G373
|
PSAI_EMIHU
|
Photosystem I reaction center subunit VIII
|
Emiliania
|
MSASFLPSILTPVVTLVFPGLMFALFFVLIEQEEIA
|
May help in the organization of the PsaL subunit.
|
Q4G373
|
Q8IVS2
|
FABD_HUMAN
|
[Acyl-carrier-protein] malonyltransferase
|
Homo
|
MSVRVARVAWVRGLGASYRRGASSFPVPPPGAQGVAELLRDATGAEEEAPWAATERRMPGQCSVLLFPGQGSQVVGMGRGLLNYPRVRELYAAARRVLGYDLLELSLHGPQETLDRTVHCQPAIFVASLAAVEKLHHLQPSVIENCVAAAGFSVGEFAALVFAGAMEFAEGLYAVKIRAEAMQEASEAVPSGMLSVLGQPQSKFNFACLEAREHCKSLGIENPVCEVSNYLFPDCRVISGHQEALRFLQKNSSKFHFRRTRMLPVSGAFHTRLMEPAVEPLTQALKAVDIKKPLVSVYSNVHAHRYRHPGHIHKLLAQQLVSPVKWEQTMHAIYERKKGRGFPQTFEVGPGRQLGAILKSCNMQAWKSYSAVDVLQTLEHVDLDPQEPPR
|
Catalyzes the transfer of a malonyl moiety from malonyl-CoA to the free thiol group of the phosphopantetheine arm of the mitochondrial ACP protein (NDUFAB1). This suggests the existence of the biosynthesis of fatty acids in mitochondria.
|
Q8IVS2
|
A0QJU9
|
NUOC_MYCA1
|
NDH-1 subunit C
|
Mycobacterium avium complex (MAC)
|
MSSPDQDPREAIAQGDDEVIDVRRGMFGAAGTGDTSGYGRLVRTVTLPGSSPRPYGSYFDDVVDTLTESLQSNGIEFHQAIEKVVVYRDELTLHVDRAALPHVAQHLRDDPRLRFEMCLGVSGVHYPHETGRELHAVYPLQSITHNRRVRLEVAVPDGDPHIPSLYRIYPTTDWHERETYDFFGIIFDGHPSLTRIEMPDDWHGHPQRKDYPLGGIPVEYKGAQIPPPDERRAYN
|
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.
|
A0QJU9
|
A9BP16
|
ISPE_DELAS
|
4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase
|
Delftia
|
MRSLHDVPAPAKLNLFLHITGRRADGYHLLQSVFMLLDWHDTLHFDRRGDGQISREDLSGMALPADDLIVRAARALQQATGCRAGVHIGVEKRLPAQAGMGGGSSDAASTLIALNRLWQLNLTRRELQRIALDLGADVPFFLCGNSAWVEGIGEHITPLEQAHALPPQRFVVVKPEAGLETLSIFRDATLKRDHAHATIEDFAADHYGFGQNDLQPVAERLQPEVKKAIDWLNSLKLHARMTGSGSAVFAPLTQTIDLKDAPGAWNVRVCSNLQAHPLKDWLKDESL
|
Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
|
A9BP16
|
Q92PB4
|
MOAA_RHIME
|
Molybdenum cofactor biosynthesis protein A
|
Sinorhizobium
|
MNTAAIDQTDARPLDTTTAPMVDPFGRAVTYLRVSVTDRCDFRCTYCMAEHMAFLPKKDLLTLEELQRLCSAFIAKGVRKLRLTGGEPLVRKNIMFLIRELGKEIEAGRLDELTLTTNGSQLSKFAAELVDCGVRRINVSLDTLDPDKFRQITRWGELARVLEGIDAALAAGLKVKINAVALKDFNDAEIPELMRWAHGRGMDLTLIETMPMGEVDEDRTDHYLPLSEMRRRLEADFTLSDIPYRTGGPARYVEVAETGGRLGLITPLTHNFCESCNRVRLTCTGTLYMCLGQNDAADLRAALRATDDDAYLAQVIDEAIGRKPKGHDFIIDREHNRPAVARHMSVTGG
|
Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate.
|
Q92PB4
|
Q9X1H3
|
YIDD_THEMA
|
Putative membrane protein insertion efficiency factor
|
Thermotoga
|
MKKLLIMLIRFYQRYISPLKPPTCRFTPTCSNYFIQALEKHGLLKGTFLGLRRILRCNPLSKGGYDPVPEEFSFKPRRRWS
|
Could be involved in insertion of integral membrane proteins into the membrane.
|
Q9X1H3
|
O84308
|
VATD_CHLTR
|
V-ATPase subunit D
|
Chlamydia
|
MSSQIKLTKNSYRAEKQKLNMLGMYLPTLKLKKALLQAEVQSAIRLAAESTVTNEQARDRMYAFAELFSIPLYTDAVEQCFSVDILEKDVENIAGVEVPLLKRVVLTSPEYSLLDTPIWLDSLLASVKEYVVSKIYAENAQERLLLLEEELRRVSIRVNLFEKKLIPTTSQTLKKIAIFLSDRSITDVGQMKMAKKKIQQHKE
|
Produces ATP from ADP in the presence of a proton gradient across the membrane.
|
O84308
|
Q87L68
|
AROB_VIBPA
|
3-dehydroquinate synthase
|
Vibrio
|
MERITVNLAERSYPISIGAGLFEDPAYLSQVLSNKNTNQKVVVISNVTVAPLYADKILHQLKQLGCDASLLELPDGEQYKNLDVFNQVMNFLLEGSYARDVVIIALGGGVIGDLVGFASACYQRGVDFIQIPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFYQPKAVIIDTNCLSTLPEREFAAGIAEVIKYGIIYDGAFFDWLEENLDRLYTLDEDALTYAIARCCQIKAEVVAQDEKESGIRALLNLGHTFGHAIEAELGYGNWLHGEAVSSGTVMAAKTSLLRGLISEEQFERIVALLRRAKLPVHTPDSMSFDDFIKHMMRDKKVLSGQLRLVLPTGIGSAEVIADTSQEVIQQAIDFGRNI
|
Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
|
Q87L68
|
Q67TB6
|
ATPE_SYMTH
|
F-ATPase epsilon subunit
|
Symbiobacterium
|
MADMSLTIITPERTVLRDAPADAVVVPVVDGSMGILKNHAPMVANLRIGVLRYKQDGVYKRVAVTGGFVEVSENRITVLADAAELAESIDVMRAMEAKRRAEARLRDRKANIDRTRAEAALRRAMVRLRAAGALDHDKD
|
Produces ATP from ADP in the presence of a proton gradient across the membrane.
|
Q67TB6
|
B5F0A4
|
RLMF_SALA4
|
rRNA adenine N-6-methyltransferase
|
Salmonella
|
MSAQKPGLHPRNRHQHRYDLAALCQTTPELTSFLIRTPAGEQSVDFANPQAVKALNKALLAHFYAVTHWDIPPGFLCPPVPGRADYIHHLADLLGETTGSIPAQATILDVGVGANCIYPLIGVHEYGWRFTGSEVSDAAMSSAQAIIQANTGLSRAIRLRRQKDPAAIFTGIIHKNEFYDATLCNPPFHDSAAAARAGSERKRRNLGQNKDDALNFGGQQQELWCEGGEVAFIKKMIAESQSFRRQVLWFTTLVSRGENLPPLYRALAEAGAVKVVKKEMAQGQKQSRFIAWTFMDDDQRRRFITRKR
|
Specifically methylates the adenine in position 1618 of 23S rRNA.
|
B5F0A4
|
D5JBW9
|
GAO_SAUCO
|
Germacrene A oxidase
|
Saussurea
|
MELSFTTSIAVATIVFVLFKLATRPKSNKKLLPEPWRLPIIGHMHHLIGTMPHRGVMDLARKYGSLMHLQLGEVSTIVVSSPKWAKEILTTHDITFANRPETLTGEIIAYHNTDIVLAPYGEYWRQLRKLCTLELLSVKKVKSFQSLREEECWNLVQEVKESGSGRPVDLSENIFKMIATILSRAAFGKGIKDQKEFTEIVKEILRQTGGFDVADIFPSKKFLHHLSGKRARLTSIHKKLDNLINNIVAEHPGNNSSKSNETLLDVMLRLKDSVEFPLTADNVKAIILDMFGAGTDTSSATVEWAISELIRCPRAMEKVQAELRQALKGKDKVKEEDIQDLSYLDLVIKETLRLHPPLPLVMPRECRQPVNLAGYDIANKTKLIVNVFAINRDPEYWKDAESFIPERFENSPITVMGAEYEYLPFGAGRRMCPGAALGLANVQLPLANILYHFNWKLPNGASHDQLDMTESFGATVQRKTHLVLVPSF
|
Involved in the biosynthesis of germacrene-derived sesquiterpene lactones . Catalyzes three consecutive oxidations of germacrene A to produce germacrene A acid . Could also catalyze the three-step oxidation of non-natural substrate amorphadiene to artemisinic acid .
|
D5JBW9
|
B0JZG0
|
S23A2_XENTR
|
Sodium-dependent vitamin C transporter 2
|
Silurana
|
MGIGRNPSSKAMESTNSTDGKYEEESKHTAFFTLPAVINGGAASSGDQDTEDTELMAIYTTESGIAEKSSLAETLDSTGSLDRQRLDMIYTVEDVPPWYLCIFLGLQHYLTCFSGTVAVPFLLAEAMCVGFDQWATSQLIGTIFFCVGITTLFQTTFGCRLPLFQASAFAFLAPARAILSLEKWKCNTTDLSITNGTELLHTEHIWYPRIREIQGAIIMSSLIEVVIGFLGLPGALLKYIGPLTITPTVSLIGLSGFQAAGERAGKHWGIAMLTIFLVLLFSQYARNVKLPLPIYKSKKGWTAYKLQLFKMFPIIMAILVSWLLCFIFTVTDVFPPDSSKYGYYARTDARQGVLTVAPWFKVPYPFQWGLPTVSAAGVIGMLSAVVASIIESIGDYYACARLSCAPPPPIHAINRGIFIEGLSCVLDGVFGTGNGSTSSSPNIGVLGITKVASRRVIQYGAAFMLLLGMIGKFSALFASLPDPVLGALFCTLFGMITAVGLSNLQFVDLNSSRNLFVLGFSIFFGLMLPSYLKQNPLVTGIAEIDQVLNVLLTTAMFVGGCTAFILDNTIPGTPEERGIRKWKRGVGKGTSGIEGMESYDLPFGMGFLRRYKCFSYLPISPTFAGYQWKALRKCGSCPRAAEEEPEPAV
|
Sodium/ascorbate cotransporter. Mediates electrogenic uptake of vitamin C, with a stoichiometry of 2 Na(+) for each ascorbate.
|
B0JZG0
|
Q74RF8
|
MALG_YERPE
|
Maltose/maltodextrin transport system permease protein MalG
|
Yersinia
|
MTKEEMQMAMVQPKSQRLRLLGTHFLMLCFIALIMFPLLMVIAISLRPGNFATGSLIPDQISWEHWKLALGMSVTHADGSVTPPPFPVMLWLWNSIKIALITAMGIVALSTTCAYAFARMRFRGKSALLKGMLIFQMFPAVLSLVALYALFDRIGQYMPFIGLNTHGGVIFAYMGGIALHVWTIKGYFETIDNSLEEAAALDGATPWQAFRLVLLPLSVPILAVVFILSFIAAITEVPVASLLLRDVNSYTLAVGMQQYLNPQNYLWGDFAAAAVLSAIPITTVFLLAQRWLVGGLTAGGVKG
|
Part of the ABC transporter complex MalEFGK involved in maltose/maltodextrin import. Probably responsible for the translocation of the substrate across the membrane.
|
Q74RF8
|
O66805
|
MURB_AQUAE
|
UDP-N-acetylmuramate dehydrogenase
|
Aquifex
|
MLFLKNVPLQNLTTIKIGGRVSFYAEPSDLKEISLCIDFSKSRDIPLFVLGNGSNTIFGDVRGLVVNLKNLKGFKVKEIKGKFFVEAFSGTPLKDLIRFSVKENVKSFYKLLGFPASVGGAVSMNAGAFGVEISDFLKEVYFVDWEGKLQKAKRDELNFSYRKSPFPKLGIVFKVVFEFERSKENILPKYEKIRRIRKEKQPINLPTSGSTFKNPEGNFAGKLLEKAGLKGFRLKNVGFSEKHANFLVNYGGGTFSEVVDLINIAKERVYENFGIVLEEEVKLIESSGSDGWKVLGA
|
Cell wall formation.
|
O66805
|
B9ISZ4
|
LRGA_BACCQ
|
Antiholin-like protein LrgA
|
Bacillus cereus group
|
MSTKKVYSFLSQAFIFSAIMLISNIIATHLPIPMPSSVIGLVILFSLLCLKVIKLEQVESLGTALTGIIGFLFVPSGISVINSLGVMGQYFVQILTVIVVATVILLAVTGLFAQFILGKDKKETEDTKELKVVNKGRKHGKVA
|
Inhibits the expression or activity of extracellular murein hydrolases by interacting, possibly with LrgB, with the holin-like protein CidA. The LrgAB and CidA proteins may affect the proton motive force of the membrane. May be involved in programmed cell death (PCD), possibly triggering PCD in response to antibiotics and environmental stresses.
|
B9ISZ4
|
Q980U7
|
HEM1_SACS2
|
Glutamyl-tRNA reductase
|
Saccharolobus
|
MSKDEELLQNYCSILFTYKTIGISNLHLYYFRETEIKSLKQLINAEFAILQTCNRVEIYLYSDTNTLKEVNKIIQYLNNIHNEPIGNQARVLCGKDAAKHLFLVASGADSLSIGEYEILSQIRSTIDMFKKLGFSGKYLQIFFERAIKVGRKVREETSISKGKVGIYSLAIDEAKKRFNDFYDRRILVIGAGEMAQKITSMLHNEGAKDVTIMNRTIEKAKQLALKFGYNYEKLDLDKLGNFDVAFISIYHENLRLENKWNTLIVDITVPPLFTGNNVITLEELERISNLNFKAREEELAKINKLVEDGINELLYDYKKEIYTEFMSKIMKRIETIRENEILRAYKELEKLGINDQQAKEILDLMTRSIIKKSFQPLFDNIRSLIFNGENSINYINFLIDIFKDGNISGFETEKIKEKQVSERSSI
|
Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
|
Q980U7
|
G7CFI3
|
EGTB_MYCT3
|
Sulfoxide synthase EgtB
|
Mycolicibacterium
|
MTGVAVPHRAELARQLIDARNRTLRLVDFDDAELRRQYDPLMSPLVWDLAHIGQQEELWLLRGGDPRRPGLLEPAVEQLYDAFVHPRASRVHLPLLSPAQARRFCATVRSAVLDALDRLPEDADTFAFGMVVSHEHQHDETMLQALNLRSGEPLLGSGTALPPGRPGVAGTSVLVPGGPFVLGVDLADEPYALDNERPAHVVDVPAFRIGRVPVTNAEWRAFIDDGGYRQRRWWSDAGWAYRCEAGLTAPQFWNPDGTRTRFGHVEDIPPDEPVQHVTYFEAEAYAAWAGARLPTEIEWEKACAWDPATGRRRRYPWGDAAPTAALANLGGDALRPAPVGAYPAGASACGAEQMLGDVWEWTSSPLRPWPGFTPMIYQRYSQPFFEGAGSGDYRVLRGGSWAVAADILRPSFRNWDHPIRRQIFAGVRLAWDVDRQTARPGPVGGC
|
Catalyzes the oxidative sulfurization of hercynine (N-alpha,N-alpha,N-alpha-trimethyl-L-histidine) into hercynyl-gamma-L-glutamyl-L-cysteine sulfoxide, a step in the biosynthesis pathway of ergothioneine.
|
G7CFI3
|
D5GHP2
|
AMPP2_TUBMM
|
Prolidase
|
Tuber
|
MTSDSTVDKILAGKYPAKQHAENVVERLLHVHPDLTDGVIYLESQRSKLYENSDQEVPFRQRRYFYYLSGCDLADSYLTYSIRDRKLTLFIPPIDPASVLWSGLPLSNSEALEKYDVDEVLPTSATALPTTSYSSLMFVIESQTSRTFHLQNTESLEPAIERARAIKDEYEVALIKKANRISALAHHSCLRAIKSAGNEREIEAVFTKECIANGAPKQAYSGIFGSGRSASTLHYVHNNQPLAGKLNLLLDAGAEYNNYASDITRTFPISGQFTKESREVYDIVLDMQKQCLAASKAGAVWDDIHILAHKVAIQGLLKIGVLRNGSVDEILSNRTSTAFLPHGLGHYLGMDTHDCGGNPNYADPDPMFKYLRKRGPLPAGAVITVEPGIYFCEFIIKPYLEDEKHAKYIDKDVLNRYWDVGGVRIEDNILITEGGYENLTNVAKEVDDMLKFING
|
Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides.
|
D5GHP2
|
P47441
|
RNH3_MYCGE
|
Ribonuclease HIII
|
Mycoplasma
|
MQHYKPADFYLIGSDESGKGDSFGGICVSAVLIEKKQLINLENLQVTDSKKLSDHTVKLLAKSIQTTVMDHHTITLDPKQYNDLTKSLKNTNLLLTNLHCQLYQKLLEKNQLLRQTVTISIDQFANQELFVNYLNKLTNFTDKTVLLPDQFLINGETKSLVIAAASILARDSFINQLQLLNQKVNYDLPKGSSHGIEQALLFLNQQRGFSQIEQFKQVAKLNFKNVTKFLQQLVY
|
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
|
P47441
|
P37255
|
PSBB_CHLRE
|
Protein CP-47
|
Chlamydomonas
|
MGLPWYRVHTVVINDPGRLISVHLMHTALVSGWAGSMALFEISVFDPSDPVLNPMWRQGMFVLPFMTRLGITQSWGGWTISGETATNPGIWSYEGVAAAHIILSGALFLASVWHWTYWDLELFRDPRTGKTALDLPKIFGIHLFLSGLLCFGFGAFHVTGVFGPGIWVSDPYGLTGRVQPVAPSWGADGFDPYNPGGIASHHIAAGILGVLAGLFHLCVRPSIRLYFGLSMGSIETVLSSSIAAVFWAAFVVAGTMWYGSAATPIELFGPTRYQWDQGFFQQEIQKRVQASLAEGASLSDAWSRIPEKLAFYDYIGNNPAKGGLFRTGAMNSGDGIAVGWLGHASFKDQEGRELFVRRMPTFFETFPVLLLDKDGIVRADVPFRKAESKYSIEQVGVSVTFYGGELDGLTFTDPATVKKYARKAQLGEIFEFDRSTLQSDGVFRSSPRGWFTFGHVCFALLFFFGHIWHGARTIFRDVFAGIDDDINDQVEFGKYKKLGDTSSLREAF
|
One of the components of the core complex of photosystem II (PSII). It binds chlorophyll and helps catalyze the primary light-induced photochemical processes of PSII. PSII is a light-driven water:plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation.
|
P37255
|
Q03AP9
|
RNY_LACP3
|
Ribonuclease Y
|
Lacticaseibacillus
|
MSSVTLVSITLAAVIALAVGLLIGFALQKKLHQNNLDRATQTAEGIIEAAKKEAATLKKEKLLEAKDENHRYRTQLEDELKDRRTEVQKSEHRLNQREDTLDRRDDTLDRKEQSLADREANLNKRQQQLDEREQDISSEISKQHTELERIAELTHEQARQQILDQTQSELTHERAVMIKESEDEAKEAADKKAKVLIADAIQRSASDIVAETTVTVVNLPNDDMKGRIIGREGRNIRTLETLTGIDLIIDDTPQAVVLSGFDPIRREIARIALEKLIQDGRIHPARIEEMVDKARKEMDDRIREIGEQAIFDVGIHNMHPDLIKILGRLHFRTSYGQNVLDHSIQVAKLTGVMAAELGEDVTLAKRAGLLHDIGKALDHEVDGSHVEIGVELATKYKEPKTVINAIASHHGDVEPTSVISVLVAAADAISAARPGARSESLENYLHRLEKLEAIANSHAGVDHSFAIQAGREVRVIVQPEKLSDDQSVILARDIRNEIEKELEYPGHIKVTVIRETRTVEYAK
|
Endoribonuclease that initiates mRNA decay.
|
Q03AP9
|
A8FP08
|
RS14Z_CAMJ8
|
30S ribosomal protein S14 type Z
|
Campylobacter
|
MAKKSMIAKAARKPKFKVRAYTRCQICGRPHSVYRDFGICRVCLRKMGNEGLIPGLKKASW
|
Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site.
|
A8FP08
|
Q9LIA8
|
UGDH2_ARATH
|
At-UGD2
|
Arabidopsis
|
MVKICCIGAGYVGGPTMAVIALKCPDVEVAVVDISVPRINAWNSDTLPIYEPGLDDVVKQCRGKNLFFSTDVEKHVREADIVFVSVNTPTKTRGLGAGKAADLTYWESAARMIADVSVSDKIVVEKSTVPVKTAEAIEKILTHNSKGIKFQILSNPEFLAEGTAIKDLFNPDRVLIGGRETPEGFKAVQTLKNVYAHWVPEGQIITTNLWSAELSKLAANAFLAQRISSVNAMSALCEATGADVTQVSYAVGTDSRIGPKFLNSSVGFGGSCFQKDILNLVYICECNGLPEVAEYWKQVIKINDYQKSRFVNRVVSSMFNSVSNKKIAVLGFAFKKDTGDTRETPAIDVCKGLLEDKARLSIYDPQVTEDQIQRDLSMNKFDWDHPLHLQPMSPTTVKQVTVTWDAYEATKDAHGICIMTEWDEFKNLDFQKIFDNMQKPAFVFDGRNIMNLQKLREIGFIVYSIGKPLDDWLKDMPAVA
|
Involved in the biosynthesis of UDP-glucuronic acid (UDP-GlcA), providing nucleotide sugars for cell-wall polymers. Required for the formation of cell wall ingrowths on the outer cell walls of nematode-induced syncytia.
|
Q9LIA8
|
A0A0E3D8Q2
|
JANB_PENJA
|
Janthitremanes biosynthesis cluster protein B
|
Penicillium
|
MDGFDVSQAPREYQAVKPLADLFVLGMGLGWVINYVGMVYTSFKERTYGMAIMPLCCNIAWEIVYCVFHPSKSRVELGVFAMGLLINFGVMYAAIIFSSREWSHAPLVERNLPWIFCIGVLGFLTGHLALAAEIGPSLAYSWGAVVCQLLLSVGGLCQLLCRGSTRGASYTLWLSRFLGSCCTVGFASLRWMYWPQSFAWLNSPLVLWSLAVFLMVDGSYGVCFWYVEQYEKSVLMGRATKAM
|
Terpene cyclase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes janthitremanes such as shearinine K or shearinine A . The geranylgeranyl diphosphate (GGPP) synthase janG catalyzes the first step in janthitremane biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase janC then forms 3-geranylgeranylindole (3-GGI) . Epoxidation by the FAD-dependent monooxygenase janM leads to a epoxidized-GGI that is substrate of the terpene cyclase janB for cyclization to yield paspaline . Paspaline is subsequently converted to 13-desoxypaspaline by the cytochrome P450 monooxygenase janP, via beta-PC-M6 in a series of alpha-face oxidations (Probable). The cytochrome P450 monooxygenase janQ is proposed to carry out sequential beta-face oxidation steps at C-7 and C-13 of 13-desoxypaspaline to form paspalicine and paspalinine respectively (Probable). The indole diterpene prenyltransferase janD may then convert paspalinine into shearinine K which is substrate of janO and/or additional enzymes for oxidation and cyclization to generate shearinine A (Probable).
|
A0A0E3D8Q2
|
O69540
|
IPYR_MYCLE
|
Pyrophosphate phospho-hydrolase
|
Mycobacterium
|
MQFDVTIEIPKGQRNKYEVDHKTGRVRLDRYLYTPMAYPTDYGFIEDTLGEDGDPLDALVLLPEPLFPGVLVEARPVGMFRMVDEHGGDDKVLCVPVNDHRWDHIHGIIDVPTFELDAIKHFFVHYKDLEPGKFVKAADWVGRDEAEAEVQRSVERFKAGGH
|
Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions.
|
O69540
|
A4XKX8
|
GUAA_CALS8
|
Glutamine amidotransferase
|
Caldicellulosiruptor
|
MQHEIVIVLDFGGQYNQLIARRVRECGVYCEIWPYDTPLEKIIEKNPKGIIFTGGPSSVYEENAPVVDKKIFEIGVPILGICYGNQLIAYFLGGKVSTALFREYGKTHIKYNTNSPLFTGLPESSICWMSHTDFVEELPEGFEILASTENCAIAAFGSREKKIYGVQFHPEVVHTEFGQEIIKNFLFNICGCKGDWKTSSFIEERINEIRKIVGNQKVVCALSGGVDSSVAAVLVHKAIGKNLFCIFVDHGLLRKGEAEEVIKTFKGQFDMNVIKVDAKERFLKALCGVIDPERKRKIIGEEFIRVFEEEASKLGDVKFLVQGTIYPDVVESGVGKAATIKSHHNVGGLPEHIKFERIIEPLRELFKDEVRRVGVELGIPEKIVKRQPFPGPGLAIRIIGEVTEEKLEILREVDWIFRKEIEACGLDEEIWQYFAVLTDMRSVGVMGDERTYDYTVALRAVTSVDGMTADWARIPYDVLERVSNEIVNTVRKVNRVVYDITSKPPATIEWE
|
Catalyzes the synthesis of GMP from XMP.
|
A4XKX8
|
A7HZL3
|
RL16_CAMHC
|
50S ribosomal protein L16
|
Campylobacter
|
MLMPKKTKYSKMMKGRNRGYAVRGIKLNFGDYGIKAVEAGRINSNQIEAARIAMTRYVNREAKVWINVFPDKPLTKKPLQTRMGKGKTGVEEWVMNIKPGRIIFELTGVNEDVARRALELSMHKLPFKTKIVTRESENEIY
|
Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs.
|
A7HZL3
|
P05452
|
TETN_HUMAN
|
Plasminogen kringle 4-binding protein
|
Homo
|
MELWGAYLLLCLFSLLTQVTTEPPTQKPKKIVNAKKDVVNTKMFEELKSRLDTLAQEVALLKEQQALQTVCLKGTKVHMKCFLAFTQTKTFHEASEDCISRGGTLGTPQTGSENDALYEYLRQSVGNEAEIWLGLNDMAAEGTWVDMTGARIAYKNWETEITAQPDGGKTENCAVLSGAANGKWFDKRCRDQLPYICQFGIV
|
Tetranectin binds to plasminogen and to isolated kringle 4. May be involved in the packaging of molecules destined for exocytosis.
|
P05452
|
B5ZY62
|
APT_RHILW
|
Adenine phosphoribosyltransferase
|
Rhizobium
|
MDKNTTSELAASIRSIPDYPKPGIIFRDITTLLGNPRAFRRAVDELVQPYAGTKIDKIAGMEARGFILGGAVAHQLSSGFVPIRKKGKLPHETVRIAYSLEYGVDEMEMHRDAVQPGEKVILVDDLIATGGTAVGATKLLRQIGAEVVGACFVIDLPDLGGRKKLEELGVVVHTLVEFSGH
|
Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
|
B5ZY62
|
P62647
|
CHEB_METMP
|
Protein-glutamate methylesterase/protein-glutamine glutaminase
|
Methanococcus
|
MSKIKVLIVDDSAFMRKVLEDILKSDDEIEVVATAKDGKEAFELVKKLEPNVITMDVEMPIMNGIDATKQIMAYKPTPILMLSAVTKQGSEATLKALDNGAVDFIEKPSGSVSLDIRKIGEKIIKQVKDASKSKVRIKSSRILENIKKEKQDESSTPKPQVEKTSGLSPEKLNDTAILIGSSTGGPPVVSSIISNIPKNTPPIFIVQHMPKGFTRVFAERMNNNSAITVKEAEHGEIVKPDHAYVAPGDSQMVLQKRGGNVYIIIDENMPKIHGTKPTVDVTAEYVTKYYGKNTIGVLLTGIGRDGANGLKMVKNKGGYTIAQNQDTCVIYGMPKTAIEMNVVDKVMDPIDIPLEIIKFAKKIGG
|
Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid.
|
P62647
|
Q03190
|
CXA4_RAT
|
Connexin-37
|
Rattus
|
MGDWGFLEKLLDQVQEHSTVVGKIWLTVLFIFRILILGLAGESVWGDEQSDFECNTAQPGCTNVCYDQAFPISHIRYWVLQFLFVSTPTLIYLGHVIYLSRREERLRQKEGELRALPSKDPHVERALAAIEHQMAKISVAEDGRLRIRGALMGTYVISVLCKSVLEAGFLYGQWRLYGWTMEPVFVCQRAPCPHVVDCYVSRPTEKTIFIIFMLVVGVISLVLNLLELVHLLCRCVSREIKARRDHDTRPAQGSASDPYPEQVFFYLPMGEGPSSPPCPTYNGLSSTEQNWANLTTEERLTSTRPPPFVNAAPQGGQKSSSRPNSSASKKQYV
|
One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.
|
Q03190
|
P0DKM4
|
TU25_LOPOL
|
OL25
|
Iotyrris
|
SLVCDLECSAEVTTCCETGTCHGITTYNCVGGTEPET
|
Acts as a neurotoxin by inhibiting an ion channel.
|
P0DKM4
|
Q0BQY5
|
ATPF1_GRABC
|
F-type ATPase subunit b 1
|
Granulibacter
|
MLLGTVVTVLSTLPAIAYAMDPESPEHEGMPQLNFANPLTTSQVVWMALILLAFYLLLSKWALPQVSQVVDDRNASIMGDLDSAHLAKAEANAAVEEMNDAIRRANLEGQAEIEKTVSAAKAKAQQEAAEAHARLERQLADAEARIASSRDTAMGALRDVATDTTQALIARLTGQFPAQDTVEQAVGQALAARS
|
Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
|
Q0BQY5
|
Q9Y8K3
|
MTRB_METBF
|
N5-methyltetrahydromethanopterin--coenzyme M methyltransferase subunit B
|
Methanosarcina
|
MSMIRIAPELNLVMDPETGTITQERKDSIQYSMEPVFERVDKLDAIADDLVNSLSPSNPLLNSWPGRENTSYMAGFYGNTFYGVIIGLAFSGLLALVIYIASLMRGVV
|
Part of a complex that catalyzes the formation of methyl-coenzyme M and tetrahydromethanopterin from coenzyme M and methyl-tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step.
|
Q9Y8K3
|
C4L3F5
|
EX7L_EXISA
|
Exodeoxyribonuclease VII large subunit
|
unclassified Exiguobacterium
|
MANPLPVSEVVRYVKRQLDDDVLLRQVAVIGEISNFKRYSSGHCYFTLKDDASRMKAVMFSRDAKQLQFEPKDGMKVIAVSKVTMYEATGDVQLYVELMRQDGIGLLFERYEARKRELEEMGWFDDERKKPLPMFPERVGIVTSPKGAALHDIATTLRRRAPHVAITFAPVAVQGEMAAPQVASAIRWMNERTDCDVLIVGRGGGSIEELWAFNEDVVVEAIYASTIPIISAVGHETDFTLSDFVADVRAATPTAAAELATAMIDAQRKDVERLDNHLHKAVRSQLDESRSRVERMINSYGLKSPRYTISQKRERFAQSEIRLEQGMRRHLTQATHQLRQLSQQLDVKRFSKTLSKQGDEVNHMVERLRRTRPLEQATLQFAQQVGRLHAVSPLAVLSRGYTFIEQDGAYVQNVKQLRDGDVSIRFRDGHAIAEVKERIVGDEERTDI
|
Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
|
C4L3F5
|
Q7WH65
|
NAGZ_BORBR
|
N-acetyl-beta-glucosaminidase
|
Bordetella
|
MSSKKKTKPVLPPGPVMVDVAGTTLTKDEKRRLRNPLVGGVILFARNFTDRRQLCALTRAIHKARKEPLLIAVDHEGGRVQRFRDDGFTALPPMQELGKLWDRDPLAAMRLATEAGYVLAAELRACGVDLSFTPVLDLDYGVSKVIGNRAFHHDARVVTMLSRALAQGLALAGMAACGKHFPGHGFVGADSHHEIPVDPRPLARILKDDAAPYAWLGDLVMPAVMPAHVIYPKVDAQPAGFSRRWVSEILRERLGYDGVVFSDDLTMEGASVAGDILARAEAALGAGCDMVLVCNRPDLADELLDRLQVQHPAASVERIRRLMPRFAAPDWDTLQNDSRYQHARRLQSQIVSG
|
Plays a role in peptidoglycan recycling by cleaving the terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from peptide-linked peptidoglycan fragments, giving rise to free GlcNAc, anhydro-N-acetylmuramic acid and anhydro-N-acetylmuramic acid-linked peptides.
|
Q7WH65
|
C6E524
|
PSD_GEOSM
|
Phosphatidylserine decarboxylase beta chain
|
unclassified Geobacter
|
MRNTDTPIAVEGYPFIAGFAAATLLLALLGQFLHLGFFVPATLFFVLTVFTVFFFRNPERVTPGDENTVVAPADGEVIFLGKVIEPHTNGEFEKISIFMSVFNVHVNRAPISGKVVDGFYTKGKFFDVRDERASFENEQQGLVLETAAGLRMVVVQVAGLIARRIVCYAKTGDSLSRGRRYGLIRFGSRLDIYLPLGTRIDLVMGQKTVAGETVLGILP
|
Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
|
C6E524
|
O18211
|
MO25M_CAEEL
|
MO25-like protein 2
|
Caenorhabditis
|
MLKPLFGKADKTPADVVKNLRDALLVIDRHGTNTSERKVEKAIEETAKMLALAKTFIYGSDANEPNNEQVTQLAQEVYNANVLPMLIKHLHKFEFECKKDVASVFNNLLRRQIGTRSPTVEYLAARPEILITLLLGYEQPDIALTCGSMLREAVRHEHLARIVLYSEYFQRFFVFVQSDVFDIATDAFSTFKDLMTKHKNMCAEYLDNNYDRFFGQYSALTNSENYVTRRQSLKLLGELLLDRHNFSTMNKYITSPENLKTVMELLRDKRRNIQYEAFHVFKIFVANPNKPRPITDILTRNRDKLVEFLTAFHNDRTNDEQFNDEKAYLIKQIQELRV
|
Regulates asymmetric cell division in Q.p neuroblast lineage . Plays a role in cell shedding during embryogenesis .
|
O18211
|
A0QKZ7
|
RL6_MYCA1
|
50S ribosomal protein L6
|
Mycobacterium avium complex (MAC)
|
MSRIGKQPVPVPAGVDVTIDGQKVSVKGPKGTLDLTVAEPITVSRNDDGAIVVTRPNDERRNRSLHGLSRTLVSNLVTGVTQGYTTKMEIFGVGYRVQLKGSNLEFALGYSHPVVIEAPEGITFAVQSPTKFSISGIDKQKVGQISANIRRLRRPDPYKGKGVRYEGEQIRRKVGKTGK
|
This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center.
|
A0QKZ7
|
Q0TJT3
|
6PGL_ECOL5
|
6-phosphogluconolactonase
|
Escherichia
|
MKQTVYIASPESQQIHVWNLNHEGALTLTQVVDVPGQVQPMVVSPDKRYLYVGVRPEFRVLAYRIAPDDGALTFAAESALPGSPTHISTDHQGQFVFVGSYNAGNVSVTRLEDGLPVGVVDVVEGLDGCHSANISPDNRTLWVPALKQDRICLFTVSDDGHLVAQDPAEVTTVEGAGPRHMVFHPNEQYAYCVNELNSSVDVWELKDPHGNIECVQTLDMMPENFSDTRWAADIHITPDGRHLYACDRTASLITVFSVSEDGSVLSKEGFQPTETQPRGFNVDHSGKYLIAAGQKSHHISVYEIVGEEGLLHEKGRYAVGQGPMWVVVNAH
|
Catalyzes the hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
|
Q0TJT3
|
P43221
|
TLPA_BRADU
|
Cytochrome c biogenesis protein TlpA
|
Bradyrhizobium
|
MLDTKPSATRRIPLVIATVAVGGLAGFAALYGLGLSRAPTGDPACRAAVATAQKIAPLAHGEVAALTMASAPLKLPDLAFEDADGKPKKLSDFRGKTLLVNLWATWCVPCRKEMPALDELQGKLSGPNFEVVAINIDTRDPEKPKTFLKEANLTRLGYFNDQKAKVFQDLKAIGRALGMPTSVLVDPQGCEIATIAGPAEWASEDALKLIRAATGKAAAAL
|
Involved in cytochrome aa3 assembly.
|
P43221
|
C6AQU6
|
TRMA_AGGAN
|
tmRNA (uracil(341)-C(5))-methyltransferase
|
Aggregatibacter
|
MQNLPVTHYSALLAEKQEKLTALLAPFNAPNLQVFASPTQHFRMRAEFRIWHEGDDFYHIMFDQQSKQRYRVDNFPIASELINRMMTALLPLLKQQTVLHHRLFQIDYLSTQSQHIIVSLLYHKALDEDWQAAAQTLRSQLQQQGFNVQIVGRASKQKICLEQDYVDEILRVHGKDYIYRQVENSFTQPNATVNSKMLEWAVDCTRNSHGDLLELYCGNGNFSIALAQNFRKVLATEIAKPSVAAAQFNIAANQINNLQIIRMSAEEFTQAMQGVREFNRLKGIDLKAYECNTIFVDPPRAGLDADTVKLVQQYERILYISCNPHTLCDNLQTLSQTHRIEKAALFDQFPYTEHMEAGVWLVRKG
|
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).
|
C6AQU6
|
Q2QW55
|
MAD33_ORYSJ
|
OsMADS33
|
Oryza sativa
|
MVRGKVQMRRIENPVHRQVTFCKRRGGLLKKARELSVLCDADVGVIIFSSQGKLHELATNGNMHNLVERYQSNVAGGQMEPGALQRQQVAEQGIFLLREEIDLLQRGLRSTYGGGAGEMTLDKLHALEKGLELWIYQIRTTKMQMMQQEIQFLRNKEGILKEANEMLQEKVKEQQKLYMSLLDLHSQQPTQPMTYGNRFFSI
|
Probable transcription factor.
|
Q2QW55
|
Q5RF97
|
BCD1_PONAB
|
Zinc finger HIT domain-containing protein 6
|
Pongo
|
MEFAAENEGKSGGGLHSVAEGVRLSPEPGREGVRDLAGAEEFGGGEEGKGLTGVKEIGDGEEGSRQRPEEIPMDLTVVKQEIIDWPGTEGRLAGQWVEQEVEDRPEVKDENAGVLEVKQETDSSLVVKEAKVGDLEVKEEVMDSSEVKEEKDNLEIKQEEKFVGQCIKEELMHGECVKEEKDFLKKEIVDDTKVKEEPPINHPVGCKRKLAMSRCETCGTEEAKYRCPRCMRYSCSLPCVKKHKAELTCNGVRDKTAYISIQQFTEMNLLSDYRFLEDVARTADHISRDAFLKRPISNKHMYFMKNRARRQGINLKLLPNGFTKRKENSTFFDKKKQQFCWHVKLQFPQSQAEYIEKRVPDDKTINEILKPYIDPEKSDPVIRQRLKAYIRSQTGVQILMKIEYMQQNLVRYYELDPYKSLLDNLRNKVIIEYPTLHVVLKGSNNDMKVLRQVKSESTKNLGNEN
|
Required for box C/D snoRNAs accumulation involved in snoRNA processing, snoRNA transport to the nucleolus and ribosome biogenesis.
|
Q5RF97
|
Q3ALC4
|
CLPP3_SYNSC
|
Endopeptidase Clp 3
|
unclassified Synechococcus
|
MPIGTPSVPYRLPGSQMERWVDIYTRLGVERILFLGSEVNDGIANSLVAQMLYLDSEDSSKPIYLYINSPGGSVTAGLAIYDTIQYVKSEVVTICVGLAASMGAFLLAAGTKGKRVALPHSRIMIHQPLGGTSRRQASDIEIEAREILRMKEMLNRSLSDMSGQSFEKIEKDTDRDYFLSAEEAKEYGLIDRVISHPNEA
|
Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
|
Q3ALC4
|
Q3UEZ8
|
NTCP4_MOUSE
|
Solute carrier family 10 member 4
|
Mus
|
MDSLDNTTLLLAPSSLLPDNLTLSPNAGSPSASTLSPLAVTSSPGPGLSLAPSPSIGFSPEATPTPEPTSSSLTVGVAGQGSSAFPRPWIPHEPPFWDTPLNHGLNVFVGAALCITMLGLGCTVDVNHFGAHVRRPVGALLAALCQFGFLPLLAFLLALIFKLDEVAAVAVLLCGCCPGGNLSNLMSLLVDGDMNLSIIMTISSTLLALVLMPLCLWIYSRAWINTPLVQLLPLGAVTLTLCSTLIPIGLGVFIRYKYNRVADYIVKVSLWSLLVTLVVLFIMTGTMLGPELLASIPATVYVVAIFMPLAGYASGYGLATLFHLPPNCKRTVCLETGSQNVQLCTAILKLAFPPRFIGSMYMFPLLYALFQSAEAGVFVLIYKMYGSEILHKREALDEDEDTDISYKKLKEEEMADTSYGTVGTDDLVMMETTQTAL
|
Transporter for bile acids.
|
Q3UEZ8
|
A4IR71
|
GREA_GEOTN
|
Transcript cleavage factor GreA
|
Geobacillus
|
MANEKQYPMTKEGKEKLEQELEYLKTVKRKEVVERIKIARGFGDLSENSEYDAAKDEQAFVESRIQMLETMIRNAVIIEEDKENPDVVSLGKSVTFIELPDGEEETYTIVGSAEADPFEGKISNDSPIAKSLIGHRVGDEVTVQTPGGEMLVKIVAVK
|
Necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by cleavage factors such as GreA or GreB allows the resumption of elongation from the new 3'terminus. GreA releases sequences of 2 to 3 nucleotides.
|
A4IR71
|
B8CMW5
|
ISCS_SHEPW
|
Cysteine desulfurase IscS
|
Shewanella
|
MKLPIYLDYAATTPVDPRVAEKMMQCMTMDGIFGNPASRSHRYGWQAEEAVDIARNQIAELINADPREIVFTSGATESDNLAIKGVAHFYQKKGKHIITSKTEHKAVLDTCRQLEREGYEVTYLQPEANGLIPVAMIEAAMREDTLLVSIMQVNNEIGVIQDIDAIGELCRSRKIVFHVDAAQSAGKMPIDVQKTKVDLMSISAHKMYGPKGIGALYVSRKPRIRLEAAMHGGGHERGMRSGTLATHQIVGFGEAAAIAKTDMDSDNERIRRLRDKLWNGINHIEETYINGDMEQRHCGSLNVSFNFVEGESLMMALKDLAVSSGSACTSASLEPSYVLRALGLNDEMAHSSIRFSIGRFTTDEEIEHAIETITESIGNLREMSPLWEMFKDGIDLDSVQWAHH
|
Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins.
|
B8CMW5
|
Q7NWP4
|
SYE_CHRVO
|
Glutamyl-tRNA synthetase
|
Chromobacterium
|
MIRTRFAPSPTGYLHIGGVRTALFSWAYARKNNGVFVLRIEDTDLERSTPESVKAILDGMHWVGLDYDEGPFYQTHRFDRYKEVIQQLLDSGHAYHCYCSKEELEAMRAEQEARGDKPRYDRRWRPEAGKTLPAIPEGVQPVVRFKTPLSGVVAWDDAVKGRIEISNEELDDLIIARPDGSPTYNFCVVVDDWDMRITHVIRGDDHVNNTPRQINILKALNAPLPVYGHLPMILNEDGQKMSKRRDAVSVVDYADKGILPEALLNYLARLGWGHGDDEFFSMEQFVEWFSLEAVSPSASRFNHEKFMWLNAQHIKAADNARLAELIAPRLAAAHVDTAHGPAIGDVLALVKERVQDLNALALEVDYFYKKREPAAADVEKHLAGDAVERMGRFADRLAALEAWTAESIHELFKPFCADEGIKMGQLGMPLRVLVCGTTQTPSVDAVLALIGKEEVLRRIRG
|
Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
|
Q7NWP4
|
O08850
|
RGS5_MOUSE
|
Regulator of G-protein signaling 5
|
Mus
|
MCKGLAALPHSCLERAKEIKIKLGILLQKPDSAVDLVIPYNEKPEKPAKAHKPSLEEVLQWRQSLDKLLQNSYGFASFKSFLKSEFSEENLEFWVACENYKKIKSPIKMAEKAKQIYEEFIQTEAPKEVNIDHFTKDITMKNLVEPSPRSFDLAQKRIYALMEKDSLPRFVRSEFYKELIK
|
Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds to G(i)-alpha and G(o)-alpha, but not to G(s)-alpha.
|
O08850
|
Q8MUF4
|
CECB_ANOGA
|
Cecropin-B
|
Anopheles
|
MNFTKLFILVAIAVLVVVGVQPVDGAPRWKFGKRLEKLGRNVFRAAKKALPVIAGYKALG
|
Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria.
|
Q8MUF4
|
Q5X8X9
|
LPXD1_LEGPA
|
UDP-3-O-acylglucosamine N-acyltransferase 1
|
Legionella
|
MNSSLRDIANLVQGMVIGNDAITVSTLSPIDNILPGSLVFAEGEDNIKLAENSEAAAILIGQGTIDSPKPLIQVKNPFKAFIALLNHFYPPRRISPGVHPTAVIGAEVQLGDEVYVGPFVVIESGSIIGNHSVLKSHIHIGHNVVIGDHTTIHPQVTIYDNCRIGSNVTIHASTVIGSDGFGYTFVDGQHLKVPHSGYVVIENNVEIGANTAIDKATLGATVIGEGTKIDNLVQIAHSVKLGKHNIICAFTGIAGSTTTGNNVIFAANVGVSDHVHIEDEVILGARTGVPPHKHLKKGTVYLGNPAKPKDVAIKHELSVNRIPLIRKNIKSLTEQVAVINKKLDIKAKEVE
|
Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
|
Q5X8X9
|
Q48KR3
|
ZIPA_PSE14
|
Cell division protein ZipA
|
Pseudomonas
|
MEIGLREWLIVIGIIVIAGILFDGWRRMRGSKGKLKFRLDRSFSNLPDEEETTSAEVLGPPRVLDTHKEPQLDEHDLPSMSASPREGKRSNSDKRGNSDKKRKDEPQQGDLNLDLDGPSLFTGRDDDFPDDKPAQRITEDKDLPPVEEVLVISVISRSEGGFKGPALLQNILESGLRFGEMDIFHRHESMAGNGEVLFSMANAVKPGVFDLDDIDHFSTRAVSFFLGLPGPRHPKQAFDVMVAAARKLAHELDGELKDDQRSVMTAQTIEHYRQRIVEFERRALTQRRG
|
Essential cell division protein that stabilizes the FtsZ protofilaments by cross-linking them and that serves as a cytoplasmic membrane anchor for the Z ring. Also required for the recruitment to the septal ring of downstream cell division proteins.
|
Q48KR3
|
P40161
|
RT106_YEAST
|
Regulator of Ty1 transposition protein 106
|
Saccharomyces
|
MSKLFLDELPESLSRKIGTVVRVLPSSLEIFEELYKYALNENSNDRSGRHKKPRIDVSSDLLKTDEISETNTIFKLEGVSVLSPLRKKLDLVFYLSNVDGSPVITLLKGNDRELSIYQLNKNIKMASFLPVPEKPNLIYLFMTYTSCEDNKFSEPVVMTLNKENTLNQFKNLGLLDSNVTDFEKCVEYIRKQAILTGFKISNPFVNSTLVDTDAEKINSFHLQCHRGTKEGTLYFLPDHIIFGFKKPILLFDASDIESITYSSITRLTFNASLVTKDGEKYEFSMIDQTEYAKIDDYVKRKQMKDKSMSEELKAKSKSKGQATDGTADQPSILQEATRQMQDEKKAGVFSDDDEENDQNFEAESDLSDGSGQESSDGAEDGEEAEEDDEEDDEEEDKKGQSALNRDNSFASINGQPEQELQYKEFKEPLELEDIPIEIDNDDDEDDEDGSGVEYD
|
Histones H3 and H4 chaperone involved in the nucleosome formation and heterochromatin silencing. Required for the deposition of H3K56ac-carrying H3-H4 complex onto newly-replicated DNA. Plays a role in the transcriptional regulation of the cell-cycle dependent histone genes by directly recruiting the SWI/SNF and RSC chromatin remodeling complexes to the histone genes in a cell cycle dependent manner. In cooperation with HIR and ASF1, creates a repressive structure at the core histone gene promoter and contributes to their repression outside of S phase. Involved in regulation of Ty1 transposition.
|
P40161
|
Q9MV56
|
MATK_CEDAT
|
Intron maturase
|
Cedrus
|
MDEFHRYGKEDSSWQQCFLYPLFFQEDLYAISHDHYLDGSSSSEPMEHFSFNDQLSFLTVKRLIGRIREQNHSIGLFVNCDPNPLVDRNKSSYFESVLEGLTLVLEVPFSTRSKYSVQGIKEWKSFRSIHSIFPFLEEKFPHSNYILDTRIPYSIHPEFLVRTFRRWIQDAPSLHPLRSVLYEYRNSPENLQRSIIVAPRVNTRFFLFLWNHYAYECESILVPLLKRSFQSRSSSHGSFPERTLFDRKIKHIIRISHRNSLKSIWFLKDPKIHYVRYGERSIIAIKGTHLLVKKCRYYLPIFRQCYFHLWSEPYRVCSHQLSKNCSSFPGYSLGVRMKPLLVRTKMPGELFITDLITDEFYPIVPIVSIIGLLAREKFCDISGRPISKLAWTSLTDDDILDRFDRIWRNFFHYYSGSFGRDGLYRIKYILSLSCAKTLACKHKSTIRVVRKELGPELFKKSFSKEREFDSPAFSSKAVARSQRERIWHSDIPQINPLANSWQKIQDLKIKNLFDQ
|
Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns.
|
Q9MV56
|
B5X582
|
TWIH_ARATH
|
DNA primase
|
Arabidopsis
|
MRFLLRLPQIHFRKLSCSMSVLMGSKQFLEFCLLPSFASYPSSPSYSSSRQVSSVSRRFRPVLASRPVSKNSPYYQRTNGLSSYNSIPRVPTPVDTEVEADKRVVLSRLVTLRRKLAEQGVDAENCPPGQHSGLICPTCEGGNSGEKSLSLFIAPDGSSATWNCFRGKCGLKGGVRADGGLASADPIEKVERKITVEGIELEPLCDEIQDYFAARAISRKTLERNRVMQKRIGDEIVIAFTYWQRGELVSCKYRSLTKMFFQERKTRRILYGLDDIEKTSEVIIVEGEIDKLAMEEAGFLNCVSVPDGAPAKVSSKEIPSEDKDTKYKFLWNCNDYLKKASRIVIATDGDGPGQAMAEEIARRLGKERCWRVKWPKKSEDEHFKDANEVLMSKGPHLLKEAILDAEPYPILGLFSFKDFFDEIDAYYDRTHGHEYGVSTGWKNLDNLYSVVPGELTVVTGIPNSGKSEWIDAMLCNLNHSVGWKFALCSMENKVRDHARKLLEKHIKKPFFDADYGRSVQRMSVEEKDEGKKWLNDTFYPIRCEMDSLPSIDWVLERAKAAVLRYGIRGLVIDPYNELDHQRTPRQTETEYVSQMLTKIKRFSQHHSCHVWFVAHPKQLQHWDGGAPNLYDISGSAHFINKCDNGIIVHRNRDENAGPLDLVQIGVRKVRNKVAGQIGDAYLCYDRTTGSYSDSPVTPGMPERRSPKRY
|
Has both DNA primase and DNA helicase activities and may be involved in organelle DNA replication. Capable of producing RNA primers of 9 to 18 bases from a single-stranded DNA template.
|
B5X582
|
P38819
|
ERP5_YEAST
|
Protein ERP5
|
Saccharomyces
|
MKYNIVHGICLLFAITQAVGAVHFYAKSGETKCFYEHLSRGNLLIGDLDLYVEKDGLFEEDPESSLTITVDETFDNDHRVLNQKNSHTGDVTFTALDTGEHRFCFTPFYSKKSATLRVFIELEIGNVEALDSKKKEDMNSLKGRVGQLTQRLSSIRKEQDAIREKEAEFRNQSESANSKIMTWSVFQLLILLGTCAFQLRYLKNFFVKQKVV
|
Involved in vesicular protein trafficking.
|
P38819
|
P01624
|
KV315_HUMAN
|
Ig kappa chain V-III region POM
|
Homo
|
MEAPAQLLFLLLLWLPDTTGEIVMTQSPATLSVSPGERATLSCRASQSVSSNLAWYQQKPGQAPRLLIYGASTRATGIPARFSGSGSGTEFTLTISSLQSEDFAVYYCQQYNNWP
|
V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition . Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens . The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen .
|
P01624
|
Q0SQE5
|
RL4_CLOPS
|
50S ribosomal protein L4
|
Clostridium
|
MPKVGLFNKEGQQVGDIQLNEQVFGVEVNKYALHQVVVAQLANKRQGTQSAKTRSEVRGGGIKPWRQKGTGRARQGSIRAPQWIKGGVVFAPKPRDYRMSIPKSMRKVAMTSALTSKVADMVVLEDLNFEAPKTKEAVKMLNAFEAKKTLIITAEVNENVYKSARNIEGVTVMPVNNINVYDLLNCKTLMITKEAVNKIEEVYA
|
Forms part of the polypeptide exit tunnel.
|
Q0SQE5
|
Q68WF6
|
GYRB_RICTY
|
DNA gyrase subunit B
|
typhus group
|
MSGIEEKCNESSYSADSIKVLKGLEAVRKRPGMYIGDVGDGSGLHHMIYEVVDNSIDEALAGYCDLIRVTLNKNGSVTVSDNGRGIPVEIHEEEGISAAEVIMTQLHAGGKFDQHSYKISGGLHGVGVSVVNALSEWLELRIWRNNKEYFIRFNNGITEAPLSIVKENIDKKGTEVTFFPSVGIFTNIEFDFVTIEHRLRELAFLNSGVKILLIDNRFEEVKKVEFFYTGGIEAYVQYIDRAKHAIHPCIVVNTEHVESGISLELAIHWNDSYHENILCFTNNIRQRDGGTHLSAFKSAITRVITSYLDTTGLNKKTKHDFSGEDTREGICCVLSVKVPDPKFSSQTKDKLVSSEVRPVVENAVYTKVLEWFEEHPIEAKAIIAKIMEAANAREAARKARELTRRKSALEVSNLPGKLADCHAKDPAISELFIVEGDSAGGTAKQGRDSKIQAILPLRGKILNVERARFDKMLSSEQIGTLITALGISVEREFSLEKLRYHKVIIMTDADVDGSHIRTLLLTFFYRHMPELINKGYLYIAQPPLYKVKSGASELYLKNEQALQNYLIKSTINDTKLILDGQEQLIGYNLEDLINKVVQFNCLLDRASKKFNRSITEILAINDLFNKKIFEPESGSRLQKALDVLNNLEESPDKTNLQVLKHENRIEFFHFSRGLKNTKILLKEQLELFEFVEISQFALSIFDIFSKRLKLIVKGKEFDVVTPSQLLNTIIECGKKGITIQRFKGLGEMNSDQLWDTTLDPTKRTLLQVRVSEVDEAEGIFSTLMGDVVEPRRLFIQANALNVMNLDI
|
A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.
|
Q68WF6
|
P20897
|
VM1H2_CRORU
|
Ruberlysin
|
Crotalus
|
QNLPQSYIELVVVADHRMFMKYNSDLNTIRTRVHEIVNFINEFYRSLNIRVSLTDLEIWSDQDFITVQSSAKNTLHSFGEWRKSVLLNRKRHDNAQLLTAIVLDDYTLGLAYLNSMCHPRNSVGLIQDHSPINLLMGVTMAHELGHNLGMEHDGKDCLRGASLCIMRPGLTPGRSYEFSDASMRYYQKFLDQYKPQCILNKP
|
This protein is a zinc protease from snake venom that induces hemorrhage.
|
P20897
|
A8HS37
|
RLMH_AZOC5
|
rRNA (pseudouridine-N3-)-methyltransferase RlmH
|
Azorhizobium
|
MRVLLICVGRLKAGAERELVTRYLDRAKAGGRALGLSGFDTIELSESAARRPEDRMAEEGQAILGALPQGADVIALDPRGKNLTSEAFAERVRTGRDGGRPAAAFLIGGADGLSEAVRARCDLMLAFGAATFPHQIVRAMLAEQVYRATTILAGHPYHRA
|
Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
|
A8HS37
|
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