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
|
|---|---|---|---|---|---|---|
Q2NU39
|
ACP_SODGM
|
Acyl carrier protein
|
Sodalis
|
MSTIEESVKAIIAEQLGVKKEEVVNNASFVDDLGADSLDTVELVMALEEEFDTEIPDEEAEKITTVQAAIDFIQASQQ
|
Carrier of the growing fatty acid chain in fatty acid biosynthesis.
|
Q2NU39
|
Q6GLG7
|
UBA5_XENTR
|
UFM1-activating enzyme
|
Silurana
|
MEKLIEELRSRVSELEEELHRVRNGEQVHEGHRAKINTMSAEVVDSNPYSRLMALKRMGIVEDYEKIRTFTVAVVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVEMANMNRLFFQPHQAGLSKVEAAEHTLRNINPDVQFEVHNYNITTLDNFQHFMDRISKGGLKEGTPVDLVLSCVDNFEARMAINTACNELVQIWMESGVSENAVSGHIQLIKPGETACFACAPPLVVAANIDEKTLKREGVCAASLPTTMGVVAGMLVQNVLKYLLNFGTVSFYLGYNAMQDFFPTMAMKPNPQCGDKYCRKQQEEFKLKEAARPKQEPIVVKEEEIVHEDNDWGIELVSEVSEEELKAASGPVPELPEGIKVAYTVPITEPTSGFIVEDSEQSLDELMAQMKNL
|
E1-like enzyme which specifically catalyzes the first step in ufmylation. Activates ufm1 by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ufm1-E1 thioester and free AMP. Activates ufm1 via a trans-binding mechanism, in which ufm1 interacts with distinct sites in both subunits of the uba5 homodimer. Trans-binding also promotes stabilization of the uba5 homodimer, and enhances ATP-binding. Transfer of ufm1 from uba5 to the E2-like enzyme UFC1 also takes place using a trans mechanism. Ufmylation is involved in reticulophagy (also called ER-phagy) induced in response to endoplasmic reticulum stress.
|
Q6GLG7
|
Q22782
|
RAB6B_CAEEL
|
Ras-related protein rab-6.2
|
Caenorhabditis
|
MSDFGNPLKKFKLVFLGEQSVGKTSLITRFMYDSFDNTYQATIGIDFLSKTMYLEDRTVRLQLWDTAGQERFRSLIPSYIRDSTVAVVVYDITNSNSFHQTSKWIDDVRTERGSDVIIMLVGNKTDLSDKRQVTTDEGERKAKELNVMFIETSAKAGYNVKQLFRRIAGALPGIIKDDPVEPPNVVTMDPIRQRQIVTDEGSCWC
|
The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes . Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion . In its active GTP-bound form, acts redundantly with rab-6.1 (in its active GTP-bound form) to positively regulate the retrograde trafficking of cargo molecules from endosomes to the Golgi compartment . Required for the retrograde trafficking of glr-1, a subunit of AMPA-type glutamate receptors (AMPRs), out of early endosomes and into the Golgi compartment in neurons . Its role in glr-1 trafficking may partly be mediated by its interaction with lin-10 and association with components of the retromer complex such as rme-8 . Together with rab-6.2, promotes the retrograde trafficking of mig-14 from endosomes to Golgi structures in the intestine . Plays a role in the epidermis to promote cuticle integrity and impermeability of the cuticle barrier to exogenous molecules . May have a role in the glycosylation of the cuticular surface . Required for seam cell division and alae formation . Required for grinder formation, which is the feeding organ that breaks down food . In contrast to rab-6.1, may play a minor role in the exocytosis of secretory vesicles (cortical granules) during the oocyte-to-embryo transition .
|
Q22782
|
Q0AJE1
|
MURG_NITEC
|
Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase
|
Nitrosomonas
|
MIMAGGTGGHVFPGLAVARAMQAEGWRVIWLGTRNGMEATLVPQHGFTIELINFSGLRGKKPVSYLLLPWRLAKACWQSFCILRRQRPQIVLGMGGYPALPGGIMAVLSGKPLLIHEQNRIAGLTNKILAKIASRILLAFPGTITDQAGKIQVTGNPVRTEIAQLPSPEVRYAKRAGKLNILVVGGSLGAQALNTVLPQALSMIPGNQRPFVTHQSGKVHLAALQQAYAEHGVTGNLVAFIEDMAVYYQNCDLVVCRAGALTIAELAAAGVASILVPYPYAVDDHQTANARFLSEHHAAVLWPQSELTANSLAQWLMTCTRTQLQTMAINARMLAMPEAAQSVVTVCQQLIETGP
|
Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
|
Q0AJE1
|
P51160
|
PDE6C_HUMAN
|
cGMP phosphodiesterase 6C
|
Homo
|
MGEINQVAVEKYLEENPQFAKEYFDRKLRVEVLGEIFKNSQVPVQSSMSFSELTQVEESALCLELLWTVQEEGGTPEQGVHRALQRLAHLLQADRCSMFLCRSRNGIPEVASRLLDVTPTSKFEDNLVGPDKEVVFPLDIGIVGWAAHTKKTHNVPDVKKNSHFSDFMDKQTGYVTKNLLATPIVVGKEVLAVIMAVNKVNASEFSKQDEEVFSKYLNFVSIILRLHHTSYMYNIESRRSQILMWSANKVFEELTDVERQFHKALYTVRSYLNCERYSIGLLDMTKEKEFYDEWPIKLGEVEPYKGPKTPDGREVNFYKIIDYILHGKEEIKVIPTPPADHWTLISGLPTYVAENGFICNMMNAPADEYFTFQKGPVDETGWVIKNVLSLPIVNKKEDIVGVATFYNRKDGKPFDEHDEYITETLTQFLGWSLLNTDTYDKMNKLENRKDIAQEMLMNQTKATPEEIKSILKFQEKLNVDVIDDCEEKQLVAILKEDLPDPRSAELYEFRFSDFPLTEHGLIKCGIRLFFEINVVEKFKVPVEVLTRWMYTVRKGYRAVTYHNWRHGFNVGQTMFTLLMTGRLKKYYTDLEAFAMLAAAFCHDIDHRGTNNLYQMKSTSPLARLHGSSILERHHLEYSKTLLQDESLNIFQNLNKRQFETVIHLFEVAIIATDLALYFKKRTMFQKIVDACEQMQTEEEAIKYVTVDPTKKEIIMAMMMTACDLSAITKPWEVQSQVALMVANEFWEQGDLERTVLQQQPIPMMDRNKRDELPKLQVGFIDFVCTFVYKEFSRFHKEITPMLSGLQNNRVEWKSLADEYDAKMKVIEEEAKKQEGGAEKAAEDSGGGDDKKSKTCLML
|
As cone-specific cGMP phosphodiesterase, it plays an essential role in light detection and cone phototransduction by rapidly decreasing intracellular levels of cGMP.
|
P51160
|
I1RL15
|
DPFGH_GIBZE
|
Diterpenoid pyrone biosynthesis cluster protein H
|
Fusarium
|
MSPLWVRRLCIRVVDSLYGSFLYLPLAILFLKRSVTGFGTGEWDESQIPKLDGKVAVVTGGNAGIGYYTVKHLASRGAKVYLGARSESRAKAAIKRLLEENPLIPQENVVWLRLDLANQSQVVDAAVELQSKEQRLDILVNNAGIDPYDYIRTADGFEMTMAVKYTNPAAAAQEESDVRVITVSSSGEAYSSPTNQFTSPKDLDDPCASPGWENSCLGQAMRYGTTKLANVLFASELQRRMDEEDANIISLSLNPGTVRTDGAANVMPFMVRPLVRFLFTAPERGADTSLFAATAEEIKENSERWKGRYLDGPGRIKVPSLRARDAVAGRNLWNITEAAVRGTGALDRL
|
Short chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of diterpenoid pyrones . The first step of the pathway is the synthesis of the alpha-pyrone moiety by the polyketide synthase dpfgA via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations (Probable). The alpha-pyrone is then combined with geranylgeranyl pyrophosphate (GGPP) formed by the GGPP synthase dpfgD through the action of the prenyltransferase dpfgC to yield a linear alpha-pyrone diterpenoid (Probable). Subsequent steps in the diterpenoid pyrone biosynthetic pathway involve the decalin core formation, which is initiated by the epoxidation of the C10-C11 olefin by the FAD-dependent oxidoreductase dpfgE, and is followed by a cyclization cascade catalyzed by the terpene cyclase dpfgB (Probable). The short chain dehydrogenase/reductase dpfgG then oxidizes the 8S hydroxy group to a ketone and the short chain dehydrogenase/reductase dpfgH reduces the ketone to the 8R hydroxy group to yield higginsianin B . Higginsianin B is further methylated by the methyltransferase dpfgI to produce the intermediate named FDDP B . The cytochrome P450 monooxygenase dfgpJ then catalyzes a three-step oxidation at C-27 to generate a carboxylic acid as well as C-26 hydroxylation . Finally, methyltransferase dpfgK methylates the carboxylic acid generated by dpfgJ, yielding the final diterpenoid pyrones from the pathway which were named FDDP D and FDDP E .
|
I1RL15
|
C1KZ12
|
RL13_LISMC
|
50S ribosomal protein L13
|
Listeria
|
MRTTYMAKPGEVERKWYVIDATGVSLGRLSSEVASILRGKNKPQFTPHIDTGDFVIIINAGKIGLTGKKATDKIYYRHSQYPGGLKSRTAGEMRTNNPEKLLELSIKGMLPKNSLGRQLFKKLHVYGGSEHEHAAQQPEVYELRG
|
This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly.
|
C1KZ12
|
A7MK11
|
MTNC_CROS8
|
2,3-diketo-5-methylthio-1-phosphopentane phosphatase
|
Cronobacter
|
MIRAIVTDIEGTTTDIRFVHNVLFPYARERLERFIRSGEQREPVNLLLNELRGEIHAPAASVDQLIETLFKFMDEDRKSPALKSIQGYIWREGYVNGDFTGHLYPDVVPALRRWSAQDIDIYIYSSGSVPAQKLLFSHSDEGDVTELLSGFFDTHVGAKRQVSSYRNISMKTGVPVHQMLFLSDIREELDAAREAGWKTVQLIRGEPDTQSTHRQVSSFDDIHPEQIPT
|
Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
|
A7MK11
|
Q97EH2
|
RS12_CLOAB
|
30S ribosomal protein S12
|
Clostridium
|
MPTISQLVRKGRKTLAAKSTAPALKECPQKRGVCTVVKTTTPKKPNSALRKIARVRLTNGYEVTAYIPGVGHNLQEHSVVLIRGGRVKDLPGVRYHIVRGTLDAAGVADRKQARSKYGAKKPKQK
|
Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit.
|
Q97EH2
|
Q0SIG6
|
TATA_RHOJR
|
Sec-independent protein translocase protein TatA
|
Rhodococcus
|
MGAMSPWHWAIVALVVIILFGSKKLPDAARGLGRSLRIFKSEVKEMQNDNSTPAPTAQQSAPAELPVADTTTAPVTPPAPVQPQHTEPKSA
|
Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
|
Q0SIG6
|
P0C245
|
TX622_PSACA
|
Vanillotoxin-2
|
Psalmopoeus
|
GACRWFLGGCKSTSDCCEHLSCKMGLDYCAWDGTF
|
Selectively activates the mammalian capsaicin receptor TRPV1, a non-selective cation channel expressed by sensory neurons of the pain pathway. Is more potent than VaTx1, but less potent than VaTx3. Interacts with distinct regions of the channel than capsaicin, since it only acts on the extracellular face of the channel, and capsaicin binds to the cytosolic side. Also activates avian TRPV1, which is insensitive to capsaicin. Produce weak inhibition on potassium channels Kv2.1/KCNB1.
|
P0C245
|
Q8YHM6
|
RS8_BRUME
|
30S ribosomal protein S8
|
Brucella
|
MSVSDPLGDMLTRIRNAVGRKKTKVSTPASKLRARVLDVLQAEGYIRGYTQSEFENGKAEIEIELKYYEGVPVIREITRVSKPGRRVYVSVKSIPQVVNGLGISILSTPKGVMADHEAREQNVGGELLCRIF
|
One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit.
|
Q8YHM6
|
P31381
|
FUN26_YEAST
|
Nucleoside transporter FUN26
|
Saccharomyces
|
MSTSADTDTIKKPILAVPEPALADTHSEEISRSGEEHESENNEHSDEEGDNYSEREQSVSTEPLDTLPLRKKLKNLSYITFFAIGIGLLWPWNCILSASQYFKHDIFKDTSIWAKIFTSSMMSFSTISSMLFNIYLAKRQYKYSRRVINGLVWEIIVFTVMCFFTILHFLLPKWFNFMFIMMLVVISSMGTAMTQNGIMAIANVFGSEYSQGVMVGQAVAGVLPSLVLFALAFIENSSVSTTGGILLYFFTTTLVVTICVVMFSVSKISRKVNENWNVEDGHITDVLLGSLRSNEEEIRIVGRIDQMEDEDHRRTNGTRDDNDEGEELQLKVPFEVLFAKLKYLVLSIFTTFVVTLVFPVFASATYVTGLPLSNAQYIPLIFTLWNLGDLYGRVIADWPMFRDQKFTPRKTFIYSLLRVAAIPLFLMFTAITSSSSGDEEHNGSVIVDLCYMLLQFLFGVTNGHVISMSFMKVPEQLDNDDEKEAAGGFTNIFVSTGLALGSIISYVFVFIIDFIIR
|
Has broad nucleoside selectivity (uridine, adenosine and cytidine) and most likely functions to transport nucleosides across intracellular membranes.
|
P31381
|
Q9H8W5
|
TRI45_HUMAN
|
RING finger protein 99
|
Homo
|
MSENRKPLLGFVSKLTSGTALGNSGKTHCPLCLGLFKAPRLLPCLHTVCTTCLEQLEPFSVVDIRGGDSDTSSEGSIFQELKPRSLQSQIGILCPVCDAQVDLPMGGVKALTIDHLAVNDVMLESLRGEGQGLVCDLCNDREVEKRCQTCKANLCHFCCQAHRRQKKTTYHTMVDLKDLKGYSRIGKPILCPVHPAEELRLFCEFCDRPVCQDCVVGEHREHPCDFTSNVIHKHGDSVWELLKGTQPHVEALEEALAQIHIINSALQKRVEAVAADVRTFSEGYIKAIEEHRDKLLKQLEDIRAQKENSLQLQKAQLEQLLADMRTGVEFTEHLLTSGSDLEILITKRVVVERLRKLNKVQYSTRPGVNDKIRFCPQEKAGQCRGYEIYGTINTKEVDPAKCVLQGEDLHRAREKQTASFTLLCKDAAGEIMGRGGDNVQVAVVPKDKKDSPVRTMVQDNKDGTYYISYTPKEPGVYTVWVCIKEQHVQGSPFTVMVRRKHRPHSGVFHCCTFCSSGGQKTARCACGGTMPGGYLGCGHGHKGHPGHPHWSCCGKFNEKSECTWTGGQSAPRSLLRTVAL
|
May act as a transcriptional repressor in mitogen-activated protein kinase signaling pathway.
|
Q9H8W5
|
Q4UR40
|
PDXA_XANC8
|
4-(phosphohydroxy)-L-threonine dehydrogenase
|
Xanthomonas
|
MVPSLALVPGEPAGIGPELCIRLAQQPRSDAHLIAYADPDTLHSAAKALCLSVRLLDPDQHARLPGDLPLHPVRQAAPTRFGTPDPANAAAVIAGLLGAAGDCLSGKLQGIVTGPVHKAVINAGGIAYTGTTELLAAQAGCPVVMMLANSIVRVALVTTHLPLRAVPEAITAEALARCLRITATAMQRDFGLEHPRIAVLGLNPHAGEDGLLGREELDVIIPVLDQLRSEGMQLIGPLPADTAFLPQKLTDFDAVVAMYHDQGLPVLKYSGFEQAVNITLGLPYPRVAVDHGTALELAGRGVADPSSLLAATALCARLAARS
|
Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP).
|
Q4UR40
|
A9KL10
|
MUTS_LACP7
|
DNA mismatch repair protein MutS
|
Lachnospiraceae
|
MAQLTPMMQQYVETKEQYKDCILFYRLGDFYEMFFEDALVASKELEITLTGKNCGQEERAPMCGIPYHAAEGYISKLIGKGYKVAICEQVEDPKLAKGIVKREVIRIVTPGTNLNTQTLDETRNNYLMGIIFTDEHCGISTVDITTGDYYVTEVENNRKILDEIYKYTPSEIVCNPEFFHCGLDVEDLKNRYQIAVSTFEDWYYDSEQSVKTLKEHFKVGSLDGLGLKDYSVGVNAAGAILKYLYNTQKNSLSHLTHITPYVTSRYMVIDSSSRRNLELTETLREKQKRGSLLWVLDKTKTAMGARMLRSFVEQPLITMDEISARYDAISELNDNVITREEIREYLNYIYDLERLMGKISYKSANPRDLIAFASSLSMLPHIKYLLSTCESALLKQIHEEMDALDDLQNLIDRSIAEEPPIGIKEGGIIKEGFHTEVDTLRKAKTEGKVWLAELEAKEKEQTGIKNLKVKYNRVFGYYLEVTNSYANLVPENWIRKQTLSNAERYTTPELKELEDKILNAEDRLFSLEYDLFAEIRDQIAEEVKRIQKTAKAVANIDAFASLAYVAERNQFIRPELNTNGTIDIKEGRHPVVEQMIPNDMFVSNDTYLDNAEKRISIITGPNMAGKSTYMRQTALIVLMAQVGSFVPASYANIGIVDRIFTRVGASDDLASGQSTFMVEMTEVANILRNATKNSLLILDEIGRGTSTFDGLSIAWAVIEHISNTSMLGAKTLFATHYHELTELEGKISGVNNYCIAVKEQGEDIVFLRKIIGGGADKSYGIQVAKLAGVPNSVLVRAREIVDQLSENDIAEKARHIVSAAEISNLTPETEGEVNTNKMYTTKVNATEVITTEVNTAKMNTTEMVSNQESVEQPRNFGQMSFFITEDTKQKKASSEFSEKLVQEINQFDLANMTPVEALLKLDKLQKKIRSHT
|
This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity.
|
A9KL10
|
A5GPE6
|
GATB_SYNPW
|
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B
|
unclassified Synechococcus
|
MAAPAATDQAWEAVIGLETHVQLGTNSKIFTAASTAFGDDPNTHIDPVVCGLPGTLPVLNQKVLEYAVKAAMALNLNIAEHSKFDRKQYFYPDLPKNYQISQYDEPIAEDGWIEVEVAEKGKDTYLKTIGIERLHMEEDAGKLVHAGSDRLAGSTHSLVDYNRAGVALAEIVSKPDLRTGREAAEYASEIRRIMRYLGVSDGNMQEGSLRCDVNISVRRGPEAPFGTKVEIKNMNSFSAIQKACEYEIQRQIKAYEAGEPIVQETRLWDESKQLTKSMRSKEGASDYRYFPDPDLGPIEVSADQRDSWRAELPELPAAKRHRYADTLGLSQYDARVLTDEKPMADYFEAVVVAGADAKLAANWITGDIAAYVNSNRLSYANLPFRPEQLAEMVQLIDGGKISGKIAKEILPELLENGGSPKAIVDERGLGMISDPAAIEAIVDELLGAHPDEVEAFRGGKTKLQGFFVGQLMKKTGGKADPKLANQILSKKLKG
|
Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
|
A5GPE6
|
Q7WFS0
|
MURD_BORBR
|
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase
|
Bordetella
|
MNTTETSRAAAPLVLILGLGETGVAAARWCARQGSPLRVADTRAQPGGLAALQAALADATVEYRLGCGEQFPPDLLDGVAQIVLSPGLVPHESPTRELLEQARERNVEVVGEIELFARALAGLAESREYRPRVLAITGTNGKTTVTALTRQLIEAGGMSARAAGNISPAALAALIDALDQDDLPQVWVLELSSFQLETTRTLAPDAAVVLNVTQDHLDWHGDMQAYAQAKARILKPARLAIVNRDDPLTVAMVESLQALNVRSFGRDVPALVGDMGLELGQGVAWLTACESNDFDEPAPAPRRKKDAPPPTRAGGRMSRLMPVDALRIRGVHNALNALAAMQLARSLDLGWGPMLRTLRDYAGEPHRAELVRSIGDVDYINDSKGTNVGATVAALEGLGQQVVLIAGGQGKGQDFSPLVPVVRRHARAVVLIGVDGAAIGKVLEPTGVPCVAAADMREAVRRAAELAQPGDAVLLSPACASFDMFRNYPHRGEVFAAEVQELALDRGEVA
|
Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
|
Q7WFS0
|
Q2VLG6
|
C163A_CANLF
|
Soluble CD163
|
Canis
|
MSKLRMVPHGNSGSADFRRCFALLCPSAVAVVSILSTCLMTNSLGRADKEMRLTDGEDNCSGRVEVKVQEEWGTVCNNGWGMDEVSVICRQLGCPTAIKAAGWANSRAGSGRIWMDHVSCRGNESALWDCKHDGWGKHNCSHQQDAGVTCSDGSSLEMRLMNGGNQCSGRIEVKFQGQWGTVCDDNFNIDHASVVCKQLECGSAVSFSGSANFGEGSGPIWFDDLVCSGNESALWNCKHEGWGKHNCDHAEDVGVICLDGADLSLRLVDGVTECSGRLEVKFQGEWGTVCDDGWDSNDAAVVCKQLGCPTAVTAIGRVNASEGSGHIWLDNLSCQGDESALWQCRHHEWGKHYCNHNEDAGVTCSDGSDLELRLVGGGSRCAGTVEVEIQKLLGKVCDRGWGLKEADVVCKQLGCGSALKTSYQRYSKVKATNTWLFLSRCSGNETSLWDCKNWQWGGLSCDHYEEAKVTCSAHREPRLVGGDIPCSGRVEVKHGDTWGTVCDSDFSLEAASVLCRELQCGTVISILGGAHFGEGNGQIWAEEFQCEGQESHLSLCSVASRPDGTCSHSRDVGVVCSRYTEIRLVNGQSPCEGRVELKILGNWGSLCNSHWDIEDAHVFCQQLKCGVALSIPGGAHFGKGSGQIWRHMFHCTGTEQHMGDCPVTALGATLCSAGQVASVICSGNQSQTLSPCNSTSLDPTRSTTSEESAVACIASGQLRLVNGGGRCAGRIEVYHEGSWGTICDDSWDLSDAHVVCRQLGCGVAINATGSAHFGEGTGPIWLDEVNCNGKESHIWQCRSHGWGQHNCRHKEDAGVICSEFMSLRLIDETSRDICAGRLEVFYNGAWGSVGKSNMSATTVEVVCRQLGCADKGSINPASSDKPMSRHMWVDNVQCPKGPDTLWQCPSSPWKQRVASSSEETWITCANKIRLQEGTSNCSGRVELWHGGSWGTVCDDSWDLEDAQVVCRQLGCGPALEALKEAAFGQGTGPIWLNDVKCKGNESSLWDCPARPWGHSDCGHKEDAAVRCSEIAMAQRSSNPRGHSSLVALGIFGVILLAFLIALLLWTQRRRQQQRLTVSLRGENSVHQIQYREMNSSLKADDLDVLTSSEYPNESDDFNDAGLISVSKSLPISG
|
After shedding, the soluble form (sCD163) may play an anti-inflammatory role.
|
Q2VLG6
|
P51369
|
CCSA_PORPU
|
Cytochrome c biogenesis protein CcsA
|
Porphyra
|
MNLEMMQNSCVNFAFGGLLTAMLVYWSSLAFPRISGLNKLAALITLLVNIALALTLSSRWFANGYFPLSNLYESLLFLAWGLTFVHLFIESKTKSRLIGAVSIPVAMFVTAFASLALPIEMQKASPLVPALKSNWLMMHVSIMMISYSILILGSLLSILFLIITRGQDINLKGSSVGTGSYTVKSLDSNPSFAFSNPSGIVQEQSNMLINSTRMNLLESIDNLSYRIIGLGFPLLTIGIVAGAVWANEAWGSYWSWDPKETWALITWLIFAAYLHCRITKSWQGKRPAILASVGFLVVWICYLGVNFLGKGLHSYGWLA
|
Required during biogenesis of c-type cytochromes (cytochrome c6 and cytochrome f) at the step of heme attachment.
|
P51369
|
Q6BL68
|
YAE1_DEBHA
|
Protein YAE1
|
Debaryomyces
|
MSSKCNGDCSCTSKVDSGVADKTEMTKNESNDIDDIWGDDDIEELDNSTADIKRMHSKQGYLDGITSAKESSLQDGFDDSFPKGAELGIIVGNILGSLISYDDQELFDQAKSELNISQVLHKRYFDEDLELRSTNDHEVIAKWQNVVQNLENK
|
The complex LTO1:YAE1 may function as a target specific adapter that probably recruits apo-RPLI1 to the cytosolic iron-sulfur protein assembly (CIA) complex machinery. May be required for biogenesis of the large ribosomal subunit and initiation of translation.
|
Q6BL68
|
C0QUC0
|
MTNA_PERMH
|
S-methyl-5-thioribose-1-phosphate isomerase
|
Persephonella
|
MRKIKDIRPIQLKDHKLYVINQLKLPKEKEWLELSTYQQVAEAIEKMIIRGAPLIGIVGAYGFAIGVKQILDEGRSLDDVRDVFDRLKNTRPTAVNLFWALERVWKKFERWTEEGRSGEELVNLLFKEAERIDLEDYHANKAIGGYGQVLLPERCNVLTHCNTGALATSGWGTALGVIRSAFENGKDITVYVDETRPYLQGSRLTAWELVEEGIPHYLITDNSAGFLMSKGIIDAIIVGADRITANGDVANKIGTYTLAVLAEAHGIPFYVAAPTSTFDLDTDSGKDIPIEERSQLEVKKCGGCDIAPEETEALNYSFDVTPASKITAIITEKGIISHVDKEHITKFLRYRGV
|
Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
|
C0QUC0
|
Q1Q8P0
|
RS7_PSYCK
|
30S ribosomal protein S7
|
Psychrobacter
|
MPRRRVVATREILPDPKFGSQTVAKFINHVMSHGKKSTAERIVYGALETVSQKRNIEDPVSFFEEVLENVRPMVEVKARRVGGATYQVPMEVRPSRRTALAMRWLAEAAAKRSEKSMALRLAGELNDAADGKGNAMKKRDEVHRMADANKAFSHYRF
|
One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA.
|
Q1Q8P0
|
Q6CSN0
|
PUL3_KLULA
|
Pulcherrimin biosynthesis cluster protein 3
|
Kluyveromyces
|
MKLTDSQKHLYSQYLAVTLIAVQFSFDTCVYLSSVVQYVKECGSDDPENYLFILQAVSAAVQVFFSFIIGDIASYVGSIKWVIIFLYFLSFVGNFLYSCAGAVSLNTLLGGRIICGAASSSGAVVYSYITAISKDRTTIFKLFSIYRTSAGICMALAQLVAILFALCDFTVRGYRITSYNAPTFASSFIILLICVLLMFVLENPPVKSARNPKNYLDAWKKFFSAGSNRLIASLILLWNMFLSTFFMCEVLYFMPIFLTLNVGWKTEYEGVAFMVSAVLGVAGSFFAPDLVKLFAKLNTPSTQDETDTSDNDKIEKEESEQKSDINTLHRNQVSLTIFALFVALIGQAFMIGASEALSNDKLPKTNSGIFFTAGLSITMLGYNFMGSSVPALFSMYIDPQVKVQLMPFIGAIAGVGKLVAPIVLAALYKTPLGLPIGVGFGMILVGISIPSLVYLRRNKM
|
MFS-type transporer required for the uptake of iron via the uptake of the siderophore pulcherrimin-iron complex.
|
Q6CSN0
|
Q6SSJ6
|
MOBA_COMTE
|
M-hydroxybenzoate hydroxylase
|
Comamonas
|
MQFHLNGFRPGNPLIAPASPLAPAHTEAVPSQVDVLIVGCGPAGLTLAAQLAAFPDIRTCIVEQKEGPMELGQADGIACRTMEMFEAFEFADSILKEACWINDVTFWKPDPAQPGRIARHGRVQDTEDGLSEFPHVILNQARVHDHYLERMRNSPSRLEPHYARRVLDVKIDHGAADYPVTVTLERCDAAHAGQIETVQARYVVGCDGARSNVRRAIGRQLVGDSANQAWGVMDVLAVTDFPDVRYKVAIQSEQGNVLIIPREGGHLVRFYVEMDKLDADERVASRNITVEQLIATAQRVLHPYKLDVKNVPWWSVYEIGQRICAKYDDVADAVATPDSPLPRVFIAGDACHTHSPKAGQGMNFSMQDSFNLGWKLAAVLRKQCAPELLHTYSSERQVVAQQLIDFDREWAKMFSDPAKEGGQGGVDPKEFQKYFEQHGRFTAGVGTHYAPSLLTGQASHQALASGFTVGMRFHSAPVVRVSDAKPLQLGHCGKADGRWRLYAFAGQNDLAQPESGLLALCRFLESDAASPLRRFTPSGQDIDSIFDLRAIFPQAYTEVALETLPALLLPPKGQLGMIDYEKVFSPDLKNAGQDIFELRGIDRQQGALVVVRPDQYVAQVLPLGDHAALSAYFESFMRA
|
Converts 3-hydroxybenzoate (m-hydroxybenzoate), and to a lesser extent p-hydroxybenzoate, to 3,4-dihydroxybenzoate (protocatechuate). Also acts on a number of analogs of 3-hydroxybenzoate substituted in the 2, 4, 5 and 6 positions.
|
Q6SSJ6
|
P0A2G4
|
CITA_SALTI
|
Citrate utilization protein A
|
Salmonella
|
MAQHTPATSRAGTFGAILRVTSGNFLEQFDFFLFGFYATYIARTFFPAESEFASLMLTFAVFGSGFLMRPVGAIVLGAYIDRIGRRKGLMVTLAIMGCGTLLIALVPGYQTIGLAAPALVLLGRLLQGFSAGVELGGVSVYLSEIATPGNKGFYTSWQSASQQVAIVVAALIGYSLNITLGHDAISEWGWRIPFFIGCMIIPLIFVLRRSLQETEAFLQRKHRPDTREIFATIAKNWRIITAGTLLVAMTTTTFYFITVYTPTYGRTVLNLSARDSLIVTMLVGVSNFIWLPIGGAISDRIGRRAVLMGITLLALITTWPVMQWLTAAPDFTRMTLVLLWFSFFFGMYNGAMVAALTEVMPVYVRTVGFSLAFSLATAIFGGLTPAISTALVKLTGDKSSPGWWLMCAALCGLAATAMLFVRLSRGYIAAENKA
|
Uptake of citrate across the boundary membrane with the concomitant transport of protons into the cell (symport system).
|
P0A2G4
|
A7MXJ9
|
TYSY_VIBC1
|
Thymidylate synthase
|
Vibrio
|
MKQYLDLCQRIVDQGTWVENERTGKRCLTVINADLTYDVANNQFPLVTTRKSFWKAAVAELLGYIRGYDNAEDFRKLGTKTWDANANLNEAWLNNPFRKGEDDMGRVYGVQGRSWAKPDGGHIDQLRKIVDDLTRDVDDRGEILNFYNPGEFHIGCLRPCMYSHHFSLLGDTLYLNSTQRSCDVPLGLNFNMVQVYVFLAIMAQITGKKPGQAYHKIVNAHIYEDQLAPMRDIQLKREPLKAATFHINPEIKSLEDLETWVTLDDFWVEGYEHHDPIQYPFSV
|
Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis.
|
A7MXJ9
|
Q98N70
|
RL11_RHILO
|
50S ribosomal protein L11
|
Mesorhizobium
|
MAKKIAGQLKLQVSAGSATPSPPIGPALGQRGINIMEFCKAFNAQTQEMEKGSPVPVVITYYQDKSFTFVMKTPPVSYFLKKAANLKSGSKEPGKVKAGTVSRDKVREIATAKMKDLNANDVEAAMRMVEGSARSMGLEVVG
|
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
|
Q98N70
|
Q5SKZ7
|
NQO15_THET8
|
NDH-1 subunit 15
|
Thermus
|
MSASSERELYEAWVELLSWMREYAQAKGVRFEKEADFPDFIYRMERPYDLPTTIMTASLSDGLGEPFLLADVSPRHAKLKRIGLRLPRAHIHLHAHYEPGKGLVTGKIPLTKERFFALADRAREALAFA
|
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 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 required for the synthesis of ATP. The Nqo15 subunit has probably a role in complex stabilization, and may be also involved in the storage of iron for iron-sulfur cluster regeneration in the complex.
|
Q5SKZ7
|
A4JDP6
|
IOLG_BURVG
|
Myo-inositol 2-dehydrogenase
|
Burkholderia cepacia complex
|
MTLQIGVIGCGAIGQDHIRRLTRTLSGARVVAVNDIDPQQARDAVTKYGLDAEIYGDGHDVVAAADVQALLVTSWGPTHEAFVLDAIAHGKPVFCEKPLAVTADGCMRIVEAEVAHGKRLVQVGFMRPYDEGYRALKRVIDSGEIGAPLMLHCAHRNQSVGERYTTDMAITDTLIHELDVLRWLLGEDYASAQVVYPKKTRHASAHLADPQIVLLETVSGVRIDVEIFVNCQYGYDIQCEVVGENGIAKLPDPPAVGLKHAARQSVEIMTDWKERFIASYDVELQAFIDGVRAGALTGPSAWDGYAAAVAADACVRAQRSAAVEPIAMAERPAFYRG
|
Involved in the oxidation of myo-inositol (MI) to 2-keto-myo-inositol (2KMI or 2-inosose).
|
A4JDP6
|
B7V9S6
|
GCS2_PSEA8
|
Gamma-glutamylcysteine synthetase 2
|
Pseudomonas
|
MTHDLAASGLRFGIEEEFFLLDASDLDIVRSAPAGFVAACRDTLGEHFAEEMFECQVEVASPVFSTLAEAARFHGQARQRLAHLAMDFGLRSLCVGTHPFADWRRARSNPAAHFARLFEDQGRVARRSLVCGLHVHVEIPPSHDRMAVLQRVLPWLPLLLALSASSPFRGGRRSGLASYRRALCGEWPRMNIPPALPDEDAYRRHLALLRETGCIREDGQVWWMIRPSSHVPTLELRICDACPRLADALSLAGLFRALVGEALDADPRALPVARDACLEENYWQALRYGCAGRYLVEGRCVGAGDWLEMAWRQCRPQARRGNEWAYQHACGLLEETSAARQLRRYRRLREAGQERHPALRRLVEELLEENLQPALAG
|
ATP-dependent carboxylate-amine ligase which exhibits weak glutamate--cysteine ligase activity.
|
B7V9S6
|
A0QF49
|
MRAY_MYCA1
|
UDP-MurNAc-pentapeptide phosphotransferase
|
Mycobacterium avium complex (MAC)
|
MRQILIAVAIALTVSILLTPALIRLFTRQGFGHHTREDGPPTHHAKRGTPSMGGVAIIAGIWAGYLGTHLAGLAFDGEGISASGLLVLSLATVLGIVGFLDDLIKIRRSRNLGLNKTAKTIGQVAAAVLFGVLALGFRNANGLTPASADLSYVREIATVTLAPGLFVLFCVVVVSAWSNAVNFTDGLDGLAAGSMAMVTAAYVLITFWQYRNACVTAPGLGCYNVRDPLDLAIVAAATAGACIGFLWWNAAPAKIFMGDTGSLALGGIIAGISVTSRTEILAVVLGSLFVAEVSSVVLQILTFRTTGRRVFRMAPFHHHFELAGWAETTVIIRFWLLTAIACGLGVALFYGEWLAAIGA
|
Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
|
A0QF49
|
Q51831
|
MURC_PORGI
|
UDP-N-acetylmuramoyl-L-alanine synthetase
|
Porphyromonas
|
MKRVYFIGIGGIGMSAIARYFHAKGFNVCGYDLTPSPITDQLIKEGIEVHFSDDLNMIPKAFFSPTDSLIVYTPAVPADHSELTYFRSNGYRVVKRAEVLGEITLMERALCVAGTHGKTTTSTLLAHLLKQSHVDCNAFLGGISNNYQSNLLLSDKSDLVVVEADEFDRSFHHLKPFMAIITSADPDHMDIYGTAENYRDSFEHFTSLIQSGGALVLKYGAPVNPRLGSDVSLFTYSSDDQQADYFASDIMIRDGRLFFTWHYPGGQLEGVELGVPVRINVENAVAAMAIAHLNGVTVEELRSGIASFKGSHRRFEKVLDTERVVLIDDYAHHPVELDAAIHSVREIYSGKHIMGIFQPHLYSRTADFYQDFARSLSMLDEVVLLDIYPARELPLPGVTSRLILDLIENPNKTLVSKNDLLDYLHGNEIPDVVLILGAGDIDRLVIPVKQYLQTLC
|
Cell wall formation.
|
Q51831
|
Q0SMU9
|
HTPG_BORAP
|
High temperature protein G
|
Borreliella
|
MKKQFDTEVNDLLYLIIHSLYSHKEIFLRELISNASDAIDKLKFLSLTNEKFKNIALEPKIEITFDDKSILIKDNGIGMNEQELTNHLGVIAKSGTKEFINNLKQDEKKSANLIGQFGVGFYSAFIVSEKVEVTSKKALESDAYIWSSDGKTGYEIEKAKKEDPGTEIKLYLNKEGLEYANKWKIQEIVKKYSNHINYPIYIKYNEPIMKDGKQEGIEEKEEKLNETTALWTKNKSEIKTEEYNEFYKNTTFDYENPLMYIHTKAEGNLEYTNLFYIPSKAPYDLYYPNTKPGVKLFINRIFITDSEGSLLPNYLRFIKGIIDCQDLPLNVSREILQQNKILSKIKSSSVKKILSELEKLSKKNPEKFSEFSKEFGRCIKEGVYSDFENREKLISLIRFKSSSVDGFVSFKEYKERMNEGQKSIYYITGGKENILKENPIVTAYKEKGFEILIMDDELDEAILNLIPEYEGLKLKAINKNETSNELKDENFKKIEEEFKDTLTRVKEILKDQIKEVNLSATLIKEPSAIIVDSNDPTYQMQKIMLSMGQEVKEIKPILELNPNNKIVQNLKNLEPEKLEKISILLFEEALLTSGMPSKNPRKFINIINEFLEKDLL
|
Molecular chaperone. Has ATPase activity.
|
Q0SMU9
|
Q1JDN4
|
RNPA_STRPB
|
Protein C5
|
Streptococcus
|
MKKTYRVKCEKDFQAIFKDGKSTANRKFVIYHLNRGQDHFRVGISVGKKIGNAVTRNAVKRKIRHVIMALGYQLKSEDFVVIARKGVESLEYQELQQNLHHVLKLAQLLEKGFESEEKH
|
RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
|
Q1JDN4
|
P56328
|
YCF12_CHLVU
|
Photosystem II reaction center protein Ycf12
|
Chlorella
|
MNLEIVFQLTALLFVVAAGPLVIVLLASRGGNL
|
A core subunit of photosystem II (PSII).
|
P56328
|
A2BP39
|
TRMB_PROMS
|
tRNA(m7G46)-methyltransferase
|
Prochlorococcus
|
MRQHVNPLSINFNQIERIPSLGEMFGDSKLNLHLDIGCAAGEFLFDLALVNTSWNYLGIEIREKLVKNAKLKVLESEIKNLYFLFGNANNILNDVQSELIIKNLKSISFYFPDPWFKKRHYKRRVIQPEFINILSNLLQKGTLIFIKTDVKDLFDYMDYTISNNFYFKTIDKKDFNYSESFNPNKVKTNREKYVINNQLDIFERIYIKI
|
Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
|
A2BP39
|
A5D3G1
|
RUVB_PELTS
|
Holliday junction ATP-dependent DNA helicase RuvB
|
Pelotomaculum
|
MKDRLISAVARPEDADVDTSLRPRLLAEYIGQEKVKETISVFIQAARGRGEPLDHVLLFGPPGLGKTTLANIIANEMGVSIRTTSGPAVERPGDLAAILTSLSQGDILFIDEIHRLSRTVEEVLYPAMEDYALDIVIGKGPGARSLRLELPRFTLVGATTRAGLLTSPLRDRFGVISRLEYYRPEDLVLIVNRSARILGIEITAEGAFEIARRSRGTPRVANRLLKRVRDYAQVRANGVITCEVAVEALKFLEVDPLGLDFADRRLLLTIIQKFGGGPVGLETIATAVNEEPETVEDVYEPYLIQLGMLARTPRGRVTTPLAFRHLGLEPAREETDQVSLW
|
The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing.
|
A5D3G1
|
Q44064
|
DRNF_AERHY
|
Periplasmic deoxyribonuclease
|
Aeromonas
|
MSRPSRVLGLPLLSLGLTLLVSTPLQAQEAQTFRAVKQDLVKLYQSHPSTFYCGCNIKFSGKKMAPDWESCGYLPRKQANRAARIEWEHVVPAWEFGHQLQCWQEGGRKNCGKSAEFNKMEGDMHNLFPAIGEVNGDRANYRFSDWNGKPNQYGKCQMLVDFKEQRVQPPKGPVRGQIARAYLYMGEQYGLRLAAQQRKLFEAWDRQYPADRWECERNRRIGKLQGNTNPFIEKQCQ
|
Endonuclease which is capable of degrading plasmid DNA.
|
Q44064
|
Q8BX94
|
OSBL2_MOUSE
|
Oxysterol-binding protein-related protein 2
|
Mus
|
MNGEEEFFDAVTGFDSDNSSIGEFSEANKISGMIDLDTSKSTRSGKNGEKPQQENGIQKHRTALPAPMFTRSDFSVWSILKKCIGLELSKITMPIAFNEPLSFLQRITEYMEHVYLIHKASSQSQPLERMQSVAAFAVSAVASQWERTGKPFNPLLGETYELIREDLGFRFISEQVSHHPPISAFYSEGLNQDFRFHGSIYPKLKFWGKSVEAEPRGTITLELLKHNEAYTWTNPTCCVHNVILGQLWIEQYGIVEIVNHRTGDKCILHFKPCGLFGKELHRVEGYIQDKNRKKLFIMYGKWTECLWGIDPASYESFKKQEKRGDQARKAKMDDGPEKANSDVPGDVADDVPVAQETVQVIPGSKLLWRINSRPPNSAQMYNFTSFTVSLNELESGMEKTLPPTDCRLRPDIRGMENGNMDLASQEKERLEEKQREARKERAKEDAEWRTRWFSPGNNPYTGAPDWLYAGHYFERNFSDCPDIY
|
Intracellular transport protein that binds sterols and phospholipids and mediates lipid transport between intracellular compartments. Increases plasma membrane cholesterol levels and decreases phosphatidylinositol-4,5-bisphosphate levels in the cell membrane. Binds phosphoinositides, such as phosphatidylinositol-4,5-bisphosphate. Exhibits strong binding to phosphatidic acid and weak binding to phosphatidylinositol 3-phosphate. Binds cholesterol, dehydroergosterol, 22(R)-hydroxycholesterol and 25-hydroxycholesterol (in vitro).
|
Q8BX94
|
Q045Z7
|
ECFA2_LACGA
|
Energy-coupling factor transporter ATP-binding protein EcfA2
|
Lactobacillus
|
MSIEFKNVDYIYAPGTPFQTQGLTNISFKIRSGSFVAIAGHTGSGKSTLMQHFDGLLLPSKGSVTIADKSITSNTSSKSLKEIRKKVGLVFQFPESQLFEETVLKDVMFGPLNFGFSEQKAKEQAIQWIRKVGLSEQVMNKSPFELSGGQMRRVAIAGVMAYEPDILCLDEPAAGLDPEGQKQMFDIFKNYQREGHTVILISHNMDDISQYADDMLVLEHGHLIKHASPKEVFSDPDWLKKHFLDEPATSKFARKLEKGGFQFSEMPLTVDSLVNEITTKLKSKGGNE
|
ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates.
|
Q045Z7
|
P21758
|
MSRE_BOVIN
|
Macrophage acetylated LDL receptor I and II
|
Bos
|
MAQWDDFPDQQEDTDSCTESVKFDARSVTALLPPHPKNGPTLQERMKSYKTALITLYLIVFVVLVPIIGIVAAQLLKWETKNCTVGSVNADISPSPEGKGNGSEDEMRFREAVMERMSNMESRIQYLSDNEANLLDAKNFQNFSITTDQRFNDVLFQLNSLLSSIQEHENIIGDISKSLVGLNTTVLDLQFSIETLNGRVQENAFKQQEEMRKLEERIYNASAEIKSLDEKQVYLEQEIKGEMKLLNNITNDLRLKDWEHSQTLKNITLLQGPPGPPGEKGDRGPPGQNGIPGFPGLIGTPGLKGDRGISGLPGVRGFPGPMGKTGKPGLNGQKGQKGEKGSGSMQRQSNTVRLVGGSGPHEGRVEIFHEGQWGTVCDDRWELRGGLVVCRSLGYKGVQSVHKRAYFGKGTGPIWLNEVFCFGKESSIEECRIRQWGVRACSHDEDAGVTCTT
|
Membrane glycoproteins implicated in the pathologic deposition of cholesterol in arterial walls during atherogenesis. Two types of receptor subunits exist. These receptors mediate the endocytosis of a diverse group of macromolecules, including modified low density lipoproteins (LDL).
|
P21758
|
B1HS22
|
LIPM_LYSSC
|
Octanoyl-[acyl-carrier-protein]:[GcvH] N-octanoyltransferase
|
Lysinibacillus
|
MTTWYFLNSGKCSPSFNMALDEALLDWHSEGLIPPVIRFYEWEPATLSIGYFQQAKKDINLDAVREQGLGFVRRPTGGRAVLHEHELTYSVIVTESYPDMPESVTEAYRVLSEGILQGFHNLGMDAYFSVPDTEEKRADLKSPKSAVCFDAPSWYELVVEGKKIAGSAQTRQKGVILQHGAILLDLDQEKLLSVFNFSSEEAKDRMRRKLPEKAVAINSLVDEPVTVEQCVTAFRDGFAKSLQIELKPFTLSEEQLEYVRALEEKKYACDEWNFKK
|
Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domain of GcvH, an intermediate carrier during protein lipoylation.
|
B1HS22
|
Q99PE4
|
P2RY4_MERUN
|
P2Y purinoceptor 4
|
Meriones
|
VHFSSSVMVLLFGLPFLVTLVCYGLMALRLCRPLPGAGQSSSRLRSLRTIAVVMTVFAVCLVPFHITRTIYYLARLLKADCQILNIVNVVYKVTRPLASANSCLDPLLYLFTGDKYRHQLQRLCRVSAPQRRITA
|
Receptor for ATP and UTP coupled to G-proteins that activate a phosphatidylinositol-calcium second messenger system. Not activated by UDP.
|
Q99PE4
|
Q9SN68
|
RAF2B_ARATH
|
Ras-related protein Rab5B
|
Arabidopsis
|
MAAAGNKSINAKLVLLGDVGAGKSSLVLRFVKDQFVEFQESTIGAAFFSQTLAVNDATVKFEIWDTAGQERYHSLAPMYYRGAAAAIIVFDVTNQASFERAKKWVQELQAQGNPNMVMALAGNKSDLLDARKVTAEDAQTYAQENGLFFMETSAKTATNVKEIFYEIARRLPRVQPTENPTGMVLPDRAMDRAVSSSCCA
|
Endosomal protein that may be involved in endocytosis . Involved in the trafficking of proteins from prevacuolar compartments (PVCs) to vacuoles . May activate the MON1-CCZ1 complex which acts as guanine nucleotide exchange factors (GEF) for Rab7 protein family, and serves as a link between Rab5 and Rab7 families in PVCs, and mediates PVC maturation . Involved in vacuolar transport of storage proteins with EREX as effector. Regulates membrane trafficking to protein storage vacuoles (PSVs) .
|
Q9SN68
|
A1UUA9
|
RL20_BARBK
|
50S ribosomal protein L20
|
Bartonella
|
MARVKRGVTAHAKHKKILKQAEGFYGRRKNTIRAAKAAVDRSKQYAYRDRKNRKRTFRALWIQRINAAVRMEGLTYGRFIDGLSKAGIEIDRKVLSDIAIHEPTVFSALVASAKKALEYLKDTTPNAFEGAVK
|
Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit.
|
A1UUA9
|
P50093
|
PHB2_CAEEL
|
Mitochondrial prohibitin complex protein 2
|
Caenorhabditis
|
MAKQGQEAMKKAIQNARGAGVGLGLVAAAGAAVYGVAQSMFTVEAGHRAIMFNRIGGLSTDLYKEGLHFRIPWFQYPIIYDIRARPNQIRSPTGSKDLQMVNIGLRVLSRPNPEHLVHIYRTLGQNWEERVLPSICNEVLKGVVAKFNASQLITQRQQVSMLVRKTLIERALDFNIILDDVSLTELAFSPQYSAAVEAKQVAAQEAQRATFYVERAKQQKQEKIVQAEGEAESAKLLGEAMKNDPGFLKLRKIRAAQKIARIVSESGNKTYLPTGGLMLNIADTDYLNVTDKRR
|
PHB proteins are essential during embryonic development and are required for somatic and germline differentiation in the larval gonad. A deficiency in PHB proteins results in altered mitochondrial biogenesis in body wall muscle cells . Required for clearance of paternal mitochondria after embryonic fertilization .
|
P50093
|
B2T740
|
RL24_PARPJ
|
50S ribosomal protein L24
|
Paraburkholderia
|
MNKIRKGDEVIVITGKDKGKRGVVLSVGEGKVIVEGINLVKKHVKPNPMKGTTGGVEAKTMPLQISNVALVDANGKASRVGIKVEGDKKVRFLKTTGAELSA
|
One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.
|
B2T740
|
Q5UXQ3
|
TRMY_HALMA
|
tRNA (pseudouridine(54)-N(1))-methyltransferase
|
Haloarcula
|
MRQFVIIGHDAPTTPEFSLDDLAGAAGRLDVLCRCVTSAFFLSHAIREDVRVHLILGDEYTVTFEGSDLRRLNPDERSTAALIRKALEEREEAIGHIPVETSPGVSLTRRGFEGTLDDVARRGTVVQLHEDGDPIVGVAPPSDPVFVLSDHHDFRDEEAALLADRADERVSLGPKALHADHSITVAHNYLDTAGFERY
|
Specifically catalyzes the N1-methylation of pseudouridine at position 54 (Psi54) in tRNAs.
|
Q5UXQ3
|
Q56577
|
NHAB_VIBAL
|
Sodium/proton antiporter NhaB
|
Vibrio
|
MPISLGNAFIKNFLGKAPDWYKVAIIAFLIINPIVFFLINPFVAGWLLVAEFIFTLAMALKCYPLQPGGLLAIEAIAIGMTSPAQVKHELVANIEVLLLLVFMVAGIYFMKHLLLFIFTKILLGIRSKTLLSLAFCFAAAFLSAFLDALTVIAVVISVAIGFYSIYHKVASGNPIGDHDHTQDDTITELTRDDLENYRAFLRSLLMHAGVGTALGGVTTMVGEPQNLIIADQAGWLFGEFLIRMSPVTLPVFFCGLITCALVEKLKVFGYGAKLPNNVRQILVDFDNEERKTRTNQDVAKLWVQGLIAVWLIVALALHLAAVGLIGLSVIILATAFTGVIEEHSMGKAFEEALPFTALLAVFFSIVAVIIDQELFKPVIDAVLAVEDKGTQLALFYVANGLLSMVSDNVFVGTVYINEVKTALIEGLITREQFDLLAVAINTGTNLPSVATPNGQAAFLFLLTSALAPLIRLSYGRMVIMALPYTIVLAIVGLMGIMFFLEPATASFYDAGWILPHSGDLTPVVSGGH
|
Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons.
|
Q56577
|
Q8PYZ8
|
HPPA1_METMA
|
Pyrophosphate-energized inorganic pyrophosphatase
|
Methanosarcina
|
MDMLIYLTPICALIGLIFAGISYKNVRNEGEGNELIKKITAAIHGGAMVYLNRQYRAIAVFVVFIAIVLALVLPNGVLTAACFVFGAVLSATAGYAGMLTATIANGRTTNAATRGIGPAFKVSFASGTVMGMSVVGLGLFGLSLSFIILGNIYTDMDLFTLLNIIAGFSFGASSIALFARVGGGIFTKAADVGADLVGKVEAGIPEDDPRNPAVIADNVGDNVGDIAGMGADLYESYVGSIIATMLLAASTAAATFPGIPVMNVVMVPLVIAAVGILASVIGTFFVRTNKTESSAIHMAFNMGLIAAIVLTVIASYVVTGHLLGGYGLNVFFSTVAGLVAGFLIGQITEHYTSYDKKPTLTVAHSCQTGSATNVITGFAKGMESTLWPAVIISIAIYIAFQLAGLYGIAIAAVGMLATLGISLSVDAYGPVADNAGGIAEMSHQKKEVRQITDTLDAVGNTTAAMGKGFAIGSAALTALSLFASYAIAVGLTSIDVMNPNVFIGLIIGAMLPFLFSSMTILAVGNAAGEVVVEVRRQFKEIKGLMEGKADPDYSKCITISTHSALKEMIPPGILAVIAPILVGLVLGAGALGGLLAGSVVSGFMLAITMSNAGGSWDNAKKFIELGNFGGKGSDAHKAGVTGDTVGDPFKDTAGPAINILIKLMSIVALVFAPLFI
|
Sodium pump that utilizes the energy of pyrophosphate hydrolysis as the driving force for Na(+) movement across the membrane.
|
Q8PYZ8
|
Q8K215
|
LYRM4_MOUSE
|
LYR motif-containing protein 4
|
Mus
|
MAASSRAQVLDLYRAMMRESKHFSAYNYRMYAVRRIRDAFRENKNVKDPVEIQALVNKAKRDLEIIRRQVHIGQLYSTDKLIIENQEKPRT
|
Required for nuclear and mitochondrial iron-sulfur protein biosynthesis.
|
Q8K215
|
Q1GB07
|
CRCB1_LACDA
|
Putative fluoride ion transporter CrcB 1
|
Lactobacillus
|
MDTVKNYLSVAFFAFWGGLARYGLTEAFSFYGTVIANLLGCFLLAFLTYFFLRKSNSRAWLTTGLGTGFVGAFTTFSSFNLDAFKLLLGGQNFGALLYFTGTIAAGFLFAWAGKQAANFAAGKLLERG
|
Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
|
Q1GB07
|
C1DBF4
|
SURE_LARHH
|
Nucleoside 5'-monophosphate phosphohydrolase
|
Laribacter
|
MRFLLSNDDGYFAPGIEALAAGLATLGTVTVVAPERDRSGASNSLTLDRPLMLRRAPNGFHFVNGTPTDCVHLAVTGMLDQQPDMVISGINHGANMGDDTVYSGTVAAATEGFLLGVPSLAVSLAAKPGEHLDTAVQVTLDIVRRMMDRPFTEPTLLNINVPDRPFHELRGTVATRLGRRHHAEPVVKSVNPRGDVVYWVGAAGPAQDAGEGTDFHAVREGFVSVTPLSIDLTGYRQLAELPAWLNP
|
Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
|
C1DBF4
|
P23660
|
GUNA_RUMAL
|
Endo-1,4-beta-xylanase
|
Ruminococcus
|
MRKPDKDADRLTTLDLARSGEVRDISAMELVGEMKTGWNLGNSLDATGAPGNASEVNWGNPKTTKEMIDAVYNKGFDVIRIPVTWGGHVGDAPDYKIDDEWIARVQEVVNYAYDDGAYVIINSHHEEDWRIPDNEHIDAVDEKTAAIWKQVAERFKDYGDHLIFEGLNEPRVKGSPQEWNGGTEEGRRCVDRLNKTFLDTVRATGGNNEKRLLLMTTYASSSMSNVIKDTAIPEDDHIGFSIHAYTPYAFTYNANADWELFHWDDSHDGELVSLMTNLKENYLDKDIPVIITEYGAVNKDNNDEDRAKWVSSYIEYAELLGGIPCVWWDNGYYSSGNELFGIFDRNTCTWFTDTVTDAIIENAK
|
Hydrolyzes both carboxymethylcellulose and xylan. Probably has a role in hydrolyzing oligosaccharides derived from cellulose, which are transported across the cell wall.
|
P23660
|
Q9NVJ2
|
ARL8B_HUMAN
|
Novel small G protein indispensable for equal chromosome segregation 1
|
Homo
|
MLALISRLLDWFRSLFWKEEMELTLVGLQYSGKTTFVNVIASGQFSEDMIPTVGFNMRKVTKGNVTIKIWDIGGQPRFRSMWERYCRGVNAIVYMIDAADREKIEASRNELHNLLDKPQLQGIPVLVLGNKRDLPNALDEKQLIEKMNLSAIQDREICCYSISCKEKDNIDITLQWLIQHSKSRRS
|
(Microbial infection) During infection, coronaviruses such as SARS-CoV-2 and the chaperone HSPA5/GRP78 are probably co-released through ARL8B-dependent lysosomal exocytic pathway for unconventional egress.
|
Q9NVJ2
|
Q6CZY7
|
RS5_PECAS
|
30S ribosomal protein S5
|
Pectobacterium
|
MAHIEKQAGELQEKLIAVNRVSKTVKGGRIFSFTALTVVGDGNGRVGFGYGKAREVPAAIQKAMEKARRNMMNVALNNGTLQHPVKGAHTGSRVFMQPASEGTGIIAGGAMRAVLEVAGVHNVLAKAYGSTNPINVVRATIDGLANMKSPEMVAAKRGKSVEEILG
|
Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body.
|
Q6CZY7
|
P81007
|
ENT_ENTCO
|
Cytolytic protein enterolobin
|
Enterolobium
|
TQRDTLTKGMTQGQIVAGPDDTKIDQSIMDQGVCATIALPFDIHVAQSVKNVMFMFAWTQKHGLAVNNLVILGVPGYLNMWKRFGESTDEPSESSKRCCYEKPTDPVSGEIVTPAFDPADEISEITHQEESADIKPVRLLDARLLGYTWVTQNHSWIVAYSDEPIKDGNEVVTLRNIGNNNFCDALRKCTDKSACIHQYLQFAWNSFGDPTVRTRQVVFEVVGWADSDTTNNNSDTLFYRTTQADNWQVLTESKTNTIGLAEVDWFNFKYETKQEVSIEIARQTWTSTLNAGVSTVSRVPKVPIKVKINVDTFLKVLFAVYKADLYDIFLQFASVFKKGGNRQYWLNYTQEPNTKSNYNHKIYNDKIRYLQEDVQVHPNETQSKWWWWSFKKVALTTMTVVALTRFKASGINGQYISARQFSGGETVSPYRLAAPFDSCLWRRSPNPLGTDGLKVALAHHPLAGASNRNKLRVSIPAQCICSITA
|
Cytolytic protein with insecticidal activity. Acts as a pro-inflammatory agent.
|
P81007
|
Q2STU0
|
SAHH_BURTA
|
S-adenosyl-L-homocysteine hydrolase
|
pseudomallei group
|
MNAAVIDSNSAQDYVVADIALAGWGRKELNIAETEMPGLVQIRDEYKAQQPLKGARIAGSLHMTIQTGVLIETLKALGADVRWASCNIFSTQDHAAAAIVEAGTPVFAFKGESLDEYWEFSHRIFEWPNGEFANMILDDGGDATLLLILGSKAEKDRSVIAKPTNEEEVALFKSIERHLEIDGSWYSKRLAHIKGVTEETTTGVHRLYQMEKDGRLPFPAFNVNDSVTKSKFDNLYGCRESLVDGIKRATDVMIAGKIAVVAGYGDVGKGCAQSLRGLGATVWVTEIDPICALQAAMEGYRVVTMEYAADKADIFVTATGNYHVINHDHMKAMRHNAIVCNIGHFDSEIDVASTRQYQWENIKPQVDHIIFPDGKRVILLAEGRLVNLGCATGHPSFVMSNSFTNQTLAQIELFTRGGEYANKVYVLPKHLDEKVARLHLARIGAQLSELSDDQAAYIGVPKAGPFKPDHYRY
|
May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine.
|
Q2STU0
|
C6DCC7
|
PCP_PECCP
|
Pyroglutamyl-peptidase I
|
Pectobacterium
|
MKTVLITAFEPFEGEAINPSWEAVKVLHQREVGGARVVACRLSCVFDLSLEELYRAIAEWQPEVVIAVGQAGGRTDISVERVAININDARIADNRGNQPIDTPIVEKGPAAYFSTLPVKALVQALRVAGIPASVSQTAGTFVCNHVMYGLLHQLHQQGDVVRGGFVHIPYSPEQAARHPGEPSMPTPLVTAALEVMIKQSLAQQVDVAVTGGALH
|
Removes 5-oxoproline from various penultimate amino acid residues except L-proline.
|
C6DCC7
|
A1K3X7
|
ACCA_AZOSB
|
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha
|
Azoarcus
|
MKTTFLDFEQPIAELEEKIEQLRFVQDDSAVDISEEIARLEVKSQALTKDLYAKLTPWQIAQVARHPQRPYTLDYVQHIFTDFEELHGDRAYADDKAIVGGLARFNGQSCVIIGHQKGRDTKEKIARNFGMPRPEGYRKAMRLMKLAEKFGLPVFTFVDTPGAYPGIGAEERGQSEAIGHNLYVMAELKVPLICTVIGEGGSGGALAIAVGDQVMMMQYSTYSVISPEGCASILWKSAEKASEAAETMGITAARLKSLGLVDKVVNEPVGGAHRDHRAAAQSLKRALAEALRQVDTLSPSELVEQRMEKLMGYGRFKEIAA
|
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.
|
A1K3X7
|
O24973
|
ARSR_HELPY
|
Transcriptional regulatory protein ArsR
|
Helicobacter
|
MIEVLMIEDDIELAEFLSEFLLQHGIHVTNYDEPYTGISAANTQNYDLLLLDLTLPNLDGLEVCRRISKQKHIPIIISSARSDVEDKIKALDYGADDYLPKPYDPKELLARIQSLLRRSHKKEEVSEPGDANIFRVDKDSREVYMHEKKLDLTRAEYEILSLLISKKGYVFSRESIAIESESINPESSNKSIDVIIGRLRSKIEKNPKQPQYIISVRGIGYKLEY
|
Member of the two-component regulatory system ArsS/ArsR that regulates genes involved in biofilm formation and acid adaptation by acting on major ammonia-producing pathways . Upon phosphorylation by ArsS, functions as a transcription regulator by direct binding to promoter regions of target genes including ureA, amiE and amiF to positively regulate their expression in response to acidic pH . Negatively autoregulates its expression .
|
O24973
|
B0RUE7
|
MSRA_XANCB
|
Peptide-methionine (S)-S-oxide reductase
|
Xanthomonas
|
MLGIGAFKQRMPRSGEALPGRTQALPLHNTHLINGHPLRGEFTGLAQVQFGLGCFWGAERKFWNVPGVYTTAVGYAGGKTPNATYSEVCSGQTGHTEAVLVVYDAQAVSFEQLLRTFWESHDPTQGMQQGNDVGTQYRSAIYCSTQAQYDAAIASRDAYQQQLTAAGYGDITTEILYPAPTFYYAEDDHQQYLAKHPNGYCGLGGTGVSCPIGLDA
|
Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
|
B0RUE7
|
Q92081
|
ACES_MYXGL
|
Acetylcholinesterase
|
Myxine
|
VPSPRPQNATVMVWIFGGGFAYGTSSLNVYDGRYLAQAEGAIVVSMNYRVGALGFLSLPGSPVPGNAGLFDQQLALRWVHGNIHRFGGNPQSVTLFGESAGSASVAPHLLSRHSQQFFQRAILQSGTLNAPWATVEDTEARRRAEALAQALGCPTDDDNELLNCLYARPPQEIVSKEGDVVIEPSIFRFPFVPVVDGHFIIDSPIVLLQQGIFKKTDLLLGVNRNEGSFFLIYGAPGFSKDHESLISREDFLENIPMIVPQGNEVSVDAIVLQYTDWLAQNDALKNRDAIEDIVGDYNVICPVVEMATRYAEFGNNVYFYFFNQRASNLPWPQWMGVI
|
Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft.
|
Q92081
|
B7SUM8
|
FBP12_RAT
|
Fatty acid-binding protein 12
|
Rattus
|
MVDQLQGTWKSVSCENFENYMKELGAGRAIRKLGCLARPVVTISTDGDRITIKTKSIFKNKEISFKLGEEFEEITPGGRKSKSTVVLDNDSLVQVQDWDGKEATIRRRLVDGKMVVESAVNNVTCTRTYQRV
|
May play a role in lipid transport.
|
B7SUM8
|
Q8BG02
|
2ABG_MOUSE
|
PP2A subunit B isoform gamma
|
Mus
|
MGEDTDTRKINHSFLRDHSYVTEADVISTVEFNHTGELLATGDKGGRVVIFQREPESKNAPHSQGEYDVYSTFQSHEPEFDYLKSLEIEEKINKIKWLPQQNAAHSLLSTNDKTIKLWKITERDKRPEGYNLKDEEGKLKDLSTVTSLQVPVLKPMDLMVEVSPRRTFANGHTYHINSISVNSDCETYMSADDLRINLWHLAITDRSFNIVDIKPANMEDLTEVITASEFHPHHCNLFVYSSSKGSLRLCDMRAAALCDKHSKLFEEPEDPSNRSFFSEIISSVSDVKFSHSGRYMLTRDYLTVKVWDLNMEARPIETYQVHDYLRSKLCSLYESDCIFDKFECAWNGSDSVIMTGAYNNFFRMFDRNTKRDVTLEASRESSKPRAVLKPRRVCVGGKRRRDDISVDSLDFTKKILHTAWHPAENIIAIAATNNLYIFQDKVNSDMH
|
The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment.
|
Q8BG02
|
Q8XE76
|
DXS_ECO57
|
1-deoxyxylulose-5-phosphate synthase
|
Escherichia
|
MSFDIAKYPTLALVDSTQELRLLPKESLPKLCDELRRYLLDSVSRSSGHFASGLGTVELTVALHYVYNTPFDQLIWDVGHQAYPHKILTGRRDKIGTIRQKGGLHPFPWRGESEYDVLSVGHSSTSISAGIGIAVAAEKEGKNRRTVCVIGDGAITAGMAFEAMNHAGDIRPDMLVVLNDNEMSISENVGALNNHLAQLLSGKLYSSLREGGKKVFSGVPPIKELLKRTEEHIKGMVVPGTLFEELGFNYIGPVDGHDVLGLITTLKNMRDLKGPQFLHIMTKKGRGYEPAEKDPITFHAVPKFDPSSGCLPKSSGGLPSYSKIFGDWLCETAAKDNKLMAITPAMREGSGMVEFSRKFPDRYFDVAIAEQHAVTFAAGLAIGGYKPIVAIYSTFLQRAYDQVLHDVAIQKLPVLFAIDRAGIVGADGQTHQGAFDLSYLRCIPEMVIMTPSDENECRQMLYTGYHYNDGPSAVRYPRGNAVGVELTPLEKLPIGKGIVKRRGEKLAILNFGTLMPEAAKVAESLNATLVDMRFVKPLDETLILEMAASHEALVTVEENAIMGGAGSGVNEVLMAHRKPVPVLNIGLPDFFIPQGTQEEMRAELGLDAAGMEAKIKAWLA
|
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).
|
Q8XE76
|
P10146
|
CCL1_MOUSE
|
T-cell activation protein 3
|
Mus
|
MKPTAMALMCLLLAAVWIQDVDSKSMLTVSNSCCLNTLKKELPLKFIQCYRKMGSSCPDPPAVVFRLNKGRESCASTNKTWVQNHLKKVNPC
|
Cytokine that is chemotactic for neutrophils.
|
P10146
|
Q3SSY3
|
RL1_NITWN
|
50S ribosomal protein L1
|
Nitrobacter
|
MATGKRLKKSREGIDRNKLYPIADAIRMVKERATSKFDETIEIAMNLGVDPRHADQMVRGVVTLPNGTGRTLRVGVFARGAKAEEAKAAGADVVGAEDLVETVQGGTIAFDRCIATPDMMPLVGRLGKVLGPRGMMPNPKIGTVTMDVAGAVKGAKGGSVEFRVEKAGIVQAGIGKASFSAEKLVENVKALADAVAKAKPAGAKGTYVQRIAVSSTMGPGVKVEPGTVLG
|
Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA.
|
Q3SSY3
|
Q06575
|
HP20_TAMSI
|
Hibernator-specific blood complex 20 kDa subunit
|
Tamias
|
MTDVWRLAIFVLMVNVLNDQVSCSGPPGPVGYPGVPGVPGPRGPPGQPGAAGRPGDPGPKGPSVKCPCRERSAFTVKFSGRLPPPSEPVVFTEVLYNTQRDLKESTGVFNCVEPGNYHFSFDVELYHCKVKIGLMKNHIQVMEKHQLSKNEYENASGAMIMPLRQGDKVWLEADVETEEPDQAKVVIYFSGFLISS
|
Plasma proteins HP-20, HP-25, HP-27 and HP-55 form a 140 kDa complex via disulfide bonds in the plasma and are hibernation specific.
|
Q06575
|
A8LPA8
|
HSLV_DINSH
|
ATP-dependent protease subunit HslV
|
Dinoroseobacter
|
MTETSFPGWHGTTIIGVKKNGKVVVAGDGQVSLGQTVIKGTARKVRRLTPGGHDVVAGFAGSTADAFTLLERLEAKLEATPGQLQRAAVELAKDWRTDKYLQKLEAMLIVTDGSLLLVITGAGDVLEPEHDIAAIGSGGNFALAAARGLMEADFDAETIARKAMQIAADICVYTNGNLTVEAIDA
|
Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
|
A8LPA8
|
Q17Z31
|
RS6_HELAH
|
30S ribosomal protein S6
|
Helicobacter
|
MRHYETMFILKPTLVEEEIKSKIEFYKEVITKHNGVIETSLDMGMRNLAYEIKKHKRGYYYVMYFKAEPSMILELERLYRINEDVLRFIVIKYDSKKEVEAWHALVDRANKKPSHAKEKHEKTEHAHSHHTEEAGSKESHSE
|
Binds together with S18 to 16S ribosomal RNA.
|
Q17Z31
|
Q85WT6
|
CHLL_PINKO
|
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
|
Pinus subgen. Strobus
|
MKIAVYGKGGIGKSTTSCNISVALARRGQKVLQIGCDPKHDSTFTLTGFLIPTIIDTLQSKDYHYEDIWPEDVIHKGYGGVDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFYEYDIILFDVLGDVVCGGFAAPLNYADYCVIITDNGFDALFAANRITASIREKARTHPLRLAGLVGNRTSRRDLINKYVEACPMPVIEVLPIIEDIRVSRVKGKTLFEMVGSEPSLNYVCNYYLGIADQILSQPEGIVPKEIPDRELFSLLSDLYLNPIGGGGQKKKIQENFLGFTRI
|
Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The L component serves as a unique electron donor to the NB-component of the complex, and binds Mg-ATP.
|
Q85WT6
|
A2XVI8
|
G1L4_ORYSI
|
Protein G1-like4
|
Oryza sativa
|
MDLSPNPDSPPSGGGNGGGGGSSSSNSSPSMGAGAPQSPSRYEAQKRRDWNTFGQYLRNHRPPLSLAQCSGAHVLEFLRYLDQFGKTKVHTAACPFFGHPSPPAPCPCPLRQAWGSLDALVGRLRAAFEENGGRPESNPFAARAVRLYLREVREHQARARGVSYEKKKRKKPQQQQLQGGDSSGLHGHQHHPPPPPPAGAAC
|
Probable transcription regulator that acts as a developmental regulator by promoting cell growth in response to light.
|
A2XVI8
|
A1RLV3
|
DXS_SHESW
|
1-deoxyxylulose-5-phosphate synthase
|
Shewanella
|
MSLDISQFPVLAQANTPNELRQLPQALLPQVADELREFLLKSVGMSSGHFASGLGTVELTVALHYVYNTPFDRLIWDVGHQAYPHKILTGRRDKMHTIRQKNGLHPFPWREESEYDTFSVGHSGTSISAALAMAVAAEKEQAGRKVVAVIGDGAMTGGMVFEAMNHAGDLHNDMLVVLNDNEMSISENVGALNNHLAQLMSGRFYTTLREGGKKVLKGMPVIKEMAKRTEEHLKGMVVPGTLFEELGFNYIGPIDGHDVDALVETMRNMRNLKGPQVLHIMTKKGRGYEPAEKDPIGWHAVPKFDPTQFKKPSTTPGLPTFSQVFGKWLCDIAEQDDKVLGITPAMREGSGMVEFSQRFPKQYFDAAIAEQHAVTLGAGFACEGYKPVVAIYSTFLQRGYDQLIHDVALQRLPVLFAIDRGGIVGADGPTHQGAFDLSFMRCIPNMVIMAPSDENECRQMLYTGYCYNAGPSAVRYPRGSATGATQVEAMTALPIGKGVIKRVGKRIALLNFGTTLASALTAADNLDATVVDMRFVKPLDAELVTEMAQTHDILVTVEENAIMGGAGSGVLELLQKLKMPKPVLQIGLPDEFIKHGSPEEVTHDLQLDAEGILAQINAYLAQ
|
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).
|
A1RLV3
|
P19338
|
NUCL_HUMAN
|
Protein C23
|
Homo
|
MVKLAKAGKNQGDPKKMAPPPKEVEEDSEDEEMSEDEEDDSSGEEVVIPQKKGKKAAATSAKKVVVSPTKKVAVATPAKKAAVTPGKKAAATPAKKTVTPAKAVTTPGKKGATPGKALVATPGKKGAAIPAKGAKNGKNAKKEDSDEEEDDDSEEDEEDDEDEDEDEDEIEPAAMKAAAAAPASEDEDDEDDEDDEDDDDDEEDDSEEEAMETTPAKGKKAAKVVPVKAKNVAEDEDEEEDDEDEDDDDDEDDEDDDDEDDEEEEEEEEEEPVKEAPGKRKKEMAKQKAAPEAKKQKVEGTEPTTAFNLFVGNLNFNKSAPELKTGISDVFAKNDLAVVDVRIGMTRKFGYVDFESAEDLEKALELTGLKVFGNEIKLEKPKGKDSKKERDARTLLAKNLPYKVTQDELKEVFEDAAEIRLVSKDGKSKGIAYIEFKTEADAEKTFEEKQGTEIDGRSISLYYTGEKGQNQDYRGGKNSTWSGESKTLVLSNLSYSATEETLQEVFEKATFIKVPQNQNGKSKGYAFIEFASFEDAKEALNSCNKREIEGRAIRLELQGPRGSPNARSQPSKTLFVKGLSEDTTEETLKESFDGSVRARIVTDRETGSSKGFGFVDFNSEEDAKAAKEAMEDGEIDGNKVTLDWAKPKGEGGFGGRGGGRGGFGGRGGGRGGRGGFGGRGRGGFGGRGGFRGGRGGGGDHKPQGKKTKFE
|
Nucleolin is the major nucleolar protein of growing eukaryotic cells. It is found associated with intranucleolar chromatin and pre-ribosomal particles. It induces chromatin decondensation by binding to histone H1. It is thought to play a role in pre-rRNA transcription and ribosome assembly. May play a role in the process of transcriptional elongation. Binds RNA oligonucleotides with 5'-UUAGGG-3' repeats more tightly than the telomeric single-stranded DNA 5'-TTAGGG-3' repeats.
|
P19338
|
Q9SU05
|
KIB1_ARATH
|
Protein KINK SUPPRESSED IN BZR1-1D 1
|
Arabidopsis
|
MTHKKQKKEMSDSEKKTFNEDSKHSILAVDLVRLILERLSFVDFHRARCVSSIWYIASKTVIGVTNPTTPWLILFPKGDVEIKKDSCKLYDPHENKTYIVRDLGFDLVTSRCLASSGSWFLMLDHRTEFHLLNLFTRVRIPLPSLESTRGSDIKIGNAVLWVDEQRKDYLVVWNISSLFGYHKKGDDRWKVFKPLENERCIIAMVFKENKLYVLSVDGNVDVFYFSGNDSPVRCATLPSSPLRKGHKVVVTLSGEVLIIVAKVEPYPRTRLCFFAVYKMDPKSSRWETIKSLAGEALILDLGITVEAKVMKNCIYFSNDQFHRYNENSLWNVSNKSGVFVYHFRSANVVQLVELLTASSRTSKILFKDARCFFPTFTSKWLL
|
Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins. Required for brassinosteroid (BR) signal transduction. Mediates ASK7/BIN2/SK21 inactivation both by competing with substrate binding (e.g. BZR1) and by promoting its ubiquitination and subsequent proteasomal degradation.
|
Q9SU05
|
Q0WUV7
|
EXL4_ARATH
|
Family II extracellular lipase 4
|
Arabidopsis
|
MCSKITLVLTLFSSYFISTDAVNGSFPALLAFGDSILDTGNNNFLLTFMKGNIWPYGRSFSMRRATGRFGNGRVFSDIVAEGLGIKKILPAYRKLFNSPSDLRTGVCFASGGAGVDPVTSKLLRVLTPKDQVNDFKGYIRKLKATAGPSRASSIVSNAVILVSQGNNDIGISYFGTPTAAFRGLTPNRYTTKLAGWNKQFMKELYDQGARKFAVMGVIPLGCLPMTRIFLGGFVITCNFFANRVAEQYNGKLRSGTKSWGREAGFRGAKFVYVDMYNTLMDVIKNYRRYGFSNEKNGCCCMITAIIPCPNPDKYVFYDFVHPSEKAYRTISKKLVQDIKNGLA
|
Required for the formation of pollen coats and male fertility.
|
Q0WUV7
|
B2SBS2
|
MINC_BRUA1
|
Probable septum site-determining protein MinC
|
Brucella
|
MNQVLTETRPIRLKGRSFLAMVLSPELPLDGWLERLDDLARRSSGFFLGRPVVLDMENLAIERAQLVYLLQALNDRGVWIMGVEGARPSLLGPGMPPAMRGGQPAADFEAPAGEPQANPGAPEPQISQAVRAPGHAVHAMPSMVITEPVRSGQSVYFPEGDVTIVGSVASGAEVVAGGSIHIYGTLRGRALAGTAGNTSARIFCRKLEAELVAIDGLYKTAEDLEPRFRGQAVQLWLDGDYMMIDTLS
|
Cell division inhibitor that blocks the formation of polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings. Prevents FtsZ polymerization.
|
B2SBS2
|
B8HNM9
|
PYRG_CYAP4
|
UTP--ammonia ligase
|
unclassified Cyanothece
|
MTKFVFVTGGVVSSIGKGIVAASLGRLLKSRNYSVSILKLDPYINVDPGTMSPFQHGEVFVTDDGAETDLDLGHYERFTDTAMSRLNSVTTGSIYQAVLNKERRGDYMGGTVQVIPHITNEIKDRILRVAKDTNPDVVIIEIGGTVGDIESLPFLEAIRQFRTEVGRQNVLYMHVTLIPWIPSAGEMKTKPTQHSVKELRSIGIQPDILVCRCDRPLYPGIKDKMSQFCDVPVKSVITCQDARSIYEVPLILEREGLAAQVLSLLNLEQRTPDLSEWQSLVEQLYRPKPPVEIAIVGKYVRLTDAYLSVMEALRHAAIAVGCELNLRWINSEDLENNNPEAYLGGVTGVVVPGGFGIRGVDGKIAAIRYAREHQIPFLGLCLGMQCCVIEWARSIAKLTDANSAEFDPQTSNPVINLLPEQQDVEVLGGTMRLGLYPCRLLSNSLAYQLYQETVIYERHRHRYEFNNAYRNLFLDTGFVVSGSSPDGRLVEIIELPEHPFFIATQFHPEFRSRPNVPHPLFKGFVQAARTHSSDRSNGHTPSETPSLSV
|
Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.
|
B8HNM9
|
Q01703
|
MSXC_DANRE
|
Homeobox protein MSH-C
|
Danio
|
MAPLSSMMNSLQGPLSQEGKLQERKSDKEDAQSNDKAAVKGCKGKALSLPFSVESLISDRTSSRTLYTSSEAGIISPTSGADERLKLSPMALYADRKIPVESVSNLSDCKRGDMEELSDKGQSGWFQTTSYTSPPRHSSPPPCTLRKHKNNRKPRTPFTTSQLLALERKFRQKQYLSIAERAEFSNSLNLTETQVKIWFQNRRAKAKRLQEAELEKLKLATKPLLPAFAFPFPLGTHVGSPPLYGPSSSFPRPALPVPGLFGGPVTYGMYYLS
|
Involved in the development of the inner ear.
|
Q01703
|
B5FGX4
|
DAPA_ALIFM
|
4-hydroxy-tetrahydrodipicolinate synthase
|
Aliivibrio
|
MFSGSIVALVTPLDTDGEVDYNSLKSLVDYHIKAGTNGIVAVGTTGESATLSVEEHVKLVMKTLEFADGRIPVIAGTGANATHEAVTFSKLFHDSGVAGCLSVTPYYNKPTQEGLFQHYKAISEATDIPQILYNVPGRTAVDLLPETVARLAELDNIVALKDATGDLERVAITRELCGENFIQLSGDDATALDFVKLGGHGVISVTSNIAAKDMATMFALAAQGKFEEAEIINQRLMPLHNDLFVEANPIPVKWAAHRLGMITHSDIRLPLTELSLSAQPTVEQALKSAGLLK
|
Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
|
B5FGX4
|
O66662
|
MURI_AQUAE
|
Glutamate racemase
|
Aquifex
|
MKIGIFDSGAGGMTVLKAIREAYPNVDVVYLGDTARVPYGIRSKETIVRYSKECANFLKDKGVDLLVVACNTASAYALEELKREFPFPVFGVIEPGVKEALRKSKTKRIGVIGTQATIKSGAYQEALKRAGAEVYSKACPLFVPLVEEGMIEGEIPKKVVEHYLKDFKGKVDTLILGCTHYPLLKREIQNFLEGVNVIDSSRATAKSLKDFVKNEGSGSLELYFTDRSQNLERLIKLILGEEVEPKITSEVFVL
|
Provides the (R)-glutamate required for cell wall biosynthesis.
|
O66662
|
F1LV46
|
I23O2_RAT
|
Indoleamine-pyrrole 2,3-dioxygenase-like protein 1
|
Rattus
|
MEAQRQDGKLASSLSLGKYHISEEYGFLLPNPLEELPDHYKPWMEIAHRLPHLIESHQLQAHVYEMPLLDCRFLTSYREQRLAHLVLAAITMGFVWQEGEAQPQKVLPRTLAIPFVEVSRSLGLPPILVHSDLVLTNWTKRNPEGPLEIGNLETIISFPGGESLQGFILVTVLVEKAAVPGIKALVLGVEAIRQHSQDTLLEALQQLRLSIQDITRALAQMHDYVDPEIFYLVIRIFLSGWKDNPVMPVGLVYEGVSTEPLKYSGGSAAQSSVLHAFDEFLGIQHCKESVDFLHRMRDYMPPSHKAFLEDLHSAPSLRDYILDSGPGGCLMAYNQCVEALGELRSYHINMVARYIISAASKARSRMLTRLSPHALEDRGTGGTAVLSFLKSVREKTMEAILCPGA
|
Catalyzes the first and rate-limiting step in the kynurenine pathway of tryptophan catabolism. Involved in immune regulation.
|
F1LV46
|
Q9PTY5
|
RANB9_XENLA
|
Ran-binding protein M
|
Xenopus
|
MSSPPLHGLSSVGHLSRDPPPRSWSPRDKCSYLGLSHGNLRVHYKGHGKTSKDAASVRSTHPIPAACGIFYFEVKIISKGRDGYMGIGLSTQGVNLNRLPGWDKHSYGYHGDDGHSFCSSGTGQPYGPTFTTGDVIGCCVNLIDNTCFYTKNGHSLGIAFTDLPPNLYPTVGLQTPGEVVDANFGQSPFVFDIEDYIREWRSKIQAQIERFPVAGEWQSMIQRMVSSYLVHHGYCSTAEAFAKSTDQTVQEELASIKNRQRIQKLVLSGRMGEAIETTQQLYPSLLERNPNLLFTLKVRQFIEMVNGTDSEVRCLGNRSLKSPDGCLGSDSNCSNGIISNKAHQTHCHSKSQSSNLNVTELNSINMTMSHQLNSYSSNDVEMETDHYSNGFSASTSNGFLNGSSRHEPELEECDTEMEVDTSHGRRQLCGGSQAAVERMICFGRELQAMSEQLRRERGKNATNKNMLKDAFSLLAYSDPWNSPVGYQLDPIQREHVCSSLNSAILDIHNLPKQPPLSLALEQASQCLEMMAQCGIGSCAFARVADYLH
|
May act as scaffolding protein, and as adapter protein to couple membrane receptors to intracellular signaling pathways. Acts as a mediator of cell spreading and actin cytoskeleton rearrangement. Core component of the CTLH E3 ubiquitin-protein ligase complex that mediates ubiquitination and subsequent proteasomal degradation of target proteins.
|
Q9PTY5
|
Q8TSZ5
|
PRIS_METAC
|
DNA primase small subunit PriS
|
Methanosarcina
|
MDKRTTQFLKSRFQSYYKNAEIGLPDHLPNREWAFIFYDDMPEKMMHRHKSFGSPGEALDYLYGMAPAHVYNSTAYYEYPDAKKMNEKNWLGAELIFDLDADHLPNAPRNYADMLELVKKEALKLLDFLLDDFGFSEQEIQLVFSGGRGYHFHIVSPKVLTLGSSERREIVNYVSGRDLEFKYFFREVAMDGDFGTGSKTFKGMKNVPMKCTLVGYDSGWGRRIALYLTDYMKRESEKKYKKDMFPELRRHEKVGDTTIKKLINIANSETGLKDILEKGRLDFDVRNFKEIAAYFMQESAEDFLHRFGASVDEPVTADIKRLIRVPGSLHGGSGMLVKKLALSELEEFDPLNDAVVFGERPVKITASKPFSVQLKGKDLRIEEGIQEVPEYAAVYLICRGVAEYGHRRNQPDTV
|
Catalytic subunit of DNA primase, an RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. The small subunit contains the primase catalytic core and has DNA synthesis activity on its own. Binding to the large subunit stabilizes and modulates the activity, increasing the rate of DNA synthesis while decreasing the length of the DNA fragments, and conferring RNA synthesis capability. The DNA polymerase activity may enable DNA primase to also catalyze primer extension after primer synthesis. May also play a role in DNA repair.
|
Q8TSZ5
|
A7H2Q3
|
ISPE_CAMJD
|
4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase
|
Campylobacter
|
MKAYAKANIFLKLTGFDSRKYHLLESRFILLKDVFDELELVDKESDSKKEFEIISNFKCENNIIQKAYLLLSRRYNNELKELFSKKSLKLTKNIPVCAGLGGGSSDCASFLLLMNETLNLKLNLQELINLSIQLGSDIAFFLSGFNSANVSGCGEIIEEFEDDIPTLKWTFPQISCQTKAVYDEFDREIFDFQKNNNQAQIYKKLSTKELLQNFKNKELNDLFTPCATLYPKMKSYLQEDFFLSGSGSSVFKVDR
|
Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
|
A7H2Q3
|
Q7T3B0
|
EIF3M_DANRE
|
Eukaryotic translation initiation factor 3 subunit M
|
Danio
|
MSVPAFIDITEEDQASELRSYLKSKGAEISEENSEGGLHVDLAQIIEACDVCLKDDDKDVESVMNSIVSLLLILETEKQEALIESLCEKLVKFREGERPSLRMQLLSNLFHGMDENTPVRHTVYCSLIKVAATCNAITFMPTDLDQVRKWIVDWNLNTEKKHTLLRLVYEALVDCKKSEAAAKVMVELLGSYTEDNASQARVDAHRCIVRALKDPNTYLFDHLLALKPVRFLEGELIHDLLTIFVSAKLISYVKFYQSNKDFIESLGLSHEQNMSKMRLLTFMGMAVEMKEISFETMQQELQIGAEDVEAFVIDAVRTKMVYSKIDQTQRKVVVSHSTHRTFGKQQWQQLYDTLCSWKQNLSTVKSSLQTLSPTA
|
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.
|
Q7T3B0
|
Q8RIL0
|
MRNCL_FUSNN
|
Mini-ribonuclease 3-like protein
|
Fusobacterium
|
MDNVDFSKDIRDYSGLELAFLGDAIWELEIRKYYLQFGYNIPTLNKYVKAKVNAKYQSLIYKKIINDLDEEFKVIGKRAKNSNIKTFPRSCTVMEYKEATALEAIIGAMYLLKKEEEIKKIINIVIKGE
|
Might be a ribonuclease involved in RNA processing.
|
Q8RIL0
|
B5RN32
|
SYI_BORDL
|
Isoleucyl-tRNA synthetase
|
Borrelia
|
MFKKVENKVHFPQLEEKILQFWNDNKIFEKSMKQREGCEEFTFYDGPPFATGLPHFGHFVPNTIKDIIPRYQTMKGKHVKRYFGWDTHGLPVEYEVEKSLKLSGRYEIEQYGIDKFNEECRNIVLRYTKEWKKIITRLGRWVDFENNYKTMDLTFMESVWWVFKTLYNKGLIYESYYVLPYSPKLATPLSNFEVNLGEYKEIHDPSLTIKFKIKDKNEYLLAWTTTPWTLPTNLGIAVGKDIDYSKVLDQEKNEIYIIGTKRLNHYYQDENKYVIIEQFKGEHLKGIEYEPLFDYFVNQRNKGAFKIHTAEYVTTDDGTGIVHIAPFGEEDYQILKKNTQTDMITPIDAECKFTSEVKDFEGLFVKDADNKIIEKLKSMNLLFKRENYLHRYPFCYRTNSPLIYRPISSWFVNIEKIKEKLIRSNEQINWIPEHLKKGRFGKWLENARDWAISRNRFWGNPIPIWKCSKTGNKICIGSREELEKLSGQKIIDLHKDKIDKITWPSKYGGTYVRTSEVLDCWFESGSMPYASKHYPFKDKDKFQNIFPADFIAEGLDQTRGWFYTLTILGTALFEKTAFKNVIVNGLVLSSDGKKMSKSLKNYTDPIQIINTFGADALRLYLIMSPVIKADDLKYSDDGVKDVLKNIIIPIWNAYSFFITYAIIDKFTPNNHVNLYKTNILDKWIISEIESLKQILNEEIDKYNLTKSIDVLLTFIDKLNNWYIRRSRRRFWKSENDNDKTDAYETLYYTLKNLMLMLAPFIPFLTEEIYQNLKTKNEKESIHLNDYPQSIKELINIELEEKMNFTRKVITIARALRASHNIKIRKPIKTIYIITKNHKEQNTLREMTEIILEEINAKEIKIKSNEEELVTYKAKANFKELGSKLGTNMKSVALAITKLSNEDILEIINGNKHTITINNNTYDITLKDIILERHERKNLKVINEDSITIGLDTLITEELYLEGLSRELIRKVQNLRKESNFNVTDRIILYTNNDEILTKIINNFENYIKTETLAITIEINNKKALKTLELDEEISVNIGIEKCLN
|
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).
|
B5RN32
|
Q2G0N5
|
RPOC_STAA8
|
Transcriptase subunit beta'
|
Staphylococcus
|
MIDVNNFHYMKIGLASPEKIRSWSFGEVKKPETINYRTLKPEKDGLFCERIFGPTKDWECSCGKYKRVRYKGMVCDRCGVEVTKSKVRRERMGHIELAAPVSHIWYFKGIPSRMGLLLDMSPRALEEVIYFASYVVVDPGPTGLEKKTLLSEAEFRDYYDKYPGQFVAKMGAEGIKDLLEEIDLDEELKLLRDELESATGQRLTRAIKRLEVVESFRNSGNKPSWMILDVLPIIPPEIRPMVQLDGGRFATSDLNDLYRRVINRNNRLKRLLDLGAPGIIVQNEKRMLQEAVDALIDNGRRGRPVTGPGNRPLKSLSHMLKGKQGRFRQNLLGKRVDYSGRSVIAVGPSLKMYQCGLPKEMALELFKPFVMKELVQREIATNIKNAKSKIERMDDEVWDVLEEVIREHPVLLNRAPTLHRLGIQAFEPTLVEGRAIRLHPLVTTAYNADFDGDQMAVHVPLSKEAQAEARMLMLAAQNILNPKDGKPVVTPSQDMVLGNYYLTLERKDAVNTGAIFNNTNEVLKAYANGFVHLHTRIGVHASSFNNPTFTEEQNKKILATSVGKIIFNEIIPDSFAYINEPTQENLERKTPNRYFIDPTTLGEGGLKEYFENEELIEPFNKKFLGNIIAEVFNRFSITDTSMMLDRMKDLGFKFSSKAGITVGVADIVVLPDKQQILDEHEKLVDRITKQFNRGLITEEERYNAVVEIWTDAKDQIQGELMQSLDKTNPIFMMSDSGARGNASNFTQLAGMRGLMAAPSGKIIELPITSSFREGLTVLEYFISTHGARKGLADTALKTADSGYLTRRLVDVAQDVIVREEDCGTDRGLLVSDIKEGTEMIEPFIERIEGRYSKETIRHPETDEIIIRPDELITPEIAKKITDAGIEQMYIRSAFTCNARHGVCEKCYGKNLATGEKVEVGEAVGTIAAQSIGEPGTQLTMRTFHTGGVAGSDITQGLPRIQEIFEARNPKGQAVITEIEGVVEDIKLAKDRQQEIVVKGANETRSYLASGTSRIIVEIGQPVQRGEVLTEGSIEPKNYLSVAGLNATESYLLKEVQKVYRMQGVEIDDKHVEVMVRQMLRKVRIIEAGDTKLLPGSLVDIHNFTDANREAFKHRKRPATAKPVLLGITKASLETESFLSAASFQETTRVLTDAAIKGKRDDLLGLKENVIIGKLIPAGTGMRRYSDVKYEKTAKPVAEVESQTEVTE
|
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
|
Q2G0N5
|
B5ZS19
|
ATPF1_RHILW
|
F-type ATPase subunit b 1
|
Rhizobium
|
MEFHFDATFFAFVGLVLFLALVVYLKVPGMMARSLDDRADQIRNELAEAKRLREEAQHLLAEYQRKRKEAEAEAAHIVAAAEREAQMLTAEAKKKTEEFVANRTALSEQKIKQAEVEAMKAVRSAAVDLAIAAAETVLGKQADAKVQSELFGNAVGQVKTRLN
|
Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
|
B5ZS19
|
B9MAC9
|
NRDR_ACIET
| null |
Diaphorobacter
|
MKCPFCSHQETQVVETRVSEDGDFIRRRRQCGACDKRFTTYERPEVNFPTVVKKDGRRVEYDREKLLGSFKLALRKRPVSTVQIDSAIERIEEKLLNLGQREILSSRIGELVMRELKKLDKVAYVRYASVYRSFEDIDEFRALVDEVRK
|
Negatively regulates transcription of bacterial ribonucleotide reductase nrd genes and operons by binding to NrdR-boxes.
|
B9MAC9
|
P60865
|
FOSB_BACCE
|
Fosfomycin resistance protein
|
Bacillus cereus group
|
MIQSINHICFSVANLEKAIEFYQNILQAKLLVKGRKLAYFDLNGLWIALNVEESIPRNEIQYSYTHIAFTVTNNEFDSLKEILIQNQVNILPGRERDDRDKRSIYFTDPDGHKFEFHTGTLQDRLQYYKEDKKYMTFY
|
Metallothiol transferase which confers resistance to fosfomycin by catalyzing the addition of a thiol cofactor to fosfomycin. L-cysteine is probably the physiological thiol donor.
|
P60865
|
B0CJ70
|
THIG_BRUSI
|
Thiazole synthase
|
Brucella
|
MLEFYGKRFESRLLLGTAQYPSPSILADAVRASLSRTVTVSLRRESGEARAGQDFWALIKALGVAVLPNTAGCHTPREAITTAHMAREVFGTNWIKLEVIGDTDTLQPDPFGLVEAARILCDEGFEVFPYMNDDLIVAERLIEAGCKVLMPWGAPIGSGRGLNNPYALKTMRAHFPDIPLVVDAGIGVPSHAAAAMELGFDAVLINTAVAKAGDPAAMARAFALAVEAGRLAYEADPIEARDMASPSTPLLGKAFL
|
Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S.
|
B0CJ70
|
O31714
|
K1PF_BACSU
|
Fructose 1-phosphate kinase
|
Bacillus
|
MIYTVTLNPSVDYIVHVEDFTVGGLNRSSYDTKYPGGKGINVSRLLKRHHVASKALGFVGGFTGEYIKTFLREENLETAFSEVKGDTRINVKLKTGDETEINGQGPTISDEDFKAFLEQFQSLQEGDIVVLAGSIPSSLPHDTYEKIAEACKQQNARVVLDISGEALLKATEMKPFLMKPNHHELGEMFGTAITSVEEAVPYGKKLVEQGAEHVIVSMAGDGALLFTNEAVYFANVPKGKLVNSVGAGDSVVAGFLAGISKQLPLEEAFRLGVTSGSATAFSEELGTEEFVQQLLPEVKVTRL
|
Catalyzes the ATP-dependent phosphorylation of fructose-l-phosphate to fructose-l,6-bisphosphate.
|
O31714
|
C0Q328
|
NHAB_SALPC
|
Sodium/proton antiporter NhaB
|
Salmonella
|
MEISWGRAMWRNFLGQSPDWYKLALLVFLIVNPFIFLANPFIAGWLLVAEFIFTLAMALKCYPLLPGGLLAIEAVIIGMTSAAHVREEVAANLEVLLLLMFMVAGIYFMKQLLLFIFTRLLLSIRSKMVLSLAFCVAAAFLSAFLDALTVVAVVISVAVGFYGIYHRVASSRGEENDMLDDSHIDPHYKTVLEQFRGFLRSLMMHAGVGTALGGVMTMVGEPQNLIIAKAAGWHFGDFFLRMSPVTVPVLVCGLLTCMLVEKMRWFGYGETLPEKVRDVLQQFDDQSRKKRTRQDKIKLIVQAVIGVWLVTALALHLAEVGLIGLSVIILATALTGVTDEHAIGKAFTESLPFTALLTVFFSIVAVIIDQHLFAPIIQFVLQASEHAQLTLFYLFNGLLSSISDNVFVGTIYINEAKAAMENGAISLKQFELLAVAINTGTNLPSVATPNGQAAFLFLLTSALAPLIRLSYGRMVWMALPYTIVLTLIGLLCVEFTLAPATEWMTQAGWLATLS
|
Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons.
|
C0Q328
|
Q5SW45
|
MKS1_MOUSE
|
Meckel syndrome type 1 protein homolog
|
Mus
|
MAEAVWSTDTGEAVYRSRDPVRNLRLRVHLQRITSSNFLHYQPAAQMGKDLIDLATFRPPQAASGHRPDEEEEEEVVIGWQEKLFSQFEVDLYQNESACQSPLDHQYRQEILKLENSGGRKNRRIFTYTDSDRYTDLEEYCQKITTSASEVPSFLAERMANVRRRRQDRRGVEGSKLKSRIVTWEPSEDFIKNNHAINTPLQTMYIMADLGPYGKLGYKVHEHVLCILKVDSNGVITVKPDFTGIKGPYRIETEGEKQEHTSAWKYTIDNVSSLAQPEEEEREQRVFKDLYGRHKEYLSSLVGTDFEMIAPGALRLFVNGEVVSAQGYEYDNLYVHFFVELPAANWSSPPFQQLSGVTQACATKSLGMDKVAYFSFPFTFEAFFLHEDESAESLPEWPVLYCKVLSLDFWQRYRVEGYGAVVLPATPGSHTLTVSTWRPMELGLVAELRRFFIGGSLELEDPSYVRIPGTFKGERLSRFGFRTETTGTVTFRLHCLQQSRAFMESNSLQKQMRSVLDRLEGFSQQSSTHNVLEAFRRARRRMQEARESLPQDLVSPTGTLT
|
Component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. Involved in centrosome migration to the apical cell surface during early ciliogenesis. Required for ciliary structure and function, including a role in regulating length and appropriate number through modulating centrosome duplication. Required for cell branching morphology.
|
Q5SW45
|
Q8Y7S7
|
CBID_LISMO
|
Cobalt-precorrin-6A synthase
|
Listeria
|
MEDFIYYNGKKYRKGYTTGTCAAAAAKACVEMILTQEEVSAVQVTTTGGTILEIPVAYQKFSKDKATAAVQKDGGDDIDATHGMWIFVDIDLTDNAEVVLDGGVGIGRATQKGISVAVGEAAINPAPRKNILATVRESLGENRGAKILVYAPEGEERAKRTMNSNLGIIGGISILGTTGIVTPMSDEGWKKSLSMELEMKRNQGLDQIILVPGNYGDDFVQNTLGFSSGNIVSMSNFVGYMLKETQRLAFKKVLMVGHFGKLVKVSAGIFTTYSKDADARAEILVANLALLGAPLSLLQAVEKCNTTEAAGELIEEAGFTQVYEVIAQKIKARSERFLKFTKPSVEIDVVTFSTERGLLAATKDIDVLREEWR
|
Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.
|
Q8Y7S7
|
A0A0P0V5U9
|
YUC1_ORYSJ
|
Flavin-containing monooxygenase YUCCA1
|
Oryza sativa
|
MDNKPAQERRETWVPGAVIVGAGPSGLAAAACLAARGVPATVLERSDSLASTWRHRMYDRLALHLPKRFCELPLLPFPEEYPTYPSKDQFVAYMEAYAAAAGVAPRFGATVEEAAFDAAVGAWRVRLDGGEVLMARWLVVATGENAEPRVPDFPGMQKFAGCAMHTSEYKSGEQFAGKKVLVVGCGNSGMEVSLDLCRHGAKPSMVVRNTVHVLPREMFGLSTFGIAMALLRWLPVQLVDRFLLTAAHLILGNTGQFGLRRPKTGPIELKNLTGRTPVLDVGTLDHIKSGKIKVVGAVKEMTRQGVRFTDGKEEQFDTIILATGYRSNVPSWLKDAGDLFTREGISKVPFPNSWRGRNGLYTVGFTQRGLLGTSSDALNVAKDIHCQWRERDRSAINVLEISNSSF
|
Involved in auxin biosynthesis . Converts the indole-3-pyruvic acid (IPA) produced by the TAA family to indole-3-acetic acid (IAA) (Probable). Functions downstream of TAR2 in auxin biosynthesis . Functions upstream of WOX11, a transcription factor that promotes the development of crown roots .
|
A0A0P0V5U9
|
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