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Full Name
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147
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taxon
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46
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sequence
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2.75k
function
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5.51k
AlphaFoldDB
stringlengths
6
10
Q5YZX1
HRCA_NOCFA
Heat-inducible transcription repressor HrcA
Nocardia
MGPMSSSTEDRRFEVLRAIVADYVATKEPIGSKTLVERHNLGVSSATVRNDMAVLEAEGYITQPHTSSGRIPTDKGYRQFVDRISEVKPLSAAERRAILQFLESGVDLDDVLRRGVRLLAQLTRQVAVVQYPTVSASTVRHIEVVALNPARLLLVVITDTGRVDQRIVELGAVVDDDDLSALRALLGAAMDGKRLAAASAAVAELPESAPQQLRDVLIRVSTVLVETLVEHPEERLVLGGTANLTRNAADFGLPGSLRQVLEALEEQVVVLKLLAAAQQPGTVTVRIGEETQVEEMRSASVVTTGYGVSGSVLGGMGVLGPTRMDYPGTIASVATVARYIGEVLAER
Negative regulator of class I heat shock genes (grpE-dnaK-dnaJ and groELS operons). Prevents heat-shock induction of these operons.
Q5YZX1
Q0HXV7
LIPA_SHESR
Sulfur insertion protein LipA
Shewanella
MNRPERLQPGVKLRDADKVSRIPVKIVPSERETMLRKPDWLRVKLPASNQRILEIKQALRSNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPLKPDADEPVKLAQTIRDMKLKYVVITSVDRDDLRDGGAQHFADCIREIRKLNPEIKIEILVPDFRGRIDAALDILSTEPPDVFNHNLETAPMHYRKARPGANYQWSLDLLKRFKERHPNVPTKSGLMMGLGETNEEIAQVLRDLREHKVEMLTLGQYLQPSKFHLPVERYVSPAEFDELKVLADELGFTHAACGPLVRSSYHADLQAQGKEVK
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Q0HXV7
Q8WT57
FAR1_ONCOC
Oo-FAR-1
Onchocerca
MYHQLILMALIGVIMANVVPFSMSNIPEEYKEFIPEEVKNFYKNLTQEDRQILRELASKHATFTNEDAALEALKNKSDKLYQKAVELRNFVKAKIDSLKPDAKAFVDEIIAKVRSLRPEDGQKLDMEKLKQAARDIIAKYEALNEETKEELKATFPNTTKIITNEKFKRIANSFLQKN
Binds retinol and different fatty acids.
Q8WT57
Q47UW3
EFG2_COLP3
Elongation factor G 2
Colwellia
MARITPIERYRNIGICAHVDAGKTTTTERVLFYTGLSHKIGEVHDGAATMDWMEQEQERGITITSAATTCFWKGMEGQFEDHRINIIDTPGHVDFTIEVERSLRVLDGAVLVLCGSSGVQPQTETVWRQMEKYAVPRIVFVNKMDRTGADFLYVVEQLKTRLGANAVPIHLAIGAEDDFEGVVDLIKMKAINWNASDQGMTFSYEEIPADMQDMAEEWRENLISEAAEANEELMDKYLEEGDLTEEEIKVGLRARTLANEIILCSCGSAFKNKGVQAVLDAVIEYLPSPTEVAAITGINDDKDESEGIRSADDEAPFSALAFKIATDPFVGTLTFFRVYSGVVQTGDSVYNPVKGKKERFGRIVQMHANDRQEIKEVRAGDIAAAIGLKDVTTGDTLCDAKHIITLERMEFPEPVISVAVEPRTLAAQEKMGIALGKLAAEDPSFRVATDDETGQTIISGMGELHLDILVERMKREFGVECNVGNPQVSYRETIRGTVEVEGKFIRQSGGKGQFGHVWLKMEPNEEGAGFEFVNEIVGGTVPKEFIPAVEKGCKEQMDSGVLAGYPLLDIKVTLYDGSFHDVDSNEIAFKVAASMGFRKGALEANPVILEPMMKVEVTTPEANMGDVVGDLNRRRGMIDGMDEGPAGSKIVNALVPLAEMFGYATDLRSATQGRASYSMEFQQYNEAPKLVAQKIMETR
Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.
Q47UW3
G1CWH0
CYC1_CLITE
Cliotide T1
Clitoria
GIPCGESCVFIPCITGAIGCSCKSKVCYRNHVIAAEAKTMDDHHLLCQSHEDCITKGTGNFCAPFPDQDIKYGWCFRAESEGFMLKDHLKMSITN
Probably participates in a plant defense mechanism (Probable). Active against Gram-negative bacteria E.coli ATCC 700926 (MIC=1.1 uM), K.pneumoniae ATTC 13883 (MIC=2.7 uM) and P.aeruginosa ATCC 39018 (MIC=4.7 uM) . Has hemolytic and cytotoxic activity .
G1CWH0
Q25337
SIR2_LEIMA
SIR2-related protein 1
Leishmania
MTGSPRAPHQEHALGEPTVEGLARYIREKDVRRILVLVGAGASVAAGIPDFRSSDTGIYAKLGKYNLDDPTDAFSLTLLREKPEIFYSIARELNLWPGHFQPTAVHHFIRLLQDEGRLLRCCTQNIDGLEKAAGVSPELLVEAHGSFAAAACIECHTPFSIEQNYLEAMSGTVSRCSTCGGIVKPNVVFFGENLPDAFFDALHHDAPIAELVIIIGTSMQVHPFALLPCVVPKSIPRVLMNRERVGGLLFRFPDDPLDTIHDDAVAKEGRSSSSQSRSPSASARREEGGTEDGSSSPNEEVEDASTSSSSDGYGQYGDYYAHPDVCRDVFFRGDCQENVLKLAECLGLREALAKRMRFSGAAPATARKTSNET
NAD-dependent deacetylase, which probably acts as a regulator of gene expression believed to help form modified chromatin structures on the genes it regulates.
Q25337
P00155
CYF_PEA
Cytochrome f
Pisum
MQTRNAFSWIKKEITRSISVLLMIYIITRAPISNAYPIFAQQGYENPREATGRIVCANCHLANKPVDIEVPQAVLPDTVFEAVVRIPYDMQVKQVLANGKKGALNVGAVLILPEGFELAPPHRLSPQIKEKIGNLSFQSYRPTKKNILVIGPVPGKKYSEITFPILSPDPATKRDVYFLKYPLYVGGNRGRGQIYPDGSKSNNNVSNATATGVVKQIIRKEKGGYEITIVDASDGSEVIDIIPPGPELLVSEGESIKLDQPLTSNPNVGGFGQGDAEIVLQDPLRVQGLLLFLASIILAQILLVLKKKQFEKVQLSEMNF
Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
P00155
A9BE82
LGT_PROM4
Phosphatidylglycerol--prolipoprotein diacylglyceryl transferase
Prochlorococcus
MEAYFATFRSPGPELLKVGFFTLRWYGLLIAFAVLIGLNLSNKLASIKGLSKNLINDLLPILVISSIIGARAYYVIFEWRNYSGSNFWSSIQAFGLTISIPTFIKVWQGGIAIHGALLAGTIAILIFCRLKQEDFWDVLDVLIPSVALGQAIGRWGNFFNNEAFGLPTDLPWKLFIPYPYRPEFFLDNNYFHPTFLYESIWNILLFLCLISLIRLSIKGKLKLPSGSLSCVYAIIYSLGRVWIEGLRTDPLCLGGVPPFCIGGIRIAQLISTILFGLGLLGLFWIYQRKKKLPSLGIIGRKHQ
Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
A9BE82
Q2YDG2
CF299_BOVIN
Cilia- and flagella-associated protein 299
Bos
MDQDEALTTVDNIVTQFNTYEDFLDSQITTLDLYYLEDEGLARQLVELGYRGTGEVVKREDFEARKAAIEIARLAERTQKKTLTSAGKDLHDNFLKALAVREEDNRSGKSVIFIRDKNSHGQEVSGYIDYAHRLKTEDFEVYFSGKKRLLPRPTDMSFYNWDSHIAIWNSTPNYQVIADNPEGLLFKYKRDRKILNVDPKAQPGDNSTRSPILTELYTQVVIFDHVSRRKT
May be involved in spermatogenesis.
Q2YDG2
Q15326
ZMY11_HUMAN
Protein BS69
Homo
MARLTKRRQADTKAIQHLWAAIEIIRNQKQIANIDRITKYMSRVHGMHPKETTRQLSLAVKDGLIVETLTVGCKGSKAGIEQEGYWLPGDEIDWETENHDWYCFECHLPGEVLICDLCFRVYHSKCLSDEFRLRDSSSPWQCPVCRSIKKKNTNKQEMGTYLRFIVSRMKERAIDLNKKGKDNKHPMYRRLVHSAVDVPTIQEKVNEGKYRSYEEFKADAQLLLHNTVIFYGADSEQADIARMLYKDTCHELDELQLCKNCFYLSNARPDNWFCYPCIPNHELVWAKMKGFGFWPAKVMQKEDNQVDVRFFGHHHQRAWIPSENIQDITVNIHRLHVKRSMGWKKACDELELHQRFLREGRFWKSKNEDRGEEEAESSISSTSNEQLKVTQEPRAKKGRRNQSVEPKKEEPEPETEAVSSSQEIPTMPQPIEKVSVSTQTKKLSASSPRMLHRSTQTTNDGVCQSMCHDKYTKIFNDFKDRMKSDHKRETERVVREALEKLRSEMEEEKRQAVNKAVANMQGEMDRKCKQVKEKCKEEFVEEIKKLATQHKQLISQTKKKQWCYNCEEEAMYHCCWNTSYCSIKCQQEHWHAEHKRTCRRKR
(Microbial infection) Inhibits Epstein-Barr virus EBNA2-mediated transcriptional activation and host cell proliferation, through direct interaction.
Q15326
A5F3G8
HSCA_VIBC3
Chaperone protein HscA homolog
Vibrio
MALLQIAEPGQSSAPHQHKLAAGIDLGTTNSLVASVRSGTASTLVDSQGRSILPSVVNYGADATRVGYPAREQAETDPHNTVISVKRLLGRSLQDINQRYPHLPYRFKASEKGLPIVQTAQGDKNPIQISADILKALAERATATLGGELAGVVITVPAYFDDAQRVATKDAAALAGLHVLRLLNEPTAAAIAYGLDSGQEGVIAVYDLGGGTFDISILRLSRGVFEVLATGGDSALGGDDFDHLIADHLQAQIGLTSLTAEQQRALINAATQAKIDLTEYMTAELNVLGWQGSLTREELENLIAPLLKKTLLSCRRALKDAGVEADEVLEVVMVGGSTRTPFVREQVGEFFGRTPLTSINPDEVVAIGAAIQADILAGNKPDAEMLLLDVIPLSLGIETMGGLVEKIIPRNTTIPVARAQEFTTFKDGQTAMSVHVVQGEREMVDDCRSLARFSLKGIPPMAAGAAHIRVTYQVDADGLLSVTALEKSTGVQAEIQVKPSYGLSDDEVTQMLKDSMAYAKEDMLARALAEQRVEADRVIEGLVSALQADGDELLNEQERQTLLQAIERLIELRNGDNADAIEQGIKDTDKASQDFASRRMDKSIRSALAGHSVDEI
Chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB.
A5F3G8
P27249
GLND_ECOLI
[Protein-PII]-UMP uridylyl-removing enzyme
Escherichia
MNTLPEQYANTALPTLPGQPQNPCVWPRDELTVGGIKAHIDTFQRWLGDAFDNGISAEQLIEARTEFIDQLLQRLWIEAGFSQIADLALVAVGGYGRGELHPLSDVDLLILSRKKLPDDQAQKVGELLTLLWDVKLEVGHSVRTLEECMLEGLSDLTVATNLIESRLLIGDVALFLELQKHIFSEGFWPSDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTSAERAELNECLHILWRIRFALHLVVSRYDNRLLFDRQLSVAQRLNYSGEGNEPVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRPIDDEFQLRGTLIDLRDETLFMRQPEAILRMFYTMVHNSAITGIYSTTLRQLRHARRHLQQPLCNIPEARKLFLSILRHPGAVRRGLLPMHRHSVLGAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFASEETRQRHPLCVDVWPRLPSTELIFIAALFHDIAKGRGGDHSILGAQDVVHFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLRYLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEEALHQIWSRCRANYFVRHSPNQLAWHARHLLQHDLSKPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGNPLSADRHEVIRFGLEQVLTQSSWQPPQPRRQPAKLRHFTVETEVTFLPTHTDRKSFLELIALDQPGLLARVGKIFADLGISLHGARITTIGERVEDLFIIATADRRALNNELQQEVHQRLTEALNPNDKG
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins GlnB and GlnK, in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
P27249
A5CVH0
ARGC_VESOH
N-acetyl-glutamate semialdehyde dehydrogenase
Candidatus Vesicomyosocius
MIKVGIIGSTGYTGLELIRLLHNHPNAKIIALCSRINASKSVIKEFPSLISYIDLDFVTPNEKKLFECDIIFFATPHGVAMNSVSKFLNKDIKIIDLGADFRIKDSTEWSKWYGMTHTQGDLLKDAVYGLPEVYNSQIKNATLIANPGCYPTAIILALKPLLETNIIDTKSIIADCKSGVSGAGRSANIATLFCEVNESLKPYNVDQHRHKPETQQVLTDIAGKEVNFFFTPHLVPMTRGMLASIYVDLIKDINVQKLFEKHYQNNKFIHILPTNVYPQTKSVKGTNNCHIGIQKSNNKLIIMSVIDNIIKGASGQAIQNMNLMFGLDEGLGLEQIGLLP
Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
A5CVH0
D4AT37
CHO2_ARTBC
Phosphatidylethanolamine N-methyltransferase
Trichophyton
MARLSGVERPDDSGLRERKAKAVEEPVKQPVEGADGAAAAAQAKKKTIGRTPDGTDILVLSIIGLHIVLLYLLPSFLRIPIFAVLFLSWRAAYNIGIGWLLHMQSNHSTMVLWARQTKIFVNPATGDNPHPQLYSFIKRELETKIPEDYSFEDAPIEYNTWLVFRRVVDLILMCDFTSYCLFAIACGSRPAEENFLVLILRWVVGLGLVLFNLWVKLDAHRVVKDFAWYWGDFFYLVDQELTFDGVFEMAPHPMYSVGYAGYYGISLMAASYKVLFISILAHAAQFAFLVLVENPHIEKTYNAPPPRKRTIESHAGLAGEEKSSRRPSESSEMVPPPSPVALPSSTHNLVGVKNLDLHRITDSSIILIQVLFFALTMLTPSTPIYQFFFVLNAAIWRLWYSVGIGYILNCQSHRREWTRHFVKFGETKEEAWNQWKGTYHLSMTLCYASFIAAAWKMYTLPENWGYGLAILKHVLGAGLIALQIWTSVSIYDSLGEFGWFFGDFFFDEAPKLTYSGIYRFLNNPERVLGLAGVWGAALITSSRAMIFLALLSHTLGIAFIQLVERPHMQKLYGRGLRQDAGLVRSIKRSLPPSFKQLHGSVDRILDESIEFIEEVLDTARPKLAAGVTTFVKDTSELFHKYPARITITRIEPDLAGYDMNDYSINVDTSDCITIRDGAEDKSEVLVFEYGSPIKVNWTAPLNHSKRDWVGLYMIGQNPSREVTNVSSWGRWVATNHGSFDSVLSEKGLIASDVVVSKPGTSNTSKKPSAKSSSGKKSSTSSSSHEVASGQMVFSGDKLWWTQGVFEFRYHHNGKHNVMATSRPFEIRIPKFDDGQIPSHVSSNGNGFMTTAIEQALLPIVQNCFDRDPEISPQTAEEPFGCETEGDLKYAKRVVYAVHQMFGIEFATEVVRADGNVQNLAWRICNAKKVLAPYSMRKSNGASTPTGESEEMK
Catalyzes the first step of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylethanolamine (PE) to phosphatidylmonomethylethanolamine (PMME).
D4AT37
Q08966
PCL8_YEAST
PHO85 cyclin-8
Saccharomyces
MANDQDPNKSLINDALTRSMSEFYDDDDDNDSDMCRANDEGEDVFDLPLKVGVSQSRNFSEVNDVLDPLSSLHGPSKKVRFEQQKQQQQHQQLHNDFNTDFNLKSPSSKKMGVEQLIQSANEINDYLANNIDKVNSFNSELLSGSGKLPGRVKSDTATQGTGRLDSMSNFALSDTELDNDDDNYLLDPLANASSTTPTVEHHGYSLLDKALSTSDKEKIYTNKVNSNSQIDTDNHSHESGNTTNNETDENESSEILDYTKFDSFPYPPSSAPNGEPPDLKVLSIECEQENEKELRRISLLLDHYESIPKIPELSDDEALSKFRENIELILQLSKKINDNANTLAISSEDPQKFVNFVMKNPPSLSFRDFIDRIQNKCMFGAVVYLGATYLLQLVFLTRDEMDGPIKLKAKLQEDQAHRIIISTIRIATKLLEDFVHSQNYICKVFGISKRLLTKLEISFMASVNFDGLMITCEKLEKTLHILDDTRQALGNT
Cyclin partner of the cyclin-dependent kinase (CDK) PHO85. Together with cyclin PCL10, negatively controls glycogen accumulation under favorable growth conditions. Involved in phosphorylation and negative regulation of glycogen synthase GSY2. Also has minor GLC8 kinase activity.
Q08966
B1W3Z5
RL5_STRGG
50S ribosomal protein L5
Streptomyces
MTATTAPRLKTRYREEIAGKLREEFSYENVMQVPGLVKIVVNMGVGDAARDSKLIDGAVKDLTTITGQKPAVTKARKSIAQFKLREGQPIGCHVTLRGDRMWEFLDRTLSLALPRIRDFRGLSPKQFDGRGNYTFGLTEQVMFHEIDQDKIDRVRGMDITVVTTATNDDEGRALLRHLGFPFKEN
This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.
B1W3Z5
P21658
FGF6_MOUSE
Heparin-binding growth factor 6
Mus
MALGQRLFITMSRGAGRVQGTLQALVFLGVLVGMVVPSPAGARANGTLLDSRGWGTLLSRSRAGLAGEISGVNWESGYLVGIKRQRRLYCNVGIGFHLQVPPDGRISGTHEENPYSLLEISTVERGVVSLFGVKSALFIAMNSKGRLYTTPSFHDECKFRETLLPNNYNAYESDLYRGTYIALSKYGRVKRGSKVSPIMTVTHFLPRI
Plays an important role in the regulation of cell proliferation, cell differentiation, angiogenesis and myogenesis, and is required for normal muscle regeneration.
P21658
P0A5J3
MAP1_MYCBO
Peptidase M
Mycobacterium tuberculosis complex
MPSRTALSPGVLSPTRPVPNWIARPEYVGKPAAQEGSEPWVQTPEVIEKMRVAGRIAAGALAEAGKAVAPGVTTDELDRIAHEYLVDNGAYPSTLGYKGFPKSCCTSLNEVICHGIPDSTVITDGDIVNIDVTAYIGGVHGDTNATFPAGDVADEHRLLVDRTREATMRAINTVKPGRALSVIGRVIESYANRFGYNVVRDFTGHGIGTTFHNGLVVLHYDQPAVETIMQPGMTFTIEPMINLGALDYEIWDDGWTVVTKDRKWTAQFEHTLLVTDTGVEILTCL
Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed.
P0A5J3
Q9JK45
KCNQ5_MOUSE
Voltage-gated potassium channel subunit Kv7.5
Mus
MPRHHAGGEEGGAAGLWVRSGAAAAAGAGGGRPGSGMKDVESGRGRVLLNSAAARGDGLLLLGTRAAALGGGGGGLRESRRGKQGARMSLLGKPLSYTSSQSCRRNVKYRRVQNYLYNVLERPRGWAFVYHAFVFLLVFGCLILSVFSTIPEHTKLASSCLLILEFVMIVVFGLEFIIRIWSAGCCCRYRGWQGRLRFARKPFCVIDTIVLIASIAVVSAKTQGNIFATSALRSLRFLQILRMVRMDRRGGTWKLLGSVVYAHSKELITAWYIGFLVLIFSSFLVYLVEKDANKEFSTYADALWWGTITLTTIGYGDKTPLTWLGRLLSAGFALLGISFFALPAGILGSGFALKVQEQHRQKHFEKRRNPAANLIQCVWRSYAADEKSVSIATWKPHLKALHTCSPTKKEQGEASSSQKLSFKERVRMASPRGQSIKSRQASVGDRRSPSTDITAEGSPTKVQKSWSFNDRTRFRPSLRLKSSQPKPVIDADTALGIDDVYDEKGCQCDVSVEDLTPPLKTVIRAIRIMKFHVAKRKFKETLRPYDVKDVIEQYSAGHLDMLCRIKSLQTRVDQILGKGQMTSDKKSREKITAEHETTDDPSMLARVVKVEKQVQSIESKLDCLLDIYQQVLRKGSASALTLASFQIPPFECEQTSDYQSPVDSKDLSGSAQNSGCLTRSASANISRGLQFILTPNEFSAQTFYALSPTMHSQATQVPMSQNDGSSVVATNNIANQISAAPKPAAPTTLQIPPPLSAIKHLSRPEPLLSNPTGLQESISDVTTCLVASKESVQFAQSNLTKDRSLRKSFDMGGETLLSVRPMVPKDLGKSLSVQNLIRSTEELNLQFSGSESSGSRGSQDFYPKWRESKLFITDEEVGAEETETDTFDGTPPPAGEAAFSSDSLRTGRSRSSQNICKTGDSTDALSLPHVKLN
Associates with KCNQ3 to form a potassium channel which contributes to M-type current, a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons. Therefore, it is important in the regulation of neuronal excitability. May contribute, with other potassium channels, to the molecular diversity of a heterogeneous population of M-channels, varying in kinetic and pharmacological properties, which underlie this physiologically important current.
Q9JK45
Q2K9M8
RL11_RHIEC
50S ribosomal protein L11
Rhizobium
MAKKVAGQLKLQVKAGSANPSPPIGPALGQRGINIMEFCKAFNAATQEMEKGMPIPVVITYYQDKSFTFAMKQPPVSYWLKKEAKITSGSKTPGKGAKAGTLTKAQIKTIAEAKMKDLNAADIEGAMAMIEGSARAMGLEVVG
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
Q2K9M8
O84746
YAJC_CHLTR
Sec translocon accessory complex subunit YajC
Chlamydia
MYSRLFFSILFFLGCCPALFADTDSPQRATFGQPAVMLGIAIVFFYFILWRPEQKRRQAMEKRKSELAVGDKVTAMGIVGTIAEIREHTVILNIASGKIEILKAAISEILKAEK
The SecYEG-SecDF-YajC-YidC holo-translocon (HTL) protein secretase/insertase is a supercomplex required for protein secretion, insertion of proteins into membranes, and assembly of membrane protein complexes. While the SecYEG complex is essential for assembly of a number of proteins and complexes, the SecDF-YajC-YidC subcomplex facilitates these functions.
O84746
A6LQR9
OBG_CLOB8
GTP-binding protein Obg
Clostridium
MFIDTAKVFVKSGNGGNGAISFRREKYVPLGGPDGGDGGKGGSIIFQVETGITTLLDFKYKKKFIAESGENGGGSKCYGKDGESLYIKVPMGTIIREAETNKIIADLSHKGQELVLLRGGKGGKGNVKFATATKQAPHYAEPGMPGDELNIVLELKLLADVGLLGFPNVGKSTLLSMTTKAKPKIANYHFTTLKPNLGVVAVDGIDPFVMADIPGIIEGAAEGVGLGIQFLRHIERTRLLIHIVDISGVEGRDPFEDFIKINEELKKYSVKLWDRPQIVVANKSDMLYDEGIFEDFKKKVQEMGFDKVFKMSAATNEGVDAVMKEAARILKDIPVKELEISEDEMYIPEEKRFTYDITVEHNKEEGYDVYIVEGTFVDRLLSAVNVNDADSLRYFHKVLRNKGIFDELREMGVKDGDMVRLNDFEFEYIL
An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control.
A6LQR9
P39009
DUN1_YEAST
DNA damage response protein kinase DUN1
Saccharomyces
MSLSTKREHSGDVTDSSFKRQQRSNKPSSEYTCLGHLVNLIPGKEQKVEITNRNVTTIGRSRSCDVILSEPDISTFHAEFHLLQMDVDNFQRNLINVIDKSRNGTFINGNRLVKKDYILKNGDRIVFGKSCSFLFKYASSSSTDIENDDEKVSSESRSYKNDDEVFKKPQISATSSQNATTSAAIRKLNKTRPVSFFDKYLLGKELGAGHYALVKEAKNKKTGQQVAVKIFHAQQNDDQKKNKQFREETNILMRVQHPNIVNLLDSFVEPISKSQIQKYLVLEKIDDGELFERIVRKTCLRQDESKALFKQLLTGLKYLHEQNIIHRDIKPENILLNITRRENPSQVQLGPWDEDEIDIQVKIADFGLAKFTGEMQFTNTLCGTPSYVAPEVLTKKGYTSKVDLWSAGVILYVCLCGFPPFSDQLGPPSLKEQILQAKYAFYSPYWDKIDDSVLHLISNLLVLNPDERYNIDEALNHPWFNDIQQQSSVSLELQRLQITDNKIPKTYSELSCL
Transducer of the DNA damage signal. Phosphorylates SML1 on serine residues. Cooperates with the PAN deadenylation complex in the regulation of RAD5 mRNA levels and cell survival in response to replicational stress.
P39009
A0A287A2K5
GASR_PIG
Cholecystokinin-2 receptor
Sus
MELLKLNRSLPGPGPGAALCRPEGPLLNGSGAGNLSCEPPRIRGAGTRELELAVRITLYAAIFLMSVAGNVLIIVVLGLSRRLRTVTNAFLLSLAVSDLLLAVACMPFTLLPNLMGTFIFGTVVCKAVSYFMGVSVSVSTLSLVAIALERYSAICRPLQARVWQTRSHAARVIVATWMLSGLLMVPYPVYTAVQPAGPRVLQCMHRWPSARIRQTWSVLLLLLLFFVPGVVMAVAYGLISRELYLGLRFDGDSDCESQSQVGSQGGLPGGAGQGPAHPNGHCRSETRLAGEDGDGCYVQLPRSRPALEMSALTAPTPGPGSGPRPAQAKLLAKKRVVRMLLVIVVLFFLCWLPVYSANTWRAFDGPGAHRALSGAPISFIHLLSYASACVNPLVYCFMHRRFRQACLDTCARCCPRPPRARPRPLPDEDPPTPSIASLSRLSYTTISTLGPG
Receptor for gastrin and cholecystokinin . The CCK-B receptors occur throughout the central nervous system where they modulate anxiety, analgesia, arousal, and neuroleptic activity (Probable). This receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system (Probable).
A0A287A2K5
B0TWU0
APT_FRAP2
Adenine phosphoribosyltransferase
Francisella
MNLDFIKDRIVAVPDFPKPGIVFRDITPLLADPQGLKMTAKAMAEELKSKGIKPTVIAGTESRGFIFGVALAEVLGLGFVPVRKPGKLPRETYKVSYQLEYGSDSLEIHKDAFKPTDKVLVVDDLLATGGTAKATVQLIEKTQASVAGLIFVIELEDLNGRKVLEGHNVSALVKY
Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
B0TWU0
A8H779
NQRD_SHEPA
NQR-1 subunit D
Shewanella
MADAKELKQVLIGPIVSNNPIALQILGVCSALAVTSKMETALVMTIALTAVCALSNLFISLIRNHIPSSVRIIVQMTIIASLVIVVDQVLQAYAYDVAKQLSVFVGLIITNCIVMGRAEAYAMKTPPMMSFMDGIGNGLGYGAILLSVGFVRELFGNGSLFGIEILSKISDGGWYQPNGLLLLPPSAFFLIGALIWIIRVMKPEQVEAKG
NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.
A8H779
A5UDH0
TYSY_HAEIE
Thymidylate synthase
Haemophilus
MKQYLELCRRIVSEGEWVANERTGKRCLTVINADLEYDVANNQFPLITTRKSYWKAAIAEFLGYIRGYDNAADFRALGTKTWDANANENAAWLANPHRRGVDDMGRVYGVQGRAWRKPNGETIDQLRKIVNNLTKGIDDRGEILTFFNPGEFDLGCLRPCMHTHTFSLVGDTLHLTSYQRSCDVPLGLNFNQIQVFTFLALMAQITGKKAGKAYHKIVNAHIYEDQLELMRDVQLKREPFPLPKLEINPDIKTLEDLETWVTMDDFKVVGYQSHEPIKYPFSV
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.
A5UDH0
A8ADP9
AROC_CITK8
5-enolpyruvylshikimate-3-phosphate phospholyase
Citrobacter
MAGNTLGQLFRVTTFGESHGLALGCIVDGVPPGIPLTEADLQHDLDRRRPGTSRYTTQRREPDQVKILSGVFEGVTTGTSIGLLIENTDQRSQDYSAIKDVFRPGHADYTYEQKYGLRDYRGGGRSSARETAMRVAAGAIAKKYLAEKHGIVIQGCLTQMGDIPLEIKDWQQVEQNPFFCPDPDKIDALDELMRALKKEGDSIGAKVTVVANGVPAGLGEPVFDRLDADIAHALMSINAVKGVEIGDGFDVVALRGSQNRDEITKEGFLSNHAGGILGGISSGQQIVAHMALKPTSSITVPGRTINRFGEEVEMITKGRHDPCVGIRAVPIAEAMLAIVLMDHLLRQRAQNADVKTDIPRW
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.
A8ADP9
Q7VQD5
RS14_BLOFL
30S ribosomal protein S14
Candidatus Blochmannia
MPRKSVQEREKKRLRLINKYFLRRSLLRKCVVDLKVSSEERWNAVLKLQTLPRDSSPSRLRNRCGRTGRPHAFLRKFGLSRMKVREAAMKGEIPGLRKSSW
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.
Q7VQD5
A1UG51
POTA_MYCSK
Spermidine/putrescine import ATP-binding protein PotA
unclassified Mycobacterium
MNQTVDGVAPNKSGPVIEIDHVTKRFADYVAVADADFSIASGEFFSMLGPSGCGKTTTLRMIAGFETPTSGAIRLEGTDVSRVPPHKRNVNTVFQHYALFPHMSVWDNVAYGPRSMKKDKSEVKRRVDELLEVVRLTDFAKRKPGQLSGGQQQRVALARALVNYPSALLLDEPLGALDLKLRHAMQFELKRIQREVGITFIYVTHDQEEALTMSDRIAVMNAGNVEQIGTPTDIYDRPATVFVANFIGQANLWSGRQTGRLNRDYVEIDVLGSKLKARPGDTAIEAGGHATLMVRPERLRVSMEPPVGDVAAVRATVRDMTFQGPVVRLSLVAPDDSPIVAHVGTEQQLPLLRPGDEVYVCWSPDASLVLPAADIPTTEDLEEMLDES
Part of the ABC transporter complex PotABCD involved in spermidine/putrescine import. Responsible for energy coupling to the transport system.
A1UG51
A3D1S4
ANMK_SHEB5
AnhMurNAc kinase
Shewanella
MKNAYYIGLMSGTSMDGVDAVLVDFSGAQPQLITSHTEAIPSHLLKGLQRLCSPSTDEINRLGRLDRNVGELFALAVNNLLTKCAIAKEDVIAIGSHGQTVRHMPNLEVGFTLQIGDPNTIATETGIDVIADFRRKDIALGGQGAPLVPAFHQQTFAEVGKKRIILNIGGIANITYLPGNSDQVLGFDTGPGNTLIDAWIQQVKSEPFDRDGAWAESGKTDQDLLTQLLSHPYFSLAYPKSTGRELFNQAWLEQQLSPFNHLDEEDIQSTLLDLTCHSIARDMIKLSNEGELYVCGGGAFNGQLMQRLAALLPGYTLNTTSALGVDPKWAEGIAFAWLAMRNHLGLPANLPAVTGASREAVLGGRFSAK
Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling.
A3D1S4
A8W3G3
YCF2_CUSEX
Protein Ycf2
Cuscuta subgen. Monogynella
MKKMMRHQVKLGILELREIMREIHNYYYLLLLDSWTKLNSVGSLIHLFFHQERFLKLFDPRIFSILLSRNLQGSPSNRYFTIKGVILFVVGVLIYRINNQNMVERKNLYLTGLFPIPMNSTGPIKDRLEEAIGSSNINRLSVLLLYFPKGKNISERYFLNPKETAGVLTITKKGSVPESNWGSRRWRNFIGVKRGNFSCPIANETVGGIDILFKDKFRKNMEFTFVYYMDDLTHNDPDWEFFYRLSTRKSENRINWNSGPLFKILVKDCISYLMSAFREKRPKGEGPESTIQSNKIRHVFHLFSIKRGTISLQNCTHFYMWQFRRDLFRSWGNNPPESSFLRNVSREISSNAWLGNKGRFFSKGRNVLSNLQYDSTGSSLVNVTDSSQLKGSEDQSIERLASIRNEDSEYHALINKREVQQLEESSMTLESDRLPKSLSGYCSTSQLFKERENPMINFMFPGEMEEFIGNPTRSVRSFCSDRWSELHLWSNPTEKSTLDHKFVKNHLSFVRGAENKEIKNLRRIITYLQKTVSIHSISSDPRWDRVPKHDPDMDSFKKNSLFFLFHRFHERNRGAYPLRHDFESEERLQEMTELFTLLISEPDLVYHKGFSFYIYIDSYGLDKKNLLNEVLNARAESKNKSLWVLSPILFRYEEIEYFFKRIRQKRVWWISCGNGLVDLKQNDDGYIRNLFNILFLMNKSDRNFEHRMQGDRKGTAIFNQRTIMKCMIKQDHTYIYKRSNGTKNFQEHLEHFLSQQKSDFKVQKRYFQVLFDQLRICLTKNLIHWFEVRKKVEKKVEKNVYKLVTFLLSKSLRFFFLPQSLHFFFIKVLRFVTEVILFLSNSFPSLCVSFGNTPIQRSEIYISELKSSNEQLCNKLFESIGFQIVHLKKLNPFLLEEFDTSNFVINVGTRSPFLLNKIPKRIFDSLPTRTNHSKYFDNKDSYFSKIFHDKDNWLNHPKPFHRSSLISSFYKANQLRFRNHLHHFLFYCNKRFPFSVEKARNTNSHFLYGQFLNILLFRKKIFSLCVGQKKHVFWSRATLSPIESQVSNIFIPKDFPQSGDEGYNLDKYFNFLIQPDPVIRRAISSIVETSGTPLTEAQKGDLERTYCKPLSDINLSDSEVNNFHEYPNFNSNMGLVHILFSGKYLSSEKHSLCLKKGAGVHKERMFTTFQRDSSFSILSETWNLFQTYLPSFFTSTGYKYLTSIFSENFSYLLSILSSRVSLFQDILGLSWRILQIRLSKMPLFLRREISSKWLHNLFLSKEMIRRKTQSSLISKHLRSTKFWEFFYSLLFLLLVAGYLVSIHFFFISRAFSELQTEFKSLKSLMTPSSAIELRKLLDKYPRSEPNSFWLKNIFLVVMEQLRDSLEEIKGFVFGLNRIGLTSGVKSIRFKNFKNKDFNIKGIGIIELILRPITRIAFSLNTRHISHTSKEIYSLIIKRKNVNGVWIDDKIESWVANSDSIHEEERKLLVQLSALTTEKRILLSLTHSDHFSKNDSGYQMIEQPGAIYLRYLVDIHQKHLMNYEFNTSCLAERRIFLAHSQTITYSQTSYGTNSFHFPSHGKPFSLRLALSPSRGILVIGSIGTGRSYLVKYLATNSYVPFITVFPNKFLDKNPQFIDDIDIDNSNNIDASDDIDMDNSDNIDDDIDRDLATELELLTWMNALTMDREMKAEIARLFITLQFELARAMSPCIIWIPNIHDLDVNESNYLSLGLLVNHLSRDCERCSPINILVIASTHIPQKVDPALIAPKKLNTCIKLRRLLIPQQRKYFFTLSYTRGFHLENKMFHTNGFGSITMGPNARDIVALTNEVLSISITQKKSIIDTNTIRSALHRQTWDLQSQVRLVQDHGILFYQIGRAVAQNVLLSNLSNCPIDPISIYLKKKSCNEGDSYLYKWYFELGTSMKKLTILLYLLSCTAGSVAQDLWSLPGPDEKNGITSYGLVENDSDLVHGLLEVEGALVGSSRTEKNCSKFENDRVTLLLRPEPRNPLERRQNGSCSILDQRFLSEKDESEFEEGALAPQQIEEDLFNHIVWAPTIWRPWGFLCIERPNELGFSYWSRSFRGKRILYDEEDELEENDSEFLQSGTMQYKTRDRSSKEKGLFRISQFIWDPADPLFFLFKDRPPGSVFSRLELFADEEMSKGLLTSQTSQIEHLFRYKYPRWFINKTQEKHFEFLIHRQRCLRTNSSLSNRSFRSNTLSESYQYLSNLFLSNGTLLDQMTKTLLRKRWLFPDEMKIGFM
Probable ATPase of unknown function. Its presence in a non-photosynthetic plant (Epifagus virginiana) and experiments in tobacco indicate that it has an essential function which is probably not related to photosynthesis.
A8W3G3
P30778
RUBR_AZOVI
Rubredoxin
Azotobacter
MSARFEGSYLGDATRLADDAVLECKICWQRYDPAEGDPVWQIPPGTPFAALPAHWRCPRCDGDREQFMVVDG
Rubredoxin is a small nonheme, iron protein lacking acid-labile sulfide. Its single Fe, chelated to 4 Cys, functions as an electron acceptor and may also stabilize the conformation of the molecule. Could be involved in hydrogenase-linked redox processes.
P30778
Q2GUT7
SEY1_CHAGB
Protein SEY1
Chaetomium
MNGHFAAVGNGPTAQQYEHGIQVIDEDKAFNTNLNDYLGETRVAEAGFNYHLISVFGSQSTGKSTLLNHLFKTEFSVMSESARRQTTKGIWMSKNKRAGANGDAATMADNILVMDVEGTDGRERGEDQDFERKSALFALATSEVLIVNIWEHQIGLYQGANMGLLKTVFEVNLQLFLKDRQSQTRSLLFFVIRDHVGNTPLANLRDTLVQDLTKIWSTLSKPQGLEDSKIEDYFDFAFAALPHKILQPEKFLEEADKLSTRFTTGHRSAKDQEFVGGVFLPEYHRRIPADGLSVYAEGVWDQIVNNKDLDLPTQQELLAQFRCDEISREVFVGFDSVIVPLEEQQAEATRLGKATVLPDLGVTGAGTREKCVKAFETQASRYHKGVYSVKRGELESKIDARLKALYQTQLSAAHKSGVAAFSDAVTNAVKAGQKAGGYEFAEIVDKQKKKTLEFFKKEAQSLLIQGVAWTNFKPQYRLFEKELDEVSARLRKEEMRRLAIRVERWVKSRLGDSIGVEFNKLGSGRGGSGAPENGEKPATEKDLWDRIWNTFSGIIREAETRFADRAKSFEASPEEVEVGLWRLRRKSWVALREKIEEEMMESNILMKLRENFEDKFRYDEEGVPRIWRPTDDIEGIYTRARESTLGLIPLLARFRLAETYAPPDLPTFVGPQPAGAEPEDEEDLAPIGGVDEEEGKSLEEEMTVLSESKRQDLVVRFKKMADGVYVEAKRSAIGGITQVPLYFYIVLLIFGWNEIVMVLRNPMLFMLLLVMGGGTYVAYTLNLLGPMMQMANAASNQAVEIGKEKLRDFLENNQTMRQAIAMPPRSQDNGIGMDRLDSRGKKAQEVEEDDDI
Cooperates with the reticulon proteins and tubule-shaping DP1 family proteins to generate and maintain the structure of the tubular endoplasmic reticulum network. Has GTPase activity, which is required for its function in ER organization.
Q2GUT7
Q47LK5
RL5_THEFY
50S ribosomal protein L5
Thermobifida
MTVTNEIDAPPIPRLKQKYREEIIPALREEFGYTNIMQVPGLTKIVVNMGVGDAARDAKLIQGAIADLSAITGQKPKINRAKKSIAQFKLRQGQPIGASVTLRGDRMWEFLDRLLTLALPRIRDFRGLSAKQFDGNGNYTFGLTEQVMFHEIDPDKVDRQRGMDITIVTTAATDEEGRSLLRRLGFPFKED
This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.
Q47LK5
C3PKP2
EFTU_CORA7
Elongation factor Tu
Corynebacterium
MAKEKFERTKPHVNIGTIGHVDHGKTTTTAAITKVLADAYPEENTAFAFDMIDKAPEEKERGITINISHVEYSTPKRHYAHVDAPGHADYIKNMITGAAQMDGAILVVAATDGPMPQTREHVLLARQVGVPYILVALNKCDMVDDEEIIELVEMEIRELLAEQDYDEEAPIVHISALKALEGDEKWVQSVIDLMQACDDSIPDPERELDKPFLMPIEDIFTITGRGTVVTGRVERGSLNVNEDIEIIGIKDKSMSTTVTGIEMFRKMMDYTEAGDNCGLLLRGTKREEVERGQVCIKPGAYTPHTKFEGSVYVLKKEEGGRHTPFMDNYRPQFYFRTTDVTGVIKLPEGTEMVMPGDNVEMSVELIQPVAMDEGLRFAIREGSRTVGAGRVTKILD
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
C3PKP2
O55029
COPB2_MOUSE
p102
Mus
MPLRLDIKRKLTARSDRVKSVDLHPTEPWMLASLYNGSVCVWNHETQTLVKTFEVCDLPVRAAKFVARKNWVVTGADDMQIRVFNYNTLERVHMFEAHSDYIRCIAVHPTQPFILTSSDDMLIKLWDWDKKWSCSQVFEGHTHYVMQIVINPKDNNQFASASLDRTIKVWQLGSSSPNFTLEGHEKGVNCIDYYSGGDKPYLISGADDRLVKIWDYQNKTCVQTLEGHAQNVSCASFHPELPIIITGSEDGTVRIWHSSTYRLESTLNYGMERVWCVASLRGSNNVALGYDEGSIIVKLGREEPAMSMDANGKIIWAKHSEVQQANLKAMGDTEIKDGERLPLAVKDMGSCEIYPQTIQHNPNGRFVVVCGDGEYIIYTAMALRNKSFGSAQEFAWAHDSSEYAIRESNSIVKIFKNFKEKKSFKPDFGAESIYGGFLLGVRSVNGLAFYDWENTELIRRIEIQPKHIFWSDSGELVCIATEESFFILKYLSEKVLAAQETHEGVTEDGIEDAFEVLGEIQEIVKTGLWVGDCFIYTSSVNRLNYYVGGEIVTIAHLDRTMYLLGYIPKDNRLYLGDKELNIVSYSLLVSVLEYQTAVMRRDFSMADKVLPTIPKEQRTRVAHFLEKQGFKQQALTVSTDPEHRFELALQLGELKIAYQLAVEAESEQKWKQLAELAISKCQFSLAQECLHHAQDYGGLLLLATASGNASMVNKLAEGAERDGKNNVAFMSYFLQGKLDACLELLIRTGRLPEAAFLARTYLPSQVSRVVKLWRENLSKVNQKAAESLADPTEYENLFPGLKEAFVVEEWVKETHADLWPAKQYPLVTPNEERNVMEEAKGFQPSRPTAQQEPDGKPASSPVIMASQTTHKEEKSLLELEVDLDNLELEDIDTTDINLDEDILDD
This coatomer complex protein, essential for Golgi budding and vesicular trafficking, is a selective binding protein (RACK) for protein kinase C, epsilon type. It binds to Golgi membranes in a GTP-dependent manner.
O55029
A4TPN1
MTNC_YERPP
2,3-diketo-5-methylthio-1-phosphopentane phosphatase
Yersinia
MIQAIVTDIEGTTTDIRFVHQVLFPYARERLTPFLRAHQQDDDIAALLVDLRREIAQPDADIETLITVLHGFMDEDRKSTVLKAIQGIIWRTGYLQADFRGHVYPEVAQQLADWHQQGLKLYVYSSGSVAAQKLLFGYSDAGDLCPLFSGYFDTHVGAKRDVSAYQKIANQLGIAPQALLFLSDIRQELDAAQLAGWHTCQLIRDLPDNDSAHPQVNRFDQIVLSLFTE
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).
A4TPN1
Q9GZL7
WDR12_HUMAN
WD repeat-containing protein 12
Homo
MAQLQTRFYTDNKKYAVDDVPFSIPAASEIADLSNIINKLLKDKNEFHKHVEFDFLIKGQFLRMPLDKHMEMENISSEEVVEIEYVEKYTAPQPEQCMFHDDWISSIKGAEEWILTGSYDKTSRIWSLEGKSIMTIVGHTDVVKDVAWVKKDSLSCLLLSASMDQTILLWEWNVERNKVKALHCCRGHAGSVDSIAVDGSGTKFCSGSWDKMLKIWSTVPTDEEDEMEESTNRPRKKQKTEQLGLTRTPIVTLSGHMEAVSSVLWSDAEEICSASWDHTIRVWDVESGSLKSTLTGNKVFNCISYSPLCKRLASGSTDRHIRLWDPRTKDGSLVSLSLTSHTGWVTSVKWSPTHEQQLISGSLDNIVKLWDTRSCKAPLYDLAAHEDKVLSVDWTDTGLLLSGGADNKLYSYRYSPTTSHVGA
Component of the PeBoW complex, which is required for maturation of 28S and 5.8S ribosomal RNAs and formation of the 60S ribosome.
Q9GZL7
A1USS3
RECA_BARBK
Recombinase A
Bartonella
MDKKKALDAALSQIERSFGKGSIMRLGQKEGVVEIETISTGSLSLDIALGVGGLPKGRIIEIYGPESSGKTTLALHAIAEAQKNGGVCAFVDAEHALDPIYARKLGVDLENLFVSQPDTGEQALEITETLVRSGAVDVLVVDSVAALTPRAEIDGEMSDSLPGLQARLMSKALRKLTASIFRSNCMVIFINQIRMKIGVMFGSPETTTGGNALKFYASVRLDIRRIGSIKDKELVVGNQTRVKVVKNKLAPPFKQVEFDIIYGEGISKLGELIDLGVKVGIVEKSGAWFSYNSQRLGQGRENAKQFLREHAEIAAEIETALRQNAGLLAIELLENVGADNIENDEEI
Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage.
A1USS3
O83822
IF3_TREPA
Translation initiation factor IF-3
Treponema
MYWGGSLADNKSLRINGSIRVREVRLVDAVGQQCGVVPTPEALRMARDINLDLVEVAPQASPPVCKILDYGKYRFEMGKKLRDSKKRQRLQTLKEVRMQPKINDHDMAFKAKHIQRFLDEGDKVKVTIRFRGRELAHTDLGFNVLQNVLGRLVCGYSVEKQAAMEGRSMSMTLTPKSKK
IF-3 binds to the 30S ribosomal subunit and shifts the equilibrum between 70S ribosomes and their 50S and 30S subunits in favor of the free subunits, thus enhancing the availability of 30S subunits on which protein synthesis initiation begins.
O83822
Q3AFM4
ISPE_CARHZ
4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase
Carboxydothermus
MLIFAPAKINLTLDILGKRPDGYHELWSVMQAITLGDLVEIEPAEGINLRVVGADLPVDSTNIAFKAVQALRAATGKAIGASITIRKKIPLEAGLAGGSADGAAVLYGLNKLYNLNLSQEELLEIGAKISADIPFCLTGGTALVQGIGEKVKKLPPLKKGYFVIYKPPFGISTKEAYLRLAGKDLTKEHPDREKILKALGKENLEDLGKFLKNLLEISALEINPEIYKYKNELLNLKPLGVLMSGSGSALFALTENLKKAKEIYYQLTLPGQKFIVRPYAAGPTCLKL
Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
Q3AFM4
Q4QLA3
SUCC_HAEI8
Succinyl-CoA synthetase subunit beta
Haemophilus
MNLHEYQAKQLFEHYGLPVKNGAVCQSVEDVDLVLAQLSGDKWAAKCQVHAGGRGKAGGVKLVQDVEEARAFAEKWLGQRLVTFQTDKLGQPVNQIYFEETCDIDKEFYLSAVVDRASQKVMFIASPAGGMNIEEVAQNSLHLLHKVEIDPLFGGLPYQGRELAFKLGLSGTQNKQFTDIFMGLSRLFLEKDLSLVEVNPLVLTKQGYLVCLDAKISVDDNALFRHKDLLALQDLTQNDAREAEAEKFQLNYVALEGDIGCMVNGAGLAMGTMDIVKLYGGKPANFLDVGGGATKERVAEAFKIILTDPSVKVILVNIFGGIVRCDLIAEGVIAAVNEVGVRVPVVVRLEGTNAEMGRQILAQSDVNILTAQSLQQAAELAVNAAKGEH
Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
Q4QLA3
Q9ZDY5
QUED_RICPR
Queuosine biosynthesis protein QueD
typhus group
MIKCTRRINFDAGHRIIGHKNKCQFLHGHHYVLEITIAANKTDTLGMVIDFGLIKNLAKKWIDANFDHNLILHQDDKEMGQQIENYTRQKIYYMRNNPTAENIATHLKNEIFPKLFVSQNFFVTSLKLYETQNCFVEV
Catalyzes the conversion of 7,8-dihydroneopterin triphosphate (H2NTP) to 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) and acetaldehyde.
Q9ZDY5
B8FKD5
DNLJ_DESAL
Polydeoxyribonucleotide synthase [NAD(+)]
Desulfatibacillum
MQDLPSSIADISDPELLGQWLEKYNEAYRAGKPMISDAHYDLLVERLREIAPDHGFLSAVEAETFADKREVRHPAPMLSTEKAYDKQSLERFVERVYKEAAQIGVTDVLFQVTPKLDGLAARDDGQILATRGNGYAGYDITNALEKGVIPQGGRGLGLGEIVAVQSYFQENLADRFEHPRNMVVGIISSDVLNISAKQALEDKQVHFVPYATLNKWEGSGKELLENSEKITQDLIQATDYPMDGMVASVMNQDVRDHMGATSHHYRWQIAIKAKGETGVTTVNAITWQVGRTGNVTPVLEVEPLKLSGATIRRVTAHNAGRIREKGAGVGASIEVIRSGEVIPKLENVLTPSDDTLIPENCPVCETPLEWNNDFLKCPNLNCKARVEQRIRHWFRILGNADWFGIKTVERLVAGGFDSLEKIYAMTEEDFLSLEFGPVQSKNLAEAINLSKSRPVEDWRFLAAFGISDLGEGDSRKILSFFPLEELLDKTRDDIVALHGFGDVTSISIEKGLKALGPTIRHMLDLGFNLQPTPLKSEMDVSSPISGKGVVFTGSMETGSRKDMEENARSLGANVQKAVTGKTDYLICGAKVGAKKTQKAQDLGVTVLTEQEYLQLVEGGESQSSPEQMSLF
DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
B8FKD5
C6E345
ACP_GEOSM
Acyl carrier protein
unclassified Geobacter
MASIEKRIKEIVAEQLGVDEAQVTNESSFMDDLGADSLDTVELVMALEEEFEIEISDEDAEKIQSVQDAIDYITDHT
Carrier of the growing fatty acid chain in fatty acid biosynthesis.
C6E345
B4EAS0
Y800_BURCJ
Nucleotide-binding protein BceJ2315_08000
Burkholderia cepacia complex
MRIVLITGISGSGKSVALNALEDAGYYCVDNLPPHVLPELARYLAQDGQRRLAVAIDARSSASLDEMPGLIRELSREHDVRVLFLNASTQALIQRFSETRRRHPLSGSLSHDADVGLLSSLEEAIERERELVAPLAEFGHQIDTSTLRANALRTWVKRFIEQKNNDLMVMFESFGFKRGVPLDADLMFDVRALPNPYYDHQLRPLTGLDQPVIAFLDALPIVHQMIDDIHAFLMKWLPHFRDDNRSYLTVAIGCTGGQHRSVFIAETLAARLAREANVIVRHRDAPVDVDASSRLVSEVDRP
Displays ATPase and GTPase activities.
B4EAS0
B8FPL1
SCPA_DESHD
Segregation and condensation protein A
Desulfitobacterium
MSNGSSVSHSANTAPYVELPAFQGPMDLLLHLIQQEKVDIYDIPIARITDQFIQVVRQMEDLDMEVTTEFLVLAAQLLQIKSRYLLPKPVKDVTVEEEGDPRQELVERLLAYRAFKQAAETLGEIQISSGQRYFREVDVDGLRSQFTPADPLAGIHFEALWHAFQRIIERAEQGEEIRTVEPDEIPIEVMVNDVLRRVILHPRGLRFSQLIRGTKRMEIIVSFLALLELLKSGKVHCEQSSQNEEIFVFPTEKAWEFTEGE
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.
B8FPL1
Q5F8C0
GLYA_NEIG1
Serine hydroxymethyltransferase
Neisseria
MFSKSVTLAQYDPDLAAAIAQEDRRQQDHVELIASENYVSCAVMEAQGSQLTNKYAEGYPAKRYYGGCEYVDIVEQLAIDRVKELFGAAYANVQPHSGSQANQAVYASVLKPGDTILGMSLAHGGHLTHGASVNISGKLYNAVTYGLDENEVLDYAEVERLALEHKPKMIVAGASAYALQIDWAKFREIADKVGAYLFVDMAHYAGLVAGGEYPNPVPFCDFVTTTTHKTLRGPRGGVILCRDNTHEKALNSSIFPSLQGGPLMHVIAAKAVAFKEALQPEFKQYAKQVKINAAVMAEELVKRGLRIVSGRTESHVFLVDLQPMKITGKAAEAALGKAHITVNKNAIPNDPEKPFVTSGIRIGSAAMTTRGFNETDARVLSNLVADVLANPEDEANLAKVRGQVTALCDKYPVYGT
Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
Q5F8C0
Q9D273
MMAB_MOUSE
Methylmalonic aciduria type B homolog
Mus
MAVWLFGGRLGLRGRLSACRLLCPRFQSRGPQGGEDGDRLQPSSTAAKIPKIYTKTGDKGFSSTFTGERRPKDDQVFEAVGTTDELSSAIGFAMELVTEKGHMFAEELQKIQCMLQDVGSALATPRSSAREAHLKHTAFQEGPVLELERWIDKYSSQLPPLKAFILPSGGKSSSALHFCRAVCRRAERRVVPLVQMGETDANVAKFLNRLSDYLFTVARYAAMKEGSQEKIYKKHDV
Converts cob(I)alamin to adenosylcobalamin (adenosylcob(III)alamin), a coenzyme for methylmalonyl-CoA mutase, therefore participates in the final step of the vitamin B12 conversion. Generates adenosylcobalamin (AdoCbl) and directly delivers the cofactor to MUT in a transfer that is stimulated by ATP-binding to MMAB and gated by MMAA.
Q9D273
Q16DS2
BCHL_ROSDO
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Roseobacter
MSPLDRTPPSLRGQDGEGSVQVHQDETAKIEGAKVFSVYGKGGIGKSTTSSNLSAAFSMLGKRVLQIGCDPKHDSTFTLTGSLVPTVIDILKEVDFHPEELRAEDFVFDGFNGVKCVEAGGPPAGTGCGGYVVGQTVKLLKQHHMLEDTDVVIFDVLGDVVCGGFAAPLQHADRALIVTANDFDSIYAMNRIIAAVQAKSKNYKVRLAGCVANRSRETDEVDRYCDTVGFNRIAHMPDLDAIRRSRLKKKTLFEMPDDEEIVQVRKEYIRLAETLWNGTEPLAPAPLPDRDIFELLGFD
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.
Q16DS2
Q02372
NDUB8_BOVIN
NADH-ubiquinone oxidoreductase ASHI subunit
Bos
MAAARAGVLGVRWLQKAARNVVPLGARTASHITKDMLPGPYPKTPEERAAAAKKYNMRVEDYEPYPDDGTGYGDYPKLPDRSQQERDPWYDWDHPDLRLNWGEPMHWDLDMYIRNRVDTSPTPVNWNLMCKHLFGFVAFMLFMFWVGETYPAYQPVGPKQYPYNNLYLERGGDPNKEPEPVVHYEI
Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Q02372
P0CB52
NANE_STRSU
ManNAc-6-P epimerase
Streptococcus
MGKISKEALKEQIKDGIIISCQALPGEPLYREEGGIMPLLVKAAQEAGAVGIRANSVRDIKEIKEVTTLPIIGIIKRDYPPQEPFITATMREVDELAALDIEVIALDCTKRERYDGLDIVDFINQIKEKYPEQLFMADISTFEEGLTAYEAGIDFIGTTLSGYTSYSRQEEGPDIELVDRLCRAGIDVIAEGKIHYPDQVKIIHDLGVAGIVVGGAITRPKEIAERFISALHK
Converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N-acetylglucosamine-6-phosphate (GlcNAc-6-P).
P0CB52
B7VKY2
CYSN_VIBA3
Sulfate adenylate transferase
Vibrio
MNSAVEAELAELGIEGYLSQHQHKSMLRFLTCGSVDDGKSTLIGRLLHDTKQIYEDQLAAVHSDSQRVGTTGEKPDLALLVDGLQAEREQGITIDVAYRYFSTQKRKFIIADTPGHEQYTRNMATGASTCDLAVILIDARKGVLDQTRRHSFISNLLGLKHFIVAVNKMDLVDYSQDRFEEIRDQYLEFAENLEGETNIQILPVSALEGINVAAPSKELAWFEGPSLLEVLENVDIDQKRSAGEFRFPVQYVNRPNLDFRGFAGTVASGRVSVGDEIKALPSGKTSKVARIVTFDGDLESAQAGLAVTLTLEDEIDISRGDLIVLENAQIESTNHVLADIVWMTEQPLQPGKAYDIKIAGKKTVGQVETVRHQYDINNLSTHAVDELPLNGIGLCEWSLNETVALDKYRESADTGGFIVIDRLTNVTVGAGLIRDRLDSVEQQVGNFSAFELEFNALVRKHFPHWDAKDLSQLLKS
With CysD forms the ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric-sulfuric acid anhydride bond driven by GTP hydrolysis by CysN coupled to ATP hydrolysis by CysD.
B7VKY2
Q65PM2
DNAA_BACLD
Chromosomal replication initiator protein DnaA
Bacillus
MKNISDLWNQALGQIEKKLSKPSFETWMKSTKAHSLQGDTLIITAPNEFARDWLESRYLHLIADTIYDLTGEELSIKFVIPQNQNEEDFMPKSPIKKMSKEEPADFPQNMLNPKYTFDTFVIGSGNRFAHAASLAVAEAPAKAYNPLFIYGGVGLGKTHLMHAIGHYVIDHNPSAKVVYLSSEKFTNEFINSIRDNKAVDFRNRYRNVDVLLIDDIQFLAGKEQTQEEFFHTFNTLHEETKQIVISSDRPPKEIPTLEDRLRSRFEWGLITDITPPDLETRIAILRKKAKAEGLDIPNEVMLYIANQIDSNIRELEGALIRVVAYSSLINKDINADLAAEALKDIIPSSKPKVITIKDIQRIVGQQFNIKLEDFKAKKRTKSVAFPRQIAMYLSREMTDSSLPKIGEEFGGRDHTTVIHAHEKISKLLSDDEQLQQQIKEIKEQLR
Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids.
Q65PM2
Q8H186
PBL1_ARATH
Protein CHANGED CALCIUM ELEVATION 5
Arabidopsis
MGSCLSSRVLNKSSSGLDDLHLSSCKSSSSATAHKTEGEILSSTTVKSFSFNELKLATRNFRSDSVVGEGGFGCVFRGWLDETTLTPTKSSSGLVIAVKRLNPDGFQGHREWLTEINYLGQLSHPNLVKLIGYCLEDEQRLLVYEFMHKGSLENHLFANGNKDFKPLSWILRIKVALDAAKGLAFLHSDPVKVIYRDIKASNILLDSDFNAKLSDFGLARDGPMGEQSYVSTRVMGTFGYAAPEYVSTGHLNARSDVYSFGVVLLELLCGRQALDHNRPAKEQNLVDWARPYLTSRRKVLLIVDTRLNSQYKPEGAVRLASIAVQCLSFEPKSRPTMDQVVRALVQLQDSVVKPANVDPLKVKDTKKLVGLKTEDKYQRNGLNKKTVGL
Contributes to pathogen-associated molecular pattern (PAMP)-triggered immunity (PTI) signaling, including calcium signaling and root growth inhibition, and defense responses downstream of FLS2 . Acts additively with BIK1 in PTI defenses . Seems not required for flg22-induced MAPK activation (Probable). Required for Pep1-induced defenses . Pep1 is an endogenous elicitor that potentiates PAMP-inducible plant responses .
Q8H186
B1MD87
IF2_MYCA9
Translation initiation factor IF-2
Mycobacteroides abscessus
MAGKARVHELAKELGVTSKEVLARLSDQGEFVKSASSTVEAPVARRLRESFGGGDKPAPAASNGAAAEAAAPPKKAGPKPGAPKPAPKKVAEPVVEAPVAPEPPAAPAAPAAPAPKPSPAARPAAAEAAAPAPAPAPAPRPGATPGPKPGAPRVPRVGNNPFSSAQPAERPAPRPQAPRPGAPRPGGASPSNMPPRPSPGSMGPRPPRPGGGPRPGGGPRPGGAGRPGGGGGGNYRGGGTGTGAPAGGPPGAGGGFRGRPGGGGGGGRPGQRGGAAGAFGRPGGAPKRGRKSKRAKRAEYENMQAPVVGGVRLPHGNGEVIRLARGASLSDFAEKIDANPASLVQALFNLGEMVTATQSVGDETLELLGGEMNYVVQVVSPEDEDRELLESFDLTYGEDEGGEEDLRTRPPVVTVMGHVDHGKTRLLDTIRKANVREGEAGGITQHIGAYQVAVEHDGTERPITFIDTPGHEAFTAMRARGAKATDIAILVVAADDGVMPQTVEAINHAQAADVPIVVAVNKIDKEGADPAKIRAQLTEYNLVAEDFGGDTMFVDISARQGTNIEQLLEAVLLTADAALDLRANPDMEAQGVAIEAHLDRGRGPVATVLIQRGTLRVGDSIVAGDAYGRVRRMVDEHGEDVEEALPSRPVQVIGFTSVPGAGDNLLVVDEDRIARQIADRRSARKRNALAARSRKRISLDDLDAALKETSQLNLILKGDNAGTVEALEEALLGIAIDDEVQLRVIDRGVGGVTETNVNLASASDAIIIGFNVRAEGKATELANREGVDIRYYSVIYQAIDEIESALKGMLKPVYEEVELGRAEIRAMFRSSKVGNIAGCLVTSGIIRRNAKARLLRDNIVVAETVTISSLRREKDDVVEVRDGYECGLTLTYNDIKEGDVIEAYELREKERV
One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex.
B1MD87
Q9USN3
UTP13_SCHPO
Probable U3 small nucleolar RNA-associated protein 13
Schizosaccharomyces
MAPIGEKKRFELEKSIEPIYTGGPVAFDSNEKILVTALTDRIIGTRSETGERLFSIKKDEDDYVTALAITSDSKKLIAAFRSRLLTIYEIPSGRRIKSMKAHETPVITMTIDPTNTLLATGGAEGLVKVWDIAGAYVTHSFRGHGGVISALCFGKHQNTWVLASGADDSRVRLWDLNSSRSMAVFEGHSSVIRGLTFEPTGSFLLSGSRDKTVQVWNIKKRSAVRTIPVFHSVEAIGWVNGQPEEKILYTAGEGNLILAWDWKSGSRLDPGVDTTHSETNAIIQVVPFSENTLLSVHSDLSLLLRKRVPGEGFITIKKLNGSFDEVIDCAWIGDDHLAVCSNTEFIDVISTDGTQVFGVLEGHTDIVLTLDSSEDGVWLATGAKDNTVRLWNLNIEDNVYKCIHVFTGHTASVTAVALGPLDVNGYPTFLASSSQDRTLKRFNLGSQLNKSDFSNRAVWTIKAHDRDVNAIQVSKDGRIIASASQDKTIKLWDSSTGEVVGVLRGHRRGVWACSFNPFSRQLASGSGDRTIRIWNVDTQQCVQTLEGHTGAILKLIYISQGTQVVSAAADGLVKVWSLSSGECVATLDNHEDRVWALASRFDGSLLVSGGADAVVSVWKDVTEEYIAKQAEELERRVEAEQLLSNFEQTEDWQQAIALALSLDRPHGLLRLFERVMTAPHQPNSITGNKDVDNVLVQLPDHQLIILFQRIRDWNTNSKTSMVAQRLLRLLLHSYSPEHLLKLSGIKDILDSMIPYTDRHLARVNDLIEDSYIVDYVI
Involved in nucleolar processing of pre-18S ribosomal RNA.
Q9USN3
B0G172
PGTB2_DICDI
Type II protein geranyl-geranyltransferase subunit beta
Dictyostelium
MTDNINKESTTTTTTIDHTTNLLIDKHVEYIVKLGSKKDSFEYWVTEHIRMNGMYWGLSSLYLLKSLDKLDKNEVIQWLLSCQKSNGGFGGNTSHDDHLLSTLSAVQILIQYDALDKIDINSVVDYVVKLQREDGSFVGDQWGEVDTRFSYAAIMCLSLLKSLDKINCEKAVEYILSCQNFDGGFGSIPGAESHAGQIFTCVGALSILNEINKIDIDKLGWWLSERQLPNGGLNGRPEKSSDVCYSWWVLSALSAIDRLHWIDNDKLKSYILKCQDNETGGIADKPGDIPDVFHTFFGICGLSLMGYFKDQIESIDPVYALGTKTLQKLGLNLPWNKNL
Catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to both cysteines in Rab proteins with an -XXCC, -XCXC and -CCXX C-terminal.
B0G172
Q8MJ02
NCTR3_MACMU
Natural killer cell p30-related protein
Macaca
MAWMLLLILIMVYPGSCALWVSQPPEIRTLEGSSAFLPCSFNASQGRLAIGSVTWFRDEVAPGKEVRNGTPEFRGRLAPLSSSRFLRDHQAELHIWDVRGHDAGIYVCRVEVLGLGVGTGNGTRLVVEKEYPQLGAGTVLLLRAGFYAVSFLSVAMGSTLYYQGKCLTWKGPRRQLPAVVPGPLPPPCGSSAHLLPPVPGG
Cell membrane receptor of natural killer/NK cells that is activated by binding of extracellular ligands including BAG6 and NCR3LG1. Stimulates NK cells cytotoxicity toward neighboring cells producing these ligands. It controls, for instance, NK cells cytotoxicity against tumor cells. Engagement of NCR3 by BAG6 also promotes myeloid dendritic cells (DC) maturation, both through killing DCs that did not acquire a mature phenotype, and inducing the release by NK cells of TNFA and IFNG that promote DC maturation.
Q8MJ02
P49173
NIP1_NICAL
Pollen-specific membrane integral protein
Nicotiana
MAKKDGNQEEEISQMEEGNIHSASNSDSNVGFCSSVSVVVILQKLIAEAIGTYFVIFAGCGSVAVNKIYGSVTFPGICVTWGLIVMVMVYTVGYISGAHFNPAVTITFSIFGRFPWKQVPLYIIAQLMGSILASGTLALLFDVTPQAYFGTVPVGSNGQSLAIEIIISFLLMFVISGVATDDRAIGQVAGIAVGMTITLNVFVAGPISGASMNPARSIGPAIVKHVYTGLWVYVVGPIIGTLAGAFVYNLIRSTDKPLRELAKSASSLRS
Aquaporins facilitate the transport of water and small neutral solutes across cell membranes.
P49173
P56363
RK14_CHLVU
50S ribosomal protein L14, chloroplastic
Chlorella
MIQPQTYLRVADNTGARELMCIRVLGGGKQRAATVGDIIIAVVKDATPNMPVKRSDIVRAVIVRTRKNVRRVNGTSIRFDENAAVIINKENNPRGTRVFGPVARELRDGNFTKIISLAPEVL
Binds to 23S rRNA.
P56363
Q608N1
MIAB_METCA
tRNA-i(6)A37 methylthiotransferase
Methylococcus
MPQKLYIETFGCQMNEYDSAKMRDLLEVSDSFELARSPEEADVLLLNTCSIRDKAQEKVFSQLGRWRPIKLRRPEVVIGVGGCVASQEGEALQKRAPYVDIVFGPQTLHRLPSMLEQVRCERRPVVDVSFPAIEKFDALPEPRADGPKAFVSVMEGCGKYCTFCVVPYTRGEEISRPVDDVIAEIVALAEQGVREVNLLGQNVNAYRGVLADGGMADLALLMHYVAAVDGIDRIRFTTSHPVEFSDALIEAFRDIPQLVSHLHLPVQSGSDRILRLMKRGHTRAEYMAKVAKLREIRPDLSLSSDFIVGFPGETDEDFEDTMALIEQLGFDQSFSFIFSARPGTPAAAMADDVPPETKRARLARLQAKIADNAAKIGASMVGSIQSVLVEGTSRKNFNELSGRTENNRVVNFAGHPRLIGQFVDVVITESLPNSLRGRLIGVAHESDFISPDSTAQIA
Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
Q608N1
Q2JTR0
TRMD_SYNJA
tRNA [GM37] methyltransferase
unclassified Synechococcus
MRFDVITLFPEFFATPLRIGLVGKALEQGIAEVHCTNPRDFATDKHRRVDDEPYGGGVGMVLKPEPFFAAVASLPRLDPCEIILLTPQGQPLNQALLQELAQKAQLILLCGQYEGFDERIRQHLATREVSLGDFVLTGGEIPALALINGVVRLLPGTVGKIDSLRSESFETGLLEYPQYTRPPEFQGHKVPPVLLSGDHRAIARWRLQQQLVRTWRRRPDLLAKRPLTPEEQQLLAEGLAEQHTDVEEQDRCL
Specifically methylates guanosine-37 in various tRNAs.
Q2JTR0
P11841
CASK_PIG
Kappa-casein
Sus
MMKSSFLIVPILALTLPFLGAEEQNQEKLTRCESDKRLFNEEKVKYIPIYYMLNRFPSYGFFYQHRSAVSPNRQFIPYPYYARPVVAGPHAQKPQWQDQPNVYPPTVARRPRPHASFIAIPPKKNQDKTAIPAINSIATVEPTIVPATEPIVNAEPIVNAVVTPEASSEFLITSAPETTTVQVTSPVV
Kappa-casein stabilizes micelle formation, preventing casein precipitation in milk.
P11841
A0KFN8
MEND_AERHH
Menaquinone biosynthesis protein MenD
Aeromonas
MSARQEFASHHATFNHVWSSLLLEELFRLGVRDIALASGSRSAPLTMAAAAHPGFRRHLHFDERGLGFMALGLAKGSGRPVAVIMTSGTAVANLWPAVAEAQLTGVPLIILSADRPPELIDNGANQAIDQQGIFGRYPVYQQNLPSPTATIPAAFVLSSVDQALAQQARTPGPVHFNCMYPEPLYPGDAYLDFSAYLAPLGDWLRSSEPWSPWQLTQAPCPCQPDWDELQGKRGLIVAGRIQDPVQAKAVAALAERLGWPLLADLQSQLRFDGRNLVHADLALQHSGFVAELARAEVLLQFGARLISKRLGQFIKQQPWQAYWLIDPQPARLDPDYRLRRRLLCDPAAFAAAHPVAHPHLPWHRLAERQQAVSQQVRSACERFSELGVCHRLNQLIRGQLFVGNSMPARLMDMLGEAGKGPSRVMTNRGASGIDGLIATAYGFAQSVQPGSNEPTTLLLGDLSALHDLNSLALLGKSSRPLVVILLNNDGGSIFRMLPVPTQDALLETYYCLPHGLHFEHAAAMFGLHYRTPASLADFERDYTTALEKGVTLIEIKVPSSEVAEDLKALGSAIRGS
Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).
A0KFN8
B7GLA4
QUEC_ANOFW
Queuosine biosynthesis protein QueC
Anoxybacillus
MKKEKAVVVFSGGQDSTTCLFWAKKHFAEVEAVTFDYNQRHRLEIDVAASIAKELNVSHTVLDMSLLHQLAPNALTRSDIAIEQKEGQLPSTFVDGRNLLFLSFAAVLAKQKGARHLVTGVCETDFSGYPDCRDVFIKSLNVTLNLAMDYQFVIHTPLMWLNKAETWKLADELGALEFVRNKTLTCYNGIIADGCGECPACVLRKRGLDQYMNEKKGANVR
Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
B7GLA4
Q319F1
FABZ_PROM9
Beta-hydroxyacyl-ACP dehydratase
Prochlorococcus
MDNKLSSENNQLSSEKILGLLPHRYPFALVDKVIENIPGERAVAVKNVTINEPQFQGHFPERPLMPGVLIVESMAQVGGIIVTQMPDLPKGLFVFAGINNVKFRKPVLPGDQLIITCDLLSIKRQRFGKVKGEAHVDGNLVCAGELMFSLVD
Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
Q319F1
A1JNP6
CYOE_YERE8
Heme O synthase
Yersinia
MMIKQYLQVTKPGIIFGNLISVVGGFLLASKGVIDYPLFLATLFGVSLVVASGCVFNNYIDRDIDRIMERTKNRVLVKGLIDPKVSLIYASILGIAGMLLLYVGANPLAMWLAVIGFVIYVGVYSLYMKRKSVYGTLIGSLSGAAPPVIGYCAVTGQFDMGALILLLIFSLWQMPHSYAIAIFRFKDYQAANIPVLPVIKGISVTKNHITLYILAFMVATLMLTLSGYAGYKYLVVAAAVSVWWLGMALRGYKATNDSVWARKLFVFSIIAITSLSVMMSVDFNVPSSAGLLTYVG
Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
A1JNP6
Q9GZY6
NTAL_HUMAN
Williams-Beuren syndrome chromosomal region 5 protein
Homo
MSSGTELLWPGAALLVLLGVAASLCVRCSRPGAKRSEKIYQQRSLREDQQSFTGSRTYSLVGQAWPGPLADMAPTRKDKLLQFYPSLEDPASSRYQNFSKGSRHGSEEAYIDPIAMEYYNWGRFSKPPEDDDANSYENVLICKQKTTETGAQQEGIGGLCRGDLSLSLALKTGPTSGLCPSASPEEDEESEDYQNSASIHQWRESRKVMGQLQREASPGPVGSPDEEDGEPDYVNGEVAATEA
Involved in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. May also be involved in BCR (B-cell antigen receptor)-mediated signaling in B-cells and FCGR1 (high affinity immunoglobulin gamma Fc receptor I)-mediated signaling in myeloid cells. Couples activation of these receptors and their associated kinases with distal intracellular events through the recruitment of GRB2.
Q9GZY6
Q6MTZ0
YQGF_MYCMS
Putative pre-16S rRNA nuclease
Mycoplasma
MTQSIIALDIGSKTIGLAYSSGVIASSLDTIRFEEYNFDQGLRQLESYLKKYNPTIIVVGYPKNMNNTIGERAEMVDYVIEMFLDMYKNFNKDQIIRIDERRTTKIAKNILIQANLTREKQKKYKDSLAAQLILELYLESRKL
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
Q6MTZ0
Q1IS40
NUOH2_KORVE
NDH-1 subunit H 2
Candidatus Koribacter
MGSIALFLLVALIKVVLVIFVLLTAVAYTVWLERKVVGRMQNRWGPTRVGPFGLLQPLADGLKFILKEDLLPPHVNKPLYILAPMLAVAMALLSISIVPFGGTLTIGHITTPLQITGIMGANGQPVDINIGLLIILGVTSIGVYGIALAGWSSNSKYSLLGSLRASAQMVSYEVSLGLSLVGVLLLSGSFSLREIVRLQQGGFWNWNIFGGFQFIAFFIYLTSAYAETNRIPFDLPEAETELVAGYHTEYSSMKFAMFFMAEYANMVTVACIASILFLGGWSGPVPGFLPPILQSLVPVFWFCLRIFAFLFIYIWVRGTLPRFRYDQLMAFSWKFLLPLSIANIMVTALFVALK
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone.
Q1IS40
Q8XAA4
RLMN_ECO57
tRNA m2A37 methyltransferase
Escherichia
MSEQLVTPENVTTKDGKINLLDLNRQQMREFFKDLGEKPFRADQVMKWMYHYCCDNFDEMTDINKVLRGKLKEVAEIRAPEVVEEQRSSDGTIKWAIAVGDQRVETVYIPEDDRATLCVSSQVGCALECKFCSTAQQGFNRNLRVSEIIGQVWRAAKIVGAAKVTGQRPITNVVMMGMGEPLLNLNNVVPAMEIMLDDFGFGLSKRRVTLSTSGVVPALDKLGDMIDVALAISLHAPNDEIRDEIVPINKKYNIETFLAAVRRYLEKSNANQGRVTIEYVMLDHVNDGTEHAHQLAELLKDTPCKINLIPWNPFPAAPYGRSSNSRIDRFSKVLMSYGFTTIVRKTRGDDIDAACGQLAGDVIDRTKRTLRKRMQGEAIDIKAV
Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity.
Q8XAA4
Q9XB61
CARA_PECCC
Carbapenam-3-carboxylate ligase
Pectobacterium
MSNSFCVVYKGSDTDINNIQRDFDGKGEALSNGYLFIEQNGHYQKCEMERGTAYLIGSLYNRTFLIGLAGVWEGEAYLANDAELLALLFTRLGANALALAEGDFCFFIDEPNGELTVITESRGFSPVHVVQGKKAWMTNSLKLVTAAEGEGALWFEEEALVCQSLMRADTYTPVKNAQRLKPGAVHVLTHDSEGYSFVESRTLTTPASNQLLALPREPLLALIDRYLNAPLEDLAPRFDTVGIPLSGGLDSSLVTALASRHFKKLNTYSIGTELSNEFEFSQQVADALGTHHQMKILSETEVINGIIESIYYNEIFDGLSAEIQSGLFNVYRQAQGQVSCMLTGYGSDLLFGGILKPGAQYDNPNQLLAEQVYRTRWTGEFATHGASCYGIDIRHPFWSHSLISLCHALHPDYKIFDNEVKNILREYADSLQLLPKDIVWRKKIGIHEGSSVNQAFANVLGSTVDNYQTKSRFTYRVYQAFLRGRLSITDVTPSQLKDLIKKD
Involved in the biosynthesis of carbapenam-3-carboxylate, a beta-lactam antibiotic of the carbapenem class. Catalyzes the ATP-dependent formation of (3S,5S)-carbapenam-3-carboxylate from (2S,5S)-5-carboxymethylproline.
Q9XB61
Q2LR33
ENO_SYNAS
2-phosphoglycerate dehydratase
Syntrophus
MTEIIEVHAREILDSRGNPTVEAEVTLLSGISGRASVPSGASTGEHEMLELRDGDPKRYLGKGVTQAVNNVIEKIAPEIVGMDCLNQRDIDYTMIALDGTENKGALGANAILSVSIACAKAAAAVVELPLYRYLGGVQAKDIPVPMMNIINGGQHADNNVDIQEFMIMPVGAPTFREGLRMSAEVFHNLKAVLKGKGYNTAVGDEGGFAPNLASNEEALAVIMAAITRAGYEPGKDIAIALDAAASSFYEKGKYILAAEKKPEKTADEMIRFYEDLANRYPIISLEDGLAEDDWEGWKALTQAMGSRIQIVGDDLFVTNKKRLEQGISKGIANSILIKLNQIGSLTETLETIQTAKEAGYTNVVSHRSGETEDSFMADVAVAANCGQIKSGSLSRSERLAKYNQLLRIEEELGDRAVYRGRSALYSVR
Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
Q2LR33
Q9NHE5
CAPS_DROME
Calcium-activated protein for secretion
Sophophora
MIDPSSSEEEGEDDAVPNVSSKGRLTNTTKGTSAVSIIGGSAGSVVGSNIPVSGSNTDLIGNQRQSNISSICNRNDVGNISVAALGSTSNKIEQICGNRADTGNLEVPSNGIPSGISQETLNQSVGSSRANSLPRPLSPSPSLTSEKHETAEPHGKHEREEEERKRRIQLYVFISRCISYPFNAKQPTDMTKRQTKISKQQLEIITQRFQAFLKGETQIMADEAFQNAVQSYHDVFLKSERVLKMVQSGASSQHDFREVFRNNIEKRVRSLPEIDGLSKETVLTSWMAKFDIILKGTGEEDSKRPSRMQQSLNSELILSKEQLYDMFQQILLVKKFEHQILFNALMLDSADEQAAAIRRELDGRMQRVGEMEKNRKLMPKFVLKEMESLYVEELKSSINLLMANLESLPVSKGNMDSKYGLQKLKRYNHSTPSFLKLILRSHGSLSKLEGDSEDGSTQLTKLDVVLTFQLEVIVMEVENGEKLQTDQAEASKPMWDTQGDFTTTHPLPVVKVKLYTENPGMLALEDKELGKVTLKPTPLSSKSPEWHRMIVPKNLPDQDIRIKIACRLDKPLNMKHCGYLYAIGKSVWKKWKRRYFVLVQVSQYTFAMCSYKEKKSEPSEMMQLDGYTVDYIEAASANLMFGIDLNGGRYFFNAVREGDSISFACDDENECSLWVMAMYRATGQSHKPTPPITQDKNSAMSKIQGDADKARKHGMEDFISTDPCTFDHATLFKTLQNLTLEYRLNDPYASLGWFSPGQVFVLDEYCARYGVRGCYRHLCYLSDLLDRAEKQHMIDPTLIHYSFAFCASHVHGNRPDGVGSITHEEKEKFSEIKERLRQLLEFQITNFRYCFPFGRPEGALKATLSLLERVLMKDIVTPVPPEEVRQMIKKSLETAALVNYTRLSNKAKIDEDLRGDVIVPAPKKLEDLIHLAELCVDLLQQNEEHYGEAFAWFSDLLVEHAEIFWSLFAVDMDRVLSEQAPDTWDSFPLFQILNDYLRTDDNLRNGRFHQHLRDTFAPLVVRYVDLMESSIAQSIHKGFEKERWESKGINAALNPAALNNAAQALNTAALNPSMILCGKKDQVNFYVPKLPKQSNSTAANDEMRNGCATSEDLFWKLDALQSFIRDLHWPDAEFRQHLEQRLKMMAVDMIEQCIQRTDSSFQSWLKKNIAFISTDYILPSEMCAMVNVILDAKNQSFKLTTIDGIDLYKFHAKIDDQIDKANVAMTQGLSGKLMSVLESTLSKLARYDEGSLIGSILSFTNVSSSGKDLGQGYVNFFRNNMDQVRGKIADDLWTLHFFEQWYSQQINMLCNWLSERVDHALHYAQVASISHIIKKIYSDFELQGVLEDKLNSKAYQAVAQRMATEEATCALTMPDACEDEPCDEIREGEEEDNGDESTSNIPRGLPKPKVAAAQAAAVTNVVAGRVGNLLGKGIGGLSSKLGSGSWF
Calcium-binding protein involved in exocytosis of vesicles filled with neurotransmitters and neuropeptides. May specifically mediate the Ca(2+)-dependent exocytosis of large dense-core vesicles (DCVs) and other dense-core vesicles. However, it probably also participates in small clear synaptic vesicles (SVs) exocytosis and it is unclear whether its function is related to Ca(2+) triggering.
Q9NHE5
Q0P7U6
BIOB_CAMJE
Biotin synthase
Campylobacter
MQIMLCAISNIASGNCSEDCKYCTQSAHVKTDIQKYRRKELSQIVLEAKMAKKNEALGFCLVTAGLGLDDEKLEYVCEAAKAVQKEVPNLLLIACNGMASVEQLKELKKAGIFSYNHNLESSKEFFPQICTTHTWESRFQTNLNAKEAGLMLCCGGIYGMGESEEDRLSFRKSLQELQPFSTPINFFIANENLKLQVPRLSADEALKIVRDTKEALPQSVVMVAGGREVVLRERQYEIFQAGAGAIVIGDYLTTKGEEPSQDIIKLKEMGFTFASECH
Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
Q0P7U6
Q9X1X7
NADA_THEMA
Quinolinate synthase
Thermotoga
MVDEILKLKKEKGYIILAHNYQIPELQDIADFVGDSLQLARKAMELSEKKILFLGVDFMAELVKILNPDKKVIVPDRSATCPMANRLTPEIIREYREKFPDAPVVLYVNSTSECKTLADVICTSANAVEVVKKLDSSVVIFGPDRNLGEYVAEKTGKKVITIPENGHCPVHQFNAESIDAVRKKYPDAKVIVHPECPKPVRDKADYVGSTGQMEKIPEKDPSRIFVIGTEIGMIHKLKKKFPDREFVPLEMAVCVNMKKNTLENTLHALQTESFEVILPKEVIEKAKKPILRMFELMG
Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate.
Q9X1X7
Q1R183
ISFD_CHRSD
Isethionate formation reductase
Chromohalobacter
MTDCVFITGATSGFGRAAAHRFAAAGWSLVLTGRRLERLEALKEELQGRVPVHIIALDVRDSDVVDAAVAALPEGFTRVRTLLNNAGLALAPQSAQHTDRSDWHTMIDTNVTGLVNVTHALLPTLIDVGEGATIVNVGSIAGQWPYPGSHVYGASKAFVKQFSYNLRCDLLGTGVRVTDLAPGIAETEFTLVRTGGDQAASDALYRGTTALTAEDIAEQMFYIATLPPHVNFNRLEVMPTRQAWSAFAIDYDA
Catalyzes the formation of isethionate from 2-sulfoacetaldehyde in the deaminative pathway of taurine. The enzyme is specific for NADPH; NADH is not a substrate. Responsible for most of the activity observed in taurine-grown cells.
Q1R183
C5CGG9
NFI_KOSOT
Deoxyribonuclease V
Kosmotoga
MKIRCLHDWNVSLEEAADIQRTLKGMLSFEFPAKKVSIVAGVDVSFPQKNLGLCVIVVMDDTLKVIESVYHTQEVHIPYVSGFLSFREGPIFIETVKKLKIVPDLFFFDGQGIAHPRGLGIAAHMGLLLEKPSLGVAKSHLFGSYNEPGRNKGDFSYMYNKTGEIIGTVLRTKKNTKPVFVSPGHMMDVDTAMSLTLKYTGKYRLPEPTRQAHILTQRLRKNHLLR
DNA repair enzyme involved in the repair of deaminated bases. Selectively cleaves double-stranded DNA at the second phosphodiester bond 3' to a deoxyinosine leaving behind the intact lesion on the nicked DNA.
C5CGG9
P86318
CYC24_RHOPL
Cytochrome c2
Rhodopseudomonas
QDAAKGEALFKQCQTCHRADKNMVGPALAGVVGRKAGTAPGFSYSPLNHAAGEAGLVWSQENVVEYLADPNAFLKKFLTDKGQADKATGSTKMTFKLANEQQRKDVAAYLATLK
Cytochrome c2 is found mainly in purple, non-sulfur, photosynthetic bacteria where it functions as the electron donor to the oxidized bacteriochlorophyll in the photophosphorylation pathway. However, it may also have a role in the respiratory chain and is found in some non-photosynthetic bacteria.
P86318
Q0ASQ1
PHNC_MARMM
Phosphonates import ATP-binding protein PhnC
Maricaulis
MTDAALALQAENLRMTFGETKALDDVSLSVKPGEMVALIGPSGSGKSTLLRVAAALQVADAESGPVSVLGKTMQQRGKLSGRVQRNRIQLGFIFQQFNLVGRLSLFQNVLVGALGRLPTWRGVLGIFPDDVKQSAMDALTRVGVESFAARRASNLSGGQQQRGAIARALVQGAQVLFADEPIASLDPVSARKVMETLRELNKDDGLTVVVTLHQVDYAKRFCDRIVALNKGRVVYDGPADGLSRDKLIEIYGPEFETAFEGGDA
Part of the ABC transporter complex PhnCDE involved in phosphonates import. Responsible for energy coupling to the transport system.
Q0ASQ1
Q8R1J3
ZCHC9_MOUSE
Zinc finger CCHC domain-containing protein 9
Mus
MTRWARVTTSNSKRPLSATSWEDMKKGSVERADQSLPNRKQCQSSRLPLRNDSPQAKRKKNKKKKEYLNEDVNGFMEYLKQNSQVLHNGQLIAADSQEVREEIAVALKKDSRREGRRLKRQAAKKNAMVCFHCRQPGHGIADCPAVLESQDMGTGICYRCGSTEHEMSKCRANVDPALGEFPFAKCFVCGEMGHLSRSCPDNTKGVYADGGSCKLCGSVEHFKKDCRENQNSDRIITVGRWAKGMSADYEDVLDVPKLQKPKTKVPKVVNF
May down-regulate transcription mediated by NF-kappa-B and the serum response element.
Q8R1J3
Q2YVZ4
SBI_STAAB
Immunoglobulin-binding protein Sbi
Staphylococcus
MKNKYISKLLVGAATITLATMISNGEAKASENTQQTSTKHQTTQNNYITDQQKAFYQVLHLKGITEEQRNQYIKTLREHPERAQEVFSESLKDSKNPDRRVAQQNAFYNVLKNDNLTEQEKNNYIAQIKENPDRSQQVWVESVQSSKAKERQNIENADKAIKDFQDNKAPHDKSAAYEANSKLPKDLRDKNNRFVEKVSIEKAIVRHDERVKSANDAISKLNEKDSIENRRLAQREVNKAPMDVKEHLHKQLDALVAQKDAEKKVAPKVEAPQIQSPQIEKPKAESPKVEVPQIQSPKVEVPQSKLLGYYQSLKDSFNYGYKYLTDTYKSYKEKYDTAKYYTDKYFKYKGTIDKTVQSVFGNGYKSYIQPLKVEDQKNYVSKSYAQVRNYVTETLNTGKVLYAFYQNPKLVNAAITTAETATSIKNIFSSFTSFFK
Plays a role in the inhibition of both the innate and adaptive immune responses. Possesses two N-terminal domains that bind the Fc region of IgG and two domains that form a tripartite complex with complement factors C3b and CFH. By recruiting CFH and C3b, the secreted form acts as a potent complement inhibitor of the alternative pathway-mediated lysis.
Q2YVZ4
Q7TNN8
LPIN3_MUSSP
Lipin-3
Mus
MNYVGQLAETVFGTVKELYRGLNPATLSGGIDVLVVRQRDGSFRCSPFHVRFGKLGVLRSREKVVDIEINGEPVDLHMKLGDSGEAFFVQELDSDEEDVPPRLCTSPIPWGGLSGFPSDSQIGTASEPEGLVITGRRKRRRRRKPRRKEDVVDSSSEELEAGVESELTLLEKPTPESPSAQEEEETSSQPKDIHPYSDGECTPQANLSSGDLMSPKSDSELELRSLEPSPLRAESHMQWVWGRLPKVAKAERPEFSLILESMAEAICALPEEPSPSSSPSEAGVDTLSPPVLHPGVRADKFHPAVEAHCEETAVDSPLAAPESKETKTQNSRGAGHPPATKSWSWTTPESHTPSGHPQVSRGKGSLKRNQHLGPSDIYLDDLPSLDSENVALYFPKSEYGMGARRWSEPSNQKLLESPNLEHIAECTLDSVDKIELSLCGGLADNRDISLEKFTQHMVSYEDLTKNPGLLDDPNLVVKINEKHYNWAVAAPMILSMQAFQKNLPESTVDKLEKEKMPRKGGRWWFSWRRKDFPAEEHSSQREKAATRKQQGEKTEVLSSDDDVPDSPVILEVPPLPSSTPGYVPTYKKSLRLSSDQIRCLNLNEGANDVVFSVTTQYQGTCRCKATIYLWNWDDKVVISDIDGTITKSDALGHILPQLGKDWTHQGITSLYHKIHLNGYKFLYCSARAIGMADLTKGYLQWVSEHGCGLPKGPILLSPSSLFSALHREVIEKKPEVFKVACLSDIQQLFLPQRQPFHAAFGNRPNDVFAYRQVGLPESRIFTVNPRGELIQELIKSHKSTYQRLGEVVELLFPPVVRGPSTDLASPEYSNLSYWRKPLPYVDFEALA
Magnesium-dependent phosphatidate phosphatase enzyme which catalyzes the conversion of phosphatidic acid to diacylglycerol during triglyceride, phosphatidylcholine and phosphatidylethanolamine biosynthesis therefore regulates fatty acid metabolism.
Q7TNN8
Q6PCT8
DHSD_RAT
Succinate-ubiquinone reductase membrane anchor subunit
Rattus
MAVLLKLGVLCSGQGARALSLRSRAVRPAFVSAFLQDQPTPGWRGTQHIHLSPSHQSGSKAASLHWTSERVVSVLLLGLIPAGYLNPCSVVDYSLAAALTLHSHWGIGQVVTDYVHGDALQKATKAGLLAVSALTFAGLCYFNYHDVGICRAVAMLWKL
Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Q6PCT8
Q8NMB8
ISPD_CORGL
MEP cytidylyltransferase
Corynebacterium
MSSTRIPVIALLAAAGRGTRLGGPIPKAFVTLRERTLLERSLQAMLTSESVDEIIILVSPDMETYARDLLRKRGLLNDPEGVRVRLVHGGGERADSVWAGLQAISLDDATPDAIVLIHDSARALTPPGMIARVVRKVHEGATAVIPVLPVSDTIKRVSPDGGVVVDTPNRAELRAVQTPQGFLLSELVAANEKFFADPNPGFIPTDDASLMEWYGADVVCVQGDPMAFKVTTPIDMMLAQRITDEAEPTIFEVPGD
Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
Q8NMB8
Q42191
OXA1_ARATH
Oxidase assembly 1 protein
Arabidopsis
MAFRQTLSIRSRLFARRNQPVYHIIPRESDHERDSFCQETSQRSYHSFLHQRSVNNSDFSKVSGGSLHLPLAPTSGFAFYRYMSSAPGVGSEKIGVMSDIAEVITDSTLQDVPAQAAAAVSEVTLAAADSFFPIAALQQCIDMVHTFTGFEWWASIVVATILIRSSTVPLLIKQMKDTTKLALMRPRLESIREEMQNKGMDSVTMAEGQKKMKNLFKEYGVTPFTPMKGMFIQGPLFICFFLAIRNMAEKVPSFQTGGALWFTDLTTPDSLYILPVITGLTFLITVECNAQEGMEGNPMAGTVKTVCRVFALLTVPMTMSFPQAIFCYWITSNLFSLMYGLVIKRPQVKKMLRIPDLPPPPPGQQPSFDLFSALKKMKAMTQDHTQNQIEPPSPVNPRLSSTSLSPVSKRLKALESQVKGRKKNSSKKK
Required for the insertion of integral membrane proteins into the mitochondrial inner membrane. Essential for activity and assembly of cytochrome c oxidase.
Q42191
Q5QW31
SYP_IDILO
Prolyl-tRNA synthetase
Idiomarina
MRSSKYLLSTLKETPSDAEIVSHQLMLRAGMIRKVAAGLYTWTPTGLRVLRKVENVVREEMEAINALEILMPMVQPADLWQESGRWDDYGPELLRIKDRNQRDFLLGPTHEEIISQLVRKEVSSYKQLPLTLFQIQTKFRDEIRPRFGVMRAREFLMKDAYSFHLTDESLQKTYDDMYKAYCRIFERLGLDYRPVIADTGSIGGSHSHEFHVLASSGEDAIAFSDSSDYAANVEMAEALAPAGERPAPNQKVEKHEVQGDELAAVLQPLSVESQQATKSFIVKAADDIDSEYVQLVLRADHELNTVKAEKLAQVAAPLEILTETEKATGVEAPYIGVVNAKLPLLVDSSAAHLADFACGANENGQWLTGVNWKRDTGDFSVVDIRNVVAGDPSPCGQGKVKIARGIEVGHIFQLGKKYSDAMKVGVLSESGKHETLTMGCYGIGVSRIVAAAIEQNNDERGICWPEALAPFQVVIVPMNMHKSARVQEAAEKLYTDLKAQGIDVLFDDRKERPGVMFTDMELIGIPHQVVVGERNLDENQVEYQSRKGGEKQKINLDDCISFIQQQL
Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS.
Q5QW31
A0B573
GGR_METTP
Geranylgeranyl reductase
Methanothrix
MRCDVVVVGAGPGGSMAAKTAAEKGLKVVLVEKRQEIGDPVRCAEGVSKARLSSMIKPDPKWIASEVKGARLYAPDGSNVVMSEDKSGDEVGYVLERKIFDRALAMDAARAGARVMVKTRALDLLRANGSVKGIRAMRYGEIIDIEADVVIGADGVESKVGRWAGIDTALKPGDIEVCAQFLLYDKGIDDEYCEFFLGNELAPGGYVWSFPKGEHLANVGLGVIGSRSEPGAPVKLLRRFVERRMPEARIVEMVVGGVPVSGPIERTIADGVMLVGDAARQSDPITGGGILNAMQAGMIAGEVVADAVSSGDTGVEGLMAYEKRWRESIGKQIARHLDLKEFFIRLSDDDLNKLMHSIQSEDVSKMDLRGMLRVLIRLNPKMLWELRHLVM
Is involved in the reduction of 2,3-digeranylgeranylglycerophospholipids (unsaturated archaeols) into 2,3-diphytanylglycerophospholipids (saturated archaeols) in the biosynthesis of archaeal membrane lipids. Catalyzes the formation of archaetidic acid (2,3-di-O-phytanyl-sn-glyceryl phosphate) from 2,3-di-O-geranylgeranylglyceryl phosphate (DGGGP) via the hydrogenation of each double bond of the isoprenoid chains.
A0B573
Q5HB23
EFTS_EHRRW
Elongation factor Ts
Ehrlichia
MKVDINAIKELRDLTGAGVGDCKDALTSCNGDIEKAKTYLREQGIAKAYKKSNKDVSDGLVAICIDGNKGAILEVNSETDFVARNEKFQKLVLNLAFLANQYGIENIEDFLKCEYANNTNINDEIMSNIAVIGENIHLNKIGCLSVSSGVVCGYIHNPIVDNLGKVGAIVALESNCDVEKLKIFARQIAMHIVATKPEALSLDVLDQNVIDKERDIIKKQVEQLNKPASVLEKIIDGRMAKFYQEVVLMNQMFIMDSQFTVSELIKKKEEELGSSINIVDYKLFIINK
Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.
Q5HB23
Q88W75
LSPA_LACPL
Signal peptidase II
Lactiplantibacillus
MWIYLILMVALVIIDQVIKAAIVSHIALGASTSIVTGLLSLTNLHNNGAAWSILEGKMWFFYLISVIALIVMGYLLWRLRGKWLYEVGISLMIAGTLGNFIDRLRIGYVVDMFQLDFINFPIFNFADSCLTVGVIFILIGVLRDDSFEK
This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Q88W75
Q5M7C7
JAGN1_XENLA
Protein jagunal homolog 1
Xenopus
MASRAGPRATGSDGSDFQHREKVAGHYKMSASLKNEIKKLIYAHLIIWMLIAAQMCVSHLKLVSKDLVAMPYQWEYPYLLSLVPSLFGLFSFPRNNISYLVISMISTGLFSIGPLIYGTLEMFPMAQQLYRHGKAYRFIFGFSAISVMYLVMVVAVQVHGWQIYYSKKLLDSWFTNTQEKKKK
Endoplasmic reticulum transmembrane protein involved in vesicle-mediated transport, which is required for neutrophil function.
Q5M7C7
Q4QLD2
GLRX4_HAEI8
Monothiol glutaredoxin
Haemophilus
METLDKIKKQISENPILIYMKGSPKLPSCGFSARASEALMHCKVPFGYVDILQHPDIRAELPTYANWPTFPQLWVEGELIGGCDIILEMYQAGELQTLLAEVAAKHA
Monothiol glutaredoxin involved in the biogenesis of iron-sulfur clusters.
Q4QLD2
B8GTX6
AMPA_THISH
Leucyl aminopeptidase
Thioalkalivibrio
MEFSVKSGNPEKQRSACVVVGVFDRRKLSSAARVLDKASGGALSTILRRGDMDGEKGQTLWLYNLPNTLCERVLLVGCGKERDFDEPAYRSVIATVARTVNKSGAVEAVNYLTDLPVKGRDTLWKISQAVTITQDSLYSFQQLKSKKEDTQRPLKRIILSVPSRADLLPGEDAVRVATAISVGTKLTRDLANLPGNICNPTYLAEQALQLKKTYKGLKVEILEEADMEKLGMGALLSVSRGSEQPAKLITLEYRGGRKDAKPVVLVGKGITFDTGGISLKPGAEMDEMKFDMCGAASVLGVMKAVAEMMLPINLVGVVAAAENMPDGKATRPGDVVTSMSGQTIEILNTDAEGRLVLCDALSYVERFDPDVVIDIATLTGACIIALGHQATGLLSNHSPLANDLLGAGKQSYDRAWELPLWDEYQEQLKSNFADMANIGGRPAGTITAACFLSRFTKKYKWAHLDIAGVAWKSGKEKGATGRPVPLLMQYLLNKAS
Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
B8GTX6
Q7VFY9
KPRS_HELHP
Phosphoribosyl pyrophosphate synthase
Helicobacter
MRGFKIFSGSAHTLFSNEVAKCLDISLSKTTINRFSDGEINVQIGESVRGKDIFIIQPTCAPANDHLMELLIMTDALKRSGAKNINAVIPYFGYARQDRKVVPRVPITAKLVANLIEQSGIHRVITMDLHAEQIQGFFDIPVDNLYGSIVFRDYLKTKSFKNPIVASPDIGGVARARHFADRIGMDLVIVDKKRERANESEVMNIIGDVDGKDVILIDDMIDTAGTMCKAADVLKSRGANSVIALGTHPVLSGPALERIAKSALDEVVVTNSIPLRVAHPKIKVLSVAPLFAEVIRRICHNESVNSLFF
Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P).
Q7VFY9
Q9JLG9
AIPL1_RAT
Aryl-hydrocarbon-interacting protein-like 1
Rattus
MDVSLLLNVEGVKKTILHGGTGELPNFITGSRVTFHFRTMKCDEERTVIDDSKQVGQPMNIIIGNMFKLEVWETLLTSMRLGEVAEFWCDTIHTGVYPMLSRSLRQVAEGKDPTSWHVHTCGLANMFAYHTLGYEDLDELQKEPQPLIFLIELLQVEAPNEYQRETWNLNNEERMQAVPLLHGEGNRLYKLGRYDQAATKYQEAIVCLRNLQTKEKPWEVEWLKLEKMINTLILNYCQCLLKKEEYYEVLEHTSDILRHHPGIVKAYYMRARAHAEVWNAEEAKADLEKVLELEPSMRKAVLRELRLLESRLADKQEEERQRCRSMLG
May be important in protein trafficking and/or protein folding and stabilization.
Q9JLG9
E0D7H6
FC2_PHOAM
Fusicoccin A biosynthetic gene clusters protein 2
Diaporthe
MGSTAEDFVIKPMKGEHGFGAEIYGLDVNNITDEQVDRLRDTIQRYLLVVLKHQHDETPQKNWELLNRLSPDAPKFTPEEWALMYNPDPQGAGILPKLGYLVLPGTERLFLMGKGYQGEDHWGLKDIDIPEVFADAYYSKPLPHEDYHNGVARFQSWHIDGPSYKIDHPMFTSFRIIKFPEGEQTVDWADGSGLTKKVKAGRTAFFSSAKLYDMLTKEEQAIADYSWAEYMYFPYEWILRCRGNPQGLLVACEGREVPDEQMDAMPRNPEDQLVLPLVWVNPVTGGKHFHVQPNIVRRVFVRSGPDEEPKIIDDVKEVRDFFTKFQYRIIRPENIYVGPEEEGDQLLFFNWGVMHSKIDYPIEMGTRTTHQGWLAGDRPPKGPVPIPDPRARSSIYYQK
Alpha-ketoglutarate-dependent dioxygenase; part of the 2 gene clusters that mediate the biosynthesis of fusicoccins, diterpene glucosides that display phytohormone-like activity and function as potent activators of plasma membrane H(+)-ATPases in plants by modifying 14-3-3 proteins and cause the plant disease constriction canker . The first step in the pathway is performed by the fusicoccadiene synthase PaFS that possesses both prenyl transferase and terpene cyclase activity, converting isopentenyl diphosphate and dimethylallyl diphosphate into geranylgeranyl diphosphate (GGDP) and successively converting GGDP into fusicocca-2,10(14)-diene, a precursor for fusicoccin H . The second step is the oxidation at the C-8 position by the cytochrome P450 monooxygenase PaP450-2 to yield fusicocca-2,10(14)-diene-8-beta-ol . The cytochrome P450 monooxygenase PaP450-1 then catalyzes the hydroxylation at the C-16 position to produce fusicocca-2,10(14)-diene-8-beta,16-diol . The dioxygenase fc-dox then catalyzes the 16-oxydation of fusicocca-2,10(14)-diene-8-beta,16-diol to yield an aldehyde (8-beta-hydroxyfusicocca-1,10(14)-dien-16-al) . The short-chain dehydrogenase/reductase fc-sdr catalyzes the reduction of the aldehyde to yield fusicocca-1,10(14)-diene-8-beta,16-diol . The next step is the hydroxylation at C-9 performed by the cytochrome P450 monooxygenase PaP450-3 that leads to fusicoccin H aglycon which is glycosylated to fusicoccin H by the O-glycosyltransferase PaGT . Hydroxylation at C-12 by the cytochrome P450 monooxygenase PaP450-4 leads then to the production of fusicoccin Q and is followed by methylation by the O-methyltransferase PaMT to yield fusicoccin P . Fusicoccin P is further converted to fusicoccin J via prenylation by the O-glucose prenyltransferase PaPT . Cytochrome P450 monooxygenase PaP450-5 then performs hydroxylation at C-19 to yield dideacetyl-fusicoccin A which is acetylated to 3'-O-deacetyl-fusicoccin A by the O-acetyltransferase PaAT-2 . Finally, a another acetylation by the O-acetyltransferase PaAT-1 yields fusicoccin A .
E0D7H6
F8S1I0
C7BL2_LACSA
Cytochrome P450 71BL2
Lactuca
MEPLTIVSLAVASFLLFAFWALSPKTSKNLPPGPPKLPIIGNIHQLKSPTPHRVLRNLAKKYGPIMHLQLGQVSTVVVSTPRLAREIMKTNDISFADRPTTTTSQIFFYKAQDIGWAPYGEYWRQMKKICTLELLSAKKVRSFSSIREEELRRISKVLESKAGTPVNFTEMTVEMVNNVICKATLGDSCKDQATLIEVLYDVLKTLSAFNLASYYPGLQFLNVILGKKAKWLKMQKQLDDILEDVLKEHRSKGRNKSDQEDLVDVLLRVKDTGGLDFTVTDEHVKAVVLDMLTAGTDTSSATLEWAMTELMRNPHMMKRAQEEVRSVVKGDTITETDLQSLHYLKLIVKETLRLHAPTPLLVPRECRQACNVDGYDIPAKTKILVNAWACGTDPDSWKDAESFIPERFENCPINYMGADFEFIPFGAGRRICPGLTFGLSMVEYPLANFLYHFDWKLPNGLKPHELDITEITGISTSLKHQLKIVPILKS
Involved in the biosynthesis of germacrene-derived sesquiterpene lactones . Component of the parthenolide biosynthetic pathway; parthenolide and conjugates are promising anti-cancer drugs highly active against colon cancer cells . Hydroxylates germacrene A acid to 6-alpha-hydroxy-germacrne A acid, a precursor of sesquiterpene lactones that spontaneously undergoes a lactonization which yields costunolide .
F8S1I0
P46379
BAG6_HUMAN
Protein Scythe
Homo
MEPNDSTSTAVEEPDSLEVLVKTLDSQTRTFIVGAQMNVKEFKEHIAASVSIPSEKQRLIYQGRVLQDDKKLQEYNVGGKVIHLVERAPPQTHLPSGASSGTGSASATHGGGSPPGTRGPGASVHDRNANSYVMVGTFNLPSDGSAVDVHINMEQAPIQSEPRVRLVMAQHMIRDIQTLLSRMETLPYLQCRGGPQPQHSQPPPQPPAVTPEPVALSSQTSEPVESEAPPREPMEAEEVEERAPAQNPELTPGPAPAGPTPAPETNAPNHPSPAEYVEVLQELQRLESRLQPFLQRYYEVLGAAATTDYNNNHEGREEDQRLINLVGESLRLLGNTFVALSDLRCNLACTPPRHLHVVRPMSHYTTPMVLQQAAIPIQINVGTTVTMTGNGTRPPPTPNAEAPPPGPGQASSVAPSSTNVESSAEGAPPPGPAPPPATSHPRVIRISHQSVEPVVMMHMNIQDSGTQPGGVPSAPTGPLGPPGHGQTLGQQVPGFPTAPTRVVIARPTPPQARPSHPGGPPVSGTLQGAGLGTNASLAQMVSGLVGQLLMQPVLVAQGTPGMAPPPAPATASASAGTTNTATTAGPAPGGPAQPPPTPQPSMADLQFSQLLGNLLGPAGPGAGGSGVASPTITVAMPGVPAFLQGMTDFLQATQTAPPPPPPPPPPPPAPEQQTMPPPGSPSGGAGSPGGLGLESLSPEFFTSVVQGVLSSLLGSLGARAGSSESIAAFIQRLSGSSNIFEPGADGALGFFGALLSLLCQNFSMVDVVMLLHGHFQPLQRLQPQLRSFFHQHYLGGQEPTPSNIRMATHTLITGLEEYVRESFSLVQVQPGVDIIRTNLEFLQEQFNSIAAHVLHCTDSGFGARLLELCNQGLFECLALNLHCLGGQQMELAAVINGRIRRMSRGVNPSLVSWLTTMMGLRLQVVLEHMPVGPDAILRYVRRVGDPPQPLPEEPMEVQGAERASPEPQRENASPAPGTTAEEAMSRGPPPAPEGGSRDEQDGASAETEPWAAAVPPEWVPIIQQDIQSQRKVKPQPPLSDAYLSGMPAKRRKTMQGEGPQLLLSEAVSRAAKAAGARPLTSPESLSRDLEAPEVQESYRQQLRSDIQKRLQEDPNYSPQRFPNAQRAFADDP
Mediates ricin-induced apoptosis.
P46379