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
|
|---|---|---|---|---|---|---|
Q8NJA1
|
TRI5_FUSMI
|
Sesquiterpene cyclase
|
Fusarium
|
MENFPTEYFLNTSVRLLEYIRYRDSNYTREERIENLHYAYNKAAHHFAQPRQQQMLKVDPKRLQASLQTIVGMVVYSWAKVSKECMADLSIHYTYTLVLDDSSDDPHPAMLNYFDDLQAGREQSHPWWALVNEHFPNVLRHFGPFCSLNLIRSTMDFFEGCWIEQYNFGGFPGSDDYPQFLRRMNGLGHCVGASLWPKDLFDERKNFLEITTAVAQMENWMVWVNDLMSFYKEFDDERDQISLVKNFVTCHEITLDEALEKLTQETLHSSKQMVAVFADKDPQVMDTIECFMHGYVTWHLCDARYRLHEIYEKVKDQDTEDAKKFCKFFEQAANVGAVAPSEWAYPQVAQLANVRAKDDMKEGQKPILSSIELVE
|
TS is a member of the terpene cyclase group of enzymes. It catalyzes the isomerization and cyclization of farnesyl pyro-phosphate to form trichodiene, the first cyclic intermediate in the biosynthetic pathway for trichothecenes. It serves to branch trichothecene biosynthesis from the isoprenoid pathway.
|
Q8NJA1
|
Q8S4P9
|
VCL_CORAV
|
Vicilin HZ.1
|
Corylus
|
MLPKEDPELKKCKHKCRDERQFDEQQRRDGKQICEEKARERQQEEGNSSEESYGKEQEENPYVFQDEHFESRVKTEEGRVQVLENFTKRSRLLSGIENFRLAILEANPHTFISPAHFDAELVLFVAKGRATITMVREEKRESFNVEHGDIIRIPAGTPVYMINRDENEKLFIVKILQPVSAPGHFEAFYGAGGEDPESFYRAFSWEVLEAALKVRREQLEKVFGEQSKGSIVKASREKIRALSQHEEGPPRIWPFGGESSGPINLLHKHPSQSNQFGRLYEAHPDDHKQLQDLDLMVSFANITKGSMAGPYYNSRATKISVVVEGEGFFEMACPHLSSSSGSYQKISARLRRGVVFVAPAGHPVAVIASQNNNLQVLCFEVNAHGNSRFPLAGKGNIVNEFERDAKELAFNLPSREVERIFKNQDQAFFFPGPNKQQEEGGRGGRAFE
|
Seed storage protein . Does not have superoxide dismutase (SOD) activity .
|
Q8S4P9
|
P30288
|
TX23A_AGEAP
|
Omega-agatoxin-4A
|
Agelenopsis
|
KKKCIAKDYGRCKWGGTPCCRGRGCICSIMGTNCECKPRLIMEGLGLA
|
Omega-agatoxins inhibit neuronal voltage-gated calcium channels. This toxin acts by modifying the gating of the high voltage activated P-type Cav2.1/CACNA1A channel. Is a potent blocker in both insect and mammalian central neurons.
|
P30288
|
A5EPD3
|
TYSY_BRASB
|
Thymidylate synthase
|
unclassified Bradyrhizobium
|
MHQYHDLLERILSDGAEKHDRTGTGTLSVFGHQMRFNLGAGFPLVTTKRLPLKAIVHELLWFLRGDTNIKYLHDHGVTIWDEWADANGDLGPVYGYQWRSWPTPDGGHIDQIANVIDMIKRNPDSRRLIVTAWNPADVEKMALPPCHCLFQFYVVNGKLSCQLYQRSADVFLGVPFNIASYALLTMMVAQVTGLKPGEFVHSFGDVHLYSNHVEQARLQLTRAPRSLPTMTLNPDVKDIFAFRYEDFALAGYDPHPHIKAEVAV
|
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.
|
A5EPD3
|
P18737
|
ZG8_XENLA
|
Gastrula zinc finger protein XlCGF8.2DB
|
Xenopus
|
TGEKPFTCKECGKGFTQKRNLASHMTIHTGEKPFSCTECGKGFTQKRNLASHLTIHTGEKPFPCTECGKGFTQKSNLVSHMKIHTGEKPFTCTECGKEFAHKHRLLGHLKIHTGEKPFSCTECGKHFAHKYHLVSHMKIHTREKPFTCTECGEHFANKVSLLGHLKMHKGEKPFTCTECGNSFTQVSSLVSHMKIH
|
May be involved in transcriptional regulation.
|
P18737
|
Q3B151
|
TAL_CHLL3
|
Probable transaldolase
|
Pelodictyon
|
MKFFIDTANLDEIRAAESLGVLDGVTTNPSLIAKIVEDPASFTRKDFMDHIKRICEIVDGPVNAEVTTLDAASMVREGEELAAIHNNVVVKCPLTIDGLKAIRSLSEKGIRTNATLVFSPNQALLAAKAGAGYVSPFVGRLDDISTDGMALVGQIVEIYDNYGLMTEVIVASIRHPQHVVESALIGADIATIPYSVIRQLANHPLTDAGLKKFMEDAAVIKK
|
Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
|
Q3B151
|
B4T5K4
|
YQGF_SALNS
|
Putative pre-16S rRNA nuclease
|
Salmonella
|
MSGTLLAFDFGTKSIGVAIGQRITGTARPLPAIKAQDGTPDWTLIERLLKEWQPDEIIVGLPLNMDGTEQPLTARARKFANRIHGRFGVTVTLHDERLSTVEARSGLFERGGYRALNKGKVDSASAVIILESYFEQGY
|
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
|
B4T5K4
|
Q60369
|
TSAC_METJA
|
tRNA threonylcarbamoyladenosine biosynthesis protein MJ0062
|
Methanocaldococcus
|
MGLKNKIIKIYELNEEERKKVLEFLKKEILNGKIVICGTDTLYGISANALNEKAVRKVYNIKRREFNKPLSICVRDKNEIEKYAYVNDLAKKIIDKFLPGPLTIILKKKPGIPDIVAKDYIGIRIPDEPIIRELSIVPLTTTSANISGKESPTTVDEIDKEVLKKVDYVIDIGKCKYSKPSTIIKIEDDKIISIREGVIPIQKLARC
|
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosphate.
|
Q60369
|
Q9BVG3
|
TRI62_HUMAN
|
Tripartite motif-containing protein 62
|
Homo
|
MACSLKDELLCSICLSIYQDPVSLGCEHYFCRRCITEHWVRQEAQGARDCPECRRTFAEPALAPSLKLANIVERYSSFPLDAILNARRAARPCQAHDKVKLFCLTDRALLCFFCDEPALHEQHQVTGIDDAFDELQRELKDQLQALQDSEREHTEALQLLKRQLAETKSSTKSLRTTIGEAFERLHRLLRERQKAMLEELEADTARTLTDIEQKVQRYSQQLRKVQEGAQILQERLAETDRHTFLAGVASLSERLKGKIHETNLTYEDFPTSKYTGPLQYTIWKSLFQDIHPVPAALTLDPGTAHQRLILSDDCTIVAYGNLHPQPLQDSPKRFDVEVSVLGSEAFSSGVHYWEVVVAEKTQWVIGLAHEAASRKGSIQIQPSRGFYCIVMHDGNQYSACTEPWTRLNVRDKLDKVGVFLDYDQGLLIFYNADDMSWLYTFREKFPGKLCSYFSPGQSHANGKNVQPLRINTVRI
|
E3 ubiquitin ligase that plays a role in antifungal immunity by mediating 'Lys-27'-linked ubiquitination of CARD9 downstream of C-type lectin receptors; leading to CARD9 activation, followed by activation of NF-kappa-B and MAP kinase p38 pathways . E3 ubiquitin ligase activity is dependent on E2 ubiquitin-conjugating enzyme UBE2D2 .
|
Q9BVG3
|
A7NRW4
|
YBEY_ROSCS
|
Endoribonuclease YbeY
|
Roseiflexus
|
MDDAEILVDVQVVPQYAAVVDATLVERAVAQTLRTDDVAGPVEISILITDDADVHRLNQTYRGVDAPTDVLSFAEDDDHSFVRPPDAPRYLGDIAISWDRVVAQAAEYGHSRERELAFLVVHGVLHLLGYDHERGPVDEADMRAREEAILGALGLSREG
|
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
|
A7NRW4
|
A9RHX1
|
THI41_PHYPA
|
Thiazole biosynthetic enzyme 1
|
Physcomitrium
|
MSISAAGVATGLGANVELKSNVGSSSSSVAGVRLFTSRKAQLRRCAAPATSASLYSDANYDLNNYKFAPIKESIVAREMTRRYMTDMITHADTDVVVVGAGSAGLSCAYELSKNPNVKVAIVEQSVSPGGGAWLGGQLFSAMIVRKPAHRFLDEIEVPYEEMENYVVIKHAALFTSTIMSKLLARPNVKLFNAVAAEDLIIRGDRVSGVVTNWALVAQNHNTQSCMDPNVMEAKVVVSSCGHDGPFGATGVKRLRSIGMIESVPGMKCLDMNAAEDAIVKHTREVVPGMIVTGMEVAEIDGSPRMGPTFGAMMISGQKAAHLALKALGLPNELDGNYKPNVHPELVLASTDDETASA
|
Involved in biosynthesis of the thiamine precursor thiazole. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylic acid (ADT), an adenylated thiazole intermediate. The reaction includes an iron-dependent sulfide transfer from a conserved cysteine residue of the protein to a thiazole intermediate. The enzyme can only undergo a single turnover, which suggests it is a suicide enzyme. May have additional roles in adaptation to various stress conditions and in DNA damage tolerance.
|
A9RHX1
|
B3QMD7
|
THIG_CHLP8
|
Thiazole synthase
|
Chlorobaculum
|
MNALRLGSYTFSSRLILGTGKFSSVSAMIEAVRASGSQLVTVALRRFNREQAEDDLFGPLSEIEGLTLMPNTSGAATAKEAVKAAHISRELSGSPFIKVEIHPNPHHLMPDPIETYEACKILAAEEFIVMPYIPADPVLAKRLEEVGCSSVMPLGSAIGSGQGLSTSAMVQLIIRESSIPVIVDAGLRSPSEACAAMEMGCEAVLVNSAIAVARDPAAMAGAFARAVEAGYDARNAGLMQRSGSAVATSPLTSFLGAGS
|
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.
|
B3QMD7
|
Q97JI7
|
YBEY_CLOAB
|
Endoribonuclease YbeY
|
Clostridium
|
MIYIDNRQNSITVDENLQNTIREVIDYALKEEGMKISYEVSVIFVDNETIREINRENREVDKVTDVLSFPMLEYGEGKVFKDIYEECDFEDEYFDEGNLVLGDIALSLERAEEQSKEYGHSFLREAAYLTVHSVLHLMGYDHMVDEDKIKMRKREEEILSHFDINR
|
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
|
Q97JI7
|
Q8BWC0
|
TPC2_MOUSE
|
Voltage-dependent calcium channel protein TPC2
|
Mus
|
MAAEEQPLLGRDRGSGQVHSGAAADQELCIDQAVVFIEDAIKYRSIYHRMDAGSLWLYRWYYSNVCQRVLGFIIFLILILAFVEVPSSFTKTADVRYRSQPWQPPCGLTETIEAFCLLAFLVDLSVKGYLVGQAQLQQNLWLLAYFMVLVVSVVDWIVSLSLACEEPLRMRRLLRPFFLLQNSSMMKKTLKCIRWSLPEMASVGLLLAIHLCLFTIIGMLLFTIGEKDEAQDQERLAYFRNLPEALTSLLVLLTTSNNPDVMIPAYTQNRAFALFFIVFTLIGSLFLMNLLTAIIYNQFRGYLMKSLQTSLFRRRLGARAAYEVLASRAGPAGTTPELVGVNPETFLPVLQKTQLNKTHKQAIMQKVQSYEGRPMLADEFQKLFDEVDKGLAKERPLKPQYQSPFLQTAQFIFSHHYFDYLGNLVALGNLLSICVFLVLDSDLLPGERDDFVLGILDYIFILYYLLELLFKVFALGLPGYLSYHSNVFDGLLTIILLVSEICTLAVYRLPHSGWKPEQYGPLSLWDMTRLMNTLIVFRFLRIIPNIKPMAEVANTILGLIPNLRAFGGILVVAYYVFAMIGINLFRGVIVPPGNSSLVPDNNSAVCGSFEQLGYWPNNFDDFAAALITLWNVMVVNNWQVILEAYKRYAGPWSMVYFVLWWLVSSVIWINLFLALLLENFLHRWDPQGHKQLLVGTKQMSVELMFRDILEEPKEEELMEKLHKHPHLHLCR
|
(Microbial infection) During Ebola virus (EBOV) infection, controls the movement of endosomes containing virus particles and is required by EBOV to escape from the endosomal network into the cell cytoplasm.
|
Q8BWC0
|
Q1QEI9
|
UBIG_PSYCK
|
3-demethylubiquinone 3-O-methyltransferase
|
Psychrobacter
|
MADDTINAINVDPSEVEKFNKLAGEWWNKTGAFATLHEINPLRLNWIEENVKRGYVSADSQKTAEMGLAGKKVLDVGCGGGILSESMARRGADVTGIDLGTENLKAASLHAEQSNLQDTLRYQHIPVEALAATHAGQFDVVTCMEMLEHVPDPAAIVDACFKLLAPGGVCVLSTINRNPKSYLFAIVGAEYVLRLLDRGTHDYAKFITPAELDKMAIDAEFARQDIIGLHYNPLTKRYWLAQNVDVNYMIAVQKPLA
|
O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.
|
Q1QEI9
|
P04652
|
TSHB_RAT
|
Thyrotropin beta chain
|
Rattus
|
MNAVVLFSVLFALACGQVSSFCIPTEYMMYVDRRECAYCLTINTTICAGYCMTRDINGKLFLPKYALSQDVCTYRDFTYRTVEIPGCPHHVAPYFSYPVALSCKCGKCNTDYSDCTHEAVKTNYCTKPQTFYLGGFSG
|
Indispensable for the control of thyroid structure and metabolism.
|
P04652
|
B8DH80
|
TMCAL_LISMH
|
tRNA(Met) cytidine acetate ligase
|
Listeria
|
MKATGIVVEYNPFHNGHKLHLNKARELTQADVVIAVMSGSFVQRGEPAIIPKWERAKMALAAGVDMVIELPVSFATQHATIFAEEAVRILDAIHVDTLFFGSEHGVAEDFTFAAKKVVENEARFDEAIQLALVDKKTSYARAYTEAFKKLFGQNLLDITKPNNILGFHYALAAQNQNPSISLQTIPREHAGYHDEEANHDQIASATAIRKLILAGKLEEASHYLPASSIAILRNYEGPFLSWKDYWSFLQYRLIQAGSEELEGIRGVSEGIQNRMQQAATKAQNFSDFIELTKTKRYSNTRLQRTALQILLNARSQTSSPYIRILGMNKTGQQYLSLHKKNISLPIVTTVSKAPVGLLEEELRATNIYTLAKGLENYQAGDFHIPPILTL
|
Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of elongator tRNA(Met), using acetate and ATP as substrates. First activates an acetate ion to form acetyladenylate (Ac-AMP) and then transfers the acetyl group to tRNA to form ac(4)C34.
|
B8DH80
|
Q9UZQ5
|
THIE_PYRAB
|
Thiamine-phosphate pyrophosphorylase
|
Pyrococcus
|
MGFREKLKLYVITDRRLKPEVKSVRQALEGGATSIQLRIKDASTKEMYEVGKEIRRLTQEYDALFFVDDRIDVALAVNADGVQLGPEDMPIEVAREIAPNLIIGASVYSLEEALEAEKKGADYLGAGSVFPTKTKRDVRVIRIEGLREIVEAVSIPVVAIGGINVENVKQVLSAGVDGIAVVSAVMGASDVKKATEELRKIIEEVLG
|
Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
|
Q9UZQ5
|
Q8KZ93
|
TRPA_BACNA
|
Tryptophan synthase alpha chain
|
Bacillus
|
MFKLDLQPTEKLFIPFITAGDPVPEVSIELAKSLQKAGATALELGVAYSDPLADGPVIQRASKRALDQGMNIVKAIELGGEMKKNGVNIPIILFTYYNPVLQLNKEYFFALLQENHIDGLLVPDLPLEESNSLQEECKSHEVTYISLVAPTSESRLKTIIEQAEGFVYCVSSLGVTGVRNEFNSSVYPFIRTVKNLSTVPVAVGFGISNREQVIKMNEISDGVVVGSALVRKIEELKDRLISAETRNQALQEFEDYAMAFSGLYSLK
|
The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
|
Q8KZ93
|
O15178
|
TBXT_HUMAN
|
Protein T
|
Homo
|
MSSPGTESAGKSLQYRVDHLLSAVENELQAGSEKGDPTERELRVGLEESELWLRFKELTNEMIVTKNGRRMFPVLKVNVSGLDPNAMYSFLLDFVAADNHRWKYVNGEWVPGGKPEPQAPSCVYIHPDSPNFGAHWMKAPVSFSKVKLTNKLNGGGQIMLNSLHKYEPRIHIVRVGGPQRMITSHCFPETQFIAVTAYQNEEITALKIKYNPFAKAFLDAKERSDHKEMMEEPGDSQQPGYSQWGWLLPGTSTLCPPANPHPQFGGALSLPSTHSCDRYPTLRSHRSSPYPSPYAHRNNSPTYSDNSPACLSMLQSHDNWSSLGMPAHPSMLPVSHNASPPTSSSQYPSLWSVSNGAVTPGSQAAAVSNGLGAQFFRGSPAHYTPLTHPVSAPSSSGSPLYEGAAAATDIVDSQYDAAAQGRLIASWTPVSPPSM
|
Involved in the transcriptional regulation of genes required for mesoderm formation and differentiation. Binds to a palindromic T site 5'-TTCACACCTAGGTGTGAA-3' DNA sequence and activates gene transcription when bound to such a site.
|
O15178
|
Q7NG92
|
UPPP_GLOVI
|
Undecaprenyl pyrophosphate phosphatase
|
Gloeobacter
|
MQQQIGIFEAIVLGFVQGITEYFPISSTAHLRVVPALLGWADPGTAYSAVIQLGSLLAVLTYFYKDLVEILSGTVRALRTGDTQSREVRLFWGIILGTIPIVIAGLALKSTLEAPGSPLRALSVIAVASIVMAALLWLSESLGKRTRTMKGIRVIDGILIGCAQALALVPGVSRSGSTLTAALFLGFQRADGARFSFLLAIPAIFLSGLLELKVLVDEGFSGGIGPIVAGFVSSTVFSYLAIAWLLKFLQTRSTLVFVIYRFFFGALLLGLLAAGLLPDIEPVRQALNLP
|
Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
|
Q7NG92
|
Q5L2C9
|
Y616_GEOKA
|
Putative metal-dependent hydrolase GK0616
|
Geobacillus thermoleovorans group
|
MATVDPIRYPIGTFQAPQQFEAGEVQEWIAAIRGLPSDLRTAVSGLNDEQLNTPYREGGWTVAQVVHHLADASMNAFLRTKWGVTEDGPTVKPFAESEWAKTADACLLPIEPSLLLLDGLHARWAALLESMTEADFHRTVRPEGAAGEMPLYVLTALYAWHGKHHTAQVASLRKRKGW
|
Possible metal-dependent hydrolase.
|
Q5L2C9
|
B4U545
|
TRUA_STREM
|
tRNA-uridine isomerase I
|
Streptococcus
|
MTRYKAIISYDGTLFSGFQRQSQARTVQEEIEKTLQKLTGGQGIQIHGAGITDAGVHAYGQVIHFDLEQKRDPEKLRFALDTQTPDDIDVISLEIAADDFHARYHKHFKTYEFLVDIGRPKNPMMRHYATHYPYPLDIAKMQAAIKDLVGTHDFTGFTAAGTSVKNKVRTITAATLTQDPKTGFLVFTFSGNGFLYKQVRNMVGTLLKIGNGRLPIEQIRLVLESKNRQLAGPTAAGNGLYLKEIIYEE
|
Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
|
B4U545
|
B7GXE2
|
UPPP_ACIB3
|
Undecaprenyl pyrophosphate phosphatase
|
Acinetobacter calcoaceticus/baumannii complex
|
MENFEVIKALFLGFVEGLTEFLPISSTGHLILFGHIIDFHSDGGRVFEVVIQLGAILAVCWLYRQKIINLIKGFFSGDVESRHFAISVLIAFSPAVIIGVLAVDFIKSVLFSPIVVAIALIVGALIIFWVESKQFEHKTDDATKITFKQALLVGLAQCVAMIPGTSRSGATIVGGMFAGLSRKAATEFSFFLAMPTMLGAATFDLIKNADVLTSDNMVNIGVGFVAAFIAALLVVKALVLFVERHTLRVFAWYRIVLGVIILIAAMFFNLSA
|
Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
|
B7GXE2
|
B7KUV9
|
TRPD_METC4
|
Anthranilate phosphoribosyltransferase
|
Methylorubrum
|
MDAFKTHLAIVASGAPLSREQARAAFDDLLSGEVTPIQAGAFLTALSVRGESEDEIVGAVSAMRARMLPVAAPEGAIDIVGTGGDHSGSYNVSTLAAILTAACGVPVAKHGNRAATSRSGAADVLAALGVKIGLPPEALARCLSEAGLCFMFAQTHHGAMRHVAPVRTELPFRTIFNMLGPLSNPAGVTAQVFGVSRPAWAEPLTRVLATLGSRRVWTVHGSDGLDEITTTGPTAVVALEDGAFRHFTLDPREVSLPLATLDDLRGGDPEHNAAALGAVLEGARNAYRDIAVLNAGAGLVVAGAAGSLAEGVARAQEAIDSGAARGTLARLVAVSNA
|
Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
|
B7KUV9
|
Q93GB7
|
TPIS_LACDL
|
Triose-phosphate isomerase
|
Lactobacillus
|
MSRTPIIAGNWKLNMNPKETVEFVNAVKDQLPDPSKVESVICAPAVDLDALLKAAEGSNLHVGAENCYWENSGAFTGETSPAVLKEMGVQYVIIGHSERRDYFHETDEDINKKAKAIFANGLTPILCCGESLEIREAGKEKEWVVSQIKADLEGLTSEQVSKLVIAYEPIWAIGTGKTASSDQAEEMCKTIRETVKDLYNEETAENVRIQYGGSVKPANIKELMAKPNIDGGLVGGASLVPDSYLALVNYQD
|
Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
|
Q93GB7
|
Q8NIC1
|
TRI5_FUSCE
|
Sesquiterpene cyclase
|
Fusarium
|
MENFPTEYFLNTSVRLLEYIRYRDSNYTREERIENLHYAYNKAAHHFAQPRQQKMLKVDPKRLQASLQTIVGMVVYSWAKVSKECMADLSIHYTYTLVLDDSSDDPHPAMVNYFDDLQAGREQAHPWWALVNEHFPNVLRHFGPFCSLNLIRSTMDFFEGCWIEQYNFGGFPGSDDYPQFLRRMNGLGHCVGASLWPKDLFDERKNFLEITTAVAQMENWMVWVNDLMSFYKEFDDERDQISLVKNFVTCHEITLDEALEKLTQETLHSSKQMVAVFADKDPQVMDTIECFMHGYVTWHLCDARYRLHEIYEKVKDQDTEDAKKFCKFFEQAANVGAVAASEWAYPPVAQLANVRAKSDVKEAQKPFLSSIELVE
|
TS is a member of the terpene cyclase group of enzymes. It catalyzes the isomerization and cyclization of farnesyl pyro-phosphate to form trichodiene, the first cyclic intermediate in the biosynthetic pathway for trichothecenes. It serves to branch trichothecene biosynthesis from the isoprenoid pathway.
|
Q8NIC1
|
P60979
|
TX13_KUKHI
|
Toxin DW13.3
|
Kukulcania
|
AECLMIGDTSCVPRLGRRCCYGAWCYCDQQLSCRRVGRKRECGWVEVNCKCGWSWSQRIDDWRADYSCKCPEDQ
|
Potently blocks vertebrate calcium channels Cav1 and Cav2. Is the most active on Cav2.2/CACNA1B (from HEK) (IC(50)=2.3 nM), followed by Cav2.1/CACNA1A (IC(50)=4.3 nM), Cav2.2/CACNA1B (from oocyte) (IC(50)=14.4 nM), Cav1.2/CACNA1C (IC(50)=26.8 nM), and Cav2.3/CACNA1E (IC(50)=96.4 nM).
|
P60979
|
Q1QE85
|
TSAD_PSYCK
|
tRNA threonylcarbamoyladenosine biosynthesis protein TsaD
|
Psychrobacter
|
MKVLGLETSCDETGLAIFDSEQVTSDNKGLLGQVLYSQIELHALYGGVVPELASRDHIRKLVPLFNELLQQCNITKDEIDAVAYTKGPGLIGALMTGALFGRSLAYGLDIPAIGVHHMEGHLLAPLMGANPPAFPFVSLLVSGGHTLLIAAHGIGQYEILGESIDDAAGECFDKAAKMLGLPYPGGPNIAKLAESGNSDAYSLPRPMLHRGLDFSFSGMKTAVHNLIKDTPCSGGSGNGSDSDPQVRADIAASFQHAVVDTLVKKCVKALKQVNMSRLVIAGGVSANSHLRKTLERELAKINATVHYAPPALCTDNGAMIAYAGYERLQAGQADDLAVSCVPRWPMTELPAV
|
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
|
Q1QE85
|
A7WNV7
|
TP1A_LITPA
|
Temporin-1PLa
|
Lithobates
|
MFTSKKSLLLLFFLGTINLSLCEEERDADEEERRDDPDEMNVEVEKRFLPLVGKILSGLIGK
|
Antimicrobial activity against the Gram-positive bacterium S.aureus.
|
A7WNV7
|
Q98QQ2
|
TMCAL_MYCPU
|
tRNA(Met) cytidine acetate ligase
|
Mycoplasmopsis
|
MAIAIIAEYNPFHNGHIYQINYVKEKFPGEKIHIILSGNYVQRGEIAIASFEKRKKIALEYGADYVHELEFEYASQAAHIFAKGALAKINSLQIDKLIFGSETNDINEFINIAKIIKDNKSQYQLFLKENLKKGLSFPKASSLASQKITGKYFQMPNDILGFEYVKQIIFNNYKITAFCHTRTNDYKSDKPSGKYASSTLIRKMIFEGKDVSKYTPMIFEKKPIRIEDLYFDFQTIIFNKTAQELRQFKLVSEGIENLFKKHINEKSYDDFVAKVNSKRYTSSRIKRIILYILLGIKN
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Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of elongator tRNA(Met), using acetate and ATP as substrates. First activates an acetate ion to form acetyladenylate (Ac-AMP) and then transfers the acetyl group to tRNA to form ac(4)C34.
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Q98QQ2
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C6AN26
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TORD_AGGAN
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Chaperone protein TorD
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Aggregatibacter
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MLHHNQMVLMGLLNMLKISIQERQFVYSWICSLLSKELTQDQLAHYQRGDFDSLFAFLKELGFTEQTEQLIATLRPMEFQQLELAADFAHTFLLEGNISAIPYMSAYLQGEELGVALNLVDQWMTHYQLGVNREQNEPSDHVSVLLAILIRLIGEQPFHVQQDFAQKALLNWLPEFVRKANNTSCETKFYAMLCNLFLAFMTEDFAV
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Involved in the biogenesis of TorA. Acts on TorA before the insertion of the molybdenum cofactor and, as a result, probably favors a conformation of the apoenzyme that is competent for acquiring the cofactor.
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C6AN26
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A4Y5U9
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TOLB_SHEPC
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Tol-Pal system protein TolB
|
Shewanella
|
MKILAKWLALAVLLCTTPTKAALDIVITEGIDAARPIAVMPFVWQGTGAPPQAIADVVMSDLVRSGTFKPLDELGLPQRNIGAVAQFQASAWGSVGAEALVLGSVKPYGTDQYLVSFDLIDLVKAQNQSLKGAVSPTEFLMDSRQTVISAAQFRQYGHRISDIVYEKLTGIRGAFLTRISYVVVNHTQKAPYQLMIADYDGFNEQMLLRSPEPLMSPTWSPDGRRLAYVSFENKKAEIFVQDLYTQVRTKVSSFPGINGAPAFSPDGKSLAVTLSKDGQPEIYVIDIATKAIKRITNHYAIDTEPSWYPDGKSLLFTSERGGKPQLYRVDLASGKVTRETFEGEWNLGGSITPDGRSMIFVNRTNGKFNIARMDLNTRFMQVLTSTRLDESPSVAPNGTMVIYGTTHQGKQVLAAVSTDGRFKARLPVGQGEVKSPSWSPFL
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Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity.
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A4Y5U9
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Q4QLR0
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YIDC_HAEI8
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Membrane protein YidC
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Haemophilus
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MDSRRSLLVLALIFISFLVYQQWQLDKNPPVQTEQTTSITATSDVPASSPSNSQAIADSQTRGRIITLENDVFRLKIDTLGGDVISSELLKYDAELDSKTPFELLKDTKEHIYIAQSGLIGKNGIDTRSGRAQYQIEGDNFKLAEGQESLSVPLLFEKDGVTYQKIFVLKRGSYDLGVDYKIDNQSGQAIEVEPYGQLKHSIIESSGNVAMPTYTGGAYSSSETNYKKYSFADMQDNNLSIDTKAGWVAVLQHYFVSAWIPNQDVNNQLYTITDSKNNVASIGYRGPVVTIPAGSQETITSSLWTGPKLQNQMATVANNLDLTVDYGWAWFIAKPLFWLLTFIQGIVSNWGLAIICVTIVVKAILYPLTKAQYTSMAKMRILQPKMQEMRERFGDDRQRMSQEMMKLYKEEKVNPLGGCLPILLQMPIFIALYWTFLEAVELRHAPFFGWIQDLSAQDPYYILPILMGISMFLLQKMSPTPVTDPTQQKVMNFMPLVFMFFFLWFPSGLVLYWLVSNLITIAQQQLIYRGLEKKGLHSRKK
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Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins.
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Q4QLR0
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C3MCT9
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UPPP_SINFN
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Undecaprenyl pyrophosphate phosphatase
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Sinorhizobium
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MADQSIISALVLGLIEGLTEFIPVSSTAHVLLAGHFLGFKSPGNTFAVLIQLGAILAILLVYFQKLLSIALALPTSVKARRFVFSVLIAFLPAALIGAAAHGFIKAVLFETPMLICVVLIVGGVILYAIDRLPLQPRYTDVFDYPPSLALKIGLFQCLAMIPGTSRSGATIAGALLMGTDKRSAAEFSFFLAMPTMLGAFTLDLYKNRDALSFDDIGVIAIGFIAAFVAGIVVVRSLLDFVSHRGFTPFAIWRIVVGTAGLVGLWLVG
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Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
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C3MCT9
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P81660
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TNNC2_ANGAN
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Troponin C, skeletal muscle
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Anguilla
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PTDAQTDARSFLSEEMIAEFKAAFDMFDTDGGGDISTKELGTVMRMLGQNPTREELDAIIEEVDEDGSGTIDFEEFLVMMVRQLKEDQAGKSEEELAEFFRVFDKNGDGFIDREEFGEILRSSGEPVSEEEIDELMADGDKNNDGKIDFDEWLKMMENIQ
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Troponin is the central regulatory protein of striated muscle contraction. Tn consists of three components: Tn-I which is the inhibitor of actomyosin ATPase, Tn-T which contains the binding EF-hand for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the inhibitory action of Tn on actin filaments.
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P81660
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Q5PK87
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THIG_SALPA
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Thiazole synthase
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Salmonella
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MLRIADKTFDSHLFTGTGKFASSQLMVEAIRASGSQLVTLAMKRVDLRQHNDAILAPLIEAGVTLLPNTSGAKTAEEAIFAAQLAREALGTHWLKLEIHPDARWLLPDPIETLKAAEALVKQGFVVLPYCGADPVLCKRLEEVGCAAVMPLGAPIGSNQGLETKAMLEIIIQQATVPVVVDAGIGVPSHATQALEMGADAVLVNTAIAVADNPVMMATAFRLAVEAGLLARQAVPGNRSTYASATSPLTGFLEALA
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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.
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Q5PK87
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O34522
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TRMB_BACSU
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tRNA(m7G46)-methyltransferase
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Bacillus
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MRMRHKPWADDFLAENADIAISNPADYKGKWNTVFGNDNPIHIEVGTGKGQFISGMAKQNPDINYIGIELFKSVIVTAVQKVKDSEAQNVKLLNIDADTLTDVFEPGEVKRVYLNFSDPWPKKRHEKRRLTYSHFLKKYEEVMGKGGSIHFKTDNRGLFEYSLKSFSEYGLLLTYVSLDLHNSNLEGNIMTEYEEKFSALGQPIYRAEVEWRT
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Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
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O34522
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Q9PR42
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UVRA_UREPA
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Excinuclease ABC subunit A
|
Ureaplasma
|
MDKIIIKGARENNLKNIDLEIPKNKLVVITGVSGSGKSSLAFDTIFAEGKRRYFESLSSYARQFLGGNDKADVESIEGLSPTIAVDQKSTNQNPRSIVGTITEIYDYLRVLFARVGTPFCPNGHGQIKSQTPKQIADFLFSLSPKSKIQILAPIEIKKGYKINDVLNNLRNQGYLRVLVNNEVYQLDENLPQFLDNKKTDVAIIVDRLILNIDHQTKTRALDAIEFALNYSGGEIAFKVNDDIHYFTQNDVCQVCGFKIKEIEPTLFSFNSPIGACEQCKGLGYNYVPDERKMIPNPNLSINEGGLDYFKNTVNTTNLDWQRFNSIIKHYKIDKTKPLKELDRKEIDLLLYGSDEAIEIDITSANNKKYSSIDYVEGVLELVNRRYQETSSELAREHYNKYMSEKVCKSCKGKKLSSQALSVLINKINIIDFIEKNIDEAIDFLLHLDLNEAQTKIANPILKEVLDRLGFLKNVGLEYLTLARPASSLSGGEAQRIRLATQIGSKLTGILYVLDEPSIGLHQRDNDKLINTLKEMRDLGNTVIVVEHDEETMLAADYLIDIGPQAGVNGGYVIAAGTPQEVMQNPNSLTGQYLSKQKDILVPKTRRSGNGHKVILKGAKHNNLKNVDLTIPLGKFICVTGVSGSGKSSLILETLVKAIEYTNFNPFVIPGEYKDLIGASNVDKIVVVNQDAIGRTTRSNPATYVGVFDDIRTVFENTIEAKARGYSKSRFSFNIKGGRCERCWGDGTIRIEMHFLPDVYISCEECHGKRYNDETLQVKFKGKSIYDVLKMPIDEALVFFENYPGIHRKLQLLVDVGLGYLELGASSTSLSGGEAQRIKLAKFLQRKPTGKTLFVLDEPTTGLHIDDVAKLIKILDKIVDGGDTVLVIEHNLDLIKVADYIIDIGPEGGNKGGKIIATGTPEQLLSKKDISYTAQYLEKYLKKN
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The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by UvrB, the UvrA molecules dissociate.
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Q9PR42
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Q9D806
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VSTM5_MOUSE
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V-set and transmembrane domain-containing protein 5
|
Mus
|
MRPLRCGERTQGIPLGLLAFWVTAARCLQSQGVSLYIPQSAINATVQQDILLSVDYICHGVPTIEWKYTPNWGVQRIVEWKPGTPANVSQSHRDRVCTFDNGSIQLFNVSVKDSGYYIVTVTEHPGSSQSGTILLRVSEIRYEDLHFVAVFFALLAAVAVVLISLMWVCNQCAYKFQRKRRYKLKESTTEEIEMKEVEC
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Cell adhesion-like membrane protein of the central nervous system (CNS) which modulates both the position and complexity of central neurons by altering their membrane morphology and dynamics. Involved in the formation of neuronal dendrites and protrusions including dendritic filopodia. In synaptogenesis, regulates synapse formation by altering dendritic spine morphology and actin distribution. Promotes formation of unstable neuronal spines such as thin and branched types. Regulates neuronal morphogenesis and migration during cortical development in the brain.
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Q9D806
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Q1LSM0
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TSAD_BAUCH
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tRNA threonylcarbamoyladenosine biosynthesis protein TsaD
|
Candidatus Baumannia
|
MRVLGIETSCDDTGVAIYDDQHGLLTNQIYSQAKIHANYGGVVPELASRDHLRKIVPLIQAALSEARLQAKNIDGVAYTAGPGLISSLMVGATVGCALAYAWKVPNIAVHHMEGHLLAPMLEINPPSFPFVALLVSGAHTQLIAVTKMGKYQLLGQSVDDAVGEAFDKTAKLLGLDYPGGPMLSKIAQQGIAGRYKFPRPMTERPGLNFSFAGLKTFAANTINIAASDAQTHADIARAFEDAVVDTLMIKCQRALDQTGFKRLVMAGGVSANQTLRNRMKKMVEQRGEEIFYARPELCTDNGAMIAYVGSVRFASLVLPQSQLAVIVRPRWPLEELTTISR
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Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
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Q1LSM0
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B7GW49
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XPT_ACIB3
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Xanthine phosphoribosyltransferase
|
Acinetobacter calcoaceticus/baumannii complex
|
MHALEQKILTEGIVLSDQVLKVDAFLNHQIDPVLMQQIGKEFAARFKDAGITKIITIEASGIAPAIMAGLELGVPVIFARKYQSLTLKDDLYRAKVFSFTKQTESTIAISNKHINSSDKALVIDDFLANGQAALGLIDLIHQANAEVVGVGIVIEKSFQPGRDLLLEKGYRVESLARVQSLADGTVTFVKE
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Converts the preformed base xanthine, a product of nucleic acid breakdown, to xanthosine 5'-monophosphate (XMP), so it can be reused for RNA or DNA synthesis.
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B7GW49
|
Q92BX6
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YIDC1_LISIN
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Membrane protein YidC 1
|
Listeria
|
MKKKNIILISVLLGALLLITGCSMDPSQNTDGFFSTYLIQPFTSFIMFVAKFVGGNYGIAIIITTLLIRALIMPLNLRTAKAQMGMQSKMAVAKPEIDEIQARLKRATSKEEQANIQKEMMAVYSKYNINPIQMGCLPLLIQMPILMAFYYAIRGSSEIASHTFLWFNLGSPDMVLAIIAGLVYLAQYFVSMIGYSPEQKKQMKIIGLMSPIMILFVSFTAPSALALYWAVGGLFLAGQTLLTKKLYMNKHPEIKVMEQEEKEFEQIVEEQNKEK
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Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins.
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Q92BX6
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Q6LN28
|
UPPS_PHOPR
|
Undecaprenyl pyrophosphate synthase
|
Photobacterium
|
MAERTIETELSAECLPKHVAVIMDGNGRWAKAKGKARVFGHKAGVEAVRKSVTTANRLGVKVLTLFAFSSENWRRPEDEVSLLMELFMTVLTREVKRLHKNNIQLRIIGDKSGFSERLQRKIATSEALTANNTGLVLNIAANYGGQWDILQATKKLAVQIAEQGLTASDITEDMLSAGMSTADLPDVDLMIRTSGECRISNFMLWQAAYAELYFTEQHWPDFDEESFANAIAWYINRERRFGCTGEQIQALIQE
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Catalyzes the sequential condensation of isopentenyl diphosphate (IPP) with (2E,6E)-farnesyl diphosphate (E,E-FPP) to yield (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30Z,34E,38E)-undecaprenyl diphosphate (di-trans,octa-cis-UPP). UPP is the precursor of glycosyl carrier lipid in the biosynthesis of bacterial cell wall polysaccharide components such as peptidoglycan and lipopolysaccharide.
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Q6LN28
|
A0ALT4
|
TRUA_LISW6
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tRNA-uridine isomerase I
|
Listeria
|
MTRYKAIISYDGSGFYGYQIQPNARTVQAEIEKALKKMHKGKNVRITASGRTDTGVHAKGQVIHFDSDLDITADKFQKALQVMTPFDISFLTVDEAPADFHARFGTVGKEYRYIVKRTKIFDPFSRNFALHYPYELDIAKMKLASECLIGEHDFTSFCSARTERDSKVRTLYSIDFYEEDEETLVIAFQGNGFLYNMVRILTGTLLDAGQGRISSEDITEALLARDRQKLISKTAPPQGLYLWRVDYE
|
Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
|
A0ALT4
|
Q2YJ75
|
VIRB5_BRUA2
|
Type IV secretion system protein virB5
|
Brucella
|
MKKIILSFAFALTVTSTAHAQLPVTDAGSIAQNLANHLEQMVKFAQQIEQLKQQFEQQKMQFDALTGNRGLGDILRDPTLRSYLPHNWRDLYEAVMSGGYLAAAGETANLLRKSQVYDPCASISDKDQRIACEAKVVKPVQDKVMTSKAYDATDKRLQEIESLMQEINKTGDPKAIAELQGRIESENAMIQNEDTRLRLYQQMAEAQDKLLDERQHELDAKDNARRGYPQPKALEAAY
|
The virB operon is essential for intracellular survival and is not involved in the invasion process. Constitutes a major determinant of virulence in mice.
|
Q2YJ75
|
G3Y424
|
YANF_ASPNA
|
Yanuthone D biosynthesis cluster protein F
|
Aspergillus subgen. Circumdati
|
MSSSAECRPIGWGGWGPDPNTSPTRAAIKWFADPRSLHHQQCACGLWNARRAMQWVIPAPPRIWIDDQPRMVKLAYILGAVTVFLTSGNAADVSPTSSVAASTTPSAADSLSSLGLSLPAGNVLVGNNETFTASSPYYEPLIDEAWSGNCRLNASCIVTPKSAQEVSLVIQVLSILDTKFSIRSGGHSSSPGFSSIGSNGVLVALERLNTLSISADRKTLTVGPGNRWEAVYQYLEQYNLTVLGGREPVVGVGGFVLGGGLSLFYNTNGLAIDTVTRFQVVTPNGTIVNATPTEHADLYKGLKGGLNNFGIIVEYDLTTNTGIDVWFEVKNYTRAETPALLAAYATYLQNADVRSNVEIQANPAYTVVLYGYLDHVSAPSAFNAFSTVPSVSTVYPPTNASLNEVLLEIGTAGVTGSSWTYTVSFSFKVTNPDFLQESYKTYLEAAASLLPSGVLLEYVPQGIIPNLVTKGQAQNGGNLLGLEATPQVWGEIFAQFPATVSQSTVASAVNDLLAKITSSAESQGVHLPYIFANDAGPDQQVLRGYGEDNLKYIATVAERYDPKGVMQKLQNDAYFVSKEL
|
FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of yanuthone D, a fungal isoprenoid epoxycyclohexenone that acts as an antibiotic against fungi and bacteria . The first step of the pathway is the synthesis of 6-methylsalicylic acid (6-MSA) by the polyketide synthase yanA . 6-MSA is then converted to m-cresol by the decarboxylase yanB . The cytochrome P450 monooxygenase yanC then catalyzes the oxidation of m-cresol to toluquinol . Epoxidation of toluquinol is then performed by the short chain dehydrogenase yanD, with the help of yanE, and a further prenylated by yanG leads to 7-deacetoxyyanuthone A . The next step is the hydroxylation of C-22 of 7-deacetoxyyanuthone A by the cytochrome P450 monooxygenase yanH to yield 22-deacetylyanuthone A . O-Mevalon transferase yanI then attaches mevalon to the hydroxyl group of 22-deacetylyanuthone A to produce yanuthone E . Finally, the FAD-dependent monooxygenase yanF oxidizes the hydroxyl group at C15 of yanuthone E to form yanuthone D . Furthermore, several branching points in the pathway lead to the production of yanuthones F and G from 7-deacetoxyyanuthone A; yanuthones H and I from 22-deacetylyanuthone A; and yanuthone J from yanuthone E .
|
G3Y424
|
Q9R2W4
|
VIRB4_BARHE
|
Type IV secretion system protein virB4
|
Bartonella
|
MSMMKRESLPEDYIPYIRHINQHVIALNSRCLMTVMVVEGVNFDTADIDQLNSLHNQLNTLLKNIADERVALYSHIIRRRETIYPESQFFSSFAATLDEKYKKKMVSQELYRNDLFVSLLWNPASDKTEQLASFFQRLAKAKKTQSEPDQEAIRKIEELSQDLIEGLESYGARLLSVYAHGGILFSEQSEFLHQLVGGRRERIPLTFGTIASTIYSDRVIFGKETIEIRHESNERFAGMFGWKEYPSKTRPGMTDGLLTAPFEFILTQSFVFKSKAAASVIMGRKQNQMINAADRASSQIEALDEALDDLESNRFVLGEHHLSLAVFANHPKALAEYLSKARAHLTNGGAVIAREDLGLEAAWWAQLPGNFSYRARSGAITSRNFAALSPFHSFPIGKLEGNVWGTAVALLKTQAGSPYYFNFHYGDLGNTFVCGPSGSGKTVIVNFLLAQLQKHNPTMVFFDKDQGAEIFVRAGGGKYKPLKNGQPTGIAPLKGMEYTEKNKVFLRNWVLKLVTAEGQTVTEEERQDIAKAIDALGNLPHAQRSLSALQLFFDNTSKEGIAIRLQRWLKGNDLGWVFDNDQDDLNLDSQFIGYDMTDFLDNEEIRRPLMMYLFNRILDLIDGRRIIIVIDEFWKALEDDSFKAFAQDRLKTIRKQNGMMLFATQSPKDALNSTIAHTIIEQCPTQIFFPNQKANYKDYVEDFKLTEREFELIQSELSRESRRFLIKQGQSSVVAELNLRGMNDEIAVLSGTTKNIELVNQIISEYGADPDIWLPIFHQRRENQ
|
The type IV secretion system VirB/VirD4 is a major virulence determinant for subversion of human endothelial cell (HEC) function. VirB-dependent changes of HEC include massive cytoskeletal rearrangements, a pro-inflammatory activation by nuclear factor NF-kappa-B, inhibition of early and late events of apoptosis, leading to an increased cell survival, and, at high infection doses, a cytostatic or cytotoxic effect, which interfers with a potent VirB-independent mitogenic activity. These changes of HEC require the T4S coupling protein VirD4 and at least one of the effector proteins BepA-G. Altogether with VirB11, may be implicated in providing the energy, via hydrolysis of ATP, for the assembly of secretion system and substrate transport.
|
Q9R2W4
|
Q3KQV3
|
ZN792_HUMAN
|
Zinc finger protein 792
|
Homo
|
MAAAALRDPAQGCVTFEDVTIYFSQEEWVLLDEAQRLLYCDVMLENFALIASLGLISFRSHIVSQLEMGKEPWVPDSVDMTSAMARGAYGRPGSDFCHGTEGKDLPSEHNVSVEGVAQDRSPEATLCPQKTCPCDICGLRLKDILHLAEHQTTHPRQKPFVCEAYVKGSEFSANLPRKQVQQNVHNPIRTEEGQASPVKTCRDHTSDQLSTCREGGKDFVATAGFLQCEVTPSDGEPHEATEGVVDFHIALRHNKCCESGDAFNNKSTLVQHQRIHSRERPYECSKCGIFFTYAADLTQHQKVHNRGKPYECCECGKFFSQHSSLVKHRRVHTGESPHVCGDCGKFFSRSSNLIQHKRVHTGEKPYECSDCGKFFSQRSNLIHHKRVHTGRSAHECSECGKSFNCNSSLIKHWRVHTGERPYKCNECGKFFSHIASLIQHQIVHTGERPHGCGECGKAFSRSSDLMKHQRVHTGERPYECNECGKLFSQSSSLNSHRRLHTGERPYQCSECGKFFNQSSSLNNHRRLHTGERPYECSECGKTFRQRSNLRQHLKVHKPDRPYECSECGKAFNQRPTLIRHQKIHIRERSMENVLLPCSQHTPEISSENRPYQGAVNYKLKLVHPSTHPGEVP
|
May be involved in transcriptional regulation.
|
Q3KQV3
|
Q9KN48
|
VASH_VIBCH
|
Transcriptional regulator VasH
|
Vibrio
|
MSQWLAFATQLVGVRKSHQLALQFVDLLTQGLDLSDSLLLLPSSDGRLLVPHDPQRQFAWSVTDFDVPFAHVLQSSNAMHLTAEELVFWQSNRTFSQLTSRVGMFDSVWIQPLPMDTRQVHSILLLMGESHGIVSAFENADFLKFIEVFSQQWSLLNDMEREEQRRLELKQSLTDIERDSAQRSLANALSRTLIGESAAMQKLREQIVSAANSQLSVMVQGETGTGKELVAAAVHELSSRKSAPFVAINCAAIPEHLLESELFGYCKGAFSGADSDKQGLIAQANGGTLFLDEIGDMPLTLQAKLLRVLESRTFRPLGGKQELSSDFRLVSATHVNLLDQVRKKEFRQDLYYRLFQYPITLPRLAARLEDIELLSEHFVRVFNLQHNTRIRGLNYRAIDCLKQYDFPGNVRELKHLIEFGCAQTADGTQVEASCFAHRLQTLPCLAPEATPVAVSVETENVDLEPSVALAGEPNFAVIHDLKQAVSQFEALIISERLNRFAGDRAKAAKSLGIPKRTLAYKCLKLEIKTP
|
Transcriptional regulator of the type VI secretion system.
|
Q9KN48
|
B6J3P6
|
UBIE_COXB2
|
Demethylmenaquinone methyltransferase
|
Coxiella
|
MNETEKSTHFGYQTVPTDQKTDKVKHVFESVAAKYDLMNDLMSLGIHRWWKDFAITQCRLRTGQRILDLAGGTGDLAKRISPLVGDEGEVVIADINAAMLNVGRRRLLDQGIFRNIQFIQADAEKLPFPNNFFDRIVIGFGLRNVTNQLAALQSMHRVIKPGGFVVILEFSKPTLAPLKAVYDAYSFQLLPRLGKLVAKDEESYRYLVESIRMHPDQEALLSKMTDAGFEDCDYHNLSGGIVAVHRGYKF
|
Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2) and the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2).
|
B6J3P6
|
Q161G7
|
YBEY_ROSDO
|
Endoribonuclease YbeY
|
Roseobacter
|
MDIDILIEDDRWAAMDLDVLVRDVLRAISDTLTLDLAAAEVSYLACDDARIALLNADFREKATATNVLSWPAADLAPVVAGAVPTTPTVDVTGALTLGDVAIAYETCEREAADLGKPLAEHVTHLIVHGTLHLLGYDHIRDSDAALMQGVEAKILGKMGFDDPYMV
|
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
|
Q161G7
|
Q82VF0
|
TGT_NITEU
|
tRNA-guanine transglycosylase
|
Nitrosomonas
|
MKFQLHCRDHEARRGTLTLAHGTVETPAFMPVGTYGAVKGLSPDELHTLGAGIILGNTFHLWLRPGLEVIGAHGGLHRLMNWDGPILTDSGGFQVFSLGALRKICEEGVRFRSPVNGDTCFLTPEESMRIQQVLNSDIVMIFDECTPYPVDMQIAESSMQLSLRWAERSKTAHAGNPNALFGIVQGGMYESLRDHSAAGLCAIGFDGYAIGGLSVGEPKADMQRILRHTAPQLPADKPRYLMGVGTPEDIVHAVAQGIDLFDCVLPTRNARNGWLYTSQGILRLRNSRYRLDTSPPDEHCDCYTCRHFTRAYLHHLQRTGEMLGARLNSLHNLHYYQRLMANIRKAIETGQFEQFARKFSGQDFMLKCASV
|
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
|
Q82VF0
|
P21797
|
TNNC1_BALNU
|
Troponin C, isoform 1
|
Balanus
|
SPDGEYAEETGLEKEQIVVLRRAFDSFDRDKKGYISPETVSDILRMMGIKVSSTSFKQIIEEIDEDGSGQIEFSEFLQLAAKFLIEEDEEAMMKELKEAFRLYDKEGNGYITTQTLKEILHELDARLTAEELVGIIEEIDEDGSGTVDFDEFMAMMTG
|
Troponin is the central regulatory protein of striated muscle contraction. Tn consists of three components: Tn-I which is the inhibitor of actomyosin ATPase, Tn-T which contains the binding site for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the inhibitory action of Tn on actin filaments.
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P21797
|
B3CLX6
|
TSAD_WOLPP
|
tRNA threonylcarbamoyladenosine biosynthesis protein TsaD
|
unclassified Wolbachia
|
MKTILAIETSCDETAVAIVNSDKQVLANEILSQVEHKKCGGVIPEIASRAHMKHLSGLIKSAMEKSNLNFCDLDAIAATSGPGLIGGLIIGTMMAKAIAHVTQKPFIAVNHLEAHALVVRLLYEVEFPFLVLLISGGHCQFLIAQDVGKYIKLGETLDDSLGEAFDKVAKTLGLSYPGGPLIEELAKKGDGMRFKLPRAMIKRSGCDLSFSGIKTAVKNLAREFVMSEQDVCDMCASFQECISDILLDRVRNAIGIAVSLNIKINDFVITGGVAANNFLKERLKKHIDLNVLSPPSNLCTDNAVMVGWTGIERLQRSYVDSLDFAPRPKWELEKYY
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Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
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B3CLX6
|
Q6G1R3
|
TSAD_BARHE
|
tRNA threonylcarbamoyladenosine biosynthesis protein TsaD
|
Bartonella
|
MRLLGIETSCDETATAVIEHTIGGNSQILSNIVWSQTDHHAPYGGVVPEIAARAHVEILDELILKALRDAHTKLKDIDAIAVTNGPGLIGGLLVGVMSAKALSLATGKPFIGVNHLEGHALTAVLTHNVHFPYLLLLVSGGHTQTILVHGVGNYQRLGTTIDDALGEAFDKTAKLLGLPYPGGPAIEKAALLGNKNRIPLPRPLKGEKRLDFSFSGLKTAVRQAATAISPLTESDVADIAASFQAAVTDTVYDRVYLALQHFTQQYPLSRHQGPRPPALVVAGGVAANQAIRLTLQELADQQGFEFIAPPLSLCTDNAAMIAFAGAQRLARGEKSSLDIAPRSRWPLDEKSAPLIGTGRRGTKA
|
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
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Q6G1R3
|
A1R8Y7
|
TYSY_PAEAT
|
Thymidylate synthase
|
Paenarthrobacter
|
MSIPTPYEDLLRDVMANGTHKSDRTGTGTRSVFGRQLRFDLAESFPLITTKRVHFKSVAVELLWFLRGDSNVKWMQDQGVSIWDEWADADGELGPVYGVQWRSWPTPDGGHIDQISELMTNLAANPDSRRHIVSAWNVSELKDMALPPCHAFFQFYVADGKLSCQLYQRSADTFLGVPFNIASYALLTRMVAQQLGLEPGEFVWTGGDVHVYDNHVDQVAEQLSREPYEYPQLKILRKPDSIFDYTLDDFEVVDYRHHPTIKAPIAV
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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.
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A1R8Y7
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Q73S85
|
Y4191_MYCPA
|
Putative S-adenosyl-L-methionine-dependent methyltransferase MAP_4191c
|
Mycobacterium avium complex (MAC)
|
MTSTRYEGDTWDLASSVGVTATMVAAARAMATRADNPLINDLFAEPLVKAVGVDLLSRLAGGELDPAELNDVHDGAAGSAGAMSRMADNMAVRTKFFDEFFLNATKAGIAQVVILASGLDARAYRLAWPAGTVVYEVDQPQVIDFKTTALAQLGAAPTAERRVVAVDLRDDWPAALRAAGFDPARPTAWSAEGLLGYLPPEAQDRLLDTITELSAPGSRLATESAPNPAPGEEEKLKERMQAISQRWRAHGFDLDMAGLVYFGERNEAAPYLAGHGWRLNSVTIRDLFAANGLDPLDDDDTRMGEMLYTWGIYE
|
Exhibits S-adenosyl-L-methionine-dependent methyltransferase activity.
|
Q73S85
|
A9MVX4
|
TREA_SALPB
|
Alpha,alpha-trehalose glucohydrolase
|
Salmonella
|
MIPPEIRRSVLLQKAIKLALAGTLLTFASFSATAADPSSDTETPQPPDILLGPLFNDVQNAKLFPDQKTFADAIPNSDPLMILADYRMQRNQSGFDLRHFVDVNFTLPKAGEKYVPPAGQSLREHIDGLWPVLTRSTKNVEKWDSLLPLPESYVVPGGRFREIYYWDSYFTMLGLAESGHWDKVADMVANFGYEIDAWGHIPNGNRTYYLSRSQPPFFAFMVELLAQHEGDDALKEYLPQLQKEYAYWMEGVETLQPGQQNQRVVKLEDGSVLNRYWDDRDTPRPESWVEDIATAKSNPNRPATEIYRDLRSAAASGWDFSSRWMDNPQQLSTIRTTTIVPVDLNALLYQLEKTLARASAAAGDRAKASHYDALANARQQAIEMHLWNNKEGWYADYDLKNNKIRDQLTAAALFPLYVNAAAKDRAAKVAAAAQAHLLQPGGLATTSVKSGQQWDAPNGWAPLQWVAAEGLQNYGQDDVAMEVTWRFLTNVQHTYDREKKLVEKYDVSSTGTGGGGGEYPLQDGFGWTNGVTLKMLDLICPQEKPCDSVPSTRPASLSATPTKTPSAATQ
|
Provides the cells with the ability to utilize trehalose at high osmolarity by splitting it into glucose molecules that can subsequently be taken up by the phosphotransferase-mediated uptake system.
|
A9MVX4
|
G4ZHR2
|
XEG1_PHYSP
|
Glycoside hydrolase family 12 protein XEG1
|
Phytophthora
|
MKGFFAGVVAAATLAVASAGDYCGQWDWAKSTNYIVYNNLWNKNAAASGSQCTGVDKISGSTIAWHTSYTWTGGAATEVKSYSNAALVFSKKQIKNIKSIPTKMKYSYSHSSGTFVADVSYDLFTSSTASGSNEYEIMIWLAAYGGAGPISSTGKAIATVTIGSNSFKLYKGPNGSTTVFSFVATKTITNFSADLQKFLSYLTKNQGLPSSQYLITLEAGTEPFVGTNAKMTVSSFSAAVN
|
Glycoside hydrolase that exhibits xyloglucanase activity . Acts as an important virulence factor during P.sojae infection but also acts as a pathogen-associated molecular pattern (PAMP) in soybean and solanaceous species, where it can trigger defense responses including cell death. XEG1-induced cell death can be suppressed by P.sojae RxLR effectors. The PAMP activity is independent of its xyloglucanase activity . XEG1 induces plant defense responses in a RLP kinase Serk3/Bak1-dependent manner in Nicotiana benthamiana. Moreover, the perception of XEG1 occurs independently of the perception of ethylene-inducing xylanase Eix2 in Tomato . With truncated paralog XLP1, is required to elevate apoplastic sugar during P.sojae infection .
|
G4ZHR2
|
Q6KZ89
|
UPPS_PICTO
|
Undecaprenyl pyrophosphate synthase
|
Picrophilus
|
MSDIGNFVSRIYESKLLEEIKKHPVPGHLGIITDGNRRYARSIGISENEGHVKGKEKLEEVLNWSMEVGIHMVTVYAFSTENFKRKSDEVNFLFNLINDAFIDLLNDERVYKNGIRVKVIGDISKLPDYLKETIKRVEGETNKFKNFRFNLAIGYGGRQEIIDAIKKIGQDILNGKIKVDNINEEMFRSYLYDKTLPDPDLILRTSGEERISNFLLWQSAYSELYFADVNWPELRKIDFLRAIYSYQNRKRRFGE
|
Catalyzes the sequential condensation of isopentenyl diphosphate (IPP) with geranylgeranyl diphosphate (GGPP) to yield (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30E,34E,38E)-undecaprenyl diphosphate (tritrans,heptacis-UPP). It is probably the precursor of glycosyl carrier lipids.
|
Q6KZ89
|
Q78XR0
|
TPC6A_MOUSE
|
Trafficking protein particle complex subunit 6A
|
Mus
|
MADAVLFEFLHTEMVAELWAPDPDPGSGGKRRSLSVLEGLGFRVGQALGERLPLETPAFREELDALKFLCRDLWAAMFQKHMDGLRTNHQGTYVLQDNSFPLLVTMGSGPQYLEEAPKFLAFTCGLLCGALHTLGFQSLVTASVASLPACKFQVVIQKS
|
May play a role in vesicular transport during the biogenesis of melanosomes.
|
Q78XR0
|
Q3LHL9
|
WGE_DROME
|
Protein winged eye
|
Sophophora
|
MATFNPGASSSAADVLSATTATATFLVPTTAAVSHPGAHTAHLQLDQFGGFSAATATPLQHHHHQQTNSSYTFVQIKREPCQVSEISSNNCHQQQQQHHQHHQHQVQHQGLSSASMTASSKTMSSSTLTTLVKIEAPSPKVSELEKSTGNSVPIGIAVARKRPQEALVPAINTPATLPLQPPLNKDLNCFGIRVADLGATSCGNLYFTGNGDLMTTGTATAEELALSAAGVNRAPSTFWQYPNALPIESVISMSPATVGLQYSREASRGQVVLLPAGPTALDPFQQAAAAAAFVWPSAYIPQAPAPGGHSAAAAAAAASLQPTPNLSSLPNFIFPSMGGHQALSTTPSYASTLQLYLAAAATATGSSTMCQHSNQQTSTTTTNSTINLSLAAGSGVTQSGNAASSLSSSSSLSASSSRFLSLATGQTGIPSLLSLPPPTGLKEEYPMPLALPPLVPLEAARDKEQALNLMRLPTPPTSATMEPSSLGHATPHHLFQSGAMATPTPALLNLSMHGNGGELPAATPLPAVSDEAALNYKLHAPLTPQTPPRLADIPVSGSTQLLPQMQDVNIQTDTPVCSEDESFPGSAKPQDPAAEAFPPPTHVQPLELTKPSEASHTQPTECHTQTEPSDIPSASQEESAEQTPPEPIETMTQATQADQTSPEDLTGLELLSNISTNSKPLVRVKQEPVEHIEQPAPQPQPVNIMPSEPTLPMPPMLEMEPTSEREPLGGLKLLCALAEQRIQEEVVQGSSLFATPSSRTPTPTSLALGTTAATPPIFEAKSCYAFGQSQGSVFPSSTSSFQMPLSSPGFPSMQGIELPTTSAGIVAELTPVKRKKHKHSKSSGSDSRKSARCSKKSKKKRHHSSSRQQFSAPAEEDLDLQDDQLQSELRNALHAVDPSYAQRFGQEVFSIMDNSMRMRLAKITRQYRKKKRKLDEISKHKKKKKCSKQQLELQQQQASQQAVQPSSALQQPQMTLSSVLGTSSPLRDYKFPKFSSSNLQASSFLRFPDKTHSFPPPPSLQQSQPEPNPLPSSSSPSTSSFVRLEPSALDAAVAIAPTTSSTSTSGSPSTKQVASARKQRKMKASTVGAAGEQTAATEAKRRFSAIDRELQLTSEHLYRDETRVLTDMGGLFYAGVMKPLRPPDVYSITLDGERGNKSHVMSREDILKDTILEVAPKSVESVPVGTRLCAYWSQQYRCLYPGRAIDSEQVVDGTASSATNAATTAPDFVSVEFDDGDSGRIRLQNIRMLLSDYPIAEYNDNPLYSVGKQKRSALRGGESGPGGVTQDHLTVPGCEDSHSHHSLGMSSDNTTSLAATMELFTQRSEKKRLKKSLKKMSKAQNGVSPATATNGGADAAALGDGVSAEDAARKHHKHKKRKKHKKHHRKNGSEEQEQQVVQQDYSAAGQEATEAPSTEMSSATSSRVKVEVKVKTEQLEMEEEESASNLMSEISDEAKGDDLVEHNNSKGSSKIAAFLPERQLWGWYGTAYRKAGVKGRARKQFYKTIKRGKETITVGDSAVFLSTGRPDRPYIGRIESMWETTTGNKVVRVAWFYHPEETTGCPKLKFPGALFESPHEDENDVQTISHRCEVLQFGSYFEKFGADSKQYQSIYDNNDTYYLAGHYNPRLQVLKLQDDIPTLEELQDTNTTTTTTETTTED
|
Functions in the determination of disk-specific identity, downstream of Hox genes. Overexpression induces ectopic wings with antero-posterior and dorso-ventral axes in the eye field. Overexpression is sufficient for ectopic expression of vg in eye disks.
|
Q3LHL9
|
Q5L3H7
|
UPPP_GEOKA
|
Undecaprenyl pyrophosphate phosphatase
|
Geobacillus thermoleovorans group
|
MHWMELWKAIILGMVEGLTEFAPVSSTGHMIMVDDLWLKSTEFLGKYAANTFKVVIQLGSILAAVVVFKDRFLDLLGVRGRHPGGHPRLNLIHVIIGLLPAGVLGVLFEDYIDEHLFSTKTVLIGLVLGALLMIAADKFAKKAARTQTVDQITYKQAFFVGLMQCLSLWPGFSRSGSTISGGVLVGMSHRAAADFTFIMAVPIMAGASGLSLLKNWQYVTAADIPFFIAGFFSAFVFALLAIRFFLELINRIRLVPFAVYRIVLAVVIYFLYF
|
Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
|
Q5L3H7
|
Q1AUH8
|
TPIS_RUBXD
|
Triose-phosphate isomerase
|
Rubrobacter
|
MAGERRPLMAANWKMNKTVREAQDYMAALLPRVADLAGEVDVAVFAPFTCLSEVARMAEGSGVLAGAQNFFYEDSGAYTGEVSAPMLLDVGARASIVGHSERRELFCETDESVARKARRAVEAGLLPVVCVGETEEERDAGRMWEKVSGQVRAVVEGLGDASGGRVVFAYEPIWAIGTGKTASPEDAQDAIGRIRGLLRELRGEGFAEEARLLYGGSIKPENISEIMAQKDVDGGLVGGASLEVGSFLQLVEAARG
|
Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
|
Q1AUH8
|
A8MK92
|
THIE_ALKOO
|
Thiamine-phosphate pyrophosphorylase
|
Alkaliphilus
|
MKYNHTVDYGLYLVSDRDVLKGRDFIKSLEEAILGGATIVQLREKEASSLEFYQLALKAKALTEKYNVPLIINDRVDIALAVDADGVHVGQSDLPAHIVRSMIGQNKILGVSTATLEESKKAAEDGADYIGVGALFPTGTKTDANPVTLDQLRYIKENMDIPVVGIGGICEDNIKTIMEVGIDGVAIVSAILGKENIKEAAESLKASIK
|
Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
|
A8MK92
|
G5CV46
|
TPS31_SOLLC
|
Viridiflorene synthase TPS31
|
Solanum subgen. Lycopersicon
|
MAPAAALMSKCQEEEEIVRPVADFSPSLWGDRFHSFSLDNQVAEKYVEEIETLKEQTRSMLMSGKTLAEKLNLIDIVERLGIAYHFEKQIDDMLNHIFNIDPNFEAHEYNDLCTLSLQFRILRQHGYYISPKIFSRFQDANGKFKESLCDDIRGILNLYEASHVRTHGEDTLEEALAFSTAHLESAAPHLKSPLSKQVTHALEQSLHKSIPRVETRYFISIYEEEELKNDVFLRFAKLDFNLLQMLHKQELSEVSRWWKDLDFVTTLPYARDRAVECYFWTMGVYAEPQYSQARVMLAKTIAMISIVDDTFDAYGIVKELEVYTDAIQRWDVSQIDRLPEYMKISYKALLDLYNDYETELSNDGRSDVVQYAKERMKEIVRNYFVEAKWFIEGYMPPVSEYLSNALATSTYYLLTTTSYLGMKSATKKDFEWLAKNPKILEANVTLCRVIDDIATYEVEKGRGQIATGIECYMRDYGVSTQVAMDKFQEMAETAWKDVNEGILRPTPVSAKILTRILNLARIIDVTYKHNQDGYTHPEKVLKPHIIALLVDSIEI
|
Sesquiterpene synthase involved in the production of viridiflorene from (E,E)-farnesyl diphosphate (FPP) . Has no activity with (Z,Z)-FPP . Can act with a low efficiency as a monoterpene synthase with geranyl diphosphate as substrate .
|
G5CV46
|
P35723
|
YET1_YEAST
|
Endoplasmic reticulum transmembrane protein 1
|
Saccharomyces
|
MSLYFTTLFLLLTVEMVMLFIFVLPLPFRIRRGIFSTYNQLTAKQQIKTIIFITGCLVGLLFIDSWKRSQIRVSLYHNDNSGSIGSSAVTPIQALASRAYNQRNMYISGFILYFSICIPTVMSIVKRLVKYQGLINEQEKQKLNKPSSNSKKDSNEADSTKLQEELRKKQISLEGLQKQVKNLEKYFDEKNQPGNVAAAEASKKGN
|
May play a role in anterograde transport of membrane proteins from the endoplasmic reticulum to the Golgi.
|
P35723
|
Q9TS87
|
TAGL_BOVIN
|
Smooth muscle protein 22-alpha
|
Bos
|
MANKGPSYGMSREVQSKIEKKYDEELEERLVEWIVMQCGPDVGRPDRGRLGFQVWLKNGVILSKLVNSLYPDGSKPVKVPENPPSMVFKQMEQVAQFLKAAEDYGVTKTDMFQTVDLFEGKDLAAVQRTLMALGSLAVTKNDGHYRGDPNWFMKKAQEHKREFTESQLQEGKHVIGLQMGSNRGASQAGMTGYGRPRQIIS
|
Actin cross-linking/gelling protein.
|
Q9TS87
|
B7GP48
|
TILS_BIFLS
|
tRNA(Ile)-lysidine synthetase
|
Bifidobacterium
|
MAYSARLRKAVGAVRATLSAVELCDVQAPEFAQHGDHAVAADAPLVLVACSGGRDSMALAAVSHIVCTSMGVRCGAVIVDHGLQEGSEQVAGEAANRCRALGLGPVIVRNATVQARGEGLEAAARQARYNELCAAARESGAIAVLLAHTMDDQAETVLIGLLRSRGVDALAGMPQVFTRSGVTFARPLLTLTRAETTGICEDLGVEYWDDPTNGDAVDGELPNDYPLRSRVRHDLLPAIERFAGFNVARHFAESARLARMDKEYLDQRSDEVMGEAVTTVDWPASSAAVSTDTPRACAAGDTNDSSHGVGLMISVRRIAREPEAIRLRVIAHALSQAGVNASAAQIAAIDRLVVDWHGQGGVSLPRGYSANRKKHVIRVCQDGAHANR
|
Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
|
B7GP48
|
Q27987
|
TSHR_BOVIN
|
Thyroid-stimulating hormone receptor
|
Bos
|
MRPTPLLRLALFLVLPSSLGGERCPSPPCECRQEDDFRVTCKDIQSIPSLPPSTQTLKFIETHLKTIPSRAFSNLPNISRIYLSIDATLQQLESHSFYNLSKVTHIEIRNTRSLTYIDSGALKELPLLKFLGIFNTGLRVFPDLTKIYSTDVFFILEITDNPYMTSIPANAFQGLCNETLTLKLYNNGFTSIQGHAFNGTKLDAVYLNKNKYLTVIGQDAFAGVYSGPTLLDISYTSVTALPSKGLEHLKELIARNTWTLRKLPLSLSFLHLTRADLSYPSHCCAFKNQKKIRGILQSLMCNESSIRGLRQRKSASALNGPFYQEYEDLGDGSAGYKENSKFQDTQSNSHYYVFFEEQEDEIIGFGQQLKNPQEETLQAFDSHYDYTVCGGSEDMVCTPKSDEFNPCEDIMGYKFLRIVVWFVSLLALLGNVFVLVILLTSHYKLTVPRFLMCNLAFADFCMGLYLLLIASVDLYTQSEYYNHAIDWQTGPGCNTAGFFTVFASELSVYTLTVITLERWHAITFAMRLDRKIRLWHAYVIMLGGWVCCFLLALLPLVGISSYAKVSICLPMDTETPLALAYIILVLLLNIIAFIIVCACYVKIYITVRNPHYNPGDKDTRIAKRMAVLIFTDFMCMAPISFYALSALMNKPLITVTNSKILLVLFYPLNSCANPFLYAIFTKAFQRDVFMLLSKFGICKRQAQAYRGQRVSPKNSTGIRVQKVPPDVRQSLPNVQDDYELLENSHLTPKQQDQTSKEYKRTVL
|
Receptor for the thyroid-stimulating hormone (TSH) or thyrotropin. Also acts as a receptor for the heterodimeric glycoprotein hormone (GPHA2:GPHB5) or thyrostimulin. The activity of this receptor is mediated by G proteins which activate adenylate cyclase. Plays a central role in controlling thyroid cell metabolism.
|
Q27987
|
Q9NP84
|
TNR12_HUMAN
|
Tweak-receptor
|
Homo
|
MARGSLRRLLRLLVLGLWLALLRSVAGEQAPGTAPCSRGSSWSADLDKCMDCASCRARPHSDFCLGCAAAPPAPFRLLWPILGGALSLTFVLGLLSGFLVWRRCRRREKFTTPIEETGGEGCPAVALIQ
|
Receptor for TNFSF12/TWEAK. Weak inducer of apoptosis in some cell types. Promotes angiogenesis and the proliferation of endothelial cells. May modulate cellular adhesion to matrix proteins.
|
Q9NP84
|
Q3IRZ2
|
URED_NATPD
|
Urease accessory protein UreD
|
Natronomonas
|
MSAVPDAFQRYGAESLAQAPAFGPGKDGVFEATLARTGDRDTRLLRDYTKVPYHLTGTLDTDPAPGLTTLCLQEPTGGVAQGDRHSITVTAREGARARVTTQSATKVHSMQANYAHLDATLEAGPDAHLEYVPGPTIVNEDARCLQTVAVDLAPSATVVVADVFVPGGLSAHEPFDFDHYHSRLEARCEERLVCADAVDLHPADGDPRDPATVADYDVVGTLYVLAPEADTEVLAEAIHARFDAHDAVTAGVSALPYESGVSVRVLGTRSADVTDAVRDAWDASRQELLGVGIPADRRY
|
Required for maturation of urease via the functional incorporation of the urease nickel metallocenter.
|
Q3IRZ2
|
B1LQ65
|
TRUD_ECOSM
|
tRNA-uridine isomerase D
|
Escherichia
|
MIEFDNLTYLHGKPQGTGLLKANPEDFVVVEDLGFEPDGEGEHILVRILKNGCNTRFVADALAKFLKIHAREVSFAGQKDKHAVTEQWLCARVPGKEMPDLSAFQLEGCQVLEYARHKRKLRLGALKGNAFTLVLREVSNRDDVEQRLIDICVKGVPNYFGAQRFGIGGSNLQGALRWAQTNTPVRDRNKRSFWLSAARSALFNQIVAERLKKADVNQVVDGDALQLAGRGSWFVATTEEVAELQRRVNDKELMITAALPGSGEWGTQREALAFEQAAVAAETELQALLVREKVEAARRAMLLYPQQLSWNWWDDVTVEIRFWLPAGSFATSVVRELINTTGDYAHIAE
|
Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs.
|
B1LQ65
|
Q9I750
|
TSSA1_PSEAE
|
Type VI secretion system component TssA1
|
Pseudomonas
|
MLDVPVLLAAVSPDSPCGDDLEYDAAFLELERIAQGQPERQMGDAVLPAEPPEWPRVRALASELFGRSKDLRVANLLLQSNVALDGLDGLADGLLLVRELLGQYWDGVYPLLDADDDNDPTFRINALTGLVAEPLLQLVWAIPLVRSRAFGPVNLRAALNAAGLQRFASETLSPEQIAGAFADADADALAATRRALDGAQEHALAIESGVAERVGSAQGLDLGPLRQLLRQALQVFDLYGPQGAGESLAPGAEAVADEQVGAAPVAAVAAPAPRASGEIANREDVLRQLDRLLEYYVRHEPSSPVPVLLKRAKTLVTADFAEIVRNLIPDGISQFETLRGPESE
|
Core component of the H1 type VI (H1-T6SS) secretion system that plays a role in the release of toxins targeting both eukaryotic and prokaryotic species. Forms a dodecameric ring-shaped structure located at one end of the T6SS sheath. May properly attach the pre-assembled sheath onto the baseplate and/or stabilize the sheaths tubular structure.
|
Q9I750
|
Q5DP50
|
TEX24_MOUSE
|
Testis-specific factor 1
|
Mus
|
MGSQSLNSTFLKVRRLSLISSNERLLGQTSGLATGSRLVTQEVDDLRVIPGSRPDLDDHQPQCSLAELPSTAHGKRKPGHLPRLRSSAVKGHAPDPNPSLSIVSKRIFKGESVIKGPEDRQTFVGPSGLPKISPKATAGEAQGKKRTMELLNKARKQEEKVSNLLDIRQLPKQEVFINNTHPCKKHLKQQPMSLEEWRRGHLGGDNTGLISQEPFRCCKRLGKKAQCQLLEVTSLEAEASLEVLKRRRRMQAMEMSKKPQDRGLGQEKAVFLSREKVKPSSHDMHLSTAERSFKPKSMPKAEDWDLSVQGTPVVLTVRDHSNVSQAQKHLGCAEIFHSRDGRCTLLKRGGA
|
Nuclear factor which might have a role in spermatogenesis.
|
Q5DP50
|
Q5P6J5
|
THIE_AROAE
|
Thiamine-phosphate pyrophosphorylase
|
Aromatoleum
|
MPDTRLRGLYLITPDSPDTTTLVAQVERALRGQPALLQYRSKQRDAALRLGQARQIAALCREAGVPFIVNDSLELALATDADGVHLGREDGDLDAARRALGPGRILGVTCYNEWPRAVAGCAAGADYVAFGAVFPSATKPAAVRAPLELFVRGRRELDVPLAAIGGITLDNAAQVIAAGASLLAVVSDVFDAPDPGARAAAYRTLFDA
|
Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
|
Q5P6J5
|
Q9JLT2
|
TREA_MOUSE
|
Alpha,alpha-trehalose glucohydrolase
|
Mus
|
MTWELHLLLLLGLGLRSQEALPPPCESQIYCHGELLHQVQMAQLYQDDKQFVDMSLATSPDEVLQKFSELATVHNHSIPKEQLQEFVQSHFQPVGQELQSWTPEDWKDSPQFLQKISDANLRVWAEELHKIWKKLGKKMKAEVLSYPERSSLIYSKHPFIVPGGRFVEFYYWDSYWVMEGLLLSEMASTVKGMLQNFLDLVKTYGHIPNGGRIYYLQRSQPPLLTLMMDRYVAHTKDVAFLQENIGTLASELDFWTVNRTVSVVSGGQSYVLNRYYVPYGGPRPESYRKDAELANSVPEGDRETLWAELKAGAESGWDFSSRWLVGGPDPDLLSSIRTSKMVPADLNAFLCQAEELMSNFYSRLGNDTEATKYRNLRAQRLAAMEAVLWDEQKGAWFDYDLEKGKKNLEFYPSNLSPLWAGCFSDPSVADKALKYLEDSKILTYQYGIPTSLRNTGQQWDFPNAWAPLQDLVIRGLAKSASPRTQEVAFQLAQNWIKTNFKVYSQKSAMFEKYDISNGGHPGGGGEYEVQEGFGWTNGLALMLLDRYGDQLTSGTQLASLGPHCLVAALLLSLLLQ
|
Intestinal trehalase is probably involved in the hydrolysis of ingested trehalose.
|
Q9JLT2
|
D7PI00
|
VRTR1_PENAE
|
Viridicatumtoxin synthesis protein R1
|
Penicillium
|
MEDTTETTETTDTTAVSRLVPLAPAPARAPSMDAVNGSFDSELTTARRFNCQSCVRKKIKCNRAVPTCASCSKAKLHCVYQSRPPRKRKRSRGEEDVYERLAQYERILHDHNLLQAAAASTPSGRDTETSAISTRAPTPVLPDAQTHTKAGKVLLSTDGRSRYIDNVLLLDAGEGDLCELPESEQEDYNHDETSPDESTPTGLLGALAAHTISGAIIGNTQSLTNLHPTYEQAAKLWQAYVKNVEPLCKILHVPTVAKMFDTVSKQPAAVSKNDECLMFVIYYFAVFSMSDDECLHEFNYPRAQLLSRYQTTVIQALVNASWLKTTAMPVLQAYTLFLIALRTQIDSHTFWILTGIAVRLAQRMGLHRDGESLGLPPFEVQMRRRLFWQLLPLDSYAGQTSGTGISISPSSWDTKQPLNINDDQIFPGMTQPPCEQRGASEMIFCLSRMELSNFYIRTGVKLKEHGDTIQFRDAEDIERLIDEVEDLIETKFLRYCDILNPLHFLTTGIVRSAIDAVRLRARMPLLKQQTITDAQRRRLCALAEKVLDTNSTIFSNPSTQNFRWQMQAFFLWDALLCILRNIAEVGFYSPSELAAAWSKVANVYANHDELVKARRTLYVTIAKVTLKAWLANPPRDSSPQPAFITALLTQHEPKGINQQQNSVLSDDKAADGASLFDEFFDNMNGTDLDINNAFNLDSSSDWLFWDQICRGTSLS
|
Probable transcription factor that regulates expression of the gene cluster that mediates the biosynthesis of viridicatumtoxin, a tetracycline-like fungal meroterpenoid with a unique, fused spirobicyclic ring system .
|
D7PI00
|
B4RE94
|
YIDD_PHEZH
|
Putative membrane protein insertion efficiency factor
|
Phenylobacterium
|
MNLYESCVRGALRAYKLTLSPLIGRQCRFFPTCSEYAAEALIGHGPVRGSWLTVRRLCRCHPWGPSGWDPPPPPRRKGAKWTCET
|
Could be involved in insertion of integral membrane proteins into the membrane.
|
B4RE94
|
Q15629
|
TRAM1_HUMAN
|
Translocating chain-associated membrane protein 1
|
Homo
|
MAIRKKSTKSPPVLSHEFVLQNHADIVSCVAMVFLLGLMFEITAKASIIFVTLQYNVTLPATEEQATESVSLYYYGIKDLATVFFYMLVAIIIHAVIQEYMLDKINRRMHFSKTKHSKFNESGQLSAFYLFACVWGTFILISENYISDPTILWRAYPHNLMTFQMKFFYISQLAYWLHAFPELYFQKTKKEDIPRQLVYIGLYLFHIAGAYLLNLNHLGLVLLVLHYFVEFLFHISRLFYFSNEKYQKGFSLWAVLFVLGRLLTLILSVLTVGFGLARAENQKLDFSTGNFNVLAVRIAVLASICVTQAFMMWKFINFQLRRWREHSAFQAPAVKKKPTVTKGRSSKKGTENGVNGTLTSNVADSPRNKKEKSS
|
(Microbial infection) In case of cytomegalovirus infection, participates in US2- and US11-mediated ER-to-cytosol retrotranslocation and subsequent degradation of major histocompatibility complex (MHC) class I heavy chains, thereby decreasing the immune detection by cytotoxic T-cells.
|
Q15629
|
B8D9V4
|
TUSC_BUCA5
|
tRNA 2-thiouridine synthesizing protein C
|
Buchnera
|
MKMVAFVFSHAPHGISLGREGLDAIFSISLIFKKISVFFIGDGVLQLIKNQQPEHILARNYTSSFSILSLYNIKDLYCCKASLLERGLNNNNNFILNIDVLDSYNLRLKLDNYDAIINF
|
Part of a sulfur-relay system required for 2-thiolation of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at tRNA wobble positions.
|
B8D9V4
|
A3N3S3
|
TATA_ACTP2
|
Sec-independent protein translocase protein TatA
|
Actinobacillus
|
MGGISIWQLLIIVAIIVLLFGTKKLRTLGTDLGESVKGFKKAMADDKSQPQDASFEKVEAKEAASTEQKAKEKEQA
|
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.
|
A3N3S3
|
Q14AK4
|
ZDH11_MOUSE
|
Zinc finger DHHC domain-containing protein 11
|
Mus
|
MKEMNICGINKNWVLPEAQENNVKKFLPRPLSRVNGWSPPLHSFQAISWITYLAMSIVTFGIFIPFLPYSWKYAANIVMGGVFIFHLIVHLIAITIDPADTNVRLKKDYTQPVPAFDRSKHTHVIQNQYCHLCEVTASKKAKHCSACNKCVSGFDHHCKWLNNCVGRRNYWFFFWSVASAAVGILGVMIILCYICIQYFVNPDELRTDPLYKEIISENTWLLFLSLWPVPVKTPIVLSIAVMALLLAIASFVMLGHLLIFHLYLITKNMSTFDYLMKTRFKKNLHPAEEKELPLQKKGDLPQEKSDNWAWPKSPPRVGSQKFPVSTLSPKSSVCFVASPPKICHSED
|
Has also a palmitoyltransferase activity-independent function in DNA virus-triggered and CGAS-mediated innate immune response . Functions as an adapter that recruits IRF3 to STING1 to promote the activation of that key transcriptional regulator of type I interferon (IFN)-dependent immune response .
|
Q14AK4
|
P12458
|
TBB2_PHYPO
|
Tubulin beta-major chain
|
Physarum
|
MREIVHVQVGQCGNQVGAKFWEVVSEEHGIDSAGTYKGDTDLQLERINVYYNEVAGSKYVPRAVLVDLEPGVLDSIRASSIGSMFRPDNFTHAQSGAGNNWAKGHYTEGAELVESVVDVVRKEAENCDCLQGFQICHSLGGGTGSGLGTLLISKIREEFPDRMMCTFSVMPSPKVSDTVVEPYNATLSIHQLVENADEVMCIDNEALYDICFRTLKLTTPTYGDLNHLVSGVMSGITACLRFPGQLNSDLRKLAVNLIPFPRLHFFLIGYAPLTARSAMGFRALTVPELTQQIFDSRNMMAASDPRHGRYLTASATFRGKMSTKEVDEQMHAVQTKNSSFFVEWIPNNIKSSVCDIPPKGMKMSATFIGNNTCIQELFKRIGLQFSAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQEASVDDEAMEDDAEAEGGAGQNEAVEEF
|
This is the major beta tubulin of mitotic spindle.
|
P12458
|
Q5WH87
|
THIE_ALKCK
|
Thiamine-phosphate pyrophosphorylase
|
Alkalihalobacillus
|
MKPFRLYAITGEEFHPGRDVVEVMEEAIQGGVDIIQLRDKTSSKKAVLEKARRLKKLAADYGIPFIVNDHIDVALAVDASGVHVGQDDLPLPEVRKLLGPDKIIGVSTHKLEEALEAEKNGADYIGVGPIFPTNSKADVVDPVTTAYIREVKEHVTIPFVAIGGIKRHNVREVIEAGAEAICVITEIVAARDVKAASQALLAAMEEASQ
|
Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
|
Q5WH87
|
P27156
|
XYLB_STRRU
|
Xylulose kinase
|
Streptomyces pseudogriseolus group
|
MSAAEGPLVVGVDTSTQSTKALVVDVATGRVVASGQAPHTVTSGAGRESDPRQWWDALCEALRQCGEAAHEAAAVSIGGQQHGLVTLDGHGEPVRPALLWNDVRSAPQGHRLIEELGGAKFWAERTGSVPAASFTVTKWAWLAEHEPEAVRATRAVRLPHDYLTERLTGQGTTDRGDASGTGWWASGTEAYDEEILGHVGLDPALLPRVVRPGEVAGTVRDSHELPFSKGTLVACGTGDNAAAALGLGVRPGTPVMSLGTSGTVYAVTQRRPADPTGTVAGFADARGDWLPLACTLNCTLAVDRVAALLGLDREAVEPGHGVTLLPFLDGERTPNLPRSSGLLHGLRHDTTGGQLLQAAYDGAVYSLLAALDLVLDEDADPSAPLLLIGGGARGTAWQQTVRRLSGRAVQVPRAAELVALGAAAQAAGLLTGEDPAAVARRWETAAGPVLEAVERDEETLDRLAGVLSDAAPLLERGTGAG
|
Catalyzes the phosphorylation of D-xylulose to D-xylulose 5-phosphate.
|
P27156
|
A7ZIN1
|
YBAB_ECO24
|
Nucleoid-associated protein YbaB
|
Escherichia
|
MFGKGGLGNLMKQAQQMQEKMQKMQEEIAQLEVIGESGAGLVKVTINGAHNCRRVEIDPSLLEDDKEMLEDLVAAAFNDAARRIEETQKEKMASVSSGMQLPPGFKMPF
|
Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection.
|
A7ZIN1
|
Q2T7H3
|
TRUA_BURTA
|
tRNA-uridine isomerase I
|
pseudomallei group
|
MRIALGIQYDGAAFCGWQSQPHGKTVQDALERALAEFAQTSLHTTVAGRTDTGVHGLGQVVHFDTDLDRADFSWVRGTNAFLPSTVAVQWAKPMPDTFHARFAAFERTYYYALYVHPVRSPMLAARAGWVHTPLDVDAMREAAEHLVGEHDFSAFRSSECQAKSPVKHLYQIGIRPDGDFIHFRFRANAFLHHMVRNLMGCLVAVGRGRYPASWLAEVLESRDRGCAAPTFMPEGLYLAHVGYPAEFAVPPAQLGSVPWSSVWADLDGRP
|
Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
|
Q2T7H3
|
Q8XXC7
|
UPP_RALSO
|
UPRTase
|
Ralstonia
|
MTQDPRFPNLFILNHPLIQHKLTHMRDKDTSTRTFRELLREITLLMGYEITRNLPLTTRHIETPMGPMDAPVIAGRKLAVVPVLRAGVGMSDGLLELIPSARVGHIGVYRDEQHRPVEYLVRLPDLEERTFILCDPMVATGHSAVHAVDVMKQRGVPDEHILFLALVAAPEGVEVFQQAHPGVKLYVASLDSHLNEHAYIIPGLGDAGDRLFGTKN
|
Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
|
Q8XXC7
|
A6TTD6
|
XPT_ALKMQ
|
Xanthine phosphoribosyltransferase
|
Alkaliphilus
|
MELLKEQIREVARVEKGNVLKVDSFLNHQLDIPLLNEIGKELKKRFQGEKVDKILTAEVSGIAIAAIAAQYFNVPVVFAKKTQSKNLDQDTYEGEVYSYTKGQAYKIRVSKRYLHEKENILIIDDFLANGEALQGLREIVVQANANLVGAGIVIEKGFQGGGKRLRAENMRIESLAIIDEMNESTLVFRDDKADLKADPKAS
|
Converts the preformed base xanthine, a product of nucleic acid breakdown, to xanthosine 5'-monophosphate (XMP), so it can be reused for RNA or DNA synthesis.
|
A6TTD6
|
B9JEG8
|
TATA_AGRRK
| null |
Agrobacterium tumefaciens complex
|
MGSLSIWHWLIVLAIALLLFGRGKIPELMGDVAKGIKSFKKGMNDDEETPPPAQSTTSRTVEHKADESK
|
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.
|
B9JEG8
|
Q5KVB5
|
UVRB_GEOKA
|
Excinuclease ABC subunit B
|
Geobacillus thermoleovorans group
|
MEGRFQLVAPYEPQGDQPQAIAKLVDGLRRGVKHQTLLGATGTGKTFTISNVIAQVNKPTLVIAHNKTLAGQLYSELKEFFPHNAVEYFVSYYDYYQPEAYVPQTDTYIEKDAKINDEIDKLRHSATSALFERRDVIIVASVSCIYGLGSPEEYRELVVSLRVGMEIERNALLRRLVDIQYDRNDIDFRRGTFRVRGDVVEIFPASRDEHCIRVEFFGDEIERIREVDALTGEVLGEREHVAIFPASHFVTREEKMRLAIQNIEQELEERLAELRAQGKLLEAQRLEQRTRYDLEMMREMGFCSGIENYSRHLALRPPGSTPYTLLDYFPDDFLIIVDESHVTLPQLRGMYNGDRARKQVLVDHGFRLPSALDNRPLTFEEFEQKINQIIYVSATPGPYELEHSPGVVEQIIRPTGLLDPTIDVRPTKGQIDDLIGEIRERVERNERTLVTTLTKKMAEDLTDYLKEAGIKVAYLHSEIKTLERIEIIRDLRLGKYDVLVGINLLREGLDIPEVSLVAILDADKEGFLRSERSLIQTIGRAARNANGHVIMYADTITKSMEVAIQETKRRRAIQEEYNRKHGIVPRTVKKEIRDVIRATYAAEETEMYEAKPAAAMTKQEREELIRTLEAEMKEAAKALDFERAAQLRDIIFELKAEG
|
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage.
|
Q5KVB5
|
O20030
|
YCF4_CHLRE
|
Photosystem I assembly protein Ycf4
|
Chlamydomonas
|
MTQNNILIRRYIIVGERRFSNYWWAIVIFLGSCGFLATGICSYLGIPNWLSLLNIGTTFSSETETLASGIVPFFPQGLLMSFYGSLGFLLSIYWSLLIFWNVGGGFNEFNKKEGFVRIFRWGYPGKNRKIDLSYSLKDIEAIRVELKQGLDAQRTIYLRLKGKREIPLTGIGQPLTLKEIEKQASELANFLQVSLEA
|
Seems to be required for the assembly of the photosystem I complex.
|
O20030
|
Q8Z3H9
|
TRUB_SALTI
|
tRNA-uridine isomerase
|
Salmonella
|
MSRPRRRGRDIHGVLLLDKPQGMSSNDVLQKVKRIYNANRAGHTGALDPLATGMLPICLGEATKFSQYLLDSDKRYRVIARLGQRTDTSDADGQIVQERPVTFSAEQLASALETFRGDIEQIPSMYSALKYQGRKLYEYARQGIEVPREARPITVYELLFIRHEGNELELEVHCSKGTYIRTIIDDLGEKLGCGAHVTYLRRLTVSKYPVDRMVTLEHLQTLVAQAEQQGVPAAQLLDPLLMPMDSPASDYPVVNLPLTSSVYFKNGNPVRTTGAPLKGLVRVTEGEDDKFIGMGEIDDEGRVAPRRLVVEYPA
|
Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
|
Q8Z3H9
|
Q9BGN4
|
TSHR_FELCA
|
Thyroid-stimulating hormone receptor
|
Felis
|
MRQTPLLQLALLLSLPRSLGGKGCPSPPCECHQEDDFRVTCKDIHRIPSLPPSTQTLKFIETHLKTIPSRAFSNLPNISRIYLSIDATLQRLESHSFYNLSKMTHIEIRNTRSLTYIDPGALKELPLLKFLGIFNTGLGVFPDLTKVYSTDVFFILEITDNPYMTSIPANAFQGLCNETLTLKLYNNGFTSIQGHAFNGTKLDAVYLNKNKYLTAIDQDAFGGVYSGPTLLDVSYTSVTALPSKGLEHLKELIARNTWTLKKLPLTLSFLHLTRADLSYPSHCCAFKNQKKIRGILESFMCNDSSIRSLRQRKSVNALNGPFDQEYEEYLGDSHAGYKDNSKFQDTRSNSHYYVFFEEQDEILGFGQELKNPQEETLQAFDSHYDYTVCGGNEDMVCTPKSDEFNPCEDIMGYKFLRIVVWFVSLLALLGNVFVLIILLTSHYKLTVPRFLMCNLAFADFCMGMYLLLIASVDLYTHSEYYNHAIDWQTGPGCNAAGFFTVFASELSVYTLTVITLERWYAITFAMRLDRKMRLRHAYAIMVGGWVCCFLLALLPLVGISSYAKVSICLPMDTETPLALAYIILVLLLNIVAFIIVCSCYVKIYITVRNPQYNTGDKDTKIAKRMAVLIFTDFMCMAPISFYALSALMNKPLITVTNSKILLVLFYPLNSCANPFLYAIFTKTFQRDVFILLSKFGICKRQAQAYRGQRVSPKNSTGIQVQKVTRNMRQSLPNMQDDYELLENSHLTPNKQSHISKEYNQTVL
|
Receptor for the thyroid-stimulating hormone (TSH) or thyrotropin. Also acts as a receptor for the heterodimeric glycoprotein hormone (GPHA2:GPHB5) or thyrostimulin. The activity of this receptor is mediated by G proteins which activate adenylate cyclase. Plays a central role in controlling thyroid cell metabolism.
|
Q9BGN4
|
P27679
|
TRI5_GIBPU
|
Sesquiterpene cyclase
|
Fusarium
|
MENFPTEYFLNTSVRLLEYIRYRDSNYTREERIENLHYAYNKAAHHFAQPRQQQLLKVDPKRLQASLQTIVGMVVYSWAKVSKECMADLSIHYTYTLVLDDSSDDPYPAMMNYFNDLQAGREQAHPWWALVNEHFPNVLRHFGPFCSLNLIRSTLDFFEGCWIEQYNFGGFPGSHDYPQFLRRMNGLGHCVGASLWPKEQFDERGLFLEITSAIAQMENWMVWVNDLMSFYKEFDDERDQISLVKNYVVSDEITLHEALEKLTQDTLHSSKQMVAVFSEKDPQVMDTIECFMHGYVTWHLCDHRYRLNEIYEKVKGQKTEDAEKFCKFYEQAANVGAVSPSEWAYPPIAQLANIRTKDVKDLKDVKDLKEIQKPLLSSIELVE
|
TS is a member of the terpene cyclase group of enzymes. It catalyzes the isomerization and cyclization of farnesyl pyro-phosphate to form trichodiene, the first cyclic intermediate in the biosynthetic pathway for trichothecenes. It serves to branch trichothecene biosynthesis from the isoprenoid pathway.
|
P27679
|
Q39PQ8
|
YIDC_GEOMG
|
Membrane protein YidC
|
Geobacter
|
MEKRALIAVILSIVFFYGYSALFPPPKKEAPAPSAQQAVTGSQPGAPQASVAAVPAPSPVPAAAVKAQQKEIAVETPDYTAVFSTQGGSLTRLVLKKYRETADLTGKHVTLVDERDPSAYTLSTRAAGIGLDPSALFVSSADSLTVEAGEEKKELAFTWISPAGVTVRKIYTFQGGNYGIDMVYQTANSGTARVGAAFQTVMTYPAVPRVKESRLETFGPVTFAQDKLTEEKVKDLVGQGKSYSAPLWSGFADKYFLSAVVGQGGSIATAAVRSTPRGMLEDTITAPETSLNPGESKSVAYRLYFGPKDLDILKAQGNSLERAIDLGWFAMLAKPLLHSLKFFYKYVHNYGIAIIIITVILKIIFYPLTHSSYKSMKQMQKLQPKMQEVREKYKNDRDAMNKAIMELYQTHKVNPVGGCLPMLVQIPVFFALYKALMFSIELRHAPFMLWIQDLAGKDPYYVTPIIMGITMVIQQKMTPSQMDPMQQKMMMALPVVFTFMFLNFPSGLVLYWLVNNVLTIIQQSYINKSIAAAEAK
|
Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins.
|
Q39PQ8
|
P82094
|
TMF1_HUMAN
|
Androgen receptor-associated protein of 160 kDa
|
Homo
|
MSWFNASQLSSFAKQALSQAQKSIDRVLDIQEEEPSIWAETIPYGEPGISSPVSGGWDTSTWGLKSNTEPQSPPIASPKAITKPVRRTVVDESENFFSAFLSPTDVQTIQKSPVVSKPPAKSQRPEEEVKSSLHESLHIGQSRTPETTESQVKDSSLCVSGETLAAGTSSPKTEGKHEETVNKESDMKVPTVSLKVSESVIDVKTTMESISNTSTQSLTAETKDIALEPKEQKHEDRQSNTPSPPVSTFSSGTSTTSDIEVLDHESVISESSASSRQETTDSKSSLHLMQTSFQLLSASACPEYNRLDDFQKLTESCCSSDAFERIDSFSVQSLDSRSVSEINSDDELSGKGYALVPIIVNSSTPKSKTVESAEGKSEEVNETLVIPTEEAEMEESGRSATPVNCEQPDILVSSTPINEGQTVLDKVAEQCEPAESQPEALSEKEDVCKTVEFLNEKLEKREAQLLSLSKEKALLEEAFDNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKKVQLACKERDAAKKEIKNIKEELATRLNSSETADLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKVKELEEELQHLKQVLDGKEEVEKQHRENIKKLNSMVERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDLHKANAAKDSEAQEAALSREMKAKEELSAALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAARKEDYLRHEIGELQQRLQEAENRNQELSQSVSSTTRPLLRQIENLQATLGSQTSSWEKLEKNLSDRLGESQTLLAAAVERERAATEELLANKIQMSSMESQNSLLRQENSRFQAQLESEKNRLCKLEDENNRYQVELENLKDEYVRTLEETRKEKTLLNSQLEMERMKVEQERKKAIFTQETIKEKERKPFSVSSTPTMSRSSSISGVDMAGLQTSFLSQDESHDHSFGPMPISANGSNLYDAVRMGAGSSIIENLQSQLKLREGEITHLQLEIGNLEKTRSIMAEELVKLTNQNDELEEKVKEIPKLRTQLRDLDQRYNTILQMYGEKAEEAEELRLDLEDVKNMYKTQIDELLRQSLS
|
Potential coactivator of the androgen receptor. Mediates STAT3 degradation. May play critical roles in two RAB6-dependent retrograde transport processes: one from endosomes to the Golgi and the other from the Golgi to the ER. This protein binds the HIV-1 TATA element and inhibits transcriptional activation by the TATA-binding protein (TBP).
|
P82094
|
Q328K4
|
ULAA_SHIDS
| null |
Shigella
|
MEILYNIFTVFFNQVMTNAPLLLGIVTCLGYILLRKSVSVIIKGTIKTIIGFMLLQAGSGILTSTFKPVVAKMSEVYGINGAISDNYASMMATIDRMGDAYSWVGYAVLLALALNICYVLLRRITGIRTIMLTGHIMFQQAGLIAVTLFIFGYSMWTTIICTAILVSLYWGITSNMMYKPTQEVTDGCGFSIGHQQQFASWIAYKVAPFLGKKEESVEDLKLPGWLNIFHDNIVSTAIVMTIFFGAILLSFGIDTVQAMAGKVHWTVYILQTGFSFAVAIFIITQGVRMFVAELSEAFNGISQRLIPGAVLAIDCAAIYSFAPNAVVWGFMWGTIGQLIAVGILVACGSSILIIPGFIPMFFSNATIGVFANHFGGWRAALKICLVMGMIEIFGCVWAVKLTGMSAWMGMADWSILAPPMMQGFFSIGIAFMAVIIVIALAYMFFAGRALRAEEDAEKQLAEQSA
|
The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II UlaABC PTS system is involved in ascorbate transport.
|
Q328K4
|
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