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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
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10
A1KB60
THIE_AZOSB
Thiamine-phosphate pyrophosphorylase
Azoarcus
MGERIRGLYLVTPDAADSATLLASVERVLPARPALLQYRNKLADPLRQLDEARSLRQLCSSAGVPLIINDDVALARAVAADGVHLGRDDGSPAAARAVLGADALIGVSCYDEWVRAEDAAAAGADYVAFGAMFPSSTKPGAVRAPLTLLTRARAALDCPVAAIGGITLDNAPALIEAGADLLAVISDVFAAADPLQRALAYSALFA
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).
A1KB60
Q880X7
UVRC_PSESM
Excinuclease ABC subunit C
Pseudomonas
MTQTFDPSAFLATCSGRPGVYRMFDADATLLYVGKAKNLKKRLASYFRKTGHAPKTGALVARIAQIETTITNNETEALLLEQTLIKEWRPPYNILLRDDKSYPYVFLSDGTYPRLSIHRGAKKAKGRYFGPYPSAGAIRESLSLLQKTFQVRQCEDSFFKNRNRPCLQYQIKRCKGPCVGLVEPEVYAEDVRHSVMFLEGRSNALSDELNASMEKAAMALDFERAAELRDQVALLRRVQDQQSMDGGTGDVDVVAAFVNPGGACVHLISVRGGRVLGSKNFFPQVGIEEEVGEVMSAFLAQYFLGGVDRELPSEVIVNVVNEDFPALIDAIEESRGREMTISHRVRGTRARWQQLAVTNAEQALAARLANRQHVASRFEALAVVLNLDEPPMRLECYDISHSSGEATVASCVVFGPEGPIKSDYRRFNIEGVTAGDDYAAMHQALTRRYSRIKAGEGKLPDVLLVDGGKGQMSMARDVLNELQVPDLILLGVAKGTTRKAGFETLYLNDAAHEFTLPGDSPALHLIQQIRDEAHRFAITGHRARRGKTRRTSTLEGIAGVGPTRRRDLLKHFGGLQELSRASIDEIAKAPGISKKLAESIYANLHSE
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision.
Q880X7
P28274
URA7_YEAST
UTP--ammonia ligase 1
Saccharomyces
MKYVVVSGGVISGIGKGVLASSTGMLMKTLGLKVTSIKIDPYMNIDAGTMSPLEHGECFVLDDGGETDLDLGNYERYLGVTLTKDHNITTGKIYSHVIAKERKGDYLGKTVQIVPHLTNAIQDWIERVAKIPVDDTGMEPDVCIIELGGTVGDIESAPFVEALRQFQFKVGKENFALIHVSLVPVIHGEQKTKPTQAAIKGLRSLGLVPDMIACRCSETLDKPTIDKIAMFCHVGPEQVVNVHDVNSTYHVPLLLLEQKMIDYLHARLKLDEISLTEEEKQRGLELLSKWKATTGNFDESMETVKIALVGKYTNLKDSYLSVIKALEHSSMKCRRKLDIKWVEATDLEPEAQESNKTKFHEAWNMVSTADGILIPGGFGVRGTEGMVLAARWARENHIPFLGVCLGLQIATIEFTRSVLGRKDSHSAEFYPDIDEKNHVVVFMPEIDKETMGGSMRLGLRPTFFQNETEWSQIKKLYGDVSEVHERHRHRYEINPKMVDELENNGLIFVGKDDTGKRCEILELKNHPYYIATQYHPEYTSKVLDPSKPFLGLVAASAGILQDVIEGKYDLEAGENKFNF
Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen.
P28274
A4JCS0
UVRC_BURVG
Excinuclease ABC subunit C
Burkholderia cepacia complex
MTSPEAADTPFEPKKILAQLPHMPGVYRYYDATGAVLYVGKARDLKKRVSSYFTKTQLSPRIAMMVTRIARIETTVTRSEAEALLLENNLIKALAPRYNILFRDDKSYPYLKLTAHRFPRMAYYRGSVDKQNQYFGPFPSAWAVRESIQILQRVFQLRTCEDSVFNNRTRPCLLHQIGRCTAPCVGAITEDDYAIDVSNAARFLLGRQSEVMNELEQKMHAFAAELKFEQAAAVRNQMSSLATVLHQQAIEVGGDSDVDILAVVAQGGRVCVNLAMVRGGRHLGDKAYFPTHVESALTLAEGGLGDEADGVDDAAAAMPDQPVEGEGDGDGGAAARVAGAGAGASVEAEVLDAFISQHYLGNRVPPVLVVSHAPASRDLLELLSEQAGHKVSLVRQPQGQRRAWLTMAEQNARIALARLLSEQGSQQARTRALAETLGLECDDLATLRIECFDISHTMGEATQASCVVYHHHKMQSGEYRRYNIAGITPGDDYAAMRQVLTRRYEKMVELAAQAAAADAATGIDGESTRQAEASSLLPNIVLIDGGKGQVEIARQVFTELGLDTSMLVGVAKGEGRKVGLETLVFADGRTPLELGKESAALMLVAQIRDEAHRFAITGMRAKRAKARQTSRLEELDGVGAKRRQRLLARFGGLRGVVAASVEELASVDGISHALAEQIYKQLH
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision.
A4JCS0
C5A338
VATD_THEGJ
V-ATPase subunit D
Thermococcus
MAELLNVKPTRMELLNLKRRIQLAKKGHKLLKDKQDALIMEFFTIYDEALQLRRELNEKMGVAFETLTRAQIEAGTLPLREAALAVKPNKEVEIKRRNVMGVSVPLIEAEGFKRKASERGYAFVSTSPFVDIAAEKFEEVLDLAVRLAEVEETLKRLAREIETTKRRVNALEYIIIPRMEATVKFIKQRLDEMERENFFRLKRVKALIEARSGS
Produces ATP from ADP in the presence of a proton gradient across the membrane.
C5A338
A3CK49
VATB_STRSV
V-ATPase subunit B
Streptococcus
MSVIKEYRTVSEVVGPLMIVDQVAGVHFNELVEIQLHDGSKRQGQVLEVQEDKAMVQLFEGSSGINLEKAKVRFTGRPLELPVSEDMVGRIFNGMGKPIDGGPAILPEKYLDIDGQAINPVARDYPDEFIQTGISAIDHLNTLVRGQKLPVFSGSGLPHKELAAQIARQATVLNSDENFAVVFVAMGITFEEAEFFMNDLRETGAIDRSVLFINLANDPAIERIATPRIALTAAEYLAYEKDMHVLVIMTDMTNYCEALREVSAARREVPGRRGYPGYLYTNLSTLYERAGRLVGKKGSVTQIPILSMPEDDITHPIPDLTGYITEGQIILSRELYNSGYRPPINVLPSLSRLKDKGSGEGKTRGDHAATMNQLFAAYAQGKQAKELAVVLGESALSETDKLYVRFTDRFEQEYINQGFQTNRTIEESLDLGWELLSILPRTELKRIKDDMIDQYLPQTKEEER
Produces ATP from ADP in the presence of a proton gradient across the membrane. The V-type beta chain is a regulatory subunit.
A3CK49
P43348
TCTP_RABIT
Translationally-controlled tumor protein
Oryctolagus
MIIYRDLISHDEMFSDIYKIREIAGGLCLEVEGKMVSRTEGNIDDSLIGGNASAEGPEGEGTESTVITGVDIVMNHHLQETSFTKEAYKKYIKDYMKSIKGKLEEQRPERVKPFMTGAAEQIKHILANFKNYQFYIGENMNPDGMVALLDYREDGVTPFMIFFKDGLEMEKC
Involved in calcium binding and microtubule stabilization.
P43348
O59490
XERA_PYRHO
Tyrosine recombinase XerA
Pyrococcus
MKEREEIVNSDILEEFATYLELEGKSKNTIRMYTYYLSKFFEEGYSPTARDALKFLAKLRKSGYSIRSLNLVIQALKSYFKFEGLDSEAEKLKNPKIPKSLPKSLTEDEVKKIVSVADNLRDKLILLLLYGAGLRVSELCNLKIEDVNFEKSFLIVRGGKGGKDRVIPISKTLLFEIERYLKTRKDNSPYLFVEKRRNRKDKLSPKTVWMLVKKYGKKVGLNVTPHQLRHSFATHMLERGVDIRIIQELLGHANLSTTQIYTKVTTKHLREAIEKAKLIETILGG
Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules.
O59490
Q28VU8
UPPP_JANSC
Undecaprenyl pyrophosphate phosphatase
unclassified Jannaschia
MSLFTLFLLALVQGITEFLPISSSGHLILLPNLLGIEDQGQAIDVAVHVGTLGAVILYFWRDVKAAIAGTPRLLTGRIDTPGAKLAFLLIIATIPVIIFGLFLEVTGIYDSLRSIAVIGWTMLIFGLVLYWADQRGGTEKQSDDWSLRDAVTMGLWQAVALIPGTSRSGITITAARFLGYDRESAARVAMLMSIPTIIATGVFAGAEVIATADAQTARDGAIAAALSFLAALAALTLMFRLLKSVSFTPYVIYRVILGVILLVIAYA
Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Q28VU8
Q8IN42
TOTZ_DROME
Protein Turandot Z
Sophophora
MYFAIRLSFVLAVLICLTGNGSARMLDADRNRLQQLQIRSQQSADANTQVDIAYEVIGIYDKYKGQGGSNVLREAQLNSQVNDFKRKTMVIDGVPAQGGVWGILGAIKKAADAVPDNVKKDAENLVKSSTKVLVRGIYDYLMGKMKH
A humoral factor that may play a role in stress tolerance.
Q8IN42
O00268
TAF4_HUMAN
Transcription initiation factor TFIID 135 kDa subunit
Homo
MAAGSDLLDEVFFNSEVDEKVVSDLVGSLESQLAASAAHHHHLAPRTPEVRAAAAGALGNHVVSGSPAGAAGAGPAAPAEGAPGAAPEPPPAGRARPGGGGPQRPGPPSPRRPLVPAGPAPPAAKLRPPPEGSAGSCAPVPAAAAVAAGPEPAPAGPAKPAGPAALAARAGPGPGPGPGPGPGPGPGKPAGPGAAQTLNGSAALLNSHHAAAPAVSLVNNGPAALLPLPKPAAPGTVIQTPPFVGAAAPPAPAAPSPPAAPAPAAPAAAPPPPPPAPATLARPPGHPAGPPTAAPAVPPPAAAQNGGSAGAAPAPAPAAGGPAGVSGQPGPGAAAAAPAPGVKAESPKRVVQAAPPAAQTLAASGPASTAASMVIGPTMQGALPSPAAVPPPAPGTPTGLPKGAAGAVTQSLSRTPTATTSGIRATLTPTVLAPRLPQPPQNPTNIQNFQLPPGMVLVRSENGQLLMIPQQALAQMQAQAHAQPQTTMAPRPATPTSAPPVQISTVQAPGTPIIARQVTPTTIIKQVSQAQTTVQPSATLQRSPGVQPQLVLGGAAQTASLGTATAVQTGTPQRTVPGATTTSSAATETMENVKKCKNFLSTLIKLASSGKQSTETAANVKELVQNLLDGKIEAEDFTSRLYRELNSSPQPYLVPFLKRSLPALRQLTPDSAAFIQQSQQQPPPPTSQATTALTAVVLSSSVQRTAGKTAATVTSALQPPVLSLTQPTQVGVGKQGQPTPLVIQQPPKPGALIRPPQVTLTQTPMVALRQPHNRIMLTTPQQIQLNPLQPVPVVKPAVLPGTKALSAVSAQAAAAQKNKLKEPGGGSFRDDDDINDVASMAGVNLSEESARILATNSELVGTLTRSCKDETFLLQAPLQRRILEIGKKHGITELHPDVVSYVSHATQQRLQNLVEKISETAQQKNFSYKDDDRYEQASDVRAQLKFFEQLDQIEKQRKDEQEREILMRAAKSRSRQEDPEQLRLKQKAKEMQQQELAQMRQRDANLTALAAIGPRKKRKVDCPGPGSGAEGSGPGSVVPGSSGVGTPRQFTRQRITRVNLRDLIFCLENERETSHSLLLYKAFLK
The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription . TFIID recognizes and binds promoters with or without a TATA box via its subunit TBP, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC) . The TFIID complex consists of TBP and TBP-associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13 . TAF4 may maintain an association between the TFIID and TFIIA complexes, while bound to the promoter, together with TBP, during PIC assembly . Potentiates transcriptional activation by the AF-2S of the retinoic acid, vitamin D3 and thyroid hormone .
O00268
B8NM70
USTYB_ASPFN
Ustiloxin B biosynthesis protein Yb
Aspergillus subgen. Circumdati
MPSDGNHLTRSTGGNGFIAVNQTERYTLPPPIKQLALEGQDPRTDNPGTDGTGAVHICKDFDGILAWADSRRLVDAKHN
Oxidase; part of the gene cluster that mediates the biosynthesis of the secondary metabolite ustiloxin B, an antimitotic tetrapeptide . First, ustA is processed by the subtilisin-like endoprotease Kex2 that is outside the ustiloxin B gene cluster, at the C-terminal side of Arg-Lys, after transfer to Golgi apparatus through the endoplasmic reticulum (ER) . Cleavage by KEX2 generates 16 peptides YAIG-I to YAIG-XVI . To process the precursor peptide further, at least two peptidases are necessary to cleave the N-terminal and C-terminal sides of the Tyr-Ala-Ile-Gly core peptide which serves as backbone for the synthesis of ustiloxin B, through cyclization and modification of the tyrosine with a non-protein coding amino acid, norvaline . One of the two peptidases must be the serine peptidase ustP; and the other pepdidase is probably ustH . Macrocyclization of the core peptide derived from ustA requires the tyrosinase ustQ, as well as the homologous oxidases ustYa and ustYb, and leads to the production of the first cyclization product N-desmethylustiloxin F . For the formation of N-desmethylustiloxin F, three oxidation steps are required, hydroxylation at the benzylic position, hydroxylation at either the aromatic ring of Tyr or beta-position of Ile, and oxidative cyclization . UstQ may catalyze the oxidation of a phenol moiety, whereas the ustYa and ustYb are most likely responsible for the remaining two-step oxidations . N-desmethylustiloxin F is then methylated by ustM to yield ustiloxin F which in turn substrate of the cytochrome P450 monooxygenase ustC which catalyzes the formation of S-deoxyustiloxin H . The flavoprotein monooxygenases ustF1 and ustF2 then participate in the modification of the side chain of S-deoxyustiloxin H, leading to the synthesis of an oxime intermediate, via ustiloxin H . Finally, carboxylative dehydration performed by the cysteine desulfurase-like protein ustD yields ustiloxin B .
B8NM70
Q3KP31
ZN791_HUMAN
Zinc finger protein 791
Homo
MDSVAFEDVSVSFSQEEWALLAPSQKKLYRDVMQETFKNLASIGEKWEDPNVEDQHKNQGRNLRSHTGERLCEGKEGSQCAENFSPNLSVTKKTAGVKPYECTICGKAFMRLSSLTRHMRSHTGYELFEKPYKCKECEKAFSYLKSFQRHERSHTGEKPYKCKQCGKTFIYHQPFQRHERTHIGEKPYECKQCGKALSCSSSLRVHERIHTGEKPYECKQCGKAFSCSSSIRVHERTHTGEKPYACKECGKAFISHTSVLTHMITHNGDRPYKCKECGKAFIFPSFLRVHERIHTGEKPYKCKQCGKAFRCSTSIQIHERIHTGEKPYKCKECGKSFSARPAFRVHVRVHTGEKPYKCKECGKAFSRISYFRIHERTHTGEKPYECKKCGKTFNYPLDLKIHKRNHTGEKPYECKECAKTFISLENFRRHMITHTGDGPYKCRDCGKVFIFPSALRTHERTHTGEKPYECKQCGKAFSCSSYIRIHKRTHTGEKPYECKECGKAFIYPTSFQGHMRMHTGEKPYKCKECGKAFSLHSSFQRHTRIHNYEKPLECKQCGKAFSVSTSLKKHMRMHNR
May be involved in transcriptional regulation.
Q3KP31
B0Y4Q5
TVP38_ASPFC
Golgi apparatus membrane protein tvp38
Aspergillus subgen. Fumigati
MPADYTSTARALSLPMSPAESLSPAEEDTRPLWSHLASSRRNTASPSVRESTGLRDQVVNQATKMLRRTKKTWRRLTFWQRIGAIGAALLAILLGLSFMIFTGQVFFWLGPVAEKWEQSWLAFFVLWLCVFFVSFPPLVGWSTFGTISGFIYGIWKGWILYATATVLGSTCSFIVSRTILSKFVNRMMERDKRFAALALTLKYDGLKLLCMIRLCPLPYSVCNGAVSTFPTVHPLMYGLATALITPKLLVPAFIGSRIRILSEKNEEMSAASKAVNICSIILTIGIGVFTGWYIYRRTLARAKELEAKERADIRRSLQADHAAHRPHGSFSEDPDVNTAATTLARDEEERIGFNDFDDDNVDLVIDDDSGSEISPNLTKKQFPGPYRDEFTDNDSDVFGDGDGPDSQMFRLHTHVRSG
Golgi membrane protein involved in vesicular trafficking and spindle migration.
B0Y4Q5
Q96493
UFOG_GENTR
UDP-glucose flavonoid 3-O-glucosyltransferase
Gentiana
MSPVSHVAVLAFPFGTHAAPLLTLVNRLAASAPDIIFSFFSTSSSITTIFSPTNLISIGSNIKPYAVWDGSPEGFVFSGNPREPIEYFLNAAPDNFDKAMKKAVEDTGVNISCLLTDAFLWFAADFSEKIGVPWIPVWTAASCSLCLHVYTDEIRSRFAEFDIAEKAEKTIDFIPGLSAISFSDLPEELIMEDSQSIFALTLHNMGLKLHKATAVAVNSFEEIDPIITNHLRSTNQLNILNIGPLQTLSSSIPPEDNECLKWLQTQKESSVVYLSFGTVINPPPNEMAALASTLESRKIPFLWSLRDEARKHLPENFIDRTSTFGKIVSWAPQLHVLENPAIGVFVTHCGWNSTLESIFCRVPVIGRPFFGDQKVNARMVEDVWKIGVGVKGGVFTEDETTRVLELVLFSDKGKEMRQNVGRLKEKAKDAVKANGSSTRNFESLLAAFNKLDS
In the presence of other necessary color factors, this glycosylation reaction allows the accumulation of anthocyanin pigments . Anthocyanidins are the preferred substrates, while flavonols are only a minor substrate in vitro .
Q96493
Q2SUI1
TRPD_BURTA
Anthranilate phosphoribosyltransferase
pseudomallei group
MTITPQEALQRTIEHREIFHDEMLHLMRLIMRGDMSPVMAAAIITGLRVKKETIGEITAAATVMREFARHVEVEDNANFVDIVGTGGDGSHTFNISTATMFVAAAAGAKVAKHGNRGVSSKSGSADVLEALGVNIDLQPEQVAASIAETGMGFMFAPNHHPAMRNIAPVRRELGVRTIFNILGPLTNPADAPNQLMGVFHPDLVGIQVRVMQRLGARHVLVVYGKDGMDEVSLGAATLVGELRDGEVREYEIHPEDFGMQMVSNRTLKVENAGESRVMLLEALGNKPGVAREIVTLNAGTALYSANVAGSIADGIQLAREAIASGRAREKVDELARFTQQFKR
Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
Q2SUI1
P38669
TBA2_NEUCR
Tubulin alpha-B chain
Neurospora
MREIISLNVGQAGCQIANSCWELYCLEHGIQPDGYLTEERKAADPDHGFSTFFSETGNGKYVPRTIYADLEPNVIDEVRTGAYRGLFHPEHMISGKEDASNNYARGHYTVGKELIDQVLDKVRRVADNCSGLQGFLVFHSFGGGTGSGFGALLMERLSVDYGKKSKLEFCVYPAPQTATSVVEPYNSILTTHTTLEHADCSFMVDNEAIYDICRRNLGLERPNYENLNRLIAQVVSSITASLRFDGSLNVDLNEFQTNLVPYPRIHFPLVAYAPVISAAKAAHEANSVQEMTMSCFEPNNQMVKCDPRHGKYMATCLLYRGDVVPNDAHAAVATLKTKRTIQFVDWCPTGFKLGICYQPPHQVPNGDLAKVNRAVCMLSNTTAIAEAWSALSSKFDLMYSKRAFVHWYVGEGMEEGEFSEAREDLAALERDYEEVAADSMEGEDVEAEY
Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
P38669
Q9U3V9
XMAS_DROME
Protein xmas
Sophophora
MAEPRPGGYNYKTLLCRNIPELFLDKYVARSHFGRFGTLVNFVLRPRRMTCTVSYASEDEAARALLDGASFQGHLFDISYADNETAPAQKTEEWVDPDIQAELSALQSGWRNEYGSGKPIKKPQNGSSGSGGSSMLPAIPVGPATAPVSRDRTPAQLRDLENMMRRPAHTSEEKFSVLDARDKLLRLNRTQHKLSGATQGHCADMCPEKERVLREFQRQVAYYELQPGSDELICHERALKQYSRSSADQETPLPHELRNETALHMTMSYLMHEIMDISERQDPQSHMGDWFHFVWDRTRSIRKEITQQELCSLGAVKLVEQCARFHIHCAARLVDADPSVFDSKINAENLTKCLQTLKYMYHDLRIKGVPCPKEAEFRGYIVLLNLADANFLWDIGQLPAELQSCPEVRQAIQFYLALQDTNFVRFFQLLADKDTSYLSACILVNYFTRLRVLGLHRLIQAYRSPRKDEVSSLPLSYIAELLSFASEQEAADFVQHYGLQINEAGRVVLSRMHTVETEYKLPRQYELVEVKRVKSVGEVVSGEPLPPRDLYLNHRPHNSFDDYGMLKSIAWTAKDQLAGMQQEEMQPQMPSQPPAVSKHSDTLFKVPMQPDGTAAGFGVFAAAAVPPASSIDGFSFVLPKSRAQEFQEQAPATQQRRAQEEAKHQALQVAIAAAKKREAELMAIHEAKVAEAERVRQQKLRERQEQQRRQQQELEEQRQREQEKLQLEKERQLKLEQLFFVQQQEREAHKQTRTLELYQEIFQDTLAEICQSEFMSHSRACRSYESMLDSITRDLVERQMEQSIYELGVMRVCIRRWRKYRRTQQEKDTLFNQLPLSFGAENPEGVVNKRSMEDSLRLSRRYRLGEPCDYGKLLAGLEEHSWLKLDLWHVLDKCLPVAQPGARRFYKLLISLSGGQEGLQLNCDLDRGLLQQPQSPDARFVDGGYIRGFSQGIGLSVMKIRDDDHDWKATDLAEANGIICLIGLDDIRLLPDRLKPLLQASRCHDVAVIVQHPANTAFVQPDIPLQELCLRSFNIFRLRKSGNNRQRLMIALESAVKFLAKATERKRVGHLHQVETREYLLVNLGSELFRRLKYAAEHDTAIRSDTQLNPQRCVDLFNEAVHRLQLVAGEDLSDWPQFPEELRVFVQPLPIESSLNTNRLEHFEPGWHLPERRQRIVQLLERCKLPKMPVLPRSSSLAEAQCQWVLDYAQISQQEDCVEQIALQAIKILQYDTDDYLNFVEYLAGERMQYILRQERNPPQGIVYNTKTLKRRFLSAWYYEFREPQIYEPVPAEENAQMLEKQPSSQAEVQQLDFDEITSKAEAVLKRFHQRQDERHTLRELNRSHKSRKRRDASDHKHAMSSLVSALKAARSDYQGKSSAVCRLVAQMVEADQVKYQWTPNLTSLIDRKDASTRHQWRPHVNHSTRHARKLPVQSISFLSRCLAKKGEHAGLTSCVLSVKTRYAPKTLHGRELLIWRQSSMRPLLLPSSNLWTGVLSKRHYVPRLRPAEEDEEVERRAVPQLRITKEQSEEEEHQLQRRKDGSRLRNECSEFYLPMGEQDYSEREEENRGHRQAYVPSELMTPELATKWQTTSVTDRDRQLLNLEQQMKTQPSVRMTTQTWFSGNHRRYRSRRSGAKRYHVVSELEGWRRSSNHQPVPVFQGQPGEQEHLRHASHKASARSMPDGQERCQMVWEQKKRSPWHRTEVTNSNKVRMPRIRAAKSAVMMAQEARNKHHRLITKKLVYRPRRTVNAVQAEETEDQDTHHRHHGGGQKMSKRAPERALLKQHLADLLAVSKPEDSFRIGYQPNAPTRQLLEQGKCYVSLRREQFIHLHPVRPNSLILAVNLEVKESPRQPVTTLHRRDGAKRPRLVEDVVKPSLITVIRQSAATWDHNGRKVPAKKSNLVGMPSKEHAYQRRLVRNTSTLEAIVKAQAKPRSEPKSPSSATDYHRVASQKLPHVTSKADISKAADPFKDLDKPRIKEKEVASSWKQAYVVRSKMYDAITPYRRRAYPGKKCITKDKTDGYFLAKRSSAAAAGSSKKVKPPKQPVVSPKVQVPSVLHKKKSRESLGPQTTKTGKL
Involved in mRNA export and mRNA coupled transcription activation . Component of the nuclear pore complex (NPC)-associated TREX-2/AMEX complex (anchoring and mRNA export complex) which functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket), thereby enabling the export of mRNAs to the cytoplasm through the nuclear pores . The TREX-2/AMEX complex also functions with the transcriptional coactivator SAGA/TFTC complex, to anchor a subset of transcription sites to the nuclear pore complex basket in order to achieve efficient transcription and export of their resulting mRNAs . Within the complex, required for localization of e(y)2 to the nuclear periphery .
Q9U3V9
B4STS7
TRMB_STRM5
tRNA(m7G46)-methyltransferase
Stenotrophomonas maltophilia group
MTNPFDSAGSKAPPKPFTVSEGRREVRSFVLRQGRFTPAQQRAFDERWPRFGIDYNGQPRDLDATFGRPAHKVLEIGFGNGAAMRFAAQHDPSRDYIGIEVHAPGVGRLLNALADDNADHVRLYHHDAVEVLQNEIADGALDEVRIYFPDPWHKKRHNKRRLLQPAFAELIVRKLRPGGRLHCATDWEDYAEQMWDVLDATAGLVNRAGPRGSVPRPDWRPQTHFETRGQKLGHGVWDLLYDRT
Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
B4STS7
P61410
THIE_BACC1
Thiamine-phosphate pyrophosphorylase
Bacillus cereus group
MSRISKAEMSRLLSVYFIMGSNNCTKDPLQILKDALEGGITIFQFREKGEGALTGEERICFAKELQAICKEYGVPFIVNDDVELALELDADGVHVGQEDEGITSVREKMGDKIIGVSTHTIEEARWAIENGADYLGVGPIFPTSTKKDTKAVQGTKGLAHFREQGITIPIVGIGGISIENTASVIEAGADGVSVISAISLAESAYESTKQLVEEVSKKGTSHKY
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).
P61410
Q07402
UREF_BACSB
Urease accessory protein UreF
Bacillus
MNRLLSLFQLCDSNFPSGSFSHSFGLETYIQEKVITDKESFKNAISVYIRKQLFFTEGLACILAYEAMEKNEPSALVELDHILFASNVAQETRSGNQRMGERMAKLCVDLYPSPILIEYTNRIKEKKAYGHSAIVFAIVAYHLKVTKETAVGAYLFANVSALVQNAVRGIPIGQTDGQRILVEIQPLLEEGVRTISQLPKEDLGAVSPGMEIAQMRHERLNVRLFMS
Required for maturation of urease via the functional incorporation of the urease nickel metallocenter.
Q07402
Q5L5I5
TAL_CHLAB
Transaldolase
Chlamydia
MSSQFEQLKLLSVLVCDTGDPELVKSSESQDATTNPSLILKVAQEPKYQELLTEAIAWGIRQNGDDVQTLTFVLDKIQVNFGLEILKHIPGRVSLEIDARLSFNTEAMVQRAIFLSELFAASGGDKKRLLVKIPGTWEGIQAVELLEKQGIACNVTLIFNLIQAIAAAKAKATLISPFVGRIYDWWIAAYGDDGYSIDADPGVASVSNIYTYYKKFDITTQIMAASFRSKEQVLALAGCDLLTVSPKLLDELKKDQSPVERKLDPAEAKKLDVQPVELTESIFRFLMNEDAMATEKLAEGIRIFSGDTQILEAAVTEFIKQIAAQDV
Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
Q5L5I5
P9WIZ6
Y3131_MYCTO
Putative NAD(P)H nitroreductase MT3217
Mycobacterium tuberculosis complex
MTAAVDGKGPAAMNTHFPDAETVRTVLTLAVRAPSIHNTQPWRWRVCPTSLELFSRPDMQLRSTDPDGRELILSCGVALHHCVVALASLGWQAKVNRFPDPKDRCHLATIGVQPLVPDQADVALAAAIPRRRTDRRAYSCWPVPGGDIALMAARAARGGVMLRQVSALDRMKAIVAQAVLDHVTDEEYLRELTIWSGRYGSVAGVPARNEPPSDPSAPIPGRLFAGPGLSQPSDVLPADDGAAILALGTETDDRLARLRAGEAASIVLLTATAMGLACCPITEPLEIAKTRDAVRAEVFGAGGYPQMLLRVGWAPINADPLPPTPRRELSQVVEWPEELLRQRC
Stimulates pro-inflammatory cytokine expression via TLR2 signaling pathway. Activation of TLR2 results in the phosphorylation and activation of NF-kappa-B. Also induces TLR2 expression. May influence the innate immune responses to facilitate the survival of M.tuberculosis in the granulomatous microenvironment.
P9WIZ6
Q07748
THI13_YEAST
Thiamine pyrimidine synthase
Saccharomyces
MSTDKITFLLNWQPTPYHIPIFLAQTKGYFKEQGLDIAILEPTNPSDVTELIGSGKVDMGLKAMIHTLAAKARGFPVTSVASLLDEPFTGVLYLKGSGITEDFQSLKGKKIGYVGEFGKIQIDELTKHYGMKPEDYTAVRCGMNVAKYIIEGKIDAGIGIECMQQVELEEYLAKQGRPASDAKMLRIDKLACLGCCCFCTVLYICNDEFLKKNPEKVRKFLKAIKKATDYVLADPVKAWKEYIDFKPQLNNDLSYKQYQRCYAYFSSSLYNVHRDWKKVTGYGKRLAILPPDYVSNYTNEYLSWPEPEEVSDPLEAQRLMAIHQEKCRQEGTFKRLALPA
Responsible for the formation of the pyrimidine heterocycle in the thiamine biosynthesis pathway. Catalyzes the formation of hydroxymethylpyrimidine phosphate (HMP-P) from histidine and pyridoxal phosphate (PLP). The protein uses PLP and the active site histidine to form HMP-P, generating an inactive enzyme. The enzyme can only undergo a single turnover, which suggests it is a suicide enzyme.
Q07748
Q9ZRX0
TCTP_PSEMZ
Translationally-controlled tumor protein homolog
Pseudotsuga
MIVYQDLLSGDELLSDSFPYKELYNGVLWEVEGKWVVQGAVDVDIGANPSAEGGDEEGVKIRLVKVVDIVDTFRLQEQPPFDKKQFLGFIKRYIKNLATKLSEERQAEFKKNVEGAAKMLVSKLSDLQFFVGESMHDDGSMVFAYYKDGATDPTFLYFADGLKEVKC
Involved in calcium binding and microtubule stabilization.
Q9ZRX0
Q03LR5
TRHO_STRTD
tRNA hydroxylation protein O
Streptococcus
MAKPIRVLLYYKYVPIENAEQFAADHLAFCKSIGLKGRILVADEGINGTVSGDYETTQKYMDYVHSLPGMEDLWFKIDEEEEQAFKKMFVRYKKEIVHLGLEDNNFDSDINPLETTGAYLSPKEFKDALLDEDTVVLDTRNDYEYDLGHFRGAIRPDIRNFRELPQWVRDHKEEFMDKRVVVYCTGGVRCEKFSGWLVREGYKDVGQLHGGIVTYGKDPEVQGELWDGKLYVFDERIAVDVNHVDPIVVGKDWFDGTPCERYVNCGNPFCNRRILTSEENEDKYLRGCSHECRVHPRNRYVSENDLSQEEVVSRLAAIGESLDVTPA
Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs.
Q03LR5
Q3SQ36
TYSY_NITWN
Thymidylate synthase
Nitrobacter
MNQYHDLLERILGEGTEKHDRTGTGTLSVFGHQMRFDLASGFPMLTTKKLPFRSIVHELLWFLRGETNIKYLKDNGVSIWDEWADANGDLGPVYGSQWRSWPARDGRGIDQIANVIDLIQRNPDSRRLIVSAWNPADVDRMALPPCHCLFQFYVAGGKLSCQLYQRSADVFLGVPFNIASYALLTMMVAQVTGLKPGDFVHSLGDAHLYSNHLDQARLQLSRPTRPLPTMTINPEVKDIFAFRYEDFRLENYDPHPHIKAEVAV
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.
Q3SQ36
C6E4K4
TRUD_GEOSM
tRNA-uridine isomerase D
unclassified Geobacter
MSIYLTAEVPGTGGVIKATPEDFLVEEIPAYLPSGQGEHCFAVLEKRGIATLEALRRLAKALGVQERDLGYAGMKDAIGITRQTISIPRVAPEKVLALEIPGITVLSASMHGNKLRLGHLKGNRFVIRVRDVAQGAAGNAEAALEIMTRRGVPNRFGVQRYGAQGNTHEIGAAMLRREFKSAVDRLIGDPAAVTDERWRLAIEAYRRGEVAESLALFPGHFRVERELLTRLVQRPDGFERAFNSVQPRMKRLYLSAFQSSLFDLVLGKRLDSFDQVNVGDIAFKHENGACFLVQDLAAEAPRAESFEISPTGPMFGCTMMESHGAQGELEREVLAAQELTLESFNLSGGLRMEGERRPLRVPIAGAEVRQDGSDLLLDFSLPRGAYATCVLSEIMKSD
Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs.
C6E4K4
B0TQA0
TRUB_SHEHH
tRNA-uridine isomerase
Shewanella
MARRSRGRFIDGILLLDKDTGMSSNFALQRVKRFFNANKAGHTGALDPLATGMLPICLGEATKFSQHLLDADKRYLVTAKLGQRTDTSDSDGEIVQTREVNFTQEQLDTALEHFRGETMQVPSMYSALKHKGQPLYKYAREGIEVPREARPINVFELNFISLEGDELTLDIHCSKGTYIRTITDDLGEMLGCGAHVIMLRRTQVAGYPYDKMVSLKQLEELVTKADAESLSLSEVLDPLLLPMDTAVSGFKEINVSDELATYLMNGNPVQVANLPVDELVRITIGDARQFVGIGQMNDDGQLAPKRLIVLREQQD
Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
B0TQA0
P82959
TXH21_CYRSC
Huwentoxin-II
Cyriopagopus
MKVTLIAILTCAAVLVLHTTAAEELEAESQLMEVGMPDTELAAVDEERLFECSFSCEIEKEGDKPCKKKKCKGGWKCKFNMCVKV
Lethal neurotoxin that blocks neuromuscular transmission. Acts cooperatively to potentiate the activity of huwentoxin-I. This toxin is active against insects.
P82959
Q4QML9
TRUD_HAEI8
tRNA-uridine isomerase D
Haemophilus
MLEQLPYLALKTPPKTTALLKAECADFIVKEHLGYEMSGDGEFVALYVRKTDCNTLFVGEKLAKFAGVSERNMGYAGLKDRRAVTEQWFCLQMPGMETPDFSQFELDGVEILTVTRHNRKIRTGSLEGNYFDILLRGAEESDELKVRLDFVANFGFPNYFTEQRFGREGHNLTQALRWAQGEIKVKDRKKRSFYLSAARSEIFNLVVAARIAKGATNQVLPNDIVQLAGSHSWFKADEKEDLTVLQVRLENQDILLTAPLIGEDILAASDIENEIVNQHSAFDSLMKQERMKAVRRPLLMKAKGFSWAFEPEGLRLKFYLPAGSYATALVRELVNYTEE
Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs.
Q4QML9
B3R8A8
ZAPD_CUPTR
Z ring-associated protein D
Cupriavidus
MILYEYPFNERIRTLLRLEDLFDRLEYFLGQDHAQQHHVALTTLFEIIDVAGRADLKTDLIKELERQRQALAPLRANPQIDQDALDSVIGEIEQGIAMLNQTVGKAGQLLTDNEWLTSIRSRAIIPGGTCEFDLPAYYAWQHRPAEDRRADILKWARPLVSLRMGTTIVLRLLREAGQSGKVIATGGSYQQMLSGRSYQLMQVYLDDSLLAFIPEMSANKYMLWVRFTQQDGDLRPRSVDADIPFLLKLCNF
Cell division factor that enhances FtsZ-ring assembly. Directly interacts with FtsZ and promotes bundling of FtsZ protofilaments, with a reduction in FtsZ GTPase activity.
B3R8A8
Q9K6X9
UVRB_HALH5
Excinuclease ABC subunit B
Halalkalibacterium (ex Joshi et al. 2022)
MSQSFELVSQYKPQGDQPNAIRQLVAGINEGKKHQTLLGATGTGKTFTMSNVIQQVNKPTLVIAHNKTLAGQLYSEFKEFFPNNAVEYFVSYYDYYQPEAYVPQSDTYIEKDASINDEIDKLRHSATSALFERNDVIIVASVSCIYGLGSPEEYKELVCSLRTGMEIERNDLLRQLVDIQYDRNDVNFTRGTFRVRGDVVEIFPASRDEQCIRVEFFGDEIDRITEVDALTGEIKGERNHVAIFPASHFVTREEKLKRATKSIEAELEERLKELHDRGKLLEAQRLEQRTRYDLEMIHEMGFCSGIENYSRHLTLRKAGETPYTLLDFFPDDFLIIIDESHVTIPQIRAMYNGDQARKGVLVDHGFRLPSALDNRPLKFEEFEHKVHQAVFVSATPGPYELEHTPEMVEQIIRPTGLLDPVIEVRPIEGQIDDLIGEINERVAKNERVLVTTLTKKMAEDLTDYLKEVGIKVRYLHSEVKTLERIEIIRQLRLGTFNVLVGINLLREGLDIPEVSLVAILDADKEGFLRAERSLIQTIGRAARNANGYVIMYADRMTKSMQIAIDETKRRRSIQEEYNRKHGITPKTIEKRIPDVIKATAMVAEDGEEYTSHAPKQKMSKKEREAVIERMEAEMKEAAKTLNFERAAELRDLILELKAEG
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.
Q9K6X9
Q41738
THI41_MAIZE
Thiazole biosynthetic enzyme 1
Zea
MATAAASSLLKSSFAGSRLPAATRTTPASLVVATGPRGAGAGPICASMSMSSSNPPYDLTSFRFSPIKESIVSREMTRRYMTDMITYADTDVVIVGAGSAGLSCAYELSKDPAVSIAIVEQSVSPGGGAWLGGQLFSAMVVRKPAHLFLDELGVAYDEAEDYVVIKHAALFTSTVMSLLLARPNVKLFNAVAVEDLIVRGGRVGGVVTNWALVSMNHDTQSCMDPNVMEAKVVVSSCGHDGPFGATGVKRLQDIGMISAVPGMKALDMNTAEDEIVRLTREVVPGMIVTGMEVAEIDGAPRMGPTFGAMMISGQKAAHLALKALGRPNAVDGTMSPPLREELMIAYKDDEVVDA
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.
Q41738
O94266
THI22_SCHPO
Hydroxymethylpyrimidine phosphate kinase 2
Schizosaccharomyces
MPYNPLYESLSNQFDPSRIETVLDPMGYTIKRRALPVSLTIAGSDCSGGAGIQADLKTMTSLGVYGMSAITCLVAENAGGVDSVEEMSPAFVESQIDCCIRDIPCHVVKTGMLGSPEIVKAVARSAKKFNFSKLVVDPVMVATSGDSLVTKDIVSVLNEELLPLTYLVTPNIPEAIVLAKNQGLDISNINSVSDMERCAAVIHKLGPKHVLLKGGHMPVNNLGLKSSDDEDLRVVDILYDGNRFYHFSSSYLKKGEVHGTGCTLSSAIASFLAWEHSLTEAVQFGIDYVHGAITHSPPINNCSTNILNHMTRLRIVPFAPGHFIEYILSHPQVVPAWKEYINHKFTNMLAKGTLPLPAFQDYLKQDYLYLVNFARAYSLKGYKENTFPNILEAAQSVIHVIEEKELHVSMCSSYGVSLQDLKSCEESPACTAYSRYILDTGAAQDVAALDFVQAPCLIGYYVIAARLMKEPFRNPQGPYQKWVDNYFCEDYLSAVRRGCRQIEEIVLKLSPERIQELIEIFIRATKFETLFWETPYYEYVTKQNLEDKEFS
Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P.
O94266
A7ZNQ8
YEGS_ECO24
Probable lipid kinase YegS
Escherichia
MAEFPASLLILNGKSTDNLPLREAIMLLREEGMTIHVRVTWEKGDAARYVEEARKLGVATVIAGGGDGTINEVSTALIQCAGDDIPALGILPLGTANDFATSVGIPEALDKALKLAIAGNAIAIDMAQVNKQTCFINMATGGFGTRITTETPEKLKAALGGVSYIIHGLMRMDTLQPDRCEIRGENFHWQGDALVIGIGNGRQAGGGQQLCPNALINDGLLQLRIFTGDEILPALVSTLKSDEDNPNIIEGASSWFDIQAPHEITFNLDGEPLSGQNFHIEILPAALRCRLPPDCPLLR
Probably phosphorylates lipids; the in vivo substrate is unknown.
A7ZNQ8
P29501
TBB2_PEA
Beta-2-tubulin
Pisum
EIVHIQGGQCGNQIGAKFWEVVCAEHGIDPTGRYGGDTDLQLERINVYYNEASCGRYVPRAVLMDLEPGTMDSVRSGPYGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYPDRMMLTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLTTPSFGDLNHLISATMSGVTCCLRFPGQLNSDLRKLAVNLIPFPRLHFFMLGFAPLTSRGSQQYRALSVPEITQQMWDSKNMMCAADPRHGRYLTASAIFRGKMSTKEVDEQMMNVQNKNSSYFVEWIPNNVKSTVCDIPPTGLKMASTFIGNSTSIQEMFRRVSEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATAEEDEYEEEEEDYHQEHDEM
Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
P29501
Q9I163
Y2418_PSEAE
Pirin-like protein PA2418
Pseudomonas
MKKVLGIYGNANRHWVGDGFPVRSLFSYNTLGQHISPFLLLDYAGPADFPPAQQRRGVGQHPHRGFETVTIVYQGEVEHHDSTGAGGRIGPGDVQWMTAASGILHEEYHSERFRSTGGTLEMVQLWVNLPSSDKMNPPRYQTLLDADIPRVGLPDRAGELRVIAGRYGRHQGPALTHSPLAVWDVQLKAGKHLALDLPKGHTCAVVVLRGTLAVGDEIVREAQVALLDRDDPRLELEANNDVQLLVLSGEPLDEPIIGYGPFVMSSREEIDQAIEDFENGRFIRAH
Putative quercetin 2,3-dioxygenase.
Q9I163
Q2TA17
ZN668_BOVIN
Zinc finger protein 668
Bos
MEVESPEERSPAPGYKRSGRRYKCLSCTKTFPNAPRAARHAATHGLADCTEEMAEAKLKPETDPKAEDASGDKVSGAAAKPRPYACPLCPKAYKTAPELRSHGRSHTGEKPFPCPECGRRFMQPVCLRVHLASHAGELPFRCAHCPKAYGALSKLKIHQRGHTGERPYTCADCGKSFADPSVFRKHRRTHAGLRPYSCERCGKAYAELKDLRNHERSHTGERPFLCSECGKSFSRSSSLTCHQRIHAAQKPYRCPACGKGFTQLSSYQSHERTHSGEKPFLCPRCGRMFSDPSSFRRHQRAHEGVKPYRCEKCGKDFRQPADLAMHRRVHTGDRPFKCLQCDKTFVASWDLKRHALVHSGQRPFRCEECGRAFAERASLTKHSRVHSGERPFHCNACGKSFVVSSSLRKHERTHRSSEATGAPPQQELVVGLALPVSMAGEGPAAPASGAALGDPPAGLLGLPSESGGVMATQWQVVGMTVEHVECQDAGVGEAPGPLGAAGEVGGEEVDEKPPQFVCRECKETFSTLTLLRRHERSHPELRPFHCTQCGKSFSDRAGLRKHSRTHSSVRPYTCPHCPKAFLSASDLRKHERTHPVPIGTPTPLEPLVALLGMPEEGPA
May be involved in transcriptional regulation.
Q2TA17
B8I0U9
TRPD_RUMCH
Anthranilate phosphoribosyltransferase
Ruminiclostridium
MIQEAIYQVINKQDLDLDKTIQVMEEIMEGRATNAQIGSFLTAMRMKGETIDEITACATVMRQKCKRIHPEKDVLDIVGTGGDEANTFNISTVSSFVVSAGGVPVAKHGGRSVSSKCGSADLLEALGINIALSAEQSAEILQKIGMCFMFAPTYHASMKYAAPVRKELSVRTIFNILGPLANPAGANMQLLGVYDENLVEPLARVLLNLGVKRAMVVHGHDGLDEVTLCNTTTICEVSNGNINSFFLSPEQLGFSRCLLKELVGGDPKKNASIALDILNGSKGPKRDIVVLNSALCLYMSYNQITLRDCVKMAEQLIDSGAAKAQLNKFIELSNSFNQEVK
Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
B8I0U9
Q91053
VSP1_GLOUS
Snake venom serine protease
Gloydius
MVLISVLANLLILQLSYAQKSSELVIGGDECNINEHRFLVALYNSRSRTLFCGGTLINQEWVLTAAHCERKNFRIKLGIHSKKVPNEDEQTRVPKEKFFCLSSKNYTLWDKDIMLIRLDSPVSNSEHIAPLSLPSSPPSVGSVCRIMGWGRISPTKETYPDVPHCANINLLEYEMCRAPYPEFGLPATSRTLCAGILEGGKDTCRGDSGGPLICNGQFQGIASWGDDPCAQPHKPAAYTKVFDHLDWIQSIIAGNTDASCPP
Thrombin-like snake venom serine protease. Has a coagulant activity. Acts on alpha-chains of fibrinogen (FGA) generating fibrinopeptide A.
Q91053
Q4FUL2
TRPA_PSYA2
Tryptophan synthase alpha chain
Psychrobacter
MTRIESTFEILKAQNKKALIPYVMAGDPNPSNFVGLLHDLVKHGADMIEVGLPFSDPMADGPTVALAGERALAAGTSTRDALKMVAEFRQQDTQTPIILMGYLNPVEIIGYDNFVALCEQSGVDGILMVDLPPAEAGSFTQHLTEHSMNEIFLLSPTTLPERREQVLTHCGGYIYYVSLKGVTGSATLDTDDVATQVQAIKAETDLPVCVGFGIRDAASAKAIGAHADGIIVGSALVQNFADIDGNDATAVAHAQQKIMAKMTELREALDSLSVSSNG
The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
Q4FUL2
P18732
ZG64_XENLA
Gastrula zinc finger protein XlCGF64.1
Xenopus
PSGKQYECPECGKTFKYKNSLTIHQRGHTEEKPFMCTQCGKCFRQKKALRRHQFIHTGEKPYVCTECEKRFLEKSQLILHQRGHTGEKPFTCTECGESFRHKQVLMRHQFIHTGEKPYECTQCGEGFLLKSKLIHHQRGHTGEKPFMCTECGKGFRQKQVLIEHQFIHTGEKPLMCTDCGKHFRQKHVLRLHKLSH
May be involved in transcriptional regulation.
P18732
Q0S3C4
TSAD_RHOJR
tRNA threonylcarbamoyladenosine biosynthesis protein TsaD
Rhodococcus
MIVMGIESSCDETGVGIVRWNGDGTCELLADEVASSVEEHARYGGVVPEVASRAHLEAIVPTMRRALAVAGIAKPDALAVTIGPGLAGALLVGVAAAKAYAAAWDVPFYAVNHLGGHVSVDTLEHGPMPPCVALLVSGGHTHLLHVEDLAKPIVELGTTVDDAAGEAFDKVARLLGLGFPGGPALDAAAQDGDRNAIPFPRGMTGPRDARHDFSFSGLKTAVARYVESKERAGEVCSVPDIAASFQEAVADVLTMKAVRAARDVGVDTLVLGGGATANSRIRALAEERCADAGLTLRVPKPRLCTDNGVMIASLGAHLIAGGAAPSLLTVASDPGLSVATSQVFS
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.
Q0S3C4
P09123
THRC_BACSL
Threonine synthase
Bacillus
MYKGLLKQYASYLPVNEKTPDVSLMEGNTPLIPLLNISKQLGVQLYGKYEGANPTGSFKDRGMVMAVAKAKEEGSEAIICASTGNTSASAAAYAARLGMKCIIVIPEGKIAHGKLAQAVAYGAEIISIEGNFDDALKAVRNIAAEEPITLVNSVNPYRIEGQKTAAFEICDQLQNAPDVLAIPVGNAGNITAYWKGFCEYEKEKGYKKPRIHGFEAEGAAAIVKGHVIEEPETIATAIRIGNPASWSYAVEAAEQSHGEIDMVSDEEILHAYRLLAKTEGVFAEPGSNASLAGVIKHVESGKIKKGETVVAVLTGNGLKDPDIAISSNQLDIASVSNDIEQIKDHIKGVIMS
Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine.
P09123
P70904
VLP23_BORHE
Variable large protein 23
Borrelia
MRKRISAIIMTLFMVLVSCNSGGVAEDPKTVYLTSIANLGKGFLDVFVTFGDMVAGAFGIKADTKKSDIGKYFNDIEKTMTTVKKRLQDEVAKNGNYVKVKEVVDKFVADVLDKIAAGAKKQLRATGDAAIGMLLNEDAAPAEVASVNSLVKGIKEIVGVVLKDNEGDAAATKTADAEKKSVGKLLGKGAADGTETQAAAASASIGAITGADILQAIAKSGKAGAGEIKIEEAKNAAEIAAAKADSKDLAIDSAKKDAVIAAGIALRAMAKDGKFAAKNNEEKSANAVNGAAASAVGKTLSTLIIAIRNTVDSGLKTINEALATVKQEDKSAEATNPAEATTSGQ
The Vlp and Vsp proteins are antigenically distinct proteins, only one vlp or vsp gene is transcriptionally active at any one time. Switching between these genes is a mechanism of host immune response evasion.
P70904
O48559
UNI_PEA
Protein UNIFOLIATA
Pisum
MDPDAFTASLFKWDPRTVLSTAPSPRPQLLDYAVTPTTAPMTYHPARLPRELGGLEELFQAYGIRYYTAAKIAELGFTVSTLVDMKDDELDDMMNSLSQIFRWDLLVGERYGIKAAIRAERRRLDEEEIKRRGLLSGDTTNALDALSQEGLSEEPVVQREKEAMGSGGGSTWEVAVVEERRKRQQIRRRRMKMKGNDHGENEEGEEEEEDNISGGGVGGGERQREHPFIVTEPAEVARGKKNGLDYLFHLYEQCREFLIQVQAIAKERGEKCPTKVTNQVFRYAKKAGASYINKPKMRHYVHCYALHCLDEEVSNELRRGFKERGENVGAWRQACYKPLVAIAARQGWDIDAIFNAHPRLSIWYGPTKLRQLCHAERNGAAASSSVSFGTTHLPF
May regulate indeterminacy during leaf and flower development.
O48559
Q148G8
UQCC3_BOVIN
Ubiquinol-cytochrome-c reductase complex assembly factor 3
Bos
MTTLRKLLLVGALLGAGAGVGTALFALVTPGEERKQAMLKEMPEQYPQRRDEAARTKELLLATLQEAAATQENVAWRKNWMSGGGGGGGGGGRSA
Required for the assembly of the ubiquinol-cytochrome c reductase complex (mitochondrial respiratory chain complex III or cytochrome b-c1 complex), mediating cytochrome b recruitment and probably stabilization within the complex. Thereby, plays an important role in ATP production by mitochondria. Cardiolipin-binding protein, it may also control the cardiolipin composition of mitochondria membranes and their morphology.
Q148G8
Q9FL26
WRKY8_ARATH
WRKY DNA-binding protein 8
Arabidopsis
MSHEIKDLNNYHYTSSYNHYNINNQNMINLPYVSGPSAYNANMISSSQVGFDLPSKNLSPQGAFELGFELSPSSSDFFNPSLDQENGLYNAYNYNSSQKSHEVVGDGCATIKSEVRVSASPSSSEADHHPGEDSGKIRKKREVRDGGEDDQRSQKVVKTKKKEEKKKEPRVSFMTKTEVDHLEDGYRWRKYGQKAVKNSPYPRSYYRCTTQKCNVKKRVERSYQDPTVVITTYESQHNHPIPTNRRTAMFSGTTASDYNPSSSPIFSDLIINTPRSFSNDDLFRVPYASVNVNPSYHQQQHGFHQQESEFELLKEMFPSVFFKQEP
Transcription factor. Interacts specifically with the W box (5'-TTGAC[CT]-3'), a frequently occurring stress-responsive cis-acting element. Functions as positive regulator of salt stress response. Binds the W box of LTI78/RD29A stress-response gene and directly regulates its transcription under salt stress. Functions antagonistically with VQ9 to regulate sodium and potassium homeostasis under salt stress by regulating the expression of downstream SOS (SALT OVERLY SENSITIVE) stress-responsive genes. The DNA-binding activity of WRKY8 is decreased by VQ9 . Functions as negative regulator of basal resistance to the bacterial pathogen P.syringae and as positive regulator of resistance to the fungal pathogen to B.cinerea . Functions as positive regulator of defense response againt tobamovirus (TMV) by regulating both the abscisic acid and ethylene signaling pathways. Positively regulates ABI4 expression and negatively modulates ACS6 and ERF104 expression by directly binding to the W box consensus motifs within their promoters .
Q9FL26
Q8NHX9
TPC2_HUMAN
Two pore calcium channel protein 2
Homo
MAEPQAESEPLLGGARGGGGDWPAGLTTYRSIQVGPGAAARWDLCIDQAVVFIEDAIQYRSINHRVDASSMWLYRRYYSNVCQRTLSFTIFLILFLAFIETPSSLTSTADVRYRAAPWEPPCGLTESVEVLCLLVFAADLSVKGYLFGWAHFQKNLWLLGYLVVLVVSLVDWTVSLSLVCHEPLRIRRLLRPFFLLQNSSMMKKTLKCIRWSLPEMASVGLLLAIHLCLFTMFGMLLFAGGKQDDGQDRERLTYFQNLPESLTSLLVLLTTANNPDVMIPAYSKNRAYAIFFIVFTVIGSLFLMNLLTAIIYSQFRGYLMKSLQTSLFRRRLGTRAAFEVLSSMVGEGGAFPQAVGVKPQNLLQVLQKVQLDSSHKQAMMEKVRSYGSVLLSAEEFQKLFNELDRSVVKEHPPRPEYQSPFLQSAQFLFGHYYFDYLGNLIALANLVSICVFLVLDADVLPAERDDFILGILNCVFIVYYLLEMLLKVFALGLRGYLSYPSNVFDGLLTVVLLVLEISTLAVYRLPHPGWRPEMVGLLSLWDMTRMLNMLIVFRFLRIIPSMKLMAVVASTVLGLVQNMRAFGGILVVVYYVFAIIGINLFRGVIVALPGNSSLAPANGSAPCGSFEQLEYWANNFDDFAAALVTLWNLMVVNNWQVFLDAYRRYSGPWSKIYFVLWWLVSSVIWVNLFLALILENFLHKWDPRSHLQPLAGTPEATYQMTVELLFRDILEEPGEDELTERLSQHPHLWLCR
(Microbial infection) Required for cell entry of coronaviruses SARS-CoV and SARS-CoV-2, as well as human coronavirus EMC (HCoV-EMC), by endocytosis.
Q8NHX9
P25295
TBG_SCHPO
Gamma-tubulin
Schizosaccharomyces
MGREIITLQAGQCGNQIGSQFWQQLCLEHGIGPDGTLESFATEGVDRKDVFFYQSDDTRYIPRAILIDLEPRVVNNILSDTYGSLYNPENILITKNGGGAGNNWANGYSHAERIFEDIMDMIDREADGSDSLEGFSLLHSIAGGTGSGLGSFLLERLNDRYPKKIIQTYSVFPNSQSVSDVVVQPYNSLLALKRLTLNADSVVVLDNAALAHIAADRLHTQNPTFHQQNQLVSTVMSASTTTLRYPGYMNNDLVSIIASLIPSPRCHFLLTSYTPFTNQQVEEAKAIRKTTVLDVMRRLLLPKNQMVSVNPSKKSCFISILDIIQGEADPADVHKSLLRIRERRYASFIPWGPASIQVALSKKSPYIKTNHRVSGLMLANHTSIASLFKRTLDQYDRLRKRNAFLEQYKKEAIFEDDLNEFDSSRDVVADLINEYEACEDPNYLSL
Tubulin is the major constituent of microtubules. The gamma chain is found at microtubule organizing centers (MTOC) such as the spindle poles or the centrosome, suggesting that it is involved in the minus-end nucleation of microtubule assembly.
P25295
Q8U1G7
UPP_PYRFU
UPRTase
Pyrococcus
MIEDKRWGGVYSFEDSPYIMEILTELRDKDTDSIKFRKGLVKLGRYMGYEITKTMDVEKVKVETPLEETEGIIVKDRRNVVIITVLRAAIPFMEGLIKVFEHARVGIVSAARGKPPKFEIEMNYIKIPQITPEDTVIVADPMIATGSTLLRVLEEVKKYGTPKRTLVVGVLAAPEGITRIKEKFPEVEIFVAKIDRELNDKGYILPGLGDAGDRAFGEPVKITTLPQVHYIE
Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
Q8U1G7
Q5R7Z3
TRAM1_PONAB
Translocating chain-associated membrane protein 1
Pongo
MAIRKKSTKSPPVLSHEFVLQNHADIVSCVAMVFLLGLMFEITAKASIIFVTLQYNVTLPATEEQATESASLYYYGIKDLATVFFYMLVAIIIHAVIQEYMLDKINRRMHFSKTKHSKFNESGQLSAFYLFACVWGTFILISENYISDPTILWRAYPHNLMTFQMKFFYISQLAYWLHAFPELYFQKTKREDIPRQLVYIGLYLFHIAGAYLLNLNHLGLVLLVLHYFVEFLFHISRLFYFSNEKYQKGFSLWAVLFVLGRLLTLILSVLTVGFGLARAENQKLDFSTGNFNVLAVRIAVLASICITQAFMVWKFINFQLRRWREHSAFQAPAVKKKPTVTKGRSSKKGTENGVNGTLTSNVADSPRNKKEKSS
Involved in the translocation of nascent protein chains into or through the endoplasmic reticulum (ER) membrane by facilitating the proper chain positioning at the SEC61 channel. Regulates the exposure of nascent secretory protein chain to the cytosol during translocation into the ER. May affect the phospholipid bilayer in the vicinity of the lateral gate of the SEC61 channel, thereby facilitating ER protein transport. Intimately associates with transmembrane (TM) domain of nascent membrane proteins during the entire integration process into the ER membrane. Associates with the second TM domain of G-protein-coupled receptor opsin/OPSD nascent chain in the ER membrane, which may facilitate its integration into the membrane. Under conditions of ER stress, participates in the disposal of misfolded ER membrane proteins during the unfolded protein response (UPR), an integrated stress response (ISR) pathway, by selectively retrotranslocating misfolded ER-membrane proteins from the ER into the cytosol where they are ubiquitinated and degraded by the proteasome.
Q5R7Z3
O32036
TRMR_BACSU
ho5U methyltransferase
Bacillus
MTDRYEQINDYIEALLKPRPDNVKRLEAYAEEHHVPIMEKAGMEVLLQILSVKQPKKILEIGTAIGYSAIRMALELPSAEIYTIERNEKRHEEAVNNIKEFQLDDRIHVFYGDALELADAVHVTAPYDVIFIDAAKGQYQNFFHLYEPMLSPDGVIITDNVLFKGLVAEDYSKIEPKRRRRLVAKIDEYNHWLMNHPDYQTAIIPVGDGLAISKKKR
Catalyzes the methylation of 5-hydroxyuridine (ho5U) to form 5-methoxyuridine (mo5U) at position 34 in tRNAs.
O32036
Q86ZP5
TBB_UNCNE
Beta-tubulin
Erysiphe
MREIVHLQTGQCGNQIGAAFWQTISGEHGLDGSGVYNGTSDLQLERTNVYFNEASGNKYVPRAVLVDLEPGTMDAVRAGPFGQLFRPDNFVFGQSGAGNNWAKGHYTEGAELVDQVLDVVRREAEGCDCLQGFQITHSLGGGTGAGMGTLLISKIREEFPDRMMATFSVVPSPKVSDTVVEPYNATLSVHQLVENSDETFCIDNEALYEICMRTLKLSNPSYGDLNHLVSAVMSGVTTCLRFPGQLNSDLRKLAVNMVPFPRLHFFMVGFAPLTSRGAHSFRAVTVPELTQQMYDPKNMMAASDFRNGRYLTCSAIFRGKVSMKEVEDQMRNVQNKNSAYFVEWIPNNVQTALCSIPPRGLKMSSTFVGNSTSIQELFKRVGDQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVHEYQQYQDASISEGEEDYEEEPQVENEE
Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Q86ZP5
A5VNL6
UREG1_BRUO2
Urease accessory protein UreG 1
Brucella
MTQKNGPLRVGIGGPVGSGKTTLTEKLCKAMRDKYSVAIITNDIYTQEDALILARRQALSEDRIIGVETGGCPHTAIREDASINLQAVVEMTRRFPDLDVVFIESGGDNLAATFSPDLADLTLYVISVCQGEEIPRKGGPGITRSDFLVINKSDLAPYVHVDLEVMEADAMRMRAKRPFGFTDLHRGKGVQEIIDFIVENGGLEPRSN
Facilitates the functional incorporation of the urease nickel metallocenter. This process requires GTP hydrolysis, probably effectuated by UreG.
A5VNL6
Q5E8U1
UBID_ALIF1
Polyprenyl p-hydroxybenzoate decarboxylase
Aliivibrio
MQYKDLRDFIGHLEDIGQLKRISHPIDPHYEMTEISDRTLRAGGPALLFENPIGYDIPVLTNLFGTPERVAIGMGRKDVLELREVGKLLAYLKEPEPPKGFKDALDKLPVFKQVLNMPTKNIRKAACQQIVWQGDDVDLDKVPVMSCWADDVAPLLTWGLTITKGPHKKRQNLGIYRQQKLSKNKVIMRWLAHRGGALDLRDWMETHPGEPFPVSVAFGADPATILGAVTPVPDTLSEYAFAGLLRGSRTEITKSISNDLEVPASAEIVLEGYIDPTEFADEGPYGDHTGYYNEVEKHHVFTVTHITMRKEPIYHSTYTGRPPDEPAVLGVALNEVFVPILQKQFPEIIDFYLPPEGCSYRMAVVTMKKQYPGHAKRVMMGVWSFLRQFMYTKFVLVCDEEVNARDWSQVTAAMSQHMDPARDSLMIENTPIDSLDFASPVVGLGSKMGLDITKKWEVELALSPNVECSLTSSEQIEGCIAEITKMCPEIIEIHLQNDNANMVVVSINKQAAGNAKKIMDAIWAQFEENKFVIVCDDDVNVSDWNDIIWAVTTRMDPARDTLFLQSVGETSKMGLDATNKWEGECLREWGTPIKKDPEVVAKIDSIWDELGIFK
Catalyzes the decarboxylation of 3-octaprenyl-4-hydroxy benzoate to 2-octaprenylphenol.
Q5E8U1
Q6H3Z3
YSL15_ORYSJ
Protein YELLOW STRIPE LIKE 15
Oryza sativa
MEHADADRTRVAPEIGSLHDEDAEADPARAREMERLQPWREQVTARGVVAAALIGFVFSVIVMKIALTTGLVPTLNISAALLAFLALRGWTRALERLGFSPRPFTRQENTVVQTCAVACYTIAFGGGFGSTLLGLNKRTYELAGNSPGNVPGSYKEPGIGWMVGLLLAISFAGNLSLIPLRKALVVDYKLTYPSGTATAVLINGFHTAQGDKNAKLQLHGFLKYFGLSLFWSFFQWFYTGGNACGFVQFPTFGLKAWKQSFFFDFSLTYVGAGMICSHLVNLSTLLGAVISWGIMWPLISKHKGDWYPANIPESSMTSLYGYKSFLCIALIMGDGLYHFVKVTGVTAKSLHNRFNRKSVSNTASEEGDMVSLDDLQRDEVFKRGTVPSWMAYSGYFLLSIIAVITIPIMFRQVKWYYVIIAYALGPVLGFANSYGAGLTDINMGYNYGKIALFVFAAWAGKDNGVIAGLVVGTLVKQLVLVSADLMHDLKTGHLTLTSPRSMLVGELIGTGIGCFIAPLTFMLFYRAFDIGNPDGYWKAPYALIYRNMAILGIEGISALPKHCLSLSVGFFAFAVLTNVARDALPARYKKLVPLPTAMAVPFLVGASFAIDMCVGSLVLFAWNKMNKKEAAFMVPAVASGLMCGDGIWTFPSSILALAKIKPPICMKFTPGS
Involved in Fe(3+) uptake from the rhizosphere and phloem transport of iron. Plays an important role in iron homeostasis during the early stages of growth. Transports Fe(3+)-phytosiderophore, but not Fe(3+)- or Fe(2+)-nicotianamine. May not transport other chelated metals.
Q6H3Z3
Q06708
VAC14_YEAST
Swollen vacuole phenotype 2 protein
Saccharomyces
MEKSIAKGLSDKLYEKRKAAALELEKLVKQCVLEGDYDRIDKIIDELCRDYAYALHQPMARNAGLMGLAATAIALGINDVGRYLRNILPPVLACFGDQNDQVRFYACESLYNIAKIAKGEILVYFNEIFDVLCKISADTENSVRGAAELLDRLIKDIVAERASNYISIVNNGSHGLLPAIKTDPISGDVYQEEYEQDNQLAFSLPKFIPLLTERIYAINPDTRVFLVDWLKVLLNTPGLELISYLPSFLGGLFTFLGDSHKDVRTVTHTLMDSLLHEVDRISKLQTEIKMKRLERLKMLEDKYNNSSTPTKKADGALIAEKKKTLMTALGGLSKPLSMETDDTKLSNTNETDDERHLTSQEQLLDSEATSQEPLRDGEEYIPGQDINLNFPEVITVLVNNLASSEAEIQLIALHWIQVILSISPNVFIPFLSKILSVLLKLLSDSDPHITEIAQLVNGQLLSLCSSYVGKETDGKIAYGPIVNSLTLQFFDSRIDAKIACLDWLILIYHKAPNQILKHNDSMFLTLLKSLSNRDSVLIEKALSLLQSLCSDSNDNYLRQFLQDLLTLFKRDTKLVKTRANFIMRQISSRLSPERVYKVISSILDNYNDTTFVKMMIQILSTNLITSPEMSSLRNKLRTCEDGMFFNSLFKSWCPNPVSVISLCFVAENYELAYTVLQTYANYELKLNDLVQLDILIQLFESPVFTRMRLQLLEQQKHPFLHKCLFGILMIIPQSKAFETLNRRLNSLNIWTSQSYVMNNYIRQRENSNFCDSNSDISQRSVSQSKLHFQELINHFKAVSEEDEYSSDMIRLDHGANNKSLLLGSFLDGIDEDKQEIVTPISPMNEAINEEMESPNDNSSVILKDSGSLPFNRNVSDKLKK
The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Regulates the synthesis of PtdIns(3,5)P2 by positive activation of FAB1 and by controlling FIG4 localization. Required for FIG4-mediated turnover of PtdIns(3,5)P2 after hyperosmotic shock. Essential for the control of trafficking of some proteins to the vacuole lumen via the multivesicular body (MVB), and for maintenance of vacuole size and acidity.
Q06708
Q9P0T7
TMEM9_HUMAN
Transmembrane protein 9
Homo
MKLLSLVAVVGCLLVPPAEANKSSEDIRCKCICPPYRNISGHIYNQNVSQKDCNCLHVVEPMPVPGHDVEAYCLLCECRYEERSTTTIKVIIVIYLSVVGALLLYMAFLMLVDPLIRKPDAYTEQLHNEEENEDARSMAAAAASLGGPRANTVLERVEGAQQRWKLQVQEQRKTVFDRHKMLS
Transmembrane protein that binds to and facilitates the assembly of lysosomal proton-transporting V-type ATPase (v-ATPase), resulting in enhanced lysosomal acidification and trafficking . By bringing the v-ATPase accessory protein ATP6AP2 and the v-ATPase subunit ATP6V0D1 together, allows v-ATPase complex formation and activation . TMEM9-controlled vesicular acidification induces hyperactivation of Wnt/beta-catenin signaling, involved in development, tissue homeostasis and tissue regeneration, through lysosomal degradation of adenomatous polyposis coli/APC . In the liver, involved in hepatic regeneration .
Q9P0T7
C3P1B4
TAGU_BACAA
Polyisoprenyl-teichoic acid--peptidoglycan teichoic acid transferase TagU
Bacillus cereus group
MKKKILFWVLGILGVLIIGGGIYAYNVYSSVSNTLKEVHQPLKRDQNNSNVGEKVSKSEPVSILLLGADERGEDKGRSDSLMVITLNPKNNSMKTVSIPRDTYTEIVGKGKSDKINHAYAFGGVDMSVATVENFLNVPINYYIEVNMEGFKDIVDAVGGVDVKNDLEFTQDGHHFAKGNIHLTGDQALAFTRMRKQDPRGDFGRQMRQRQVMQGVIKKGASFSSLTGYGDVLSAIQKNVKTNLTQDQMFDMQKNYKDCLKNSEDIQIPGDGHKAADGIWYYYVPDAAKQDLTNKLRTHLEVTK
May catalyze the final step in cell wall teichoic acid biosynthesis, the transfer of the anionic cell wall polymers (APs) from their lipid-linked precursor to the cell wall peptidoglycan (PG).
C3P1B4
A8ACY2
UBIE_CITK8
Demethylmenaquinone methyltransferase
Citrobacter
MVEDSQETTHFGFQTVAKEQKADMVAHVFHSVASKYDVMNDLMSFGIHRLWKRFTIDCSGVRRGQTVLDLAGGTGDLTAKFSRLVGETGNVILADINDSMLKMGREKLRNIGVIGNVKYVQANAEALPFPDNTFDCITISFGLRNVTEKEKALRSMYRVLKPGGRLLVLEFSKPIIEPLSKAYDAYSFHILPRIGSVVANDADSYRYLAESIRMHPDQDTLKAMMQDAGFESVDYYNLTAGVVALHRGYKF
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).
A8ACY2
O13059
VSP1_TRIGA
Snake venom serine protease 1
Trimeresurus
MVLIRVLANLLILQLSYAQKSSELVVGGDECNINEHRSLVAIFNSTGFFCSGTLINQEWVVTAAHCDSNNFKMKFGAHSQKVLNEDEQIRNPKEKFICPNKKNNEVLDKDIMLIKLDSSVSNSEHIAPLSLPSSPPSVGSVCRIMGWGSITPTKVTYPDVPYCANINLLDDAECKPGYPELLPEYRTLCAGIVQGGKDTCGGDSGGPLICNGQFHGIVSYGAHPCGQSLKPGIYTTVFDYNDWIKSIIAGNTAATCPP
Snake venom serine protease that may act in the hemostasis system of the prey.
O13059
P42724
TFXB_RHILT
Trifolitoxin-processing protein TfxB
Rhizobium
MDFVQRFVIDRSFHLRYYSLDAYLYRAVDQVAWDADITHNRLFWDIWSAFMQPRSLVDAVETLSDYDPDEVAAAIEGMCESGIIEPVGLKDRQFDPLTVELSHVPQAWDYHLVSSRIDWINYLDGKDVKRQDLEQMDKHLSEEAVPSNFHKAANSRPKYDLPSLVPLTAFEFNNSASVAFGHEKAPLPNELSLDIITLLLNYAAAKTDTVNMYATGEHLRKAVPSGGARHPIEFYVVVGDEIAGIEAGVYHYNVRHHRLDAIEIASTSLKALQEASSVLPRSRSKPFGFAFIHTCRFERSMFRYREPRSYRVMQFDLGHIHANEVLAAKILGLDFSETFSVPESIVESVLTLDPFIESAMSAFVVHRHENHHD
The actions of the proteins TfxB, TfxD and TfxF are implicated in the processing of the inactive trifolitoxin (TfxA) precursor into the active peptide.
P42724
Q2SPJ7
TRHO_HAHCH
tRNA hydroxylation protein O
Hahella
MSQYVICALYKFVALDNFEALRAPLLEVMEKNEVKGTLLLAREGVNGTVSGTREGMDALLAWLKSDPRLADLSYKESYDENIPFYRTKVKLKKEIVTMGVEGIDPKRVVGTYVKPQDWNALITDPEVLLIDTRNDYEVQIGKFKNAINPNTETFREFPDYVKSNLDPAKHKKVAMYCTGGIRCEKSTAYLKELGFEDVYHLEGGILKYLEDVPQEESTWEGECFVFDNRVAVDHSLNKGSYDQCHACRMPISAEDMQSEHYKKGVSCPHCYDKVSEDQLRRFAAREQQIELAKSRGEEHIGSEAAKAIKKRQAEKKLKRKNYHQHLTQGAE
Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs.
Q2SPJ7
P06016
VSAC_TRYBB
Variant surface glycoprotein ANTAT 1.1C
Trypanosoma
LHPQQALAQTAGRPLADVVGKTLCTYSKTAKRQAANLAQTLQRASSAAKQSRQAQQLAALALAKLPDYKEAAATLLIYATHKIQDAQASIENWTGENTKLVGQAMYSSGRIDELMLLLEGHREDGANGQDKTCLGAAAGGNTVNEFVKTECDTESGHNIEADNSNIGQAATTLSQESTDPEASGGASCKITANLATDYDSHANELPLLGGLLTIHNAGGFKTGQSLQTAAPTNKLISALKNKGAGVAAKLATVTSAAPTSKQELKTLLASKGERAKLQAANDEYNNWKPGAKPEDFDAHIKKVFGAEDGKDSAYALALEGISIEVPQKPGTTESKQLYSMQPKDLMAALIGTIAEIQKAAATKAPCPKHKLTSAESDALCSKIKDANECNSKPFCSYNSTETDTAKKCQFNETKADKSGVSLPKTGPTGTEATTDKCKDKTKDECKSPNCKWEGETCKDSSILVTKKFALSLVSAAFASLLF
VSG forms a coat on the surface of the parasite. The trypanosome evades the immune response of the host by expressing a series of antigenically distinct VSGs from an estimated 1000 VSG genes.
P06016
A1VES8
XGPT_DESVV
Xanthine phosphoribosyltransferase
Desulfovibrio
MSTADRYRKVFPVTWEQLHRDAKALSWRLLEKGPYKGIIAIARGGLVPAAVIARELDIHLVETICISSYQWQEQTSSHKVLKTVEGRGEGWLIIDDLVDTGGTARLVREMLPEAHFATVYAKPAGRPLVDTFITEVSQDTWILFPWDSEVQYVVPLVNQPQQS
Purine salvage pathway enzyme that catalyzes the transfer of the ribosyl-5-phosphate group from 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to the N9 position of the 6-oxopurines guanine and xanthine to form the corresponding ribonucleotides GMP (guanosine 5'-monophosphate) and XMP (xanthosine 5'-monophosphate), with the release of PPi. To a lesser extent, also acts on hypoxanthine.
A1VES8
C1DH67
TRPA_AZOVD
Tryptophan synthase alpha chain
Azotobacter
MSRLQTRFAELKQADRAALVTFVTAGDPDYETSLAILKGLPEAGADVIELGMPFTDPMADGPAIQLANIRALGAGQNLVKTLRMVRAFREGDRTTPLVLMGYFNPIHYYGVERFIAEAREAGVDGLIVVDLPPEHNEDLCDPAQAAGLDFIRLTTPTTDDKRLPRVLAGSSGFVYYVSVAGVTGAHAASLEHVEQAVARLRRHTDLPLCIGFGIRSPEHAGSVARLAEGVVVGSALVDRIAKAGSKEQAVGDVLGLCRELAEGVRRARR
The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
C1DH67
P32966
UVRC_PSEPH
Excinuclease ABC subunit C
Pseudomonas
MTDPFDPSAFLSTCSGRPGVYRMFDSDTRLLYVGKAKNLKSRLASYFRKTGLAPKTAALVGRIAQIETTITANETEALLLEQTLIKEWRPPYNILLRDDKSYPYVFLSDGEFPRFSIHRGAKKQKGKYFGPYPSAGAIRESLSLLQKTFMVRQCEDSYYKNRTRPCLQYQIKRCKAPCVGLVEAEVYAEDVRHSVMFLEGRSNALTDELSAGMEQAASTLDFEKAAELRDQISLLRRVQDQQSMEGGSGDVDVVAAFVNPGGACVHLISVRGGRVLGSKNFFPQVGIEEEVAEVMSAFLGQYFLSSPERDLPSELIVNVVHEDFPALIAAIQELRGRELSISHRVRGTRARWQQLAVTNAEQALSARLANRQHVAARFEALAEVLNLDEPPQRLECYDISHSSGEATVASCVVFGPEGPLKSDYRRYNIEGVTAGDDYAAMHQALTRRFSKLKDGEGKLPDILLVDGGKGQLSMARDVLNELAVPDLILLGVAKGATRKTGFETLYLNDAAHEFTLKGDSPALHLIQQIRDEAHRFAITGHRARRGKTRRTSTLEDVAGVGPKRRRDLLKHFGGLQELSRASIEEIAKAPGISKKLAELIYANLHSE
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision.
P32966
O26981
THIRX_METTH
Thioredoxin
Methanothermobacter
MMKIQIYGTGCANCQMLEKNAREAVKELGIDAEFEKIKEMDQILEAGLTALPGLAVDGELKIMGRVASKEEIKKILS
Does not function as a glutathione-disulfide oxidoreductase in the presence of glutathione and glutathione reductase. Has low thioredoxin activity in vitro.
O26981
B7N528
YDIB_ECOLU
NAD-dependent shikimate 5-dehydrogenase
Escherichia
MDVTAKYELIGLMAYPIRHSLSPEMQNKALEKAGLSFTYMAFEVDNDSFPGAIEGLKALKMRGTGVSMPNKQLACEYVDELTPAAKLVGAINTIVNDDGYLRGYNTDGTGHIRAIKESGFDIKGKTMVLLGAGGASTAIGAQGAIEGLKEIKLFNRRDEFFDKALAFAQRVNENTDCVVTVTDLADQQAFAEALASADILTNGTKVGMKPLENESLVNDISLLHPGLLVTECVYNPHMTKLLQQAQQAGCKTIDGYGMLLWQGAEQFTLWTGKDFPLEYVKQVMGFGA
The actual biological function of YdiB remains unclear, nor is it known whether 3-dehydroshikimate or quinate represents the natural substrate. Catalyzes the reversible NAD-dependent reduction of both 3-dehydroshikimate (DHSA) and 3-dehydroquinate to yield shikimate (SA) and quinate, respectively. It can use both NAD or NADP for catalysis, however it has higher catalytic efficiency with NAD.
B7N528
Q56242
UVRA_THET8
Excinuclease ABC subunit A
Thermus
MDRIVIRGAREHNLKNISLELPRGKFIVITGVSGSGKSTLAFDTIYAEGQRRYVESLSSYARQFLGVMDKPEVESIEGLSPAISIDQKTTSHNPRSTVGTVTEIHDYLRLLFARVGQAFCPECGRPIEKQSASEITDRLLKRPPGTRAILMAPLVRGRKGEYRKLFQQLLKEGYARVRVDGVIYLLEEAQGLSLEKYEKHDIDLVIDRVVLKEEERPRIAEAVELALLRGEGLLRVLYPDTGEEELFSEKFACPEHGSVLEELEPRIFSFNSPYGACPACSGLGYRQEFDPELVVNPELSLAEGAILPWSRGRDTGRSYLWDRLRALAEHLGFDLKTPFKDLPEEAKRAVLYGLPEPFEVVFRRGGKETFRVEVRYEGVIPWLEKRYQESDSEGVREALEGFMSLRPCPACGGTRYKREVLSVKVAGRNIAEVSALPVREALAFFQGLEKTLPPFQAQIARPILREIVERLGFLVDVGLDYLTLDRAANTLSGGEAQRIRLATQVGSGLTGVLYVLDEPSIGLHPRDNQRLIRTLKRLRDLGNTLIVVEHDEETMRAADWIVDMGPGAGIHGGEVVAQGTLEDILKSPQSLTGAYLRGEKRIPVPKERRKGNGKWLVLKGARAHNLKNVTLRIPLGRFVAITGPSGSGKSTLVHDVLYAALAQRLMRAKTTPGPYEALEGVEHLDKVIEIDQSPIGRTPRSNPATYTGVFDEIRDLFAKTPEARKRGYGPGRFSFNVKGGRCEACGGDGTVKIEMLFLPDLYVPCEVCKGKRYNKETLEVKLRGKSIADVLDMTVEEALDFFQNVPSIARKLQLMVDVGLGYMKLGQPSPTLSGGEAQRIKLATELGRKATGRTLYILDEPTTGLHFDDVAKLLSVLHRLVDAGNTVVVIEHNLDVVKTADWVIDLGPEGGDRGGEIVAEGTPEEVALTGSPTGAFLARIPEIAARIGVAAD
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.
Q56242
Q2S1Z6
TRPD_SALRD
Anthranilate phosphoribosyltransferase
Salinibacter
MNTLLQTIADGDPLSRPEAEEAMATMMSGSARDEHIAALLMGLRTRGETLDELVGFTKTMREFAVSVETDDPQTIDLCGTGGDGASTFNISTTASFIAAGAGATVAKHGNRSVSSQSGSADVLEALGVQIDLEKEGVEHCLHEAGIAFLFAPFFHPAMRHVMPVRKALGVRTFFNILGPLCNPAGVTRQIVGAFDTSTAQTMVRILAELDADHVITLHADDGLDEVSISASTTLFEYDASDQNPVPRSHEVGPERHDLDRASISTLEGGTAQQNASILRNILSGEDQGPRRDVALLNAAYALHVSDQYADLDACLEAAAESIDSGAALDALNTLASVSKEAKSE
Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
Q2S1Z6
G3X9G7
ZN809_MOUSE
Zinc finger protein 809
Mus
MGLVSFEDVAVDFTLEEWQDLDAAQRTLYRDVMLETYSSLVFLDPCIAKPKLIFNLERGFGPWSLAEASSRSLPGVHNVSTLSDTSKKIPKTRLRQLRKTNQKTPSEDTIEAELKARQEVSKGTTSRHRRAPVKSLCRKSQRTKNQTSYNDGNLYECKDCEKVFCNNSTLIKHYRRTHNVYKPYECDECSKMYYWKSDLTSHQKTHRQRKRIYECSECGKAFFRKSHLNAHERTHSGEKPYECTECRKAFYYKSDLTRHKKTHLGEKPFKCEECKKAFSRKSKLAIHQKKHTGEKPYECTECKKAFSHQSQLTAHRIAHSSENPYECKECNKSFHWKCQLTAHQKRHTGVTYFQEVVFQQITVSDWTGNLSENGPHRPTWTWAYGIMDFVKAWSRCIIGGGL
Transcription factor specifically required to repress retrotransposons in embryonic stem cells. Recognizes and binds retroviral DNA sequences from a large subset of mammalian retroviruses and retroelements and repress their expression by recruiting a repressive complex containing TRIM28/KAP1 .
G3X9G7
P18725
ZG5_XENLA
XlCGF5.1
Xenopus
MLQIKTEKEELDCGDDQNPKESSAVPLTDGASPEPQPQILQIKIKEEEPDYEYYLPTIKREMDPVPGAASPLAESEILQIKIKEEEPDSEDDGNSAATSAVTFRDWDNCWSDEENWDDSRPQLNQYNSDFPGSADTANTPAINTVLSRGNGLFVVNQEKRVATNSSCQSDTGHVDCSVGSEPSGFICCKCGDSFAHHSDLHTHLYACAGHNITSSFTNASEEGQHSHKNGGVLPREKPFKCTVCGKCFTLKNSLQLHHRIHTGEKPFTCTECGKSFAQSCSLQLHSRTHTGYNPYVCTECGKRFSSNSGLRRHMRTHTGVKPYACKECGKFFSDLSTLHRHQNSHKGEKPFICTECGKGFTLKDSLHRHQRTHTGEKPFICSQCGKSYSQSSNLIKHQMIHTGVKPFSCSECGKCFAVKDGLRNHQRVHMRRNYSAAQNVAEFSL
Binds to RNA homomers.
P18725
B1JVZ5
UBIA_BURCC
4-HB polyprenyltransferase
Burkholderia cepacia complex
MLARFPLYLRLVRMDKPIGSLLLLWPTLNALWIASDGRPRWPLLVIFTLGTLLMRSAGCAMNDYADRDFDRHVKRTADRPLTSGKIRAWEAVAIAVGLSFIAFLLILPLNTLTKELSVVALFVAGSYPFMKRFFAIPQAYLGIAFGFGIPMAFAAVQDTVPMLAWVMLVANIFWSVAYDTEYAMVDRDDDIKIGIRTSALTFGRFDVAAVMACYAATLGIYVWIGVTLGFGLAYWAGWAAAVGCALYHYTLIKDRERMPCFAAFRHNNWLGGVLFAGIAVHYLLAGN
Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 3-octaprenyl-4-hydroxybenzoate.
B1JVZ5
Q0BI45
UBIA_BURCM
4-HB polyprenyltransferase
Burkholderia cepacia complex
MLARFPLYLRLVRMDKPIGSLLLLWPTLNALWIASDGHPRWPLLAIFVLGTLLMRSAGCAMNDYADRDFDRHVKRTADRPLTSGKIRAWEAVAIAVVLAFISFLLIQPLNTLTKELSVVALFVAGSYPFMKRFFAIPQAYLGIAFGFGIPMAFAAVQDTVPMLAWVMLIANIFWSVAYDTEYAMVDRDDDIKIGIRTSALTFGRFDVAAVMLCYAATLGIYVWIGVTLGFGLAYWAGWAAAVGCALYHYTLIKDRERMPCFAAFRHNNWLGGVLFAGIAAHYLLAGTAGN
Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 3-octaprenyl-4-hydroxybenzoate.
Q0BI45
B3QLU3
TAL_CHLP8
Probable transaldolase
Chlorobaculum
MKFFIDTASLDEIKAANELGVLDGVTTNPSLIAKIVKDPANFTYADFKAHIKKICDIVDGPVSAEVTTLKAEEMIAQGEELAAIHENVVIKCPLTVEGLKAIKHFSSNGIKTNATLVFSPTQALLAAKAGADFVSPFVGRLDDISTNGMELVKQIVTIYDNYGYLTEVIVASVRNPLHVVESAMVGADIATIPYSVIKQLANHPLTDKGLEKFMEDAGVMKP
Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
B3QLU3
A8GF80
TRPD_SERP5
Anthranilate phosphoribosyltransferase
Serratia
MQTILEKLYRSESMNQQESQQLFSAIVRGELEPSQLAAALISMKIRGEHPEEIAGAAKALLADALPFPRPDYPFADIVGTGGDGTNSINISTASAFVAAACGAKVAKHGNRSVSSRSGSSDLLAAFGIRLDLPAEEARKALDELGVCFLFAPQYHTGFRHAMPVRQQLKTRTVFNVLGPLINPARPPLALIGVYSPELVLPIAETLRVLGYQRAAVVHGGGMDEVAIHATTHVAELNNGEIESYQLTPQSFGLQSYPLEALLGGSPEENRDILARLLQGKGDPAHAAAVAANVALLLKLFGHEDLRQNAQQALDMIHSGQAYERVTALAARG
Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
A8GF80
Q6P2B1
TNPO3_MOUSE
Transportin-3
Mus
MEGAKPTLQLVYQAVQALYHDPDPSGKERASFWLGELQRSVHAWEISDQLLQIRQDVESCYFAAQTMKMKIQTSFYELPTDSHASLRDSLLTHIQNLKDLSPVIVTQLALAIADLALQMPSWKGCVQTLVEKYSNDVTSLPFLLEILTVLPEEVHSRSLRIGANRRTEIIEDLAFYSSTVVSLLMTCVEKAGTDEKMLMKVFRCLGSWFNLGVLDSNFMANNKLLALLFEVLQQDKTSSNLHEAASDCVCSALYAIENVETNLPLAMQLFQGVLTLETAYHMAVAREDLDKVLNYCRIFTELCETFLEKIVCTPGQGLGDLRTLELLLICAGHPQYEVVEISFNFWYRLGEHLYKTNDEVIHSIFKAYIQRLLHALARHCQLEPDHEGVPEETDDFGEFRMRVSDLVKDLIFLIGSMECFAQLYSTLKEGNPPWEVTEAVLFIMAAIAKSVDPENNPTLVEVLEGVVHLPETVHTAVRYTSIELVGEMSEVVDRNPQFLDPVLGYLMKGLCEKPLASAAAKAIHNICSVCRDHMAQHFNGLLEIAHSLDSFMLSPEAAVGLLKGTALVLARLPLDKITECLSELCSVQVMALKKLLSQEPSNGISSDPTVFLDRLAVIFRHTNPIVENGQTHPCQKVIQEIWPVLSETLNKHRADNRIVERCCRCLRFAVRCVGKGSAALLQPLVTQMVNVYHVHQHSCFLYLGSILVDEYGMEEGCRQGLLDMLQALCIPTFQLLEQQNGLQNHPDTVDDLFRLATRFIQRSPVTLLRSQVVIPILQWAIASTTLDHRDANSSVMRFLRDLIHTGVANDHEEDFELRKELIGQVMSQLGQQLVSQLLHTCCFCLPPYTLPDVAEVLWEIMQVDRPTFCRWLENSLKGLPKETTVGAVTVTHKQLTDFHKQVTSAEECKQVCWALRDFTRLFR
Importin, which transports target proteins into the nucleus. Specifically mediates the nuclear import of splicing factor serine/arginine (SR) proteins, such as RBM4, SFRS1 and SFRS2, by recognizing phosphorylated SR domains. Also mediates the nuclear import of serine/arginine (SR) protein CPSF6, independently of CPSF6 phosphorylation. The nuclear import process is regulated by the small GTPase Ran that partitions between cytoplasm and nucleus in the predominantly GDP- and GTP-bound form, respectively. Importin associates with target cargo proteins in the cytoplasm, and the competitive binding of GTP-bound Ran induces the release of cargos in the nucleus.
Q6P2B1
Q969M1
TM40L_HUMAN
Protein TOMM40-like
Homo
MGNTLGLAPMGTLPRRSPRREEPLPNPGSFDELHRLCKDVFPAQMEGVKLVVNKVLSSHFQVAHTIHMSALGLPGYHLHAAYAGDWQLSPTEVFPTVVGDMDSSGSLNAQVLLLLAERLRAKAVFQTQQAKFLTWQFDGEYRGDDYTATLTLGNPDLIGESVIMVAHFLQSLTHRLVLGGELVYHRRPGEEGAILTLAGKYSAVHWVATLNVGSGGAHASYYHRANEQVQVGVEFEANTRLQDTTFSFGYHLTLPQANMVFRGLVDSNWCVGAVLEKKMPPLPVTLALGAFLNHWRNRFHCGFSITVG
Potential channel-forming protein implicated in import of protein precursors into mitochondria.
Q969M1
F6HH45
TRM52_VITVI
tRNA methyltransferase 5 homolog 2
Vitis
MLLDESKFDLQLKLWALRIPSQLCKVASRILNGYLLDKPRVKPITEDPTCETNRYIILSERIKNPDLSDIPEDKRDELKVLCKIEVVPYSLTLGYSYWSADHVLKQILPDGVEVPSSFETITFSLCHIAHLNITGELLPYKDVIAKVIYDKNYPRIKTVVNKVGTITNEFRVPKFEILVGKDDMVTEVKQYRATFKLDYSLVYWNSRLEHEHMRLVSQFRPGQIICDMFSGVGPFAIPAAQKGCLVYANDLNPDSIRYLKINAKINKVDDNIWAYNMDARKFISQLMEVPVHEILPEPDVPVLKATEECSIQANVQTESQNGGLTVEAIGVHSDDSSNMDGIEGSCTVADDTVAAVKKHSGSCEEENGTYDNATVSVVGRRKDRMNKRMRGSESSSNIKPWEHVDHVIMNLPASAIQFLDAFRGLIQRKYWKGSLPWIHCYCFIRANETNEMIISEAETALNASIQEPILHRVRDVAPNKAMFCLSFRLSEEACFKEDATKSLLDSSGDL
Specifically methylates the N1 position of guanosine-37 in various cytoplasmic and mitochondrial tRNAs. Methylation is not dependent on the nature of the nucleoside 5' of the target nucleoside. This is the first step in the biosynthesis of wybutosine (yW), a modified base adjacent to the anticodon of tRNAs and required for accurate decoding.
F6HH45
C0HLF6
TOP1C_OXYTA
Oxyopinin-1c
Oxyopes
FRGLAKLLKIGLKSFARVLKKILPKAAKAGKSLAKSLADENAIRQQNQ
Disrupts cell membranes, particularly those rich in phosphocholine, through formation of pores. Has antimicrobial activity, hemolytic activity and insecticidal activity.
C0HLF6
Q2HJE9
TI17B_BOVIN
Mitochondrial import inner membrane translocase subunit Tim17-B
Bos
MEEYAREPCPWRIVDDCGGAFTMGVIGGGVFQAIKGFRNAPVGMRHRLRGSVNAVRIRAPQIGGSFAVWGGLFSTIDCGLVRLRGKEDPWNSITSGALTGAVLAARSVPLAMVGSAMMGGILLALIEGVGILLTRYTAQQFRNAPPFLEDPGQLPSKEGTPGPGYPSYQQYH
Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane.
Q2HJE9
B1YTH7
UBIA_BURA4
4-HB polyprenyltransferase
Burkholderia cepacia complex
MLARFPLYLRLVRMDKPIGSLLLLWPTLNALWIASDGHPRWPLLAIFALGTLLMRSAGCAMNDYADRDFDRHVKRTADRPLTSGKIRAWEAVAIAVVLAFISFLLIQPLNTLTKELSVVALFVAGSYPFMKRFFAIPQAYLGIAFGFGIPMAFAAVQDTVPMLAWVMLIANIFWSVAYDTEYAMVDRDDDIKIGIRTSALTFGRFDVAAVMLCYAATLGIYVWIGVTLGFGLAYWAGWAAAVGCALYHYTLIKDRERMPCFAAFRHNNWLGGVLFAGIAAHYLLAGTAGN
Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 3-octaprenyl-4-hydroxybenzoate.
B1YTH7
B2I7X4
TSAD_XYLF2
tRNA threonylcarbamoyladenosine biosynthesis protein TsaD
Xylella
MKIIGIESSCDETGVAVYDTALSGSAALRAHSVYSQVALHAEYGGVVPELASRDHVRKLLPLLRQTLAEAKLSVEELDGVAYTAGPGLVGALLVGAGVARALAWALEVPAIGVHHMEGHLLSPLLEDDPPEVPFVALLVSGGHTQLVAVDAIGDYRLLGETLDDAAGEAFDKVAKLMGLPYPGGPQLAALAERGIPGRFCFTRPMVDRPGLDFSFSGLKTQVLLAWRNSDQSDAIRVDVARGFEDAVVDTLAIKCERALDTVACQTLVVAGGVGANKCLRARLQAMCRQRGGRACFPRPALCTDNGAMIAFAGALRLQAGQQSDVAVRVTPRWDMAALPPLVSRSCRR
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.
B2I7X4
A8MXK1
VSTM5_HUMAN
V-set and transmembrane domain-containing protein 5
Homo
MRPLPSGRRKTRGISLGLFALCLAAARCLQSQGVSLYIPQATINATVKEDILLSVEYSCHGVPTIEWTYSSNWGTQKIVEWKPGTQANISQSHKDRVCTFDNGSIQLFSVGVRDSGYYVITVTERLGSSQFGTIVLHVSEILYEDLHFVAVILAFLAAVAAVLISLMWVCNKCAYKFQRKRRHKLKESTTEEIELEDVEC
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.
A8MXK1
Q54ZX8
Y7331_DICDI
SET and MYND domain-containing protein DDB_G0277331
Dictyostelium
MIPNNINNRKKLKLPELFKEKYGFNKKGIELRYCDGEKGMGIFSNRKFNKGEKIMKIEPYVWSVAKHAIVCDECLKNKLDLEEGKTLKRCSNCKLVYYCSTDCQTKAWKIHKQECKILSTIPSTTDKKNINTKSTTMLLRLFIKRNLELINNNNNNNNNNNNNNNNNDNHITGQYEIIDGLLNHKDIRSDNNEYKSFSSGFCSLLGEDPQLKAPIVLEYLLKLEPNCITIPRCEASSIGLYPLMLFFNHSCKPNISIINNRKELLIITNKIIEKDEELFINYSPAICYRNERLDNLKQCFFFNCKCTLCLGEEKIKSKDLYITCNINNCGGRINQEIDININNNNNNNNNNNNNSNNNNNNNNSNEEILKCYKCLKVYKGQEKDEILKKKLIIKNLQNKLSTNTDQININQEFKSLLELYCKEIHPTDPLFYEIVNKTQLFYLGNNNKFISDNELSTIYHPRYQIMIKYHLLQVQNLEYEYCRQMLDYVNTLATTSYFKDALNILTDLMSNHLSQIDFYGFNRDELLSLLYNLQHEYKNNIKTSRKIIN
Probable methyltransferase.
Q54ZX8
Q12TL1
TRPD_METBU
Anthranilate phosphoribosyltransferase
Methanococcoides
MKYYLQKLIDGHDLSMVESEAAMGQILESATDAQVGAFVMGMKMKGETSDEVAGFAKGMLNVANMIRPKVDGILVDTCGTGGDRHNTINISTAAAIVAAAAGVTVAKHGNHSFTSLSGSADVFKELGVKIDLEPDLVKSSIEDIGIGFMLAPKFHPAMKRMVGPRKELAVRTMFNILGPLTNPTGAKAQVIGVFDKDLCNLMAEVLKKLGKEHVMVFHGDGMDEISTLSETFVAELKDGIISNYTLTPEELGVARAKATDIVGGTPEENAHDLLYILNGEKGAKRDIVVVNAAAAIYVAGLAISIKDAIPLAEEAIDSRKALNKLKELVEFTSGNKVDNEAFNTGQSLRNEVC
Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
Q12TL1
Q04W54
TRMB_LEPBJ
tRNA(m7G46)-methyltransferase
Leptospira
MSQDLEQKLWSIASGIPFVSDYFLQASPARKLKKENLFSKVFETYFLELGSGWGEVAIAMALQRRNTGFVLMEKKFDRIRHTIREIEKHSLDNVKILCVNFNWFLADVFEENLFSEILLNFPDPWPKKRHHKKRTINSKFIESLRVLLPEKGKFSFATDYGPYARKTIRLFRDSEIFKPETMEFRLERKEIPVSHFERKKRKEGKRIYYIDQILIRK
Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Q04W54
Q21VT9
YCIB_ALBFT
Inner membrane-spanning protein YciB
Rhodoferax
MKILIDFFPILLFFGAYKAYDIYIGTGVLMAATLIQMGLIYTLDRKLTVMHKITLALILVFGTLTLVLHDERFIKWKPTVLYAAMAIGLALAVWVWKKNFLKLLLGSQMELPDPVWMRLNMVWVVYCVFMSLINAYVAAYYSTEAWVNFKLWGYAFPLVFIVAQGFYISRYLKTDEPKA
Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis.
Q21VT9
A5PJS6
UBP10_BOVIN
Ubiquitin-specific-processing protease 10
Bos
MALRSPQYIFGDFSPDEFNQFFVTPRASVELPPYGGTVLCGAQAADDLPDGHDYQRIEFGVNEVIEPSDTLPRTPNYSISSTLNPQAPEFILSCTTSKKLPDDIDKEVNYSSANCQYPGPALALDGGSPAEAEALENDGVSGGLGQRERKKKKKRPPGYYSYLKDGGEGGPSAEALVNGHAGPAVSNSVGAEDTDLMGDVPTAGTPRTWGSPQDATDFVSDAGPAGAFPGALDGGARTAGQLEGCPGADSEASCLPAEAGRDTLLRTAVAQPSVGTDTTENLGVTNGQILESLGEGTAANGVELHTVESSDSDPAKAESAPPPADAPASAAGTVPASQPAKSWASLFHDSKPSSSSLPVVSVETKYSPPATSPLVSEKQAEVKEGLVPVSEDPVAIKIAELLENVTLIHKPVSLQPRGLINKGNWCYINATLQALVACPPMYHLMKLIPLYSKVQRPCTSTPMIDSFVRLMNEFTNMPVPPKPRQALGDKIVRDIRPGAAFEPTYIYRLLTVIKSSLSEKGRQEDAEEYLGFILNGLHEEMLNLKKLLSPNNDKLTISNGPKSHSVNEDEQEEPGEGSEDEWEQVGPRNKTSVTRQADFVQTPITGIFGGHIRSVVYQQSSKESATLQPFFTLQLDIQSDKIRTVQDALESLVARESVQGYTTKTRQEVEISRRVTLEKLPPVLVLHLKRFVYEKTGGCQKLIKNIEYPVDLEISKELLSPGVKNKNFKCHRTYRLFAVVYHHGSSATGGHYTTDVFQIGLNGWLRIDDQTVKVVSQQQVVRPAAERTAYLLYYRRVDLL
Hydrolase that can remove conjugated ubiquitin from target proteins such as p53/TP53, BECN1, SNX3 and CFTR. Acts as an essential regulator of p53/TP53 stability: in unstressed cells, specifically deubiquitinates p53/TP53 in the cytoplasm, leading to counteract MDM2 action and stabilize p53/TP53. Following DNA damage, translocates to the nucleus and deubiquitinates p53/TP53, leading to regulate the p53/TP53-dependent DNA damage response. Component of a regulatory loop that controls autophagy and p53/TP53 levels: mediates deubiquitination of BECN1, a key regulator of autophagy, leading to stabilize the PIK3C3/VPS34-containing complexes. In turn, PIK3C3/VPS34-containing complexes regulate USP10 stability, suggesting the existence of a regulatory system by which PIK3C3/VPS34-containing complexes regulate p53/TP53 protein levels via USP10 and USP13. Does not deubiquitinate MDM2. Deubiquitinates CFTR in early endosomes, enhancing its endocytic recycling. Involved in a TANK-dependent negative feedback response to attenuate NF-kappaB activation via deubiquitinating IKBKG or TRAF6 in response to interleukin-1-beta (IL1B) stimulation or upon DNA damage. Deubiquitinates TBX21 leading to its stabilization.
A5PJS6
Q07VB6
UBIG_RHOP5
3-demethylubiquinone 3-O-methyltransferase
Rhodopseudomonas
MAMQSETPGNPASTVDPAEIAKFSKLSAEWWDPTGRMAPLHKINPHRVAFIRDAACRKFDRNPKSLNSLAGLRMIDIGCGAGLLCEPFTRLGAQVIGIDPSATNIAAAKVHAEKSRLLIDYRNTTAEAMDPRERFDIVLAMEVIEHVTDVGAFLGRCAAMMKPTGLMVVATLNRNWKSFALAIVGAEYVMRWLPRGTHQWDKFVTPEELTRHLQNSRLAVTEQAGLVYNPLADKWNLSADMDVNYMMVAESAG
O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.
Q07VB6
P58923
U7A_CONTU
Conotoxin TVIIA
Gastridium
SCSGRDSRCPPVCCMGLMCSRGKCVSIYGE
By structural similarity with conotoxin GS, may inhibit the sodium channel (Nav). No effect was observed upon intracranial injections into mice and intraperitoneal injections into goldfish (25 ug).
P58923
A1W560
UPPP_ACISJ
Undecaprenyl pyrophosphate phosphatase
unclassified Acidovorax
MDTLLLLKAAIMGVVEGLTEFLPISSTGHLILAGSLLGFDDAKAKVFDIAIQTGAIFAVILVYWQRIRATLVALPTERQARRFALNVLIGFLPAVLLGLLLGKAIKAHLFTPVVVASTFILGGFVILWAERRQQAAVRIHAVDDMTPLDALKVGLVQCLAMVPGTSRSGATIIGGMLLGLSRKAATDYSFFLAIPTLIGAGVYSLYKERALLSAADIPLFAVGLVFSFISAWLCVRWLLRYISLHSFVPFAWYRIAFGLVVLATAWSGLVTWAE
Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
A1W560
B3STU4
VCL_CARIL
Cariv
Carya
MVTKAKIPLFLFLSALFLALVCSSLALETEDLSNELNPHHDPESHRWEFQQCQERCQHEERGQRQAQQCQRRCEEQLREREREREREEIVDPREPRKQYEQCRETCEKQDPRQQPQCERRCERQFQEQQERERRERRRGRDDDDKENPRDPREQYRQCEEHCRRQGQGQRQQQQCQSRCEERFEEEQRRQEERERRRGRDNDDEENPRDPREQYRQCQEHCRRQGQGQRQQQQCQSRCEERLEEEQRKQEERERRRGRDEDDQNPRDPEQRYEQCQQQCERQRRGQEQQLCRRRCEQQRQQEERERQRGRDRQDPQQQYHRCQRRCQTQEQSPERQRQCQQRCERQYKEQQGREWGPDQASPRRESRGREEEQQRHNPYYFHSQGLRSRHESGEGEVKYLERFTERTELLRGIENYRVVILEANPNTFVLPYHKDAESVIVVTRGRATLTFVSQERRESFNLEYGDVIRVPAGATEYVINQDSNERLEMVKLLQPVNNPGQFREYYAAGAQSTESYLRVFSNDILVAALNTPRDRLERFFDQQEQREGVIIRASQEKLRALSQHAMSAGQRPWGRRSSGGPISLKSQRSSYSNQFGQFFEACPEEHRQLQEMDVLVNYAEIKRGAMMVPHYNSKATVVVYVVEGTGRFEMACPHDVSSQSYEYKGRREQEEEESSTGQFQKVTARLARGDIFVIPAGHPIAITASQNENLRLVGFGINGKNNQRNFLAGQNNIINQLEREAKELSFNMPREEIEEIFERQVESYFVPMERQSRRGQGRDHPLASILDFAGFF
Seed storage protein.
B3STU4
P31816
TPM_LOCMI
Tropomyosin
Locusta
MDAIKKKMQAMKLEKDNALDRALLCEQQARDANLRAEKAEEEARALQKKIQTIENDLDQTQESLGQVMAKLEEKEKALQNAESEVAALNRRIQLLEEDLERSEERLATATAKLAEASQAADESERARKILENRSLADEERMDALENQLKEARFLAEEADKKYDEVARKLAMVEADLERAEERAEAGESKIVELEEELRVVGNNLKSLEVSEEKANQREEEISNRLRTLTTRLKEAEARAEFAERSVQKLQKEVDRLEDELVIEKEKYKIIGDDLDSAFVELIL
Tropomyosin, in association with the troponin complex, plays a central role in the calcium dependent regulation of muscle contraction.
P31816
Q86TV6
TTC7B_HUMAN
Tetratricopeptide repeat protein 7-like-1
Homo
MATKKAGSRLETEIERCRSECQWERIPELVKQLSAKLIANDDMAELLLGESKLEQYLKEHPLRQGASPRGPKPQLTEVRKHLTAALDRGNLKSEFLQESNLIMAKLNYVEGDYKEALNIYARVGLDDLPLTAVPPYRLRVIAEAYATKGLCLEKLPISSSTSNLHVDREQDVITCYEKAGDIALLYLQEIERVILSNIQNRSPKPGPAPHDQELGFFLETGLQRAHVLYFKNGNLTRGVGRFRELLRAVETRTTQNLRMTIARQLAEILLRGMCEQSYWNPLEDPPCQSPLDDPLRKGANTKTYTLTRRARVYSGENIFCPQENTEEALLLLLISESMANRDAVLSRIPEHKSDRLISLQSASVVYDLLTIALGRRGQYEMLSECLERAMKFAFEEFHLWYQFALSLMAAGKSARAVKVLKECIRLKPDDATIPLLAAKLCMGSLHWLEEAEKFAKTVVDVGEKTSEFKAKGYLALGLTYSLQATDASLRGMQEVLQRKALLAFQRAHSLSPTDHQAAFYLALQLAISRQIPEALGYVRQALQLQGDDANSLHLLALLLSAQKHYHDALNIIDMALSEYPENFILLFSKVKLQSLCRGPDEALLTCKHMLQIWKSCYNLTNPSDSGRGSSLLDRTIADRRQLNTITLPDFSDPETGSVHATSVAASRVEQALSEVASSLQSSAPKQGPLHPWMTLAQIWLHAAEVYIGIGKPAEATACTQEAANLFPMSHNVLYMRGQIAELRGSMDEARRWYEEALAISPTHVKSMQRLALILHQLGRYSLAEKILRDAVQVNSTAHEVWNGLGEVLQAQGNDAAATECFLTALELEASSPAVPFTIIPRVL
Component of a complex required to localize phosphatidylinositol 4-kinase (PI4K) to the plasma membrane. The complex acts as a regulator of phosphatidylinositol 4-phosphate (PtdIns(4)P) synthesis. In the complex, plays a central role in bridging PI4KA to EFR3B and FAM126A, via direct interactions .
Q86TV6
Q5X149
TRHO_LEGPA
tRNA hydroxylation protein O
Legionella
MKDIIIASFYKFIPLNDFESLREPILTKMHEIGIKGTIILAHEGVNGGFAGNREQMNVFYDYLRSDSRFADLHFKETYDNKNPFDKAKVKLRKEIVTMGVQKVDPSYNTGTYLSPEEWHQFIQDPNVILLDTRNDYEYELGTFKNAINPDIENFREFPDYVQRNLIDKKDKKIAMFCTGGIRCEKTTAYMKEQGFQHVYQLHDGILNYLESIPESESLWEGKCFVFDDRVAVDQKLDRVYPQLPQDYKYEREQK
Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs.
Q5X149
Q1QZV1
TAL_CHRSD
Transaldolase
Chromohalobacter
MTQLEALKQLSMVVADTGDLEAIKRYQPHDATTNPSLILKAFELPGYQALIDETLAQVKADIADPQARVDEAVDRLSVAMGSEITQLIPGRVSTEVAAKLSFDREASIAKAHRLIELYEQRGIGRERVLIKLASTWEGIRAAEQLEKEGIQCNLTLLFSEAQARACFDAGVYLISPFVGRVTDWYKQKTGQEYTPEEDPGVVFVRKVCDIASRYRYDTVVMGASFRTKGQILGLAGCNRLTISPALLEELESEEGDIERKISDVGDASERLAPIDEAAFRWGLNQDAMATEKLAEGIRRFADDQATLEEKLAARLG
Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
Q1QZV1