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2.75k
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5.51k
AlphaFoldDB
stringlengths
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A1Z6M6
TTC4_DROME
Tetratricopeptide repeat protein 4 homolog
Sophophora
MKQMAAQKAWTDEERLELAAQLDAELDAFIDGLEKKRYEEGWPEDRWQEEMDKHPFFMKRAPQPGDDVHPMFEGLQKLKYDPEENTRDELALNYKEDGNFYMKHKKFRMAIYSFTEGIKTKTDNPDVLAVLYNNRSAAHFFIKNYRSSLSDAQRALFYKPDYTKARWRSAQCAYELERFDLCTQMCEELLEVDVDNEVAIALLHKNKMKKLEIERNQRKEAAEAKRRLTRFHRLRDAIEQRAIKFDDQKVGKKDVLSEELLYPKFLPLEDHPVHLDEDGSTLIWPAAFSYPEFLYSDFYQQLPETTTMRDCLATLLTEKLPYDKAHNYRLGNVHVYYENRKVGCVHKVDEEKQLAEIIAEKGFFVSGGALLFYVVHKDSRVEQEFINERRRPMVYS
May act as a co-chaperone for HSP83.
A1Z6M6
Q9Y882
TBG_SCHJP
Gamma-tubulin
Schizosaccharomyces
MGREIITLQAGQCGNQVGSQFWQQLCLEHGICPDGTLEDFATEGLDRKDVFFYQSDDTRYIPRAILLDLEPRVVNNILSDTYGSLYNPENIFVATDGGGAGNNWAHGYAHAEKIFEDIVDMIDREAEGSDSLEGFSLLHSIAGGTGSGLGSYLLERLNDRFPKKIVQTYSVFPNNRSVSDVVVQPYNSLLTLKRLTLNADAVVVLDNAALAHIAADRLHIQNPTFHQQNQLVSTVMSASTTTLRYPGYMNNDLVSIIASLIPTPRCHFLSTSYTPFTSQQVEDARTIRKTTVLDVMRRLLQPKNRMVSVNPGKQSCFISILNIIQGEADPNDVHKSLLRIRERKLATFIPWGPASIQVALSKKSPYIKTNHRVSGLMLANHTSIASLFKRTLDQYDRLRKRNAFLDQYRKESIFENSLDEFDNSREVVADLIREYEACEQPEYLSM
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.
Q9Y882
C4K6N8
UVRB_HAMD5
Excinuclease ABC subunit B
Candidatus Hamiltonella
MRKAFKLHSNFKPSGDQPEAIHQLKEGLKNGLMHQTLLGVTGSGKTFTVANVIADLNRPTMILAPNKTLAAQLYGEMKDFFPENAVEYFVSYYDYYQPEAYVPSSDTFIEKDAAVNEHIEQMRLSATKALLERQDVIVVASVSAIYGLGDPDLYLKMMLHLTKGMIIDQRAILARLSELQYSRNDQVFQRGTFRVRGENIDIFPAESSDFAVRIELFDDEVERLSLFAPLTGHIQKTVPRFTVYPKTHYVTPRARILQSMEEIKIELAQRREQLLANNKLVEEQRLTQRTQFDLEMMNELGYCSGIENYSRYLSGRAAGEPPPTLFDYLPSEGLLVIDESHVTIPQIGGMYKGDRSRKQTLVEYGFRLPSALDNRPMRFEEFESLAPQTIYISATPGPYELGKSAGELIEQVVRPTGLLDPVIEVRPVATQVDDLLSEIRQRVVIDERVLVTTLTKRMAEDLTEYLAEQGERVRYLHSDIDTVERVEIIRDLRLGEFDVLVGINLLREGLDMPEVSLVAILDADKEGFLRSERSLIQTIGRAARNLNGKAILYGDKITVSMKKAIDETERRRKKQESYNKEKGIVPKKLEKKIRDILELGQSYTKGKARKRTTTLEENSTNYTALSPKAIKKKIDELEQKMHDHAQNMEFEKAGQLRDEIQQLTLLLNAPQ
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.
C4K6N8
B2RYU6
TPC2L_RAT
Trafficking protein particle complex subunit 2-like protein
Rattus
MAVCIAVIAKENYPLYIRSTPTENELKFHYMVHTSLDVVDEKISAMGKALVDQRELYLGLLYPTEDYKVYGYVTNSKVKFVMVVDSSNTALRDNEIRSMFRKLHNSYTDVMCNPFYNPGDRIQSRAFDTMVTSMMVQVC
May play a role in vesicular transport from endoplasmic reticulum to Golgi.
B2RYU6
A7H2D5
UVRC_CAMJD
Excinuclease ABC subunit C
Campylobacter
MTKEKLENELKTLPNSAGVYEYFNQEGKLLYVGKAKNLKNRVKSYFAFTPNLHANPGNSLRIQKMIQETVHLEFITTNSEADALILENSFIKQLHPKYNILLRDDKTYPYIYVDFKEEFPRFEITRKLVKKSKIKYFGPFFKGARELLDALYLYYPLKQKASCKSPCIFYQISRCLAPCDKRISKEKYREILDEAMHALLNPSVLLKNLEKQMLVLAQNENYEEAAKIRDQIATIKDLEVKVEIDIAKLEDFEVFALAFKNSMLSTLRFVVQNGKIISVNSKITPIKNDIQWDKNEIYKQLILENFSMDIPLLASVIYVYEEFEDRMLLEKILSQRFDKKISIKIPKIGEKRKICDLAFQNALLNIEKEQKNHDFTIQKELKSYFELENLPNDIEIFDNSHLQGVANVGAMVTYSVNSWDKSKYRKFHLKHKNDYDQMREVLTRRALDFDKIPPPDLWLIDGGKVLLDLAKEIILSTGANVDILAISKEKIDAKAHRAKGGAKDKIHSLKGEFSLSVNDKKLQFLQKLRDEAHRFAISFHQNTKKKQDLKSSKLANLGLSLGVIQKLLAYYGNFESIYKADFKDLAMLVGKKAAQKIKEN
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.
A7H2D5
Q8UC06
YCIB_AGRFC
Inner membrane-spanning protein YciB
Agrobacterium tumefaciens complex
MVAEISPLLKFVLELGPLMVFFFANSRGEWLASTFPVLTEFGGPIFIATGLFMIATATALTVSWILTRKLPIMPLISGIVVFVFGALTLWLQNDTFIKMKPTIVNTLFGVILLGGLFFGQSLLGYVFNSAFKLTDEGWRKLTLRWGVFFLFLAVLNEVVWRMFTTDTWVAFKVWGTMPITIIFTMAQMPFVMRHSVEPLGKDEK
Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis.
Q8UC06
P44503
THRC_HAEIN
Threonine synthase
Haemophilus
MNLYNIKHPEEQVTFSQAVRQGLGRDQGLFFPEVIPQLNNINELLELPLVERSQKILGALIDGELPQATLDAMVKNAFTFPAPLEKVEENIYALELFHGPTLAFKDFGGRFMAQALAAVRGDGKITILTATSGDTGAAVAHAFYGLENINVVILYPKGKISPLQEKLFCTLGGNIRTVAINADFDACQALVKQAFDDVELRQAIGLNSANSINISRLLAQVCYYFEAVAQLPKEKRDNVVVSVPSGNFGNLTAGLIAKTLGLPIKRFVASTNANDTVPRYLKSGNWDPKTTVATLSNAMDVSRPNNWPRVEELFKRNGWDLTDLGSGMLSDSETEDTLKAMQSKGYLCEPHGAIAYQVLKDQLKASETGIFLCTAHPAKFKESVERILGIQLPLPETLDKHNQLPLLSDEMDNDFAQLRAYLLKS
Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine.
P44503
Q9P0L1
ZKSC7_HUMAN
Zinc finger protein 64
Homo
MTTAGRGNLGLIPRSTAFQKQEGRLTVKQEPANQTWGQGSSLQKNYPPVCEIFRLHFRQLCYHEMSGPQEALSRLRELCRWWLMPEVHTKEQILELLVLEQFLSILPGELRTWVQLHHPESGEEAVAVVEDFQRHLSGSEEVSAPAQKQEMHFEETTALGTTKESPPTSPLSGGSAPGAHLEPPYDPGTHHLPSGDFAQCTSPVPTLPQVGNSGDQAGATVLRMVRPQDTVAYEDLSVDYTQKKWKSLTLSQRALQWNMMPENHHSMASLAGENMMKGSELTPKQEFFKGSESSNRTSGGLFGVVPGAAETGDVCEDTFKELEGQTSDEEGSRLENDFLEITDEDKKKSTKDRYDKYKEVGEHPPLSSSPVEHEGVLKGQKSYRCDECGKAFNRSSHLIGHQRIHTGEKPYECNECGKTFRQTSQLIVHLRTHTGEKPYECSECGKAYRHSSHLIQHQRLHNGEKPYKCNECAKAFTQSSRLTDHQRTHTGEKPYECNECGEAFIRSKSLARHQVLHTGKKPYKCNECGRAFCSNRNLIDHQRIHTGEKPYECSECGKAFSRSKCLIRHQSLHTGEKPYKCSECGKAFNQNSQLIEHERIHTGEKPFECSECGKAFGLSKCLIRHQRLHTGEKPYKCNECGKSFNQNSHLIIHQRIHTGEKPYECNECGKVFSYSSSLMVHQRTHTGEKPYKCNDCGKAFSDSSQLIVHQRVHTGEKPYECSECGKAFSQRSTFNHHQRTHTGEKSSGLAWSVS
May be involved in transcriptional regulation.
Q9P0L1
P75809
YBJI_ECOLI
5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YbjI
Escherichia
MSIKLIAVDMDGTFLSDQKTYNRERFMAQYQQMKAQGIRFVVASGNQYYQLISFFPEIANEIAFVAENGGWVVSEGKDVFNGELSKDAFATVVEHLLTRPEVEIIACGKNSAYTLKKYDDAMKTVAEMYYHRLEYVDNFDNLEDIFFKFGLNLSDELIPQVQKALHEAIGDIMVSVHTGNGSIDLIIPGVHKANGLRQLQKLWGIDDSEVVVFGDGGNDIEMLRQAGFSFAMENAGSAVVAAAKYRAGSNNREGVLDVIDKVLKHEAPFDQ
Catalyzes the dephosphorylation of 5-amino-6-(5-phospho-D-ribitylamino)uracil, and thus could be involved in the riboflavin biosynthesis pathway . Is also able to dephosphorylate flavin mononucleotide (FMN), erythrose 4-phosphate and other phosphoric acid esters .
P75809
P27155
XYLB_STAXY
Xylulose kinase
Staphylococcus
MAYVIGIDIGTSALKTLVVNKSGDVVESYSVSYNTAHPKSGYSEIDPEIWYEATLESLKYILNHYTHNDLTGISFSGQMHGLVVIDQEGNPIRPAILWNDTRTSQEVEDIKKNLGLNSLLQLTQNTVLEGFTLPKLMWLKNHEQDNYKRIYKFMLPKDYIVYKLTGNVYTEPSDAAGTIMFSVKDENWSTELLHRLNIDPSICPEIIASHQKSGQLTEKVKNTLGIDSNINVYQGGANNACGALGSGITDEQKQLVSIGTSGVALSIENSTDYENDGNVHYFNHCVPNQKYIMGVTLSAGYSLEWLKQLISADENFTTFLKDINQSEVGANGLMYTPYLLGERTPHNDASVRGSFIGLDANTTQLDMKRAVIEGITYSINESIHIMKNNAININEIVSIGGGAKNNQWLQIQADIFNTTITTRTEEQGPAYGAAMIAAMGEQWFNTFNEMSEAWIAYHQKVYPIETNTKSYQDLFNIYKTIYD
Catalyzes the phosphorylation of D-xylulose to D-xylulose 5-phosphate.
P27155
Q05311
UVRD_SALTY
DNA helicase II
Salmonella
MDVSYLLDSLNDKQREAVAAPRSNMLVLAGAGSGKTRVLVHRIAWLLSVENNSPYSIMAVTFTNKAAAEMRHRIGQLMGTSQGGMWVGTFHGLAHRLLRAHHMDANLPQDFQILDSEDQMRLLKRLIKAMNLDEKQWPPRQAMWYINSQKDEGLRPHHIQSYGNPVEQTWQKVYQAYQEACDRAGLVDFAELLLRAHELWLNKPHILQHYRERFTNILVDEFQDTNNIQYAWVRLLAGDTGKVMIVGDDDQSIYGWRGAQVENIQRFLNDFPGAQTIRLEQNYRSTSNILSAANALIENNNGRLGKKLWTDGVDGEPISLYCAFNELDEARFVVNRIKTWQDNGGALAQCAILYRSNAQSRVLEEALLQASMPYRIYGGMRFFERQEIKDALSYLRLIANRNDDAAFERVVNTPTRGIGDRTLDVVRQTSRDRQLTLWQVCRELLQEKALAGRAASALQRFMELIDALAQETADMPLHVQTDRVIKDSGLRTMYEQEKGEKGQTRIENLEELVTATRQFSYNDEDEDLMPLQAFLSHAALEAGEGQADTWQDAVQLMTLHSAKGLEFPQVFIVGMEEGMFPSQMSLDEGGRLEEERRLAYVGVTRAMQKLTLTYAETRRLYGKEVYHRPSRFIGELPEECVEEVRLRATVSRPVSHQRMGTPLAENDTGYKLGQRVRHAKFGEGTIVNLEGSGEHSRLQVAFQGQGIKWLVAAYAKLETV
Has both ATPase and helicase activities. Unwinds DNA duplexes with 3' to 5' polarity with respect to the bound strand and initiates unwinding most effectively when a single-stranded region is present. Involved in the post-incision events of nucleotide excision repair and methyl-directed mismatch repair.
Q05311
Q5BJD5
TM41B_HUMAN
Protein stasimon
Homo
MAKGRVAERSQLGAHHTTPVGDGAAGTRGLAAPGSRDHQKEKSWVEAGSARMSLLILVSIFLSAAFVMFLVYKNFPQLSEEERVNMKVPRDMDDAKALGKVLSKYKDTFYVQVLVAYFATYIFLQTFAIPGSIFLSILSGFLYPFPLALFLVCLCSGLGASFCYMLSYLVGRPVVYKYLTEKAVKWSQQVERHREHLINYIIFLRITPFLPNWFINITSPVINVPLKVFFIGTFLGVAPPSFVAIKAGTTLYQLTTAGEAVSWNSIFILMILAVLSILPAIFQKKLKQKFE
(Microbial infection) Critical host factor required for infection by human coronaviruses SARS-CoV-2, HCoV-OC43, HCoV-NL63, and HCoV-229E, as well as all flaviviruses tested such as Zika virus and Yellow fever virus . Required post-entry of the virus to facilitate the ER membrane remodeling necessary to form replication organelles .
Q5BJD5
P31688
TPS2_YEAST
Trehalose-6-phosphate phosphatase
Saccharomyces
MTTTAQDNSPKKRQRIINCVTQLPYKIQLGESNDDWKISATTGNSALFSSLEYLQFDSTEYEQHVVGWTGEITRTERNLFTREAKEKPQDLDDDPLYLTKEQINGLTTTLQDHMKSDKEAKTDTTQTAPVTNNVHPVWLLRKNQSRWRNYAEKVIWPTFHYILNPSNEGEQEKNWWYDYVKFNEAYAQKIGEVYRKGDIIWIHDYYLLLLPQLLRMKFNDESIIIGYFHHAPWPSNEYFRCLPRRKQILDGLVGANRICFQNESFSRHFVSSCKRLLDATAKKSKNSSNSDQYQVSVYGGDVLVDSLPIGVNTTQILKDAFTKDIDSKVLSIKQAYQNKKIIIGRDRLDSVRGVVQKLRAFETFLAMYPEWRDQVVLIQVSSPTANRNSPQTIRLEQQVNELVNSINSEYGNLNFSPVQHYYMRIPKDVYLSLLRVADLCLITSVRDGMNTTALEYVTVKSHMSNFLCYGNPLILSEFSGSSNVLKDAIVVNPWDSVAVAKSINMALKLDKEEKSNLESKLWKEVPTIQDWTNKFLSSLKEQASSNDDMERKMTPALNRPVLLENYKQAKRRLFLFDYDGTLTPIVKDPAAAIPSARLYTILQKLCADPHNQIWIISGRDQKFLNKWLGGKLPQLGLSAEHGCFMKDVSCQDWVNLTEKVDMSWQVRVNEVMEEFTTRTPGSFIERKKVALTWHYRRTVPELGEFHAKELKEKLLSFTDDFDLEVMDGKANIEVRPRFVNKGEIVKRLVWHQHGKPQDMLKGISEKLPKDEMPDFVLCLGDDFTDEDMFRQLNTIETCWKEKYPDQKNQWGNYGFYPVTVGSASKKTVAKAHLTDPQQVLETLGLLVGDVSLFQSAGTVDLDSRGHVKNSESSLKSKLASKAYVMKRSASYTGAKV
Phosphatase catalytic subunit of the trehalose synthase complex that catalyzes the production of trehalose from glucose-6-phosphate and UDP-alpha-D-glucose in a two step process.
P31688
A6TYN9
XPT_STAA2
Xanthine phosphoribosyltransferase
Staphylococcus
MELLGQKVKEDGVVIDEKILKVDGFLNHQIDAKLMNEVGRTFYEQFKDKGITKILTIEASGIAPAIMAALHFDVPCLFAKKAKPSTLTDGYYETSIHSFTKNKTSTVIVSKEFLSEEDTVLIIDDFLANGDASLGLYDIAQQANAKTAGIGIVVEKSFQNGHQRLEEAGLTVSSLCKVASLEGNKVTLVVEE
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.
A6TYN9
A7FYI3
TIG_CLOB1
PPIase
Clostridium
MNVKVENIEKNVVKLEITVDSEKFNEAVKKSFKKNAKRFNVPGFRKGKAPLNIIKKYYGEGVLFEDAINFCCEDTYPKAIEENNIKPVDYPQIDVVQIGEGKDFIYTAEVTTVPEVKLGEYKGVEVKKVSYEVEDEAVENELKSMQEKNARVSLKEEGEIEKGNIAIIDFKGYVDGKAFEGGEAKDYEIEIGSGTFIGDFEDQLVGLKKDESKEVNVSFPEEYGREDLNGKPATFEVTIKDIKVKELPALDDEFAKEVSEFDTLEELKSDIKDRMKKELSEKAKAEYEEAVVEAVGANAEIEIPKVMIEKEIENMVRDLEMRLKYQGLDLKSYYEFTNSSEEKVKEYMRETAEKRVKTDLIMQEIAKVEDIKATEEELKEKAMEVAKQYGQKDVEKTAELIANAQKAYLEIDIVNGKVLDLLVESSKEIA
Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
A7FYI3
Q8ZU54
UPPS_PYRAE
Undecaprenyl pyrophosphate synthase
Pyrobaculum
MWASGSVKIPTHIAVIPDGNRRYAKKTGIDFYHAYKKGVEKVRNFLTWALEFRDIKNVTFFALSTENLQRSKIELEILFRIFEDELRRTLEDPLIHDNKVRVRFIGDRSLLPGKVVKYIDELESVTKNYSNYHLTIALGYGGRAEIVRCIKRVLSGEVRLETFSEEELFQCLDTRGIPNPEPDVVVRTGGEKRLSNFLLYQTAYSELIFLEKLWPEVEREDLVYIIEEYSRRQRRFGR
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.
Q8ZU54
A4IZ40
UVRC_FRATW
Excinuclease ABC subunit C
Francisella
MIVDNSKDFDLKSFLANLTTHSGVYRMLDKHGEIIYVGKAKNLKNRVNSYFSKGAKDSKTLMMVEQIARIEITITPSDYEAYLLENNLIKQHRPKYNILFKDDKSYPYLVISRDKFPRVSFYRGKSAYKKGQCFGPYVSISSVKNTLNTIQKIFPIRQCENSYYKSRVRPCLQYQIKRCLAPCVGLVSQQQYDEQLAILKKFLAGKFSSVLEEISAKMYQASEDMEYEKAQVYRDQLVVLRKLQQQQIVDIQEDKTFDVIGIYMQDSYASIALLQIQNGDVVADRHWSIDAKGQDKTSIMHAFLSHFYLGDEIRNIWPKNIILSKVEFADITDLMNSISQKIGQAINWIIAPAADNLKWLKLAEVNARQKLNIYTSSKSQYQKRLESLKEFLELEKDIKRIECFDISHFQGEATIASCVVYTDDGEDRKSHRRYNIKDIKSGDDYAAIHQAVSRRVSSGLEADNLPDVMIIDGGKGQIHQAEAVFREYGIQDKVQIVSLGKGVERISGKEKIYKGFDDTEYTLDEHNPGFLLLRQVRDSAHDHAIKGQRKKVSANRQSSIIEEIEGVGPKRRKALMMYFGGWQELSRASVDEIAKVKGISKKLAQEIWECFH
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.
A4IZ40
Q3IIM0
UVRC_PSET1
Excinuclease ABC subunit C
Pseudoalteromonas
MSEFDHVQFLKTLSSEPGVYCMLDSDNQVIYVGKAKHLKKRVSSYFRSNITDSKTRVLVSNICNVEVTLTNTETEALLLENNLIKKYQPRYNILLRDDKSYPYILLTNHKHPRLAFHRGSRKVKGEYFGPFPSAGAVSESLRLMQKIFPIRQCEDVYYRARSRPCLQYQLKRCSAPCVNKVSDEDYTEQVDYVRKFLTGKSHEVIADLIKKMEAASQQLNFELAAKVRDQIMLLRKMQEQQSISGNFAEMDVVGFAHLNGLNGIHLLMIRDHKVLGSKTYFPKVPKDSSEQEILTSFLGQYYLAPGATGRIAKEIILPFEIQESDVLGQALTQISERKVTLKVVTRGERAQYLQLANKNALNSITVKQSTQDSINKRYAQLKATLRLDDITRMECFDISHTMGENTVASCVVFDSQGPNTKEYRRYNVTGITGGDDYAAMEFALNKRYNKLVDEDKIPDVIFIDGGKGQLGRAEQYFATWPHAKMPLLVGVAKGTSRKPGLETLLIDGGRKTIPMDSDAPALHLIQHIRDESHRFAIAGHRNKRQKQRTQSLLEEINGVGAKRRQTLLKYLGGMQGVKAANIEQLKKVPGISPDMADKIFNHLHDKG
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.
Q3IIM0
A0AKE9
TMCAL_LISW6
tRNA(Met) cytidine acetate ligase
Listeria
MKATGIVVEYNPFHNGHQLHLNKARELTKADVVIAVMSGSFVQRGEPAILPKWERTKMALAAGVDMVVELPVSFATQHATIFAEESVRILDALHVDALFFGSEHGVSEDFLTAAKTVVEHEASFNQAIQLALIDKKTSYARAYTETFKQSFGTELLDVTKPNNILGFHYALAIQKQNPTISLQTMARIHAGYHDIEANHDQIASATAIRKLLLAGNLEEASRYLPASSIEILKNYDGPFLSWENYWALLKYRLIQAETDELEGIRNVSEGIQNRMQIAATKAQYFSDFIESMKTKRYSNARIQRTALQILLNARNIPSAPYIRILGMNKTGQKYLSHHKKNISLPIVTTVSKAAPGLLEEDLRATNIYTLVKGLENYQAGDFHIPPILKSQT
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.
A0AKE9
P81129
VKT2_STIHL
Kunitz-type protease inhibitor SHPI-2
Stichodactyla
SFCLEPKRVGRCKGYFPRFYFDSKTGKCTPFIYGGCGGNGNNFETLHQCRAICRA
Inhibitor of serine, cysteine, and aspartic proteinases.
P81129
P32086
TBP_PLAFA
Transcription initiation factor TFIID TBP subunit
Plasmodium (Laverania)
MNFLEQDQLFLENINQDNVVSAHYTSEYDNNEKEKSDDLKNKLVHKNISLNIHNIISSANLCIDINLRLVAVSIRNAEYNPSKINTLIIRLNKPQCTALIFKNGRIMLTGTRTKKDSIMGCKKIAKIIKIVTKDKVKFCNFKIENIIASANCNIPIRLEVLAHDHKEYCNYEPELFAGLVYRYKPTSNLKSVILIFVSGKIIITGCKSVNKLYTVFQDIYNVLIQYKN
General transcription factor that functions at the core of the DNA-binding multiprotein factor TFIID. Binding of TFIID to the TATA box is the initial transcriptional step of the pre-initiation complex (PIC), playing a role in the activation of eukaryotic genes transcribed by RNA polymerase II.
P32086
P06707
TNNC1_ASTLP
Troponin C, isotype alpha
Astacus
MDSLDEEQVSALQKAFDSFDTDSKGFITPETVGIILRMMGVKISERHLQQVISETDEDGSGEIEFEEFAELAAKFLSEEDEEALKKELKEAFRIYDRGGDGYITTQVLREILKELDNRLTEDNLDEIIEEIDEDGSGTIDFMEFMKMMTG
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.
P06707
Q253A8
YIDD_CHLFF
Putative membrane protein insertion efficiency factor
Chlamydia
MSFKSLLKNLPKFFFLGLIHIYRWTISPLLGSPCRFFPTCSQYALQALKHHGCIKGLGFTIKRIGKCGPWHPGGVDLVPMTTLEESLDISPATNDDDSCDSQA
Could be involved in insertion of integral membrane proteins into the membrane.
Q253A8
Q82WU3
TYSY_NITEU
Thymidylate synthase
Nitrosomonas
MYQYLDLMRHVLQYGHKKSDRTGTGTLSVFGYQMRFDLQTGFPLVTTKKCHVKSIIHELLWFLRGETNIDYLKRNGVSIWDEWADENGDLGPIYGHQWRSWAASDGTVIDQISQVIQQIKETPDSRRMIVSAWNVGDLDKMKLAPCHVLFQFYVADGRLSCQLYQRSADIFLGVPFNIASYSLLTLMIAQCCDLQPGEFVHTFGDAHLYLNHLEQARLQLEREPRALPAMQLNSTVRNIFDFGYEDFTLHDYDPYPPIKAPVAV
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.
Q82WU3
A4SM99
UBIG_AERS4
3-demethylubiquinone 3-O-methyltransferase
Aeromonas
MNSDANVDLTEIAKFEAIASRWWDMEGEFKPLHQINPVRLDWITDKSGGLFGKRILDIGCGGGILSESMARRGAHVTGIDMGKEPLGVARLHALEQGVELQYQQMTAEEHASQTPDQYDVVTCMEMLEHVPDPASVLRAIATLVRPGGRVFISTINRNPKAYLMMIIGAEYLMKMVPKGTHDHKKFITPAELCRMGEAAGLLVRDMSGVHYAPLSNQFKLGKNVDVNYMVEFIRPEHG
O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.
A4SM99
O75865
TPC6A_HUMAN
Trafficking protein particle complex subunit 6A
Homo
MADTVLFEFLHTEMVAELWAHDPDPGPGGQKMSLSVLEGMGFRVGQALGERLPRETLAFREELDVLKFLCKDLWVAVFQKQMDSLRTNHQGTYVLQDNSFPLLLPMASGLQYLEEAPKFLAFTCGLLRGALYTLGIESVVTASVAALPVCKFQVVIPKS
May play a role in vesicular transport during the biogenesis of melanosomes.
O75865
Q4UPU5
TSAD_XANC8
tRNA threonylcarbamoyladenosine biosynthesis protein TsaD
Xanthomonas
MKVLGIESSCDETGVAVYDTALSGVPALRAHAVYSQIALHAEYGGVVPELASRDHVRKLLPLIRQTLDEAGLRIDELDGVAYTAGPGLVGALLVGAGVARALAWALEVPAIGVHHMEGHLLAPLMEDDPPQPPFVALLVSGGHTQLVSVKALGAYEVLGETLDDAAGEAFDKTAKMMGLPYPGGPQLAALAETGTPGRYKFARPMTDRPGLDFSFSGLKTQVLLAWRGSDQSDTTRADIARGFEDAVVETLAIKCLRALDTADCNTLVVAGGVGANKRLRARLQEAAQRRGGRVCFPRPALCTDNGAMIAFAGALRLEAGEHADAAVQVTPRWDMASLPPLAAARESGIGNRES
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.
Q4UPU5
A2BLW3
TRM56_HYPBU
tRNA ribose 2'-O-methyltransferase aTrm56
Hyperthermus
MSYSHPASRYERVYVLRIGHRPERDKRITTHVGLVARAFGANGFILGDTCDEKVMESLKDVIDRWGGSMELACGVNSRRYVLEWKRAGGEVIHLTMYGLHVDDVIEEIKRSSKPKLIIVGAEKVPPFFYEYADYNVAIGHQPHSEVAALAIFLHKLYEGKELYIDFPRAKLRIVPSARGKKVVSREA
Specifically catalyzes the AdoMet-dependent 2'-O-ribose methylation of cytidine at position 56 in tRNAs.
A2BLW3
Q8NEG5
ZSWM2_HUMAN
Zinc finger SWIM domain-containing protein 2
Homo
MLRRGYKASERRRHLSERLSWHQDQALSSSIYLLREMGPTGFLLREEEPEYMDFRVFLGNPHVCNCSTFPKGGELCKHICWVLLKKFKLPRNHESALQLGLGEREISDLLRGIHRVQTPQPGTNDENEHVEEDGYIKQKEIDSEDICSICQELLLEKKLPVTFCRFGCGNSIHIKCMKILANYQSTSNTSMLKCPLCRKEFAPLKLILEEFKNSSKLVAAAEKERLDKHLGIPCNNCKQFPIEGKCYKCTECIEYHLCQECFDSCCHLSHTFTFREKRNQKWRSLEKRADEVVKYIDTKNEIEEKMSHFQEKQGQVYTPKHIVRSLPLQLITKNSKLLAPGYQCLLCLKAFHLGQHTRLLPCTHKFHRKCIDNWLFHKCNSCPIDGQVIYNPLTWKNSAVNGQAHQSVSNRDIIHLSKQKEPDLFIPGTGLVLKQNRLGILPSIPQCNFDELNTPQSPKDAYENTTIDNLCSIKLDNSNSKKLTYDYKISQHFPRYLQDLPTVSFGKIPSQTLLPPIVHKNIVCPTAMESPCISGKFHTSLSRMTKGCKCNNHNLKKTPATKIREDNKRSTLLPEDFNLIVNWSTAKLSLSKRYSNCMGEITRKCSHLSRQPVSHSVNTKSTELSLIIEGVQL
E3 ubiquitin-protein ligase involved in the regulation of Fas-, DR3- and DR4-mediated apoptosis. Functions in conjunction with the UBE2D1, UBE2D3 and UBE2E1 E2 ubiquitin-conjugating enzymes.
Q8NEG5
Q66IR0
ZPLD1_XENLA
Zona pellucida-like domain-containing protein 1, secreted form
Xenopus
MEPIWLLLLLAIFTVSVSAQFNGYNCDANQHSRFPAERDITVYCGVQTITMKINFCTVLFSGYSESDLSLNGKHGDAHCRGFINNNTFPAVVIFTINLSTLESCENSLVVSTVPGVNAYGIASMVQIGNISGYIDTPDPPTIISYLPGLLYKFSCSYPLEYLVNNTQLASSSAAISVREGNGTFISTLNLLLYNDSTYSQQLLIPSAGLPLKTKIYAAVRATNLDGRWNVLMDYCYTTPSGNPSDDIRYDLFLSCDKDPQTTIFENGKSQMGRFSFEVFRFVKHKNQKMSTVFLHCITKLCRSDDCHYLTPTCHNRDRRDAVIRTTLTPYSLSGNAVVSAGPIITRSDETPANNSQLAHPGNQQFQINSVTSALISGVVILGATSLSFFIIALTLLNRKKQNSLVLCGIRNPVFN
Glycoprotein which is a component of the gelatinous extracellular matrix in the cupulae of the vestibular organ.
Q66IR0
Q9M306
ZDH10_ARATH
Zinc finger DHHC domain-containing protein At3g48760
Arabidopsis
MLDLQPSDRRHGAPSSSGGVSGGDELIRTYKGWKGNNVFFLGGRLVFGPDARSILITVFLITAPVIVFCIFVGRKFIDDFPHHRGVSVLAVAVGLILLDLVFLLLTSARDPGIIPRNLYPPEPESNEGNGEPRLAHTPQSRLPRTKDMIVNGITVKIKYCDTCMLYRPPRASHCSICNNCVEKFDHHCPWLGQCIGLRNYRFYFMFVLCSTLLCIYVHVFCWIYVKRIMDSENINIWKSFLKTPASIALIIYTFICVWFVGGLTCFHLYLMSTNQSTYENFRYRYDRHENPFNKGIVGNFMEVFCTNVAVSQNSFREKVSKEPAIPPRTVNGGMSSPSLQKVSNDIEMGRKPVWHETVEEELGDIEKDMEAGVASRDLSRMLPPEESEGRGIMHSRESSRGRGIMHSRESSRGRRGGSWELSSRVNEDLRTRDESVSRVGEDSSESSDNDASRDLHVEIYDAVTSRGRTGTGIGRL
Palmitoyl acyltransferase.
Q9M306
B2IT63
URED_NOSP7
Urease accessory protein UreD
Nostoc
MICNSQIAEGWHGKLNLVYADRQGATQLIYNQQQAPLKVQRPFYPEAEKVCHSVILHTAGGMVGGDRLSSNIHLQPQAQALITTAAASKIYRSNGLQARQTIQMQVDPGACLEWLPQETILFNDAIYRQDLRVELATGASWLGWEITRFGRSARGEKFLQGEWRSHTEIWQQSVPLWIDRQCLRGSEDIFHSPHGLAGKPIVGSLVWVGGAVSAEIVEKTRSLWNGEGEVGASRLQHGLLCRYRGSSTSEVRNWFIDVWQLLRVSFLNRGNCIPRVWQV
Required for maturation of urease via the functional incorporation of the urease nickel metallocenter.
B2IT63
Q5UXT1
UPPP_HALMA
Undecaprenyl pyrophosphate phosphatase
Haloarcula
MNPILVAILLGLLQGVLEWIPVSSEGGVALASTVVTGVSPAASTRLALFLHAGTAVAATAYYRTEVRTILHSIRQLSRRPFADETADLSFIVIATAATAVTGLPAYMVLDAAVSELEGGLFLALVGGLLVITGLLQRFAAALSLGEREIPDGFDAVLVGVLQGLAILPGVSRSGTTVSALLLRGHEGESSLRLSFLLSIPAALAANVLVLVDDGIPAIEPLPAVVALIVSAVVGYLTVDALVRLVRQVPFWAVCTVFGGLGVVGGLLVAL
Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP).
Q5UXT1
Q8R8M9
UVRC_CALS4
Excinuclease ABC subunit C
Caldanaerobacter
MDLQEKLKLLPEKPGVYLMKDEEGNIIYVGKASVLKNRVRQYFQNTDNHPPKVKVMLSHVEDFEYIVTDTELEALMLECNLIKKYKPKYNVLLKDDKNYPYIKITVAEDYPRIMFTRKIDMDGSKYFGPYGSAFAVRETIKLVRKMFPIRTCNVNIEKSLGKVRECLYYHIGLCSAPCTGRIEKEEYRKLVDQAVMFLEGKREWLVEKLKEEMQKAADELRFEEAARLRDQIFAIEKISEKQKVTSINEDEQDVISMARSDDIAHIEVFFVREGKLSGREHYYMKNTEGMGREEIISSFIKQFYESSPSVPKEIIIDVELEEKDLLEDWLSQKRGNRVSITVPLRGKKKELVDMVYQNAVEALKNEILAREKILKDPAVLELSNLLGIEYPKRIEAYDISNVRGEDNVGSMVVFVDGKPKKSEYRKFTIKYVEGQDDYQSMREMIERRFLHALEEKKQIEEGTLSKEKAKFIEMPDLILVDGGIGHVNAALEVIEKLGISVPVYGMVKDSRHRTRGLVGVSGEVQMPVTGRAFRLVAQIQEEAHRFAITFHRERQSKRFKTDLLNIKGIGEKRAKVLYEAFGSIEEIKKASLEELKKVKGMNERSAKAVYEYFHGEV
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.
Q8R8M9
P57668
TPX_PSEAE
Thioredoxin-dependent peroxiredoxin
Pseudomonas
MAQVTLKGNPVNVDGQLPQKGAQAPAFSLVGGDLADVTLENFAGKRKVLNIFPSVDTPTCATSVRKFNVEAGKLANTVVLCISADLPFAQKRFCGAEGLENVVNLSTLRGREFLENYGVAIASGPLAGLAARAVVVLDEQNKVLHSELVGEIADEPNYAAALAAL
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.
P57668
A7E3S5
WDR4_BOVIN
WD repeat-containing protein 4
Bos
MASSAGLALCGHALVVRGGSRLLATSTSSSDGDSLFIYDCSAAEKKSQENKGEDGQPVDQGSDTVLASTFSKSGSYFVLTDDSKRLILFRTNPWQCLSVRTVVRRCTALTFTASEEKILVADKSGDVYSFSVLEPHGGGRLELGHLSMLLDVAVSPDDRFVLTADRDEKIRVSWAAAPHSIESFCLGHTEFVSRIFVVPNHPELLLSSSGDCTLRLWEYRSGRELHCCPLTSLQEPTEPWSDKRFAVSRITYWSQEDCVALSCDGLPVVYIFQLDAAQRQLVPRQLLTFQHRVWDAAFEEGHGLWVLQDCREDPLVLYRPVGGQWQSAPESAELRRVCAHVRVNWAMLEGCAGVDSGFSSLYKATCDNMTTYLKKKEERLQQQLEKKRRQAPPPGPNGPTKKMRAGELAQGCSS
Non-catalytic component of a methyltransferase complex required for the formation of N(7)-methylguanine in a subset of RNA species, such as tRNAs, mRNAs and microRNAs (miRNAs). In the methyltransferase complex, it is required to stabilize and induce conformational changes of the catalytic subunit. Required for the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. Also required for the formation of N(7)-methylguanine at internal sites in a subset of mRNAs. Also required for methylation of a specific subset of miRNAs, such as let-7. Acts as a regulator of embryonic stem cell self-renewal and differentiation. Independently of METTL1, also plays a role in genome stability: localizes at the DNA replication site and regulates endonucleolytic activities of FEN1.
A7E3S5
F8WLS6
UGT6_CATRO
UDP-glycosyltransferase 85A23
Catharanthus
MGSLSSSDYSKKPHAVCIPYPAQGHINPMLKLAKLLHYKGFHITFVNTEFNHKRLLKSRGSDSLKGLHSFQFKTIPDGLPPSDVDATQDIPSLCESTTTHCLVPFKQLLQKLNDTSSSEVPPVSCVVSDAVMSFTISAAQELDIPEVLFWTPSACGVLGYMHYAQLIDKGLTPLKDASYFSNGFLDQVLDWIPGMEGIRLRDLPTFLRTTNPDEYMIKFILQETERSKKASAIVLNTFQELESEVIDSLSTLLPPIYPIGPLQILQNQVDDESLKVLGSNLWKEEPECLEWLDTKDPNSVVYVNFGSITVMTNDQLIEFAWGLANSKQNFLWIIRPDLISGESSILGEEFVEETKERGLIASWCHQEQVINHPAIGGFLTHNGWNSTIESISSGVPMICWPFFAEQQTNCRFCCNKWGIGMEINSDVKRDEVESLVKELMVGEKGKEMKKKALEWKNIAEVTTTKPDGSSYSNLEKLIKVLKSKPSH
Iridoid glucosyltransferase acting exclusively on 7-deoxyloganetin. No activity with 7-deoxyloganetic acid.
F8WLS6
Q06204
YL446_YEAST
Putative hexokinase YLR446W
Saccharomyces
MTIESTLARELESLILPADSIVNVVDQFQEELLSRLQTNTISMLPQCLVPDKRSRWNPEDKILTIDFGGTRLKFAIISLPQIVIEYNDAFELTYNIVDSNFFNQIIYTICTRLAANGYIKKKNESSEASKFFVSVTFSFPLNPEGEVVAMGKGFVMTDTLQGSTVKQLIQSSFHRIISENIEEFFCTMNVCHVINDAIAVSLTSKFICENDSISLIIGTGTNACFEVPYGYLPPFKRDALRETLPSSYNKETLNFKHVLINSEIGFIGKNVIALQPFDIHGAISYEMPLECVTSGKWLPLSLKNILLQYNIIPKNFPVEFNGELVCQLAEDCTNAWFENEHYALICQIARLLIKRAAFYVAAIVQAIDIITGCKNYNFIHIGYVGSFLHNSNFYREQIKYYSSIHIKLQFLNHSNLLGAAIATYLNKSDNQVQ
Catalyzes the phosphorylation of hexose, such as D-glucose and D-fructose, to hexose 6-phosphate (D-glucose 6-phosphate and D-fructose 6-phosphate, respectively). Mediates the initial step of glycolysis by catalyzing phosphorylation of D-glucose to D-glucose 6-phosphate.
Q06204
P83747
TX3_THEBL
TlTx3
Theraphosa
DDCLGMFSSCDPNNDKCCPNRVCRVRDQWCKYKLW
Blocks Kv4.2/KCND2 voltage-gated potassium channels probably by shifting the voltage-dependence of channel activation to more depolarized potentials and by binding to the S3-S4 linker region of the voltage sensor domain.
P83747
O78425
YCF17_GUITH
ORF48
Guillardia
MEQKNKKNTIPWIWGFNVYAENWNGRLAMISFLLIICVEFITNKNVLDLVKLN
Possible role in chlorophyll and/or carotenoid binding.
O78425
Q64WF9
TILS_BACFR
tRNA(Ile)-lysidine synthetase
Bacteroides
MIQNRVAQYIEKEKLFCLNDKVLVTLSGGADSVALLRLLLSMGYTCEAAHCNFHLRDKESDRDEAFVRRLCHESGVLLHIEHFDTTQYATKKHISIEMAARELRYEWFETLRKQREASVIATAHHKDDSVETVLLNLIRGTGINGLLGIRPRNGNIVRPLLCLSREEIIAYLQYIDQDYVTDSTNLLDEYTRNKIRLNLLPLMKEINPSVKESIIRTTNYLNDAATLYNQSIGEARKRILTPEGIRIEALLQEPVPEAILFEVLHPLGFNTTQIDNIRQTLDGQPGKVFLGKGWRVIKDRDLLLIEEDTTAEESQPPFRLVMEEYDYTSEFIIPKDKNTACFDADKINKTWEIRKWKPGDVFIPFGMTGKKHVSDYLTDKKFSLSEKEKQWVLCFGEQIAWLIGERTDNRFKVNENTKRVIIVRIVSEHSDFIEE
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.
Q64WF9
Q7NUY8
TIG_CHRVO
PPIase
Chromobacterium
MQVQLETLSNLERRMNIALPMAAIETQVAERLKRVARGAKIQGFRPGKAPLKIVEMNYGAQVREEVMGEQVQQGFYKAVTEQSLRVAGYPRFEPVAAGDDKESFKFAATFEIYPEVKVGELAGKEIEKPNTVVGDAEIEKTIDILRKQRTRYNRVEREAAEGDRVIIDFKGAIDGVAFEGGSSENFPFVLGQGQMLAEFEAGIVGAKEGDIKTVEVNFPEDYHGKDVAGKTAVFEILVKNVAEATLPEVNEEFAKALGISDGDVEKMRGEIRKNVEREVKRRLQARIKENVMQALIDATELELPKALVSLEIGRLVEQARRDMQQRGMNVKDMPFPPELFAAQAERRVKLGLILSEIVEANKLEAKPEQVRAMITEFADSYEQPEDVLAWYYESADRLEGPTSMVLEDNVVEFVLSQANVVAKDLSFDELMGSQA
Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Q7NUY8
P57831
TGT_PASMU
tRNA-guanine transglycosylase
Pasteurella
MKYELDKTDGNARRGRLVFERPQGTFTVETPAFMPVGTYGTVKGMTPEEVRATGAEILLGNTFHLWLRPGQEVMRKHGDLHDFMQWHRPILTDSGGFQVFSLGKLRKITEEGVKFQNPINGERIFLSPEKSMEIQYDLGSDIVMIFDECTPYPATFDYAKKSMEMSLRWAKRSRDRFDELGNKNALFGIIQGGVYEELRKVSVEGLVNIGFDGYAVGGLAVGEPKEDMHRILEYVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVSDGIVKIRNAKYREDTSPLDPECDCYTCKHYTKAYLYHLDKCGEILGARLNTIHNLRYYQRLMAQIRQAIEEDRFEAFVQEFYAKMGKPVPPMQSEIKSDEG
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).
P57831
A7FFS4
UNG_YERP3
Uracil-DNA glycosylase
Yersinia
MSPSLTWHDVIGQEKEQPYFKDTLAYVAAERRAGKTIYPPQKDIFNAFRLTELDQVKVVILGQDPYHGPNQAHGLSFSVLPGVPAPPSLGNIYKELVTDIPGFQRPNHGFLQSWAEQGVLLLNTVLTVEAGKAHSHANLGWETFTDKVIVALNEHREGVIFMLWGSHAQKKGRIINTERHYILKAPHPSPLSAHRGFLGCKHFSQANQLLQQQNQQPIDWQPKLPAVE
Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
A7FFS4
B2GKC1
TRHO_KOCRD
tRNA hydroxylation protein O
Kocuria
MSVPKIVLFYVFTPLADPEAVKLWQLNLAQRSGVKGRIIVSEQGINATVGGDIHDVKAYVRGLKEYAPFQHADIKWSDGAGDDFPRLSVKVRPELVTFDAPDLIRVTEHGVEGGGTHLTPHEVHELVERRGEDVVFFDGRNQLEAEIGRFRGAVVPRTETTRDFLRELDSGAYDHLKDKALVTYCTGGIRCEVLSGLLRNRGFRDVYQLDGGIVRYGEAYGDRGLWDGSLYVFDERRHMEFSLSARSLGRCVQCGEATPRYVNCANQQCRRLFLCCETCTGAGARTRCADCVPVAA
Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs.
B2GKC1
A1DJ52
XYNA_NEOFI
1,4-beta-D-xylan xylanohydrolase A
Aspergillus subgen. Fumigati
MVSFSYLLLACSAIGALAAPVESEDTSFNETALHEFAERGGTPSSTGWNNGYYYSFWTDGGGDVTYTNGAGGSYSVNWRNVGNFVGGKGWNPGSARTINYGGSFNPSGNGYLAVYGWTTNPLIEYYVVESYGTYNPSSGGTFKGTVNTDGGTYNIYTAVRYNAPSIEGTKTFTQYWSVRTSKRAGGTVTMANHFNAWSRLGMNLGTHNYQIVATEGYQSSGSSSITVY
Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.
A1DJ52
P77509
YPHE_ECOLI
Uncharacterized ABC transporter ATP-binding protein YphE
Escherichia
MFTATEAVPVAKVVAGNKRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDEATLTRRAAELGVRAVYQELSLVEGLTVAENLCLGQWPRRNGMIDYLQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDEPTSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQVAGDVMLENTSTHHIVSLMLGRDHVDIAPVAPQEIVDQAVLEVRALRHKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDMLKRGIGYTPENRKEAGIIPWLGVDENTVLTNRQKISANGVLQWSTIRRLTEEVMQRMTVKAASSETPIGTLSGGNQQKVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHGTFSQEFHAPVNVDELMSAILSVH
Probably part of a binding-protein-dependent transport system YphDEF. Probably responsible for energy coupling to the transport system.
P77509
B3H0C8
UBIG_ACTP7
3-demethylubiquinone 3-O-methyltransferase
Actinobacillus
MNNIDQTELDKFEKMAATWWDPNGSFKPIHLLNPLRLDYIQQKANGLFGKKVLDVGCGGGILSEAMAKAGANVTGIDMTTEPLDVARKHAEESGLTIDYRQTTIEDFVQNQTACHAEKFDVITCMEMLEHVPDPLSIIQSCKALLKPDGVLFFSTINRTLKAYMLVIIGAEYVLKMLPKGTHEFEKFIKPAELLNWCDMANLRCQEMKGYHFNPLTEKFWLNNDVSCNYIAMLK
O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.
B3H0C8
Q5L299
YHAM_GEOKA
3'-5' exoribonuclease YhaM
Geobacillus thermoleovorans group
MAKGIIHYEVGEQVDLFLLIKSATKGIASNGKPFLTLILQDKSGDIEAKLWDVSPDDEERYVPECIVKVAGDIHNYRGKLQLRIRSIRPAHPGDAVRIDDFLEKAPLGREEMKAKVMEYIFAMENPNIQRITRYLLKKYEKAFFEYPAATKNHHEFISGLAYHVVSMLELAKALIHLYPSLNKDLLYAGVILHDLGKVIELSGPVSAAYTLEGNLLGHISIMVSEISKAAEQLGIQGEEVVILQHLVLAHHGKAEWGSPKPPLVKEAEVLHYIDNLDAKITMIDRALEKVKPGEFTERVFALDNRSFYKPAFLSVSKPKNPGSKE
Shows a 3'-5' exoribonuclease activity.
Q5L299
Q7ZWN5
TPIS_XENLA
Triose-phosphate isomerase
Xenopus
MSPRKFFVGGNWKMNGDKKSLGELINTLNSGKMNADTEVVCGAPAIYLDFARQKLDAKIALSAQNCYKVAKGAFTGEISPAMIKDCGATWVILGHSERRHVFGECDELIGQKVAHALSEGIGVIACIGEKLDQREAGITEKVVFEQTKAIADNVKDWSKVVLAYEPVWAIGTGKTATPEQAQEVHKKLREWVKTNVSEGVAQSVRIIYGGSVTGGTCRELAGQPDIDGFLVGGASLKPEFIEIINAKH
It is also responsible for the non-negligible production of methylglyoxal a reactive cytotoxic side-product that modifies and can alter proteins, DNA and lipids.
Q7ZWN5
B9M644
TRUD_GEODF
tRNA-uridine isomerase D
Geotalea
MHPYLTGNIPGTGGIFKETPEDFLVTEIPIYTPCGEGEHIYAEIEKRGITTLEAIRRLAKALGIGERDVGYAGMKDAKGITRQTISLPRVAPEQVLGLELPGIKVLSAVPHRNKLKVGHLRGNRFRIRIGGVGADAATIAIAVLDILEKRGVPNFFGEQRYGAQGNSHLIGGAILRNDYRGAVDALIGEPDKVTDERWRRAIEAFKAGDLAKSLETFPPHCRTERELLQKLVKQPEAHEKAFRAVHPRLRKLYLSAFQADLFDRVVQQRMDSLDQVVHGDVAFKHDNGACFLVTDAAAEAPRAAAFEISATGPMFGCRMKEPEGETLAMERRLLETEDLTLPSFDLEGGLRMEGERRPLRVPIAEIGVEADGAGLFLEFSLPKGSYATTVLREVMKS
Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs.
B9M644
Q6MD02
YQGF_PARUW
Putative pre-16S rRNA nuclease
Candidatus Protochlamydia
MENKPKPSRILGIDFGMSRIGLAQSDERKIIAMPLITVHTEKKSEQTVIKLLETISQLCETQKCEIEEIVIGLPLMMSGRTGFLADEVKHFAQLLQQLTPIPIRLWDERLTTVQAERSLRESQLTRKKRSKVVDIVSASIILQSYLDSRC
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
Q6MD02
Q393X8
TRUA_BURL3
tRNA-uridine isomerase I
Burkholderia cepacia complex
MRIALGIQYDGAAFCGWQAQPHGKTVQDRLEHALAEFARVPLHTTVAGRTDTGVHGLGQVVHFDTDLDREVFSWVRGTNAFLPSTVAVQWAKPMPETFHARFSAFERTYYYALYVHPVRSPMLAGRAGWIHTPLDDDAMRAAAAHLIGEHDFSSFRSSECQSKTPVKHLYQIDVRRVGHFVHFRFRANAFLHHMVRNLMGCLVAVGRGRYPADWLADVLAGRDRNLAAPTFMADGLYLAHVGYPAEFAVPPAQLGSVPWSSVWADLDPQS
Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Q393X8
P66954
TPX_STAAM
Thioredoxin-dependent peroxiredoxin
Staphylococcus
MTEITFKGGPIHLKGQQINEGDFAPDFTVLDNDLNQVTLADYAGKKKLISVVPSIDTGVCDQQTRKFNSEASKEEGIVLTISADLPFAQKRWCASAGLDNVITLSDHRDLSFGENYGVVMEELRLLARAVFVLDVDNKVVYKEIVSEGTDFPDFDAALAAYKNI
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.
P66954
O30144
WTPC_ARCFU
Molybdate/tungstate import ATP-binding protein WtpC
Archaeoglobus
MFLKVRAEKRLGNFRLNVDFEMGRDYCVLLGPTGAGKSVFLELIAGIVKPDRGEVRLNGADITPLPPERRGIGFVPQDYALFPHLSVYRNIAYGLRNVERVERDRRVREMAEKLGIAHLLDRKPARLSGGERQRVALARALVIQPRLLLLDEPLSAVDLKTKGVLMEELRFVQREFDVPILHVTHDLIEAAMLADEVAVMLNGRIVEKGKLKELFSAKNGEVAEFLSARNLLLKVSKILD
Part of the ABC transporter complex WtpABC involved in molybdate/tungstate import. Responsible for energy coupling to the transport system (Probable).
O30144
Q80W92
VAC14_RAT
Protein VAC14 homolog
Rattus
MNPEKDFAPLTPNIVRALNDKLYEKRKVAALEIEKLVRDFVAQNNTVQIKHVIQTLSQEFALSQHPHSRKGGLIGLAACSIALGKDSGLYLKELIEPVLTCFNDADSRLRYYACEALYNIVKVARGAVLPHFNVLFDGLSKLAADPDPNVKSGSELLDRLLKDIVTESSKFDLVGFIPLLRERIYSNNQYARQFIISWILVLVSVPDINLLDYLPEILDGLFQILGDNGKEIRKMCEVVLGEFLKEIKKNPSSVKFAEMANILVIHCQTTDDLIQLTAMCWMREFIQLAGRVMLPYSSGILTAVLPCLAYDDRKKSIKEVANVCNQSLMKLVTPEDDEPDEPKSVAQKQTEPNPEDSLPKQEGTASGGASGPCDSSFGSGISVFTSASTDRAPVTLHLDGIVQVLNCHLSDTTIGMMTRIAVLKWLYHLYIKTPRKMFRHTDSLFPILLQTLSDESDEVVLKDLEVLAEIASSPAGQTDDPGAPDGPDLQVNHSELQVPTSGRANLLNPPNTKGLECSPSTPTMNSYFYKFMINLLQTFSSERKLLEARGPFIIRQLCLLLNAENIFHSMADILLREEDLKFASTMVHTLNTILLTSTELFQLRNQLKDLKTLESQNLFCCLYRSWCHNPVTTVSLCFLTQNYRHAYDLIQKFGDLEVTVDFLTEVDKLVQLIECPIFTYLRLQLLDVKNNPYLMKALYGLLMLLPQSSAFQLLSHRLQCVPNPELLQTEDCLKAAPKSQKGDSPSIDYTELLQHFEKVQKQHLEVRHQRSGRGDHLDRRVVL
Scaffold protein component of the PI(3,5)P2 regulatory complex which regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Pentamerizes into a star-shaped structure and nucleates the assembly of the complex. The pentamer binds a single copy each of PIKFYVE and FIG4 and coordinates both PIKfyve kinase activity and FIG4 phosphatase activity, being required to maintain normal levels of phosphatidylinositol 3-phosphate (PtdIns(3)P) and phosphatidylinositol 5-phosphate (PtdIns(5)P). Plays a role in the biogenesis of endosome carrier vesicles (ECV) / multivesicular bodies (MVB) transport intermediates from early endosomes.
Q80W92
Q1WSC1
TRUA_LIGS1
tRNA-uridine isomerase I
Ligilactobacillus
MTQRFKVTLAYDGTNFAGFQAQPNQRTVQFVLEKAINKMSKKDEYITVYGSGRTDSGVHALGQVVHFDFPHPISAKGMLRGLNSMLPLDCEVVDCKIVPNDFHSRYTTHGKRYLYRVSRGEFVNPFKRLYTGHYKYPLDIEKIKEAMPDVEGTHDYSSFVASGSQAKSHVRTIYEAKVYEDKVNDEIVFEFYGNGFLYNQVRIMVATLLEIGNGKRPVHDFLRLYEVKDRSQARQTAPASGLYLKEVYYDEEDEKL
Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Q1WSC1
Q5FWH2
UNKL_MOUSE
RING finger protein unkempt-like
Mus
MPSVSKAAAAALSGSPPQTEKPTHYRYLKEFRTEQCSLFLQHKCSQHRPFTCFHWHFLNQRRRRPLRRRDGTFNYSPDIYCSKYDEATGLCPDGDECPYLHRTTGDTERKYHLRYYKTGTCIHETDARGHCVKNGLHCAFAHGPLDLRPPVCDIRELQAQEALQNGQLSGGDGVPDLQPGVLASQAMIEKILGEDPRWQDSNFVLGSYKTEQCPKPPRLCRQGYACPHYHNSRDRRRNPRRFQYRSTPCPSVKHGDEWGEPSRCDGGDSCQYCHSRTEQQFHPEIYKSTKCNDMRQTGYCPRGPFCAFAHTEKSLAMVNEWSCRDLSSNSTSAYSSQPGSAKRKDSPSEGSQKATEDSKQNHLAVFSVAHPLAHSISSSVASSLASSTGSGSSSPTTLPTLPARALPLDPAGNTVGAVIGSALDLRLSDINIASLDKDLEEQDLGLTGPRSLAGSAPVTIPGSLPRSPSLHSSSSLSTSPLSSLSQSLSGPLVSSAMTPPQQPPPLRSEPATLGSAASSYSSLGLNGVPGSIWDFVSGSFSPSPSPILNSGPSASSSASPNSAELARVRRQLDEAKRKIRQWEESWQQVKQACDAWQREAQEAKERARVADSDRQLALQRKEEVEAKVKQLQEELEGLGLSSLPGLQSLGDISDIPLPKLHSLQSKLRLDLEAVDGVIFQLRAKQCVACQERAHGTVLRPCQHRVLCEPCAASTPECPYCKGQPLPW
May participate in a protein complex showing an E3 ligase activity regulated by Rac1. Ubiquitination is directed towards itself and possibly other substrates, such as Baf60b/Smarcd2. Intrinsic E3 ligase activity has not been proven.
Q5FWH2
Q6F1M4
TMFO1_MESFL
Folate-dependent tRNA(M-5-U54)-methyltransferase 1
Mesoplasma
MQKEVNIIGAGLAGCEAAYLLANNGVKVNLFEVKSLMKNDIQKTNDLGELVCSNTLRSKSKKNAAGILKNEMKLLNSLVIKAALENEIPGDDALSVDRFGFSKYITDKIKNHKNINLIEQEVSEVDYTKVTIIASGPLTTDKLGKNIELMTGNEKLFFLDASAPIITKDSIDFNKVYWASRHNDGKDGQYICIPLNEEQFNAFVEELKNAETIKLKSFEKEIYFKGCQPIEQIAKTSKKVLLNGPLSPNNLIDENGNTPFAVVQLRQDDAIDSLYNFVGFQTNIKWPEQKRILQTLPGLENLNIVRFGVMHKNYYINSPKLLNRSLQVKRNKNIFFAGQITGVEGYIESASSGILTAINVLAYLNNIKIEQPSRKSMLGALNFYITNPKHDKLKPMKCNLGILDQQNKNAKSEFYSFDESEREIRRFIKGINNFAKIGENNE
Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs.
Q6F1M4
A1S464
TRUB_SHEAM
tRNA-uridine isomerase
Shewanella
MARRTKGRNIDGIVLLDKPTGMSSNHALQRVKRIYNASKAGHTGALDPLATGMLPVCLGEATKFSQHLLDADKRYLVTAKLGQRTDTSDSDGEVVSERPLNFTQEALDAALDSFRGDTLQVPSMFSALKYQGQPLYKYAREGKEVPREARPITVFELNFIKLEGDELTLDIHCSKGTYIRTIIDDLGEKLGCGAHVIMLRRTAVAGYPYERMVTIEALEALLEQAEKEGVEPKTLLDPLLLPMDTAVANFPEVNIPDAVAPYLMNGNPVRVAGVSSDSLLRITLGEARRFVGVGAINDDGLLAPKRLVVFYDDEA
Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
A1S464
B5EZX4
YIHI_SALA4
Der GTPase-activating protein YihI
Salmonella
MKKPTSAPRSKAFGKQRRKTREELNQEARDRKRLKKHRGHAPGSRAAGGNSASGGGNQNQQKDPRIGSKTPVPLGVTEKVTQQHKPKSEKPMLSPQAELDLLETDERLDALLERLEAGETLSAEDQAWVDAKLDRIDELMQKLGLSYDDDEEDDEEDEKQEDMMRLLRGGN
A GTPase-activating protein (GAP) that modifies Der/EngA GTPase function. May play a role in ribosome biogenesis.
B5EZX4
B4TE51
TRMD_SALHS
tRNA [GM37] methyltransferase
Salmonella
MFIGIVSLFPEMFRAITDYGVTGRAVKKGLLNIQSWSPRDFTHDRHRTVDDRPYGGGPGMLMMVQPLRDAIHAAKAAAGEGAKVIYLSPQGRKLDQAGVSELATNQKLILVCGRYEGVDERVIQTEIDEEWSIGDYVLSGGELPAMTLIDSVARFIPGVLGHEASAIEDSFADGLLDCPHYTRPEVLEGMEVPPVLLSGNHAEIRRWRLKQSLGRTWLRRPELLENLALTEEQARLLAEFKTEHAQQQHKHDGMA
Specifically methylates guanosine-37 in various tRNAs.
B4TE51
A9KY50
TOLB_SHEB9
Tol-Pal system protein TolB
Shewanella
MKILAKWLALAVLLCTTPAKAALDIVITEGVDAARPIAVMPFVWQGPGAAPQAIADVVMSDLVRSGTFKPLDELGLPQRNIGTVAQFQANSWSSVGAEALVLGTVKPYGTDQYLVSFDLIDLVKAQNQALKGPVSATEFLMDSRQTVISAAQFRQYGHRISDIVYEKLTGIRGAFLTRISYVVVNHTQKAPYQLMVADYDGVNEQMLLRSPEPLMSPTWSPDGRRLAYVSFENKKAEIFVQDLYTQVRTKVSSFPGINGAPAFSPDGKSLAITLSKDGQPEIYIIDIATKAIKRITNHYAIDTEPSWYPDGKSLIFTSERGGRPQIYRVELSSGKVSRETFEGEWNLGGSITPDGRSMIFVNRTNGKFNIARMDLSTRFMQVLTSTRLDESPSVAPNGTMVIYGTTYQGKQVLAAVSTDGRFKARLPAGQGEVKSPSWSPFL
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.
A9KY50
P04053
TDT_HUMAN
Terminal deoxynucleotidyltransferase
Homo
MDPPRASHLSPRKKRPRQTGALMASSPQDIKFQDLVVFILEKKMGTTRRAFLMELARRKGFRVENELSDSVTHIVAENNSGSDVLEWLQAQKVQVSSQPELLDVSWLIECIRAGKPVEMTGKHQLVVRRDYSDSTNPGPPKTPPIAVQKISQYACQRRTTLNNCNQIFTDAFDILAENCEFRENEDSCVTFMRAASVLKSLPFTIISMKDTEGIPCLGSKVKGIIEEIIEDGESSEVKAVLNDERYQSFKLFTSVFGVGLKTSEKWFRMGFRTLSKVRSDKSLKFTRMQKAGFLYYEDLVSCVTRAEAEAVSVLVKEAVWAFLPDAFVTMTGGFRRGKKMGHDVDFLITSPGSTEDEEQLLQKVMNLWEKKGLLLYYDLVESTFEKLRLPSRKVDALDHFQKCFLIFKLPRQRVDSDQSSWQEGKTWKAIRVDLVLCPYERRAFALLGWTGSRQFERDLRRYATHERKMILDNHALYDKTKRIFLKAESEEEIFAHLGLDYIEPWERNA
Template-independent DNA polymerase which catalyzes the random addition of deoxynucleoside 5'-triphosphate to the 3'-end of a DNA initiator. One of the in vivo functions of this enzyme is the addition of nucleotides at the junction (N region) of rearranged Ig heavy chain and T-cell receptor gene segments during the maturation of B- and T-cells.
P04053
A1BJV5
TAL_CHLPD
Probable transaldolase
Chlorobium
MKFFIDTASLEEIQAAKDLGMLDGVTTNPSLIARIVGDASSFSYQDFREHIRRIAEIADGPVSAEVTTTDAEEMIHEGEALAAIHENVVVKCPLTIDGLKAIRHLSEKGIRTNATLVFSPNQALLAAKAGASYVSPFVGRLDDISTEGMALVEQIITIYDNYGYLTEVIVASIRHPRHVVESAMMGADIATIPFSVIRQLANHPLTDAGLKKFMEDAAILKKESDA
Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
A1BJV5
O33285
Y274C_MYCTU
Putative envelope-preserving system protein Rv2742c
Mycobacterium tuberculosis complex
MLVDELGVKIVHAQHVPAPYLVQRMREIHERDENRQRHAQVDVQRRRDQPERGQHQHRRNRDADHHPDGRTLAGQIVAHPVSHRVRQPRPVAIADVLPRVGPRADCVVAHSLQGSPRRRERRRGQTAHQRLGRRSGNAIACPLYLENAAGPEPDTKRAEGRRFGAFGGGDLRWMADRVPRQGSGRRGLGSRSGAGVPQGADARGWRHTADGVPRVGQPAIRRGVPGFWCWLDHVLTGFGGRNAICAIEDGVEPRVAWWALCTDFDVPRSMGRRTPGG
Involved in preservation of envelope integrity and tolerance to surface stress . Reverses the inhibitory effect of PspA on ClgR activity . Facilitates intracellular growth of M.tuberculosis .
O33285
P19425
V15A2_AEDAE
OOSH
Stegomyia
MNKIIAALVLFTAVIGALADYPAPPPPPPKPYHAPPPPPYHAPPHHAPAPLHPVVHTYPVKAPAAKCGANLLVGCAPSVAHVPCVPVHPHPPPPAHY
Has an oostatic activity. Inhibits trypsin biosynthesis in the midgut epithelial cells which indirectly reduces the vitellogenin concentration in the hemolymph resulting in inhibition of oocyte development.
P19425
Q8K945
TUSC_BUCAP
tRNA 2-thiouridine synthesizing protein C
Buchnera
MEKIAFVFSHAPHGTSFGKEGLDVILGVSSIIKKISLFFIGDGVLQILKHSKSENILARNYTSSFRILSIYDIKNFYCCKSSLIDRGLYSHNQFILKVNILNSYFFRIKLDDHDAIINF
Part of a sulfur-relay system required for 2-thiolation of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at tRNA wobble positions.
Q8K945
Q39258
VATE1_ARATH
Vacuolar proton pump subunit E1
Arabidopsis
MNDGDVSRQIQQMVRFIRQEAEEKANEISVSAEEEFNIEKLQLVEAEKKKIRQDYEKKEKQADVRKKIDYSMQLNASRIKVLQAQDDIVNAMKDQAAKDLLNVSRDEYAYKQLLKDLIVQCLLRLKEPSVLLRCREEDLGLVEAVLDDAKEEYAGKAKVHAPEVAVDTKIFLPPPPKSNDPHGLHCSGGVVLASRDGKIVCENTLDARLDVAFRMKLPVIRKSLFGQVTA
Subunit of the peripheral V1 complex of vacuolar ATPase essential for assembly or catalytic function. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. Required for Golgi organization and vacuole function in embryogenesis.
Q39258
P08405
TY1A_YEASX
Gag-p4
Saccharomyces
MESQQLSQHSPNSHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNPSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLRPETY
Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription.
P08405
Q0VFM0
ZFPL1_XENTR
Zinc finger protein-like 1
Silurana
MGLCKCPKRKVTNLFCFEHRVNVCEHCLVANHAKCIVQSYLQWLQDSDYNPNCRLCNTLLSSKETARLVCYDLFHWSCLNDLATQLPPNTAPAGYRCPSCQGPVFPPSNLVSPVAATLREKLSTVNWARAGLGLPLIEVAEPVDDTMSHDETDYRDWSVVNSSSDNLSETPETTSQTGYAYNSVPTSVAQHSLNVNMSQDHAVTIRDTGSDSLTINAGSSPRKVYDTRETARGQDAVIDFDDDKYRRRPTLSWLARILRNRSGSKSRPASSMQRFLVILIIGVLGFLTLILLMSKLGRASADNDPNLDPLLNPHIHVGKE
Required for cis-Golgi integrity and efficient ER to Golgi transport.
Q0VFM0
Q3IFN9
THIC_PSET1
Thiamine biosynthesis protein ThiC
Pseudoalteromonas
MSNTAKKSSRRETRAAASEYIYNLTGQPFPNSHKVYVEGTQNNIRVGMREITLSDTYIGGSDENPVYEPNEPLRVYDTSGPYTDPNFKLDVRQGLAKFREQWIESRGDTELLESVTSRFTQQRMADEGLDHLRFEHLPKIRRGKAGKNVTQMHYARQGIITPEMEYVAIRENMGRKKIHAELLAAQHKGESFGASIPDFITPEFVRDEIARGRAILPNNINHPETEPMIVGRNFLVKVNANIGNSSVSSSIEEEVEKMVWSTRWGADTVMDLSTGRYIHETREWVVRNSPVPIGTVPIYQALEKVNGVAEDLTWEIFRDTLIEQAEQGVDYFTIHAGVLLRYVPMTAKRVTGIVSRGGSIMAKWCLAHHKENFLYTHFEDICEILKQYDICFSLGDGLRPGSIADANDEAQFSELRTLGELTKLAWKHDVQVFIEGPGHVPMHMIKANMDEQLKHCDEAPFYTLGPLTTDIAPGYDHITSGIGAAQIAWYGCAMLCYVTPKEHLGLPNKEDVKEGLITYKIAAHAADLAKGHPGAQERDNALSKARFEFRWHDQFNIGLDPERAREYHDETLPQESGKVAHFCSMCGPKFCSMKISQEVREYAKDLEARGIDPANAADTITIKMIDVEAQMKAKSDEFKKTGSEIYHKAI
Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction.
Q3IFN9
A4X9Z2
TRPD_SALTO
Anthranilate phosphoribosyltransferase
Salinispora
MGERTWPHLLAALLRGDELCTADTAWAMGEIMSGSAGPAQIAGFAVALRAKGETPTELAGLVEAMLTHAVPVNLPAELRATAVDVVGTGGDLAHTVNISTMASLVVAGAGVRVVKHGNRAASSSCGTADVLEFLGLPLDLGPEAVATCVAEAGIGFCFAARFHPGMRHAGPVRRELGVPTAFNFLGPLTNPARPRAGAVGCFDARMAPVMAAVFAARGDSALVLRGEDGLDEFTTAAPTRVWAAQDGTVREALLDATDLGIPRATLADLRGGDVAYNAEAVRRLLAGETGPVRDAVLVNAAAALATQGPLDADLTEALQAGLLRAADSIDSGAAARTLERWIDVAQTVRPAAV
Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
A4X9Z2
A8M0W3
YBEY_SALAI
Endoribonuclease YbeY
Salinispora
MSIEIANESGVDIDTDAVLAVARHALDEMGVNQLAELSVLLVDIDYMAELNHRWMGGDGPTDVLAFPMDEGSVDHGPGESAVAGTEPALLGDIVLCPEVAAKQAATAGHSAADELHLLTVHGVLHLLGYDHAEPDEEREMFALQARLLAGWRSTRST
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
A8M0W3
O93523
VM3BP_BOTJA
Disintegrin-like bothropasin
Bothrops
MIEVLLVTICLAAFPYQGSSIILESGNVNDYEVVYPRKVTALPKGAVQPKYEDAMQYEFKVNGEPVVLHLEKNKGLFSKDYSETHYSPDGREITTYPAVEDHCYYHGRIENDADSTASISACNGLKGHFKLQRETYFIEPLKLSNSEAHAVFKYENVEKEDEAPKMCGVTQNWKSYEPIKKASQLVVTAEQQKYNPFRYVELFIVVDQGMVTKNNGDLDKIKARMYELANIVNEILRYLYMHAALVGLEIWSNGDKITVKPDVDYTLNSFAEWRKTDLLTRKKHDNAQLLTAIDFNGPTIGYAYIGSMCHPKRSVAIVEDYSPINLVVAVIMAHEMGHNLGIHHDTDFCSCGDYPCIMGPTISNEPSKFFSNCSYIQCWDFIMKENPQCILNEPLGTDIVSPPVCGNELLEVGEECDCGTPENCQNECCDAATCKLKSGSQCGHGDCCEQCKFSKSGTECRASMSECDPAEHCTGQSSECPADVFHKNGQPCLDNYGYCYNGNCPIMYHQCYALFGADVYEAEDSCFKDNQKGNYYGYCRKENGKKIPCAPEDVKCGRLYCKDNSPGQNNPCKMFYSNDDEHKGMVLPGTKCADGKVCSNGHCVDVATAY
Inhibits platelet aggregation.
O93523
B1MVY3
TRUA_LEUCK
tRNA-uridine isomerase I
Leuconostoc
MTRYKAIVAYDGSNFFGFQVQTKSGVEVQRTVQGELNKAVNQMAKQPVTPIKVVGASRTDTGVHAFGQVVHFDLPFDINPVGVSKGLNTLLPRDILIKAVTKVSDDFHARFSTHAKRYFYRVSTTAFTDPFKRHYTGHFHWHLDTSRIQEALPDLIGEHDFASFAASGNQTASTVRTITSAQLIEKPDEQELVFVFEGNAFLYNQIRIMVGVLLEIGNGRREIHDIQRLIAVKDREQARFTAPASGLYLDEIDYGENPAN
Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
B1MVY3
Q6DB75
YIHI_PECAS
Der GTPase-activating protein YihI
Pectobacterium
MNRPVKGVADKAEKSKVKRKTREELEREARERKRDKKHRGHSAGSRTQEKASTDQNSGQRKVADPRIGSKKPVQLGVLDSAIVKPKPKSKPSEPVEKVVAAKPTMSPEEELAMLENDTRLDALLDRLDSGETLSAKDQSWVDETLDRIDILMEELGIELGDDDEEEQQEDMLQLLKRNNPKDAL
A GTPase-activating protein (GAP) that modifies Der/EngA GTPase function. May play a role in ribosome biogenesis.
Q6DB75
Q71Z84
TPX_LISMF
Thioredoxin-dependent peroxiredoxin
Listeria
MTQVTFKHNPVTLVGTERKVGDKAPNFTVVNRDLEEVTLHDYDGKVRLISVVPSIDTSVCSTQTRKFNEEASNLDNTVVLTISVDLPFAQKKWCAAEGLPNAITLSDHRDLSFGEAYGVVMKELRLLARSVFVVNAAGEIVYTEVVPEGSDHPNYEAAIEAAKKA
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.
Q71Z84
Q6ITB4
VKT2_OXYMI
Kunitz-type serine protease inhibitor microlepidin-2
Oxyuranus
MSSGGLLLLLGLLTLWEVLTPVSSKDRPDFCELPADTGPCRVGFPSFYYNPDEKKCLEFIYGGCEGNANNFITKEECESTCAA
Serine protease inhibitor.
Q6ITB4
Q4FLQ5
YQGF_PELUB
Putative pre-16S rRNA nuclease
Candidatus Pelagibacter
MITIEDFKIKHTNKVRFIGLDLGSKRIGVSICDERQSIATPFKTINKTNTNELIDELKIIIKDNNIGGIIVGNPVNMDGSLGRSAQSVNDVASNISKSIDLPVILWDERLSTVGAFNLSSLLDVNVSKRVKTIDQNAAAFILQGAIDFLNN
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
Q4FLQ5
Q9PAR9
UVRA_XYLFA
Excinuclease ABC subunit A
Xylella
MTALIRIRGARTHNLKNLDLDLPRNTLIVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLSVMEKPDLDQIEGLSPAISIEQKSTSHNPRSTVGTITEIYDYLRLLYARVGQPRCPDHHYPLEAQTVSQMVDHVLTLDPEQRYMLLAPVVRERKGEHTQVFEQLRAQGFVRVRVDGELYEIDVVPTLTLRQKHTIEAVIDRFRPREDIKQRLAESFETALKLGNGMASVQTLDTTTTTPHLFSSKYSCPVCDYSLPELEPRLFSFNAPMGACPACNGLGVTEFFDPAKVVIHPDLSLSAGAVRGWDRRNAYYFQLIASLAKHYTFDIDASWESLPEEIRHTILFGSGDEQINFIYLTEAGGRTKRKHRFEGIVPNLERRYRETESAAVREELAKYVSTRTCPECGGTRLNRAARNVFVADRTLPELTVLPINDALEFFKTLRLPGWRGEIAIKIVKEIGERLGFLVDVGLDYLTLERKADTLSGGEAQRIRLASQIGAGLVGVMYVLDEPSIGLHQRDNERLLGTLTRLRDLGNTVIVVEHDEDAIRQADHILDIGPGAGVHGGEICAQGSLEQIMAAPRSLTGQYLSGRRRIEIPKQRHPPNATKMLHLRGACGNNLKGVNLDIPEGLFTCITGVSGSGKSTLINDTLFTLAANEINGASHPIAPYASVDGLELFDKVVDIDQSPIGRTPRSNPATYTGMFTPLRELFAQVPEARARGYSPGRFSFNVRGGRCEACEGDGLIKVEMHFLPDVYVPCDVCHGKRYNRETLEIRYKGYNINDVLEMTVEDALKLFEAVPAIARKLETLVDVGLSYLKLGQSATTLSGGEAQRVKLSKELSRRDTGRTLYILDEPTTGLHFYDIEALLAVLHKLRDAGNTVIVIEHNLDVIKTADWVIDLGPEGGGRGGEILVAGTPEAVAAHPHSHTGHFLAKLLPPKDVSNCGHRDPGEEVDIAQTVHR
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.
Q9PAR9
P47165
XPT1_YEAST
Xanthine phosphoribosyltransferase 1
Saccharomyces
MAENERMYISYNNIHKLCQGVAKHILARNERPDIIIAITGGGMIPARIIRSFLKTKGQKNIPIQAIGLSLYEDLGLDNSVETIGKEVIRTQWLDFGALNQHFDSLIGKKVLIVDEVDDTRTTLHYAVSELEKEIAEQQKVLNRMSEETVISIFVLHNKDKPKRAGLPDSMMNSGRYIAAQTVPDKWLCYPWDAEDIEEHTMLAKAQGHD
May act as a xanthine phosphoribosyltransferase involved in the synthesis of purine nucleotides. Such activity is however unclear in vivo.
P47165
Q06813
YP078_YEAST
Uncharacterized protein YPR078C
Saccharomyces
MQTISGVLPTVLSPSELRSDDERTFQFDEEAEITTHLTESEDLRRLINETAQLGVRVDHIHDKTDQEIARLEKVIKEVTESDTFFRSCSGWFKTNKNFSDSESSSNTQLKSLSQLHGRYDRDWRQRLNKWFRKNKSKLALPSDNNLEEVNDDKVYGYGEDLMERGKTPYFSDIDDFMNGLNIISPLTPDDFENDDTLVKIDETCQIHSASEPEKTSISPTFGKNIKKELVTDDTESIISGPPLQENKKTLLKYRYVRTSLDMLGSEKSSSKNNSGGMFRIFHKSANFGDKNQENVPRVWDTLRNNLGREIYLLQGRFKKWTTKHQNLKKGQPCKDEDAVTVPLPSSDPGKETQLETKLCFVPEPGDQPLVQA
Induces the SOS system when expressed in E.coli, therefore, it may play a role in DNA metabolism and/or in genome stability.
Q06813
Q0AHA4
TYSY_NITEC
Thymidylate synthase
Nitrosomonas
MHPYLDLMRHVLQYGHKKTDRTGTGTLSIFGYQMRFDLQQGFPLVTTKQCHVKSIIHELLWFLRGDTNIDYLKKNGISIWNEWADKSGELGPVYGHQWRSWTVSGDKSIDQIAQVIQQIKATPDSRRMIISAWNVGDLDKMALAPCHVLFQFYVVDGKLSCQLYQRSADIFLGVPFNIASYSLLTLMIAQCCNLKPGEFIHTFGDAHLYLNHLEQARLQLTREPKSLPIMELNPAIRNILDFRYEDFTLHNYDPHPPIKAPVAV
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.
Q0AHA4
Q8CRF7
TOP3_STAES
DNA topoisomerase III
Staphylococcus
MKSLILAEKPSVGRDIANALNLQQKSNGYIEGKQYIVTWALGHLVTNATPEQYNPSYKEWNLEDLPIIPKKMKTVVISKTNRQFKIVKSLILDKNVKEIIIATDAGREGELVARLILDKVGNKKPIKRLWISSVTKKAIQEGFKQLKNGNAYQNLYEAALARSEADWIVGINATRALTTKYDAQLSLGRVQTPTIQIVKSRQDEINYFKPEKYYTLSINVDGYDLNLKQQKRYKDKKELELIEHKIKHQEGKILEVKGKNKKSYAQPLFNLTDLQQEAYKRYKMGPKETLNTLQHLYERHKLVTYPRTDSNYLTDDMVDTIQERLRAILATDYKSHVRDLISESFSSKMHIFNNQKVSDHHAIIPTEVRPSIEQLSQREFKIYMLIAERFLENLMNPYLYEVLTIHAQLKDYNFVLKEIIPKQLGYKALKDQTSSHTLTHSFKEGQLFKVHRIEIHEHETKAPEYFNEGSLLKAMENPQNHIDLNDKKYAKTLKHSGGIGTVATRADIIEKLFNMNALESRDGKIKVTSKGKQILELSPSELTSPILTAQWEEKLMLIEKGKYNSQKFIQEMKNFTFKVVNKIKSSEQKYKHDNLTTTECPTCGKFMIKVKTKNGQMLVCQDPKCKTKKNIQRKTNARCPNCKKKMTLFGKGKEAVYRCVCGHTETQSQMDKRMRDKTNGKVSRKEMKKYINKKEEIDNNPFKDALKNLKL
Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone.
Q8CRF7
Q6R3K9
YSL2_ARATH
Protein YELLOW STRIPE LIKE 2
Arabidopsis
MENERVEREQSQFQEDEFIDSRKPPPWRKQITVRAIVASLLIGIVYSVICLKLNLTTGLVPNLNISSALLAFVFLKSWTKVLQKAGIATTPFTRQENTIAQTCAVACYSISLAGGFASYLLGLNRRTYEETGVNTEGNNPRGIKEPGVGWMTSFLFVTSFIGLVVLVPLRKVMIIDYKLTYPSGTATAVLINGFHTSKGDKTAKKQIRGFIKSFGLSFFWAFFGWFYSGGEKCGFSQFPTFGLQALDKTFYFDFSMTYVGAGMICSHLVNLSLLFGAILSWGIMWPLIARLKGEWFPATLKDNSMQGLNGYKVFICIALILGDGLYNFVKILFFTGRSFHSRLSKTNSISTLVEVPEDSTKESDNLKRENEVFVRESIPLWMACVGYLFFSLVSIIAIPLMFPQLKWYFVLVAYLLAPSLSFCNAYGAGLTDMNMAYNYGKAALFVMAALAGKNDGVVAGMVACGLIKSIVSVSADLMHDFKTGHLTQTSPRSMLVAQAIGTAIGCVVAPLTFFLFYKAFDVGNQNGEYKAPYAMIYRNMAIIGVQGPSALPKHCLELCYGFFAFAVAANLARDLLPDKPGKWIPLPMAMAVPFLVGGSFAIDMCIGSLVVYVWKKVNRKKADVMVPAVASGLICGDGLWILPSSLLALAKVRPPICMNFTAAH
May be involved in the lateral transport of nicotianamine-chelated metals in the vasculature.
Q6R3K9
Q88KX1
TAL_PSEPK
Transaldolase
Pseudomonas
MTSKLEQLKQFTTVVADTGDLDAITRLKPVDATTNPSLLLKAAAIPGYADLLKQVKADAKGNVDLACDKFAVAVGSGILKVIPGRISTEVDARLSFDEPALLNKARQLIALYEAAGVAKERVLIKLASTWEGIRAAEQLEKEGIQTNLTLLFSFAQAQACADAGVFLISPFVGRIYDWYKKSTGQEYVGAEDPGVQSVTRIYNYYKANGYNTVVMGASFRNIGQIEQLAGCDRLTISPELLQQLSDDQGELPQVLKPGNAGEAKQHLNESQFRWAMNEDAMGTEKLAEGIRQFARDQEKLEKLIAEKA
Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
Q88KX1
Q1GU13
TATA_SPHAL
Sec-independent protein translocase protein TatA
Sphingopyxis
MGSFSIWHWLVVGILVLLLFGKGRFSDMMGDVAKGIKSFKKGMSEDDAPTPAPKQIDAQRAPDLSATPTPTAETENR
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.
Q1GU13
Q28WI9
TRHO_JANSC
tRNA hydroxylation protein O
unclassified Jannaschia
MYVVAALYHFTRFADPDALRAPLRSIAEAGNVRGSLLLAPEGINGTIAGPRAGIDAVLAHIKGLPGCAGLEWKESTATAAPFGKLKVRLKTEIVSMGAPGLDPADVGTHVAPAEWNALISAPDVAVIDTRNAYEVEIGTFEGAVDPATESFRDFPAWWQANKHRFANQRIAMFCTGGIRCEKSTAYLKEQGVEEVFHLKGGILKYLEDVPEDQSLWQGGCFVFDERVAVGHGLAELPFDLCRACRHPISCEEKADLAFEEGVSCPRCMDVHSDADRARFRERQKQIALAKARGEAHLGAGD
Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs.
Q28WI9
Q9K7E3
THRC_HALH5
Threonine synthase
Halalkalibacterium (ex Joshi et al. 2022)
MSQWRGLLQEYKEFLPVTEETPLLTLGEGNTPLIPLENLSKEWGVKAYVKYEGANPTGSFKDRGMVMAVAKAKEEGSRTIICASTGNTSAAAAAYGARAGLRCIVVIPEGKIALGKLAQAVMYGAEVLEIKGNFDHALDIVRSISEKEPITLVNSVNPYRIEGQKTSAFEICDALGQAPDVLAIPVGNAGNITAYWKGFKEYHEKKGTGLPQMRGFEAEGAAAIVRNQVIEEPETIATAIRIGNPASWTYAVEAAAESNGKIDEVTDEEILAAYQLLAQKEGVFAEPASCASIAGLRKQIASGEIKKGSTVVCVLTGNGLKDPNTAMSTIDVNPAVLPNDEQAFLDHIKGGVPK
Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine.
Q9K7E3
Q38XA4
YBEY_LATSS
Endoribonuclease YbeY
Latilactobacillus
MDIQIIDETKIVPEAQIKLVEDVLEFAGQKLELAEDTEMSVTFVTNERIRQINQEYRNTDRATDVISFAIEEDPEEEGLPANFEELFDIPKNIGDLFVSLEKAAEQAETYGHSFERELGYTMVHGFLHLNGYDHIHTEDEVKMIPLQETILDEFGLKR
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
Q38XA4
P00934
THRC_ECOLI
Threonine synthase
Escherichia
MKLYNLKDHNEQVSFAQAVTQGLGKNQGLFFPHDLPEFSLTEIDEMLKLDFVTRSAKILSAFIGDEIPQEILEERVRAAFAFPAPVANVESDVGCLELFHGPTLAFKDFGGRFMAQMLTHIAGDKPVTILTATSGDTGAAVAHAFYGLPNVKVVILYPRGKISPLQEKLFCTLGGNIETVAIDGDFDACQALVKQAFDDEELKVALGLNSANSINISRLLAQICYYFEAVAQLPQETRNQLVVSVPSGNFGDLTAGLLAKSLGLPVKRFIAATNVNDTVPRFLHDGQWSPKATQATLSNAMDVSQPNNWPRVEELFRRKIWQLKELGYAAVDDETTQQTMRELKELGYTSEPHAAVAYRALRDQLNPGEYGLFLGTAHPAKFKESVEAILGETLDLPKELAERADLPLLSHNLPADFAALRKLMMNHQ
Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine. To a lesser extent, is able to slowly catalyze the deamination of L-threonine into alpha-ketobutyrate and that of L-serine and 3-chloroalanine into pyruvate. Is also able to rapidly convert vinylglycine to threonine, which proves that the pyridoxal p-quinonoid of vinylglycine is an intermediate in the TS reaction.
P00934
Q8TL44
TRPB2_METAC
Tryptophan synthase beta chain 2
Methanosarcina
MYRNDVKEISMEQTKIILDENEMPKKWYNVLADLPSPIDPPLDPRTWQPISPDALEPIFPKALIMQEMSSDRYIDIPEEVLDVYRLWRPSPLFRAHQLEKVLKSPAKIYYKYEGVSPAGSHKTNTSIAQAYYNMKEGTERLTTETGAGQWGSALSLACNYFDLECKVYMVRSSFYQKPYRKSLITLWGGNVVPSPSPDTEFGRKILQEQPDTPGSLGIAISEAVEDAIAHENTKYSLGSVLNHVVLHQTVIGAECKQQLAQVEEYPDVVIGCCGGGSNLGGIGLEFIKDRLEGKHSARVVAVEPSACPSLTKGEYRYDFGDTAEMTPLLKMYTLGHKHVPPAIHAGGLRYHGDSPIISKLCSEGLMEAVSYDQQEVFDAAVQFARTEGIVPAPESSHAIRCAIDEALAAKQTGEEKTILFNLSGHGHFDMSSYDKYFSGELM
The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
Q8TL44
A4WRQ2
TRMFO_CERS5
Folate-dependent tRNA(M-5-U54)-methyltransferase
Cereibacter
MTRSLHIVGAGMAGSEAAWQAAEMGVPVVLHEMRPRVGTFAHRTGQFAEMVCSNSFRSDDDERNAVGLLHWEMRAARGLIMEMASAHRLPAGGALAVDRDPFAESVTARLREHPLISVVDEELAELPSDGDWIIATGPLTSSSLAESIRAVTGAQSLAFFDAIAPIVYAESIDMSVAWRQSRYDKGETEDERTAYINCPMTRDQYEAFIDALLAAEKTEFHEGETAGYFDGCLPIEVMAERGRETLRHGPMKPVGLTNAHKPQDKAHAVVQLRRDNKLGTLYNIVGFQTKMKYGAQTSVFRMIPGLENASFARLGGIHRNTFLNSPTLLDDRMRLKLRPNIRFAGQVTGVEGYVESAAMGLLAGRMAAAEILGRDLPPPPPETAMGALITHITGGAEAKTFQPMNVNFGLFPPIDARGGRRGRKDRYKAYTHRAKAAFTEWLAA
Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs.
A4WRQ2
A8WCF8
TPRGL_RAT
Mossy fiber terminal-associated vertebrate-specific presynaptic protein
Rattus
MLQLRDTVDSAGTSPTAVLAAGEDAGAGRQGAGTPLRQTLWPLNVHDPTRRARVKEYFVFRPGTIEQAVEEIRAVVRPVEDGEIQGVWLLTEVDHWNNEKERLVLVTDQSLLICKYDFISLQCQQVVRVALSAVDTISCGEFQFPPKSLNKREGFGVRIQWDKQSRPSFINRWNPWSTNMPYATFIEHPMAGMDEKTASLCHLESFKALLIQAVKKAQKESPLPGQANNVLVLDRPLLIETYVGLMSFINNEAKLGYSMTRGKIGF
Presynaptic protein involved in the synaptic transmission tuning. Regulates synaptic release probability by decreasing the calcium sensitivity of release.
A8WCF8
Q5EA37
YJU2B_BOVIN
Coiled-coil domain-containing protein 130
Bos
MGERKGVNKYYPPDFNPEKHGSLNRYHNSHPLRERARKLSQGILIIRFEMPYNIWCDGCKNHIGMGVRYNAEKKKVGNYYTTPIYRFRMKCHLCVNYIEMQTDPANCDYVIVSGAQRKEERWDMEDNEQVLTTEHEKKQKLEMDAMFRLEHGEADRSTLKKALPTLSHIQEAQSAWKDDFALNSMLRKRFREKKKAMQEEEERDQALQAKASLAIPLVPETEDDRRLAALLKFHTLDSYEDKQKLKRTEIISRSWFPSTPGASASSSSSSKTNSVLKKLAQNRRATPTSSPVTMGHLGIVRRRSREVPESPQHVAETFKSGEPQLPEGTNQNRPVSPQDCSLETAETPKNSSALGQEESCQDRPQPPPDTSPEAPNPQDTPQPCSLGSSLVADYSGSESE
May be involved in mRNA splicing.
Q5EA37
A3QIE3
UBIB_SHELP
Ubiquinone biosynthesis protein UbiB
Shewanella
MTIKSMRRAYQVVKTVLQYGLDDLIPAKLKPWYFRLLRWSFFWLTNQHKDKVGGERLKLAMQELGPVYIKFGQMLSTRRDLLSDEWAEELAMLQDRVPPFDSAIARAQIEAELGAPIETYFDNFDDTPLASASISQVHTATLKSNGEEVVLKVLRPNVEEKVHADLLLMTQSAQVLETLLGHGNRLRPAEVVEDYRTTIEGELNLKLEALNAIKLRNNFIDSGALYIPKMYEEFCFTRLIVMERIYGVPVSDRAALEAQGTNLKLLAERGVELFFTQVFRDNFFHADMHPGNIFVSTEHPEDPFYIGLDCGIMGTLTEQDKRYLAENFLAFFNRDYTRIAQLYIESGWVAADTDLVAFEQAIKVVCEPMFNKPLDEISFGHVLLELFRTARRFDMVVQPQLVLLEKTLLYIEGLGRQLYPQLDLWQTAKPFLESWMAEQMGPLGMAKKIKKQFPYWTDKLPELPELVYDNLKMGKNFVNSQNQLLDRYLKQQQKAHKSNYLLITSAVLVICGSILFSQNATLWASYACIGIGATLWLLGWRSRPKNRKF
Is probably a protein kinase regulator of UbiI activity which is involved in aerobic coenzyme Q (ubiquinone) biosynthesis.
A3QIE3
A9W900
TRPD_METEP
Anthranilate phosphoribosyltransferase
Methylorubrum
MDAFKTHLAIVASGAPLSREQARAAFDDLLSGEVTPIQAGAFLTALSVRGESEDEIVGAVSAMRARMLPVAAPEGAIDIVGTGGDHSGSYNVSTLAAILTAACGVPVAKHGNRAATSRSGAADVLAALGVKIGLPPEALARCLSEAGLCFMFAQTHHGAMRHVAPVRTELPFRTIFNMLGPLSNPAGVTAQVFGVSRPAWAEPLTRVLATLGSRRVWTVHGSDGLDEITTTGPTAVVALENGAFRHFTLDPREVGLPLATLDDLRGGDPEHNAAALGAVLEGTRNAYRDIAVLNAGAGLVVAGAAGSLAEGVARAQEAIDSGAARGTLARLVAVSNA
Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
A9W900
Q87VG1
THIC_PSESM
Thiamine biosynthesis protein ThiC
Pseudomonas
MSTKPKNAAHLSESAQVDSGSVQPFTRSQKIYVQGSRPDIRVPMREVTLDVTPTDFGGEINAPVTVYDTSGPYTDPNVIIDVRKGLADVRSPWIDSRNDTERLPGLSSHFGQQRLSDAELTALRFAHVRNPRRAKAGANVSQMHYARQGIITAEMEYVAIRENMKLQEARAAGLLTQQHAGHSFGASIPKEITAEFVREEIARGRAIIPANINHVELEPMIIGRNFLVKINGNIGNSALGSSIEEEVAKLTWGIRWGSDTVMDLSTGKHIHETREWIIRNSPVPIGTVPIYQALEKVGGAAEDLTWELFRDTLIEQAEQGVDYFTIHAGVLLRYVPLTAKRVTGIVSRGGSIMAKWCLAHHQENFLYTHFEDICEIMKAYDVSFSLGDGLRPGSIADANDAAQFGELETLGELTKIAWKHDLQTMIEGPGHVPMQLIKENMDKQLECCDEAPFYTLGPLTTDIAPGYDHITSGIGAAMIGWFGCAMLCYVTPKEHLGLPNKDDVKTGIITYKIAAHAADLAKGHPGAQIRDNALSKARFEFRWEDQFNLGLDPDTARSYHDETLPKDSAKVAHFCSMCGPKFCSMKITQEVREYAANQRIEAVDVDVARGLAEQAERFKQEGSQLYKKV
Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction.
Q87VG1
B1ILL2
YBEY_CLOBK
Endoribonuclease YbeY
Clostridium
MIYIDNRQNKIKVNEELENKIKEIIDYALKEEKVNIDYEISVVFIDNNSIKEINKDYRNIDKATDVLSFPMLDYEEGKVFKDIYLNYEFDESDLDEGNLVLGDIALSLEKAEEQSKEFGHSFLRETCYLTIHSVLHLLGYDHMEEDEKVIMRQREEEILKSFNLHR
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
B1ILL2