accession
stringlengths 6
10
| name
stringlengths 6
11
| Full Name
stringlengths 1
147
⌀ | taxon
stringlengths 3
46
⌀ | sequence
stringlengths 16
2.75k
| function
stringlengths 6
5.51k
| AlphaFoldDB
stringlengths 6
10
|
|---|---|---|---|---|---|---|
P32243
|
OTX2_HUMAN
|
Orthodenticle homolog 2
|
Homo
|
MMSYLKQPPYAVNGLSLTTSGMDLLHPSVGYPATPRKQRRERTTFTRAQLDVLEALFAKTRYPDIFMREEVALKINLPESRVQVWFKNRRAKCRQQQQQQQNGGQNKVRPAKKKTSPAREVSSESGTSGQFTPPSSTSVPTIASSSAPVSIWSPASISPLSDPLSTSSSCMQRSYPMTYTQASGYSQGYAGSTSYFGGMDCGSYLTPMHHQLPGPGATLSPMGTNAVTSHLNQSPASLSTQGYGASSLGFNSTTDCLDYKDQTASWKLNFNADCLDYKDQTSSWKFQVL
|
Transcription factor probably involved in the development of the brain and the sense organs. Can bind to the bicoid/BCD target sequence (BTS): 5'-TCTAATCCC-3'.
|
P32243
|
Q8PAL4
|
BAME_XANCP
|
Outer membrane protein assembly factor BamE
|
Xanthomonas
|
MRNLLLVAAVALSTAGCGIIYKQPIYQGNLIKQTAVEQLQVGQSKQQVSALLGTPSIPDPFHAQRWDYTSTQRVDRLARTDVKNFTVFFENEQVVRWEGDYFPAQDEQLAKSAPKQFGRNLARDKKKQRGR
|
Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane.
|
Q8PAL4
|
Q1GFL4
|
DTD_RUEST
|
Gly-tRNA(Ala) deacylase
|
unclassified Ruegeria
|
MRALLQRVSAASVTVDNAVIGEIGPGLLVFVCAMRGDSEAEATQLVQKIARLRIFRDDAGKMNRSVSDTSGAVLVVSQFTLGADTRSGTRPGFSKAAAPDEGMRLYHCFCAKMRETGLTVQTGEFGADMKVSLVNDGPVTLWLDTDDRRNTSAGSG
|
An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo and helps enforce protein L-homochirality.
|
Q1GFL4
|
B8DSU2
|
MRAY_BIFA0
|
UDP-MurNAc-pentapeptide phosphotransferase
|
Bifidobacterium
|
MIALIIGILTSLIITLVGTPLLIRIVHKLNYGQYIRQDGPKSHQVKRGTPTLGGVVIVLAVVLGWCASALYRFCTTGARPTWAAILALFAMVSMGVLGFIDDFAKVRKKQNEGLTVGGKFFGQVVFATIFAVLALIVPTRSGFPVAQAGMSFIEKPFLSFEFAGRIVAIILFVIWVNFLMAAWTNAVNLSDGLDGLCAGSSMIAFVGYAIIAMWQMYHLKGQAHSGFTYAVSDPLDLGIIACCAAVACLGFLWYNCNPASIFMGDTGSLALGGLFAALSIITHTEFLAMIIGGLFVVETLSDVIQVGYFKATHKRVFKMAPIHHHFELCGWSESKVVVRFWIVELMFVITGLIIFYGNWVGLSGLWHH
|
Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
|
B8DSU2
|
P82047
|
CYB_CERNN
|
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
|
Cervus
|
GILLLVLFLMSLVLFAPDLLGDPDNYTPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALVSSILILILMPLLHTSKQRSMMFRPFSQCLFWILVADLLTLTWIGGQPVEYPFIIIGQLASVLYFFIILVLMPITSTIENNLLKW
|
Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
|
P82047
|
B5XR94
|
MDTI_KLEP3
|
Spermidine export protein MdtI
|
Klebsiella
|
MQQFEWIHAAWLAVAIVLEIIANVFLKFSDGFRRKVYGILSLAAVLGAFSALSQAVKGIDLSVAYALWGGFGIAATIAAGWVLFGQRLNNKGWAGLILLVAGMVLIKLA
|
Catalyzes the excretion of spermidine.
|
B5XR94
|
P0C262
|
T214B_PIPCE
|
Translocon at the inner envelope membrane of chloroplasts 214
|
Piper
|
MKPEEIRVNGKEIFKDEEEEDKDLFWFEKPLVTLLFDYKRWNRPLRYIKNDRFENAVSNKMSQYFFHTCPSDGKKIISFTYPPSLSTIEEIIQKRMSLYTTEKGSPEDLYNNWVYTNKKKKNNLSNELINRIEAIEKGSVSIDVLEKRIRLCHDENEQKCLPKWYDPFFNGPYRGTITKVDSQNEDEHFGEMTWKKKIYDIPHKLKNSQEFEEKRNTFHFNRKLLSTDSNNLFTPIGEFDEELASSFYLKEIFLDSEKKSLYSENQKKNGKQPVDTIKNNSNDQALRKHEIEIEKMNKKLPRWSYKLIDDLEQQEEENPEESTGNPGIRSRKAKRVVIYTDKDQNIHTDTSTDSDQAEEIALIRYSQQSDFRRDLIKGSMRSQRRKTLILEMFQANAHPPLFLDRLNKTSFSFNFSKMSMGKELEFKTANSENAEKREAVIKEKTDKSDRLAIAETWDSVTFAQPIRGCILVAQSIVRKYIILPTLIIGKNLGRILFWQSPEWDEDFHEWKKEMHIKCTYNGVQLSETEFPKAWLTDGIQIKILFPFSLKPWHRSKQTSLQVDPIKVKKQNFCFLTVWGRETEQPFGPPRKNPPFFKPILKELKKEMINRFFRVPKTLKNGTKGFMKVEKEKTTLIIQIVFFLKRKMKEFLFVFVKVNPTPLVRSQKIYESNENEKNSILSNKITYESNIQKKSTIDLKNLSLTEKKIKDLSDHTSIIRNQIERVAKDKKRIYLISDRNPSTGETGWYDKDKGRESKKGIWQIFKKRSTRLIRKWPYFLKSLIQKIYTETLLFTISSTDDYAKFFIESTKKSLNKHIYNDEKDKRVIDEINQNTIEFISTINRSFSNITNIFNNSNKNSLTYFELFSLSQAYVFLKLSQTQVFNLYCLGSLLQYHGASTLFKKKIKDYLGSQGIFNFKLKQKKLQNSGINDWKNWLRSHYQYNLPKIRWSRIVPQKWRNRINERRTIKKKGSIFSHSYAKENDQFIYYKKQKNFRMNSLTNQKEKLKKHYRYDLSSYKYLHYEELKNSPLISRSPFQIKGGQEIPYNYNNYNRPKYESFFYVPEIIAINDYLIMGEYVFNTDKNRDRKYLDWGILNLGFKKNINIEYWTHMDTRPFSQDTRTRSNDYRVVENKNLFFLRIHQEINPSNQKNTLFDWMGMNEEMLYYSISSIEPWFFPEFVPRYDIYKIKPCIIPIKSLFLNFYGKESISKNINVNRKANHDTSSNFKKYPVFKNINQEEKEGQGQEVLRSNAQNQQKSFIEKDYKESDIQKPRTKAQSKNNKETELDSFLKKYLLFQLRWNNSLNQKVIDNIKVYSLLLRLKNPREIAISSIQRGEMRLDVMLFQKDITLSGLIKGGLLVIEPIRLYLKWDFQFFMYQIVGISLVHKDKQQIKTRCRIKEYVDKMDFDGSFLPYGKTLVKGHEKHYDLLVPEHILSPRRRRELRILMSFNSGKENIMGRGPFILNGKSVRNCEPFFYEDKYLDTDANKFIQFKFFLWPNYRLEELACMNRYWFDSNNGSRFSMLRIRMYPRHRIL
|
Involved in protein precursor import into chloroplasts. May be part of an intermediate translocation complex acting as a protein-conducting channel at the inner envelope.
|
P0C262
|
Q59448
|
SODC_FRATH
|
Superoxide dismutase [Cu-Zn]
|
Francisella
|
MTAFYKLCGMSMLSLVLADCTFLSANKPYDRDHDGELIVHMKDVNTHKEVGTITISPYIHDGNQEGMLITPHLYNLPANTTHGMHIHINPSCEDNGIAAGGHWDPDNTQKHLGPYNDNGHKGDLPVLVVNADGTATEPVVAPKLNSLEELAGHSLMLHAGGDNYSDKPQPLGGGGARMWCGVIAD
|
Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
|
Q59448
|
Q4V4I9
|
CCHA1_DROME
|
Neuropeptide CCHamide-1
|
Sophophora
|
MWYSKCSWTLVVLVALFALVTGSCLEYGHSCWGAHGKRSGGKAVIDAKQHPLPNSYGLDSVVEQLYNNNNNNQNNQDDDNNDDDSNRNTNANSANNIPLAAPAIISRRESEDRRIGGLKWAQLMRQHRYQLRQLQDQQQQGRGRGGQGQYDAAAESWRKLQQALQAQIDADNENYSGYELTK
|
Ligand for the CCHamide-1 receptor CCHa1-R.
|
Q4V4I9
|
C0QQM7
|
RS19_PERMH
|
30S ribosomal protein S19
|
Persephonella
|
MGYKGKWNERFKNPYVNEKLLKKIRKMNETGERKIIKTWDRACTITEEMVGHTIAVYNGMKFIPVYIQPEMVGHKLGEFSLTRTFRGHPDKSAKAVKKK
|
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
|
C0QQM7
|
Q9Z2I4
|
ROBO3_MOUSE
|
Retinoblastoma-inhibiting gene 1 protein
|
Mus
|
MLRYLLKTLLQMNLFADSLARDISNSSELLFGFNSSLAALNPSLLPPGDPSLNGSRVGPEDAMPRIVEQPPDLVVSRGEPATLPCRAEGRPRPNIEWYKNGARVATAREDPRAHRLLLPSGALFFPRIVHGRRSRPDEGVYTCVARNYLGAAASRNASLEVAVLRDDFRQSPGNVVVAVGEPAVMECVPPKGHPEPLVTWKKGKIKLKEEEGRITIRGGKLMMSHTFKSDAGMYMCVASNMAGERESGAAELVVLERPSFLRRPINQVVLADAPVNFLCEVQGDPQPNLHWRKDDGELPAGRYEIRSDHSLWIDQVSSEDEGTYTCVAENSVGRAEASGSLSVHVPPQFVTKPQNQTVAPGANVSFQCETKGNPPPAIFWQKEGSQVLLFPSQSLQPMGRLLVSPRGQLNITEVKIGDGGYYVCQAVSVAGSILAKALLEIKGASIDGLPPIILQGPANQTLVLGSSVWLPCRVIGNPQPNIQWKKDERWLQGDDSQFNLMDNGTLHIASIQEMDMGFYSCVAKSSIGEATWNSWLRKQEDWGASPGPATGPSNPPGPPSQPIVTEVTANSITLTWKPNPQSGATATSYVIEAFSQAAGNTWRTVADGVQLETYTISGLQPNTIYLFLVRAVGAWGLSEPSPVSEPVQTQDSSLSRPAEDPWKGQRGLAEVAVRMQEPTVLGPRTLQVSWTVDGPVQLVQGFRVSWRIAGLDQGSWTMLDLQSPHKQSTVLRGLPPGAQIQIKVQVQGQEGLGAESPFVTRSIPEEAPSGPPQGVAVALGGDRNSSVTVSWEPPLPSQRNGVITEYQIWCLGNESRFHLNRSAAGWARSVTFSGLLPGQIYRALVAAATSAGVGVASAPVLVQLPFPPAAEPGPEVSEGLAERLAKVLRKPAFLAGSSAACGALLLGFCAALYRRQKQRKELSHYTASFAYTPAVSFPHSEGLSGSSSRPPMGLGPAAYPWLADSWPHPPRSPSAQEPRGSCCPSNPDPDDRYYNEAGISLYLAQTARGANASGEGPVYSTIDPVGEELQTFHGGFPQHSSGDPSTWSQYAPPEWSEGDSGARGGQGKLLGKPVQMPSLSWPEALPPPPPSCELSCPEGPEEELKGSSDLEEWCPPVPEKSHLVGSSSSGACMVAPAPRDTPSPTSSYGQQSTATLTPSPPDPPQPPTDIPHLHQMPRRVPLGPSSPLSVSQPALSSHDGRPVGLGAGPVLSYHASPSPVPSTASSAPGRTRQVTGEMTPPLHGHRARIRKKPKALPYRREHSPGDLPPPPLPPPELRDKLALGSAGSRQHVFPRARAQWGEESGAGSASRGPTSSQRGPHPDGKESQGRGRGLEACRSPNSPQLPLDSCIWSTLKLSLVSFIPSK
|
Thought to be involved during neural development in axonal navigation at the ventral midline of the neural tube . In spinal cord development plays a role in guiding commissural axons probably by preventing premature sensitivity to Slit proteins thus inhibiting Slit signaling through ROBO1 . Required for hindbrain axon midline crossing .
|
Q9Z2I4
|
P56647
|
RBL_SETIT
|
Ribulose bisphosphate carboxylase large chain
|
Setaria
|
MSPQTETKASVGFKAGVKDYKLTYYTPEYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVPGEADQYICYIAYPLDLFEEGSVTNMFTSIVGNVFGFKRSRALRLEDLRIPPAYAKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRACYECLRGGLDFTKDDENVNSQPFMRWRDRFVFCAEAIYKAQAETGEIKGHYLNATAGTCEEMIKRAAFARELGVPIVMHDYLTGGFTANTSLSYYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRMSGGDHIHSGTVVGKLEGEREITLGFVDLLRDDFIEKDRSRGIFFTQDWASMPGVIPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGTAANRVALEACVQARNEGRDLAREGNEIIKAACKWSPELAAACEVWKEIKFEGSKAMDTL
|
RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.
|
P56647
|
Q8DKX6
|
Y723_THEVB
|
Nucleoid-associated protein tlr0723
|
Thermosynechococcus
|
MAQGQGFGFGLGKMKELAAAIQKAQQVQEGAKKLQEDLERMDIEGQAAGGAVKVIMSGTQEPRRVEISPDLLSEGAEVLSDLVTAAMRDAYQKSTATMRERMEELTGSLNVPGLG
|
Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection.
|
Q8DKX6
|
Q9AET4
|
SECA1_STRGN
|
Protein translocase subunit SecA 1
|
Streptococcus
|
MANILRTIIENDKGELRKLEKMANKVIAYSDQMAALSDEELKAKTDEFKQRYQNGESLDDLLYEAFAVVREGAKRVLGLYPYPVQIMGGIVLHHGDVPEMRTGEGKTLTATMPVYLNALAGEGVHVVTVNEYLTERDATEMGELYSWLGLSVGINLAAKSPAEKREAYACDITYSTNSEIGFDYLRDNMVVRAENMVQRPLNYALVDEVDSILIDEARTPLIVSGPVSSETNQLYHMADSFVKSLNKDDYIIDVPSKTIGLSDSGIDKAESYFKLDNLYDIENVALTHFIDNALRANYIMILDIDYVVSEEQEILIVDQFTGRTMEGRRYSDGLHQAIEAKEGVPVQDETKTSASITYQNLFRMYKKLSGMTGTAKTEEEEFRETYNIRVIPIPTNRPIARIDHEDLLYPSLESKFKAVVEDVKERHLKGQPVLVGTVAVETSDYLSKKLVAAGIPHEVLNAKNHYREAQIIMNAGQRGAVTIATNMAGRGTDIKLGEGVRELGGLCVIGTERHESRRIDNQLRGRSGRQGDPGESQFYLSLEDELMRRFGSERIKAVLDRFKLSEEESVIKSKMFTRQVEAAQKRVEGNNYDTRKQVLQYDDVMREQREIIYAERHDVITANRDLAPEIHAMIKRTIDRFVDGNSRAPQEEKLDSILYFAKYNLVPEESISLSDLQGLSDEEIKANLYERALEVYNSQIAKLRDEEAVREFQKVLILRVVDNKWTDHIDALDQLRNAVGLRGYAQNNPVVEYQSESFRMFNDMIGSIEFDVTRLMMKAQIHEQERPRTEHNIVTTATRNISAQESDLPADVDLAKVGRNELCPCGSGKKFKNCHGRR
|
Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
|
Q9AET4
|
B0UDK8
|
BCHL_METS4
|
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
|
Methylobacterium
|
MNIAIRNPVATRPAERREEGSLQVALDPDLRIDTAKVFAVYGKGGIGKSTTSSNLSVAFSKLGKRVLQIGCDPKHDSTFTLTKRLAPTVIDALEAVKFHAEELRVEDFVVEGYNGVMCVEAGGPPAGTGCGGYVVGQTVKLLKEHHLLEETDVVVFDVLGDVVCGGFASPLQHADRALIVTANDFDSIFAMNRIVAAIHAKAKNYGVRLGGVIANRSAATDEIDRFNAAVGLRRLAHFQDLDVVRRSRLRKATLFEMESSPELDAVLAEYLALAEALWAGVEPLEAEPMRDRDLFEFLGFD
|
Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The L component serves as a unique electron donor to the NB-component of the complex, and binds Mg-ATP.
|
B0UDK8
|
B7NLY4
|
CRCB_ECO7I
|
Putative fluoride ion transporter CrcB
|
Escherichia
|
MLQLLLAVFIGGGTGSVARWLLSMRFNPLHQAIPLGTLTANLIGAFIIGMGFAWFSRMTNIDPVWKVLITTGFCGGLTTFSTFSAEVVFLLQEGRFGWTLLNVFVNLLGSFAMTALAFWLFSASTAH
|
Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
|
B7NLY4
|
A6U5U0
|
PYRD_SINMW
|
Dihydroorotate oxidase
|
Sinorhizobium
|
MIGGLEHLARRGLFLFDPEAAHGLSITALKTGLVPSCAAPADPRLQQSVAGLAFPNPVGMAAGYDKNAEVPEALLKIGFGFTEIGTVTPRPQPGNDKPRLFRLIEDEAVINRLGFNNEGHGAALARLKACSREALIGVNIGANKDSADRIADYVTGIRTFYAVARYFTANISSPNTPGLRDLQARESLATLLSAVLAAREDEAGKCGRRVPVFLKIAPDLTEEGMDDIAAEVLAQGLDGLIVSNTTLARARLRDRKQASEVGGLSGKPLFEKSTAVLARMRRRVGPDLPIIGVGGVSSAETAAEKIRAGADLVQLYSCMVYEGPSLPGRIVRGLSALCDREKLASIREIRDSRVDYWTGMNV
|
Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
|
A6U5U0
|
Q76FS2
|
TBB8_ORYSJ
|
Beta-8-tubulin
|
Oryza sativa
|
MREILHIQGGQCGNQIGAKFWEVICGEHGVDPTGTYTGTSPQQLERINVYFNEASGGRHVPRAVLMDLEPGTMDSLRSGPIGGIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYPDRMMLTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLTNPSFGDLNHLISATMSGVTCCLRFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYRALTVPELTQQMWDAKNMMCAADPRHGRYLTASAMFRGRMSTKEVDEQMINVQNKNSSYFVEWIPNNVKSSVCDIPPVGLSMASTFVGNSTSIQEMFRRVSEQFTAMFRRKAFLHWYTSEGMDEMEFTEAESNMNDLVAEYQQYQDATAEDDYDEDDDAAAADEA
|
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.
|
Q76FS2
|
Q8CCT4
|
TCAL5_MOUSE
|
Transcription elongation factor S-II protein-like 5
|
Mus
|
MEKFYKENEGKPENKGRAEDEGSTEEGGKADEDKSDAEGKPARQGKLEVEGGPGEQAQQKGEGKPEKQGKSDGEGKRQGESKPDSQAKSASEARAAEKRPAEDYVPRKAKRKTDRGTDDSPKNSQEDLQDRHVSSEEMMRECADMTRAQEELRKRQKMGGFHWVPRDAQDALVPRGQRGVRGVRGGGGRGQKDLEDAPFV
|
May be involved in transcriptional regulation.
|
Q8CCT4
|
Q6AG49
|
IF2_LEIXX
|
Translation initiation factor IF-2
|
Leifsonia
|
MGPDRRIVAAKPRVHEVASELGVDSKIALAKLKEMGEFVKGPSSSIEPPVARKLRAALEAEGHLPGAGGDKTAAQASPAPRPPRPATADGSGAPKPQAPMSVAERQAAAEKAASEKAAAEKVAASEAADAKPAAGAPADTAKPSSPPRPSGVSAPRPGNNPFASNQGMGQRPSAPRPGNNPFSSSQGMGQRPSPSNIPRPAPPRPGSPRIGAPRPGGGQRQGGGGRPGFQQRPGSAGGGAGGGLQRPGGAGAGGFSGPRTGGGGGRGRGPGGGTAGAFGRGGGKSKARKSKRAKRQEFEMREAPSLGGVTVPRGDGGTAIRLRRGASISDFADKIDANPASLVTVLFHLGEMATATESLDEATFQILGEELGYKVQVVSPEDEDKELLEGFDIDLDAELEGESDEDLEIRPPVVTVMGHVDHGKTRLLDAIRSANVVEGEAGGITQHIGAYQVWTEHEGIERAITFIDTPGHEAFTAMRARGAQVTDIAILVVAADDGIMPQTIEALNHAQAANVPIVVAVNKVDKPEANPAKVRQQLTEFSLVAEEYGGDVMFVDVSARNNIGIQELLDAVLLTADAGLDLRANPNKDARGVAIEAKLDKGRGAVATVLIQSGTLRVGDAIVAGTAYGRVRAMADENGDPVLEAAPSRPVQVQGLSSVPRAGDTFIVTEEDRTARQIAEKREAAERNAQLAKARKRISLEDFTRALEEGKVEALNLIIKGDVSGAVEALEESLMKIEVDDSVSLRILHRGVGAITESDIDLATIDNAIVIGFNVRPDVKARERAAREGVDVRFYSVIYNAIDDIESSLKGMLKPEFEEVQSGVADIREVFRSSKFGNIAGVIVRSGTITRNAKARVIRDGVVIADNLAIESLRRFKDDVTEVRTDFECGIGLGKYNDIQVGDEIETIEMREKPRV
|
One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex.
|
Q6AG49
|
Q4A8E1
|
GLYA_MESH7
|
Probable serine hydroxymethyltransferase
|
Mesomycoplasma
|
MYKKIKLRDQQISELINLESKRQNSQIELIASENYASEDVILANGTSLSNKYGEGYPGKRYYGGCTFIDQIEKIAIERVKKLFKIEYANVQPYSGSSANAAVFAALLKPGDKILGLDLNAGGHLSHGYKINFSGMFYSGISYFLDENELLDYEAIEKIALKTKPNLIICGYSAYSRKIDFARFRQIADKVNAFLLADIAHIAGLIAAGQHPSPVGYAHIITSTTQKTLRGPRGGLILTSSKEIAAKIDKVVFPGIQGGPFFHTIAAKAVAFKEALEPWFKEYCAQIVKNAAHFASEFIKKGIRIVSQGTENHLFTIDVLSSYNLNGKQAQILLESVNIITNKNTIPNDTLSPFVTSGLRLGTPAMTSRGFKEQEFSQMAEIIDFVLRKKELNALEIKEIKKKVKILTKNFPIKKSYWP
|
Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules.
|
Q4A8E1
|
Q3SZT1
|
GSG1_BOVIN
|
Germ cell-specific gene 1 protein
|
Bos
|
MGLPKGFSSQRKRLSAVLNMLSLSLSTASLLSNYWFVGTQKVPKPLCGKGLPAKCFDVPVPLDGGGTNASSPEVVHYSWETGDDRFTFHAFRSGMWLSCAEIMEEPGERCRSFLELTPPTEREILWLSLGAQFAYIGLELISFILLLTDLLFTGNPGCSLKLSAFAAISSVLSGLLGMVGHMMYSQVFQATANLGPEDWRPHAWNYGWAFYTAWVSFTCCMASAVTTFNTYTRLVLEFKCRHSKSFRGAPGCQPHHHQCFLQQLACTAHPGGPVTSYPQFHCQPIRSISEGVDFYSELHDKELQQGSSQEPETKAAGSSVEEC
|
May cause the redistribution of PAPOLB from the cytosol to the endoplasmic reticulum.
|
Q3SZT1
|
P60606
|
CTXN1_HUMAN
|
Cortexin-1
|
Homo
|
MSATWTLSPEPLPPSTGPPVGAGLDAEQRTVFAFVLCLLVVLVLLMVRCVRILLDPYSRMPASSWTDHKEALERGQFDYALV
|
May mediate extracellular or intracellular signaling of cortical neurons during forebrain development.
|
P60606
|
E0W4Y2
|
AV241_PHYSO
|
Avirulence homolog protein 241
|
Phytophthora
|
MRQYCLLLIVLALAAALSDNAVASTLAVARSEIGAPSAVYSERLLRSEPQDEDTFEDRAFGLNWLRLRWLRLGAAKAKTTDVISARESKWIEAWANKNLSPNYVYKQLGLAKQGDKAMQSQNYRIFEAYTERLFAKDQALYTKWLDAKMTPEDVYKALKLDKLLGAKAANSPDFRRYEVYMFKWHELN
|
Effector that triggers cell death in a variety of plant species (including tobacco, tomato and soybean), regardless of the Rps genes present . Avh241 interacts with the plant immune system via at least two different mechanisms, one recognized by plants dependent on subcellular localization and one promoting infection independent on membrane localization . The cell death triggered by Avh241 in N.benthamiana requires the two host mitogen-activated protein kinases, MEK2 and WIPK .
|
E0W4Y2
|
Q6EW50
|
RR14_NYMAL
|
30S ribosomal protein S14, chloroplastic
|
Nymphaea
|
MARKSLIQREKKRQKLEEKYHLIRRSSKKEISKVSSLDEKWEIHVKLQSPPRNSAPIRLHRRCFLTGRPRANYRDFGLSGHVLREMVHACLLPGATRSSW
|
Binds 16S rRNA, required for the assembly of 30S particles.
|
Q6EW50
|
A9MQT5
|
TTCA_SALAR
|
tRNA 2-thiocytidine biosynthesis protein TtcA
|
Salmonella
|
MQDNQKVKKKEQYNLNKLQKRLRRNVGEAIADFNMIEEGDRIMVCLSGGKDSYTMLEILRNLQQSAPINFSLVAVNLDQKQPGFPEHILPAYLEQLGVEYKIVEENTYGIVKEKIPEGKTTCSLCSRLRRGILYRTATELGATKIALGHHRDDILQTLFLNMFYGGKMKGMPPKLMSDDGKHIVIRPLAYCREKDIVRFAEAKAFPIIPCNLCGSQPNLQRQVIADMLRDWDKRYPGRIETMFSAMQDIVPSHLCDTNLFDFKGIAHGSEVVDGGDLAFDREEIPLQPAGWQPEEDDTPLETLRLDVIEVK
|
Catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(2)C32). The sulfur atoms are provided by the cysteine/cysteine desulfurase (IscS) system.
|
A9MQT5
|
A8AQN3
|
TUSD_CITK8
|
tRNA 2-thiouridine synthesizing protein D
|
Citrobacter
|
MRFAIVVTGPAYGTQQASSALQFAHALVNEGHELSSVFFYREGVYNANQLTSPASDEFDLVRAWQQLGAQHGVALNICVAAALRRGIVDETEAKRLALASANLQPGFSLSGLGALAEASLTCDRVVQF
|
Part of a sulfur-relay system required for 2-thiolation of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at tRNA wobble positions. Accepts sulfur from TusA and transfers it in turn to TusE.
|
A8AQN3
|
Q8LHP0
|
ELOF1_ORYSJ
|
Transcription elongation factor 1 homolog
|
Oryza sativa
|
MGKRKSAAKPPPKKRMDKLDTVFSCPFCNHGSSVECRIDMKNLIGEASCRICQENFSTTVNALTEPIDIYSEWIDECERVNNVEDDDGA
|
Transcription elongation factor implicated in the maintenance of proper chromatin structure in actively transcribed regions.
|
Q8LHP0
|
Q2G0B1
|
MGRA_STAA8
|
Regulator of autolytic activity
|
Staphylococcus
|
MSDQHNLKEQLCFSLYNAQRQVNRYYSNKVFKKYNLTYPQFLVLTILWDESPVNVKKVVTELALDTGTVSPLLKRMEQVDLIKRERSEVDQREVFIHLTDKSETIRPELSNASDKVASASSLSQDEVKELNRLLGKVIHAFDETKEK
|
Regulatory protein involved in autolytic activity, multidrug resistance and virulence. Controls autolysis by inactivating LytM, LytN (autolysins) and SarV (autolysis activator) and activating ArlRS, LrgAB and LytSR (autolysis inhibitors). Acts as a dual regulator for resistance to multiple drugs by inactivating NorB and tet38 and activating NorA. Positively controls the expression of virulence accessory gene regulator (agr) to promote alpha-hemolysin (hla) transcription and down-regulates staphylococcal accessory regulator (sarS), leading to repression of surface protein A (spa). Binds directly to hla promoter to augment its activation. Binds to sarS promoter to down-regulate spa expression.
|
Q2G0B1
|
Q96DZ5
|
CLIP3_HUMAN
|
Cytoplasmic linker protein 170-related 59 kDa protein
|
Homo
|
MTKTDPAPMAPPPRGEEEEEEEEDEPVPEAPSPTQERRQKPVVHPSAPAPLPKDYAFTFFDPNDPACQEILFDPQTTIPELFAIVRQWVPQVQHKIDVIGNEILRRGCHVNDRDGLTDMTLLHYACKAGAHGVGDPAAAVRLSQQLLALGADVTLRSRWTNMNALHYAAYFDVPDLVRVLLKGARPRVVNSTCSDFNHGSALHIAASSLCLGAAKCLLEHGANPALRNRKGQVPAEVVPDPMDMSLDKAEAALVAKELRTLLEEAVPLSCALPKVTLPNYDNVPGNLMLSALGLRLGDRVLLDGQKTGTLRFCGTTEFASGQWVGVELDEPEGKNDGSVGGVRYFICPPKQGLFASVSKISKAVDAPPSSVTSTPRTPRMDFSRVTGKGRREHKGKKKTPSSPSLGSLQQRDGAKAEVGDQVLVAGQKQGIVRFYGKTDFAPGYWYGIELDQPTGKHDGSVFGVRYFTCPPRHGVFAPASRIQRIGGSTDSPGDSVGAKKVHQVTMTQPKRTFTTVRTPKDIASENSISRLLFCCWFPWMLRAEMQS
|
Functions as a cytoplasmic linker protein. Involved in TGN-endosome dynamics. May modulate the cellular compartmentalization of AKT kinase family and promote its cell membrane localization, thereby playing a role in glucose transport in adipocytes.
|
Q96DZ5
|
Q7LZM1
|
MYG_URILO
|
Myoglobin
|
Uria
|
MGLSDQEWQHVLTIWGKVESDLAGHGHQVLMRLFQDHPETLDRFEKFKGLKTPDQMKGSEDLKKHGVTVLTQLGKILKQKGNHESELKPLAQTHATKHKIPVKYLEFISEAIIKVIAEKHASSFGADSQAAMKKALELFRNDMASKYKEFGFQG
|
Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
|
Q7LZM1
|
Q9M5Q1
|
FUT1_PEA
|
Xyloglucan alpha-(1,2)-fucosyltransferase
|
Pisum
|
MNMLIKRVIAIKNPRGDDNNNNKLSDLETLTDKCTTCPLTLMRVMAFFVVSFMLFSVLFSLSVVLRDPPSDAAISSTTTLFQLNQGLGSDDFDSVELLNDKLLGGLLADGFDEKSCLSRYQSAIFGKGLSGKPSSYLISRLRKYEARHKQCGPYTESYNKTVKELGSGQFSESVDCKYVVWISFSGLGNRILTLVSAFLYALLTDRVLLVDPGVDMTDLFCEPFPDASWFVPPDFPLNSHLNNFNQESNQCHGKILKTKSITNSTVPSFVYLHLAHDYDDHDKLFFCDEEQLFLQNVPLLIMKTDNYFIPSLFLMPSFEQELNDLFPKKEKVFHFLGRYLLHPTNNVWGLVVRYYDAYLAKVDERIGIQIRVFDTDPGPFQHVLDQVLACTLKESILPDVNREQNINSSSGTPKSKAVLITSLSSGYFEKVRDMYWEFPTETGEVVGIYQPSHEGYQQTQKQFHNQKAWAEMYLLSLTDVLVTSSWSTFGYVAQGLGGLKPWILYKPENRTAPNPPCQRAMSMEPCFHAPPFYDCKAKRGTDTGALVPHVRHCEDMSWGLKLVDN
|
Involved in cell wall biosynthesis. Adds the terminal fucosyl residue on xyloglucan side chains.
|
Q9M5Q1
|
A0LDT3
|
CLPX_MAGMM
|
ATP-dependent Clp protease ATP-binding subunit ClpX
|
Magnetococcus
|
MPNNSSDSSSILHCSFCGKSQNEARKLIAGPSVFICDECVDLCMEIIREDKSDQLEKKRGGVPTPMEIKSTLDDYVIGQDNAKRTLAVAVYNHYKRLESNDTSADVEISKSNVLMIGPTGSGKTLLAQTLARLLDVPFTITDATTLTEAGYVGEDVENIILRLLQAADNDVEKAQRGIVFIDEIDKISRKSDNPSITRDVSGEGVQQALLKIIEGTVASVPPQGGRKHPQQEYLQVDTTNILVICGGAFNGLEKVIEKRSSKHHGIGFGATVRKNSKEESVNVLLKELEPEDLLAFGLIPEFVGRLPVVATLEELSKEALVRILTEPKNALVKQYQKLLEMENVKLTFTDGALEALAQRAIERKTGARGLRALLESTLLDIMFEIPSKQGVREVVINREVVEKQIEPLLIYAEEALEANA
|
ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.
|
A0LDT3
|
Q1GRY1
|
MURB_SPHAL
|
UDP-N-acetylmuramate dehydrogenase
|
Sphingopyxis
|
MSATATLPAVRGKLTPQAPLAPLVWFKSGGAADWLFEPKDVDDLADFLRDLDPAIPVMALGLGSNLIVRDGGFPGVVVRLGKAFAKVEPIDATTLRCGGGASGILVSSTARDAGIAGMEFLRSIPGTVGGFVRMNGGAYGGEVKDILVDCDVVLRSGERKTLALADLGYTYRHSELPEGAVVVGATFRGRPGASAAIQAEMDRISASREASQPLRSRTGGSTFKNPAGHKAWQLVDAAGCRGLMVGGAQVSEKHTNFLINTGDATSADIEALGEEVRRRVKDKSGIELQWEIQRVGKAE
|
Cell wall formation.
|
Q1GRY1
|
P29396
|
RL7_THEMA
|
50S ribosomal protein L7/L12
|
Thermotoga
|
MTIDEIIEAIEKLTVSELAELVKKLEDKFGVTAAAPVAVAAAPVAGAAAGAAQEEKTEFDVVLKSFGQNKIQVIKVVREITGLGLKEAKDLVEKAGSPDAVIKSGVSKEEAEEIKKKLEEAGAEVELK
|
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation.
|
P29396
|
B3EWP2
|
HYAL_CRODU
|
Venom spreading factor
|
Crotalus
|
MQAKAPMYPNEPFLVFWNAPTTQCRLRYKVDLDLNTFHIVTNAR
|
Snake venom endo-hyaluronidase that degrades hyaluronan to smaller oligosaccharide fragments. In venom, it is not toxic by itself, but increases the diffusion of other venom proteins such as crotoxin (a neurotoxic and myotoxic PLA2) by degrading the extracellular matrix. In addition, it displays antiedematogenic activity, since it significantly diminishes the oedematogenic activity of crotoxin (probably by direct substrate hydrolysis, since hyaluronan possesses strong water-binding capacity).
|
B3EWP2
|
A7ZYL1
|
AROA_ECOHS
|
5-enolpyruvylshikimate-3-phosphate synthase
|
Escherichia
|
MESLTLQPIARVDGTINLPGSKSVSNRALLLAALAHGKTVLTNLLDSDDVRHMLNALTGLGVSYTLSADRTRCEIIGNGGPLHAEGALELFLGNAGTAMRPLAAALCLGSNDIVLTGEPRMKERPIGHLVDALRLGGAKITYLEQENYPPLRLQGGFTGGNVDVDGSVSSQFLTALLMTAPLAPEDTVIRIKGDLVSKPYIDITLNLMKTFGVEIENQHYQQFVVKGGQSYQSPGTYLVEGDASSASYFLAAAAIKGGTVKVTGIGRNSMQGDIRFADVLEKMGATICWGDDYISCTRGELNAIDMDMNHIPDAAMTIATAALFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGHDYIRITPPEKLNFAEIATYNDHRMAMCFSLVALSDTPVTILDPKCTAKTFPDYFEQLARISQAA
|
Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.
|
A7ZYL1
|
A8YUJ8
|
ATPD_LACH4
|
F-type ATPase subunit delta
|
Lactobacillus
|
MALSREEVAARYGAALFGYAQDNKVLDNVYDEMMELKKAVIATPQVISVLSDPILNSKDKKDFLTAIEKNFSEEVQGFLNLLLEYDRFAYLVDIIDQFAVLYDDKNKIASGTATTAVKLDDDQLKRLGDGFAKKYNLNTVRLENKVDPSILGGVILQVKDRVIDGSVKNKLKKIRAQIIDEN
|
This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction.
|
A8YUJ8
|
Q02RB4
|
RNH2_PSEAB
|
Ribonuclease HII
|
Pseudomonas
|
MQLGLDFNLVEDLVAGVDEVGRGPLCGPVVTAAVILDPSRPILGLNDSKKLSEARREALFEEIREKALAWCIARAEVEEIDRLNILHATMLAMQRAVEGLSVTPRLALIDGNRCPKLAVPSAPVVKGDSQVPAIAAASILAKVSRDREMVELDRVYPGYGMAGHKGYPTAVHLEALSRLGPTPIHRRSFAPVRELLDVPVQ
|
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
|
Q02RB4
|
Q3ABX8
|
RUVC_CARHZ
|
Holliday junction resolvase RuvC
|
Carboxydothermus
|
MKIIGIDPGTAIVGVGVLEKKNGKLIVKNFQAITTPPIAKEKRLKIIFQKLNEILIQEKPEIVVVEELFFSKNVKTAISVGEARGVVLLASALNDIPVLELKPVEVKTIVTGYGHAPKSQVEYMIAKLLGLKTPPKPDDVADALAIAYAGFLKMGGLL
|
Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group.
|
Q3ABX8
|
O08983
|
HPS1_MOUSE
|
Hermansky-Pudlak syndrome 1 protein homolog
|
Mus
|
MKCVLVATEGAEVLFYWTDEEFAESLRLKLQQSEDEEEELPVLEDQLSTLLAPVIISSMTMLEKLSDTYTCFSTENDNHLYVLHLFGEYLFVAINGDHSESEGDLRRKLCVLKYLFEVHFGLVTVDGQLIRKELRPPDLEERARVWKHFQRLLGTYSYLRDREQSFAVEAVERLIHPQLCEQSIETLERHVVQAINASPERGGEEVLHAFLLVHCKLLAFYSGHGASTLRPADLLALILLVQDLQPSPGTTEEEEEEEDSDSPQRRPKSSQNIPVQQARSQSTSVPTRSSRETDTDSISLPEEYFTPAPSPGDQSSGSLVWLDGGTPPSDALQMAEDTPEGLASHSPELPSPRRIFLDANIKENYCPLVPHTMYCLPLWPGINMVLLTKSPSTPLALILYQLLDGFSLLEKKLKEGQEAGSALRSQPFVADLRQKMDKFIKNRVGQEIQNTWLEFKSKAFSRSEPGSSWELLQVCGKLKRQLCVIYRLSFLVTAPSRGGPHLPQHLQDRAQKLMKERLLDWKDFLLVKSRRNVTMVSYLEDFPGLVHFIYVDRTTGQMVAPSLSPNEKMSSELGKGPLAAFVKAKVWALVRLARRYLQKGCTTLLFQEGDFRCSYFLWFENDMGYKLQMIEVPVLSDDSVPIGVLGGDYYRKLLRYYSKSHPSEPVRCYELLTLHLSVIPTDLLVQQASQLARRLGEASRVTLP
|
Component of the BLOC-3 complex, a complex that acts as a guanine exchange factor (GEF) for RAB32 and RAB38, promotes the exchange of GDP to GTP, converting them from an inactive GDP-bound form into an active GTP-bound form. The BLOC-3 complex plays an important role in the control of melanin production and melanosome biogenesis and promotes the membrane localization of RAB32 and RAB38.
|
O08983
|
Q9UGJ1
|
GCP4_HUMAN
|
Gamma-ring complex protein 76 kDa
|
Homo
|
MIHELLLALSGYPGSIFTWNKRSGLQVSQDFPFLHPSETSVLNRLCRLGTDYIRFTEFIEQYTGHVQQQDHHPSQQGQGGLHGIYLRAFCTGLDSVLQPYRQALLDLEQEFLGDPHLSISHVNYFLDQFQLLFPSVMVVVEQIKSQKIHGCQILETVYKHSCGGLPPVRSALEKILAVCHGVMYKQLSAWMLHGLLLDQHEEFFIKQGPSSGNVSAQPEEDEEDLGIGGLTGKQLRELQDLRLIEEENMLAPSLKQFSLRVEILPSYIPVRVAEKILFVGESVQMFENQNVNLTRKGSILKNQEDTFAAELHRLKQQPLFSLVDFEQVVDRIRSTVAEHLWKLMVEESDLLGQLKIIKDFYLLGRGELFQAFIDTAQHMLKTPPTAVTEHDVNVAFQQSAHKVLLDDDNLLPLLHLTIEYHGKEHKADATQAREGPSRETSPREAPASGWAALGLSYKVQWPLHILFTPAVLEKYNVVFKYLLSVRRVQAELQHCWALQMQRKHLKSNQTDAIKWRLRNHMAFLVDNLQYYLQVDVLESQFSQLLHQINSTRDFESIRLAHDHFLSNLLAQSFILLKPVFHCLNEILDLCHSFCSLVSQNLGPLDERGAAQLSILVKGFSRQSSLLFKILSSVRNHQINSDLAQLLLRLDYNKYYTQAGGTLGSFGM
|
Gamma-tubulin complex is necessary for microtubule nucleation at the centrosome.
|
Q9UGJ1
|
A1SMP3
|
MDH_NOCSJ
|
Malate dehydrogenase
|
Nocardioides
|
MSSTPLKVAVTGAAGQIGYSLLFRLASGSLLGDRPIELRLLEITPALKALEGVVMELDDCAFPNLAGVQIGDDAEQIFDGVNLALLVGARPRGPGMERGDLLSANGAIFTAQGKALNKVAADDVRIGVTGNPANTNALIAMTNAPDIPQARFSALTRLDHNRAISQLAAKTGAAVTDIKKMTIWGNHSATQYPDVFHAEIGGRNAAEVVGDQDWIESTFIPTVAKRGAAIIEARGSSSAASAASATIDAARDWLFGSADADWVSMAVVSDGSYGVPEGLISSFPVTTKDGDWEIVQGLEIDDFSRAKIDASTAELADEREAVKELGLI
|
Catalyzes the reversible oxidation of malate to oxaloacetate.
|
A1SMP3
|
O62667
|
S28A1_PIG
|
Solute carrier family 28 member 1
|
Sus
|
MEDNTPRQRDPISLTSVANGLENMGAELLESLEEGRAPGSDSSPAEVGGGWSKAGPEHLGRRSLQPALRVRRFCREHTQLFRWICTGLLCTAFAAFLLIACLLDFQRALALFVLFCVVLFFLAHSLLKRLLGPKLLRCVKPLRHPCLNLWFKRGLALAAFLGLVLWLVLDTAQRPEQLVSFGGICVFILLLFAGSKHHRAVSWRAVSWGLGLQFALGLFVIRTEPGFIAFQWLGDQIQIFLSYTEAGSSFVFGEALVKDVFAFQVLPIIVFFSCAMSVLYYVGLMQWVILKISWLMQATMGTTATETLSVAGNIFVSQTEAPLLIRPYLADMTLSEIHVVMTGGYATIAGSLLGAYISFGIDAASLIAASVMAAPCALALSKLVYPEVEESKFKREEGVKLTYGDAQNLLEAASSGAAMSVRVVTNIAANLIAFLAVLAFINAALSWLGDMVDVQGLSFQLICSYVLRPVAFLMGVAWEDCPVVAELLGMKLFLNEFVAYQELSGYKQRRLAGAEEWVGSRKQWISVRAEILTTYALCGFANFSSIGIMLGGLTSMVPQRKGDFSQIVLRALCTGACVSLVNACVAGILYVPRGAEVDCVSFLNTTLSSSSFEVYQCCRQFFQSTSLEFSPEALDNCCRFYNHTICV
|
Sodium-dependent and pyrimidine-selective transporter. Exhibits the transport characteristics of the nucleoside transport system cit or N2 subtype (N2/cit) (selective for pyrimidine nucleosides and adenosine). Transports uridine, cytidine, thymidine, and nucleoside-derived drugs.
|
O62667
|
B4RJC9
|
HSLO_NEIG2
|
Heat shock protein 33 homolog
|
Neisseria
|
MNQTAINRADARTRFIFDDMPVRGLHVRLENVWQHIVKQKNYPAAIRCALGELLAAGVLLSGNLKNEGTLIVQVQGQGKLKMLVAEATSDRTVRATARWDETAEIADDESLGDLLGGNGVFVLTLQPKDGEPWQGVVPLEGGSIAQMLVNYMKRSEQLDTHIALSASDEAAGGLLVQRLPEEVLDEEAWEHVSTLARTLTAEELAELDAQHVLYRLFHETPPRVFEPETFESSCTCSRGKVSDMLLMLGGEEVGGVVAEQGSIEVDCDFCHSKYVFDETDVNALFGEDVVGVAKGLPRHTVQ
|
Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.
|
B4RJC9
|
Q6LM60
|
CYSH_PHOPR
|
PAdoPS reductase
|
Photobacterium
|
MPNYALADLLEKTKIEQILQLAEINAELEALSAQERVRWALANLGSEFALASSFGIQSAVMLHLVTNESPKVPVILTDTGYLFPETYQFIDQLTLRLSLNLYVYRAEISSAWQEARHGKLWEQGVDGIKQYNRLNKVEPMRRALDELNVSAWFSGLRREQSSSRASLPVLAIQNGVFKFLPLIDWTDNDIEQYLNQYDLPYHPLRDEGYLSMGDTHTTKKWEPGMTEEETRFFGLKRECGLHEEDAESDGSGI
|
Catalyzes the formation of sulfite from phosphoadenosine 5'-phosphosulfate (PAPS) using thioredoxin as an electron donor.
|
Q6LM60
|
Q95KM6
|
CLD2_CANLF
|
Claudin-2
|
Canis
|
MASLGLQLVGYILGLLGLLGTLVAMLLPSWRTSSYVGTSIVTAVGFSKGLWMECATHSTGITQCDIYSTLLGLPADIQAAQAMMVTSSAISSLACIVSVVGMRCTVFCQDSRAKDRLAVVGGVFFIIGGLLGFIPVAWNLHGILRDFYSPLVPDSMKFEIGEALYLGIISSLFSLVAGIILCFSCPLQGNRSDYYDSYQAQPLATRGSPRPGQPPKAKSEFNSYSLTGYV
|
Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.
|
Q95KM6
|
Q6CLS0
|
MCA1_KLULA
|
Metacaspase-1
|
Kluyveromyces
|
MYPGRAKPTYNNQQAQQAQSQVGYQTGYSNAQPQQQYYTAPQQQNVSGSSMSFQHQFYPPPNQSPPQYNTGQYARPAAPPPGQQNYRNDIQQNHASGTVNGPSGYQQPQAMYKPPSQVQHTGPNNQVAYQYSQCTGRRKALLIGINYFGSANELRGCINDSHNMFNFLTQRYGYKAEDIVMLNDDTTDPVRVPTKANMLRAMQWLVKDARPNDALFFHYSGHGGQTEDLDGDEEDGMDDVIYPVDFQMAGHIVDDDMHAIMVSPLQPGVRLTALFDSCHSGTVLDLPYTYSTKGVIKEPNMWKDVGSSGLQAAMAYATGNTTSLVSSLGNVFTTITKSNNNVDRERVKQIKFSPADVIMFSGSKDNQTSADATENGQNTGAMSWAFLTVLSKQPQQSYLSLLQNMRAELSSKYTQKPQLSCSHEIDTNLQFLL
|
Involved in cell death (apoptosis).
|
Q6CLS0
|
B2UMP4
|
GATA_AKKM8
|
Glutamyl-tRNA(Gln) amidotransferase subunit A
|
Akkermansia
|
MSKIQGTLAQWRDRLRRKELSPAELVNLTADAIEADRTTNAYISFDREAALHAAAGADISSPLAGIPIAVKDNINVLGQPTRCASRLLSPYVAPYDATSIRLLKEAGGIPLGRTNMDEFAMGASGENSAYGITRNPEAPDRIPGGSSSGSAAAVASATAIAALGSDTGGSIRQPAGHCGIVGLKPTYGRVSRYGLVAFASSLDQIGPMTRTVEDAAILLQAISGHDRKDSTSANCPVPDFEAALGRDVKGLKVGIPSEYFTSGNHPGISEAVQNTVKQLESLGAELVEVNLPHADAVVAAYYIIACAEASSNLSRFDGVRYGKRAEDAAGLVELFSRTREEGFGPEVKRRIILGTYVLSSGYYDAYYSRAQKVRSLVARDFAEAFSRVDIIVGPTSPAPAPKIGDSALDHLQTYLADIYTIPANLAGLPAMSIPCGTVRESGMELPVGFQMMAPHFREDLLLKTGFALGK
|
Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
|
B2UMP4
|
Q9RU88
|
NUOC_DEIRA
|
NDH-1 subunit C
|
Deinococcus
|
MTAPDAGLPETNLRDTAARSTRRLAESRDVAPLLAELGLSAEEGLQPTAAVEAGELLHTAQQLRARGFMLLDVIGVDYSRYTAPRPQPFAVLYSVAHPRDHRRLFLRVWLSEGEAVDSLFPIWKAANYLEREVYDLLGIEFTGHPDLRKVLTPDDLEGHPLRKDFPLGETPTLFREGRFLDPAAFRAGLSGQQRGLTGYRGEMRRGERRREDIVPPLLPEGGPK
|
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
|
Q9RU88
|
Q4QLF7
|
MURC_HAEI8
|
UDP-N-acetylmuramoyl-L-alanine synthetase
|
Haemophilus
|
MKHSHEEIRKIIPEMRRVQQIHFIGIGGAGMSGIAEILLNEGYQISGSDIADGVVTQRLAQAGAKIYIGHAEEHIKGASVVVVSSAIKDDNPELVASKQKRIPVIQRAQMLAEIMRFRHGIAVAGTHGKTTTTAMISMIYTQAKLDPTFVNGGLVKSAGKNAHLGASRYLIAEADESDASFLHLQPMVSVVTNMEPDHMDTYEGDFEKMKATYVKFLHNLPFYGLAVMCADDPVLMELVPKVGRQVITYGFSEQADYRIEDYEQTGFQGHYTVICPNNERINVLLNVPGKHNALNATAALAVAKEEGIANEAILEALADFQGAGRRFDQLGEFIRPNGKVRLVDDYGHHPTEVDVTIKAAREGWGDKRIVMIFQPHRYSRTRDLFDDFVQVLSLVDALIMLDVYAAGEAPIVGADSKSLCRSIRNLGKVDPILVSDTSQLGDVLDQIIQDGDLILAQGAGSVSKISRGLAESWKN
|
Cell wall formation.
|
Q4QLF7
|
C5D9D1
|
RBFA_GEOSW
|
Ribosome-binding factor A
|
unclassified Geobacillus
|
MNLRATRVGEQMKKELSDIIGRKLKDPRIGFVTVTDVRVTGDLQQAKVYISVLGDEEQRQNTLKGLEKAKGFIRSEIGQRIRLRKTPEIFFEIDESIEYGNRIEQLIRQISTEHEGGKKEEENKEE
|
One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Associates with free 30S ribosomal subunits (but not with 30S subunits that are part of 70S ribosomes or polysomes). Required for efficient processing of 16S rRNA. May interact with the 5'-terminal helix region of 16S rRNA.
|
C5D9D1
|
B2RLV5
|
RSGA_PORG3
|
Small ribosomal subunit biogenesis GTPase RsgA
|
Porphyromonas
|
MDGVVIKNTGSQYLVRCTDGTELYCMAKGNLRLKGIRSTNPVAVGDRVEIVPASQDGQPAYIKRIHPRRNYIIRRASNLSKESHILGANLDAAVLVCTINDPVTTTVFIDRFLATAEAYRVPVILAFNKIDCYTQEDRLQLDRLSAVYTAIGYPCCHVSAITGEGLPDLKSLLDGKLTLLAGHSGVGKSSLINALIPHADLRTGAISQAHHTGMHTTTFSQMIDFPDLSPGSALIDTPGIKGFGTLEMGEYEVSHYFPEIFAASKGCRFGNCTHTHEPGCAVLEALRRGEIAESRYISYLSILEDENAERYRPEY
|
One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase that catalyzes slow GTP hydrolysis, GTPase activity is stimulated by the 30S ribosomal subunit.
|
B2RLV5
|
A7FDT5
|
AAEA_YERP3
|
p-hydroxybenzoic acid efflux pump subunit AaeA
|
Yersinia
|
MSTFSLKIIRVGITVLVVVLAVIAIFNVWAFYTESPWTRDAKFTADVVAIAPDVSGLLTEVPVKDNQLVQKGQILFVIDQPRYQQALAEAEADVAYYQTLAAEKQREFSRRHLLGIQALSQEEIDQASNVLQTVQHQLAKTIAVRNLARLDLERTTIRAPAEGWVTNLNVHAGEFINRGATAVALVKKDTFYILAYLEETKLEGVKPGYRAEITPLGSNRILHGTVDSISAGVTNSSSSADSKGLATIDNNLEWVRLAQRVPVKIHLDSEDQQYLYPAGTTATVVITGPNDRDPHQASPMTKLMHRLREFG
|
Forms an efflux pump with AaeB.
|
A7FDT5
|
A1JJ57
|
LSRK_YERE8
|
Autoinducer-2 kinase
|
Yersinia
|
MSQFSTTTSGDYLMALDAGTGSVRAVIFDLNGNQIAAGQAEWLHLPVPDVPGSMEFDLTTNWKLTCQCIRQALHQANLPASAIRAVAACSMREGIVLYDRSGKPIWACANVDARASREVSELKELYNNGFELEVYQCSGQTLALSAMPRLLWLAHYRPDIYRQAGTLTMISDWLANMLSGELAVDPSNAGTTGMLDLVTRNWQPNLLEMAGLRADILSPVKETGTLLGHVTAEAAQECGLLAGTPVVMGGGDVQLGCLGLGVVQPGQTAVLGGTFWQQVVNLPKPITDPNMNTRINPHVIPGMVQAESISFFTGLTMRWFRDAFCAEEKLLAQRLGIDTYSLLEDMAARVPAGAYGVMPIFSDVMRFKSWYHAAPSFINLSLDPEKCNKATLFRALEENAAIVSACNLAQIAEFSGVKASSVVFAGGGAKGKLWSQILADVTGIPVRVPVVKEATALGCAIAAGVGVGLYEALDKTGEQLVRWEREYQPNIEHKALYQAAKTNWQAVYTDQLTLVDSGLTTSLWKAPGL
|
Catalyzes the phosphorylation of autoinducer-2 (AI-2) to phospho-AI-2, which subsequently inactivates the transcriptional regulator LsrR and leads to the transcription of the lsr operon. Phosphorylates the ring-open form of (S)-4,5-dihydroxypentane-2,3-dione (DPD), which is the precursor to all AI-2 signaling molecules, at the C5 position.
|
A1JJ57
|
Q9YDX2
|
TRMY_AERPE
|
tRNA (pseudouridine(54)-N(1))-methyltransferase
|
Aeropyrum
|
MSLYVVISPTGRTDGNIPARGYAGPSGRLDVIARAYNAILEPNATLAALLMGGPLPPRLLIAPLSCKDIVRSERSFMIEASRALRGRRSCFTVNDEGVEALASLLRRFKPRILLAEKGGDISSHWGEMCSSSPTFIAGSHLDPPHGLIKHLERSLGGFLRVSVGPLSLHTDHVFLLVSALRLPMHATSIEHH
|
Specifically catalyzes the N1-methylation of pseudouridine at position 54 (Psi54) in tRNAs.
|
Q9YDX2
|
Q9SVL0
|
ZHD7_ARATH
|
Homeobox protein 28
|
Arabidopsis
|
MELGGKCNAITTTTMISTEVKPHTDPEPEAKPESDPSMALFPIKKENQKPKTRVDQGAKYRECQKNHAASTGGHVVDGCCEFMAGGEEGTLGALKCAACNCHRSFHRKEVYGHRNSKQDHQLMITPAFYSSNSSYKPRVMHPTGEIGRRTSSSSEDMKKILSHRNQNVDGKSLMMMMMRKKKRVRTKINEEQKEKMKEFAERLGWRMQKKDEEEIDKFCRMVNLRRQVFKVWMHNNKQAMKRNNSNISE
|
Putative transcription factor.
|
Q9SVL0
|
Q2K7B5
|
COBQ_RHIEC
|
Cobyric acid synthase
|
Rhizobium
|
MARTIMLQGTGSDVGKTVLVAGLCRLAANAGLTVRPFKPQNMSNNAAVADDGGEIGRAQWLQSMAARTPSSVHMNPVLLKPQSENGSQIIVQGRVFGQAKGRDYQRLKPQLLGAVLESFENVCAGADLVVVEGAGSPAEINLRTGDIANMGFATKAGVPVVLVGDINRGGVIASLVGTQAILDEGDRAMIAGYLINKFRGDVSLFDDGIRAIEGFTGWPCFGVVPWLQAATRLPAEDSVVLERLARSGTGALKIAVPMLPRIANFDDLDPLRAEADVELVFVRGGERLPADASLVILPGSKSTISDLADLRVQGWDRDLAAHVRRGGRVIGICGGYQMLGRTVRDPLGIEGGRIEAAGLALLDVETEMAPEKTVRNSQARSSEYDVSLAGYQIHLGVTRGPDCVRPSAIIDGAPDGALSADGRIMGTYLHGLFGSDAYRARLLQSFGLSGERRNYRDSVEQALDEIAGELERHLDPHWLAGLLG
|
Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation.
|
Q2K7B5
|
Q65RY3
|
MRAY_MANSM
|
UDP-MurNAc-pentapeptide phosphotransferase
|
Basfia
|
MLVWFAKFLEQYYSGFNVVSYLTFRSVLALLTALLLSLWIGPKMIRRLQIFKFGQEVRNDGPESHFQKRGTPTMGGLMILATITVSTLLWGDLSNPYIWFSLFVLLGYGAIGFVDDYRKIKYKNTDGLIARWKYFWLSLVSLIAIFGMYALGKDTDATRLVVPFFKEIMPQLGLFYVVLAYFVIVGTSNAVNLTDGLDGLAIMPTVFVAGAFAIIAWATGNVEISKYLYIPYIKYTSELVIFCTAIVGAGLGFLWFNTYPAQVFMGDVGSLALGGALGTIAVLVRQEFLLVIMGGVFVMETVSVILQVGSYKLRKKRIFRMAPIHHHYELKGWPEPRVIIRFWIISLMLVLFGLVTLKLR
|
Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
|
Q65RY3
|
Q292E8
|
CIAO1_DROPS
|
Probable cytosolic iron-sulfur protein assembly protein Ciao1
|
Sophophora
|
MGRLILEHTLQGHKGRIWGVAWHPKGNVFASCGEDKAIRVWSLSGNTWSTKTILSDGHKRTIREIRWSPCGQYLASASFDATTAIWSKSSGEFECNATLEGHENEVKSVSWSRSGGLLATCSRDKSVWIWEVAGDDEFECAAVLNAHTQDVKRVVWHPTKDILASASYDNTIKMFAESQLDSDWDCTATLSSHTSTVWSIDFDAEGDRLVSCSDDKTLKIWRAYHPGNDAGIATPDKQSVWKCVCTLSGQHSRAIYDVSWCKLTGLIATGCGDDGIRIFKETSDSKRDEPTFEQLTAEETAHEQDVNAVEWNPAVAGQLISCSDDGTIKIWKVDD
|
Essential component of the cytosolic iron-sulfur (Fe/S) protein assembly machinery. Required for the maturation of extramitochondrial Fe/S proteins.
|
Q292E8
|
P12780
|
NOLJ_RHIFR
|
Host-inducible protein B
|
Sinorhizobium
|
MDIRLDSRRAIQAGPLVTTGRIAGAALRMARPFLGIARRLQFKAKAFELALRSVALQLMNDAMADADEAMEETEEDADALGGPRQEVRAVSDGTIVTEREMTCPQNRYCHECSWTGAAAGQNVAAKGAGAAVPGPNRRTGSGERRGYG
|
Involved in efficiency of soybean nodulation and in nodulation delay.
|
P12780
|
Q4JW94
|
MURC_CORJK
|
UDP-N-acetylmuramoyl-L-alanine synthetase
|
Corynebacterium
|
MSDQLQTTDLSRVHMVGIGGAGMSGIARILLDRGYQVSGSDMKESRSIMALRAAGAQIQVGHAEDNLRLSGEMPTVVVTSFAAIPQDNPELVGAREAGIPVLRRSDILALLLQDRRAFLLAGTHGKTSTTSMAVAALQAAGQDPSFAIGGQLNRAGTNAHNGTGEVFVAEADESDGSFLSYSPEIAVVTNIEPDHLDYFKTESAYREVFEKFAHRIVPGGFLVVCLDDPGSAALAEELIAGAEEGNPLPFTVVGYGTAEGCDAHPSVPPAAIIESTEVTAEGTVSALRLTEEVKKAAEEAAGTYSLRVAIPGIHMVLNAAAAVLGSVLLGADVDKVIAGIGGFDGVRRRFEYHGTRQDVEVYDDYAHHPTEVAAVLAAARQRVEARGGRIVAVFQPHLYSRTMNFADEFAEALSLADQVVLLDIFGAREEPVEGVDSRIIGNKIDASTDWVFEPDFSKVSSVVAGLVQPGDMVLTIGAGTVTMLADEILLELDRGDRG
|
Cell wall formation.
|
Q4JW94
|
A5E598
|
KAD2_LODEL
|
Adenylate monophosphate kinase
|
Lodderomyces
|
MSVEELKDTVHKLHERIQQLEKKVGVLPSSQPDFAKQLRLVLIGAPGSGKGTQSTDLKDKFCACHLATGDMLRSQVKQGTPLGLEAKKIMDQGGLVNDEIMIGMIKQELETNQDCKKGFILDGFPRTIPQAEKLDSMLKDRKTPLENAIELKIDDELLVDRITGRLVHPASGRSYHKIFSPPKKEMTDDITGEPLVQRSDDNEAALKKRLVTYHAQTEPIVEYYKKTGIWQGIDASQKPAKVWKDILKCLGQ
|
Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. Adenylate kinase activity is critical for regulation of the phosphate utilization and the AMP de novo biosynthesis pathways.
|
A5E598
|
A8FX85
|
Y2851_SHESH
|
Nucleoid-associated protein Ssed_2851
|
Shewanella
|
MFGKGGMGNLMKQAQQMQDKMAKVQEEIARMEVTGEAGAGLVKVTMTGSHSVRKVDIDPSLLEDDKEMLEDLIAAACNDAARRVEENQKERMAEVTGGMQLPPGMKMPF
|
Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection.
|
A8FX85
|
A3MWJ1
|
NEP1_PYRCJ
|
16S rRNA (pseudouridine-N1-)-methyltransferase Nep1
|
Pyrobaculum
|
MILVLAEAALELVPESLWRHPAIVADARRRGKKPGEILLDRARHHVAMAKLDKAERRGRPDIVHQVLLAFQYSLLNRAGRGRAFVHTVGDYIISVKPETRVPKNYNNFVSLMEQLFKVGRVPPEGEALMEARRGSLAALLEELGGKWVALHEQGRAVSFAELGRAVADAVVVVGGFPHGDFENKWILEGAEAVYKIGNVSLDAAQAVCRAVAAAEAALGLI
|
Methyltransferase involved in ribosomal biogenesis. Specifically catalyzes the N1-methylation of the pseudouridine corresponding to position 914 in M.jannaschii 16S rRNA.
|
A3MWJ1
|
P35631
|
AP1_ARATH
|
Agamous-like MADS-box protein AGL7
|
Arabidopsis
|
MGRGRVQLKRIENKINRQVTFSKRRAGLLKKAHEISVLCDAEVALVVFSHKGKLFEYSTDSCMEKILERYERYSYAERQLIAPESDVNTNWSMEYNRLKAKIELLERNQRHYLGEDLQAMSPKELQNLEQQLDTALKHIRTRKNQLMYESINELQKKEKAIQEQNSMLSKQIKEREKILRAQQEQWDQQNQGHNMPPPLPPQQHQIQHPYMLSHQPSPFLNMGGLYQEDDPMAMRRNDLELTLEPVYNCNLGCFAA
|
Transcription factor that promotes early floral meristem identity in synergy with LEAFY. Is required subsequently for the transition of an inflorescence meristem into a floral meristem. Is indispensable for normal development of sepals and petals in flowers. Regulates positively the B class homeotic proteins APETALA3 and PISTILLATA with the cooperation of LEAFY and UFO. Interacts with SEPALLATA3 or AP3/PI heterodimer to form complexes that could be involved in genes regulation during floral meristem development. Regulates positively AGAMOUS in cooperation with LEAFY. Displays a redundant function with CAULIFLOWER in the up-regulation of LEAFY. Together with AGL24 and SVP, controls the identity of the floral meristem and regulates expression of class B, C and E genes. Represses flowering time genes AGL24, SVP and SOC1 in emerging floral meristems.
|
P35631
|
A6VXW3
|
HTPG_MARMS
|
High temperature protein G
|
Marinomonas
|
MATDTQKETLGFQTEVKQLLHLMIHSLYSNKEIFLRELISNASDAVDKLRFESVANADLLAEDPNLRVRIEFDKDTNTVVIDDNGVGMSREEAITNLGTIAKSGTSAFLEQLSGDQKKDSQLIGQFGVGFYSAFIVADKVTVETRRAGVAADQAVRWVSDGSGEFTIENIEKDSRGTRIILHLKAGEKEFADNFRLRHLVTKYSDHISIPVEMEKPVYPEMDEEGNPKPVDENKAPEYEAVNSAKALWTRPRNEVTDEEYQEFYKHISHDYQEPLKWSHNKVEGKLEYSSLLYIPSKAPYDLWNRDMQRGLKLYVQRVFIMDEAEAFLPPYMRFVKGVVDSNDLSLNVSREILQNDHAVDSMRSALTKRVLDMLGKMAKNEPEDYQKFWDEFGNVIKEGPADDMGNKDKIAGLLRFSSTHTDAAAQTVSLADYIERMQEGQDKIYYIYAESHNTAKNSPHLEILRKKGFEVLLLSDRIDEWMMSSLQEFEGKSFQDVTKGKLDLADQENEEEKKEKEEKAEKMKPLLDRMKAVLNEKVAGVNSTDRLTNSPACLVVGEYDMGLQMRRLLEQAGQKLPESKPTLEVNPDHPIVAKMDSETDEERFADMAWLLFEQATLSEGGQLEDPATFVSRMNKLIVQLSK
|
Molecular chaperone. Has ATPase activity.
|
A6VXW3
|
O31428
|
SKFF_BACSU
|
Putative bacteriocin-SkfA transport system permease protein SkfF
|
Bacillus
|
MPFLIMLLFVGAIGFQVSFVSRSTTWDMSIAGWVLTGVFILYTAFGLFSNRLPSQMADIIWLYGTATSFSKVVYSVLFFSVTWKALLWIISAIFGDVLIVLLSGDHINLLGRSIIFVGLFFIAEVWLMSVSCARTVKKMKRVYVLVFLLMLGIYSICLYRFFFLQHSSGIWESIARFISGVGLVFDTLSPLYVVVFIGIITVSFMTIAFTSRQVEMKESLVKEAEFWEEFQERQFGSGQIIQKPKTTWWGLQGLNGIWSFLWLELLLFKKYLFFHSIHTVMLSGVFYVVIFMYPEWFYLLFFLIVSAVMLSSYYSGIVRHSQSGTLHLFPGALWKKIIILELTNTVWLYILYCVSITFMAVGNLVYWYIYGLGIYIWFMTIRLFAFTHTNRNDIKLSLPQYYKSFFMALGLSGICLYVIHLLTADWYTLVVVVCIGSLSWCLFYRFR
|
Probably part of the ABC transporter SkfEF involved in the export of the bacteriocin SKF. Probably responsible for the translocation of bacteriocin SkfA across the membrane.
|
O31428
|
P45586
|
CU79A_LOCMI
|
LM-ACP 79A
|
Locusta
|
GFLGGGYGGGLGLGGYGGGYGLGGGLGGGLGGIGLAAAPAVGIAAAPAIGIAAAPATLVRTRVVPGPARLVQPPPVVQKQVIQPPPIVQTRLIQPPAQLVQGPPQVIHEQTPALIKTAVPAPSFGYKSLLH
|
Component of the cuticle of migratory locust which contains more than 100 different structural proteins.
|
P45586
|
A0RR26
|
ATPB_CAMFF
|
F-ATPase subunit beta
|
Campylobacter
|
MKGIISQVMGPVVDVDFKDYLPKINEAIEVNFTVEGNTHKLILETAAHLGDNRVRTIAMDMSEGLTRGLDAIALGSPISVPVGEKVLGRIFNVIGDLIDEGEEEKFDKKWSIHRDPPAFEDQSTKSEIFETGIKVVDLLAPYAKGGKVGLFGGAGVGKTVIIMELIHNVAFKHSGYSVFAGVGERTREGNDLYNEMKESGVLDKVALCYGQMNEPPGARNRIALTGLTMAEYFRDEMGLDVLMFIDNIFRFSQSGSEMSALLGRIPSAVGYQPTLASEMGRLQERITSTKKGSITSVQAVYVPADDLTDPAPATVFAHLDATTVLNRAIAEKGIYPAVDPLDSTSRMLDPQILGEEHYKIARGVQAVLQKYKDLQDIIAILGMDELSEEDKLTVDRARKIEKYLSQPFFVAEVFTGSPGKYVSLEETIAGFKGILEGKYDQLPENAFYMVGNIDEAIAKAEKMRA
|
Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
|
A0RR26
|
Q1J043
|
PRMA_DEIGD
|
Ribosomal protein L11 methyltransferase
|
Deinococcus
|
MLVYHLPGTLDTREADLDLLWAAGATGLEERGGVIRAYFDTRTELPPQVSDGEWREEADQDWLAEFKRTLRPVRAGRVTIVPPWLREEVEAGQLPLVIEPGMAFGTGHHATTRLAVEALSALNLATLGPRGTGARVLDVGTGSGVLAIAAALLGAGFALGVDIDPITIPIARENAQINGIPASRVRFAEGTLGADPLTFPDEGVDTYDVVVANLYAELHDLLAGEYAAHLVPGGALILTGILTVKLPLVHAALDREGFTNVQETLDGEWALVTARAPLG
|
Methylates ribosomal protein L11.
|
Q1J043
|
Q7M8D4
|
RL3_WOLSU
|
50S ribosomal protein L3
|
Wolinella
|
MEFLVEKIGMSRTISVPSTPVTLLKVKDAKVCEVLGNGKALVAYAQGKDANKAIEGQQKKYNLSKEFNRFATLEVANGEAGDQDVAPLAQAVRVKVSLQTKGRGFTGVMKRWNFAGGPAAHGHRFKRRTGSIGNREWPGRVQPGKKMAGQYGNEKVTVQNEIVSFDAENKILVLKGSIPGFNGAFGRIKVVK
|
One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.
|
Q7M8D4
|
Q8H7N9
|
ATL31_ORYSJ
|
RING-type E3 ubiquitin transferase Os03g0188200
|
Oryza sativa
|
MAHRRIALAVLVTLLLSAFRPCLAQQSNDDTSKHHRSATAGGFTPTTVVVLVALITAFVLLTVFSVLINRCAQARAPPRRAFRSTASHQPVGGAAAASRASRGLDKEVVEAFPTAVYGDVKARMAAKSGPLECAVCLAEFADSDELRVLPACCHVFHPDCIDPWLAAAVTCPLCRANLTAPPVSLAAAESSDLTAPEEAVQEEESEELDEASLMATFTPESVIDFGATHDHEFDRAGYPHYRRTQSAMDAAPDRHTLRLPEHVMKELAADRRHRRAASLAGYPDSVERTPRWLTSLWRSVSWQRQSRADWDAGEEHGGSKRVHPVAGAQDETPSGSGSDGSKENSDSDALNRV
|
Possesses E3 ubiquitin-protein ligase in vitro.
|
Q8H7N9
|
P14491
|
RLX3_STAAU
|
Protein rlx
|
Staphylococcus
|
MATTKISSTKSTSRAINYAEKRAEEKSALNCDIDYAKSSFKATREMYGKTDGNEGHVVIQSFKPNEVTPEQCNQLGLELAEKIAPNHQVAVYTHNDTDHVHNHIVINSIDLETGKKFNNNKKALHDIRQANDEICVSHNLSIPEEKAKLRYTQAEYSVLNKGKTSWKDEIRHAIDQSQAASYEELGNDLQQNGIKIERITDKTITYRHLEEDKKVRGKKLGEDYDKGGLEIGFNRQNEQREEQARQRELEQARREKIKRDKEREKEWARFNRSTQAIRQNRERSEREERERERKARELEEQNRRAREERARQERENKHTHEKTRGFDLEL
|
This protein is probably required for relaxation complex formation and plasmid mobilization by conjugative plasmids.
|
P14491
|
C4LBQ6
|
SURE_TOLAT
|
Nucleoside 5'-monophosphate phosphohydrolase
|
Tolumonas
|
MKILVSNDDGVNAQGLHCLSEALCSLGEVIVVAPDRNRSGASNSLTLENPIRVETLETGKRYSVKGTPTDCVHFAVNKLLDPWPDIVVSGINHGANLGDDVIYSGTVAAATEGRHMGLPAVAVSLVGETHFASAAHYACLLVSRLRTHPLPSDQILNVNVPDLPLEQIKGIKVTRLGNRHRGEKMIVMQDPRGKPVYWIGPPGEKQDAGEGTDFHAIEQGYVSITPLQVDMTAYGSVSELTTWVGEFK
|
Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
|
C4LBQ6
|
Q04KR8
|
MNME_STRP2
|
tRNA modification GTPase MnmE
|
Streptococcus
|
MITREFDTIAAISTPLGEGAIGIVRLSGTDSFAIAQKIFKGKDLNKVASHTLNYGHIIDPLTGKVMDEVMVGAMKSPKTFTREDIIEINTHGGIAVTNEILQLAIREGARLAEPGEFTKRAFLNGRVDLTQAEAVMDIIRAKTDKAMNIAVKQLDGSLSDLINNTRQEILNTLAQVEVNIDYPEYDDVEEATTAVVREKTMEFEQLLTKLLRTARRGKILREGISTAIIGRPNVGKSSLLNNLLREDKAIVTDIAGTTRDVIEEYVNINGVPLKLIDTAGIRETDDIVEQIGVERSKKALKEADLVLLVLNASEPLTAQDRQLLEISQDTNRIILLNKTDLPETIETSKLPEDVIRISVLKNQNIDKIEERINNLFFENAGLVEQDATYLSNARHISLIEKAVESLQAVNQGLELGMPVDLLQVDLTRTWEILGEITGDATPDELITQLFSQFCLGK
|
Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
|
Q04KR8
|
Q47DK8
|
GUAA_DECAR
|
Glutamine amidotransferase
|
Dechloromonas
|
MSHQKILILDFGSQVTQLIARRVREAKVFCEIHPYDVSEEFIRNYGAKGIILSGGPSSVTEGDTPRAPEVVFQLGVPVLGICYGMQTMAQQLGGKVMTAEAAGKSREFGYSEVRAHGHTALLNDIADFYSPEGHGMLKVWMSHGDSVMELPAGFVKMASTASCPIAAMADESRKFYAVQFHPEVTHTQQGRAILERFVHGICGCGTDWVMGDYIAEAVDAIRRQVGDEEVILGLSGGVDSSVAAALIHKAIGDQLTCVFVDHGLLRLNEGDMVMEMFARNLGVKVIRVDAVDDFMGKLAGVSDPEQKRKIIGKEFVEVFQVESKKLAAAKWLAQGTIYPDVIESAGKGKKGAHTIKSHHNVGGLPEDMHLKLLEPLRELFKDEVRELGIALGLPREMVYRHPFPGPGLGVRILGEVTLKAAHLLQRADAIFIDELRATHATERDVAAGACTEADIGKSWYDLTSQAFAVFLPVKSVGVMGDGRTYENVVALRAVVTSDFMTAHWAHLPYELLGRVSNRIINEVRGLNRVVYDVSGKPPATIEWE
|
Catalyzes the synthesis of GMP from XMP.
|
Q47DK8
|
Q8XKN1
|
RNZ_CLOPE
|
tRNase Z
|
Clostridium
|
MLNVTLLGTGGGMPMPNRFLSSVVMNFNGRKILLDCGEGTQVSMRVNGTGFKSIDIICISHLHGDHIYGLPGLLSTIGNSGRVEDIYIIGPNGIKEVIEGFLITLPYLPYKLNILEDASNLEFMVKKEKIELVELNEKISSDLTIETLGLDHSSPCLGYSFNIRRGRKFNVEKALMNKVPKELWSKLQRNEEVSLNGVKYYSYMVLGDERKGIKLSYTTDTRPTEDIPGFIKESDLYICEGTYGSEEDMHKAIKNKHMTFKEAANLAKKGQVKELLLTHFSPSINDPKEFINNAREVFENLHAGSDGEERVLNFKE
|
Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.
|
Q8XKN1
|
A7H8W4
|
DEOB_ANADF
|
Phosphodeoxyribomutase
|
unclassified Anaeromyxobacter
|
MDRRRFVILVADSVGCGALPDARAYGDEGSDTLGNTSRAVGGLSLPVLGRMGIGHLTPILGVPPEPSPLAFHGRMAERSQGKDTITGHWEMMGIVLSEPLALFPRGFPPEILDPFLRETGLPGVLGNVAASGTEIIRELGEEHQRTGMPIVYTSADSVFQIAAHEETVPLETLYAWCRVARRILDPYRVARVIARPFVGKPGEYVRTYHRKDFSIATPGRTVLEKLVDARVPVVGVGKIPDIFDRKGITDELHTAGNADGLAKTEALLDRVDHGLVFVNLVDFDMLYGHRNDPQGYARALEEMDRALPRILGKLRPGEVAALTADHGCDPTTPSTDHSREYVPLVVHAPGRGGGALGTRGSFADLGATVADFFGVRHETGRSFLGDLGP
|
Phosphotransfer between the C1 and C5 carbon atoms of pentose.
|
A7H8W4
|
Q969M3
|
YIPF5_HUMAN
|
YPT-interacting protein 1 A
|
Homo
|
MSGFENLNTDFYQTSYSIDDQSQQSYDYGGSGGPYSKQYAGYDYSQQGRFVPPDMMQPQQPYTGQIYQPTQAYTPASPQPFYGNNFEDEPPLLEELGINFDHIWQKTLTVLHPLKVADGSIMNETDLAGPMVFCLAFGATLLLAGKIQFGYVYGISAIGCLGMFCLLNLMSMTGVSFGCVASVLGYCLLPMILLSSFAVIFSLQGMVGIILTAGIIGWCSFSASKIFISALAMEGQQLLVAYPCALLYGVFALISVF
|
Plays a role in transport between endoplasmic reticulum and Golgi. In pancreatic beta cells, required to transport proinsulin from endoplasmic reticulum into the Golgi .
|
Q969M3
|
Q1JF50
|
PEPX_STRPD
|
X-prolyl-dipeptidyl aminopeptidase
|
Streptococcus
|
MRYNQFSYIPTSLERAAEELKELGFDLDLQKTAKANLESFLRKLFFHYPDSDYPLSHLIAKNDMDALSFFQSEQELSKEVFDLLALQVLGFIPGVDFTEADAFLDKLAFPIHFDETEIIKHIHHLLATRCKSGMTLIDDLVSQGMLTMDNDYHFFNGKSLATFDTSQLIREVVYVEAPLDTDQDGQLDLIKVNIIRPQSQKPLPTLMTPSPYHQGINEVANDKKLYRMEKELVVKKRRQITVEDRDFIPLETQPCKLPIGQNLESFSYINSYSLNDYFLARGFANIYVSGVGTAGSTGFMTSGDYAQIESFKAVIDWLNGRATAYTSHSKNHQVRADWANGLVCTTGKSYLGTMSTGLATTGVDGLAMIIAESAISSWYNYYRENGLVCSPGGYPGEDLDVLTELTYSRNLLAGDYLRHNDRYQELLNQQSQALDRQSGDYNQFWHDRNYLKNAHQIKCDVVYTHGLQDWNVKPRQVYEIFNALPSTINKHLFLHQGEHVYMHNWQSIDFRESMNALLCQKLLGLANDFSLPEMIWQDNTCPQNWQERKVFGTSTIKELDLGQELLLIDNHYGEDEFKAYGKDFRAFKAALFEGKANQALVDILLEEDLPINGEIVLQLKVKSSENKGLLSAQILDYGKKKRLGDLPIALTQSSIDNGQNFSREPLKELPFREDSYRVISKGFMNLQNRNNLSSIETIPNNKWMTVRLPLQPTIYHLEKGDTLRVILYTTDFEHTVRDNSNYALTIDLSQSQLIVPIASN
|
Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline.
|
Q1JF50
|
Q99Y98
|
ALR_STRP1
|
Alanine racemase
|
Streptococcus
|
MISSFHRPTVARVNLQAIKENVASVQKHIPLGVKTYAVVKADAYGHGAVQVSKALLPQVDGYCVSNLDEALQLRQAGIDKEILILGVLLPNELELAVANAITVTIASLDWIALARLEKKECQGLKVHVKVDSGMGRIGLRSSKEVNLLIDSLKELGADVEGIFTHFATADEADDTKFNQQLQFFKKLIAGLEDKPRLVHASNSATSIWHSDTIFNAVRLGIVSYGLNPSGSDLSLPFPLQEALSLESSLVHVKMISAGDTVGYGATYTAKKSEYVGTVPIGYADGWTRNMQGFSVLVDGQFCEIIGRVSMDQLTIRLPKAYPLGTKVTLIGSNQQKNISTTDIANYRNTINYEVLCLLSDRIPRIY
|
Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
|
Q99Y98
|
Q6LPI7
|
PYRC_PHOPR
|
Dihydroorotase
|
Photobacterium
|
MTTITITRPDDWHVHLRDGDVLKDTVRDISRYMGRAIIMPNLIPPVIDTESALSYRERIIAQGPQGNFSPLMVIYLTDNTSAEEIHKAKASGHVYAAKLYPAGATTNSDSGVTSIDHIRPALQAMQEAGMQLLIHGEVTAHDIDIFDREKVFLETVLAPIVEQFPNLRMVLEHITTADAVEFVTNAGPNVGATITAHHLMFNRNHMLVGGIRPHFYCLPILKRNIHQDALVKAATSGNPKFFLGTDSAPHAQGRKESACGCAGSYTAHAAIELYAEVFEAADALDKLEAFSSFNGPDFYNLPRNTDTITLKKESWNVPETMAFGGDEVVPIRAGEAMLWKVI
|
Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
|
Q6LPI7
|
A7NIW0
|
NUOC_ROSCS
|
NDH-1 subunit C
|
Roseiflexus
|
MALDNPTVLARLQAALPDALLGSSEFRGDLSVHVRPERIVDVARFLRDDPELRYHFLENLCGVDYLGREPRFEVVYHLLSFANRHRICLKVGVSERNPSVPSLTELWPGANYHERETFDMFGIVFTGHPCLDRILMPEDWEGHPLRKDVPLGAEEVAFTFNQDRIYAHKPFAKE
|
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
|
A7NIW0
|
C6DGZ4
|
TRPA_PECCP
|
Tryptophan synthase alpha chain
|
Pectobacterium
|
MERYQQLFNRLSEKKEGAFVPFVTLGDPSPEQSLKIIDTLIAAGADALELGVPFSDPLADGPTIQDANLRAFAAGVTPGQCFEMLATIRQKYPDIPIGLLMYANLVFSNGIDEFYQRCAQVGVDSVLVADVPVAESAPFRTAALRHGIAPIFICPPNADDELLREIASYGRGYTYLVSRAGVTGAEKRAQLPLNHLVAKLNEYHAAPPLQGFGISDPTQVRETLASGAAGAISGSAIVRIIEKNLNQPDVMLSELHTFVSEMKAATRS
|
The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
|
C6DGZ4
|
G5EHQ6
|
HTR2_MAGO7
|
Secreted nuclear effector HTR2
|
Pyricularia
|
MHLKASSILALLVIGANAYPASANSAAALVPEPQQPEAPAVAGSTVGAQVDIHHPRLEARYGRDEPQIMCGYCGKRFWNKPDLEKHIKLKPSKGGHKGQPYKEHSWNRPT
|
Secreted effector that translocates into the nuclei of host cells to reprogram the expression of immunity-associated genes by binding to effector binding elements (EBEs) in rice . Binds the 5'-CCACCTCC-3' EBE of promoters from targeted rice genes and probably recruits a yet to be determined host repressor . Causes ambivalent immunity with increased susceptibility to the hemibiotrophic pathogens Magnaporthe oryzae and Xanthomonas oryzae pv. oryzae, but enhances resistance to Cochliobolus miyabeanus, a necrotrophic pathogen .
|
G5EHQ6
|
P52616
|
FLJB_SALTY
|
Phase 2 flagellin
|
Salmonella
|
MAQVINTNSLSLLTQNNLNKSQSALGTAIERLSSGLRINSAKDDAAGQAIANRFTANIKGLTQASRNANDGISIAQTTEGALNEINNNLQRVRELAVQSANSTNSQSDLDSIQAEITQRLNEIDRVSGQTQFNGVKVLAQDNTLTIQVGANDGETIDIDLKQINSQTLGLDSLNVQKAYDVKDTAVTTKAYANNGTTLDVSGLDDAAIKAATGGTNGTASVTGGAVKFDADNNKYFVTIGGFTGADAAKNGDYEVNVATDGTVTLAAGATKTTMPAGATTKTEVQELKDTPAVVSADAKNALIAGGVDATDANGAELVKMSYTDKNGKTIEGGYALKAGDKYYAADYDEATGAIKAKTTSYTAADGTTKTAANQLGGVDGKTEVVTIDGKTYNASKAAGHDFKAQPELAEAAAKTTENPLQKIDAALAQVDALRSDLGAVQNRFNSAITNLGNTVNNLSEARSRIEDSDYATEVSNMSRAQILQQAGTSVLAQANQVPQNVLSLLR
|
Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella.
|
P52616
|
Q5WZL2
|
RL3_LEGPL
|
50S ribosomal protein L3
|
Legionella
|
MMIGLLGRKIGMTRVFTPEGVSVPVSVVEVHPNRVSQVKTAANDGYSAVQLTGGIKKSSKVSKPVAGHFAKAQIDAGDMQVEFRIDSEDAFTPGQVISVADVFTAGQYVDVSGLTKGKGFAGTVKRHNFRTQDASHGNSRSHRVPGSIGQNQTPGRVFKGKKMAGHMGNARCTIQSLELVKVDSERNLLLIKGAIPGAPGSRVEIKPAVKKQARGE
|
One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.
|
Q5WZL2
|
A0QLS0
|
THIC_MYCA1
|
Thiamine biosynthesis protein ThiC
|
Mycobacterium avium complex (MAC)
|
MTAIVEPSVTTGPIAGSSKVYRELDGVPGARVPFRRVHLSTGDHFDLYDTSGPYTDPDATIDLTAGLPARPGRVRDRGTQLQRARAGEITAEMAFIAAREGMPAELVRDEVARGRAVIPANHNHPEIEPMIIGKAFATKVNANIGNSAVTSSIAEEVDKMVWATRWGADTIMDLSTGKNIHETREWILRNSPVPVGTVPIYQALEKVKGDPTLLTWEIYRDTVIEQCEQGVDYMTVHAGVLLRYVPLTAKRVTGIVSRGGSIMAAWCLAHHRESFLYTNFDELCEIFARYDVTFSLGDGLRPGSIADANDAAQFAELRTLGELTKIAKSHGVQVMIEGPGHVPMHKIVENVRLEEEWCEEAPFYTLGPLATDIAPAYDHITSAIGAAIIAQAGTAMLCYVTPKEHLGLPDRKDVKDGVIAYKIAAHAGDLAKGHPHAQERDNALSQARFEFRWNDQFALSLDPDTAREYHDETLPAEPAKTAHFCSMCGPKFCSMRITQDVRDYAAKHGLDSEEAIEAAMADKSREFAEHGNRVYLPLAQ
|
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.
|
A0QLS0
|
A1WZH3
|
FMT_HALHL
|
Methionyl-tRNA formyltransferase
|
Halorhodospira
|
MAARIVFAGTPDFAVPGLDALVEAGVRPVAVFTQPDRPAGRGRRLTPPPVKRAAERHGLGVHQPERLGAEEAEQIRALAPDLMVVVAYGQILRRNVLDVPRFGCVNVHASLLPRWRGAAPIQRALLAGDEQTGVTLMQMDEGLDTGPMLARKATPISADETAGSLHDRLARIGADLLVAHLPEILAGAITPEPQPDDGVTYAAKLTNDESWLDPTEPAEQLERRVRALAPVPGARLQLGETPVRVLAARACAGRPEDRAGTVAAVGSGGIEVATGEGRLEITRLKPAGGREQTAADYLNGRRLVPGEPVQ
|
Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
|
A1WZH3
|
B0TF89
|
SYDND_HELMI
|
Non-discriminating aspartyl-tRNA synthetase
|
Heliomicrobium
|
MMIDMFTGLKRSHRGGDLRIDHAGQTVTLMGWVQRRRDHGGLIFVDLRDRSGLVQVVFSPEVGKEAFTKAEDVRNEYVLAVTGDVRPRPEGTVNANLPSGQIDVYARQLWVLNSAKTPPFYIEDGVDVDETVRLKYRYLDLRRPEMQRNLIIRHKTAKAMRDFLDRNGFLEIETPMLTKSTPEGAREFMVPSRIHPGEFFVLPQSPQLYKQILMVAGMERYFQIVRCFRDEDLRADRQPEFTQLDIEMSFTQMDDLLTLMEEMVAHIFKEALGKEISTPFRRIPYAEAMGRFGSDKPDLRFGLELIDLTETVKDVEFKVFASVVKGGGEVKAINAKGCAHFSRKEIDDLTKGVAVYGAKGLAYIQMTEEGPKSPIAKFFTDEQLNAVLDRLGAEKGDLLLFVADKPSVVAASLGFLRQELARRLNLIDSEKLEFAWVVDFPLVEYDPEEKRYNAIHHPFTAPKDEDLDLLDKEPGKVRAKAYDLVLNGVELGGGSLRIYRRDIQEKMFAILGLTAEEAYQKFGFLLDAFDYGTPPHGGIAFGLDRMIMLMTGRDTIRDVIAFPKTQSASDMMVDAPSAVTPRQLKELHIKLDLPVKAPKAEPAKK
|
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
|
B0TF89
|
Q20F20
|
PSBH_OLTVI
|
Photosystem II 10 kDa phosphoprotein
|
Oltmannsiellopsis
|
MATEKTAQDTGIETALGTLLRPLNSEYGKVAPGWGTTVLMGTFMALFAVFLVIILEIYNSSVLLEDVPMSWQ
|
One of the components of the core complex of photosystem II (PSII), required for its stability and/or assembly. PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
|
Q20F20
|
P34742
|
E13A_HORVU
|
Beta-1,3-endoglucanase GI
|
Hordeum
|
TIGVCYGVVANNLPPANEVVQLYRSNGLTGMRIYFADAKALSALRGSGIGLILDVGGNDVLASLAANASNAANWVRDNVRPYYPAVNIKYIAAGNEVWGGDTQNIVPAMRNLGAALKAPGLGTIKVSTSIRFDAVTNTFPPSNGVFAQAYMTDVARLLASTGAPLLTNVYPYFAYKDNPRDIQLNYATFRPGTTTVRDPNTGLTSQCLFDAMVDAVVAALERSGAPGVRVVVSESGWPSASGFAATADNARAYNQGLIDHVGGGTPKRPGALETYIFAMFNENFKTGELTEKHFGLFNPDKSPAYPIRFQ
|
May provide a degree of protection against microbial invasion of germinated barley grain through its ability to degrade fungal cell wall polysaccharides. Does not hydrolyze (1,3;1,4)-beta-D-glucans, (1,6)-beta-D-glucan, CM-cellulose, insoluble (1,3)-beta-D-glucans or aryl beta-D-glycosides.
|
P34742
|
A0LRQ7
|
GLMM_ACIC1
|
Phosphoglucosamine mutase
|
Acidothermus
|
MAVSGTAAGTGLASTPRLFGTDGVRGIANRDLTAELALDLAVAAAHVLAQAGAFEGHRPLAVVGRDPRASGEFLEAAVVAGLASAGVDVLRLGVLPTPAVAYLTAALDADLGVVLSASHNPMPDNGIKFLARGGHKLPDDIEDAVAARLGEPWTRPVGRFVGRVRDYPEGLDQYVEHVLATSDQRLDGLRVVVDCAHGAASVVSPAVLRRAGATVVPIGCEPDGYNINDGHGSTNIETLQAAVRREGADAGIAHDGDADRCLAVDAAGDVVDGDQILAILALAWQEAGRLAHDTVVATVMSNLGLKLGLAAHGISVVETAVGDRYVLEAMRAGGYVLGGEQSGHIIMLDYATTGDGVLTGLQLLGRMAATGRPLADLARVVRRLPQVLRNVTGVDKTRVDTDPVINKELAAARGELGDGGRVLLRASGTEPVVRVMVEAETEADAERVAERLARVVRERLG
|
Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate.
|
A0LRQ7
|
B9KNJ3
|
MRAY_CERSK
|
UDP-MurNAc-pentapeptide phosphotransferase
|
Cereibacter
|
MLYLLTAFSDGGDIFNLFRYLTFRAGAAFFTALIFGFLFGRPLIDFLRRKQGKGQPIRDDGPTTHFAKAGTPTMGGLLILSALVVSTLLWARLDNPYVWIVLLVTVAFGLIGFADDYAKVKKQNTKGVPGRVRFLIGLLIAALAAIAAAWSHPPDLTLQLAMPFFKDALINLGWFFVPFAMVVIVGAANAVNLTDGLDGLAIMPVMIAGTTLGVIAYVVGNFNLTDYLGVHFVPGTGELLIFSSALVGGGLGFLWYNAPPAAVFMGDTGSLALSGALGAIAVCTKHEIVLAIVGGLFVTEALSVIIQVLYFKRTGRRVFLMAPIHHHFEKKGWAEPQIVIRFWIISLILALIGLSTLKLR
|
Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
|
B9KNJ3
|
A5U5E1
|
NDK_MYCTA
|
Nucleoside-2-P kinase
|
Mycobacterium tuberculosis complex
|
MTERTLVLIKPDGIERQLIGEIISRIERKGLTIAALQLRTVSAELASQHYAEHEGKPFFGSLLEFITSGPVVAAIVEGTRAIAAVRQLAGGTDPVQAAAPGTIRGDFALETQFNLVHGSDSAESAQREIALWFPGA
|
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
|
A5U5E1
|
B1ING1
|
DNLJ_CLOBK
|
Polydeoxyribonucleotide synthase [NAD(+)]
|
Clostridium
|
MDNKLEKMKELVEELNQYAYEYYVLDNPSISDKEYDLKYDELVILEKKTEVTLPYSPTQRVGDKILGEFSKYTHKGRLWSLDKAQNMEQLIEWHNRNLKVIEQYNSMSEDKLPELRYIVTKKFDGLTVNCTYDENGILIKSATRGTGIIGEDITAQIKTIKTVPLKIKNSHVIEVHGEAIMTKTAFEEYNKAAQVPLKNLRNGAAGALRNLDIKETARRNLSAFFYDVGYNEGPEFKSYREMMNFIKNMGLPQDKYIKECTNMEEVEKEIEYIESIRGELDYDIDGAVIVVDDIKTREILGYTIKFPKWAIAYKFEAKEITTKLLDVEWNVGRSGRVTPTALLEPVELGGVTVKRATLNNMDDIKRKNVKLGAKVLVRRSNDVIPEIMGVVEESLEESEEIQAPDRCPYCNSHLVQNGVHYYCENTLSCKPQMVKSIVHFASREAMNIAGFSEKTAEQLFEKLDIKSIADLYKIKKEELLTLEKFKDKKSQNLIDAIQNSKNCDLASFIYALGIPNVGKKTANDLVMKFKTLESIKNTTIEQLVEVPDVGEIVAKSIYDFFEDEKIISNIEELLNLGVKPYYEEERIDENPFMDKTIVVTGSLNNYSRGEIKDKLQSLGAKVSSSVSKNTDYVLVGEKPGSKYEKAIELGVKVINEEEFSNKIK
|
DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
|
B1ING1
|
Q10254
|
ALG10_SCHPO
|
Dolichyl-phosphoglucose-dependent glucosyltransferase alg10
|
Schizosaccharomyces
|
MFLGKAIILILWIFLAFTGLLAIQYYVPNPYLDEIFHIAQAQRFCRKDWDWDPAITTPPGLYLVSVALSPFIGCSNVSLRLINWLVGVIGLPWLINDIVSLLNNRKGDVVTYFAYTLSSLPPLWFFSFLYYTDIGSTFFVLLAYDFALRKSAFSSSVSCFFSLWFRQTNIVWMVFIAVTYFASNMSFFNPHLAEATFADVLLTIISFLGVFLKNLRRFSCPILSYGAVFCSFLAFLLWNGSIVLGDKSHHQASIHLSQINYFLWFFFFFSFPSYIIKYLMSHSRRSKLLSAVFSKKSFLIVSVLLLIAHFNTIFHPFILADNRHYLFYVFNRLFRIWWLKYLGPFSYLILYYFFLDISKLQMTSLTFFLLISTTILTLVPAPLVEFRYFLLPFLFWRFHLPLPSGRECLMEYALHMVINSVTLYIFLFRTFIWPSEPNALQRFMW
|
Adds the third glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Glc(2)Man(9)GlcNAc(2)-PP-Dol.
|
Q10254
|
B1VP90
|
KPTA_STRGG
|
Probable RNA 2'-phosphotransferase
|
Streptomyces
|
MDERRTVKVSKYLSKHLRHQPERIGLTLDENGWVAVEELLRAAARHGFAFSRAELDHVVAANDKRRFTVENGCAADGVHGDRIRANQGHTVAVDLDLPPAEPPAHLYHGTVARVMDAIRTEGLRPMARHHVHLSPDRETATRVGARRGRPLVLTVDAGAMHRAGHVFRVSANGVWLADAVPPRFLLLRG
|
Removes the 2'-phosphate from RNA via an intermediate in which the phosphate is ADP-ribosylated by NAD followed by a presumed transesterification to release the RNA and generate ADP-ribose 1''-2''-cyclic phosphate (APPR>P). May function as an ADP-ribosylase.
|
B1VP90
|
A1BJH0
|
CRCB_CHLPD
|
Putative fluoride ion transporter CrcB
|
Chlorobium
|
MLMKQVSAFLLVGIGGFLGSAARYGASLLLSPVAGGLPLATFSVNIIGCFFIGFISELALSTTLVSPESRLFLVTGFCGGFTTFSSYIFENASLLKDGQMLYTSAYLAGSVIGGFVALYSGTFFAKIWT
|
Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
|
A1BJH0
|
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