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
|
|---|---|---|---|---|---|---|
A6TGQ0
|
THIE_KLEP7
|
Thiamine-phosphate pyrophosphorylase
|
Klebsiella
|
MYQPDFPPVPFRLGLYPVVDSVAWIERLLEAGVRTLQLRIKDRRDSEVEDDVIAAIALGRRYHARLFINDYWQLAIKHQAYGVHLGQEDLETTDLSAIRQAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSAPQGLEQLARHIQRLADYPTVAIGGISLEKAPGVLATGVGSIAVVSAITQAADWRAATDQLLALAGAGDE
|
Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
|
A6TGQ0
|
Q5E8M1
|
FPG_ALIF1
|
DNA-(apurinic or apyrimidinic site) lyase MutM
|
Aliivibrio
|
MPELPEVETSRLGITPHLQGQTIKAIVVRTDKLRWPIPQELQKLVGQRVQSIRRRAKYLMIDTPKGSAIIHLGMSGSLRVLDEEVPSAKHDHVDLVLENGKVLRYNDPRKFGAWLYSEVGVAHQVLSKLGPEPLTNEFNSEYFAEKAKNKKTVVKQFIMNNAVVVGVGNIYASESLFMAQIHPKTSVGSLKASQITLLVAEIKKVLETAIKQGGTTLKDFNQVDGKPGYFAQELHVYGRAKKKCLLCSSIIQEEKIGQRNTFWCGHCQPFNK
|
Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.
|
Q5E8M1
|
A3DJ13
|
TSAD_ACET2
|
tRNA threonylcarbamoyladenosine biosynthesis protein TsaD
|
Acetivibrio
|
MKDILILGIETSCDETSASVVKNGRQVLSNVISSQVALHQKYGGVVPEIASRKHVELIMPVIHQSLEEAGIKIEQVDAIGVTYGPGLVGALLVGLSAAKALAFALDKPLIGVHHIEGHIAANYIEHSLLEPPFVCLVASGGHSHIVYVQDYDKFEIMGKTRDDAAGEAFDKVARAVGLGYPGGPIIDKTAKLGNSKAIDFPRVHFGDQSLDFSFSGLKTAVLNYINSMEQKGEKYSVEDVCASFQAAVVDVLTDNLISAARIKGVKKVALAGGVAANSLLRSELVEKAKGLGLEVFYPKPVLCTDNAAMIACAAYYEFLRGHTSDVYLNAIPGLKLGER
|
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.
|
A3DJ13
|
P23594
|
PP2A1_YEAST
|
Serine/threonine-protein phosphatase PP2A-1 catalytic subunit
|
Saccharomyces
|
MDTDLDVPMQDAVTEQLTPTVSEDMDLNNNSSDNNAEEFSVDDLKPGSSGIADHKSSKPLELNNTNINQLDQWIEHLSKCEPLSEDDVARLCKMAVDVLQFEENVKPINVPVTICGDVHGQFHDLLELFKIGGPCPDTNYLFMGDYVDRGYYSVETVSYLVAMKVRYPHRITILRGNHESRQITQVYGFYDECLRKYGSANVWKMFTDLFDYFPITALVDNKIFCLHGGLSPMIETIDQVRELNRIQEVPHEGPMCDLLWSDPDDRGGWGISPRGAGFTFGQDVSEQFNHTNDLSLIARAHQLVMEGYAWSHQQNVVTIFSAPNYCYRCGNQAAIMEVDENHNRQFLQYDPSVRPGEPSVSRKTPDYFL
|
Exact function not known, phosphatase 2A performs an essential cellular function.
|
P23594
|
A0A0B4J240
|
TVA10_HUMAN
|
T cell receptor alpha variable 10
|
Homo
|
MKKHLTTFLVILWLYFYRGNGKNQVEQSPQSLIILEGKNCTLQCNYTVSPFSNLRWYKQDTGRGPVSLTIMTFSENTKSNGRYTATLDADTKQSSLHITASQLSDSASYICVVS
|
V region of the variable domain of T cell receptor (TR) alpha chain that participates in the antigen recognition . Alpha-beta T cell receptors are antigen specific receptors which are essential to the immune response and are present on the cell surface of T lymphocytes. Recognize peptide-major histocompatibility (MH) (pMH) complexes that are displayed by antigen presenting cells (APC), a prerequisite for efficient T cell adaptive immunity against pathogens . Binding of alpha-beta TR to pMH complex initiates TR-CD3 clustering on the cell surface and intracellular activation of LCK that phosphorylates the ITAM motifs of CD3G, CD3D, CD3E and CD247 enabling the recruitment of ZAP70. In turn ZAP70 phosphorylates LAT, which recruits numerous signaling molecules to form the LAT signalosome. The LAT signalosome propagates signal branching to three major signaling pathways, the calcium, the mitogen-activated protein kinase (MAPK) kinase and the nuclear factor NF-kappa-B (NF-kB) pathways, leading to the mobilization of transcription factors that are critical for gene expression and essential for T cell growth and differentiation . The T cell repertoire is generated in the thymus, by V-(D)-J rearrangement. This repertoire is then shaped by intrathymic selection events to generate a peripheral T cell pool of self-MH restricted, non-autoaggressive T cells. Post-thymic interaction of alpha-beta TR with the pMH complexes shapes TR structural and functional avidity .
|
A0A0B4J240
|
Q7SDH9
|
PSF1_NEUCR
|
DNA replication complex protein 1
|
Neurospora
|
MPMYGDLGNKLVQHAKRTQNLSHLPPYQTELVRAVAREIRDLDKDVASLLEPFQGSFDPSAEQATACTLLVNHLSMRRNKRCLLAYHRIRTDKLEELVWNGADILDLAGQTTGGPKGVTEGNEGGGTTSSLSPQEEDYFRQFGDLLALYKGQWTDIDLTGSLEPPRDLFIDVRVLKDAGEIQTEYGAINLTKNSQFYVRQGDVERLIVQGYLQKLG
|
The GINS complex plays an essential role in the initiation of DNA replication.
|
Q7SDH9
|
Q8PXV2
|
MFNB_METMA
|
4-(hydroxymethyl)-2-furancarboxaldehyde-phosphate synthase
|
Methanosarcina
|
MKLLVSPINSEEAIIASIGGADIVDVKNPKEGSLGANFPWVIREVKAVVNGRQPISATIGDFNYKPGTAALAALGAAVAGADYIKVGLYDIQTESQALELLTKITRAVKDYNPLKKVVASGYSDYKRINSISPLLLPAVAAEAGVDVVMVDTGVKDGKSTFEFMDEKELKEFTDLAHSYGLENAIAGSLKFEDIPLLERIGPDIIGVRGMVCGGDRSTSIRQELVEKLVAECQA
|
Catalyzes the formation of 4-(hydroxymethyl)-2-furancarboxaldehyde phosphate (4-HFC-P) from two molecules of glyceraldehyde-3-P (GA-3-P).
|
Q8PXV2
|
P0DMM0
|
APOE_PHYMC
|
Apolipoprotein E
|
Physeter
|
MKVLWVALVITLLAGCQAEEVKPAPEPEVQLGQEWPGWQGSQPWEQALGRFWDYLRWVQTLSDQVQEELLSTQVIQELTVLMDETMKEVKAYREELEEQLGPVAQETQARVSKELQAAQARLASDMQDVRGRLAQYRSEVQAMMGHTTDELRDRLASHLRKLRKRLLRDAEDLQKRLAVYRAGALEGSERSVSAIRERLGPLVEQGRARAATVGTLASQTLRERAEAWHQKLRGRVEEMGTQARDHLEEMREQLDEVRAKVEEQGTQMRLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQLAMATSSTSAPSENH
|
APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apoliproteins are amphipathic molecules that interact both with lipids of the lipoprotein particle core and the aqueous environment of the plasma. As such, APOE associates with chylomicrons, chylomicron remnants, very low density lipoproteins (VLDL) and intermediate density lipoproteins (IDL) but shows a preferential binding to high-density lipoproteins (HDL). It also binds a wide range of cellular receptors including the LDL receptor/LDLR and the very low-density lipoprotein receptor/VLDLR that mediate the cellular uptake of the APOE-containing lipoprotein particles. Finally, APOE has also a heparin-binding activity and binds heparan-sulfate proteoglycans on the surface of cells, a property that supports the capture and the receptor-mediated uptake of APOE-containing lipoproteins by cells.
|
P0DMM0
|
Q2W2L3
|
RPOA_MAGSA
|
Transcriptase subunit alpha
|
Magnetospirillum
|
MIQKNWQELIKPNKLHVEPGADPQRTAIVVAEPLERGFGMTLGNSLRRVLLSSLQGAAVTAIQIDGVLHEFSSIPGVREDVTDIILNIKTLGLRMHGEGPKRMHLRAVGPGEVTAGLIEVGHDIEIMDPELVLCTLDEGAKLNIEFTVETGKGYVPASQNRPEDSPIGLIPIDAIFSPVRKVAYKVENTRVGQVTDYDKLSMTVETNGAVTPDDAVALAARILQDQLQLFINFEEPTAVVEEEKKDELPFNKNLLRKVDELELSVRSANCLKNDNIIYIGDLVQKTEAEMLRTPNFGRKSLNEIKEVLAQMGLHLGMEIANWPPENIEELAKKLEEPY
|
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
|
Q2W2L3
|
Q128P8
|
PNCB_POLSJ
|
Nicotinate phosphoribosyltransferase
|
unclassified Polaromonas
|
MIITSLLDTDLYKFTMMQVVLHQFPGAEVEYRFKCRNAGAPGIGKLAPYVNEIREEIRGLCNLRFQDAELAYLKAMRFIKSDFVDFLGIFKLNEKYVSVTALPSGEIEVSIKGPWLHTILFEIPVLAIINEVYFRNTQKQPDLTEGRKRLDTKILELQADGLRELKIADYGTRRRFGKVWHEEVLRTLVTRLGTGMSGQLAGTSNVLFAMKLGLTPLGTMAHEYLQACQALGPRLRDSQVFGFESWAREYRGDLGIALSDVYGMSAFLRDFDMYFCKLFDGARHDSGDPFEWGERMLAHYVKNRVDPRTKTLIFSDALTVPRTIELYQQFRGRCQLAFGIGTNLTNDLGYEPLQIVIKMIRCNGQPVAKLSDTPSKNMCEDEKYLAYLRQVFEIG
|
Catalyzes the synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate at the expense of ATP.
|
Q128P8
|
B2IYE4
|
AROA_NOSP7
|
5-enolpyruvylshikimate-3-phosphate synthase
|
Nostoc
|
MDTIEIPALNRPVDATVEIPGSKSLTNRALLVAALAQGDSILENALFSEDSEYFAKCLEQLGIPITLNPHLAQIQLAGRGGEIPAKQADLFVGLSGTTARFISALVALGNGEYRLDGVPRMRERPMGDMLTVLETGGATVNFEGNSGFMPYTVYSQGFAGGNFCLKANQTSQQLSALLMIAPYAQQDTIFEVEGTLVSLSYIKMTCRLMADFGVEVIQIGDNQFQIKAGQRYQAQHYTVEPDASNASYFFAAAAVTGGRVRVKHLTKQSCQGDILWLNVLEQMGCQIKDSDDYTEVTGPKQLQGIDIDMNDISDLVQTLAAIAPFASSPITIRNVEHIRYKETDRIKAVVTELRRLGVQVEEFPDRLKIEPGPITPAEIETYHDHRMAMAFAVTGLKVPGIVIKDPGCTAKTFPDYFTRFFQMLEQ
|
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.
|
B2IYE4
|
J9VND4
|
PBP1_CRYNH
|
Poly(A)-binding protein-binding protein
|
Cryptococcus neoformans species complex
|
MSNERGRGRGGNRGGRGGMEGGSARRGAWRNGPPPAGSFPHSRGGSPALGQSPTPRMSINDHMHDLKIVQGERKGFQTDTDISRAAGPVERELQPWVPDGPSPPPQSNGGSGNADFETFGTTNNITWDQFETNERLFGAKTDFKEELYTTKLNKSGPDFHKREKEAERLAKQIMGQTSKNAHIAEERGQATDIRDEEEKYSGVSRAPNAYVPPSARRAMGQSSAALRPNPTFESNTNGSTPIPAKPASPAAHETAPPAPERRISDDPVGSKPEAPAMKVTGTTIRPITENAEVTVNGTNVTAETKPELSGVVNEWRQFVGTEREKVEAKKQSVLKSEKEKQLADFKKFQANFKVPLPLPKDILPILSKDEAKQKDIEAKATNALQAAKERKLSIAKDSPAKSPVILNSVKSDAPKPAPPKKIVMKIPEIPPFNPAKRKAPAVPVPESATQDIKLITSPAPSNGSLASQATKLNPTASTFVFKPRADAAPFKPGQPSVSPSIAPHQPSAGPSNTSASTAVPKGNAFFRDKLPEKTHINAREDFNPWKHGPVPRPNTVGTGWPYPGRKVGVPPPFMSPAAPPQMQMQFEDDPTSPSPHPAQPAMMPGMPPNYPPYGRFQPGMPPPYGVPGGMQNPMFSPGPHFSPHPGQPMGQPQHMMPGGPQPNMPMYFQNGMPQNPAFLPPQMQQFPHNPQRPGPGPGPGGPQMFYPNQMPPMPHQTPLQQHPVPFSGPSPAQPQFQHQHQHQHQHPHQQAPPPPPVQMSPAHSTPSGPGGVVQGGPQQNGQTQG
|
Involved in post-transcriptional regulation of gene expression by interactions with poly(A)-binding protein.
|
J9VND4
|
Q04J43
|
STKP_STRP2
|
Eukaryotic-type Ser/Thr protein kinase
|
Streptococcus
|
MIQIGKIFAGRYRIVKQIGRGGMADVYLAKDLILDGEEVAVKVLRTNYQTDPIAVARFQREARAMADLDHPHIVRITDIGEEDGQQYLAMEYVAGLDLKRYIKEHYPLSNEEAVRIMGQILLAMRLAHTRGIVHRDLKPQNILLTPDGTAKVTDFGIAVAFAETSLTQTNSMLGSVHYLSPEQARGSKATVQSDIYAMGIIFYEMLTGHIPYDGDSAVTIALQHFQNPLPSVIAENSSVPQALENVIIKATAKKLTNRYRSVSEMYVDLSSSLSYNRRNESKLIFDETSKADTKTLPKVSQSTLTSIPKVQAQTEHKSIKNPSQAVTEETYQPQAPKKHRFKMRYLILLASLVLVAASLIWILSRTPATIAIPDVAGQTVAEAKATLKKANFEIGEEKTEASEKVEEGRIIRTDPGAGTGRKEGTKINLVVSSGKQSFQISNYVGRKSSDVIAELKEKKVPDNLIKIEEEESNESEAGTVLKQSLPEGTTYDLSKATQIVLTVAKKATTIQLGNYIGRNSTEVISELKQKKVPENLIKIEEEESSESEPGTIMKQSPGAGTTYDVSKPTQIVLTVAKKVTSVAMPSYIGSSLEFTKNNLIQIVGIKEANIEVVEVTTAPAGSVEGMVVEQSPRAGEKVDLNKTRVKISIYKPKTTSATP
|
Protein kinase involved in signal transduction pathways that regulate various cellular processes. Likely senses intracellular peptidoglycan subunits present in the cell division septa of actively growing cells; thus, intracellular unlinked peptidoglycan may serve as the signal molecules that trigger StkP phosphorylation activity on a set of substrates. Plays a crucial role in the regulation of cell shape and cell division of S.pneumoniae through control of at least DivIVA activity. Is involved in competence triggering, and is required for the expression of the central competence operon comCDE. StkP also plays an important role for bacterial survival in vivo. Identified target substrates that are specifically phosphorylated by StkP in vivo, mainly on threonine residues, are DivIVA, GlmM, PpaC, MapZ, KhpB (also called EloR/Jag, shown in strains R6 and Rx1) and StkP itself. Autophosphorylated StkP is a substrate for the cotranscribed protein phosphatase PhpP (shown in the avirulent strain Rx / Cp1015); PhpP and StkP appear to constitute a functional signaling couple in vivo.
|
Q04J43
|
B5ZXG4
|
DCTA_RHILW
|
C4-dicarboxylate transport protein
|
Rhizobium
|
MIAAPFDAVADSTGKKPFYSHLYVQVLAAIAAGILLGHFYPELGAQLKPLGDAFIKLVKMIIAPVIFLTVATGIAGMSDLKKVGRVAGKAMLYFLTFSTLALVIGMVVANVVQPGAGMNIDPASLDPTAVATYASKAHEQSIVGFLTNIIPTTIVGAFADGDILQVLFFSVLFGIALAMVGEKGEQVVNFLNALTAPVFKLVAILMKAAPIGAFGAMAFTIGKYGIGSIANLAMLIGTFYLTSLLFVLVVLGAVARYNGFSILALLRYIKEELLLVLGTSSSEAALPGLMNKMEKAGCKRSVVGLVIPTGYSFNLDGTNIYMTLAALFIAQATGINLSWGDQILLLLVAMLSSKGAAGITGAGFITLAATLSVVPSVPVAGMALILGIDRFMSECRALTNLVGNAVATIVVARWENELDTAQLARALGGQAEESAPAGLQPAE
|
Responsible for the transport of dicarboxylates such as succinate, fumarate, and malate from the periplasm across the membrane.
|
B5ZXG4
|
Q03125
|
NRG1_YEAST
|
Zinc finger protein MSS1
|
Saccharomyces
|
MFYPYNYSNLNVSTMPALPGISAFDGMQDEENVEISPERKYQTLLPVLTNSHVVENELKHKLNKTAFDFRYQTKSENGSEKWEPKYLITPNLQTRSVSFDNSSVQYNSDSSEKSSLSQLTCNSSIIQQPENGIVSNDAYNKMANSRYSLKTRKQRTDPRNTLSDEEDLEQRRKYICKICARGFTTSGHLARHNRIHTGEKNHCCPYKGCTQRFSRHDNCLQHYRTHLKKGQ
|
Transcriptional repressor involved in regulation of glucose repression. Binds to UAS-1 in the STA1 promoter.
|
Q03125
|
Q9PE40
|
CLPX_XYLFA
|
ATP-dependent Clp protease ATP-binding subunit ClpX
|
Xylella
|
MSEDRPSRSGDGNKILYCSFCGKSQREVRKLIAGPSVFICDECVELCNDIIREELEEKSQSARSSLPKPKEILEVLDQYVIGQQRAKRTLAVAVYNHYKRIESRHKNDDIELAKSNILLVGPTGSGKTLLAETLARLLNVPFTIADATTLTEAGYVGEDVENIIQKLLQKCDYDVERAQHGIVYIDEIDKISRKSENPSITRDVSGEGVQQALLKLIEGTVASVPPQGGRKHPQQEFLQVDTKNILFICGGAFAGLDKVIQQRCTEAGGIGFGVKVKSSESKRDVGKVLAGVEPEDLIKFGLIPEFVGRLPVVATLDELDESALVKILTEPKNAITKQFKKLFEMENVELEFRQDALSAVARKALKRKTGARGLRTIVELVLLDTMYELPSQEGISKVVVDESVIENKSEPYLIYQTMPAKVASGE
|
ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.
|
Q9PE40
|
Q0G9I9
|
CYB6_LIRTU
|
Cytochrome b6
|
Liriodendron
|
MSKVYDWFEERLEIQAIADDITSKYVPPHVNIFYCLGGITLTCFLVQVATGFAMTFYYRPTVTEAFASVQYIMTEANFGWLIRSVHRWSASMMVLMMILHVFRVYLTGGFKKPRELTWVTGVILAVLTASFGVTGYSLPRDQIGYWAVKIVTGVPEAIPVIGSPLVELLRGSASVGQSTLTRFYSLHTFVLPLLTAVFMLMHFPMIRKQGISGPL
|
Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
|
Q0G9I9
|
B4EC68
|
GUAA_BURCJ
|
Glutamine amidotransferase
|
Burkholderia cepacia complex
|
MHDKILILDFGSQVTQLIARRVREAHVYCEIHPNDVSDDFVREFAPKAVILSGSHASTYEDHQLRAPQAVWDLGVPVLGICYGMQTMAVQLGGKVEWSDHREFGYAEMRAHGHTRLLDDIEDFTTAEGHGMLKVWMSHGDKVAELPPGFALMASTPSCPIAGMADEARGYYAVQFHPEVTHTVKGRQIIERFVLQIAGAKPDWIMKNHIEEAVAKIREQVGDEEVILGLSGGVDSSVAAALIHRAIGDQLTCVFVDHGLLRLNEGKMVLDMFEGRLHAKVVHVDASDQFLGHLAGVTDPEAKRKIIGREFVEVFQAEAKKLSKAKWLAQGTIYPDVVESGGTKTKKATTIKSHHNVGGLPETLGLKLLEPLRDLFKDEVRELGVALGLPPEMVYRHPFPGPGLGVRILGEVKREYADLLRRADAIFIEELRGTTATAQDAAAGLCGEADVGKSWYDLTSQAFAVFLPVKSVGVMGDGRTYDYVTSLRAVQTTDFMTAHWAHLPYALLGRASNRIINEVRGINRVVYDISGKPPATIEWE
|
Catalyzes the synthesis of GMP from XMP.
|
B4EC68
|
Q7V8D2
|
SYT_PROMM
|
Threonyl-tRNA synthetase
|
Prochlorococcus
|
MPIIALPDGNKKKFDQPVTIMEVAESLGPGLAKAAIAGRVNGVLLDTCIPIEKDSEVNIITAKDQDGIETIRHSFAHLIGHAVKQLYPEAKMAIGPVIEDGFYYDIAYDHPFTPKDLEAIEARMKELVKLDYDVNVEIVSKEEARKEFEKRCEPYKIEIVDEIPENEIIKLYRHQEYTDMCRGPHVPNTRHLRTFKLMKVSGAYWRGDSNKTMLQRIYGTAWGSSKELKAYLKRLEEAEKRDHRRIAKQMSLFHTQEEAPGMIFWHAKGWAIYQVLEQYIRETLSLHDYQEIRTPQVVDRSLWEKSGHWEKFKDDMFTTTSENREYAIKPMNCPCHVQIFNQGLKSYRDLPIRLAEFGSCLRNEPSGSLHGLMRVRNFVQDDAHIFCTELQVQEEVSKFIDLVFEVYRSFGFDSVLIKLSTRPEKRVGSDEIWDKSEKALSDALDAKGLAWDLLPGEGAFYGPKIEFSLKDCLGRVWQCGTIQVDFSMPERLGASYVAEDSQRRTPVMLHRAILGSFERFIGILIEHYAGRLPIWLAPVQVVVMGITDRNAQACQDICKKLSALEYRTEVDLRNEKIGFKVREHTLQRVPFLIIIGDKEQQSGEVAVRTREGKDFGSMPLKGFTSLLDEAIALKGRSGVS
|
Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr).
|
Q7V8D2
|
Q65LS8
|
HPR_BACLD
|
Protease production regulatory protein Hpr
|
Bacillus
|
MNRAEEPYTVKEALLFSQRMAQLSKALWKSIEKDWQQWIKPYDLNINEHHILWIAYQLNGASISEIAKFGVMHVSTAFNFSKKLEERGYLEFSKKLNDKRNTYIQLTPKGEEVFLKILESYDPTRNAVLKGAQPLHQLYGKFPEIVEMMSIIRHIYGDDFMEIFEKSFSNIENEFTSEEGKMKKKQEAKEAGESIEVDKPLEPLKN
|
Negative regulator of protease production and sporulation.
|
Q65LS8
|
Q7U5C2
|
HEM3_PARMW
|
Pre-uroporphyrinogen synthase
|
Parasynechococcus marenigrum
|
MALTELRIASRRSQLAMVQTNWVKAELEKAHPGLTITVEAMATQGDKILDVALAKIGDKGLFTKELEAQMLVGRAEIAVHSLKDLPTNLPEGLMLGCITEREDPADALVVNAKNANHKLDTLPEGAVVGTSSLRRLAQLRHHYPHLSFKDVRGNVITRLEKLDSGDYDCLILAAAGLERLGFGNRIHQIIPGDISLHAVGQGALGIECVEDKPEVLEIIKVLEHTTTSRRCLAERAFLRELEGGCQVPIGVNSQINNEELTLTGMVASLDGKRLIRDEASGSAADPESIGIELAGKLKHQGAGAILKEIFDEVRPEA
|
Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
|
Q7U5C2
|
Q8RX56
|
UNC13_ARATH
|
Protein PROTON ATPASE TRANSLOCATION CONTROL 1
|
Arabidopsis
|
MEEENAVEILQRYRRDRRKLLDFMLAGSLIKKVIMPPGAVTLDDVDLDQVSVDYVINCAKKGGMLELAEAIRDYHDHIGLPYMNSVGTADEFFLATIPESSGSPPKRAPPPIPVLISSSSPMVTNPEWCESPSAPPLMRSESFDSPKAQELTVDDIDDFEDDDDLDEVGNFRISRRTANDAADLVPRLPSFATGITDDDLRETAFEILLACAGASGGLIVPSKEKKKEKSRSRLIKKLGRKSESVSQSQSSSGLVSLLEMMRGQMEISEAMDIRTRQGLLNALAGKVGKRMDSLLVPLELLCCVSRTEFSDKKAYLRWQKRQLNMLAEGLINNPVVGFGESGRKATDLKSLLLRIEESESLPSSAGEVQRAECLKSLREVAISLAERPARGDLTGEVCHWADGYHLNVRLYEKLLLCVFDILNDGKLTEEVEEILELLKSTWRVLGITETIHYTCYAWVLFRQYVITSERGLLRHAIQQLKKIPLKEQRGPQERLHLKTLKCRVDNEEISFLESFLSPIRSWADKQLGDYHLHFAEGSLVMEDTVTVAMITWRLLLEESDRAMHSNSSDREQIESYVLSSIKNTFTRMSLAIDRSDRNNEHHLALLAEETKKLMKKDSTIFMPILSQRHPQAIAFSASLIHKLYGNKLKPFLDGAEHLTEDAVSVFPAADSLEQYLLELMTSVCGEDTSGPYFKKLIPYEVESLSGTLVLRWINSQLGRILSWVERAYKQEHWDPISPQQRYGSSIVEVFRIVEETVDQFFALKVPMRSIELSALFRGIDNAFQVYTNHVMEKLASKDDLVPPVPVLTRYKKETAIKVFVKKELFDSKHLDERRSINIDVPATAMLCVQLNTLHYAVSQLSKLEDSMWLRWIAKKPREKIVIRKSMVEKSKSFNQKESFEGSRKDINAALDRICEFTGTKIIFCDLREPFIENLYKPNVSQSRLEGLIEALDTELGQLCSVIMEPLRDRIVTSLLQASLDGLLRVLLDGGASRVFHPSESKLLEEDVEVLKEFFISGGDGLPRGVVENQVARVRLVVKLHGYETRELIDDLRSRSSLEMQQGGKGKLGADTQTLVRVLCHRNDSEASQFLKKQYKIPRSHG
|
Controls the tethering of the proton ATPase AHA1 to the plasma membrane. Is essential for stomatal opening in response to low concentration of carbon dioxide and light.
|
Q8RX56
|
A3MYU1
|
SYT_ACTP2
|
Threonyl-tRNA synthetase
|
Actinobacillus
|
MPIITLPDGSQRQFDNPVSVMEVAQSIGAGLAKATIAGRVNGERRDACDIISEDSSLEIITAKDEDGLEIIRHSCAHLLGHAIKQLFPNVKMAIGPTIDNGFYYDVDLDRSLTQEDLDAIEKRMLELAKTNYDVVKKRVSWQEARDTFEKRGEPYKMAILDENIERTATPALYHHEEYIDMCRGPHVPNMRFCHHFKLQKVAGAYWRGDSKNKMLQRIYGTAWADKKQLAEYLTRLEEAAKRDHRRIGKALDLYHMQEEAPGLVFWHNDGWTIFRELETFVRTKLKEYDYQEVKGPFMMDRVLWERTGHWQNYADLMFTTQSENREYAIKPMNCPGHVQIFNQGLKSYRDLPIRMAEFGSCHRNEPSGSLHGLMRVRGFTQDDAHIFCTEDQIESEVTSCIRMVYDIYSTFGFSNIQVKLSTRPENRIGDDAMWDRAEDGLAKALTANGLSYEIQEGEGAFYGPKIEFALRDCLDREWQCGTIQLDFALPGRLDASYVAEDNGRRTPVMIHRAILGSIERFIGIITEEYAGFFPTWLAPTQAVVMNITDSQADYVQKVTKALSDAGIRVKSDLRNEKVGFKVREHTLRRVPYMLVCGDKEIEAGKVSVRTRKGADLGTFTIDEFVEILKNQVKARGLKLLGEE
|
Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr).
|
A3MYU1
|
A7GZK0
|
RL7_CAMC5
|
50S ribosomal protein L7/L12
|
Campylobacter
|
MAITKEDVLEFISNLSVLELSELVKEFEEKFGVSAAPVMVAGGAVAGGAAEAAEEKTEFNLVLVDSGDKKINVIKVVRALTGLGLKEAKDAVEGTPSVLKEGISKDEAEAAKKELEEAGAKVELK
|
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation.
|
A7GZK0
|
A1VYJ5
|
RPOC_CAMJJ
|
Transcriptase subunit beta'
|
Campylobacter
|
MSKFKVIEIKEDARPRDFEAFQLRLASPEKIKSWSYGEVKKPETINYRTLKPERDGLFCAKIFGPIRDYECLCGKYKKMRFKGVKCEKCGVEVANSKVRRSRMGHIELVTPVAHIWYVNSLPSRIGTLLGVKMKDLERVLYYEAYIVENPGDAFYDNESTKKVEYCDVLNEEQYQNLMQRYENSGFKARMGGEVVRDLLANLDLVALLNQLKEEMAATNSEAKKKTIIKRLKVVENFLNSNLNANTDSDEAVPNRPEWMMITNLPVLPPDLRPLVALDGGKFAVSDVNDLYRRVINRNTRLKKLMELDAPEIIIRNEKRMLQEAVDALFDNGRRANAVKGANKRPLKSLSEIIKGKQGRFRQNLLGKRVDFSGRSVIVVGPKLRMDQCGLPKKMALELFKPHLLAKLEEKGYATTVKQAKKMIENKTNEVWECLEEVVKGHPVMLNRAPTLHKLSIQAFHPVLVEGKAIQLHPLVCAAFNADFDGDQMAVHVPLSQEAIAECKVLMLSSMNILLPASGKSVTVPSQDMVLGIYYLSLEKAGAKGSHKICTGIDEVMMALESKCLDIHASIQTMVDGRKITTTAGRLIIKSILPDFVPENSWNKVLKKKDIAALVDYVYKQGGLEITASFLDRLKNLGFEYATKAGISISIADIIVPNDKQKAIDEAKKQVREIQNSYNLGLITSGERYNKIIDIWKSTNNVLSKEMMKLVEKDKEGFNSIYMMADSGARGSAAQISQLAAMRGLMTKPDGSIIETPIISNFREGLNVLEYFISTHGARKGLADTALKTANAGYLTRKLIDVAQNVKITIEDCGTHEGVEINEITADSSIIETLEERILGRVLAEDVIDPITNSVLFAEGTLMDEEKAKILGESGIKSVNIRTPITCKAKKGICAKCYGINLGEGKLVKPGEAVGIVSAQSIGEPGTQLTLRTFHSGGTASTDLQDRQVSAQKEGFIRFYNLKTYKNKEGKNIVANRRNAAILLVEPKIKTPFKGVINIENIHEDVIVSIKDKKQEVKYILRKYDLAKPNELAGVSGSIDGKLYLPYQSGMQVEENESIVEVIKEGWNVLNRIPFASEILVEDGEPVVQNIKAGEKGTLKFYILKGDGLDRVKNVKKGDIVKEKGFFVVIADENDREAKRHYIPRESKIEFNDSEKIDDANTIIASAPKKERKVIAEWDAYNNTIIAEIDGVVSFEDIEAGYSADEQIDEATGKRSLVINEYLPSGVRPTLVIAGKGDKAVRYQLEPKTVIFVHDGDKIAQADILAKTPKAAAKSKDITGGLPRVSELFEARKPKNAAVIAEIDGVVRFDKPLRSKERIIIQAEDGTSAEYLIDKSKHIQVRDGEFIHAGEKLTDGVVSSHDVLKILGEKALHYYLISEIQQVYRGQGVVISDKHIEVIVSQMLRQVKVVDSGHTKFIEGDLVSRRKFREENERIIRMGGEPAIAEPVLLGVTRAAIGSDSVISAASFQETTKVLTEASIAGKFDYLEDLKENVILGRMIPVGTGLYGEQNLKLKEQE
|
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
|
A1VYJ5
|
Q4ZLU8
|
RPIA_PSEU2
|
Phosphoriboisomerase A
|
Pseudomonas syringae
|
MTQDQLKQAVAQAAVDFILPKLDDKSIVGVGTGSTANCFIDALAKHKAAFDGAVASSQATAARLKAHGIPVYELNTVSDLEFYVDGADESDEHLNLIKGGGAALTREKIVAAVANTFICIADGSKLVPVLGAFPLPVEVIPMARSHVARQLVKLGGDPVYREGVLTDNGNIIIDVHNMSITNPVELEAQINAIVGVVTNGLFAARPADLLLLGTAEGVKTLTR
|
Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
|
Q4ZLU8
|
Q08920
|
NCBP2_YEAST
|
NCBP 20 kDa subunit
|
Saccharomyces
|
MSLEEFDEVKYDHSTKRLDTPSRYLLRKARRNPNGLQELRESMKSSTIYVGNLSFYTSEEQIYELFSKCGTIKRIIMGLDRFKFTPCGFCFIIYSCPDEALNALKYLSDTKLDEKTITIDLDPGFEDGRQFGRGKSGGQVSDELRFDFDASRGGFAIPFAERVGVPHSRFDNSSSQSNTNNYIPPPDAMGTFRPGFDEEREDDNYVPQ
|
Component of the CBC complex, which binds co-transcriptionally to the cap of pre-mRNAs and is involved in maturation, export and degradation of nuclear mRNAs. The CBC complex is required for efficient pre-mRNA splicing through efficient commitment complex and spliceosome formation. Together with NPL3, the CBC complex is required for export of mRNAs out of the nucleus. The CBC complex is also involved in nuclear mRNA degradation, probably by directing the mRNAs to the sites of degradation. Affects replication of the positive-strand RNA virus BMV.
|
Q08920
|
Q8KA50
|
PT1_BUCAP
|
Phosphotransferase system, enzyme I
|
Buchnera
|
MISGILASPGIAFGNVLLLKKEEIVINRQNISTENIKTEINKFFNGRKKSVKQLTEIKIATGEKFGKKKEGIFEGHIMLLEDEELEKEIINLITEKKISAAEATKFIIEGQAKALEKIKDEYLKNRAIDVRDIGSRLLKNILNISIVDLNNIKNQVILISKDLTPSETAQINLKYILGFITDLGGPTSHTSIMARSLEIPAIVGTVNITKKVKNNDFIILDSLNNEIIINPSDQIINEKKQVERKYFFKKENLKKLRNLYATTTDGHNIKIGSNIGNIQDIYSAKKNGAECIGLYRTEFLFMGRNALPTENEQFQAYKEIAESMENKPVIIRTMDIGGDKDLPYMNLPKEENPFLGWRAIRISMDRKEILHAQLRAILRASAFGKIYILFPMIISVEEIRTLKIEVHKLQIQLKKEHLVFDENIKIGIMIETPASAIIADHLIKEVDFFSIGTNDLTQYTLAVDRGNDLISHLYNPISPSVIQLIKQVIDISHLHGKWTGMCGELAGDERVTTLLLGMGLDEFSMSSTSIPKIKEIIRKTSFSKSQELAKKVLKAATTKEILDLLNKFII
|
General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr).
|
Q8KA50
|
Q0HS04
|
APAH_SHESR
|
Diadenosine tetraphosphatase
|
Shewanella
|
MAHYFVGDVQGCFAELKRLLAEVDFNPSRDELWAVGDLVARGPDSLATLRYFQSLGDAGKTVLGNHDLHLLALHGKLKRDKPSDNLAPLLNAPDIASLIDWLRQQPLMRELPEHKVIMTHAGVPPQWSLDVLRQESQLVSQALKQSDYLEALISQMYSDTAERWDPSAIGLNRLRFCINALTRMRYLYVDGHLDFDCKQPPEDCSNPQLRPWFEFTSALRQSHTLVFGHWAALMGKVNDPKLKALDTGCCWGEYLTLWHLEKDQKITQKKLKKG
|
Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP.
|
Q0HS04
|
A1W581
|
DER_ACISJ
|
GTP-binding protein EngA
|
unclassified Acidovorax
|
MKPVIALVGRPNVGKSTLFNRLTKSRDAIVADFAGLTRDRHYGNGRQGKHEYIVIDTGGFEPDASSGIYREMARQTQQAVAEADVVVFVVDVRGGLSAQDHDIANYLRRLGKPCVLAGNKAEGMQDSMHLAEFYELGLGEVHPVSAAHGQGVRSLVDLALKPLALPEIEEEDAAAEKNVIRLAVAGRPNVGKSTLINTWLGEERLVAFDMPGTTRDAISVPFERNGQKFELIDTAGLRRKGKVFEAIEKFSVVKTLQAIESANVVLLLLDATQGVTDQDAHIAGYILESGRAVVIAVNKWDAVDDYGRQQLERSIETCLSFLKFAPLHFISAKKRQGIGPLWSSIIQAYKSANRKMPTPVLTRLLQEAVQFQSPKRSGMFRPKMRYAHQGGMNPPVIVIHGNSLEHVTDAYKRFLEARFRKEFDLVGTPLRIEMKTSSNPYTDKQNS
|
GTPase that plays an essential role in the late steps of ribosome biogenesis.
|
A1W581
|
Q0RDP7
|
RNH2_FRAAA
|
Ribonuclease HII
|
Frankia
|
MRPRGVVIRRDAGLFGYERALVRCGLGPVAGVDEAGRGACAGPLVVAAVVLGPDGRRRLSPRLADSKLLTEQVREGLFDEVLRAAADWSAVVIPAAEIDRTGVHVANITGMRRAVARLGHRPGYVLTDGFAVAGFGTESLAVVKGDRVAACIAAASIVAKVTRDRIMRALHTRYAEYDFAQHKGYVTAAHAAALARYGPCDEHRKSYVNVAAHAVPTREARSLRLEDRVLATSLHGVTETA
|
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
|
Q0RDP7
|
Q8RLX0
|
SOXA_CHLTI
|
Thiosulfate-oxidizing multienzyme system protein SoxA
|
Chlorobaculum
|
MKKTIQRGLFTGALVLLTAMTSKPAHAAVNYQALVDADVKKFQGYFLKEFPGVKLEDFGDGVYALDEDSRKQWKEMEEFPPYELDVEAGKALFNKPFANGKSLGSCFSNGGAVRGMYPYFDEKRKEVITLEMAINECRVANGEKPYAPKKGDIARVSAYIASISRGQKIDVKVKSKAAYDAYMKGKEMFYAKRGQLNMSCSGCHMEYSGRHLRAEIISPALGHTTHFPVFRSKWGEIGTLHRRYAGCNENIGAKPFPAQSKEYRDLEFFQTVMSNGLKFNGPASRK
|
C-type monoheme cytochrome, which is part of the SoxAX cytochrome complex involved in sulfur oxidation. The SoxAX complex catalyzes the formation of a heterodisulfide bond between the conserved cysteine residue on a sulfur carrier SoxYZ complex subunit SoxY and thiosulfate or other inorganic sulfur substrates. This leads to the liberation of two electrons, which may be transferred from the SoxAX complex to another cytochrome c and which then may be used for reductive CO(2) fixation.
|
Q8RLX0
|
B0KSC5
|
ISPF_PSEPG
|
2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
|
Pseudomonas
|
MRIGHGYDVHRFCDGDFITLGGVRIPHKYGLLAHSDGDVLLHALSDALLGAAALGDIGKHFPDTDPQFKGADSRALLRHVVGIVRAKGWKVGNVDATIVAQAPKMAPHIETMRQLIAEDLQVELDQVNVKATTTEKLGFTGREEGIAVHSVALLLPA
|
Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP).
|
B0KSC5
|
Q7UFU6
|
QUEC_RHOBA
|
Queuosine biosynthesis protein QueC
|
Rhodopirellula
|
MERRLVNSTSQSKTESAQQDAGKAVVLLSGGLDSATCVAIARDQGFEVHAISFRYGQRHDGELDRAAKQASLMGVVSHRVIDIDLAQLGGSALVDSSIAVPKSDHVDKIAGDIPVTYVPARNTIFLSYALAVAETLGSRDIFIGVNALDYSGYPDCRPEFIDAFQTMARLATKAGVEDEHSLTIHTPLLHWTKAEIIQRGIELGVDYSQTLSCYDPQGSSDEMRPCGQCDACLLRAKGFAENEIADPAIG
|
Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
|
Q7UFU6
|
C1DKZ4
|
LFTR_AZOVD
|
Phenyalanyltransferase
|
Azotobacter
|
MLTCLQRDSLSFPPLERALHQPNGLLAVGGDLSAERLIQAYRHGCFPWYQAGQPILWWSPDPRTVLFPRELHVSRSLRKVLRQERFQVSFDRDFAAVIQACAGPRDYADGTWITPEMRKAYQELHHRGIAHSVEVWQNGVLVGGLYGLAIGQLFFGESMFSHADNASKVGFATLVERLERWGFVLIDCQMPTQHLQSLGARSIPRTEFSDYLMHHLDLPSTADWIA
|
Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
|
C1DKZ4
|
B2ADA5
|
GH6D_PODAN
|
Probable exoglucanase GH6D
|
Podospora anserina
|
MRAVYAILAGLLATGSASPLEARQSGNPFVGRSLFVNPKYSESLERTRQAFLSRGDQTNAAKVQYVQNKVGTFVWISNIFLLRDIDDAIRNARAAQSRGEKPIVGLVLYNLPDRDCSAGHSSGELSLDQNGLNRYRTEYVQPFAQKLKAASDLQFAVILEPDAIGNMVTGTTAFCRNARGPQQDGIAYAIQQLQASNIHLYLDVANGGWLGWADNLKPTTILQKAGSNARIRGYSSNVSNYNPYSTNNPPPYTAGSPSADESRYATSLGNALRERGLPTNFIIDQGRVALDGARKEWGEWCNVSPAGFGQPFTTNTNNPNVDAILWVKPGGESDGTCGMSGAPQAGAWFDAYAQMLTTNAHPEIRADGGGGGSPAPGPSSTAVAPSPSATPGGNCAARWAQCGGQGWTGPTCCAQGTCQASNQWYSQCL
|
Probable exoglucanase that may play an important function in biomass degradation by catalyzing the hydrolysis of cellulose.
|
B2ADA5
|
A9AES0
|
MINC_BURM1
|
Probable septum site-determining protein MinC
|
Burkholderia cepacia complex
|
MSLKKSPFFELRSGSVDTLLFTVKTTDLDALRAELVKRFEATPEFFADDVVAIDVRRLADGERVALADIRQMLSDVRMRPVGVVALATQGWATEAGLPLLEARDRRAPAAKAADEAEPVAAPAVEAAAAPAAEPTPEPGAASQPAGVQTLVIDRPLRSGQQIYAKGDLVVLAPVSHGAEIIAEGNIHIYAPLRGRALAGVHGNHDARIFCTCLEPELISIAGIYRTTENPLPADVLGKSVQIRLEEEKLMIEPLRLT
|
Cell division inhibitor that blocks the formation of polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings. Prevents FtsZ polymerization.
|
A9AES0
|
B2JA13
|
PSBH_NOSP7
|
Photosystem II reaction center protein H
|
Nostoc
|
MAQRTRLGDILKPLNSEYGKVAPGWGTTPVMAVFMALFFVFLLIILQLYNRSLLVQDVLVDWRSLGR
|
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.
|
B2JA13
|
B1JX26
|
UREG_BURCC
|
Urease accessory protein UreG
|
Burkholderia cepacia complex
|
MNAPAPSSVRRTKKLPPLRVGIGGPVGSGKTTLLEMLCKAMRDRYDLVAITNDIYTKEDQRLLTVAGALPEERIMGVETGGCPHTAIREDASINLEAVDRMLARFPDADIVFIESGGDNLAATFSPELSDLTIYVIDVAGGEKIPRKGGPGITKSDLLVINKTDLAPLVGANLDVMASDTRKMRGERPYVMTNLKALDGVADVIAFIEKKGLLTV
|
Facilitates the functional incorporation of the urease nickel metallocenter. This process requires GTP hydrolysis, probably effectuated by UreG.
|
B1JX26
|
B4SJX6
|
MURC_STRM5
|
UDP-N-acetylmuramoyl-L-alanine synthetase
|
Stenotrophomonas maltophilia group
|
MIRRLHDTNDLVRAFPRVHFVGIGGTGMSGIAEVMLTLGYEVSGSDNADNVATRRLASLGARIMRGHSAANVLGTDCVVVSSAIREDNPELMEARSQRIPIMPRAAMLAELMRFRRGIAVAGTHGKTTTTSLTAAVLSEGGLDPTFVIGGQLLAAGANAKLGGGQWLVAEADESDGSFLRLNPLMSIITNIDADHLENYGNDFARVQAAFAEFLQRLPFYGLAVLCIDDPEVAALAAKTPRHVMSYGMSPQADVRAENVVQEGSRMRFTLRLPQGTSQEVVLALPGKHNVLNALAAAAVGWQLGVAPDAIARALEGFAGVGRRFNDLGEVTTASGAKVRIIDDYGHHPSELEAVFAAARGGWADKRLVVAFQPHRYSRTRDQFDKFAAVLSSVDALVLSEVYPAGEEPIAGADSHALARAIRARGRSEPVVVGKAAELASVLPDVLQDGDLLLMMGAGDIGAVATHIAVEGFKGEGEA
|
Cell wall formation.
|
B4SJX6
|
Q8DD43
|
TRMA_VIBVU
|
tmRNA (uracil(341)-C(5))-methyltransferase
|
Vibrio
|
MATLDVNPQRYQQQLAEKVQRLTDMFAPYQAPELEVFESPDQHYRMRAEFRVWHEGEEMYYIMFNQETREKYRVDQFPAASRLINDLMPLLIDAMKDNESLRRKLFQVDFLSTLSGEILVSLLYHRQLDDAWIENAKALKQRLNDEGFNLNLIGRARKMKIVLDRDYVVEKLDVNGKPYTYQQVENSFTQPNGKVAEKMLEWAVDCTQESQGDLLELYCGNGNFSLALAQNFERVLATELAKPSVESAQYNIAANKIENVQIIRMSAEEFTEAMEGKREFRRLKDNGIDLKSYNCNTIFVDPPRSGMDVDTCKMVQGYERILYISCNPETLKENLDILSETHHITRFALFDQFPYTHHMEAGVMLERKA
|
Dual-specificity methyltransferase that catalyzes the formation of 5-methyluridine at position 54 (m5U54) in all tRNAs, and that of position 341 (m5U341) in tmRNA (transfer-mRNA).
|
Q8DD43
|
A7Z4C5
|
COAD_BACVZ
|
Pantetheine-phosphate adenylyltransferase
|
Bacillus amyloliquefaciens group
|
MASIAVCPGSFDPVTYGHLDIIRRGANVFEQVYVCVLNNSSKQPLFTVEERCELLREVTKDIPNVTVETSQGLLIDYAKKKRAKAIIRGLRAVSDFEYEMQGTSVNRVLDESIETFFMMTNNQYSFLSSSIVKEVAKYNGPVSEFVPPEVEQALMQKFKG
|
Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
|
A7Z4C5
|
Q47BG9
|
AMPA_DECAR
|
Leucyl aminopeptidase
|
Dechloromonas
|
MEFSIKSGSPEKQRSACVVVGVFESRKMTLPAELLDKASGGYISDIVRRGDMEGKAGSTLLLHSVPSTLCDRILLVGLGKEKDFREKEFASAIRTAVKVLNETGAFDASIFLTELPVRKRSIAWRVRQTAMIALDATYKFDQFKSKKEEIRRPLRKLTISVERRNELAPAEEALAQGLAIAEGMAMAKTLGNLPPNICHPTYLAEQAQAMAEEFKLGCEILDRAEMEKLGMHSLLSVARGSHQPPKLIVLTYKGARASEKPIVLVGKGVTFDTGGISLKPGAEMDEMKYDMCGAASVLGTMQAVARMALPINLTVVVPATENMPGGNATRPGDIVTSMSGQTIEILNTDAEGRLILCDALTYAERFEPDTVIDVATLTGACVVALGSIATGLFANKDALARDLLDAGEDANDRGWHMPLWDDYQELLKSPFADMANIGGRWGGAISAACFLSRFTKKFDWAHLDIAGTAWKSGADKGATGRPVPMLAYYLLQRAGKLN
|
Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
|
Q47BG9
|
O18728
|
FSCN2_BOVIN
|
Retinal fascin
|
Bos
|
MPTNGLHQVLKIQFGLVNDTDRYLTAESFGFKVNASAPSLKRKQMWVLEPDPGEGTAVLFRSSHLGRYLSAEEDGRVACEAERPGRDCRFLVLPQPDGRWVLQSEPHGRFFGGTEDQLSCFATAITPAELWTVHLAIHPQAHLLSVSRRRYAHLCPQEDEIAADSNTPWGVDALVTLIFQNRQYCLKSCDSRYLRSDGRLVWEPEARARYTLEFKAGKLAFKDCDGHYLAPVGPAGTLRAGRNTRPGKDELFDLEESHPQVVLVAANHRYVSVRQGVNVSANQDEELDHETFLMQIDQETKKCTFYSSTGGYWTLVTHGGIQATATQVSENTMFEMEWRGRRVALKASNGRYVCMKKNGQLAAISDFVGEDEEFTLKLINRPILVLRGLDGFVCHRRGSNQLDTNRSVYDVFHLSFSDGAYQIRGRGGGFWHTGSHGSVCSDGERAEDFLFEFRERGRLAIRARSGKYLRGGASGLLRADADAPAGVALWEY
|
Acts as an actin bundling protein. May play a pivotal role in photoreceptor cell-specific events, such as disk morphogenesis.
|
O18728
|
P0CW43
|
FWDC_METMP
|
Tungsten-containing formylmethanofuran dehydrogenase II subunit C
|
Methanococcus
|
MNELILNLKGDVSVPVEMDKILPEKIQEMSLEEISGIELIQGNKTAKVSEIFDVELKESDVAKVTINNCCKKVKRIGEKMTSGEIVVNGDAGMYIGVEMKGGKITVNGDAESWVGQNLKGGEIIINGNAENYVGSAYRGDWRGMSGGKITITGNAGSELGEYLKGGTIVIKGNTKIMPGIHQNGGMIIIEGDIEGRAGGEMMKGAIVVYGKILEPLPSFKFEGIVEDPLVKLSKKDAGTQLKGTFIKFSGDYVNTKPKGQLYAAIENNKNLI
|
Catalyzes the reversible oxidation of CO(2) and methanofuran (MFR) to N-formylmethanofuran (CHO-MFR). This enzyme is oxygen-labile.
|
P0CW43
|
C5BB97
|
HLDD_EDWI9
|
ADP-L-glycero-beta-D-manno-heptose-6-epimerase
|
Edwardsiella
|
MIIVTGGAGMIGSNIVKALNDKGYTDILVVDNLKDGTKFVNLVDLDITDYMDKEDFIAGIVAGDDFGDIDAVFHEGACSSTTEWDGKYVMDNNYQYSKELLHFCLERQIPFLYASSAATYGMTDKFVEDRHYEGPLNVYGYSKFLFDQYVRRILPHAKSQICGFRYFNVYGPREGHKGGMASVAFHLNTQINNGEQPKLFEGSENFRRDFIYVGDVADVNLWFWENGVSGIFNCGTGNAESFQAVADAVVAYHQKGSVTYIPFPDKLKGRYQAFTQADTTQLRAAGYSRPFKTVAQGVREYMEWLNRKP
|
Catalyzes the interconversion between ADP-D-glycero-beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose.
|
C5BB97
|
C5B7R2
|
LEUC_EDWI9
|
Isopropylmalate isomerase
|
Edwardsiella
|
MGKTLYQKLYDAHIVHQTPGETPLLYIDRHLVHEVTSPQAFDGLRAQRRRVRRPEHTFATMDHNVSTQSRDIHACGEMARVQMETLMANCREFGVQLYDLHHPHQGIVHVIGPEQGMTLPGSTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLKQDRARTMQVVIQGRCAEGISAKDIVLAVIGHLGHAGGTGYVVEFCGPAVEALSMEGRMTLCNMAIELGAKAGLIAPDETTFAYLQGRPFAPQGAQWQQAVDHWRTLRSDADARYDRTVTLQADDIAPQVTWGTNPGQVIAIDTPIPSPASLSDPIARASAHKALAYMDLQPGTRMSDVAIDRVFIGSCTNSRIEDLRAAAAVARGRRVAPGVQAMVVPGSGPVKAQAEAEGLDKIFTEAGFEWRLPGCSMCLAMNNDRLGSGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAVCGHFADIRQFQEPAHD
|
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
|
C5B7R2
|
C0RFV3
|
DCUP_BRUMB
|
Uroporphyrinogen decarboxylase
|
Brucella
|
MNLKVLKVIDGETVFPPPIWMMRQAGRYLPEYRETRKKAGSFLDLCYSPDLAVEVTLQPIRRFGFDAAILFSDILVVPHALGRDLRFEEGKGPLMTPIDADEIFWLETEGVAKRLEPVYETVRLVREQLPDETTLLGFCGAPWTVATYMIAGHGTPDQAPARLFAYRFPEAFEKLLNDLADVSAEYLIEQLGAGADAVQIFDSWSGVLDEDCFERFCIRPVARIVQKVRAVYPQARIIGFPKGAGMLYAGYREKTGVDMLGLDWSVPLSFAALLQEEGAVQGNLDPLRVVAGGNALDEGVDAILERMGQGPLVFNLGHGITPQAPIENVQRMIDRVRGGKS
|
Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
|
C0RFV3
|
Q0STR1
|
HFQ_CLOPS
|
RNA-binding protein Hfq
|
Clostridium
|
MNKSINNLQDIFLNNARKERIPVTIFLVNGVQLKGIVKGFDSFTVVLDSDGKQQLVYKHAISTVSPAKPILFNSAQVFDN
|
RNA chaperone that binds small regulatory RNA (sRNAs) and mRNAs to facilitate mRNA translational regulation in response to envelope stress, environmental stress and changes in metabolite concentrations. Also binds with high specificity to tRNAs.
|
Q0STR1
|
P33376
|
PHLD_BACCE
|
Phosphatidylcholine cholinephosphohydrolase
|
Bacillus cereus group
|
MKKKVLALGAAITLVAPLQSVAFAHENDGGQRFGVIPRWSAEDKHKEGVNSHLWIVNRAIDIMSRNTTLVKQDRVALLNEWRTELENGIYAADYENPYYDNSTFASHFYDPDNGKTYIPYAKQAKETGAKYFKLAGESYKNKDMKQAFFYLGLSLHYLGDVNQPMHAANFTNLSYPQGFHSKYENFVDTIKDNYKVTDGNGYWNWKGTNPEDWIHGAAVVAKQDYAGIVNDNTKDWFVRAAVSQEYADKWRAEVTPMTGKRLMDAQRVTAGYIQLWFDTYGNR
|
Required, with sphingomyelinase, to effect target cell lysis (hemolysis).
|
P33376
|
B1LM67
|
BIOF_ECOSM
|
8-amino-7-ketopelargonate synthase
|
Escherichia
|
MSWQEKINAALDARRAADALRRRYPVAQGAGRWLVADDRHYLNFSSNDYLGLSHHPQIIRAWKLSAEQFGVGSGGSGHVSGYSVAHQALEEELAEWLGYSRALLFISGFAANQAVITAMMAKEDRIVADRLSHASLLEAASLSPSPLRRFAHNDVTHLARLLASPCPGQQLVVTEGVFSMDGDSAPLEEIQQVTQQHDGWLMVDDAHGTGVIGEQGRGSCWLQKVKPELLVVTFGKGFGVSGAAVLCSNTVADYLLQFARHLIYSTSMPPAQAQALRASLAVIRSDEGDARREKLAALITRFRAGVQDLPFTLADSWSAIQPLIVGDNSRALQLAEKLRQQGCWVTAIRPPTVPAGTARLRLTLTAAHEMQDIDRLLEVLHDNG
|
Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide.
|
B1LM67
|
A4XYC6
|
G6PI_PSEMY
|
Phosphohexose isomerase
|
Pseudomonas
|
MAYYQQPHDITRLPAWQALQQHRAEMAGFSMREAFAGDPRRFQRFSLDSCGLLLDYSKNLITEKSLELLIQLAEQADLHEAIAALYNGERVNASEGRAALHTALRSPIGRRLLVDGNDIIPEVHRVLNQVTELVSRIHSGLWRGYSEKPIKEVVNIGIGGSFLGPQLVSEALRPFTQRGVRCHYLANIDGSEFRELTARLDPETTLFIVSSKSFGTLETLKNTLAARDWYLAMGGPEEQLHRHFIAVTSNRKAAIEFGIGEENIFPMWDWVGGRYSLWSAIGLPIALAIGVSNFKELLAGAYAMDEHFTQAPLAENMPVLMALLGVWYTNFWGAQSHAILPYDHYLRNFTKHLQQLDMESNGKSVRQDGTPLDIATGPIIWGGVGCNGQHAYHQLLHQGRLLVPADFIVPVNSYNPLSDHHQWLFANCLSQAQALMQGKTREEAEVELRAKGLSEDEVQRLAPHKVIPGNRPSNILVMNRIAPFNLGALVALYEHKVFVQSAIWGINAFDQWGVELGKEMGKEVYQRLTGASGEPASDASTQGLIEHFRSQHRG
|
Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
|
A4XYC6
|
Q1RIX0
|
IF2_RICBR
|
Translation initiation factor IF-2
|
belli group
|
MTDNQENKPKKLTLSNTKLSLNKSFDSLASTQSFVNAKSKTLVEVRKSYSGSTTTLSLNKEKGSLETGSSSGSEEFNRRLSILKKAAEQSKLNDNSQISTLSKLASINQSIASQEDPIEVEQEESSDTNKVKEEPKIEEVKDIEESTLQTPKKKEDIFVKSPLVGTRTRYGIESEKTVDKVTENKVIAPKPKVEESRKFKKTDLFNMVGDDENDNRNRTRSLASIKRAREKEKRKSLVQAPEKVYREITLPEVIGVGDFANAMSERVSDVIKELMKLGILANASQTIDADTAELVATHLGHAVKRVQESDVENILITNDKEEDLRSRAPVVTVMGHVDHGKTSLLDALKSTDVASGETGGITQHIGAYRVTLADGRAITFIDTPGHEAFSEMRSRGAGVTDIVIIVVAADDGIKPQTVEAINHAKAANVPIIVAINKIDKPDIDIERVKNELYMYEIIGEEAGGDVMVIPISALKKINLDKLEEAILLIAEMQNLKASPFGSASGVVIESKIEKGRGALTTMLVQRGTLKSGDIIIAGTAYGKVKKMTNDKGIEVLEATPSVPIEIQGLSHVPHAGDMFNVVQTEKQAKDIAEYRERVAKEKKISIAPRSSLEDLFLKASGSSKIKELPLIIKGDVHGSVEAIAGSLLKLPNDEVKLRILHSGVGPITESDVSLAHASSAIIVGFNVRAGANAKTAAEKEKVEIRYYSIIYDLLDDVKAIMSGMLDPIIREQYIGSVEIRQIFNITKIGKIAGSYVTRGIIKKGAGVRLLRDNIVIHEGKLKTLKRFKEEVKEVREGYECGIAFENYEDIREGDTVEVFELIQEKKQL
|
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.
|
Q1RIX0
|
B9LMX0
|
AROC_HALLT
|
5-enolpyruvylshikimate-3-phosphate phospholyase
|
Halorubrum
|
MNGNRFGRLFQVTTYGESHGEAMGVTVSGVPAGVELDEEAIQAQLDRRKPGQSMITTSRGEPDEVVVNSGVQDGYTTGTPIGMVIQNKDARSGKYEPYVTAPRPSHGDYTYSAKFGTRNWGGGGRSSARETVNWVAAGAVAEQVLDASEYDVEIKAHVNQIGDVEADDVSFEQILDHSEENDVRCADPEAAAEMQELIERYQEAGDSIGGSIYFECRGVPRGLGAPRFDGFPSRLGQAMFSIPATTGVEFGLGKDAVNVTGSERNEDWTFDDGESFDHVESEEGDPVPVGNDHGGLQGGITTGEPIYGEATWHAPTSIPKKQRSADWETGEEKDVQVVGRHDPVLPPRAVPVVEAMLYCTVLDFMLLAGRINPDRVDGNPGQYDTDYHPSSPDND
|
Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.
|
B9LMX0
|
Q4WKW9
|
FGNA_ASPFU
|
Partially reducing polyketide synthase fngA
|
Aspergillus subgen. Fumigati
|
MSFPQVDVPSLPVGSASTQDTSPVSGPFNSSDSDHDIVNGGQANGSPFTEPIAICGLGLRLPGGIRDGDSFWDLLVNGRDARMPIPASRYNISGFDGSLDGRDPIKTTHGYFLDEDLSSLDASFFSMTKTELEKCDPQQRQLLEVTRECLEDAGETDYRGRNVGCYIGNFGHDWMEISLREPQHSRSYNVLGYSDMILANRVSYEYDLRGPSVVIKTACSASLVALHEACRALQARDIPSAIVGGTSLILAPTLTSNFFGEGILSPEASCKTFDESADGFARAEGVTAIYVKRLDDALRDGNPIRAVIRGTGTNSDGKSMGIMSPSAEAHEALMRQVYDQAGLSPRETAFVEEKRRLSNASKCHGTGTATGDPIEATAVGNVFSERGVYIGSVKPNVGHSEGCSGITSLIKAVLALEHKTIPPNIKFRNPNPKIPFVEKKLVVPIQPTPFPLDKAERISVNSFSIGGSNAHIDAYKSYARDHPDAISDIAYTLAVRRERLPHRAFAIWQNGELQTSSLSKASAVPPAITMIFSGQGAQWAEMGKKLIETEASFRHDLASMDSILQSLRKPPCWSILEELQKPAEDSQINRAEMAQPLCTALQVALFHQLKRLGIKPTAVVGHSSGEIAAAYAAGYITLEYALAVAYYRGYITKNADRSRGAMAAVRLSATEVLPFLRTGVCIACENSPSSTTISGDKEALKEILARLKEEKPDVFARLLKVEMAYHSRASETLLLVLRSTHIFADHMKPLGIEYLELLRAENNFGIPRSADKALFLSSVICKPMVDTASFGPEYWVDNLNSPIWHQDSTATFLSALGRMYQEAVPLAVKALFPEERRALCGLPVYPWDHSESYWYESRLSSAWRQRPFPHHSLLGERTVDSPDFSPIWRNMLSLEDVTWIADHKIRRDVVFPLAGYIAMAGEAIRQTTGVDVGYRLRDVEARKALVLTDFKATEVVTVLHAHTGVPAEGPSWYDFSIASCHGGSWLIHCTGQVSPLAETLSLSWEPESASQRSLPRELTPMRFYEAMARVGVVFGPEFQRLVDITSSATDPLAEARVMSPAPRENKRPFALHPTAIDACIQLLIVAAARGLCRNLDQLEVPVVVGNVEVVSRGSANLRALAQDFTQGVECVTENSKLALRMSGLQLAPLAAEVADQIDVHAGARLQWLPDFDFVDHSGLFNKPQRPSLEIELEEQLTLLCVLESMDKVAHIPPCHPHLAKYREWLALQVRMAEAGQYTLVEHAKEWVGLPRVKRQKLIQDTYAKILDLPGRHAYSVGIKRICEHADQIFTGEADTLDLLMQDDILAELYDSVSFGYGDFVRLLSSNRPNLRILEVSAGTGGTTEQTLRGLVDSSSLPPYSVYTFTDVSAGFFPQAKERFAYAPNMEFRTFDISQDGLIQGFEAASYDIILAPNVVHATASLKETLSNLEPLLKPNGFIILTELCSLIKSPNYIFGNFVGWWLGEADGRDWEPYVQPEQWDAELKAAGFTGVNAVVPDQDVPSYRLAATIISQPARKADVPEIDRAVTLLYQSADADIVERLQLYLRDSGWQVDKCQLGEEMPPKGQDIIASVRLESDFFGEDLSPDRLAAFQALIRHLDAEKVLWLCPRFQVRCKDPQSAQTLGVAQTVRTELNLPLFTLEIDTNETRFEELVHRVLQKIRTTKDEASLHADKEFVVTDGQVCIGRYHPFDLKKELPSRALTLDSAAAYLLVGGTGGLGRSMTTWMVEYGATELILLSRRAGKDRESQSLSQELEQMGCSVHLVAGSVENPEDIARSIASAKKPIKGVFQLAMVLQDAPLLEMTYSDWVNVNGPKVTGTWNLHHALKDQPLDFFWLASSILTAVDTPGQANYLATGTFLEAFCQYRHSLGLPASVLNICPVEGVGFVAENAHAKKNMKAQGIYTLREREFLDFVELSLIDSTPSAGGNTSPTATPPGPWVNRSQVVMGLRSEQGLGDPHNRASWRHNRRMRLYHNRRTQESESARDGKNGAKASALQAFLERVREMGDEGLLRGEGVDFLAFEVGKKIHDLMLKPDEEVEIGRTLAQIGLDSLMAIELRRWIKQVFGLTMSVLEIMGSGSLKQLAEDLAAKYAEKIQQ
|
Partially reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of fumigermin that inhibits germination of spores of the inducing S.rapamycinicus, and thus helps the fungus to defend resources in the shared habitat against a bacterial competitor . The partially reducing polyketide synthase fngA alone is sufficient for the production of fumigermin . FgnA catalyzes the condensation of 3 malonyl-CoA units to an acetyl-CoA starter, and 3 methylations to yield fumigermin . It is remarkable that the five cluster genes including fgnA are conserved in distantly related fungi, supporting the assumption of a fumigermin cluster; it is thus possible that originally all five genes were functional, but that the genes encoding tailoring enzymes became inactive from mutations, similar to the case of the fgnA gene in strains A1163 and Af293 (Probable).
|
Q4WKW9
|
Q4UTA3
|
RS6_XANC8
|
30S ribosomal protein S6
|
Xanthomonas
|
MSRHYEVVFLVHPDQSEQVPAMIERYKSLIEGGNGTIHRLEDWGRRQLAYPIQNLVKAHYVLLNIEVDQAVLSELVESFRFNDAVLRHLVIKRDGPDTEQSLIMKSKDEKGDKPERSERRRRDDEEGDAAPAATDTDGDNAEAA
|
Binds together with S18 to 16S ribosomal RNA.
|
Q4UTA3
|
Q5VH50
|
MATK_BATMA
|
Intron maturase
|
Batis
|
MEEFQVYLELHKAHNFLYPLFFQEYIYALAHNHRLNRLNRSSLFQNGDYDNKFSSLIVKRLIFRMYQQNNFIISTKNLNQNTFFSHNKNLYYQIISVVLAVIVEIPFSIRFISSLEGKELVKSHNLQSIHSIFPFLEDKFSHLNYVLNVLIPHPIHLEILLQTLRYWIKDASSLHLLRFYLYEYSNLKNFFIPKKSTLNPRFFLFLYNSYVYQYESILFFLRKQSSHLQSNSFGILIERIYFYGKIESLLKVFIKKFQDILWLSKDPFMHYVRYRGKSILASKHGPLLISKWKYYFVNLWQCHFYVWSQSKRVHIKQLSKDYLNFLGYLSSLRLNFLVVRSQMLENSYLIDNVIKKFHTKIPMSSIIASLAKARFCNVLGHPISKSTWTDSSDSEILDRFVRIYRNLAHYYSGSSKKKNLYRIKYILRVSCVKTLARKHKSTVRAFLKRLGSDFLEEFLLEEEQVLSLMFSRVFSVSQRFYRVRIWYLDIFYINDFVNH
|
Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns.
|
Q5VH50
|
Q5HCR7
|
CLFB_STAAC
|
Fibrinogen-binding protein B
|
Staphylococcus
|
MKKRIDYLSNKQNKYSIRRFTVGTTSVIVGATILFGIGNHQAQASEQSNDTTQSSKNNASADSEKNNMIETPQLNTTANDTSDISANTNSANVDSTTKPMSTQTSNTTTTEPASTNETPQPTAIKNQATAAKMQDQTVPQEANSQVDNKTTNDANSIATNSELKNSQTLDLPQSSPQTISNAQGTSKPSVRTRAVRSLAVAEPVVNAADAKGTNVNDKVTASNFKLEKTTFDPNQSGNTFMAANFTVTDKVKSGDYFTAKLPDSLTGNGDVDYSNSNNTMPIADIKSTNGDVVAKATYDILTKTYTFVFTDYVNNKENINGQFSLPLFTDRAKAPKSGTYDANINIADEMFNNKITYNYSSPIAGIDKPNGANISSQIIGVDTASGQNTYKQTVFVNPKQRVLGNTWVYIKGYQDKIEESSGKVSATDTKLRIFEVNDTSKLSDSYYADPNDSNLKEVTDQFKNRIYYEHPNVASIKFGDITKTYVVLVEGHYDNTGKNLKTQVIQENVDPVTNRDYSIFGWNNENVVRYGGGSADGDSAVNPKDPTPGPPVDPEPSPDPEPEPTPDPEPSPDPEPEPSPDPDPDSDSDSDSGSDSDSGSDSDSESDSDSDSDSDSDSDSDSESDSDSESDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSDSESDSESDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSRVTPPNNEQKAPSNPKGEVNHSNKVSKQHKTDALPETGDKSENTNATLFGAMMALLGSLLLFRKRKQDHKEKA
|
Cell surface-associated protein implicated in virulence by promoting bacterial attachment to both alpha- and beta-chains of human fibrinogen and inducing the formation of bacterial clumps.
|
Q5HCR7
|
P80457
|
XDH_BOVIN
|
Xanthine oxidoreductase
|
Bos
|
MTADELVFFVNGKKVVEKNADPETTLLAYLRRKLGLRGTKLGCGEGGCGACTVMLSKYDRLQDKIIHFSANACLAPICTLHHVAVTTVEGIGSTKTRLHPVQERIAKSHGSQCGFCTPGIVMSMYTLLRNQPEPTVEEIEDAFQGNLCRCTGYRPILQGFRTFAKNGGCCGGNGNNPNCCMNQKKDHTVTLSPSLFNPEEFMPLDPTQEPIFPPELLRLKDVPPKQLRFEGERVTWIQASTLKELLDLKAQHPEAKLVVGNTEIGIEMKFKNQLFPMIICPAWIPELNAVEHGPEGISFGAACALSSVEKTLLEAVAKLPTQKTEVFRGVLEQLRWFAGKQVKSVASLGGNIITASPISDLNPVFMASGTKLTIVSRGTRRTVPMDHTFFPSYRKTLLGPEEILLSIEIPYSREDEFFSAFKQASRREDDIAKVTCGMRVLFQPGSMQVKELALCYGGMADRTISALKTTQKQLSKFWNEKLLQDVCAGLAEELSLSPDAPGGMIEFRRTLTLSFFFKFYLTVLKKLGKDSKDKCGKLDPTYTSATLLFQKDPPANIQLFQEVPNGQSKEDTVGRPLPHLAAAMQASGEAVYCDDIPRYENELFLRLVTSTRAHAKIKSIDVSEAQKVPGFVCFLSADDIPGSNETGLFNDETVFAKDTVTCVGHIIGAVVADTPEHAERAAHVVKVTYEDLPAIITIEDAIKNNSFYGSELKIEKGDLKKGFSEADNVVSGELYIGGQDHFYLETHCTIAIPKGEEGEMELFVSTQNAMKTQSFVAKMLGVPVNRILVRVKRMGGGFGGKETRSTLVSVAVALAAYKTGHPVRCMLDRNEDMLITGGRHPFLARYKVGFMKTGTIVALEVDHYSNAGNSRDLSHSIMERALFHMDNCYKIPNIRGTGRLCKTNLSSNTAFRGFGGPQALFIAENWMSEVAVTCGLPAEEVRWKNMYKEGDLTHFNQRLEGFSVPRCWDECLKSSQYYARKSEVDKFNKENCWKKRGLCIIPTKFGISFTVPFLNQAGALIHVYTDGSVLVSHGGTEMGQGLHTKMVQVASKALKIPISKIYISETSTNTVPNSSPTAASVSTDIYGQAVYEACQTILKRLEPFKKKNPDGSWEDWVMAAYQDRVSLSTTGFYRTPNLGYSFETNSGNAFHYFTYGVACSEVEIDCLTGDHKNLRTDIVMDVGSSLNPAIDIGQVEGAFVQGLGLFTLEELHYSPEGSLHTRGPSTYKIPAFGSIPTEFRVSLLRDCPNKKAIYASKAVGEPPLFLGASVFFAIKDAIRAARAQHTNNNTKELFRLDSPATPEKIRNACVDKFTTLCVTGAPGNCKPWSLRV
|
Key enzyme in purine degradation. Catalyzes the oxidation of hypoxanthine to xanthine. Catalyzes the oxidation of xanthine to uric acid. Contributes to the generation of reactive oxygen species.
|
P80457
|
Q16629
|
SRSF7_HUMAN
|
Splicing factor, arginine/serine-rich 7
|
Homo
|
MSRYGRYGGETKVYVGNLGTGAGKGELERAFSYYGPLRTVWIARNPPGFAFVEFEDPRDAEDAVRGLDGKVICGSRVRVELSTGMPRRSRFDRPPARRPFDPNDRCYECGEKGHYAYDCHRYSRRRRSRSRSRSHSRSRGRRYSRSRSRSRGRRSRSASPRRSRSISLRRSRSASLRRSRSGSIKGSRYFQSPSRSRSRSRSISRPRSSRSKSRSPSPKRSRSPSGSPRRSASPERMD
|
Required for pre-mRNA splicing. Can also modulate alternative splicing in vitro. Represses the splicing of MAPT/Tau exon 10. May function as export adapter involved in mRNA nuclear export such as of histone H2A. Binds mRNA which is thought to be transferred to the NXF1-NXT1 heterodimer for export (TAP/NXF1 pathway); enhances NXF1-NXT1 RNA-binding activity. RNA-binding is semi-sequence specific.
|
Q16629
|
B0R611
|
CBIM_HALS3
|
Energy-coupling factor transporter probable substrate-capture protein CbiM
|
Halobacterium
|
MHIMEGFLPGIWALVWFVVAIPVISYGALKTARLARNDELNKSHIAVAAAFIFVLSALKIPSVTGSTSHPTGTGIAVVLFGPAVTAFLSAIVLLYQALLLGHGGLTTLGANVVSMGVVGPVAGWVVFRALNPYLDLQKATFAAAVIADWTTYLVTSIQLGVAFPSGPGVAGVVDSIVRFASVFSITQIPIGIVEGALAAGLIGYIAMSRQSIKTRLGVTA
|
Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import.
|
B0R611
|
C6BUK3
|
DAPAT_MARSD
|
LL-diaminopimelate aminotransferase
|
Maridesulfovibrio
|
MPEFKLADRLATLPPYLFAEIDRLKAEVAAQGVDIISLGIGDPDLPTPDFIIEALHKAAKNPVNHQYPSYVGLLTFRQAVADWYKERFDVELDATKEVVSLIGSKEGIAHFPLAFVNPGDLVLVASPNYPVYPVASGFAGGEVEIVPLLEENDFLPNLDAISDEKWDKCKIFFVNYPNNPTSATATPEFYAELVAKAKKHNVIIAADAAYTEVYYDEDKKPISILETPGAKDVAIEFHSLSKTYNMTGWRCGMAVGNASLVAGLGKIKENVDSGIFQAVQEAGIVALKEGEPYVKEFRKIYKERRDCVIEALEKINISCKVPDASIFVWAKTPEGYTSSEFVSKLLKETGVVVTPGNGFGESGEGYFRISLTVDTDRLKEAVSRISKL
|
Involved in the synthesis of meso-diaminopimelate (m-DAP or DL-DAP), required for both lysine and peptidoglycan biosynthesis. Catalyzes the direct conversion of tetrahydrodipicolinate to LL-diaminopimelate.
|
C6BUK3
|
A4QWP8
|
MEP_MAGO7
|
Fungalysin MEP
|
Pyricularia
|
MRYSLSLALLGVAAVTVVAHPHTPGRHGVERRAIDLDAFRLQPTAEYVPKEEVPDQSSLAFISNDNYVDVATDLVKSVAPGIEFRVVGDHYVGTNGVAHVNFKQTAHGIDIDNADFNVNVRDGKVFSYGNSFFTGKIPEESPLKKRDFSDPTVALTGATTVLQLPISGEAKAEAKEGTETYTLKGTSGAVSDPEARLVYLVRDDSLALTWRVETDIEDNWLLSYVDANNKEQVHGVVDYVSHASFQVYPWGTNDPLEAGAARVTLTDPWDKASSPFGWLSDGTSTYTTTRGNNAIAQSNPSGGTAYLNNYRPTNANSIFSYPWTPAMSPPSSFVDFSATQLFYTANVFHDLLYKLGFTEAAGNFQVNNNGKGGLGNDQVILNTQDGSGTNNANFATPPDGQNGRMRMYIWTYTTPQRDSSLEAGVVIHEYTHGLSNRLTGGPSNSGCLSALEAGGMGEGWSDFFATAARIKQNDTADTDYPMGEWVAANPKGIRAYPYSTSLTRNPQTYATTNTLSTVHPIGNVWATVLYEVLWALVGKHGLQVSTFPTFDASGVPTSGNFLAQKLVLDGMALQPCNPNFVQARDAIIDADQALTGGANKCELWTAFAKRGLGSGAKYAASKRSVESKTIPAGVC
|
Secreted metalloproteinase that allows assimilation of proteinaceous substrates.
|
A4QWP8
|
Q6NWG0
|
TSN36_DANRE
|
Tetraspanin-3c
|
Danio
|
MDCGIITSKTILLLLSLIFWAAGAALAYVGSYVIKSYNNFEDFMSDRHTLIPAAIIIGVAVVMFIIGFVGCCATLRESKVGLGLFLIIIMLIFAAEVTAFVFGIIYRGRIRGDLEKSMNDVFLKYDGLNSETHAVDYLQSQLECCGVKNQTDWTLTSWFAQHNNTVPQSCCKANMTQCTGQLSQPDLLNTQGCEAKLEQVLQDVLSYAMLVILGFAIIKFFGMLSVCVITCKSKKNEYQPLYA
|
Plays a role in migration and segregation of pigment cells (melanophores and xanthophores). Contributes to pigment stripe patterning in the epidermis.
|
Q6NWG0
|
O14640
|
DVL1_HUMAN
|
DSH homolog 1
|
Homo
|
MAETKIIYHMDEEETPYLVKLPVAPERVTLADFKNVLSNRPVHAYKFFFKSMDQDFGVVKEEIFDDNAKLPCFNGRVVSWLVLAEGAHSDAGSQGTDSHTDLPPPLERTGGIGDSRPPSFHPNVASSRDGMDNETGTESMVSHRRERARRRNREEAARTNGHPRGDRRRDVGLPPDSASTALSSELESSSFVDSDEDGSTSRLSSSTEQSTSSRLIRKHKRRRRKQRLRQADRASSFSSITDSTMSLNIVTVTLNMERHHFLGISIVGQSNDRGDGGIYIGSIMKGGAVAADGRIEPGDMLLQVNDVNFENMSNDDAVRVLREIVSQTGPISLTVAKCWDPTPRSYFTVPRADPVRPIDPAAWLSHTAALTGALPRYGTSPCSSAVTRTSSSSLTSSVPGAPQLEEAPLTVKSDMSAVVRVMQLPDSGLEIRDRMWLKITIANAVIGADVVDWLYTHVEGFKERREARKYASSLLKHGFLRHTVNKITFSEQCYYVFGDLCSNLATLNLNSGSSGTSDQDTLAPLPHPAAPWPLGQGYPYQYPGPPPCFPPAYQDPGFSYGSGSTGSQQSEGSKSSGSTRSSRRAPGREKERRAAGAGGSGSESDHTAPSGVGSSWRERPAGQLSRGSSPRSQASATAPGLPPPHPTTKAYTVVGGPPGGPPVRELAAVPPELTGSRQSFQKAMGNPCEFFVDIM
|
Participates in Wnt signaling by binding to the cytoplasmic C-terminus of frizzled family members and transducing the Wnt signal to down-stream effectors. Plays a role both in canonical and non-canonical Wnt signaling. Plays a role in the signal transduction pathways mediated by multiple Wnt genes. Required for LEF1 activation upon WNT1 and WNT3A signaling. DVL1 and PAK1 form a ternary complex with MUSK which is important for MUSK-dependent regulation of AChR clustering during the formation of the neuromuscular junction (NMJ).
|
O14640
|
C3N0D7
|
CAPPA_SULIA
|
Phosphoenolpyruvate carboxylase
|
Sulfolobus
|
MRIIPRTMSTQHPDNAKVPEWAKSEVIEGEDEVKEAFLAYSMYGVHEVMWDAEGKDVDTHVVRKLLSNYPDYFREHILGKDVFLTYRLPNPKVEGADRKVFAETMESIPITYDLAEKFYGNGITVPVFEVILPMTTSNLEIISVARYYEKAVANEDELELYNGVKVKDLVGEIYPKVIEVIPLVEDRDSLQNIDNIVEGYYKVIKPKYMRVFLARSDPAMNYGMITAVLSVKIALSELYKLSESLNFEIYPIIGVGSLPFRGHLSPENYEKVLEEYKGVYTYTIQSAFKYDYDYDKVKSAISSINNSRIGPAKILEKYEEDVLRKITILYTERYQPIIESLANAINDVSVLLPRRRARKLHIGLFGYSRSAGKVSLPRAISFVGSLYSIGIPPELIGISSLSNLDEKEWDIFKQNYVNFKHDLQTAARFFNWESFELIKDIWKISEDTIAKIKEDIDYAESVIGIKLGDIDYDSRKHILMSSLFLLSFKEKILQESKKYLYEMALIRRSLG
|
Catalyzes the irreversible beta-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.
|
C3N0D7
|
Q47758
|
DDL_ENTFA
|
D-alanylalanine synthetase
|
Enterococcus
|
MKIILLYGGRSEEHDVSVLSAYSVLNAIYYKYYQVQLVFISKDGQWVKGPLLSERPQNKEVLHLTWAQTPEETGEFSGKRISPSEIYEEEAIVFPVLHGPNGEDGTIQGFMETINMPYVGAGVLASANAMDKIMTKYLLQTVGIPQVPFVPVLRSDWKGNPKEVFEKCEGSLIYPVFVKPANMGSSVGISKVENREELQEALEEAFRYDARAIVEQGIEAREIEVAILGNEDVRTTLPGEVVKDVAFYDYDAKYINNTIEMQIPAHVPEEVAHQAQEYAKKAYIMLDGSGLSRCDFFLTSKNELFLNELNTMPGFTDFSMYPLLWENMGLKYSDLIEELIQLALNRFK
|
Cell wall formation.
|
Q47758
|
Q58DT1
|
RL7_BOVIN
|
60S ribosomal protein L7
|
Bos
|
MEGAEEKKKKVPAVPETLKKKRKNFAELKIKRLRKKFAQKMLRKARRKLIYEKAKHYHKEYRQMYRTEIRMARMARKAGNFYVPAEPKLAFVIRIRGINGVSPKVRKVLQLLRLRQIFNGTFVKLNKASINMLRIVEPYIAWGYPNLKSVNELIYKRGYGKINKKRIALTDNALIARSLGKYGIICMEDLIHEIYTVGKRFKEANNFLWPFKLSSPRGGMKKKTTHFVEGGDAGNREDQINRLIRRMN
|
Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. Binds to G-rich structures in 28S rRNA and in mRNAs. Plays a regulatory role in the translation apparatus; inhibits cell-free translation of mRNAs.
|
Q58DT1
|
P32879
|
3S11_AIPLA
|
Short neurotoxin A
|
Aipysurus
|
LTCCNQQSSQPKTTTDCADNSCYKKTWQDHRGTRIERGCGCPQVKPGIKLECCKTNECNN
|
Binds to muscle nicotinic acetylcholine receptor (nAChR) and inhibit acetylcholine from binding to the receptor, thereby impairing neuromuscular transmission.
|
P32879
|
Q8A483
|
RL16_BACTN
|
50S ribosomal protein L16
|
Bacteroides
|
MLQPKKTKFRRQQKGRAKGNAQRGNQLAFGSFGIKALETKWITGRQIEAARIAVTRYMQRQGQIWIRIFPDKPITRKPADVRMGKGKGAPEGFVAPVTPGRIIIEAEGVSYEIAKEALRLAAQKLPITTKFVVRRDYDIQNQNA
|
Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs.
|
Q8A483
|
B7HHH6
|
CYSH_BACC4
|
Thioredoxin-dependent 5'-adenylylsulfate reductase
|
Bacillus cereus group
|
MLTYETWEENVVSFSEEDETKGALSVLNWAYKEYKDEVVYACSFGVEGMVLLHIINQVNPSAKVVFLDTNVHFQETYELIQKVRERFPSLNIIEKQPELTLDEQAKLHGEKLWESNPNLCCKIRKILPLEKSLVVEKAWISGLRREQSETRKHTKFINQDHRFQSIKVCPLIHWTWKEVWRYVYKHSLPYNPLHDVGYPSIGCEKCTLPVGDGGDSRDGRWAGKVKTECGLHYQ
|
Catalyzes the formation of sulfite from adenosine 5'-phosphosulfate (APS) using thioredoxin as an electron donor.
|
B7HHH6
|
P06389
|
RK22_TOBAC
|
50S ribosomal protein L22, chloroplastic
|
Nicotiana
|
MLKKKKTEVYALGEHISMSADKARRVINQIRGRSYEETLMILELMPYRACYPILKLIYSAAANASYNMGSSEANLVISKAEVNGGTTVKKLKPRARGRSFPIKRSTCHITIVMKDISLDDEYVEMYSLKKTRWKKKSTAMPYRDMYNSGGLWDKK
|
The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome.
|
P06389
|
Q0I7X4
|
CY550_SYNS3
|
Low-potential cytochrome c
|
unclassified Synechococcus
|
MASFFSTLRRSLNRLLIALPVLLGLMISTPAQAAQWDAETLTVPADGDGALVTFSEQEIKTGRKVFNVSCGTCHAGGITKTNQNVGLDTETLALATPARDNVASLVDYLQDPTSYDGEYSIADLHPSMRSRDLYPAMRDLTDEDLRLMSGYILVAPKVLGVDWGGGKIYF
|
Low-potential cytochrome c that plays a role in the oxygen-evolving complex of photosystem II.
|
Q0I7X4
|
Q5L411
|
RL5_GEOKA
|
50S ribosomal protein L5
|
Geobacillus thermoleovorans group
|
MNRLKEKYLNEVVPALMSKFNYKSIMQVPKIEKIVINMGVGDAVQNPKALDSAVEELTLIAGQRPVVTRAKKSIAGFRLRQGMPIGAKVTLRGERMYEFLDKLISVSLPRVRDFRGVSKKSFDGRGNYTLGIKEQLIFPEIDYDKVNKVRGMDIVIVTTANTDEEARELLALLGMPFQK
|
This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.
|
Q5L411
|
Q8CTZ3
|
BIOW_STAES
|
Pimeloyl-CoA synthase
|
Staphylococcus
|
MYSIKMRASHEDIHISGAETMCEFEDLENYLKKYFNKAFNHENGNIDFLNLKIEKVKAPIQTLVALPVVENLNDTLTQLAKQTGVSEYALNKGLEFIKNDITYTGAIILSAQTGQRLDSTEQRGIRVTQLAFKTCKCNGEISERVKDARALATCINAFEGVKAELCVSDDLHYTTGYFASPKLGYRRIFNIKEKGTRHGGRIIFVDEGIHLNEYVSFLETVPKEIIEK
|
Catalyzes the transformation of pimelate into pimeloyl-CoA with concomitant hydrolysis of ATP to AMP.
|
Q8CTZ3
|
Q14296
|
FASTK_HUMAN
|
Fas-activated serine/threonine kinase
|
Homo
|
MRRPRGEPGPRAPRPTEGATCAGPGESWSPSPNSMLRVLLSAQTSPARLSGLLLIPPVQPCCLGPSKWGDRPVGGGPSAGPVQGLQRLLEQAKSPGELLRWLGQNPSKVRAHHYSVALRRLGQLLGSRPRPPPVEQVTLQDLSQLIIRNCPSFDIHTIHVCLHLAVLLGFPSDGPLVCALEQERRLRLPPKPPPPLQPLLRGGQGLEAALSCPRFLRYPRQHLISSLAEARPEELTPHVMVLLAQHLARHRLREPQLLEAIAHFLVVQETQLSSKVVQKLVLPFGRLNYLPLEQQFMPCLERILAREAGVAPLATVNILMSLCQLRCLPFRALHFVFSPGFINYISGTPHALIVRRYLSLLDTAVELELPGYRGPRLPRRQQVPIFPQPLITDRARCKYSHKDIVAEGLRQLLGEEKYRQDLTVPPGYCTDFLLCASSSGAVLPVRTQDPFLPYPPRSCPQGQAASSATTRDPAQRVVLVLRERWHFCRDGRVLLGSRALRERHLGLMGYQLLPLPFEELESQRGLPQLKSYLRQKLQALGLRWGPEGG
|
Required for the biogenesis of some mitochondrial-encoded mRNAs, specifically stabilizes ND6 (NADH dehydrogenase complex subunit 6) mRNA, and regulates its levels.
|
Q14296
|
Q9QXW0
|
FBXL6_MOUSE
|
F-box protein FBL6
|
Mus
|
MAPVASRRVRRRVRSSKRPDARGRSAEDWWWDRLAPRGSGYHLLQADSMLLVLPDLEPPRARAHRRARRRAPRSLARGPTAVAKPRTKPRPEPSLDQGLDSGWGDRIPLEVLVHIFGLLVAAHGPMPFLGRAARVCRHWHEATSHPSLWHTVTLSPSLVGRAGKGNLKGEKKLLACLEWLVPNRFSQLQSLTLIHWKSQVHSVLELVSKFCPRLTFLKLSDCHTVTAETLVMLARACCQLHSLDLHHSMVESTAVVSFLEEAGSRMRKLWLTYSSQTTAILGALLDNCCPQLQVLQVSTGMNCNNTPLQLPVEALQKGCPQLQVLRLLNLIWLPKPCGRGVPQGPGFPSLEELCLAGSTCNFVSNEVLGRLLHRSPKLRMLDLRGCARVTPSGLCHLPCQELEQLYLGLYGISDGLTLAKDGSPLLTRKWYHTLRELDFSGQGFSEKDLEQALAVFSGTPGGLHPALCSLNLRGTRVTPSTVSSVISGCPGLLYLNLESCRCLPRGLKRVYRGLEEVQWCLEQLLTSPPSAKEPT
|
Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex.
|
Q9QXW0
|
Q3SK28
|
IHFA_THIDA
|
Integration host factor subunit alpha
|
Thiobacillus
|
MTTLTKADLAELLFEKVGLNKREAKDVVESFFDEIRLALEKGDIVKLSGFGNFQCREKPQRPGRNPKTGEEMPISARRVVTFHASQKLKSQVEGARIGTPSQE
|
This protein is one of the two subunits of integration host factor, a specific DNA-binding protein that functions in genetic recombination as well as in transcriptional and translational control.
|
Q3SK28
|
Q9WVC6
|
SGK1_MOUSE
|
Serum/glucocorticoid-regulated kinase 1
|
Mus
|
MTVKAEAARSTLTYSRMRGMVAILIAFMKQRRMGLNDFIQKIASNTYACKHAEVQSILKMSHPQEPELMNANPSPPPSPSQQINLGPSSNPHAKPSDFHFLKVIGKGSFGKVLLARHKAEEVFYAVKVLQKKAILKKKEEKHIMSERNVLLKNVKHPFLVGLHFSFQTADKLYFVLDYINGGELFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKENIEHNGTTSTFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNKPLQLKPNITNSARHLLEGLLQKDRTKRLGAKDDFMEIKSHIFFSLINWDDLINKKITPPFNPNVSGPSDLRHFDPEFTEEPVPSSIGRSPDSILVTASVKEAAEAFLGFSYAPPVDSFL
|
Serine/threonine-protein kinase which is involved in the regulation of a wide variety of ion channels, membrane transporters, cellular enzymes, transcription factors, neuronal excitability, cell growth, proliferation, survival, migration and apoptosis. Plays an important role in cellular stress response. Contributes to regulation of renal Na(+) retention, renal K(+) elimination, salt appetite, gastric acid secretion, intestinal Na(+)/H(+) exchange and nutrient transport, insulin-dependent salt sensitivity of blood pressure, salt sensitivity of peripheral glucose uptake, cardiac repolarization and memory consolidation. Up-regulates Na(+) channels: SCNN1A/ENAC, SCN5A and ASIC1/ACCN2, K(+) channels: KCNJ1/ROMK1, KCNA1-5, KCNQ1-5 and KCNE1, epithelial Ca(2+) channels: TRPV5 and TRPV6, chloride channels: BSND, CLCN2 and CFTR, glutamate transporters: SLC1A3/EAAT1, SLC1A2 /EAAT2, SLC1A1/EAAT3, SLC1A6/EAAT4 and SLC1A7/EAAT5, amino acid transporters: SLC1A5/ASCT2, SLC38A1/SN1 and SLC6A19, creatine transporter: SLC6A8, Na(+)/dicarboxylate cotransporter: SLC13A2/NADC1, Na(+)-dependent phosphate cotransporter: SLC34A2/NAPI-2B, glutamate receptor: GRIK2/GLUR6. Up-regulates carriers: SLC9A3/NHE3, SLC12A1/NKCC2, SLC12A3/NCC, SLC5A3/SMIT, SLC2A1/GLUT1, SLC5A1/SGLT1 and SLC15A2/PEPT2. Regulates enzymes: GSK3A/B, PMM2 and Na(+)/K(+) ATPase, and transcription factors: CTNNB1 and nuclear factor NF-kappa-B. Stimulates sodium transport into epithelial cells by enhancing the stability and expression of SCNN1A/ENAC. This is achieved by phosphorylating the NEDD4L ubiquitin E3 ligase, promoting its interaction with 14-3-3 proteins, thereby preventing it from binding to SCNN1A/ENAC and targeting it for degradation. Regulates store-operated Ca(+2) entry (SOCE) by stimulating ORAI1 and STIM1. Regulates KCNJ1/ROMK1 directly via its phosphorylation or indirectly via increased interaction with SLC9A3R2/NHERF2. Phosphorylates MDM2 and activates MDM2-dependent ubiquitination of p53/TP53. Phosphorylates MAPT/TAU and mediates microtubule depolymerization and neurite formation in hippocampal neurons. Phosphorylates SLC2A4/GLUT4 and up-regulates its activity. Phosphorylates APBB1/FE65 and promotes its localization to the nucleus. Phosphorylates MAPK1/ERK2 and activates it by enhancing its interaction with MAP2K1/MEK1 and MAP2K2/MEK2. Phosphorylates FBXW7 and plays an inhibitory role in the NOTCH1 signaling. Phosphorylates FOXO1 resulting in its relocalization from the nucleus to the cytoplasm. Phosphorylates FOXO3, promoting its exit from the nucleus and interference with FOXO3-dependent transcription. Phosphorylates BRAF and MAP3K3/MEKK3 and inhibits their activity. Phosphorylates SLC9A3/NHE3 in response to dexamethasone, resulting in its activation and increased localization at the cell membrane. Phosphorylates CREB1. Necessary for vascular remodeling during angiogenesis.
|
Q9WVC6
|
P23620
|
PHOB_PSEAE
|
Phosphate regulon transcriptional regulatory protein PhoB
|
Pseudomonas
|
MVGKTILIVDDEAPIREMIAVALEMAGYECLEAENTQQAHAVIVDRKPDLILLDWMLPGTSGIELARRLKRDELTVDIPIIMLTAKGEEDNKIQGLEVGADDYITKPFSPRELVARLKAVLRRTGPGDSEAPIEVGGLLLDPISHRVTIDGKPAEMGPTEYRLLQFFMTHQERAYTRGQLLDQVWGGNVYVEERTVDVHIRRLRKALGEVYENLVQTVRGTGYRFSTKS
|
This protein is a positive regulator for the phosphate regulon. Transcription of this operon is positively regulated by PhoB and PhoR when phosphate is limited.
|
P23620
|
Q8EHD3
|
UPPP1_SHEON
|
Undecaprenyl pyrophosphate phosphatase 1
|
Shewanella
|
MDTFQVIILALIQGLTEFLPISSSAHLILPAQLLGWEDQGLSFDVAVNTGSLFAVVIYFRHELWAMFKAWIASIVKGQHSDDSKLAWWIILATLPAVFFGFMAKDFIATHLRNTGVIAVTTVVFGLLLWWADKMSRHDLTIYQTGWRKALLIGFAQALALIPGTSRSGATMTAALMLGLSRDAAARFSFLMSVPVSLGAAILVGKDLAESPLPIDYQALTLGTVISFAAAYLCIHYFLKIISRMGMTPFVIYRLALGAVLCGFIFL
|
Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
|
Q8EHD3
|
O33406
|
MBHL_AFIC5
|
Membrane-bound hydrogenase large subunit
|
Afipia
|
MSVIQTPNGYKLDNSGRRVVVDPVTRIEGHMRCEVNVDSNNVIRNAVSTGTMWRGLEVILKGRDPRDAWAFVERICGVCTGCHALASVRAVENALDIRIPPNAHLIREIMAKVLQWHDHVVHFYHLHALDWVNPVNALKADPKATSELQQLVGPNHPMSSPGYFRDIQNRLKRFVESGELGIFKNGYWDNPAYKLSPEADLMATAHYLEALDIQKEIVKIHTIFGGKNPHPNFMVGGVPCAINMDGDLAAGAPLNMERLNFVRARIEEAYEFSKNVYIPDVIAIATFYKGWLYGGGLSATNVMDYGDYAKVNYDKSTDQLKGGAILNGNWNEVFPVDAADPEQIQEFVAHSWYKYPDEAKGLHPWDGVTEHNYALGPNTKGTRTDIKQLDEAAKYSWIKSPRWRGHAVEVGPLSRYILNYAQGNQYVIEQVDSSLAAFNKLAGTNLTPKQALPSTIGRTLARALEAHYCAAMMLDDWKELIGNIKAGDSSTANVEKWDPSTWPKEAKGYGLVAAPRGANGHWIRIKDGKIANYQCIVPTTWNGSPRDPAGNIGAFEASLMNTPMERPEEPVEILRTLHSFDPCLACSTHVMSEDGENLAKVTVR
|
This enzyme recycles the H(2) produced by nitrogenase to increase the production of ATP and to protect nitrogenase against inhibition or damage by O(2) under carbon- or phosphate-limited conditions.
|
O33406
|
Q8D3J7
|
ATPF_WIGBR
|
F-type ATPase subunit b
|
Wigglesworthia
|
MNINATIFGQTIAFFLFVFFCMKYIWPNLISLVEKRRENIAQALNEAKQAKLNLKISKEKAKKRIESAQIKCKNIINEANETKKLLIEEAKKEAIKIKEHIISQGRLDILDEKKRMCEDLKTKISEIIVMSVEKIIESSINKKISDNIIERSISKINKIKG
|
Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
|
Q8D3J7
|
Q61249
|
IGBP1_MOUSE
|
p52
|
Mus
|
MAASEDELLLPRLPELFETSKKLLEDVEVATEPTGSRTIQDKVSKGLELLEKAAGMLSQLDLFSRNEDLEEIASTDLKYLMVPALQGALTMKQVNPSKRLDHLQRAREHFVHFLTQCHCYHVAEFQLPQTKTNSAENNTASSSMAYPNLVAMASQRQAKIERYKQKKEVEHRLSALKSAVESGQADDERVREYHLLHLRRWIAVSLEELESIDQEIKILKEKDSPREETACHSSLPEKPPMKPFILTRNKAQAKVFGTGYPSLATMTVSDWYEQHQKYGVLPDRGIAKPASADFQRAAQQQEDQEQKDEESEEKALHRMREWDDWKDTHPRGYGNRQNMG
|
Associated to surface IgM-receptor; may be involved in signal transduction. Involved in regulation of the catalytic activity of the phosphatases PP2A, PP4 and PP6 by protecting their partially folded catalytic subunits from degradative polyubiquitination until they associate with regulatory subunits.
|
Q61249
|
Q04K71
|
GUAC_STRP2
|
Guanosine 5'-monophosphate oxidoreductase
|
Streptococcus
|
MLNEFPIFDYEDIQLIPNKCVIKSRAEADTSVTLGNHTFKLPVVPANMQTILDENVAEQLAKGGYFYIMHRFDEAGRIPFIKRMHDQGLIASISVGVKDYEYDFVSQLKADAPEYITIDIAHGHADSVISMIQHIKKELPDTFVIAGNVGTPEAVRELENAGADATKVGIGPGKVCITKVKTGFGTGGWQLAALRWCAKAARKPIIADGGIRTHGDIAKSIRFGASMIMIGSLFAGHIESPGKTIEVDGEQFKEYYGSASQYQKGAYKNVEGKRILLPAKGHLQDTLTEMEQDLQSAISYAGGRQVADLKHVDYVIVKNSIWNGDASH
|
Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides.
|
Q04K71
|
Q1GBL8
|
RL3_LACDA
|
50S ribosomal protein L3
|
Lactobacillus
|
MTKGILGRKVGMTQIFTKDGVLVPVTVIEATPNVVMQVKTVENDGYEAVQLGYQDKREVLSNKPEKGHADKAKTSPKRFIRELRGVELSDYEVGSEVTVETFKEGDVVNVTGTSRGHGYQGNIKRHHQSRGPETHGSRYHRIPGSMGSIINRVPKGKKLPGHMGVKTVTIENLVVEKVVADKNVLMIKGNVPGAKNSLIVVKSSAKASK
|
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.
|
Q1GBL8
|
B2VEK6
|
ASTB_ERWT9
|
N-succinylarginine dihydrolase
|
Erwinia
|
MSAREVNFDGLPGLTHHYAGLSFGNEASARHQHQVSNPKLAALQGLKKMKTLADLGYAQGVIPPHERPNIEALRQLGFSGSDAQVLAQAAKQAPKLLSAVSSASAMWVANAATVSPSVDSRDGRVHLTVANLNNKYHRSIEAPTTAALLRAIFRDDEHFSVHDALPQVALFGDEGAANHNRFSNGYGEPGVQLFVYGCAQAGGIRPLHYPARQTREASEAVARLNQLDAARTLYAQQDPVVIDAGVFHNDVIAVSNQQTLFCHQRAFLNQPQLMARLAQKVPGFNLIEVPDERVSVADAVATYLFNSQLLSKDNGKMLLILPEEARRHAGVWRWLTEMVAGDGTIDELKVLDLRESMCNGGGPACLRLRVVLNAQQQAAVNPAVMMNETLYATLCGWVERHYRDRLSQADLADPQLLSEGREALDELTKLLDLGHVYRFQQ
|
Catalyzes the hydrolysis of N(2)-succinylarginine into N(2)-succinylornithine, ammonia and CO(2).
|
B2VEK6
|
B4TMY9
|
TORD_SALSV
|
Chaperone protein TorD
|
Salmonella
|
MNKQPALAQEQYACVYAWLALLFFREVDDEGLIQLQSAEIADWLALLKRQPALAASVALLEQKIAALSLRQDAQLELAADFCGLFLMTDKKSALPYASQYPQQEPGMIKHLLLEAGMEVNDDFKEPTDHLAIYLELLSHLHFSLGESFQQRRMNKLRQKTLSSLLEWLPEFTNNCFKHDSYGFYAALSQLLLAIVRFDDGKEDLSIVAAE
|
Involved in the biogenesis of TorA. Acts on TorA before the insertion of the molybdenum cofactor and, as a result, probably favors a conformation of the apoenzyme that is competent for acquiring the cofactor.
|
B4TMY9
|
Q8RSW1
|
PSBL_SYNP2
|
Photosystem II reaction center protein L
|
unclassified Synechococcus
|
MERNQNPNRQPVELNRTSLYLGLLLIAVLGILFSSYFFN
|
One of the components of the core complex of photosystem II (PSII). 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. This subunit is found at the monomer-monomer interface and is required for correct PSII assembly and/or dimerization.
|
Q8RSW1
|
Q6PB90
|
PCDBE_MOUSE
|
Protocadherin beta-14
|
Mus
|
METSLHKAPQKRQVTAIIFLLLLWEAGSATITYSVLEETDRGSLVGNLAKDLGLSLRELITRGAQILSKGNKQLLQLEQKSGNLLLKEKLDREELCGSTNPCILHFQVLLKSPVQFIQGEIQLQDVNDHAPEFMEDEILLKILESSLPGAVFPLKIAQDLDVGSNTVQNYTISTNAHFHLLTRNHSDGRKYPELVLDKALDREEQAQIRLTLTAMDSGSPPKTGTTQVVIVVLDINDNAPEFAQGLYEVQVQENSPVGSLVLTVSARDLDAGTHGELSYSLFQSSNQVLQAFEVNTDTGEIRVRKLLDFEEIQSYRMEIEASDGGGLSGKCTVVIHVMDVNDNAPELTMSVLISEIPENSPETIVAIFGISDPDSGDNGKMVCSVQDRLPFLLKPNEENFYTLVTERALDRESRAEYNITITVSDMGTPRLTTQHTITVQVSDINDNAPAFTHTSYTMFVRENNSPALHIGTISATDSDSGSNAHITYSLLPPHDPQLALNSLISINADNGQLFALRALDYEALQAFEFHVGATDGGSPALSSQALVRVVVLDDNDNAPFVLYPMQNASAPCTELLPRAAEPGYLVTKVVAVDRDSGQNAWLSFQLLKTTEPGLFSVWAHNGEVRTTRLLSERDVPKHRLLLLVKDNGEPPHSASVTLHVLLVDGFSQPYLPLPEVARDPAQEDVLTLYLVIALASVSSLFLVSVLLFVGVRLCRKAGETSLGGCSVPEGHFPGHLVDVSGTGTLSQSYQYEVCLTGGTGTNEFKFLKPVLPNFLNEGGYRNTEENSNFRDSLGFS
|
Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.
|
Q6PB90
|
P08850
|
HBA_ACCGE
|
Hemoglobin alpha-A chain
|
Accipiter
|
MVLSANDKTNVKNVFTKIGGHAEEYGAETLERMFTTYPPTKTYFPHFDLHHGSAQIKAHGKKVVGALIEAVNHIDDIAGALSKLSDLHAQKLRVDPVNFKLLGQCFLVVVAIHHPSVLTPEVHASLDKFLCAVGNVLTAKYR
|
Involved in oxygen transport from the lung to the various peripheral tissues.
|
P08850
|
P61430
|
SYCP2_ARATH
|
Synaptonemal complex central region protein ZYP1b
|
Arabidopsis
|
MQKLGFPAMKSFDQLRSLPGSAKTYFFSTRPPQDSVSSGSFSNLKLTAEKLVKDQAAMRTDLELANCKLKKSMEHVYALEEKLQSAFNENAKLRVRQKEDEKLWRGLESKFSSTKTLCDQLTETLQHLASQVQDAEKDKGFFETKFNTSSEAINSLNQQMRDMSLRLDAAKEEITSRDKELEELKLEKQHKEMFYQTERCGTASLIEKKDAVITELETTAAERKLKIEKLNSQLEKLHLELTTKEDEVIHLVSIQEKLEKEKTNVQLSSDELFEKLVRSEQEVKKLDELVHYLIAELTELDKKNLTFKEKFDKLSGLYDTHFMLLRKDRDLASDRAQRSFDQLQGELFRVAAEKEALESSGNELSEKIVELQNDKESLISQLSGVRCSASQTIDKLEFEAKGLVLKNAETESVISKLKEEIDTLLESVRTSEDKKKELSIKLSSLEIESKDKYEKLQADAQRQVGELETLQKESESHQLQADLLAKEVNQLQTIIEEKGHLILQCNENEKNINQQIIKDKELLATAETKLAEAKKQYDLMLESKQLELSRHLKELSQRNDQAINEIRRKYDVEKHEIINSEKDKVEKIIKELSTKYDKGLSDCKEESKRQLLTIQEEHSSRILNIREEHESKELNLKAKYDQELRQNQIQAENELKERITALKSEHDAQLKAFKCQYEDDCKKLQEELDLQRKKEERQRALVQLQWKVMSDNPPEEQEVNSNKDYSHSSVKVKESRLGGNKRSEHITESPFVKAKVTSVSNILKEATNPKHHSKVTHREYEVETNNGRIPKRRKTRQTTMFQEPQRRSTRLTPKLMTPTIIAKETAMADHPHSANIGDLFSEGSLNPYADDPYAFD
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Required for chromosome synapsis and normal fidelity of crossing over.
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P61430
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Q6AYP0
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ALLC_RAT
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Allantoate amidinohydrolase
|
Rattus
|
MADTPKEGKLTRFLDFTQLIDLASECVGGKVLFATDDFFGPAENLIKSNNPSFKENEYTEFGKWVDGWETRRKRIPGHDWCVIQLGIQGIIRGIDVDISYFSGNYAPRMSIQAANLSEDTVTNIPPRGVKMGAAATSEEFVAITELKSHSWDYLVPMSELKPGDPDSSHNYFFVNSQQRWTHIRLNIFPDGGVARLRVYGTGQRDWAALDSTEPVDLVAIAFGGVCVGFSNAHFGHPNNMIGVGDPKSIADGWETARRLDRPPVLEGNENGFLQVPGCEWAVFRLAHPGVITQIEIDTKYFKGNSPDSCKVDGCILTTLEEEDMIRQKWSLPAHKWKPLLPVTKLTPNQNHLLDSLTLELQDVITHARITIAPDGGVSRLRLKGFPSSICLLRPLREKPMLRFSLKAGFRANL
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The function of this enzyme is unclear as allantoicase activity is not known to exist in mammals.
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Q6AYP0
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P52803
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EFNA5_HUMAN
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EPH-related receptor tyrosine kinase ligand 7
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Homo
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MLHVEMLTLVFLVLWMCVFSQDPGSKAVADRYAVYWNSSNPRFQRGDYHIDVCINDYLDVFCPHYEDSVPEDKTERYVLYMVNFDGYSACDHTSKGFKRWECNRPHSPNGPLKFSEKFQLFTPFSLGFEFRPGREYFYISSAIPDNGRRSCLKLKVFVRPTNSCMKTIGVHDRVFDVNDKVENSLEPADDTVHESAEPSRGENAAQTPRIPSRLLAILLFLLAMLLTL
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Cell surface GPI-bound ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Induces compartmentalized signaling within a caveolae-like membrane microdomain when bound to the extracellular domain of its cognate receptor. This signaling event requires the activity of the Fyn tyrosine kinase. Activates the EPHA3 receptor to regulate cell-cell adhesion and cytoskeletal organization. With the receptor EPHA2 may regulate lens fiber cells shape and interactions and be important for lens transparency maintenance. May function actively to stimulate axon fasciculation. The interaction of EFNA5 with EPHA5 also mediates communication between pancreatic islet cells to regulate glucose-stimulated insulin secretion. Cognate/functional ligand for EPHA7, their interaction regulates brain development modulating cell-cell adhesion and repulsion.
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P52803
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A9A2G6
|
HPCAL_NITMS
|
3-hydroxypropionyl-coenzyme A synthetase [ADP-forming]
|
Nitrosopumilus
|
MAAVKKIFDEIIETDHKVITEESSKSILKNYGVKVPPYALVTSAEEAAKEAKKIGFPLVMKVVSPQILHKTDVGGVKVGLDNVADVKKTFTDMYGRLSKKKGVNVKGILLEKMVPKGVELIVGIQNDSQFGPIIMVGMGGIMTEVMKDVAFRMLPITTSDAKSMLNELKGSKLLKGFRGSEPIDTNLVAKMLVNIGKLGVENADYINSIDFNPVIVYPKSHYVVDAKIILNKEKKKNSISKAKPSITDMETFFTPKSVALVGASASPGKIGNSILDSLVNYDFKGKVYPINPKADKIFGQKCYPSVADIPGKVDLVVVSVDLSMTPPVLEDCAKKGVHSVVIVSGGGKELGGERAAYEAEVARLSKKHKIRIIGPNCIGMFNAANRLDCAFQGQERMVRSKLGPVAFFSQSGTMGISMLESADTFGLSKMISFGNRSDVDEADMIWYAANDPQTKVIGLYVEGFGDGRKFINVAKRVMKEKKKPIVIWKSGRTAAGAKQAASHTGSLGGSNAIIMGAFKQAGIISVDSYQELAGVLKALAWQPAAKGNKVAMTSNGAGPMIGGIDQLEKFGLAIGKLSPKLLKKMKSRFPPAVPIHNGNPADVGGGATADDYQFVIQQFMDEKNIDIAMPWFVFQDDPLEETIVDHLAGFQKKAKKPLLCGGNGGPYTEKMIKLIEKHNVPVYQDLRTWVAAASALHQWGKISKK
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Involved in thaumarchaeal hydroxypropionate/hydroxybutyrate (HP/HB) cycle, a modified version of the autotrophic HP/HB cycle of Crenarchaeota. Catalyzes the formation of 3-hydroxypropionyl-CoA, ADP and phosphate from 3-hydroxypropionate, coenzyme A (CoA) and ATP. Can also use 4-hydroxybutyrate, propionate and butyrate, with poor catalytic efficiency.
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A9A2G6
|
P0A3S0
|
NCZS_STRML
|
Mitomalcin
|
Streptomyces
|
AAPTATVTPSSGLSDGTVVKVAGAGLQAGTAYDVGQCAWVDTGVLACNPADFSSVTADANGSASTSLTVRRSFEGFLFDGTRWGTVDCTTAACQVGLSDAAGNGPEGVAISFN
|
NCS has antibiotic activity (for Gram-positive bacteria) and antitumor activity (for certain mouse tumors). NCS binds non-covalently to a chromophore which is the cytotoxic and mutagenic component of the antibiotic. The chromophore binds to DNA as a weak intercalator and causes single- and double-strand breaks.
|
P0A3S0
|
P29754
|
AGTRA_MOUSE
|
Angiotensin II type-1 receptor A
|
Mus
|
MALNSSTEDGIKRIQDDCPRAGRHSYIFVMIPTLYSIIFVVGIFGNSLVVIVIYFYMKLKTVASVFLLNLALADLCFLLTLPLWAVYTAMEYRWPFGNHLCKIASASVSFNLYASVFLLTCLSIDRYLAIVHPMKSRLRRTMLVAKVTCIIIWLMAGLASLPAVIHRNVYFIENTNITVCAFHYESRNSTLPIGLGLTKNILGFLFPFLIILTSYTLIWKALKKAYEIQKNKPRNDDIFRIIMAIVLFFFFSWVPHQIFTFLDVLIQLGVIHDCKIADIVDTAMPITICIAYFNNCLNPLFYGFLGKKFKKYFLQLLKYIPPKAKSHSSLSTKMSTLSYRPSDNMSSAAKKPASCSEVE
|
Receptor for angiotensin II, a vasoconstricting peptide, which acts as a key regulator of blood pressure and sodium retention by the kidney. The activated receptor in turn couples to G-alpha proteins G(q) (GNAQ, GNA11, GNA14 or GNA15) and thus activates phospholipase C and increases the cytosolic Ca(2+) concentrations, which in turn triggers cellular responses such as stimulation of protein kinase C.
|
P29754
|
A9BTA2
|
RPOZ_DELAS
|
Transcriptase subunit omega
|
Delftia
|
MARITVEDCLEQIPNRFQLVLAATYRARMLSQGHTPRIETKNKPGVTALREIAEGKVGLEMLKKVPG
|
Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
|
A9BTA2
|
Q92NM8
|
DNLJ_RHIME
|
Polydeoxyribonucleotide synthase [NAD(+)]
|
Sinorhizobium
|
MLNQRKSVEQLNEAEAAEELAFLAAELARHDMLYHGKDAPEISDADYDALKRRNDLIEERFPVLVREDSPSRKVGAAPSLTFAPVVHARPMLSLDNTFSDEDARAFVAGVYRFLGKLPDGSIAFTAEPKIDGLSMSLRYENRRLVTAATRGDGTTGENVTANVRTIGMIPQTLPADAPDVVEIRGEIYMAKSDFAALNAEMAAQGRPLYVNPRNTASGSLRQLDAKVTANRKLRFFAYAWGEMSAMPADTQLGMVETFKAWGFPVNPLMQRFFSADELLEHYHHIERERPDLDYDIDGVVYKVDRLDLQARLGFRSRSPRWATAHKFPAEQAFTRLKGIDIQVGRTGALTPVARLEPITVGGVVVTNATLHNEDYIRGVGNTGEPIRDGRDVRIGDMVIVQRAGDVIPQIVDVVMDERPEGAEPYRFPTTCPICGSHAVRDINEKTGKVDAVRRCTGGFVCRAQAVEHLKHFVSRNAFDIEGLGSKQIEFFFESEDENLRIRTAPEIFTLERRQEASLNKLENTDGFGKVSVRKLYEAINARRSIALHRLIYALGIRHVGETTAKLLARSYGSYEHFGAAMTEAAGFSGDAWNELNSIDGIGEVVARAIVEFYKEPRNLKVVSELLQEVTPESAELPVATDSPVAGKTVVFTGSLEKMTREEAKAKAESLGAKVAGSVSKKTDIVVAGPGAGSKLDKARELGVQTMDEDEWLALIGG
|
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.
|
Q92NM8
|
P50864
|
CWLD_BACSU
|
Cell wall hydrolase
|
Bacillus
|
MRKKLKWLSFLLGFIILLFLFKYQFSNNDSWKPWSLPLSGKIIYLDPGHGGPDGGAVGGKLLEKDVTLEVAFRVRDYLQEQGALVIMTRESDTDLAPEGTKGYSRRKAEDLRQRVKLINHSEAELYISIHLNAIPSQKWSGAQSFYYGKYAENEKVAKYIQDELRRNLENTTRKAKRIHGIYLMQNVTKPGALIEVGFLSNPSEATLLGKPKYQDKVASSIYKGILRYFTEKGDPPE
|
Cleaves the peptide side chain from the N-acetylmuramic acid residues in peptidoglycan. This is a step in the formation of muramic delta-lactam residues in spore cortex.
|
P50864
|
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