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
|
|---|---|---|---|---|---|---|
B2TZB5
|
DADA_SHIB3
|
D-amino acid dehydrogenase
|
Shigella
|
MRVVILGSGVVGVASAWYLNQAGHEVTVIDREPGAALETSAANAGQISPGYAAPWAAPGVPLKAIKWMFQRHAPLAVRLDGTQFQLKWMWQMLRNCDTSHYMENKGRMVRLAEYSRDCLKALRAETNIQYEGRQGGTLQLFRTEQQYENATRDIVVLEDAGVPYQLLESSRLAEVEPALAEVAHKLTGGLQLPNDETGDCQLFTQNLARMAEQAGVKFRFNTPVDQLLCDGEQIYGVKCGDEVIKADAYVMAFGSYSTAMLKGIVDIPVYPLKGYSLTIPIAQEDGAPVSTILDETYKIAITRFDNRIRVGGMAEIVGFNTELLQPRRETLEMVVRDLYPRGGHVEQATFWTGLRPMTPDGTPVVGRTRFKNLWLNTGHGTLGWTMACGSGQLLSDLLSGRTPAIPYEDLSVARYSRGFTPSRPGHLHGAHS
|
Oxidative deamination of D-amino acids.
|
B2TZB5
|
B1W447
|
RL11_STRGG
|
50S ribosomal protein L11
|
Streptomyces
|
MPPKKKKVTGLIKLQINAGAANPAPPVGPALGQHGVNIMEFCKAYNAATESQRGMVVPVEITVYEDRSFTFVTKTPPAAKLILKAAGVDKGSGEPHKTKVAKLTAAQVREIATTKLPDLNANDLDAASKIIAGTARSMGITVEG
|
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
|
B1W447
|
Q9ZKW2
|
Y889_HELPJ
|
Probable iron chelatin transport system permease protein jhp_0822
|
Helicobacter
|
MLKTYHIALACVILAVVVLLFGGESLSLEEWQEVCLNVKNHFLHNEELSSLSVIILEIRLPRVILALLVGASLSGSGVVMQTILRNPLVDPFLLGISSGAMLGVAMAIAVVESNIAILAFFGAILPSLAVLAMNRVLGNSVLSLVLSGVVLSAFLSALAGAIKFFVIPQKAQAIVVWLLGSLSLSSYKDCLIAFIGLSLGFIPLFLLRWRINLLSLSDAQSLSLGINPVLLRSLCLVCVSVASALAVSVSGTIGWIGLVIPHVARLFFGANLQKLLLSSLLMGAFFLLLADVVAKTITPYDLPVGIATSVLGAPFFLWLLFRTRGV
|
Part of a binding-protein-dependent transport system for an iron chelatin; probably responsible for the translocation of the substrate across the membrane.
|
Q9ZKW2
|
Q1ML15
|
RLME_RHIL3
|
rRNA (uridine-2'-O-)-methyltransferase
|
Rhizobium
|
MTKAPIAGNRTGRKLGQRVKNKKMKASSRQWLERHINDPYVQRAQLEGYRARAAFKLLEIDEKHHILRGARRIIDLGAAPGSWSQIAAKVTGSTDDDIRVAAIDFLEMTQLPGVKILQLDFLDPSAPEKLLEAVGGTPDLVISDMAAPTTGHHRTDHLRTMHLCEVAAHFAVEVLGEGGHFLTKTFQGGTERELLAMLKQNFRQVVHVKPNSSRAESVEMFLLAKGFKGRKAEGEAEEA
|
Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit.
|
Q1ML15
|
P28411
|
RBL_DRORE
|
Ribulose bisphosphate carboxylase large chain
|
Drosera
|
NVGFKAGVKEYKLTYYTPDYETLDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTNLDRYKGRCYHIEPVAGEENQYIVYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRVLRLEDLRIPPAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFVFCVEAIYKAQAETGEIKGHYLNATAGTSEEMIKRAVFARELGVPIVMHDYLTGGFTANTSLSHYCRDNGLLLHIHRAMHAVIDRQKNHGIHFRVLAKALRMSGGDHIHSGTVVGKLEGERDITLGFVVLLRDDYIEKDRSRGIYFTQPWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLAREGNEIIRKASKWSPELAAACEVWKEIKFEFQAMDTL
|
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.
|
P28411
|
Q3K731
|
GMHA_PSEPF
|
Sedoheptulose 7-phosphate isomerase
|
Pseudomonas
|
MDMQSRIRQLFQASIDTKQQAMDVLAPHIEQASQVMVNALLNEGKMLSCGNGGSAGDAQHFSSELLNRFERERPSLPAIALTTDSSTITSIANDYSYNEVFSKQIRALGQPGDVLLAISTSGNSANIIQAIQAAHDREMIVVALTGRDGGGMASLLLPEDVEIRVPANVTARIQEVHLLAIHCLCDLIDSQLFGSEE
|
Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate.
|
Q3K731
|
Q84T61
|
HSFA1_ORYSJ
|
Heat stress transcription factor 3
|
Oryza sativa
|
MEAAVAAAAAAAGAVTTAVAPPPGAAVSNGVATAPPPFLMKTYEMVDDPATDAVVSWGPGNNSFVVWNTPEFARDLLPKYFKHSNFSSFVRQLNTYGFRKVDPDRWEFANEGFLRGQKHLLKTINRRKPTHGNNQVQQPQLPAAPVPACVEVGKFGMEEEIEMLKRDKNVLMQELVRLRQQQQTTDHQLQTLGKRLQGMEQRQQQMMSFLAKAMHSPGFLAQFVQQNENSRRRIVASNKKRRLPKQDGSLDSESASLDGQIVKYQPMINEAAKAMLRKILKLDSSHRFESMGNSDNFLLENYMPNGQGLDSSSSTRNSGVTLAEVPANSGLPYVATSSGLSAICSTSTPQIQCPVVLDNGIPKEVPNMSAVPSVPKAVAPGPTDINILEFPDLQDIVAEENVDIPGGGFEMPGPEGVFSLPEEGDDSVPIETDEILYNDDTQKLPAIIDSFWEQFLVASPLSVDNDEVDSGVLDQKETQQGNGWTKAENMANLTEQMGLLSSHHTG
|
Transcriptional regulator that specifically binds DNA of heat shock promoter elements (HSE).
|
Q84T61
|
Q33C52
|
ATPF_NICTO
|
ATPase subunit I
|
Nicotiana
|
MKNVTDSFVSLGHWPSAGSFGFNTDILATNPINLSVVLGVLIFFGKGVLSDLLDNRKQRILNTIQNSEELRGGAIEQLEKARSRLRKVETEAEQFRVNGYSEIEREKLNLINSTYKTLEQLENYKNETIQFEQQRAINQVRQRVFQQVLRGALGTLNSCLNNELHLRTISANIGMLGTMKEITD
|
Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
|
Q33C52
|
P14215
|
PPM1_LIMPO
|
Polyphemusin I
|
Limulus
|
RRWCFRVCYRGFCYRKCR
|
Significantly inhibits the growth of Gram-negative and Gram-positive bacteria.
|
P14215
|
A7I1R8
|
SYP_CAMHC
|
Prolyl-tRNA synthetase
|
Campylobacter
|
MKFSKFFAPTLKEAPKDAILPSHVFLIRAGFIEQLGSGLYNFLPLGEMVIEKIKAVIKDEMDKTGALQVNFSFVTPSEFWQESGRYNVYGKELLRIKDRKENGFVLSPTNEESSVKMIANKITSYKQLPIHIYQINTKFRDEARPRFGLLRGREFIMKDGYSFHANMEDLKREFDVMEKTYTNIFSRLGLNFRAVEADSGAIGGSGSKEFMVLAQNGEDDILVCESCKYAANIEAAVRVKREAPCAAPETEKMQKFHTPNMKTIDDVANFFKVDKFFTVKAVIKKAVFVDKSEIVLFFVRGDDELQETKALNACGALEFEDASEDEIKKAGLIAGFCGPAGLPDDINFYIDKELKNERNLIVGANEKDYHIVGFAVTNFKDERFVDLSQVRAGDCCPKCGAKLDIKKGIEVGHIFQLGQKYSKAMNAIFLDENGKAVPFFMGCYGIGVSRLLAVMIEAGHDEKGCIWNTQTAPFKLEIIISNSKDEDASNFAIQLYEKCKNAGISTLLDDRKERFGVKMNDFELIGFPFAVLVGKGLKDGNVELIERKGLNKKIVSSGEIFETLKGILC
|
Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS.
|
A7I1R8
|
Q54305
|
RAPK_STRRN
|
Chorismatase
|
Streptomyces violaceusniger group
|
MTPPVTAPYCRFEKLGASDLDGDETLLGVIEHRTGHTGVSLAEGCPRTAVHTTTREDESFAEAWHAEGPKESGSHDGVAWARTPDYLFGVARVPEGGRYAAGTAAVYTGIFDLIGTLGYPSLARTWNYVSGINTPNADGLEVYRDFCVGRAEALDARGIDPATMPAATGIGAHGGGITCYFIAARAGDRVNMENPAVLTAHRYPQRYGPRPPVFSRATWLSPPGADDGRLFVSATAGIVGHETVHHGDVAAQCEVSLENIARVIGAENLGRHGLRRGYALADVDHLKVYVRHREDISTVRRICAERLSREATVAVLHTDIARTDLLVEIEGVVA
|
Involved in the biosynthesis of the macrocyclic amino acid-linked polyketides rapamycin which is a potent immunosuppressant that prevents T-cell proliferation through initial binding to the immunophilin FKBP12. Catalyzes the hydrolysis of chorismate via a 1,4-conjugate elimination of water to yield (4R,5R)-4,5-dihydroxycyclohexa-1,5-dienecarboxylic acid (DCDC).
|
Q54305
|
Q9Y800
|
MUG97_SCHPO
|
Meiotic expression up-regulated protein 33
|
Schizosaccharomyces
|
MSILNSGSCMMTDTNQNMECKVDFKKGEFDLQPLQINQFGFTKTQLHKPLTRNLSNKEDTHVPKRQKVSEPYFRGETERNVKSHQDRAASIYHEAMNGASGIHKQMSLPEYSPQMGNSWEIQVPMTTRHSISETPTKPFTATTAIAGSAGSLPRNTTIGLPGPSALLKHESGKNENQVRVCLYHKHYSRWYLPFDKDDDNQLVEAYAKYFSSENRPSIFYVLQGISFGPECEYVLRRKHWWNPWAEKVMRREIVERKIDTHPGCRTVAERYEQIEASGSEELLIIPIYKINMWVLSLLLFSAGGSVLIGLWMRLSDPSFAHGMLLNLGIGSIGSFLYLLSNTWCR
|
Required for correct meiotic chromosome segregation. Appears to also have role in sporulation.
|
Q9Y800
|
Q6D654
|
BTUD_PECAS
|
Vitamin B12-transporting ATPase
|
Pectobacterium
|
MQLRQASVLPRLSPTNAECRPGELLHIIGPNGAGKSTLLARAAGLLAGEGEVYLAGTPLSQYTAADLAVRRAYLAQQQPPLALMPVFQYWQRHQPPLAQEYAVEKVVHFLAERLMLTDKLARPLTQLSGGEWQRVRLVAALLQIWPTINPHARLLLLDEPTNSLDVAQQVALDSLLSELCRLGIAVVVCAHDLNHSAHHADRVWLLSAGVLVAQGETEDVMLPEVLSPVFGVAFQRHVVDGRNWIITRSA
|
Part of the ABC transporter complex BtuCDF involved in vitamin B12 import. Responsible for energy coupling to the transport system.
|
Q6D654
|
A1SSQ6
|
PYRG_PSYIN
|
UTP--ammonia ligase
|
Psychromonas
|
MTTKYIFVTGGVVSSLGKGIAAGSLAAILEARGLDVTILKLDPYINVDPGTMSPIQHGEVFVTDDGAETDLDLGHYERYIRTRMTARNNFTTGRVYSEVMAKERRGDYLGATIQVIPHITNEIQERIVAGGKGHDIAIVELGGTVGDIESQPFLEAIRQLGLKVGRDSVIYMHLTLLPYLKTAGEVKTKPTQHSVKELRSLGIQPDILVCRSEVNIPINERVKIALFCNVTEKSVILLRDVDSIYKIPALLKAQGLDEICVKRFGLDCPEADLSEWAQVVSEEANTSNEVIIGMVGKYTELPDAYKSVNEALKHGGLKNAASVKIKYIDSQDVEVRGVSILEGVDAILVPGGFGERGIEGKILAAQYARVNKIPYLGICLGMQVAIIEFARNVAGLKNAHSTEFEANCDQPVVGLITEWLDKTGEVEQRTENSDLGGTMRVGAQLCHLKKGSKVFDMYGTKEIFERHRHRYEVNNNLLPILEKAGLVVTGLSEDKKLVEIIEIPNHPWFVASQFHPEFTSTPRDGHPLFKGFIKSAIDHQQGRFE
|
Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.
|
A1SSQ6
|
Q8DKF0
|
LEUC_THEVB
|
Isopropylmalate isomerase
|
Thermosynechococcus
|
MSMSRGTLFDKVWEQHTVATLPSGQTQLFIGLHLIHEVTSPQAFAMLRERGLPVLYPQRTIATVDHIVPTDTLARPLQDALAEEMLQALEANCRAHNIPFFGIGSGRQGIVHVIAPEQGLTQPGMTIACGDSHTSTHGAFGAIAFGIGTSQVRDVLATQTLALNKLKVRKVEVNGSLAAGVYAKDVILHVIRHLGVKGGVGYAYEFAGTTFGQLSMEERMTVCNMAIEGGARCGYVNPDETTFAYLKGRPFAPQGKAWDEAVAWWRSLASDADAEYDDVVTFAAADIAPTVTWGITPGQSVAVDETLPTLESLPVAERAIAAEAYAYMDLQPGQPIQGTKIDVCFIGSCTNGRISDLRQAAKVVEGRKVKPGVKAFVVPGSERVKAQAEAEGLDVVFKAAGFEWRNPGCSMCLAMNPDKLQGRQISASSSNRNFKGRQGSPSGRTLLMSPAMVAAAAIAGEVTDVRAFL
|
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
|
Q8DKF0
|
Q8EQT9
|
RBFA_OCEIH
|
Ribosome-binding factor A
|
Oceanobacillus
|
MAELRAHRIAEQMKKELGEILSRKIKDPRVGFVTVTDVEVTGDLQQAKVYISVLGDEKKKQDTLLGLSKAKGFIRSEIGNRIRLRKTPEITFEFDEALEQGNRIETILRDLNK
|
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.
|
Q8EQT9
|
Q23361
|
ALG12_CAEEL
|
Mannosyltransferase ALG12 homolog
|
Caenorhabditis
|
MEGTEWIVIIVTIIHIILAPGTKVEESFNVQATHDLMFHLPTNLSNYDHSQFPGVVPRTFIGPISLAILSSPMSFIFRFWAIPKMWQLLLIRATLGLMNAMAFLYFARSVNRKFGRETAMYLRLIMCTQFHYIFYMSRPLPNTFALILVMIVFERLLEGRYESAVRYATASVILFRCELVLLYGPIFLGYMISGRLKVFGFDGAIAIGVRIAAMCLAVSIPIDSYFWGRPLWPEGEVMFFNVVENRSHEYGTQPFLWYFYSALPRCLLTTTLLVPLGLLVDRRLPQIVLPSVIFIFLYSFLPHKELRFIIYVLPIFCLSAAVFCARMLINRHKSFFRMILFFGVILHLLANVLCTGMFLLVASKNYPGFDALNYLQFQNRFDAKKPVTVYIDNACAQTGVNRFLHINDAWTYNKTENLKPADLENFDFLVLGTYGNTLKTEVESKFVTWHRPLFFVNSFHQYKIKKSRQFPWIYPEIIYTEKAVVLKNRNYK
|
Adds the eighth mannose residue in an alpha-1,6 linkage onto the dolichol-PP-oligosaccharide precursor (dolichol-PP-Man(7)GlcNAc(2)) required for protein glycosylation.
|
Q23361
|
P56780
|
PSBH_ARATH
|
Photosystem II 10 kDa phosphoprotein
|
Arabidopsis
|
MATQTVEDSSRSGPRSTTVGKLLKPLNSEYGKVAPGWGTTPLMGVAMALFAVFLSIILEIYNSSVLLDGISVN
|
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.
|
P56780
|
Q1MH39
|
LEXA_RHIL3
|
LexA repressor
|
Rhizobium
|
MLTRKQQELLLFIHERMKESGVPPSFDEMKDALDLASKSGIHRLITALEERGFIRRLPNRARALEVIKLPEAYSPSIQPRRGFSPSVIEGSLGKPQPVATPAPAKSVADNGNSVSVPVMGRIAAGVPISAIQNNTHDIVVPADMLGSGEHYALEVKGDSMIDAGIFDGDTVIIRNGSTASPGDIVVALVDDEEATLKRFRRKGASIALEAANPAYETRIFGPDRVKVQGKLVGLIRRYH
|
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
|
Q1MH39
|
A4TC20
|
Y3714_MYCGI
|
Nucleotide-binding protein Mflv_3714
|
Mycolicibacterium
|
MTRQGMRDDLRGEADSVVHDGTDDIDNENDIDNGIDNENGNGIDVVLVTGLSGAGRGTAAKVLEDLGWYVADNLPPELIAQMVDLGLAAGSRITQLAAVMDVRSRGFTGDLDWVRSELATRNIVPRVVFLEASDDILVRRYEQNRRSHPLQGNQTLAEGIAAERAMLAPVRASADLVIDTSALSVHGLRDSIERAFAAETVAHTNVTVESFGYKYGLPMDADTVMDVRFLPNPHWIDRLRPHTGQNADVRDYVLGQPGADEFLDSYHQLLNVVIDGYRREGKRYMTVAIGCTGGKHRSVAMAEALAARLAGSDALTVRVLHRDLGRE
|
Displays ATPase and GTPase activities.
|
A4TC20
|
B0KK60
|
RPOB_PSEPG
|
Transcriptase subunit beta
|
Pseudomonas
|
MAYSYTEKKRIRKDFSKLPDVMDVPYLLAIQLDSYREFLQAGASKDHFRDVGLHAAFKSVFPIISYSGNAALEYVGYRLGEPAFDVKECVLRGVTFAVPLRVKVRLIIFDKESSNKAIKDIKEQEVYMGEIPLMTENGTFVINGTERVIVSQLHRSPGVFFDHDRGKTHSSGKLLYSARIIPYRGSWLDFEFDPKDCVFVRIDRRRKLPASVLLRALGYSTEEVLNTFYTTNVFHISGEKLSLELVPQRLRGEVAVMDIHDETGKVIVEQGRRITARHINQLEKAGVKQLDVPMEYVLGRTTAKAIVHPATGEILAECNTEMTTELLIKVAKAQVVRIETLYTNDIDCGPFISDTLKIDTTSNQLEALVEIYRMMRPGEPPTKDAAETLFNNLFFSAERYDLSAVGRMKFNRRIGRTEIEGSGVLSKEDIVEVLKTLVDIRNGKGIVDDIDHLGNRRVRCVGEMAENQFRVGLVRVERAVKERLSMAESEGLMPQDLINAKPVAAAVKEFFGSSQLSQFMDQNNPLSEITHKRRVSALGPGGLTRERAGFEVRDVHPTHYGRVCPIETPEGPNIGLINSLAAYARTNQYGFLESPYRVVKEGVVSDDIVFLSAIEEADHVIAQASAAMNEKKQLIDELVAVRHLNEFTVKAPEDVTLMDVSPKQVVSVAASLIPFLEHDDANRALMGSNMQRQAVPTLRADKPLVGTGMERNVARDSGVCVVARRGGVIDSVDASRIVVRVNDDEVETGEAGVDIYNLTKYTRSNQNTCINQRPLVSKGDKVQRSDIMADGPSTDMGELALGQNMRIAFMAWNGFNFEDSICLSERVVQEDRFTTIHIQELTCVARDTKLGPEEITADIPNVGEAALNKLDEAGIVYVGAEVGAGDILVGKVTPKGETQLTPEEKLLRAIFGEKASDVKDTSLRVPTGTKGTVIDVQVFTRDGVERDSRALAIEKMQLDEIRKDLNEEFRIVEGATFERLRSALNGQVVDGGAGLKKGTVITDEVLDGLEHGQWFKLRMAEDALNEQLEKAQQYIVDRRRLLDDKFEDKKRKLQQGDDLAPGVLKIVKVYLAIRRRIQPGDKMAGRHGNKGVVSVIMPVEDMPHDANGTPVDVVLNPLGVPSRMNVGQILETHLGLAAKGLGEKIDRMLEEQRKAAELRVFLTEVYNEIGGRQENLDEFTDEEILALANNLKKGVPMATPVFDGAKEREIKAMLKLADLPESGQMVLFDGRTGNKFERPVTVGYMYMLKLNHLVDDKMHARSTGSYSLVTQQPLGGKAQFGGQRFGEMEVWALEAYGAAYTLQEMLTVKSDDVNGRTKMYKNIVDGDHRMEPGMPESFNVLIKEIRSLGIDIDLETE
|
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
|
B0KK60
|
O55164
|
MPDZ_RAT
|
Multi-PDZ domain protein 1
|
Rattus
|
MLETIDKNRALQAAERLQSKLKERGDVANEDKLSLLKSVLQSPLFSQILSLQTSLQQLKDQVNVATLATANADHAHTPQFSSAIISNLQSESLLLSPSNGNLEAISGPGAPPAMDGKPACEELDQLIKSMAQGRHVEIFELLKPPCGGLGFSVVGLRSENRGELGIFVQEIQEGSVAHRDGRLKETDQILAINGQVLDQTITHQQAISILQKAKDTIQLVIARGSLPHISSPRISRSPSAASTVSAHSNPTHWQHVETIELVNDGSGLGFGIIGGKATGVIVKTILPGGVADQHGRLCSGDHILKIGDTDLAGMSSEQVAQVLRQCGNRVKLMIARGAVEETPAPSSLGITLSSSTSTSEMRVDASTQKNEESETFDVELTKNVQGLGITIAGYIGDKKLEPSGIFVKSITKSSAVELDGRIQIGDQIVAVDGTNLQGFTNQQAVEVLRHTGQTVRLTLMRKGASQEAEITSREDTAKDVDLPAENYEKDEESLSLKRSTSILPIEEEGYPLLSTELEETEDVQQEAALLTKWQRIMGINYEIVVAHVSKFSENSGLGISLEATVGHHFIRSVLPEGPVGHSGKLFSGDELLEVNGINLLGENHQDVVNILKELPIDVTMVCCRRTVPPTALSEVDSLDIHDLELTEKPHIDLGEFIGSSETEDPMLAMSDVDQNAEEIQTPLAMWEAGIQAIELEKGSRGLGFSILDYQDPIDPANTVIVIRSLVPGGIAEKDGRLFPGDRLMFVNDINLENSTLEEAVEALKGAPSGMVRIGVAKPLPLSPEEGYVSAKEDTFLCSPHTCKEMGLSDKALFRADLALIDTPDAESVAESRFESQFSPDNDSVYSTQASVLSLHDGACSDGMNYGPSLPSSPPKDVTNSSDLVLGLHLSLEELYTQNLLQRQHAGSPPTDMSPAATSGFTVSDYTPANAVEQKYECANTVAWTPSQLPSGLSTTELAPALPAVAPKYLTEQSSLVSDAESVTLQSMSQEAFERTVTIAKGSSSLGMTVSANKDGLGVIVRSIIHGGAISRDGRIAVGDCILSINEESTISLTNAQARAMLRRHSLIGPDIKITYVPAEHLEEFRVSFGQQAGGIMALDIFSSYTGRDIPELPEREEGEGEESELQNAAYSSWSQPRRVELWREPSKSLGISIVGGRGMGSRLSNGEVMRGIFIKHVLEDSPAGKNGTLKPGDRIVEVDGMDLRDASHEQAVEAIRKAGSPVVFMVQSIVNRPRKSPLPSLPHSLYPKCSFSSTNPFAESLQLTSDKAPSQSESESEKATLCSVPSSSPSVFSEMSSDYAQPSATTVAEDEDKEDEFGYSWKNIQERYGTLTGQLHMIELEKGHSGLGLSLAGNKDRTRMSVFIVGIDPTGAAGRDGRLQIADELLEINGQILYGRSHQNASSIIKCAPSKVKIIFIRNADAVNQMAVCPGSAADPLPSTSESPQNKEVEPSITTSASAVDLSSLTNVYHLELPKDQGGLGIAICEEDTLNGVTIKSLTERGGAAKDGRLKPGDRILAVDDELVAGCPIEKFISLLKTAKTTVKLTVGAENPGCQAVPSAAVTASGERKDSSQTPAVPAPDLEPIPSTSRSSTPAIFASDPATCPIIPGCETTIEISKGQTGLGLSIVGGSDTLLGAIIIHEVYEEGAACKDGRLWAGDQILEVNGIDLRKATHDEAINVLRQTPQRVRLTLYRDEAPYKEEDVCDTFTVELQKRPGKGLGLSIVGKRNDTGVFVSDIVKGGIADADGRLMQGDQILMVNGEDVRNATQEAVAALLKCSLGTVTLEVGRIKAAPFHSERRPSQSSQVSESSLSSFSLPRSGIHTSESSESSAKKNALASEIQGLRTVEIKKGPADALGLSIAGGVGSPLGDVPIFIAMMHPNGVAAQTQKLRVGDRIVTICGTSTDGMTHTQAVNLMKNASGSIEVQVVAGGDVSVVTGHQQELANPCLAFTGLTSSTIFPDDLGPPQSKTITLDRGPDGLGFSIVGGYGSPHGDLPIYVKTVFAKGAAAEDGRLKRGDQIIAVNGQSLEGVTHEEAVAILKRTKGTVTLMVLS
|
Member of the NMDAR signaling complex that may play a role in control of AMPAR potentiation and synaptic plasticity in excitatory synapses . Promotes clustering of HT2RC at the cell surface .
|
O55164
|
Q9VJ71
|
CP310_DROME
|
CYPCCCXA1
|
Sophophora
|
MWLLLPILLYSAVFLSVRHIYSHWRRRGFPSEKAGITWSFLQKAYRREFRHVEAICEAYQSGKDRLLGIYCFFRPVLLVRNVELAQTILQQSNGHFSELKWDYISGYRRFNLLEKLAPMFGTKRLSEMFGQVQKVGDHLIHHLLDRQGQGCPQEVDIQQKLRVYSVNIIANLIYGLDINNFEHEDHILTSYLSHSQASIQSFTLGRLPQKSSYTYRLRDLIKQSVELREDHGLIRKDILQLLVRFRNGNEVSGDKWQLEPINDADKLLSIKRLAKVAEDLLKVSLDAVASTVTFTLLEILQEPLIVEKLRAEIKELSNENGQLKFEELNGLRYMDMCLKETLRKYPPLPIIERVCRKSYSLPNSKFTIDEGKTLMVPLLAMHRDEKYFSEPMKYKPLRFLQTANDVGQCEDKTKSNVFIGFGIGGSQCVGQNFAKLVIKVALIKLLQNFHLELDANQVKTLKVSHRPAPFIHTKDGLKVKLKRREINTKFYS
|
May be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides.
|
Q9VJ71
|
Q0S3F9
|
RS5_RHOJR
|
30S ribosomal protein S5
|
Rhodococcus
|
MPGRQRRDGGSGPAGQNGPNTGDNRGGGDRRGGGRDDRRGGQSAEKSNHIERVVTINRVSKVVKGGRRFSFTALVIVGDGNGLVGVGYGKAKEVPAAIQKGVEEARKSFFRVPMIGSTITHPVQGEAAAGVVMLRPASPGTGVIAGGAVRAVLECAGIHDILSKSLGSDNAINVVHATVAALKGLQRPEEVAARRGLALEDVAPAGMLRARAQAGSVK
|
Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body.
|
Q0S3F9
|
A9MHZ9
|
LFTR_SALAR
|
Phenyalanyltransferase
|
Salmonella
|
MRLVQLSRHSIAFPSPEGALREPNGLLALGGDLSPARLLMAYQHGIFPWFSPGDPILWWSPDPRAVLWPEEFHLSRSMKRFHNTSPYRVTLNYAFDRVIDGCTNHRDEGTWITRGIEEAYRRLHELGHAHSIEVWRDQELVGGMYGVSQGALFCGESMFSRKENASKTALLVFCAEFIHHGGKLIDCQVLNSHTASLGAIEIPRCDYLEHLSRLRQQPLVSRFWVPRTLFLPRK
|
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.
|
A9MHZ9
|
Q3A9Q7
|
RPOB_CARHZ
|
Transcriptase subunit beta
|
Carboxydothermus
|
MIPVQVGKKIRYSYAKFPEILELPYLIEIQKKSYQWFLDEGLREVFREISPITDFTGNLSLEFLDYYLGKPKYSVEECKERDFTYSAPLRVKVRLLNKETGEIKEQEVFLGDFPLMTEKGTFIFNGAERVVISQMVRSPGVYFSEQVDPNGKKMYLATIIPNRGAWLEFETDVNDHIYVRIDRTRKLPVTVLLKALGYESKGRIAELFDHDDKIIATLERDNTDSREEALIEIYKKLRPGEPPTVESAKTLLDSMFFDPKRYDLGNVGRYKLFKKLNHGVLYRYLEEDGEKEYDKYLNDYVPVKREFIRELTNEDIIYTIRYLLGLMRGQGKVDDIDHLGNRRLRSVGELLQNQFRIGLARMERVVRERMTIQDADSLTPQVLINTRPIVAAIKEFFGSSQLSQFMDQTNPLAELTHKRRLSALGPGGLSRERAGFEVRDVHHSHYGRMCPIETPEGPNIGLIGNLTTYARVNEFGFIETPYRKVDKERGVVTNEIVYLTADEEEKYIIAQANVRLSPEGKFLDEMVNARHGSEILHVEPSKVDFVDVSPKQVFSVATSLIPFLEHDDANRALMGANMQRQAVPLIRTEAPVVGTGIEYKAAKDSGVVVLAKNPGVVERVTADEIVIRNDQGQIDRYKLIKFQRSNQGTCINQKPIVRKGERVEKDQIIADGPSTDHGELALGKNVLVAYMPWEGYNYEDAILISEKLVKEDVFTSIHIEEYECDARDTKLGPEEITRDIPNVGEDALKDLDERGIIRIGAEVRPGDILVGKVTPKGETELTAEERLLRAIFGEKAREVRDTSLRVPHGESGKVVDVKVFSRENGDELSPGVNMLVRVYIAQKRKISVGDKMAGRHGNKGVVARILPEEDMPFLPDGTPVEIVLNPLGVPSRMNIGQILECHLGWAAKALGINVATPIFNGATEEDIFEALRKAGLPEDGKIEVRDGRTGEPFDSRVTVGYVYMLKLAHLVDDKIHARSTGPYSLVTQQPLGGKAQFGGQRFGEMEVWALEAYGAAYTLQEILTIKSDDVVGRVKTYEAIVKGENIPEPGVPESFKVLIKELQSLGLDVKVLTDNDEEVEIKEIDDDIGEKAEEYGLAASIADRDEVKNEYYEEEVEADFEINDDFDGDLED
|
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
|
Q3A9Q7
|
C4LBU6
|
RS12_TOLAT
|
30S ribosomal protein S12
|
Tolumonas
|
MATINQLVRKPRVKQVVKSSVPALNACPQKRGVCTRVYTTTPKKPNSALRKVCRVRLTNGFEVTSYIGGEGHNLQEHSVVLIRGGRVKDLPGVRYHTVRGALDCSGVKDRKQSRSKYGVKKPKA
|
Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit.
|
C4LBU6
|
Q465S2
|
RL37_METBF
|
50S ribosomal protein L37e
|
Methanosarcina
|
MSKGTSSMGKRQKRTHAKCRRCGSVSFNVHTKQCTSCGFGKTSRIRAYKWQAKCKY
|
Binds to the 23S rRNA.
|
Q465S2
|
Q3IKD8
|
RNFA_PSET1
|
Rnf electron transport complex subunit A
|
Pseudoalteromonas
|
MTEYVLLLIGTVLVNNFVLVQFLGLCPFMGVSSKLDTAIGMSLATTFVLTLASVTSYLVNQYILIPLDITYLRTMSFILVIAVVVQFTEMVVRKTSPTLYRLLGIFLPLITTNCAVLGVALLNIKEDHSFLQSAVYGFGAAVGFSLVLVLFAALRERLAAADVPTPFKGASIALITAGLMSMAFMGFTGLVKF
|
Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
|
Q3IKD8
|
B6HLP8
|
CHYD_PENRW
|
Chrysogine biosynthesis cluster protein D
|
Penicillium chrysogenum species complex
|
MCGISAFLCHPGKASSNEQANAQTRHVVDELEHSLDLVGHRGPDARGHIDILTIGLGHVRLSIIDLSLSGNQPFHDQDNSIHAVVNGELYDHEYYRDQLASEFQFVGTSDCEIVIALYKHYGLSFISHLRGEFAFVLWDANRQLLIAARDRYGIKSLYYTVVQGKLLVATEIKSFLAFGLQPEWCVRTLRDQSWRIESRTFFKGVHRVLPGHYLISRPNEREEQKPYWDLEYPDKLSHDARSEEEIVQGVRKRLLEAVKIRLKADVPVAIYLSGGIDSSSVAGMVADLMRQGTKLGNESNSVPSNMKCFTVQFDEDSGADESAIARRTANWLGVDIHLVKMDEEALASRFEDAVWHSEIPLPDLNGMGRLALAEAVHAQGIKVVITGEGSDEHFAGYDAFRADLLSEPDHSWPALQLPETDRQKALAMAAKQVKYGIFGEYSETVPDATKRMLNHSHVTSTIARVGSLPFSNWTTSYGNDLPETSLIEGFDGRVRDNITKRWHPLHTAQYLFTKSFMPHFILRYNGDNIDMVNQVESRCPFLDHHLTEYVNNVPPSLKLKYLPEEKSFREKYILREAVKPYVTDEIYNISKKAYMGPRKFWPGGPLHRKIKQLVTKENVESLGFVDWNATQEAVEKAFTKQDPMGLRRTITVAQFIVLGKRFGVKPAGALPN
|
Amidase; part of the gene cluster that mediates the biosynthesis of the yellow pigment chrysogine . the NRPS chyA mediates the condensation of anthranilic acid and alanine into the intermediate 2-(2-aminopropanamido)benzoic acid . The remainder of the pathway is highly branched yielding at least 13 chrysogine-related compounds . The malonyl transferase chyE converts 2-(2-aminopropanamido)benzoic acid and 2-(2-aminopropanamido)benzamidine into 2-(2-(2-carboxyacetamido)propanamido)benzoic acid and 3-((1-((2-carbamoylphenyl)amino)-1-oxopropan-2-yl)amino)-3-oxopropanoic acid, respectively . ChyD is an amidase, being responsible for the amidation of the carboxylic acid moiety of 2-(2-aminopropanamido)benzoic acid, 2-(2-(2-carboxyacetamido)propanamido)benzoic acid and 2-(2-((4-amino-1-carboxy-4-oxobutyl)amino)propanamido)benzoic acid . ChyC is involved in the same reactions as ChyD, but plays a more minor role in the amidation reactions compared to chyD . The oxidoreductases chyH and chyM are involved in oxidation reactions that form N-pyruvoylanthranilamide from 2-(2-aminopropanamido)benzamidine and (1-((2-carbamoylphenyl)amino)-1-oxopropan-2-yl)glutamine, respectively . N-pyruvoylanthranilamide is further converted via two further branches in the pathway, yielding chrysogine and additional chrysogine-related coumpounds . Chrysogine is likely formed by a spontaneous ring closure from N-pyruvoylanthranilamide .
|
B6HLP8
|
A4W3A3
|
NADE_STRS2
|
NH(3)-dependent NAD(+) synthetase
|
Streptococcus
|
MTLQETIIKELGVKPSIDPKEEIRRSIDFLKDYLKKHPFLKTYVLGISGGQDSTLAGRLAQLTMEEMRAETGDDSYQFIAIRLPYGVQADESDAQAALAFIQPDVSLTINIKESTDAMVAAVNANGLAMSDFNKGNAKARMRMIAQYAIAGERKGAVIGTDHAAENITGFFTKHGDGGADILPLFRLNKRQGKQLLAALGADEKLYLKVPTADLEEDKPGLADEVALGVTYNQIDDYLEGKTIDPQSQTIIEGWWNKTAHKRHLPITIFDDFWK
|
Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
|
A4W3A3
|
A1WQ79
|
FMT_VEREI
|
Methionyl-tRNA formyltransferase
|
Verminephrobacter
|
MKVVFAGTPGFARVALQRLLDAGFSLPLVLTRPDQPAGRGLQWQASPVKQCALAHGLAVAQPRSLRLDGRYPQDAAAARAALLAAQAEVMVVAAYGLILPQWVLDLPARGCLNIHASLLPRWRGAAPIQRAIEAGDTHTGVTIMQMDAGLDTGAMLLSQGSAIAPTDTTATLHDRLAALGADLIVQALEKMAAGADLPALAQPAQGVAYARKIEKSESSIDWSLPAQRIGQRIRAFDPAPGASTTCNGTSIKLWGYAIDGATIDGQRGVPRMHPGQILSADDSGIAVACGQGTALRLTVLQRAGGKRLAAADFLRGFALQPGMWLGAARA
|
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.
|
A1WQ79
|
B2V2K0
|
ERA_CLOBA
|
GTPase Era
|
Clostridium
|
MFKSGFVTIVGRPNVGKSTLLNYIMGEKLSIVSNKPQTTRNNIQTILTGDDYQIVFVDTPGIHKPKHKLGEYMVNSAKDSTNDVDLVLFLTNPDEEIGKGDKFILESLKDKKCPVYLVLNKIDESTPERVAKSLEMYSSEFNFKEIVPIAAIKGKNVDTLVDLMKTELPEGPKYYPEDMITDVPERFVVSEIVREKALRCLRDEVPHGIAVDIIQMKQSDNGTYHIEVDLICEKDSHKGIIIGKNGQMLKKIGETSRYELERFLRTKVNVKIWVKVRKEWRDNQNLLKELGYKKK
|
An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism.
|
B2V2K0
|
B9DPE0
|
PNP_STACT
|
Polynucleotide phosphorylase
|
Staphylococcus
|
MSQEKKVFKTEWANRPLSIETGQMAKQANGAVLVRYGDTVVLSTATASKEPRDGDFFPLMVNYEEKMYAAGKIPGGFKKREGRPADEATLTARLIDRPIRPLFPKGYRHDVQIINMVLSADPDCSPEMAAMIGSSMALSVSDIPFQGPIAGVNVGYIDGEYVINPTVEQKEVSRLDLEVAGHRDAVNMVEAGASEITEKEMLDAIFFGHEEIKRLVDFQQEIIDYLQPEKTEFIPKERNAEVEEKVTALTEEKGLKDAIQTFDKKEREENIDAIRDEVVAEFEDEENPDNDEVIAEVNSILNDLVKEEVRRQIADEKVRPDGRKPDEIRPLDSEVGLLPRAHGSGLFTRGQTQALSVLTLGAMSEYQLIDGLGTEEEKRFMHHYNFPNFSVGETGPVRAPGRREIGHGALGERALRYIIPDTKDFPYTVRIVSEVLESNGSSSQASICGSTLALMDAGVPIKAPVAGIAMGLVTRDDNYTILTDIQGMEDALGDMDFKVAGTEKGITAIQMDIKIDGLTREIIEEALEQARVGRLTILNHMLETIDQPRPELSAYAPKVETMTIKPEKIRDVIGPGGKKINEIIDETGVKLDIEQDGTIFIGAVDQDMINRAREIIEDITREAEVGQVYNAKVRRIEKYGTFVELFPGKDALLHISQIANQRINKVEDVLKLGDTIEVKVTEIDDKGRVNASHRALLNKED
|
Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
|
B9DPE0
|
Q9FI23
|
DEF16_ARATH
|
Plant defensin 1.2a
|
Arabidopsis
|
MAKFASIITLIFAALVLFAAFDAPAMVEAQKLCEKPSGTWSGVCGNSNACKNQCINLEGAKHGSCNYVFPAHKCICYVPC
|
Confers broad-spectrum resistance to pathogens. Has antifungal activity in vitro.
|
Q9FI23
|
Q8A6A7
|
RUVA_BACTN
|
Holliday junction ATP-dependent DNA helicase RuvA
|
Bacteroides
|
MIEYVRGELAELSPATAVIDCNGVGYAANISLNTYSAIQGKKNCKLYIYEAIREDAYVLYGFADKQEREIFLLLISVSGIGGNTARMILSALSPAELVNVISTENANLLKTVKGIGLKTAQRVIVDLKDKIKTMGATVAGGSASAGMLLQSASVEVQEEAVAALTMLGFAAAPSQKVVLAILKEEPDAPVEKVIKLALKRL
|
The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB.
|
Q8A6A7
|
C4K1H9
|
GLYA_RICPU
|
Serine hydroxymethyltransferase
|
spotted fever group
|
MNIFNNNLHETDKEINEIIKHEKLRQSNVIELIASENFVSPAVLEAQGALLTNKYAEGYPSKRFYNGCEEVDKAENLAIERVKKLFNCKYANVQPHSGSQANQAVYLALLQPGDTVLGMSLDSGGHLTHGAAPNMSGKWFNAVSYSVNKETYLIDYDEIERLADLHKPKLLIAGFSAYPRNIDFAKFREIVDKVGAYFMADIAHIAGLVATGEHQSPIPYAHAVTSTTHKTLRGPRGGLILSKDEEIGHKINSALFPGLQGGPLMHIIAAKAVAFLENLQPEYKSYIQQVISNAKALASSLQERGYDILTGGTDNHIVLVDLRKDGITGKLAANSLDRAGITCNKNAIPFDETSPFITSGIRLGTPACTTRGFKEKDFVLVGHMVADILDGLKNNEDNSALEQKVLNEVTKLIELFPFYG
|
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. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
|
C4K1H9
|
Q92609
|
TBCD5_HUMAN
|
TBC1 domain family member 5
|
Homo
|
MYHSLSETRHPLQPEEQEVGIDPLSSYSNKSGGDSNKNGRRTSSTLDSEGTFNSYRKEWEELFVNNNYLATIRQKGINGQLRSSRFRSICWKLFLCVLPQDKSQWISRIEELRAWYSNIKEIHITNPRKVVGQQDLMINNPLSQDEGSLWNKFFQDKELRSMIEQDVKRTFPEMQFFQQENVRKILTDVLFCYARENEQLLYKQGMHELLAPIVFVLHCDHQAFLHASESAQPSEEMKTVLNPEYLEHDAYAVFSQLMETAEPWFSTFEHDGQKGKETLMTPIPFARPQDLGPTIAIVTKVNQIQDHLLKKHDIELYMHLNRLEIAPQIYGLRWVRLLFGREFPLQDLLVVWDALFADGLSLGLVDYIFVAMLLYIRDALISSNYQTCLGLLMHYPFIGDVHSLILKALFLRDPKRNPRPVTYQFHPNLDYYKARGADLMNKSRTNAKGAPLNINKVSNSLINFGRKLISPAMAPGSAGGPVPGGNSSSSSSVVIPTRTSAEAPSHHLQQQQQQQRLMKSESMPVQLNKGLSSKNISSSPSVESLPGGREFTGSPPSSATKKDSFFSNISRSRSHSKTMGRKESEEELEAQISFLQGQLNDLDAMCKYCAKVMDTHLVNIQDVILQENLEKEDQILVSLAGLKQIKDILKGSLRFNQSQLEAEENEQITIADNHYCSSGQGQGRGQGQSVQMSGAIKQASSETPGCTDRGNSDDFILISKDDDGSSARGSFSGQAQPLRTLRSTSGKSQAPVCSPLVFSDPLMGPASASSSNPSSSPDDDSSKDSGFTIVSPLDI
|
May act as a GTPase-activating protein (GAP) for Rab family protein(s). May act as a GAP for RAB7A. Can displace RAB7A and retromer CSC subcomplex from the endosomal membrane to the cytosol; at least retromer displacement seems to require its catalytic activity . Required for retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN); the function seems to require its catalytic activity. Involved in regulation of autophagy . May act as a molecular switch between endosomal and autophagosomal transport and is involved in reprogramming vesicle trafficking upon autophagy induction. Involved in the trafficking of ATG9A upon activation of autophagy. May regulate the recruitment of ATG9A-AP2-containing vesicles to autophagic membranes .
|
Q92609
|
Q59M69
|
NNRD_CANAL
|
ATP-dependent NAD(P)HX dehydratase
|
Candida
|
MLRNKSQKELLHLSRQLIQPLLPNFHKGQAGKIVVIGGNEDYTGAPFFASHSAALVGADLSHVICEKAAGPVIKSYSPDLMIHPYLMDLDNPHLNLNNSELEKLKNLPIDEIIKTNDNAVLNKLIDELILPKVTSLLNRIDIVVVGPGFGRDPLMLKSLIRIIEEVKVLNLPIILDADSLYLVSLSPKIIANYPKAIITPNVVEFQRIAKALSIDADLSESNKDKLIDQTIEVSRKLGDIIVFRKGEHDLIVKSSKFLINEITGSNKRVGGQGDTLTGAIATLVNWSNNYILRLWDNQVVVNWSNNYILRLWDNQVDLDQEDANLLACFAASSVVRNASSKAFNKYGRSMQTSNVHEYLHESFTELFGDSIFRTSNI
|
Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ATP, which is converted to ADP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration.
|
Q59M69
|
A7GT90
|
APT_BACCN
|
Adenine phosphoribosyltransferase
|
Bacillus cereus group
|
MDFKQHIAIVPDYPKEGIVFKDITPLMNNGKAYKAATDEIVAYAKERNIDLVVGPEARGFIIGCPVSYALEVGFAPVRKLGKLPREIIKVDYGKEYGKDVLTIHKDAIKPGQRVLITDDLLATGGTIEATIQLVEELGGIVAGIAFLVELTYLEGREKLEGYDVLVLEKY
|
Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
|
A7GT90
|
A8EW86
|
EFG_ALIB4
|
Elongation factor G
|
Aliarcobacter
|
MARKIPLHRVRNIGIAAHIDAGKTTTTERILFYTGVSHKIGEVHEGAATMDWMEQEQERGITITSAATTCHWNHPKTNEQLQVNIIDTPGHVDFTIEVERSMRVLDGAVAVFCSVGGVQPQSETVWRQANKYGVPRIIYVNKMDRTGANFFNVEAQVRDRLKANPVPIQVPIGAEENFRGMVDLIKMKAYTYNLDAQAGEMYKIEDIPADLEDVVAEYREKLIEAAAESSEELMEKYLEGTELTEDEIVAGLKKRCLAMEITPMVCGTSFKNKGVQPLLDAVAMYLPAPTEVADIKGETQDGDAIIVPSTDKGEVAALAFKIMTDPFVGQLTFTRVYRGVLESGTYVLNSTKMKKERIGRLLKMHANSREEIKELYAGEIGAVVGLKDTITGDTLASEKDPVILERMDFPDPVISVAVEPKTKADQEKMGIALGKLAEEDPSFRVNTDEESGQTIISGMGELHLEILVDRMKREFKVEAEVGAPQVAYRETIRNAVKQEYKYAKQSGGKGQYGHVYLEIKPLPSGSEPNFKFNNEIKGGVVPKEYIPAVEKGCAEAMLGGILAGYPMVDIEVTLYDGSYHDVDSSEMAFKLAASMGFKQGCRSAAAGAVILEPIMKVEIETPEDYMGDVIGDCNKRRGQVQSMDDRAGIKLVTAMIPLSEMFGYSTDLRSMSQGRATYSMIFDAYQEVPRNVSEEIMKKRNG
|
Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.
|
A8EW86
|
A4SCU2
|
PURA_CHLPM
|
IMP--aspartate ligase
|
Chlorobium
|
MESKPFSLPSQSATVLIGTQFGDEGKGKLVDYLSDQYDIVVRYQGGANAGHTICFDGKSVVLHLIPSGIFNEKCVCVIGNGVVIDPVALLEEIATVEALGYEVKGRLFISHNAHLIMPYHKRLDSLSESAQGDQKIGTTGRGIGPSYEDKFARKGIRVVDLLNAEVLQEKLRENLAQKNRLFTTIYDGEEIDVESMVREYEEFDKIIDPYITNTQLYLNRQLREGRTVLLEGAQGSLLDVDHGTYPFVTSSNPTSGGACTGSGIAPNHIGKVIGVCKAYMTRVGNGAFPTELFDETGEELGRVGHEFGATTGRKRRCGWIDLVAMRYAVAVNGITELALTKLDVLDGFEEIQVCNSYTLDGKEIFDFPTDHETLSRVKPVLTPMKGWMASNADARNFEEMRPAAKQFVEFLENELEVPVTFISVGPGRNETVFR
|
Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
|
A4SCU2
|
A6X1J9
|
PURL_BRUA4
|
Phosphoribosylformylglycinamidine synthase subunit II
|
Brucella
|
MTISNTRDITPELIEAHGLKPDEYQRILDLIGREPTFTELGIFSAMWNEHCSYKSSKKWLRTLPTTGPRVIQGPGENAGVVDIGDGDCVVFKMESHNHPSYIEPYQGAATGVGGILRDVFTMGARPVAAMNALRFGEPDHPKTRHLVSGVVSGVGGYGNAFGVPTVGGEVNFDKRYNGNILVNAFAAGLAKHDGIFLSEAKGVGLPVVYLGAKTGRDGVGGATMASAEFDESIEEKRPTVQVGDPFTEKCLLEACLELMASGAVIAIQDMGAAGLTCSAVEMGAKGDLGIELILDHVPVREENMTAYEMMLSESQERMLMVLKPEKEAEAQAIFRKWGLDFAIVGKTTDDLRFRVIHQGEEVANLPIKDLGDEAPEYDRPWMEPGKHAPLPASNVPQVEDYSTALLKLIGSPDLSSRRWVYEQYDTLIQGNSLQVPGGDAGVIRVEGHDTKALAFSSDVTPRYCEADPFEGGKQAVAECWRNITATGAEPLASTDNLNFGNPEKPEIMGQLVKAIEGIGEACRALDFPIVSGNVSLYNETNGQAILPTPTIAGVGLIPDWTQTAKIGGMQDGDTLVLLGGDGTHLGQSIYLRDLFDRADGPAPTVDLALEKRNGEFVRSAIRNGQVTACHDLSDGGLAIAVAEMAIKSGKGAELDAGDGLPHAVLFGEDQARYVVAATAEMAKLIALNAEGAGVPFRVLGTVGGDSLKIGNVVDVSVADLTDAFEGWFPGFMSGEPVSDN
|
Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
|
A6X1J9
|
Q48CT4
|
PQQD_PSE14
|
Pyrroloquinoline quinone biosynthesis protein D
|
Pseudomonas
|
MKHDPQFRALTPKWHQGYRFQYEPAQKAHVVLYPEGMIKLNDSAALIGGLIDGKRTITAIIHELQQQFPNVPELGMDVDEFMEGTKKKNWIDLV
|
Functions as a PqqA binding protein and presents PqqA to PqqE, in the pyrroloquinoline quinone (PQQ) biosynthetic pathway.
|
Q48CT4
|
Q55GK8
|
KIL1_DICDI
|
Membrane-associated sulfotransferase kil1
|
Dictyostelium
|
MSTTSMILTKKNIIILSIIIITIIAYQFYITSPQSFPSSNTITNTINTSGKGLDYTELLNLQKDLKAQQTEIRKQLEQLKYSINDINQNQNENQNQINNEYNNNKLNDEQENNNNNNYNNNNNNNNNELINYKERIKKKSKEQPNTCIPVEGKLLCLPNFIVIGTMKSGTTFLDYYLQKHPQIAHHSKKEIWYFNSYYANGIEWYAKHFEQYTSLENQKLIGEATPFYINNPNTAPRLFTTLKNAKLILLLRDPVERSLSQYHFSIQWLKRNKSPPLEYSFEHLIHEEADVIETCIRGHERYKEAFKQRKEIEKNGGGGLLNDNTSGEEFNLVDPFYTLHSEKNWTFYKDCIRCDKCFQIGSILHTSGHPTFGMLAKSLYFEQLDYWLNFFPLEQIHIIRYEDISSQPESVLSELEDFLDINHIDYGEFKPRNVVQHDPMNQEIKSYLINYFKQSNEKLYNLLNRDFKWQN
|
Sulfotransferase involved in intracellular killing of bacteria.
|
Q55GK8
|
F5CPE4
|
3S166_MICAT
|
MALT0066C
|
Micrurus
|
MKTLLLTLVVVTIVCLDFGHTLICYNYETPLDKTTECCGNGVTTCFAKSWRDHRGLRTDRGCGCPNVKPGVTINCCKTDRCNG
|
Binds to muscle nicotinic acetylcholine receptor (nAChR) and inhibit acetylcholine from binding to the receptor, thereby impairing neuromuscular transmission.
|
F5CPE4
|
A5N376
|
ALR_CLOK5
|
Alanine racemase
|
Clostridium
|
MFQKYRPVWEEINLDNLVYNIGQIKSKIGNKELIGVIKADAYGHGAVEIAKVLLENGVSRLAVAILDEAIELRKNKIKVPIMVLGIIPHAFLDEIMNYDIEPIVPSYSYASKLSKLAESKDKKIKVHIALDTGMGRIGFSIDPNSVEEIGKISKLPNIEIQSLFSHFSTADETDKAYSCEQFKKYKLLYEELVKKNVKINMRTISNSAAIMELPDTYCDLVRPGIIMYGYYPSTEVDKNNLSIKPIMTLKANVVYVKVLESGSYIGYGRKFKCNRKSVIATLPLGYADGYTRRLFGKAKVIINGKFAPVVGNICMDQCMVDVTDVGEVNIGDEVVLIGEKDGLKFNADDIAEITGTISYEVLCMIGRRVPKLYIKGGEVVKIKNYVISSDS
|
Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
|
A5N376
|
Q5GT55
|
TRMD_WOLTR
|
tRNA [GM37] methyltransferase
|
unclassified Wolbachia
|
MFDVTILTIFPEMFPGFLNYSLAGKALEKKIWNLQVINIRFFAKDRHLTVDHIPYGGGAGMIMRPDVVGDAVDSVLSTHKDTKFIYMTPSGTKFDQSIARELVGFPHITILCGRFEGIDQRVIDEYTPYELSIGDYILSGGEPAAMVILDVCVRLLPGVVNNSGSITEESFSYSGGVLEYPQYTRPKQWRKHRVPKILLSGNHKKISDWRQKQSQVITKRRRPELLDGEINDKFT
|
Specifically methylates guanosine-37 in various tRNAs.
|
Q5GT55
|
Q8U8I2
|
SDH_AGRFC
|
Serine 3-dehydrogenase
|
Agrobacterium tumefaciens complex
|
MSGTILITGATSGFGQATARRFVKEGWKVIGTGRRAERLEALAAELGQAFHGIAFDITDEDATEKALAALPDGFRDIDILVNNAGLALGTAPAPQVALKDWQTMVDTNITGLLNITHHLLPTLIKQKGIVVNLSSVAAHYPYLGGNVYGGTKAFLRQFSLGLRSDLHGKGVRVTSIEPGMCETEFTLVRTGGNQEASDNLYKGVNPITADDIANTIYWVASQPKHININSLELMPVNQSFAGFQVYRES
|
Catalyzes the oxidation of the hydroxyl group of serine to form 2-aminomalonate semialdehyde which is spontaneously converted into 2-aminoacetaldehyde and CO(2). Also acts on D-serine, L-glycerate, D-glycerate and 2-methyl-DL-serine. Does not act on O-methyl-DL-serine and L-threonine.
|
Q8U8I2
|
A5TY73
|
GYRB_MYCTA
|
DNA gyrase subunit B
|
Mycobacterium tuberculosis complex
|
MAAQKKKAQDEYGAASITILEGLEAVRKRPGMYIGSTGERGLHHLIWEVVDNAVDEAMAGYATTVNVVLLEDGGVEVADDGRGIPVATHASGIPTVDVVMTQLHAGGKFDSDAYAISGGLHGVGVSVVNALSTRLEVEIKRDGYEWSQVYEKSEPLGLKQGAPTKKTGSTVRFWADPAVFETTEYDFETVARRLQEMAFLNKGLTINLTDERVTQDEVVDEVVSDVAEAPKSASERAAESTAPHKVKSRTFHYPGGLVDFVKHINRTKNAIHSSIVDFSGKGTGHEVEIAMQWNAGYSESVHTFANTINTHEGGTHEEGFRSALTSVVNKYAKDRKLLKDKDPNLTGDDIREGLAAVISVKVSEPQFEGQTKTKLGNTEVKSFVQKVCNEQLTHWFEANPTDAKVVVNKAVSSAQARIAARKARELVRRKSATDIGGLPGKLADCRSTDPRKSELYVVEGDSAGGSAKSGRDSMFQAILPLRGKIINVEKARIDRVLKNTEVQAIITALGTGIHDEFDIGKLRYHKIVLMADADVDGQHISTLLLTLLFRFMRPLIENGHVFLAQPPLYKLKWQRSDPEFAYSDRERDGLLEAGLKAGKKINKEDGIQRYKGLGEMDAKELWETTMDPSVRVLRQVTLDDAAAADELFSILMGEDVDARRSFITRNAKDVRFLDV
|
A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.
|
A5TY73
|
Q9ERG3
|
GLHA_MICMO
|
Thyrotropin alpha chain
|
Microtus
|
MDYYRKYAAVFLVMLSMFLHSLHSLPDGDLIIQGCPECKLKENKYFSRLGNPVYQCMGCCFSRAYPTPARSKKTMLVPKNITSEATCCVAKSFTKTTVLGYARVENHTECHCSTCYYHKV
|
Shared alpha chain of the active heterodimeric glycoprotein hormones thyrotropin/thyroid stimulating hormone/TSH, lutropin/luteinizing hormone/LH and follitropin/follicle stimulating hormone/FSH. These hormones bind specific receptors on target cells that in turn activate downstream signaling pathways.
|
Q9ERG3
|
A5CF69
|
NDK_ORITB
|
Nucleoside-2-P kinase
|
Orientia
|
MNMEYTLSILKPDVIKRNIIGKVNTYIENSGLKIIAQKTLLLTKVQAENFYIIHKDRAYYQSLVQNMTSGPVVVQVLYGLNAVKKYREIIGATNPCDAKKGTIRGDIAKSIDENTVHGSDSLENADIEIKFFFALIEYAYL
|
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.
|
A5CF69
|
Q51366
|
GM4D_PSEAE
|
GDP-D-mannose dehydratase
|
Pseudomonas
|
MTRSALVTGITGQDGAYLAKLLLEKGYRVHGLVARRSSDTRWRLRELGIEGDIQYEDGDMADACSVQRAVIKAQPQEVYNLAAQSFVGASWNQPVTTGVVDGLGVTHLLEAIRQFSPETRFYQASTSEMFGLIQAERQDENTPFYPRSPYGVAKLYGHWITVNYRESFGLHASSGILFNHESPLRGIEFVTRKVTDAVARIKLGKQQELRLGNVDAKRDWGFAGDYVEAMWLMLQQDKADDYVVATGVTTTVRDMCQIAFEHVGLDYRDFLKIDPAFFRPAEVDVLLGNPAKAQRVLGWKPRTSLDELIRMMVEADLRRVSRE
|
Catalyzes the conversion of GDP-D-mannose to GDP-4-dehydro-6-deoxy-D-mannose.
|
Q51366
|
Q96L42
|
KCNH8_HUMAN
|
Voltage-gated potassium channel subunit Kv12.1
|
Homo
|
MPVMKGLLAPQNTFLDTIATRFDGTHSNFILANAQVAKGFPIVYCSDGFCELAGFARTEVMQKSCSCKFLFGVETNEQLMLQIEKSLEEKTEFKGEIMFYKKNGSPFWCLLDIVPIKNEKGDVVLFLASFKDITDTKVKITPEDKKEDKVKGRSRAGTHFDSARRRSRAVLYHISGHLQRREKNKLKINNNVFVDKPAFPEYKVSDAKKSKFILLHFSTFKAGWDWLILLATFYVAVTVPYNVCFIGNDDLSTTRSTTVSDIAVEILFIIDIILNFRTTYVSKSGQVIFEARSICIHYVTTWFIIDLIAALPFDLLYAFNVTVVSLVHLLKTVRLLRLLRLLQKLDRYSQHSTIVLTLLMSMFALLAHWMACIWYVIGKMEREDNSLLKWEVGWLHELGKRLESPYYGNNTLGGPSIRSAYIAALYFTLSSLTSVGFGNVSANTDAEKIFSICTMLIGALMHALVFGNVTAIIQRMYSRWSLYHTRTKDLKDFIRVHHLPQQLKQRMLEYFQTTWSVNNGIDSNELLKDFPDELRSDITMHLNKEILQLSLFECASRGCLRSLSLHIKTSFCAPGEYLLRQGDALQAIYFVCSGSMEVLKDSMVLAILGKGDLIGANLSIKDQVIKTNADVKALTYCDLQCIILKGLFEVLDLYPEYAHKFVEDIQHDLTYNLREGHESDVISRLSNKSMVSQSEPKGNGNINKRLPSIVEDEEEEEEGEEEEAVSLSPICTRGSSSRNKKVGSNKAYLGLSLKQLASGTVPFHSPIRVSRSNSPKTKQEIDPPNHNKRKEKNLKLQLSTLNNAGPPDLSPRIVDGIEDGNSSEESQTFDFGSERIRSEPRISPPLGDPEIGAAVLFIKAEETKQQINKLNSEVTTLTQEVSQLGKDMRNVIQLLENVLSPQQPSRFCSLHSTSVCPSRESLQTRTSWSAHQPCLHLQTGGAAYTQAQLCSSNITSDIWSVDPSSVGSSPQRTGAHEQNPADSELYHSPSLDYSPSHYQVVQEGHLQFLRCISPHSDSTLTPLQSISATLSSSVCSSSETSLHLVLPSRSEEGSFSQGTVSSFSLENLPGSWNQEGMASASTKPLENLPLEVVTSTAEVKDNKAINV
|
Pore-forming (alpha) subunit of voltage-gated potassium channel. Elicits a slowly activating, outward rectifying current. Channel properties may be modulated by cAMP and subunit assembly.
|
Q96L42
|
P67090
|
USPD_ECO57
|
Universal stress protein D
|
Escherichia
|
MAYKHIGVAISGNEEDALLVNKALELARHNDAHLTLIHIDDGLSELYPGIYFPATEDILQLLKNKSDNKLYKLTKNIQWPKTKLRIERGEMPETLLEIMQKEQCDLLVCGHHHSFINRLMPAYRGMINKLSADLLIVPFIDK
|
Required for resistance to DNA-damaging agents.
|
P67090
|
Q8JFY4
|
GHRL_ANGJA
|
Ghrelin-21
|
Anguilla
|
MRQMKRTAYIILLVCVLALWMDSVQAGSSFLSPSQRPQGKDKKPPRVGRRDSDGILDLFMRPPLQDEDIRHITFNTPFEIGITMTEELFQQYGEVMQKIMQDLLMDTPAKE
|
Ligand for growth hormone secretagogue receptor type 1 (GHSR). Induces the release of growth hormone from the pituitary. Has an appetite-stimulating effect, induces adiposity and stimulates gastric acid secretion. Involved in growth regulation.
|
Q8JFY4
|
Q9PE76
|
RL3_XYLFA
|
50S ribosomal protein L3
|
Xylella
|
MGCYSMGFVGRKAGMSRVFLEDGCSIPVTLIEATANRVVQIKTSDVDGYDAVQVTVGSRRSVLVNKPESGHFAKAKVEAGRGLWEFRVEKTQLGSYSVGSEVGLSIFAVGQKVDIQGITKGKGFQGTIKRHNFRMGDATHGNSLSHRAPGSLGQRQTPGRVFPGKKMSGHMGAVRQSVQNLEVVKIDVERCLIAVRGAIPGASGGDVLIRSASKI
|
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.
|
Q9PE76
|
Q9JS61
|
ILVD_NEIMB
|
Dihydroxy-acid dehydratase
|
Neisseria
|
MPEYRSKTSTHGRNMAGARALWRATGVMETDFGKPIIAVANSFTQFVPGHVHLHNMGQLVAREIEKAGAIAKEFNTIAIDDGIAMGHSGMLYSLPSRDLIADSIEYMVNAHCADALVCISNCDKITPGMLIAAMRLNIPTIFVSGGPMEAGKVIGVANIQPERRLDLIDAMIESADDNVSNRQVEEVEQNACPTCGSCSGMFTANSMNCLTEALGLSLPGNGSYLATHAGRKELFLEAGRMIVEITKRYYEQNDETVLPRSIATKKAFENAMTMDIAMGGSTNTILHLLAVANEAGVDFKMADIDRLSRVVPCICKTAPNNHDYYMEDVHRAGGIFAILKELDKAGKLHTDVHTIHAPTLKDAIEQWDVTNPENTRAIERFKAAPGGVRTTQAFSQNRMWKTLDLDREKGCIRDVAHAYSQDGGLAVLFGNIAERGCVVKTAGVDESILKFTGRARVFESQEDAVEGILGNQIVAGDIVIIRYEGPKGGPGMQEMLYPTSYLKSKGLGKACALLTDGRFSGGTSGLSIGHASPEAAEGGAIGLVHEGDTVEIDIPNRSIHLAISDEELAARRAEMEARGSKAWKPKNRDRYVSAALRAYGAMATSADKGAVRDVAQIER
|
Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively.
|
Q9JS61
|
Q3B5Y0
|
ACCD_CHLL3
|
Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta
|
Pelodictyon
|
MVWFKRVKPFIRTTDRRDVPEGLWSKCEDCGAMLHRRQLEENLNTCNECGHHFRISPYRYFSILFDNEEFTEFDDCLRAADPLTFVDTKKYPDRVHDTIEKSGKTEACRNAFGKSAGADLVISAMDFGFIGGSMGSVVGEKISRAADKAIELNAPLIVISQSGGARMMEGAFSLMQMAKTAARLTRLGENRLPFISLMTDPTMGGISASFAMLGDLNISEPKALIGFAGPRVIRDTIKRDLPEGFQRAEFLQEHGFVDMIVHRKELKQRLAKTLAMMRVEG
|
Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.
|
Q3B5Y0
|
Q7UIC5
|
RPOA_RHOBA
|
Transcriptase subunit alpha
|
Rhodopirellula
|
MTMHIRWRGMELPSSLEVDRDSLTQTYGKFSAEPFERGFGASIGNSMRRVLLSSLVGSAVTQIKIRGAQHEFTTIPGVLEDVTDIVLNVKSLIVNSNTDSTRVITVERNTAGVVTGADVQTDADVEIINKDHVICTLTDDVPFMMEMVVETGRGYVPSTEHSSVDHEIGIIPIDAVFSPIVRVRYEVEATRVGQKTNYDRLNLEIWTDGTINPEMALTEAAKILRKHLNPFVQYRELGPSIFSAARGGAGSPEAQLEAKLNMTLADLRLSVRANNCLESENIMTVRDLVQRTEDSLLEVRNFGDTTLNEVREKLSQYGLHLGMRVPNQPLF
|
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
|
Q7UIC5
|
P73301
|
IF1_SYNY3
|
Translation initiation factor IF-1
|
unclassified Synechocystis
|
MSKQDLIEMEGTVMESLPNAMFRVDLDNGFNVLAHISGKIRRNYIKILPGDRVKVELTPYDLTKGRITYRLKNKK
|
One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex.
|
P73301
|
B0K2J6
|
COBQ_THEPX
|
Cobyric acid synthase
|
unclassified Thermoanaerobacter
|
MALKLMIQGTASSVGKSLLVAAFCRIFKQDGYRVAPFKSQNMALNSYITDEGLEIGRAQAMQAEAAGVKPSYHMNPILLKPSSDKKSQVVLRGKVYKNMSAAEYHQFKPQLLKFIKEDFDFLASQNDIVVIEGAGSPAEINLRDRDVVNMGMAEMVNAPVLLVGDIDKGGVFASIAGTLLLLKENERNRIEGVLINKFRGDIEILKPGLEMLENIVHKKVLGVVPYMDVHIDEEDGATERFYRRSTEGDIEIAVINLPHISNFTDFEPLAKVPGVKLRYVNKGERIGDCDVVIIPGTKNTIGDLQALKGYRLDKEIFEMRKKGKFIVGICGGYQILGKVIKDPGRIESTTSEIEGLGLLDVETVIENEKTTTQIKAVIRNNLPSILSPLRNIAVEGYEIHMGKSRILGDCQPFSVITHRNGEKIEVYDGCISDDGKVFGTYIHGIFENREFVREFINIVRKSKGLSPIEEIIDYKEFKEREYDKLADIVRKSIDMKKVYEIMERYKD
|
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.
|
B0K2J6
|
P47645
|
ATP6_MYCGE
|
F-ATPase subunit 6
| null |
MSPREIVLKETNQIDFISNQSIFDISPISGWKPFAPTDQILGIFIVFVLLLTFFIFYKLKLKKADSLKNNSYFLLLFQMLFVWVQDTTADLLGEENKKFAPYFLMLLLYIVSSNLVSLLGGISPPTSSLTFTFSLGLATFIGIVVMGIRYQRWNFFKEFAFGITVKGKKYSTFIPNPFSILSGFAPLFSISLRLWGNILAGTVILALFYNFWIFIFSSINNQPLALSLGTVFAGLITPVLHIYFDVIAGVLQGYVFVMLTYNYWAKMRNQGLENNNASELHFKGIKVIQENI
|
Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
|
P47645
|
Q3SMH2
|
MURC_THIDA
|
UDP-N-acetylmuramoyl-L-alanine synthetase
|
Thiobacillus
|
MKHAVKHIHFIGIGGVGMSGIAEVLLNLGYAVSGSDLADNAVTQRLAKLGARIHRGHAPSNIAGADAVVTSTAVQESNPEVVAAREKKIPIVPRALMLAELMRLRQGIAIAGTHGKTTTTSLVASILGEAGMDPTYVIGGKLTAAGTNARLGQGDFLVAEADESDASFLYLTPVIAIVTNIDADHMDTYGHDFDRLKTAFVDFCQRLPFYGMAVLCIDDANVREILPRITKPITTYGFDPAAQVRAVDTRFEHGQMRFTVKREGMADLDVTLNQPGLHNVLNALAAIAVATEVGASDAAIVKALAEFHGVGRRFQRYGEHPTKDGGCYWLIDDYGHHPVEMAATLAAARGAFPGRRLVLVFQPHRYSRTRDCFEDFVKVLSETDALVLTEVYPAGEAPIVAADGRALARAVRVAGKVEPVFVENVADVAATVRDLVQADDVVLVMGAGSIGQVAPALGERDAP
|
Cell wall formation.
|
Q3SMH2
|
P38865
|
CTR2_YEAST
|
Copper transport protein CTR2
|
Saccharomyces
|
MDDKKTWSTVTLRTFNQLVTSSLIGYSKKMDSMNHKMEGNAGHDHSDMHMGDGDDTCSMNMLFSWSYKNTCVVFEWWHIKTLPGLILSCLAIFGLAYLYEYLKYCVHKRQLSQRVLLPNRSLTKINQADKVSNSILYGLQVGFSFMLMLVFMTYNGWLMLAVVCGAIWGNYSWCTSYSPEIDDSSLACH
|
Provides bioavailable copper via mobilization of vacuolar copper stores and export to the cytoplasm.
|
P38865
|
A1A3F7
|
GATC_BIFAA
|
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C
|
Bifidobacterium
|
MPTFTKEEIVHLGDLARIALTDEEITRLQGDLNVIAESINKVQEVATDDVEPTANPVPLEAYLRPDVPETPLTQAEATAGAPVSEAGMFVAPRILGQE
|
Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
|
A1A3F7
|
Q7V3G3
|
RBFA_PROMP
|
Ribosome-binding factor A
|
Prochlorococcus
|
MPNNYRIAKISSLLKKEITLILQNDLENDLLRSNFINISKIELSGDLQFCKIYITSTAEEAIRKEIVEELNLAKTYIRHTLGQRIEMRRVPEMTFKDDTVLEKGLSVLKLLAELKNKKHNQDSKVEGNNKNV
|
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.
|
Q7V3G3
|
B2RH54
|
FIMA1_PORG3
|
Major fimbrial subunit protein type I
|
Porphyromonas
|
MKKTKFFLLGLAALAMTACNKDNEAEPVTEGNATISVVLKTSNSNRAFGVGDDESKVAKLTVMVYNGEQQEAIKSAENATKVEDIKCSAGQRTLVVMANTGAMELVGKTLAEVKALTTELTAENQEAAGLIMTAEPKTIVLKAGKNYIGYSGTGEGNHIENDPLKIKRVHARMAFTEIKVQMSAAYDNIYTFVPEKIYGLIAKKQSNLFGATLVNADANYLTGSLTTFNGAYTPANYANVPWLSRNYVAPAADAPQGFYVLENDYSANGGTIHPTILCVYGKLQKNGADLAGADLAAAQAANWVDAEGKTYYPVLVNFNSNNYTYDSNYTPKNKIERNHKYDIKLTITGPGTNNPENPITESAHLNVQCTVAEWVLVGQNATW
|
Structural subunit of the major fimbriae. These long, filamentous pili are attached to the cell surface; they mediate biofilm formation, adhesion onto host cells and onto other bacteria that are part of the oral microbiome . They play an important role in the invasion of periodontal tissues . Fimbriae and their constituents are major virulence factors. FimA proteins from different strains have highly divergent sequences, and this has been used for classification . The sequence-based classification correlates with pathogenicity .
|
B2RH54
|
P0A4Y7
|
ARGB_MYCBO
|
NAG kinase
|
Mycobacterium tuberculosis complex
|
MSRIEALPTHIKAQVLAEALPWLKQLHGKVVVVKYGGNAMTDDTLRRAFAADMAFLRNCGIHPVVVHGGGPQITAMLRRLGIEGDFKGGFRVTTPEVLDVARMVLFGQVGRELVNLINAHGPYAVGITGEDAQLFTAVRRSVTVDGVATDIGLVGDVDQVNTAAMLDLVAAGRIPVVSTLAPDADGVVHNINADTAAAAVAEALGAEKLLMLTDIDGLYTRWPDRDSLVSEIDTGTLAQLLPTLESGMVPKVEACLRAVIGGVPSAHIIDGRVTHCVLVELFTDAGTGTKVVRG
|
Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
|
P0A4Y7
|
P70582
|
NUP54_RAT
|
Nucleoporin Nup54
|
Rattus
|
MAFNFGAPSGTSGTSTATAAPAGGFGGFGTTTTTAGSAFSFSAPTNTGSTGLLGGTQNKGFGFGTGFGTSTGTGTGLGTGLGTGLGFGGFNTQQQQQQQQTSLGGLFSQPAQAPAQSNQLINTASALSAPTLLGDERDAILAKWNQLQAFWGTGKGYFNNNIPPVEFTQENPFCRFKAVGYSCMPNNKDEDGLVVLIFNKKETDIRSQQQQLVESLHKVLGGNQTLTVNVEGIKTLPDDQTEVVIYIVERSPNGTSRRVPATTLYAHFEQANIKTQLQQLGVTLSMTRTELSPAQIKQLLQNPPAGVDPIIWEQAKVDNPDSEKLIPVPMVGFKELLRRLKVQDQMTKQHQTRLDIISEDISELQKNQTTTMAKIAQYKRKLMDLSHRTLQVLIKQEIQRKSGYAIQAEEEQLRVQLDTIQGELNAPTQFKGRLNELMSQIRMQNHFGAVKSEEKYYIDADLLREIKQHLKQQQEGLSHLISIIKDDLEDIKLVEHGLNETIHSRGGVFS
|
Component of the nuclear pore complex, a complex required for the trafficking across the nuclear membrane.
|
P70582
|
A6TC90
|
NUDK_KLEP7
|
GDPMK
|
Klebsiella
|
MSLNIHVIKDKILSENWFVLRNMTYELTRADGSVVRHKREVYDRGNGATVLLYNRHKQTVVLVRQFRVATWVNGNHDGMLIETCAGLLDNDEPEACIRKEAVEETGYEVGEVRKLFELFMSPGGVTEVVHFFIAEYSDAQRTTSGGGVDDEAIEVLELPFSQALQMVADGEIRDGKAVILLQYLQTSGLMSGNSDKSD
|
Nucleoside diphosphate sugar hydrolase that hydrolyzes GDP-mannose as its preferred substrate, yielding GMP and mannose-1-phosphate.
|
A6TC90
|
Q9DAU7
|
WFDC2_MOUSE
|
WAP domain-containing protein HE4
|
Mus
|
MPACRLCLLAAGLLLGLLLFTPISATGTDAEKPGECPQLEPITDCVLECTLDKDCADNRKCCQAGCSSVCSKPNGPSEGELSGTDTKLSETGTTTQSAGLDHTTKPPGGQVSTKPPAVTREGLGVREKQGTCPSVDIPKLGLCEDQCQVDSQCSGNMKCCRNGCGKMACTTPKF
|
Broad range protease inhibitor.
|
Q9DAU7
|
A8MTJ3
|
GNAT3_HUMAN
|
Gustducin alpha-3 chain
|
Homo
|
MGSGISSESKESAKRSKELEKKLQEDAERDARTVKLLLLGAGESGKSTIVKQMKIIHKNGYSEQECMEFKAVIYSNTLQSILAIVKAMTTLGIDYVNPRSAEDQRQLYAMANTLEDGGMTPQLAEVIKRLWRDPGIQACFERASEYQLNDSAAYYLNDLDRITASGYVPNEQDVLHSRVKTTGIIETQFSFKDLHFRMFDVGGQRSERKKWIHCFEGVTCIIFCAALSAYDMVLVEDEEVNRMHESLHLFNSICNHKYFSTTSIVLFLNKKDIFQEKVTKVHLSICFPEYTGPNTFEDAGNYIKNQFLDLNLKKEDKEIYSHMTCATDTQNVKFVFDAVTDIIIKENLKDCGLF
|
Guanine nucleotide-binding protein (G protein) alpha subunit playing a prominent role in bitter and sweet taste transduction as well as in umami (monosodium glutamate, monopotassium glutamate, and inosine monophosphate) taste transduction. Transduction by this alpha subunit involves coupling of specific cell-surface receptors with a cGMP-phosphodiesterase; Activation of phosphodiesterase lowers intracellular levels of cAMP and cGMP which may open a cyclic nucleotide-suppressible cation channel leading to influx of calcium, ultimately leading to release of neurotransmitter. Indeed, denatonium and strychnine induce transient reduction in cAMP and cGMP in taste tissue, whereas this decrease is inhibited by GNAT3 antibody. Gustducin heterotrimer transduces response to bitter and sweet compounds via regulation of phosphodiesterase for alpha subunit, as well as via activation of phospholipase C for beta and gamma subunits, with ultimate increase inositol trisphosphate and increase of intracellular Calcium. GNAT3 can functionally couple to taste receptors to transmit intracellular signal: receptor heterodimer TAS1R2/TAS1R3 senses sweetness and TAS1R1/TAS1R3 transduces umami taste, whereas the T2R family GPCRs act as bitter sensors. Functions also as lumenal sugar sensors in the gut to control the expression of the Na+-glucose transporter SGLT1 in response to dietaty sugar, as well as the secretion of Glucagon-like peptide-1, GLP-1 and glucose-dependent insulinotropic polypeptide, GIP. Thus, may modulate the gut capacity to absorb sugars, with implications in malabsorption syndromes and diet-related disorders including diabetes and obesity.
|
A8MTJ3
|
Q82W18
|
LPTD_NITEU
|
LPS-assembly protein LptD
|
Nitrosomonas
|
MNTLKLCLILYACLVLLPVRVMSADLSPASSERQPIYIEADHIDGHYQQEIEAIGNVRMRRGDQTLTADRVKYYQSNENVEVEGNAQLERPDDILWGSYLQMNLNDNTGQLSEPRYLQKDGNGRGDGNLLLLEGENQYRFKKARYTTCPEDDHDWYILADDLEIDKEKKVGTARHASVRFKDVPILYVPWMNFSFGNERKTGFLSPIMGNTSRSGVEVSVPFYWNIAPNYDATITPRLMSRRGVMLNNEFRYIGQTLNGRFLLDYLPNDLETDTTRYGMQLNHFHNLGAGWFGMINYNSASDRNYFRDLGNNILFTSQTNLLQQGFASYFRELGRNGTLTFSTLLQQFQTLQDPRAPIISPFKILPRFTLNAAKRNVYGLDFDFSGSFTHFSHSTLPHGLRTTFLPGVSLPLENSFGFIRPRVSLHHTRYDLNEPANPAANDKHLSRTVPIFSFDSGIVLERDTTLARENFVQTIEPRVFYTYIPYRDQQLLPNFDSAEMDFSYPQLFLERRFSGEDRINDANEITLAVSSRLIHSATGNERLRFSAGQRIRFSDRRVILTSPQVTRAGSDFIAELSGGITQNIKTDTGIQLNQNNFLIEKIRTGISYRPAPGKVINAGYRFTRDVLEQVDLSTQWPFLKKWQGFAAINYSLKDDKLLAGLLGLEYNACCWSLRFVTSHFTTATQRTSTNIFVQLELNDLMRIGTNPVRVLQQTIPGYMRTDL
|
Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane.
|
Q82W18
|
A9KFM0
|
ALR_COXBN
|
Alanine racemase
|
Coxiella
|
MNRATATINVTALKHNLSQIKALAPKSLAWVMIKSNGYGHGLVRVAKALSDANAFGVACIDEALTLREVGIKSPIIVMKGFYNEAELSQFARHRLGAVIHCSDQVSLLEKTNLTSSLSVWLKIDTGMNRLGFSVEQSPAVYNQLKTSSSIQKPIGLMTHLADADNENKTFTELQIKRFFSVTEKMIGPKSIVNSAGFFAYPNALVDWIRPGIILYGISPFGINYNSFKEKIEKKFRPVMTLSAKIIAIKNRRQNDSVGYGCTWSCPEDMPIAIVSIGYGDGYPRHAPSGTPVLLNGKICPLIGRVSMDMIAIDLRSQPNAQVGDDVILWGEGLPVEIIAEKAGTIAYELLCKITQRVQFIEIEK
|
Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
|
A9KFM0
|
A0Q669
|
IF1_FRATN
|
Translation initiation factor IF-1
|
Francisella
|
MAKEDCIEMEGVVLEALPNTMFRVELENGHIVTAHISGKMRKNYIRILTGDKVVVEITPYDLTKGRIKFRSK
|
One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex.
|
A0Q669
|
Q2K386
|
DAPF_RHIEC
|
PLP-independent amino acid racemase
|
Rhizobium
|
MSATVEFARMNGLGNKILVVDMRGRSDKVTPAAAVALNADPQTEFDQIMAIHDPKADGTDAFIDILNSDGSKAQACGNGTRCVVQALAAETGRKAFTFQTVAGILNAIEHEDGTISVDMGKPVFDWDRIPLAEEFHDTSRIELQIGPIDNPLLHSPSAMSMGNPHAIFWVDKDVMSYDLARFGPLLENHPMFPERANITLAQVTSPTTMTTRTWERGAGLTLACGSAACSAAVSAARTGRTGRKVKINVASAKPPAMLSIEWRERDDHVIMTGPAEWEWSGRLDPATGCWSRDDAREVEAQ
|
Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan.
|
Q2K386
|
A5VPH9
|
OMP2B_BRUO2
|
Porin Omp2b
|
Brucella
|
MNIKSLLLGSAAALVAASGAQAADAIVAPEPEAVEYVRVCDAYGAGYFYIPGTETCLRISGYVRYDVKGGDDVYTGSDRKGWDKGARFALMFNTNSETELGTLGTYTQLRFNYTSNNSRHDGQYGDFSDDRDVADGSVSTGTDLQFAYITLGGFKVGIDESEFHTFTGYLGDIINDDVISAGSYRTGKIAYTFTGGNGFSAVIALEQGGEDVDNDYTIDGYMPHVVGGLKYAGGWGSIAGVVAYDSVIEEWATKVRGDVNITDRFSVWLQGAYSSAATPNQNYGQWGGDWAVWGGLKYQATQKAAFNLQAAHDDWGKTAVTANVAYELVPGFTVTPEVSYTKFGGEWKNTVAEDNAWGGIVRFQRSF
|
Forms passive diffusion pores that allow small molecular weight hydrophilic materials across the outer membrane.
|
A5VPH9
|
A6VBC3
|
MURA_PSEA7
|
UDP-N-acetylglucosamine enolpyruvyl transferase
|
Pseudomonas
|
MDKLIITGGNRLDGEIRISGAKNSALPILAATLLADTPVTVCNLPHLHDITTMIELFGRMGVQPIIDEKLNVEVDASSIKTLVAPYELVKTMRASILVLGPMLARFGEAEVALPGGCAIGSRPVDLHIRGLEAMGAQIEVEGGYIKAKAPVGGLHGGQFFFDTVSVTGTENLMMAAALANGRTVLQNAAREPEVVDLANCLNAMGANVQGAGSDTIVIDGVKRLGGARYDVLPDRIETGTYLVAAAATGGRVKLKDTDPTILEAVLQKLEEAGAHINTGNNWIELDMKGNRPKAVNIRTAPYPAFPTDMQAQFISMNAVAEGTGAVIETVFENRFMHVYEMNRMGAQILVEGNTAIVTGVPRLKGAPVMATDLRASASLVIAGLVAEGDTLIDRIYHIDRGYECIEEKLQLLGAKIRRVPG
|
Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine.
|
A6VBC3
|
P75145
|
PTMA_MYCPN
|
PTS system mannitol-specific EIIA component
|
Mycoplasma
|
MKLLKNNIYINVYLKNKQEIFEFVFKKFKEDGAVLDSFLPAIVERDKAASVAIGNYLFLPHPVYDEIANIQKEKMVFIGLKDVINIDGQPIKFICGLALKGEHQMDALQSLAIAFSDPEEVEKLVKDKDLTQDKVLEFLAKHN
|
The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II CmtAB PTS system is involved in D-mannitol transport.
|
P75145
|
P46644
|
AAT3_ARATH
|
Transaminase A
|
Arabidopsis
|
MKTTHFSSSSSSDRRIGALLRHLNSGSDSDNLSSLYASPTSGGTGGSVFSHLVQAPEDPILGVTVAYNKDPSPVKLNLGVGAYRTEEGKPLVLNVVRKAEQQLINDRTRIKEYLPIVGLVEFNKLSAKLILGADSPAIRENRITTVECLSGTGSLRVGGEFLAKHYHQKTIYITQPTWGNHPKIFTLAGLTVKTYRYYDPATRGLNFQGLLEDLGAAAPGSIVLLHACAHNPTGVDPTIQQWEQIRKLMRSKGLMPFFDSAYQGFASGSLDTDAKPIRMFVADGGECLVAQSYAKNMGLYGERVGALSIVCKSADVAGRVESQLKLVIRPMYSSPPIHGASIVAVILRDKNLFNEWTLELKAMADRIISMRKQLFEALRTRGTPGDWSHIIKQIGMFTFTGLNPAQVSFMTKEYHIYMTSDGRISMAGLSSKTVPHLADAIHAVVTKAV
|
Amino acid aminotransferase important for the metabolism of amino acids and Krebs-cycle related organic acids. No activity with D-Asp or D-Ala as amino donors. In plants, it is involved in nitrogen metabolism and in aspects of carbon and energy metabolism.
|
P46644
|
A5GIT5
|
RL14_SYNPW
|
50S ribosomal protein L14
|
unclassified Synechococcus
|
MIQQESFLTVADNSGAKRIQCIRVLGTNRRYAHVGDVIVAAVKDAMPNMGVKKSDVVKAVVVRTKATLRRDTGNSIRFDDNAAVIINDDKNPKGTRVFGPVARELRERNFTKIVSLAPEVI
|
Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome.
|
A5GIT5
|
P67284
|
RNY_STRP1
|
Ribonuclease Y
|
Streptococcus
|
MVNIILLIVSALIGLILGYALISIRLKSAKEAAELTLLNAEQEAVDIRGKAEVDAEHIKKTAKRESKANRKELLLEAKEEARKYREEIEQEFKSERQELKQLETRLAERSLTLDRKDENLSSKEKVLDSKEQSLTDKSKHIDERQLQVEKLEEEKKAELEKVAAMTIAEAREVILMETENKLTHEIATRIRDAERDIKDRTVKTAKDLLAQAMQRLAGEYVTEQTITSVHLPDDNMKGRIIGREGRNIRTLESLTGIDVIIDDTPEVVILSGFDPIRREIARMTLESLIADGRIHPARIEELVEKNRLEMDNRIREYGEAAAYEIGAPNLHPDLIKIMGRLQFRTSFGQNVLRHSVEVGKLAGILAGELGENVALARRAGFLHDMGKAIDREVEGSHVEIGMEFARKYKEHPVVVNTIASHHGDVEPDSVIAVLVAAADALSSARPGARNESMENYIKRLRDLEEIATSFDGVQNSFALQAGREIRIMVQPEKISDDQVVILSHKVREKIENNLDYPGNIKVTVIREMRAVDYAK
|
Endoribonuclease that initiates mRNA decay.
|
P67284
|
Q8X9Z2
|
MURE_ECO57
|
UDP-N-acetylmuramyl-tripeptide synthetase
|
Escherichia
|
MADRNLRDLLAPWVPDAPSRALREMTLDSRVAAAGDLFVAVVGHQADGRRYIPQAIAQGVAAIIAEAKGEATDGEIREMHGVPVIYLSQLNERLSALAGRFYHEPSDNLRLVGVTGTNGKTTTTQLLAQWSQLLGETSAVMGTVGNGLLGKVIPTENTTGSAVDVQHELAGLVDQDATFCAMEVSSHGLVQHRVAALKFAASVFTNLSRDHLDYHGDMEHYEAAKWLLYSEHHCGQAIINADDEVGRRWLAKLPDAVAVSMEDHINPNCHGRWLKATEVNYHDSGATIRFSSSWGDGEIESHLMGAFNVSNLLLALATLLALGYPLADLLKTAARLQPVCGRMEVFTAPGKPTVVVDYAHTPDALEKALQAARLHCAGKLWCVFGCGGDRDKGKRPLMGAIAEEFADVAVVTDDNPRTEEPRAIINDILAGMLDAGHAKVMEDRAEAVTCAVMQAKENDVVLVAGKGHEDYQIVGNQRLDYSDRVTVARLLGVIA
|
Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan.
|
Q8X9Z2
|
P00040
|
CYC_SCHGR
|
Cytochrome c
|
Schistocerca
|
MGVPQGDVEKGKKIFVQRCAQCHTVEAGGKHKTGPNLHGLFGRKTGQAPGFSYTDANKSKGITWDENTLFIYLENPKKYIPGTKMVFAGLKKPEERADLIAYLKESTK
|
Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.
|
P00040
|
O76041
|
NEBL_HUMAN
|
Actin-binding Z-disk protein
|
Homo
|
MRVPVFEDIKDETEEEKIGEEENEEDQVFYKPVIEDLSMELARKCTELISDIRYKEEFKKSKDKCTFVTDSPMLNHVKNIGAFISEAKYKGTIKADLSNSLYKRMPATIDSVFAGEVTQLQSEVAYKQKHDAAKGFSDYAHMKEPPEVKHAMEVNKHQSNISYRKDVQDTHTYSAELDRPDIKMATQISKIISNAEYKKGQGIMNKEPAVIGRPDFEHAVEASKLSSQIKYKEKFDNEMKDKKHHYNPLESASFRQNQLAATLASNVKYKKDIQNMHDPVSDLPNLLFLDHVLKASKMLSGREYKKLFEENKGMYHFDADAVEHLHHKGNAVLQSQVKYKEEYEKNKGKPMLEFVETPSYQASKEAQKMQSEKVYKEDFEKEIKGRSSLDLDKTPEFLHVKYITNLLREKEYKKDLENEIKGKGMELNSEVLDIQRAKRASEMASEKEYKKDLESIIKGKGMQAGTDTLEMQHAKKAAEIASEKDYKRDLETEIKGKGMQVSTDTLDVQRAKKASEMASQKQYKKDLENEIKGKGMQVSMDIPDILRAKRTSEIYSQRKYKDEAEKMLSNYSTIADTPEIQRIKTTQQNISAVFYKKEVGAGTAVKDSPEIERVKKNQQNISSVKYKEEIKHATAISDPPELKRVKENQKNISNLQYKEQNYKATPVSMTPEIERVRRNQEQLSAVKYKGELQRGTAISDPPELKRAKENQKNISNVYYRGQLGRATTLSVTPEMERVKKNQENISSVKYTQDHKQMKGRPSLILDTPAMRHVKEAQNHISMVKYHEDFEKTKGRGFTPVVDDPVTERVRKNTQVVSDAAYKGVHPHIVEMDRRPGIIVDLKVWRTDPGSIFDLDPLEDNIQSRSLHMLSEKASHYRRHWSRSHSSSTFGTGLGDDRSEISEIYPSFSCCSEVTRPSDEGAPVLPGAYQQSHSQGYGYMHQTSVSSMRSMQHSPNLRTYRAMYDYSAQDEDEVSFRDGDYIVNVQPIDDGWMYGTVQRTGRTGMLPANYIEFVN
|
Binds to actin and plays an important role in the assembly of the Z-disk. May functionally link sarcomeric actin to the desmin intermediate filaments in the heart muscle sarcomeres . Isoform 2 might play a role in the assembly of focal adhesion .
|
O76041
|
P69658
|
CA1A_CONPU
|
Alpha-conotoxin PIA
|
Chelyconus
|
SDGRDAAANDKATDLIALTARRDPCCSNPVCTVHNPQICG
|
Alpha-conotoxins bind to the nicotinic acetylcholine receptors (nAChR) and inhibit them . This toxin blocks mammalian nAChRs (alpha-6 or -3/beta-2 or -3 > alpha-3/beta-2 > alpha-3/beta-4) when heterologously expressed in Xenopus oocytes . Does not block the muscle nor the major neuronal nAChR alpha-4/beta-2 . Discriminates between nAChRs containing alpha-6 and alpha-3 subunits, being selective for alpha-6 . Also reduces the frequency of responses from the giant fiber (GF)-dorsal longitudinal muscle pathway in the D.melanogaster GF circuit, but has no effect on the GF-tergo trochanteral muscle pathway .
|
P69658
|
P97931
|
UNG_MOUSE
|
Uracil-DNA glycosylase
|
Mus
|
MIGQKTLYSFFSPTPTGKRTTRSPEPVPGSGVAAEIGGDAVASPAKKARVEQNEQGSPLSAEQLVRIQRNKAAALLRLAARNVPAGFGESWKQQLCGEFGKPYFVKLMGFVAEERNHHKVYPPPEQVFTWTQMCDIRDVKVVILGQDPYHGPNQAHGLCFSVQRPVPPPPSLENIFKELSTDIDGFVHPGHGDLSGWARQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNLSGLVFLLWGSYAQKKGSVIDRKRHHVLQTAHPSPLSVHRGFLGCRHFSKANELLQKSGKKPINWKEL
|
Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
|
P97931
|
A0A140JWS6
|
PTMI_PENSI
|
Penitrem biosynthesis cluster 1 protein I
|
Penicillium
|
MSSFKSQCEIIIDKPAHVVYDFVTTVSNWIGIHPACKGIEGDDGLDKEATVGLRFTETIDVRGWVFQCHWEVRKMVKDQYFEFSLPTDFILPPVYNTIITYIFDPIGDNKTRFIRTMINCTNADATPEQKADFADTDMHTDYLNAVKARLEMS
|
Part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase ptmG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase ptmC then forms 3-geranylgeranylindole (3-GGI) . Epoxidation by the FAD-dependent monooxygenase ptmM leads to a epoxidized-GGI that is substrate of the terpene cyclase ptmB for cyclization to yield paspaline . Paspaline is subsequently converted to 13-desoxypaxilline by the cytochrome P450 monooxygenase ptmP, the latter being then converted to paxilline by the cytochrome P450 monooxygenase ptmQ . Paxilline is converted to beta-paxitriol via C-10 ketoreduction by the short-chain dehydrogenase ptmH which can be monoprenylated at the C-20 by the indole diterpene prenyltransferase ptmD . A two-step elimination (acetylation and elimination) process performed by the O-acetyltransferase ptmV and ptmI leads to the production of the prenylated form of penijanthine . The FAD-linked oxidoreductase ptmO then converts the prenylated form of penijanthine into PC-M5 which is in turn transformed into PC-M4 by the aromatic dimethylallyltransferase ptmE . Five sequential oxidative transformations performed by the cytochrome P450 monooxygenases ptmK, ptmU, ptmL, ptmN and ptmJ yield the various penitrem compounds. PtmK, ptmU and ptmM are involved in the formation of the key bicyclic ring of penitrem C via the formation of the intermediates secopenitrem D and penitrem D. PtmL catalyzes the epoxidation of penitrem D and C to yield penitrem B and F, respectively. PtmJ catalyzes the last benzylic hydroxylation to convert penitrem B to prenitrem E and penitrem F to penitrem A .
|
A0A140JWS6
|
Q5FSM8
|
DPO4_GLUOX
|
DNA polymerase IV
|
Gluconobacter
|
MEQRRIVHIDMDAFYASVKQRDDPSLRGRPLAVGRGEARGVVAAASYEARRFGVRSAMPSVTAKRLCPELLFVPARFDVYRSVSAQIHDIFSRYTPLIQPLSLDEAYLDLTDHLGAYGSATLVADRIRADIHAETGLTASAGVSYNRFLAKLASDYRKPDGLFVITPAMGPEFVAALPVDAFHGIGPAMARKMRALGIETGADLRERDIETLTRHFGKAATFYYGISRGIDHRPVVVNRERKSLGTEQTYLRDLTSEADAHQALTQIAATLWGSAQRRQLQARTVTLKVKYADFRQITRARTLSAPVPSEEVLLETGQSLMAPLFPFVPGVRLLGLTLSGFHAAESPPCDQMELLF
|
Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.
|
Q5FSM8
|
Q2JT18
|
RL21_SYNJA
|
50S ribosomal protein L21
|
unclassified Synechococcus
|
MTYAIVETSGKQLWVEPGRFYDVDRLPGTEENSPLALSQVLLINHEGQVTLGHPYVPEAVVRARVLQHRRGNKIIVYKMRPKKGTRKKRGHRQPLTRVLIESIELNGTTLATAQSAPPSTSEATTDTTGIPAAEE
|
This protein binds to 23S rRNA in the presence of protein L20.
|
Q2JT18
|
C0ZG49
|
LSPA_BREBN
|
Signal peptidase II
|
Brevibacillus
|
MWYYLIAAVIIALDQFTKYLIVKYMELGESIPLIADVFHLTSHRNMGAAFGILQNRRWFFIAITAVVVIGIVISLIRLGKKQPRASLALSFVLGGAVGNFIDRAMSGQVVDFLDFTLIHFPIFNVADMAITIGVGILLLDVFLDGKKNR
|
This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
|
C0ZG49
|
Q45980
|
FLIP_CAUVC
|
Flagellar biosynthetic protein FliP
|
Caulobacter
|
MIRDLFKSVIGAKAEDLRRAAIISVLAAIACAIMPAAAMAQSAVNINLGTGAGLTERVVQLVGLMTVLSLAPSIVIMTTSFVRIVVVLGLLRTAIGVQQSPPNPVLISLALFLTAIVMAPTFERSYDAGIKPLLDQQMELPEAFEAASGPVKQFMLSQVDRDDLALFVRLSKIPQPRTAAETPLRVVTPAFMISELKRAFEIGFLLFIPFLVIDLVVASVLMSMGMMMLPPASISLPFKLIFFVLVDGWRLVAGSLVESFQRGAGG
|
May be a component of the flagellum. It is required for normal cell division. May be implicated in the secretion of virulence factors.
|
Q45980
|
G5E8Q8
|
AGRF5_MOUSE
|
G-protein coupled receptor 116
|
Mus
|
MRSPRTFTFYFLLLVICSSEAALSTPTEPIVQPSILQEHELAGEELLRPKRAAAAGDRVAEEYMVDIEISFENVSFLESIRAHLNNLSFPIRGTEADILNIAMTTVCTPAGNDLLCFCEKGYQWSEERCLHSLTCQDYDSALPGGYCSCLKGLPPQGPFCQLPEAFITLKLKVRLNIGFQEDLKNTSSALYRSYKTDLERAFRAGYRTLPGFRSVTVTQFTKGSVVVNYVVRVTSAPLPGSIHKANEQVIQNLNHTYKMDYNSFQGTPSNETKFTVIPEFIFEGDNVTLECETEFVTSNTSWYYGEKRSDIQNSDKYSIHTTVINNISLITRLTIYNFTQHDAGMYGCNVTLDIFEYGTVRKLDVTPIRILAKEERKVVCDNHPISLNCCSENIANWSSIEWKQEGKISILGNPESDLESSCSTYTLKADGTQCPSGSSGTTVIYTCEFVSAYGARGSKNIAVTFTSVANLTITRDPISVSEGQSFSITCLSDVSSFDEVYWNTSAGIKIHPRFYTMRRYQDGAESVLMVKTSTREWNGTYHCIFRYKNSYSIATKDVTVHPLPLVSDIMMDPLEASGLCTSSHQFKCCVEEDAGEEYAVTFHVDSSSFPAEREVIGKQACYTYSLPANLPRCPKDIAVFCHFTNAANSSVRSPSMKLKLIPRENVTCQDPIIGIGDPGKVIQKLCQFSGVYGSPGQAIGGTVTYKCVGTQWKEESRACISAPINGLLQVAKALIKSPTQDQKLPTYLRDLSVSAGKEEQDIRSSPGSLGAIISILDLLSTVPTQVNSEMMRDILATINVILDKSALNSWEKLLQQQSNQSSQFLHSVERFSQALQLGDSTPPFLAHPNVQMKSMVIKRGHPQIYQQQFIFKDSDLWGDVAIDECQLGNLQPDSSIVTVAFPTLKAILAQDVQRKTSSNSLVMTTTVSHNIVKPFRISMTFKNNHRSGGKPQCVFWNFSLANNTGGWDSSGCSVEDDGRDNRDRVFCKCNHLTSFSILMSPDSPDPGSLLKILLDIISYIGLGFSIVSLAACLVVEAMVWKSVTKNRTSYMRHICIVNIAFCLLIADIWFIVAGAIHDGRYPLNETACVAATFFIHFFYLSVFFWMLTLGLMLFYRLIFILHDASKSTQKAIAFSLGYGCPLIISSITVGVTQPQEVYMRKNACWLNWEDTRALLAFAIPALIIVVVNVSITVVVITKILRPSIGDKPGKQEKSSLFQISKSIGVLTPLLGLTWGFGLATVIQGSNAVFHIIFTLLNAFQGLFILLFGCLWDQKVQEALLHKFSLSRWSSQHSKSTSIGSSTPVFSMSSPISRRFNNLFGKTGTYNVSTPETTSSSLENSSSAYSLLN
|
Receptor that plays a critical role in lung surfactant homeostasis . May play a role in controlling adipocyte function .
|
G5E8Q8
|
A8GI21
|
ACPS_SERP5
|
4'-phosphopantetheinyl transferase AcpS
|
Serratia
|
MAVLGLGTDIVEMARIEAVVERSGDRLARRVLSEAEWELYQQHQQPVRFLAKRFAVKEAVAKAFGTGIRNGLAFNQFEVFNDGLGKPNIRLHARAAELAKEMGVTSIHVSLADERRYACATVIIEG
|
Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
|
A8GI21
|
B7L0X9
|
CYSN_METC4
|
Sulfate adenylate transferase
|
Methylorubrum
|
MTIHQSPEAFGYDAFLRQHQNKEVLRFITCGSVDDGKSTLIGRLLHDTKQIFDDQVTALQRDSRKHGTQGGEVDFALLVDGLQAEREQGITIDVAYRFFSTDRRSFIVADTPGHEQYTRNMATGASTADLAVILVDARHGLTRQSRRHALLVSLLGIRRVALAINKMDLVGWSQDKFEAIVSGFQAFAAPLNFTEVRAIPLSAKNGDNVVLPGTAATWYTDVPLLRYLEEVPVKSEERAAAFRMPVQWVNRPNSDFRGFSGLIASGSVAPGDAVTVAPSGKTSTIARIFTADGDLERASEGQSVTLVLADEVDASRGAVIATSDAPLTLTDSLDVRLFWAAESDLVPGANLWAKVGTQTVNAVVKAVHRRIDPETGQAGPADKLAVNDIGDVTLTLDRQIAVDPYAENRDTGSLILIDRETTDTAALGLVQTIVASSKVAPAPTASVTASAEPARSGGLLAGLKRLFGG
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With CysD forms the ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric-sulfuric acid anhydride bond driven by GTP hydrolysis by CysN coupled to ATP hydrolysis by CysD.
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B7L0X9
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Q65RB5
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NADE_MANSM
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NH(3)-dependent NAD(+) synthetase
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Basfia
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MKTAAYADYLIQWLENQRTELYGMDGYTLGVSGGIDSAVCAHLAARTGAPVQALILPAEVTSPSDVADAQATLESAGIDGQIISIAPWYDLIMQQLSPVLNSEPERVNVLKGNLMARLRMIALFTTAQSHRSIVLGTDNAAEWLTGYFTKFGDGAADVLPLAGLRKEQVFELGRYLGVPQSVLDKKPSAGLWAGQTDEAEMGVTYAEIDAYLRGETVSPQALQQIRFWHNRSHHKRMLPPKPKSPDEAEC
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Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
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Q65RB5
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Q5JDN5
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DGGGP_THEKO
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Geranylgeranylglycerol-phosphate geranylgeranyltransferase
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Thermococcus
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MEFKAFIEITRPHNCLLAGIVGVLGSIVAAGGLPELKTAILVFLVVFLGCAGGNTINDYFDYEIDKINRPERPLPRGAMSRKAALWYSVALFATGIVLAWFINIWDFLLAIVAYVTMFIYAWKLKPMPFIGNVVVASLTGATPLYGAIAVGEIGLAGTLALCAFLVNVAREVIKDIEDIEGDMAKGAKTLPILIGRKRAAYVGALFAILTVVASFLPIKAGIGLGYLAMLPVDAVILYSAFLILRSQDRETAHRAQILLKVSVFLAVVAFLIASLVR
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Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids.
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Q5JDN5
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P56502
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BAR3_SCHCM
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Pheromone B alpha 3 receptor
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Schizophyllum
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MLDPTYPLFPTFAFLGFVLALVPLPWHLQAWNSGTCFFMVWTALGCLNQFVNSIVWKDNAINSAPIWCEISIRITMGLSVGLPASSLCIIRRLYHIAKVRAVSHTRAEKMRVIIIDALICVLFPLVYIAMQYIVQGHRFNILENVGCYPAVFNTPVTYVVSYIWPVLIGMVSATYSVLALIEFNRHRLQFSQFLHSNSTLSVSRYLRLMALAMTEMCCTVPLGIFVIVLNCTSTPIEPWVSLKATHYWYSRVDQYPAVVWRSSHLVVVCNELTRWLAPVSAMLFFAYFGFAQEARRNYAAAWAWACRALGLPERIATLPTTKSKGPGFAEKFAAKAKGLSSFNVKDFTSEFSSKAHDFTSKAKQYTLPRPMPQTPSSSGFSSSESTRFGSSVDGKELPSPTTKEFSSPIPIHLSGMQTLVSFDSNKDLPSPPAYDVEAQYGPYNIDNRVSYHIADAGVRASYPMGVAYSSDSEHRRINPHATFTSANNDTDEPTSPALPDTPSSCSSSATFSTLQSRDFIVLPSTTDVTRDTGSLPIRRSPAGPPRLPSLSQLFGISSMRAEGRDVEAQVQDVATGTAAPTTTAPAPASTTIAPATTTATAPTTTANIQRGEPDVPTSPRTHRASV
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Receptor for the BAP3 pheromone, a prenylated mating factor.
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P56502
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Q9BI40
|
GATC_CAEEL
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Glutamyl-tRNA(Gln) amidotransferase subunit C, mitochondrial
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Caenorhabditis
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MNLIFTRIIRRFGEGKRKTPFPGDPILVPDEPYDSKIQESQLSPMPQIDAKLINHLERLSLVRFDSEQAVANLRSSIRVAKRLELVDVEGVEPMHTVWEDQECPTFEDVEEDPLPIEEVFRNASLRFDDFFVTPPGNLPLESKERFDLNVINEWDTIGKPVAPEVKLTRMTERKK
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Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
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Q9BI40
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Subsets and Splits
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