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AlphaFoldDB
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B8I7Y3
RS19_RUMCH
30S ribosomal protein S19
Ruminiclostridium
MSRSVKKGPYVLDSLLKKIEEMNKANDKKVIKTWSRASTIFPQMVGHTIAVHDGKKHVPVYITEDMVGHKLGEFAPTRTYKGHSGNEKSTSLR
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
B8I7Y3
Q72NQ4
RL21_LEPIC
50S ribosomal protein L21
Leptospira
MYAIISVGNRQYKVTQDQEFLTEKTGKNAGESFDAKVLLFAESNNKVHIGQPELKTARVSLKVLEDVKGDKIHGYVYKRRKNYQKAWGHRQQLQKVKVVSLSAV
This protein binds to 23S rRNA in the presence of protein L20.
Q72NQ4
Q604V5
MURD_METCA
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase
Methylococcus
MHDRLIDENPTCGFVRLGLDVRSRVIVLGLGATGLSTVRFLRCHGFECAVMDSRLAPPGLQDLREAFPDVPLFLGDFSRSALAAATHLVVSPGLSLDLAEIRESHRCGVRVFGDLDLFACCVRAPVVAITGANGKSTVTTLVGLMAKAAGVNAAVGGNLGTPMLDLLDAAAELYVLELSSFQLERSELFEADVATVLNISPDHMDRYPDLASYAEAKRRVFRGEGLMVLNQDDPLVAAMYRPGRRAVRFGLGSGDELDYSLARWEGRAWLLAKGVPLLPADEVRIKGRHNLANALAAVAIADACGFDRQAMVGVLRTFPGLDHRMQWVADIGGVAYVNDSKATNVGACIAALSGLEGKVVLIAGGDGKGADFSSLVPVAAEKLRAAVLMGRDGPLIDEVLKGVVPTIRVKTMFEAVRAARGVAQSGDTVLLAPACASLDQYEDYQERGRDFAATVRSLA
Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
Q604V5
Q08C75
VACHA_DANRE
Solute carrier family 18 member 3-A
Danio
MATEESGGLAQTAAVKLSEMGERTKQLGNAIQDPERQRRIILVIVCVALLLDNMLYMVIVPIVPDYLAHLESESEQAHVKGNSSINITQNENFDLQIGVLFASKAILQLLVNPLTGTFIDRVGYDIPLLIGLSIMFVSTCIFAFAENYATLFMARSLQGLGSAFADTSGIAMIADKYAEESERSRALGIALAFISFGSLAAPPFGGVLYEFAGKRFPFIALACVCLADGILCLTVLKPFSSRTRENMPVGTPIYKLMIDPYIAVVAGALTTCNIPLAFLEPTIANWMEETMNASQWQIGITWLPAFFPHILGVYLTVKLAAKYPHLQWFYGALGMVIIGASSCIVPACKNFEQLIIPLCGVCFGIALVDTALLPTLAFLVDVRHVSVYGSVYAIADISYCVAYALGPIVAGKIVHDLGFVQLNLGMGLANVLYAPALLLLRNVSLMKPSHSERNMLLEEGATGLYDTIRMEERQRKKHGYSSSGNCVPIDENGTFAGQSKSFSEEETSEPEYI
Involved in acetylcholine transport into synaptic vesicles.
Q08C75
Q2G4K2
TSAD_NOVAD
tRNA threonylcarbamoyladenosine biosynthesis protein TsaD
Novosphingobium
MALILGIESSCDETAAAVIDSNGASLEARIVAQRIASQDEAHRPYGGVVPEIAARAHAEVLSPMIAAVLADAGIGLDDLDAIAATAGPGLIGGVMVGLVTGKALAMAADKPLIAVNHLEGHALSPRLAEPSLQYPYLLLLVSGGHCQILEVAGVGQFRRLATTIDDALGEAFDKTAKILGLGYPGGPAVERMAREGNPKAVPLPRPLVGSGEPHFSFAGLKSAVMRAKDAGVHGDADIAASFQQAAIDCVIDRTRIALETASPGMTALVVAGGVAANAALRGALEGLAESHGLSLVAPPPKLCTDNAAMIGWAGAERLALGYVDPLDVAARPRWPLDENAAPVRGAGVKA
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.
Q2G4K2
Q9HCY8
S10AE_HUMAN
S100 calcium-binding protein A14
Homo
MGQCRSANAEDAQEFSDVERAIETLIKNFHQYSVEGGKETLTPSELRDLVTQQLPHLMPSNCGLEEKIANLGSCNDSKLEFRSFWELIGEAAKSVKLERPVRGH
Modulates P53/TP53 protein levels, and thereby plays a role in the regulation of cell survival and apoptosis. Depending on the context, it can promote cell proliferation or apoptosis. Plays a role in the regulation of cell migration by modulating the levels of MMP2, a matrix protease that is under transcriptional control of P53/TP53. Does not bind calcium.
Q9HCY8
Q2PFW9
NOVA1_MACFA
Ventral neuron-specific protein 1
Macaca
MMAAAPIQQNGTHTGVPIDLDPPDSRKRPLEAPPEAGSTKRTNTGEDGQYFLKVLIPSYAAGSIIGKGGQTIVQLQKETGATIKLSKSKDFYPGTTERVCLIQGTVEALNAVHGFIAEKIREMPQNVAKTEPVSILQPQTTVNPDRIKQVKIIVPNSTAGLIIGKGGATVKAIMEQSGAWVQLSQKPDGINLQERVVTVSGEPEQNRKAVELIIQKIQEDPQSGSCLNISYANVTGPVANSNPTGSPYANTAEVLPTAAAAAGLLGHANLAGVAAFPAVLSGFTGNDLVAITSALNTLASYGYNLNTLGLGLSQAAATGALAAAAASANPAAAAANLLATYASEASASGSTAGGTAGTFALGSLAAATAATNGYFGAASPLAASAILGTEKSTDGSKDVVEIAVPENLVGAILGKGGKTLVEYQELTGARIQISKKGEFVPGTRNRKVTITGTPAATQAAQYLITQRITYEQGVRAANPQKVG
Functions to regulate alternative splicing in neurons by binding pre-mRNA in a sequence-specific manner to activate exon inclusion or exclusion. It binds specifically to the sequences 5'-YCAY-3' and regulates splicing in only a subset of regulated exons. Binding to an exonic 5'-YCAY-3' cluster changes the protein complexes assembled on pre-mRNA, blocking U1 snRNP binding and exon inclusion, whereas binding to an intronic 5'-YCAY-3' cluster enhances spliceosome assembly and exon inclusion. Binding to 5'-YCAY-3' clusters results in a local and asymmetric action to regulate spliceosome assembly and alternative splicing in neurons. Binding to an exonic 5'-YCAY-3' cluster changed the protein complexes assembled on pre-mRNA, blocking U1 snRNP (small nuclear ribonucleoprotein) binding and exon inclusion, whereas binding to an intronic 5'-YCAY-3' cluster enhanced spliceosome assembly and exon inclusion. With NOVA1, they perform unique biological functions in different brain areas and cell types. Autoregulates its own expression by acting as a splicing repressor. Acts to activate the inclusion of exon E3A in the glycine receptor alpha-2 chain and of exon E9 in gamma-aminobutyric-acid receptor gamma-2 subunit via a distal downstream UCAU-rich intronic splicing enhancer. Acts to regulate a novel glycine receptor alpha-2 chain splice variant (alpha-2N) in developing spinal cord.
Q2PFW9
Q48MQ4
RUTA_PSE14
Pyrimidine monooxygenase RutA
Pseudomonas
MDIGIFIPIGNNGWLISSNAPQYMPTFELNKQIVQTAEGYGFDFALSMIKLRGFGGKTEFWEHNLESFTLMAGLAAVTSKIQLFATVATLTIPPAIAARMASTIDSISNGRFGINLVTGWQKPEYEQMGLWPGDEFFHTRYEYLAEYAQVLRDLWATGSSDFKGEHFSMQDCRVSPRPKADMKLICAGQSEAGMAFSAQYADYNFCFGKGVNTPTAFAPTAQKLIEANEKTGRNVTSCVLFMIIADDTDEAARARWEHIKDGADEEAIAWLSEKGSADKSAGSNLRQMADPTSAVNINMGTLVGSWATVARMLDEVASVPGTQGVMLTFDDFVKGVEDFGEKIQPLMTSRKHIAQLKEVV
Catalyzes the pyrimidine ring opening between N-3 and C-4 by an unusual flavin hydroperoxide-catalyzed mechanism, adding oxygen atoms in the process to yield ureidoacrylate peracid, that immediately reacts with FMN forming ureidoacrylate and FMN-N(5)-oxide. The FMN-N(5)-oxide reacts spontaneously with NADH to produce FMN. Requires the flavin reductase RutF to regenerate FMN in vivo.
Q48MQ4
Q1G9D6
MIAA_LACDA
Isopentenyl-diphosphate:tRNA isopentenyltransferase
Lactobacillus
MQKVVAIVGPTAVGKTSLAIEIAKKLDGEIVSGDSMQIYKEVAIGTAKASREEQAEVKHYLVDAHSVFEDFSVKNFVDEARSAIGEIAGKGKLPIIAGGTGFYVNALLNDMQLGDKEEEAASVDPEWEVFLAANGPQALWEELNKKDPEAAKKIPVANSRRSLRALSVISRTGGLFSKQQAEIKTRYDYLIIGLNSDREAIYQRINQRVDLMMEAGLLEEARFVYEHRAGEHQVLQAIGYKEFFPYFAGEASLETCVMALKTASRRYAKRQLTYFRNKLPVEWYDPLTDPNCANRIAVRIEEWMKEEK
Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Q1G9D6
B9KIX9
ISPH_ANAMF
4-hydroxy-3-methylbut-2-enyl diphosphate reductase
Anaplasma
MEAVQQNHSVCRGYCGVMLRSRSGGFFRRGFMLGNVEVILARPRGFCAGVERAVRTLESVASRYAGTREVYALHEIVHNLHVVNSFKKMGVKFVSALHEVPEGAVLVFSAHGVSQQIKEESRRKGLTVVDATCPLVTKVHLEIQRYDKSGYQVILVGHKGHREVEGSMGQVSNPVVLVQNVQDVQSIKTPSAAKLAYVTQTTLSMDDTAEIINALKLRFPQIVGPDLRDICYATQNRQTAVKAMSQMVDVVLAIGSKNSSNSNRLLDLAKAQNARAYLIDSYRNIDLEWLIGARRIGITAGASAPEILVQEVIDYLGLHANLKVRTMDGVSENITFKLPELD
Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
B9KIX9
C0HKT2
CORZ_AGRIP
Corazonin
Agrotis
MSANVTLLLIFVTLASVTAQTFQYSRGWTNGKRDQGHLRPELKELINNMDKILSPCQKNKLKYLLEGKPVTERLLIPCDILDTEEYPRALTERNLNAMMDAFY
Cardioactive peptide. Corazonin is probably involved in the physiological regulation of the heart beat.
C0HKT2
Q4IJM4
CSN5_GIBZE
COP9 signalosome complex subunit 5
Fusarium
MEASALKAWELDNNVQLVDPKRDALYNFDADAQKAINKEQPWKQDPSHFKHVRISATALIKMTMHARSGGNLEVMGLMQGYTQGDTFIVTDAFRLPVEGTETRVNAQDEANEYIVEYLDLCRAQGRQENVVGWYHSHPGYGCWLSGIDVDTEAMQQQFQDPFLAVVIDPDRTINSGKVDIGAFRTYPADYKPSGGVTSDGFQAVPLAKAAEFGAHASRYYSLEVSHFKSSLDSHLLELLWHKYWVQTLSQNPLITNRDYGNKQLLDLSSKIKEATTGITRNRAGQGMMMGMSTKSSDKAVDKLAKEANLIASKERSGLIANQVKASLFNDLGSKANPTSE
Catalytic Component of the COP9 signalosome (CSN) complex that acts as an regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunit of SCF-type E3 ubiquitin-protein ligase complexes.
Q4IJM4
C4L9M9
HFQ_TOLAT
RNA-binding protein Hfq
Tolumonas
MAKGQSLQDPFLNALRRERIPVSIYLVNGIKLQGQVESFDQFVILLKNTVSQMVYKHAISTVVPARPVAHHTAPAAGDSDSQSEE
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.
C4L9M9
Q2NW34
OBG_SODGM
GTP-binding protein Obg
Sodalis
MKFVDEATILAAAGDGGNGCVSFRREKYIPRGGPDGGDGGDGGDVWLLADENLNTLIDYRFEKNFRAERGQNGQSCDCTGKRGKDIIIKVPVGTRVLDSGTNEVMGDMTRHAQRLMVAKGGFHGLGNTRFKSSVNRAPRQKTGGTKGEIREIQLELMLLADVGMLGLPNAGKSTFIRAVSAAKPKVADYPFTTLVPSLGVVRMDNEQSFVVADIPGLIEGAADGAGLGIRFLKHLERCQVLLHLIDLAPVDESDPVENARIIVTELERYSENLASKPRWLVFNKADLLDPEEAASRANAIAKVLGWEEKYYLISAANRDGVKALCWDVMAFINAHPKEQAAPEAAPEKVEFMWDDYHRDQLQQEEAEETLDDDWDEDGVETIYQR
An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control.
Q2NW34
P07800
CHEZ_SALTY
Chemotaxis protein CheZ
Salmonella
MMQPSIKPADEGSAGDIIARIGSLTRMLRDSLRELGLDQAIAEAAEAIPDARDRLDYVVQMTAQAAERALNSVEASQPHQDAMEKEAKALTQRWDEWFDNPIELSDARELVTDTRQFLRDVPGHTSFTNAQLLDIMMAQDFQDLTGQVIKRMMDVIQEIERQLLMVLLENIPEQSARPKRENESLLNGPQVDTSKAGVVASQDQVDDLLDSLGF
Plays an important role in bacterial chemotaxis signal transduction pathway by accelerating the dephosphorylation of phosphorylated CheY (CheY-P). Acts on free CheY-P.
P07800
Q8UAA5
GPMI_AGRFC
2,3-bisphosphoglycerate-independent phosphoglycerate mutase
Agrobacterium tumefaciens complex
MRTPKPVVLTILDGWGLNEDTSSNAPVLANTPTMDRLFATCPNATLTTFGPNVGLPTGQMGNSEVGHTNIGAGRIVAMDLGQIDLAIEDGSFFRNAAMLDFAATVKAAGGVAHLMCVVSDGGVHGHILHGQAAVKLMVSHGLKVVVHAITDGRDVAPQSAEDFVAALVASLPQGASIGTVIGRYYAMDRDNRWERVEKAYDAMVLGKGEHARDAVSAVAQSYANKVTDEFILPTVIDGYEGFKAGDGLFCLNFRADRAREILLAIGADDFDGFAREKPVLSALLGMVEYSTRHSDFMTTAYPKRDIVNTLGAWVAKQGLTQFRLAETEKYPHVTFFLNGGKEEPEVGEDRFMPKSPKVATYDLQPEMSAAEVTEKFVEVIGKGYDLIVTNYANPDMVGHTGDLQAAIKACEAVDRGLGAVVAALEKVGGAMLVIADHGNCETMVDPVTGGPHTAHTTNPVPVILFGGPEGAKVHDGILADVAPTLLQLMNVPLPPEMTGKSLIDL
Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Q8UAA5
A0JD36
TRDV2_HUMAN
T cell receptor delta variable 2
Homo
MQRISSLIHLSLFWAGVMSAIELVPEHQTVPVSIGVPATLRCSMKGEAIGNYYINWYRKTQGNTMTFIYREKDIYGPGFKDNFQGDIDIAKNLAVLKILAPSERDEGSYYCACDT
V region of the variable domain of T cell receptor (TR) delta chain that participates in the antigen recognition . Gamma-delta TRs recognize a variety of self and foreign non-peptide antigens frequently expressed at the epithelial boundaries between the host and external environment, including endogenous lipids presented by MH-like protein CD1D and phosphoantigens presented by butyrophilin-like molecule BTN3A1. Upon antigen recognition induces rapid, innate-like immune responses involved in pathogen clearance and tissue repair . Binding of gamma-delta TR complex to antigen triggers phosphorylation of immunoreceptor tyrosine-based activation motifs (ITAMs) in the CD3 chains by the LCK and FYN kinases, allowing the recruitment, phosphorylation, and activation of ZAP70 that facilitates phosphorylation of the scaffolding proteins LCP2 and LAT. This lead to the formation of a supramolecular signalosome that recruits the phospholipase PLCG1, resulting in calcium mobilization and ERK activation, ultimately leading to T cell expansion and differentiation into effector cells . Gamma-delta TRs are produced through somatic rearrangement of a limited repertoire of variable (V), diversity (D), and joining (J) genes. The potential diversity of gamma-delta TRs is conferred by the unique ability to rearrange (D) genes in tandem and to utilize all three reading frames. The combinatorial diversity is considerably increased by the sequence exonuclease trimming and random nucleotide (N) region additions which occur during the V-(D)-J rearrangements .
A0JD36
Q9EUR1
SCPB_STRMT
Segregation and condensation protein B
Streptococcus
MSTLAKIEALLFVRGEDWIRVRQLAELLSLPPTGIQQSLEKLSQKYEKDLDSSLDLIETGGAYRLVTKPQFSEILKEYSKAPINQSLSRPALETLSIIAYKQPITRIEIDAIRGVNSSGALAKLQAFDLIREDGKKEVLGRPNLYVTTDYFLDYMGINHLEELPVIDELEIQAQESQLFGERIEEDENQ
Participates in chromosomal partition during cell division. May act via the formation of a condensin-like complex containing Smc and ScpA that pull DNA away from mid-cell into both cell halves.
Q9EUR1
O30641
MTMC1_METBA
Monomethylamine corrinoid protein 1
Methanosarcina
MANQEIFDKLRDAIVNQNVAGTPELCKEALAAGVPALDIITKGLSVGMKIVGDKFEAAEIFLPQIMMSGKAMSNAMEVLTPELEKNKKEGEEAGLAITFVAEGDIHDIGHRLVTTMLGANGFQIVDLGVDVLNENVVEEAAKHKGEKVLLVGSALMTTSMLGQKDLMDRLNEEKLRDSVKCMFGGAPVSDKWIEEIGADATAENAAEAAKVALEVMK
Acts as a methyl group carrier between MtmB and MtbA.
O30641
Q57TL0
RIHC_SALCH
Purine/pyrimidine ribonucleoside hydrolase
Salmonella
MTASLHIILDTDPGIDDAAAIAAALFAPQLDLQLITTVAGNVSVEKTTRNALQLLHFWNSDIPLAQGAATPLLRPLRDAAYVHGESGMEGYDFVDHQRQPLAKPAFIAIRDVLMNAPEPMTLVAIGPLTNIALLLMHYPECACNIRRLVLMGGSAGRGNFTPNAEFNIAVDPEAAALVFRSGLEIVMCGLDVTNQAMLSPDFLNKLPALNRTGKMLHSLFNHYRSGSMRTGVRMHDLCAIAWLVRPELFTLQSCFVAVETQGEYTAGTTVVDIEGRLGQPANAQVALALDVDGFRQWVAEVFAYAP
Hydrolyzes both purine and pyrimidine ribonucleosides with a broad-substrate specificity.
Q57TL0
Q5E2Y8
UNG_ALIF1
Uracil-DNA glycosylase
Aliivibrio
MALTWNSIISAEKKKAYYQSMSEKIDAQRSLGKSIFPKEEHIFTAFDLTPFHDVKVVILGQDPYHGEGQAHGLSFSVLPGVKIPPSLRNMYKELAEDIPGFTIPEHGYLKTWAEQGVLLLNTVLTVEEAKAHSHAKFGWETFTDAIIKKINDDMEGVIFLLWGAHAQKKGANIDTSRHFILQAPHPSPLSAHRGFFGCKHFSQTNELLRKQNLSEINWGAVTSS
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.
Q5E2Y8
Q6HPA4
PURL_BACHK
Phosphoribosylformylglycinamidine synthase subunit II
Bacillus cereus group
MSLMLEPNPTQIKEERIYAEMGLTDEEFAMVEKILGRLPNYTETGLFSVMWSEHCSYKNSKPVLRKFPTTGERVLQGPGEGAGIVDIGDNQAVVFKMESHNHPSAIEPYQGAATGVGGIIRDVFSMGARPVALLNSLRFGELQSPRVKYLFEEVVAGIAGYGNCIGIPTVGGEVQFDPCYEGNPLVNAMCVGLINHEDIKKGQAHGAGNTVMYVGASTGRDGIHGATFASEELSESSEAKRPAVQVGDPFMEKLLIEACLELIQLDALVGIQDMGAAGLTSSSAEMASKAGMGIEMYLDDVPQRETGMTPYEMMLSESQERMLIVVKKGREQEIVDLFEKYGLAAVTMGKVTEDKMLRLFHKGEMVAEVPADALAEEAPIYHKPSKEAAYFAEFQQMKMETPKVENYKETLFALLQQPTIASKEWVYDQYDYQVRTSTVVTPGSDAAVVRVRGTEKGLAMTTDCNSRYIYLDPEVGGKIAVAEAARNIVCSGGEPLAITDCLNFGNPEKPEIFWQIEKSVDGMSEACRMLQTPVIGGNVSMYNERSGEAVYPTPTVGMVGLVHDLKHVTTQEFKQAGDLVYVIGETKAEFGGSELQKMLHGKIFGQSPSIDLDVELKRQKQVLAAIQAGLVQSAHDVAEGGLAVAISESAIGANGLGATVKLDGEATAALFAESQSRFVITVKRENKEAFEKAVEAIQVGEVTNTNEVTIHNEKNEVLLTANVDEMRKAWKGAIPCLLK
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.
Q6HPA4
A7GQZ8
HUTI_BACCN
Imidazolone-5-propionate hydrolase
Bacillus cereus group
MLDILLTNIGQLLTMDQEDGVLRQEAMKTLPVIESGAVGIKDGVIMFVGTAEEAKGLQAREIIDCEGKVVSPGLVDPHTHLVFGGSRENEIALKLQGVPYLEILEQGGGILSTVNATKKASKEELVKKANFHLDRMLSFGVTTVEAKSGYGLDDETEWKQLEVVAQLQKEHPIDLVSTFLGAHAVPKEYKGKSKEFLQWMLDLLPAIKEKELAEFVDIFCETGVFSVEESKEFLLEAKELGFDVKIHADEIDPLGGAEAAAEIGAASADHLVGASDKGIEMLANSNTVATLLPGTTFYLNKESFARGRKMIDEGVAVALATDFNPGSCPTENIQLVMSIAMLKLKMTPEEVWNAVTVNSAYAINRGDVAGKIRVGRKADLVLWDAHHYAYVPYHYGVSHVNTVWKNGNLAYTRGDKAWSKATI
Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate. It is the third step in the universal histidine degradation pathway.
A7GQZ8
Q9FIA0
U76C2_ARATH
Cytokinin-N-glucosyltransferase 2
Arabidopsis
MEEKRNGLRVILFPLPLQGCINPMLQLANILHVRGFSITVIHTRFNAPKASSHPLFTFLQIPDGLSETEIQDGVMSLLAQINLNAESPFRDCLRKVLLESKESERVTCLIDDCGWLFTQSVSESLKLPRLVLCTFKATFFNAYPSLPLIRTKGYLPVSESEAEDSVPEFPPLQKRDLSKVFGEFGEKLDPFLHAVVETTIRSSGLIYMSCEELEKDSLTLSNEIFKVPVFAIGPFHSYFSASSSSLFTQDETCILWLDDQEDKSVIYVSLGSVVNITETEFLEIACGLSNSKQPFLWVVRPGSVLGAKWIEPLSEGLVSSLEEKGKIVKWAPQQEVLAHRATGGFLTHNGWNSTLESICEGVPMICLPGGWDQMLNSRFVSDIWKIGIHLEGRIEKKEIEKAVRVLMEESEGNKIRERMKVLKDEVEKSVKQGGSSFQSIETLANHILLL
Involved in the N-glucosylation of cytokinins. Catalyzes the formation of both the 7-N and the 9-N-glucosides.
Q9FIA0
A0KV76
FADJ_SHESA
3-hydroxyacyl-CoA dehydrogenase
Shewanella
MEKTFNLTRREDGIAILMMDVPGETMNTLKAEFGPEISEILSEIKRDSSIRGLVLISGKKDSFVAGADISMLDACQTAGDAKALSQQGHVVFNELEALNIPVVAAIHGACLGGGLELALACHQRVCSDDGKTMLGVPEVQLGLLPGGGGTQRLPRLVGITTALDMMLTGKQIRPKQALKMGLVNDVVPQTILLQTAVEMALAGKRTAKPVKKSLVNQLLEGTGFGRNIIFDQAAKQVVKKTQGNYPAPAKIIDCVRQGMAKGMQKGLEVEASHFAELVVSKESEALRSIFFATTEMKKETGAEGATPRKVKKAVILGGGLMGGGIASVTTTKAKIPARVKDINEKGLSNALSYAYKLLDKGVKRRHMTPAVRDNLMALMTTTTEYKGVKDADIVVEAVFEDLALKHQMVKDIERECGEHTIFASNTSSLPIGQIAQAASRPENVIGLHYFSPVEKMPLVEVIAHAKTSPETIATTVAFARKQGKTPIVVQDGAGFYVNRILALYMNEAAQLLLEGQSIEHLDKALVKFGFPVGPITLLDEVGIDVGAKIAPILEKELGERFKAPAAFDKLLSDDRKGRKNGKGFYQYAAGNKASSKKKAVDESVYAVLGIKPGMDKDLSAVAERCVVQMLNEAVRCLDDGIIASPRDGDIGAIFGIGFPPFLGGPFHYIDTLGADNLVNILERYQAQYGDRFEPCPRLKAMAAEKARFF
Catalyzes the formation of a hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3-hydroxyacyl-CoA dehydrogenase activities.
A0KV76
O17972
NPHP1_CAEEL
Nephronophthisis homolog
Caenorhabditis
MSIFGSILSLQDAINRFPQFEYQINRLEKEQKDTEAASRASFRKHFVRQCQELHRQLDDHRNRIEKAKTDETYKKENALEQLDKLKQRLTALSPEKEQLSFSVSVDSQSEEEKPKMAAIGRRKSTMYNDDESEDSDNDSEIIETDVQLDDPLPSQPQPPQQQHQQPQPKPRQPITITKPLESKTLNERQELDEVISRLQNPSRGDSGEVMEPVVVRGNVFVAIDSWDAEAEGDLELIKGKKYRITQTRSDGWWTALDEYGQRGLVPKTYLQHVKEKPKNVPSKVSSRLGVRDSVIGISTTTDPSRREANRQASRVDDCLGKAYDNDTHLSLVCHMAPRLSTSNIGFHDLFWSHYKDQVYKRTVHISKIIRLVRFEKMPLIEHKALVRMALVDITNPKSTQIVSNVHTLVPRVKSSTWYFEKKESQTRSCIEFSDFVLRSNYRSPTVVLVVEASHLVKTQIGIEEKSLGHTYLRLIIDDKAVPSRTNVLYLDDEVMTKMKLPEASKRRVLVQVMDVPKDKVSYVDSLPDVIVFNALYLPFFHFYRRRAGTILIRDNRNPLSAEFISDPLLSVFPFVCDQHDIMDIMLKIWKTKKKVLAKKNEAEQTAEFFQTFLHTAFFIHGIRMISYDVKDDLTLSIRQQTMQRFVDALNKGLFKQFIADQQCKPINIIDYSLDLLGNHSID
Plays a role in the extension of dendrites from phasmid ciliated sensory neurons . May be necessary for initial assembly of the cilium.
O17972
P36501
LANA_STRPY
Antibacterial peptide SA-FF22
Streptococcus
MEKNNEVINSIQEVSLEELDQIIGAGKNGVFKTISHECHLNTWAFLATCCS
Lanthionine-containing peptide antibiotic (lantibiotic) active on certain Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores.
P36501
Q6G1B6
NTPPB_BARQU
7-methyl-GTP pyrophosphatase
Bartonella
MMADTLILASLSSYRAQLLKKAGLNFLIEGASFDEREIGKIEKVKTPKELSCFLASAKAKNVSDRFPDALVIGCDQVLDLEGQIFHKVTSKKEAYQRLCTLSGKTHSLHSAVALFRNGRKIWVEAFSAHMSVRPLSSKFIKRYLAYVGTDVLNSVGVYQIEGEGIHLFEKIDGDFFTIIGLPLLPLLVKLRHLGIICD
Nucleoside triphosphate pyrophosphatase that hydrolyzes 7-methyl-GTP (m(7)GTP). May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Q6G1B6
O64966
HMDH1_GOSHI
3-hydroxy-3-methylglutaryl-coenzyme A reductase 1
Gossypium
METHRRSSTNSIRSHKPARPIALEDDSTKASDALPLPLYLTNAVFFTLFFSAVYFLLCRWREKIRSSTPLHVVTFSEIVAILASVASFIYLLGFFGIDFVQSLVLRPSADVWATEDDEVESEVLLRNEDARHVPCGQALDRSIRSLQPPEPIVTAEKVFDEMPVTVMTEEDEEIIRSVVCGMTPSYSLESKLDDCKRAAAIRREALQRITGKSLSGLPLDGFDYESILGQCCEMPVGYEQIPVGIAGPLLLNGREYSVPMATTEGCLVASTNRGCKAIHLSGGATSVLLRDGMTRAPVVRFGTAKRAADLKLYLEDPENFETLACVFNRSSRFARLQSIKCAIAGKNLYLRFSCFTGDAMGMNMVSKGVQNVLDFLQTDFPDMDVIGISGNFCSDKKPAAVNWIEGRGKSVVCEAIINGDVVTKVLKTSVESLVELNMLKNLTGSAMAGALGGFNAHASNIVTAVYIATGQDPAQNVESSHCITMMEAVNGGKDLHVSVTMPSIEVGTVGGGTQLASQSACLNLLGVKGASKESPGANSILLATIVAGAVLAGELSLMSALAAGQLVKSHMKYNRSSKDVSKVSS
Catalyzes the synthesis of mevalonate. The specific precursor of all isoprenoid compounds present in plants.
O64966
Q57FU7
DNAE2_BRUAB
Error-prone DNA polymerase
Brucella
MVPYFEMAAASNFSFLCGASHPQELVERAHALDLSGIGIADRNTLAGVVRAHAQWKDIRKESGFRLFIGCRLSFIDGTPDMVVYPRDRAAYGQLCRLLTEGKHRAAIKGECHLEWADLLFRARQFQIAVFPPDEDEPDFAARLTEIAQAAPGSVWLALTMPHQGQDGRRAERIARFAAQAGVPLIATNDVLYHHPDRRPLQDVLTATRHHTTVFAAGRLLEKNAERHLKPPHEMVRLFRDYPEAIAATADFVAPITFQLDELKYAYPDEPIPPGKTAQQHLYDLVWEGAARHYGADMIPPKVQGLINKELALIARLEYEPYFLTVYDIVTHAREKGILCQGRGSAANSVVCFCLGITGVNPTQVDLLFERFISAERKEPPDIDVDFEHERREEVMQYVYDRYSRDRAAIVATVISYRSRSAIRDVGKALGLSEDVTAALANTVWGLSGGGIDRQHIRQAGLDPDNPIIQRAVELAITLIGFPRHLSQHVGGFVLTRDRLDETVPIGPAAMDKRSFIEWDKDDIDEVGLMKVDVLSLGMLTCIRKAFDLIHQHKPQLYGGEKLTLASLPRKDKAVYDMLCKGDSLGVFQVESRAQMNMLPRLRPQEFYDLVIEVAIVRPGPIQGDMVHPYLRRRSGQEPCTLPSPSPQHGPANELQQILGKTKGVPLFQEQAMRIAMEAAKFTPEEANQLRRAMATFRKMGTIHTMEKKMIDGMVNRGYDRTFAENCFNQIKGFGEYGFPESHAASFAHLVYISAWLKCHHPEVFAAALLNSQPMGFYAPAQIVRDAREHGVTVLPVDVNFSQWDNILEETPDVHLALRLGFRQIDGFSKRDTELLIADRQEPYRTIEDMHRRLRLDRRAFTLLADADAFGSLDIDRRAALWAVRRLPNDETLPLFRAAAASELAQEPRTKLPEMAASEHVIADYETTRLSLKGHPLQYLREGLAAEGVSTCRAVQEGADGRRMKVAGVVTVRQRPGSAKGVVFLTIEDETGIANIVIWPKIMKVFRREVMSARLIHIEGRIQRSLEGVVHLVAAKLQDRSAALIEMSGREAQRLIAPSQMAHHPRNVRVMPNSRDFH
DNA polymerase involved in damage-induced mutagenesis and translesion synthesis (TLS). It is not the major replicative DNA polymerase.
Q57FU7
Q8RWZ3
IBR3_ARATH
Protein INDOLE-3-BUTYRIC ACID RESPONSE 3
Arabidopsis
MGSSTGDLVTRIQSAHRFDHDALFRFAADNVSGFPTNPSQFKVSQFGHGQSNPTFLIEVGSGSSLKRYVLRKKPPGKLLQSAHAVDREFQVLRALGEHTQVPVPKVFCLCTDPAVIGTAFYIMEFMEGRIFIDPKLPNVAPERRNAIYRATAKALASLHSADVDAIGLEKYGRRGNYCKRQIDRWFKQYLASTSEGKPERNPKMFELVDWLRKNIPAEDSTGATSGLVHGDFRIDNLVFHPSEDRVIGIIDWELSTLGNQMCDVAYSCMHYIVNVQLDKEHVSEGFETTGLPEGMLSMPEFLLEYCSASGKPWPAANWKFYVAFSLFRAASIYTGVYSRWLMGNASAGERARNTGVQANELVESALGYIARENVLPEHPPSVQRDVSPSYESLVDGSGRFIPNRKVLELRQKLIKFMETHIYPMENEFSKLAQSDMRWTVHPQEEKLKEMAKREGLWNLFVPVDSAARARRELAATENKHNLSGKSFDQLFGEGLTNLEYGYLCEIMGRSVWAPQVFNCGAPDTGNMEVILRYGNKEQISEWLIPLLEGRIRSGFAMTEPQVASSDATNIECSIRRQGDSYVINGTKWWTSGAMDPRCRVLILMGKTDFNAPKHKQQSMILVDMRTPGISVKRPLTVFGFDDAPHGHAEISFENVVVPAKNILLGEGRGFEIAQGRLGPGRLHHCMRLIGAAERGMELMAQRALSRKTFGKFIAQHGSFVSDLAKLRVELEGTRLLVLEAADHLDKFGNKKARGILAMAKVAAPNMALKVLDTAIQVHGAAGVSSDTVLAHLWATARTLRIADGPDEVHLGTIGKLELQRASKL
Involved with IBR1 and IBR10 in the peroxisomal beta-oxidation of indole-3-butyric acid (IBA) to form indole-3-acetic acid (IAA), a biologically active auxin . May be responsible for catalyzing the first step in IBA-CoA beta-oxidation . May play a role in defense response to pathogenic bacteria .
Q8RWZ3
Q8VDS7
CE57L_MOUSE
Cep57-related protein
Mus
MDSELSQSMVGSYLNPPERMHLPSFTQNEAFQNCHPGTPPKMFNSPNNQALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHQELIKQKKDISIQLSSAQSRCILLEKQLEYTKRMVLNVEREKTMILEQQAQLQREKEQDQMKLHAKLEKLHVLEKECLRLTATRQTAEDKIKCLEEKLKEEEHQRRLFQDRACEKTNCLKREPPQQRDHKFRTPTFERKKPFRTTSQARANPQSSGEPVSICDSLSELLMTMEEELDQMNMEHRELLRQTMQPGNHSVSEDIEQELEQLAKKMESKGDQISKLKKHQDSVRKLQEKIENSRINESSGIHGNPKGSKNLKTSPRKCVSETSSFQRDRGFQPVQVHSLQSKLRRDDIKWEQ
Centrosomal protein which may be required for microtubule attachment to centrosomes.
Q8VDS7
C5B8Y2
RNC_EDWI9
Ribonuclease III
Edwardsiella
MNPIVINRLQRKLGYTFRQHDLLMQALTHRSASSKHNERLEFLGDSILSFVIANALYHRFPRVDEGDMSRMRATLVRGNTLAEMAREFDLGECLRLGPGELKSGGFRRESILADTVEALIGGIFLDSDIQTIERLILDWYRSRLEEISPGDKQKDPKTRLQEFLQGRHLPLPSYLVVQVRGEAHDQEFTIHCQVSGLSAPVVGVGSSRRKAEQAAAEQALKQLELE
Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism.
C5B8Y2
A6VLF9
TRMA_ACTSZ
tmRNA (uracil(341)-C(5))-methyltransferase
Actinobacillus
MQQLPIEKYDELLAEKCRKLTALLAPFDAPALTVFPSPTQHFRMRAEFRLWHDYSENRGGNLYHIMFDKTTKQRYRVDQFPVASQLINRMMATILPLLKEQDVLSRKLFQIDYLSTLSEQIIVSLLYHKTLTDEWQEAAQALKVRLRNLGFSVQIIGRATKQKICLDQDFVDEELSVGDKKYVYRQVENSFTQPNAALNCKMLEWAIDCTRDSQGDLLELYCGNGNFSIALAQNFRKVLATEIAKPSVAAAQFNIAANQVDNLQIIRMSAEEFTQAVNGVRAFNRLKGIDLQAYECHTIFVDPPRAGLDSDTVKLVQKYDRILYISCNPQTLCENLQILSQTHRIERAALFDQFPYTEHMEAGVWLMRK
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).
A6VLF9
Q1C774
PURR_YERPA
Purine nucleotide synthesis repressor
Yersinia
MATIKDVAKHAGVSTTTVSHVINKTRFVAENTKAAVWAAIKELHYSPSAVARSLKVNHTKSIGLLATSSEAPYFAEVIEAVENSCYSKGYTLILCNSHNNLDKQKAYLAMLAQKRVDGLLVMCSEYPDQLLGMLEDYRNIPMVVMDWGTARGDFTDSIIDNAFEGGYLAGRYLIERGHRDIGAIPGQLARNTGGGRHQGFLKALEEANIPVREEWIVQGDSEPESGYKAMHQILTQKHRPTAVFCGGDIMAMGAICAADELGLRVPQDISVIGYDNVRNARYFSPALTTIHQPKERLGETAFAMLLDRIVSKREDPQTIEVHPKLVERRSVADGPFRDYRR
Is the main repressor of the genes involved in the de novo synthesis of purine nucleotides, regulating purB, purC, purEK, purF, purHD, purL, purMN and guaBA expression. PurR is allosterically activated to bind its cognate DNA by binding the purine corepressors, hypoxanthine or guanine, thereby effecting transcription repression.
Q1C774
A3LRM2
ENOPH_PICST
2,3-diketo-5-methylthio-1-phosphopentane phosphatase
Scheffersomyces
MAIDTVVLDIEGTVCPITFVKEKLFPYFLEKLPSFLSEISNFTSLQADDKDPIKAILSQLPEQIRTSKDSVLEYFNDLVRRDIKDPILKQLQGFIWKLGYENGDLKAPVYEDSIEFIKTFPSKTENKRIYIYSSGSIKAQILLFGYVDENGKSVDLNEYLSGYFDITTAGFKTQSSSYTKILEDIGKEHGGSVLFLSDNVLEVEAALEAGMESYVVVRPGNAPLTEDDKTKYKIITSLEQL
Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
A3LRM2
A4XZ90
RL3_PSEMY
50S ribosomal protein L3
Pseudomonas
MTIGVVGRKCGMTRIFTEEGVSIPVTVIEIEPNRVTQFKNEESDGYRAVQVTVGERRASRVSKAQAGHFAKANVAAGRTVMEFRLEEGDYQAGDLINAEIFQAGQLVDVTGQSKGKGFAGTIKRWNFRGQDNTHGNSVSHRVPGSIGQCQTPGRVFKGKKMSGHMGAERVTVQSLEVVRVDAERNLLLVKGAVPGATGGDVIVRPAVKA
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.
A4XZ90
B0R6A7
COST_HALS3
Compatible solute transducer protein
Halobacterium
MSEPTADAGDNSPSSTDTAPLDRVKAIALLPLRSYLVKFAVALLVILVIIAAGGFWVQADATATLEANTEQQLEQEAVSDATEIGDWLERNEQSVLIASNNPRLGFNTTAADKQAYVTQLVAAELDADRIADVHVADPTVGGASDARIVASTDEDARGTRVSADTHPWVDRTRSIGRDTVVSTNPYRTAGGQRVVSSMSVAADLTHVLVVEYTAGDLSDQFGAGIDGTFTQVVRPTSDATAVLFSDAGTDAVGQPYIPDRSQSEIPALDSATEQGQFTNTPTKDSVLDREYVAAYTTVPGKNWVVVKHAPSESAFALSNQIRTGILGFILVALVGVVLVGGTIGRNTAAAVQSLSAAAAEIEAGNYDVDVASSRRDEIGQLFASIGSMRDALVTQIDEAEAAREQATEAQQDAEAERERAEDARERAEDAKADAEALAAELEAQAERYSDVMAACADGDLTRRMPADDTDNEAMAAIAASFNEMLAQWEHTIIDIQEFADAVATASEEAEVGAADAERASGQVSESVQEIAGAADEQRNMLDTVSGEMTDLSAAIEEVAASADSVAEHSHQTAEIARDGEQTAEDAIERSLTVQEAIDATVQNVEALDDQMAEISEIVDLISDIAEQTNMLALNANIEAARADKSGDGFAVVADEVKDLAEETQESAGDIERRITEVQSQTTATVAEARAAEESMDAGIDAVEEVVDAFTAVSDHADETDTGVQEISDTTDDQAASTEEAVSMTEEVADLSDSTAGEAQSVSAAAEEQAASMSEISDSVESLSGQAEQLKALLSEFEVDADRDVTPTQTD
Mediates chemotaxis towards compatible osmolytes. Probably transduces the signal from the substrate-binding protein CosB to the histidine kinase CheA.
B0R6A7
O27372
RPO11_METTH
DNA-directed RNA polymerase subunit L
Methanothermobacter
MEVILDKRNEMEIVFEGETHTLCNVLRSILMEDEKVKAAAYSIDHPIVGEPQLYIRAGSPKKSLKAAAETLRDRCDEFRRLIESL
DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
O27372
Q9K951
EFP_HALH5
Elongation factor P
Halalkalibacterium (ex Joshi et al. 2022)
MISVNDFKTGLTIEVDNGIWQVMEFQHVKPGKGAAFVRSKLRNLRTGAVQEKTFRAGEKVSKAHIENRRMQYLYASGDVHTFMDNETFEQLELSTAQIEHELKFLKENMEVHVISYQGETLGVEVPNTVELTVTETEPGIKGDTASGGTKPATLETGLTVQVPFFVNEGDVLVIDTRSGDYVSRA
Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
Q9K951
A4XYD7
RS15_PSEMY
30S ribosomal protein S15
Pseudomonas
MALSVEEKAQIVNEYKQAEGDTGSPEVQVALLTANINKLQGHFKANGKDHHSRRGLIRMVNQRRKLLDYLKGKDTTRYSALIGRLGLRR
Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome.
A4XYD7
Q6P4T1
SNX19_MOUSE
Sorting nexin-19
Mus
MKAQTVSPTQGTISESSYVHSNLWSSRKLMIVGVLVGWLLVIHLLVNMWLLILLCASLVALGGWLGSTAILGASGQLHLERFITITTCPPCPEAERQLEQEINRTIQMIIRDFVLSWYRSVSHEPAFEAEMEAAMKGLVQELRRRMSIVDSHALTQRVLTLCGCHLQSYIQAKEATAKEQSCPVQPSQLWDAYCQVTAPHPAMSCPTTEVTYARGIVNLILKELVPKPHLETRTGRHVVVEVITCNVILPLISKLSDPDWIHLILVSIFSKYRHDAAQGTKPPCSSSVLEQPSVPTSLPLIVEVESLPVGKASSPATAPVHLTSSEPAPSPEIEEGHEAVEGDLPGMLEEKKVGNSSSHFLQPDIRGPLFLCEDSELESPLSELSKETILLMTPGNFLSDRIQDALCALDDSGALEPKDGEGSECMEGAEAEEAPGTDTETGMLVSVLNCPEIQIDTADKEVEQGDDTSLTALLEEPEKPCPLRPSCLDKDLASGVCSLEPAMPPVPLSSSPPGPLSSATFSFESLSSPDGPVVIQNLRITGTITAREHSGTGFHPYTLYTVKYETVLNGENSSGLQQLAYHTVNRRYREFLNLQTRLEEKPDLRKFIKNVKGPKKLFPDLPFGNMDSDRVEARKSLLESFLKQLCAIPEIGNSEEVQEFLALNTDARIAFVKKPFMVSRIDKMVVSAIVDTLKTAFPRSEPQSPTEELSEAENESKPQTEGKKASKSRLRFSSSKIAPALSIAEAQDKILYCLQEGNSESEVLSMSGMESFIEKQTKLLRIQPAEVPDKDPQQVPKEYVDSGLLDKAVVAQELNKSGPGTETELADTAFDLILLLLMEQWKWLCTESMQKFLHIIFGTLVQRWLEVQVANLTCPQRWAQYLHLLRESIWPGGVLPKFPRPGRTQAQKAATEKQALQSLMDLLPDFLVEILGVNKCRLSWSLVLESFQQPLINRHLIYCLGDIILELLDLSASVEECAPATSASDSPGSLKKMAVST
Plays a role in intracellular vesicle trafficking and exocytosis . May play a role in maintaining insulin-containing dense core vesicles in pancreatic beta-cells and in preventing their degradation. May play a role in insulin secretion . Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)) .
Q6P4T1
A5VLG3
GATA_LIMRD
Glutamyl-tRNA(Gln) amidotransferase subunit A
Limosilactobacillus
MDFYQTSLSQLHDDLVNKKISATELTKETFDHIKGNEDQVKAFISLNEDQALKRAAEIDAKGISADQLTAGVPLAVKDNILTKGLTTTAASKMLENFNPVYDATVVEKLNAADYINVGKTNLDEFAMGSSTENSAFFTTHNPWDLTRVPGGSSGGSAAAVAAGDVLGALGTDTGGSIRMPASFNGVVGMKPTYGRVSRWGIIAFGSSFDQVGWLTQNVKDNALLTALISGNDERDMTSSLKEVPDWAAQLNENTNVKGLRIAVPKEYFDGLDEDVQEVIKAALDHLESLGAIVDEVSLPHTKYGVPAYYILASSEASSNLQRYDGIRYGFRAADVKNLEDVYVRSRSEGFGEEVKRRIMLGTFSLSAGFYDAYFNKAAKVRRLIAQDFEDVFKDHDVIVGATGASTAFKIGAEIDDPQTMYMNDVLTVPVNMAGLPAMSIPAGFSAKNGMPVGLQIIGKAFDEQTVYNTGYVFEQTTDFHKKTPKLGGQN
Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
A5VLG3
Q6A8P5
GATA_CUTAK
Glutamyl-tRNA(Gln) amidotransferase subunit A
Cutibacterium
MNELLTLTAAELGERIAARQISSEEVTQAHLDRISEVDGDIHAFLLVDHAGALDAARRIDARIADGEHLGPLAGVPLAVKDLFCTKGIATTASSQMLEGWIPPYDSTIVTRCKDAGMVILGKTNLDEFAMGSSTETSAFGPTHNPWDLERVPGGSGGGSAASLASFQAPLALGTDTGGSIRQPGAVTGTVGIKPTYGSTSRYGVIAMASSLDTPGPCARTVLDAALLHQAIAGHDAMDQTTINQPTPAVVEAARQTDVSGVRIGVVTELSGQVYDPQVEARFHEAVEMLIEAGAEVVEVSCPNFDLALPAYYLIQPAEVSSNLARYDAMRYGLRVNDDGEHSAEQVMRATRGAGLGAEAKRRIILGTYALSAGYYDAYYGSAQKVRTLIQRDFEKAWQMCDVLVSPATPTTAFRLGERTADPMAMYRSDLCTVPANMAGSPAGSFPIGLSETDGMPVGMQVMAPIMADDRIYRVGAALERLLHEKWGAPLLAKAPEVRGER
Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
Q6A8P5
Q1CV46
DNAK_HELPH
Heat shock protein 70
Helicobacter
MGKVIGIDLGTTNSAMAVYEGNEAKIIANKEGKNTTPSIVAFTDKGEILVGESAKRQAVTNPEKTIYSIKRIMGLMFNEDKAKEAEKRLPYKIVDRNGACAIEISGKVYTPQEISAKILMKLKEDAESYLGESVTEAVITVPAYFNDSQRKATKEAGTIAGLNVLRIINEPTSAALAYGLDKKESEKIMVYDLGGGTFDVTVLETGDNVVEVLATGGDAFLGGDDFDNRVIDFLASEFKSETGIEIKNDVMALQRLKEAAENAKKELSSAMETEINLPFITADATGPKHLVKKLTRAKFESLTEDLMEETISKIESVIKDAGLTKNEISEVVMVGGSTRIPKVQERVKAFINKELNKSVNPDEVVAVGASIQGGVLKGDVKDVLLLDVTPLSLGIETLGGVMTKVIDRGTTIPAKKSQVFSTAEDNQPAVSIMVLQGERELARDNKSLGKFDLQGIAPAPRGVPQIEVTFDIDANGILTVSAQDKNTGKSQEIKISGSSGLSDSEIEKMVKDAELHKEEDARKKEVIEARNHADSLAHQTQKSLDEHKTNLNENDANEIQNAINALKDCIKNDNATKAELEDKTKALAQAAQKLGEAMANKNNAEQPKKKDDDVIDAEVE
Acts as a chaperone.
Q1CV46
A2RMR1
RL20_LACLM
50S ribosomal protein L20
Lactococcus cremoris subsp. cremoris
MARVKGSVATRKRRKRILKLAKGYYGAKHRLFKTAKEQVMNSYYYAFRDRRQKKRDFRKLWIARINAAARMNGLSYSKLMHGLKLADIEVNRKMLADIAIADAAAFTALAEEAKKALAK
Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit.
A2RMR1
Q2M3M2
SC5A9_HUMAN
Solute carrier family 5 member 9
Homo
MSKELAAMGPGASGDGVRTETAPHIALDSRVGLHAYDISVVVIYFVFVIAVGIWSSIRASRGTIGGYFLAGRSMSWWPIGASLMSSNVGSGLFIGLAGTGAAGGLAVGGFEWNATWLLLALGWVFVPVYIAAGVVTMPQYLKKRFGGQRIQVYMSVLSLILYIFTKISTDIFSGALFIQMALGWNLYLSTGILLVVTAVYTIAGGLMAVIYTDALQTVIMVGGALVLMFLGFQDVGWYPGLEQRYRQAIPNVTVPNTTCHLPRPDAFHILRDPVSGDIPWPGLIFGLTVLATWCWCTDQVIVQRSLSAKSLSHAKGGSVLGGYLKILPMFFIVMPGMISRALFPDEVGCVDPDVCQRICGARVGCSNIAYPKLVMALMPVGLRGLMIAVIMAALMSSLTSIFNSSSTLFTIDVWQRFRRKSTEQELMVVGRVFVVFLVVISILWIPIIQSSNSGQLFDYIQAVTSYLAPPITALFLLAIFCKRVTEPGAFWGLVFGLGVGLLRMILEFSYPAPACGEVDRRPAVLKDFHYLYFAILLCGLTAIVIVIVSLCTTPIPEEQLTRLTWWTRNCPLSELEKEAHESTPEISERPAGECPAGGGAAENSSLGQEQPEAPSRSWGKLLWSWFCGLSGTPEQALSPAEKAALEQKLTSIEEEPLWRHVCNINAVLLLAINIFLWGYFA
Involved in sodium-dependent transport of D-mannose, D-glucose and D-fructose.
Q2M3M2
Q3M5C9
RPOC1_TRIV2
Transcriptase subunit gamma
Trichormus
MRPAQTNQFDYVKIGLASPERIRQWGERTLPNGQVVGEVTKPETINYRTLKPEMDGLFCERIFGPAKDWECHCGKYKRVRHRGIVCERCGVEVTESRVRRHRMGYIKLAAPVAHVWYLKGIPSYISILLDMPLRDVEQIVYFNSYVVLSPGNAETLTYKQLLSEDQWLEIEDQIYSEDSQLQGVEVGIGAEALLRLLADINLEQEAESLREEIGSAKGQKRAKLIKRLRVIDNFIATGSKPEWMVMTVIPVIPPDLRPMVQLDGGRFATSDLNDLYRRVINRNNRLARLQEILAPEIIVRNEKRMLQEAVDALIDNGRRGRTVVGANNRPLKSLSDIIEGKQGRFRQNLLGKRVDYSGRSVIVVGPKLKIHQCGLPREMAIELFQPFVINRLIRSGMVNNIKAAKKLISRNDPSVWDVLEEVIEGHPVMLNRAPTLHRLGIQAFEPILVEGRAIQLHPLVCPAFNADFDGDQMAVHVPLSLESQAEARLLMLASNNILSPATGRPIITPSQDMVLGAYYLTAENPGATKGAGKYFASLDDVIMAFQQEQIDLHAYIYVRFDGEVESDQPDTDPLEVTNNDDGSRTVLYKYRRVREDAQGNLISQYVRTTPGRVIYNKAIQEALAS
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Q3M5C9
Q9MB35
PERQ_SEDLI
Thioredoxin-dependent peroxiredoxin Q
Sedum
QTLQTSSQSQFHGLKFSHASSFKSPSAPLRKNSIFAKVTKGSTPPPFTLKDQEGRPVSLSKFKGKPVVVYFYPADETPGCTKQACAFRDSYEKFKKAGAEVVGISGDSSESHKAFAKKYKLPFTLLSDEGNKVRKEWGVPSDLFGTLPGRETYVLDKNGVVQLVYNNQFQPEKHIDETLKLLQSLK
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.
Q9MB35
A2BTV4
GRPE_PROM5
HSP-70 cofactor
Prochlorococcus
MIEEQSDNVENKDENVSMDNNISENLPIAEEQTNEDKKLPDDNNEKIDAEDLKNTITNNDARLEQLEKEHETLKSQYVRIAADFDNFRKRQSRDQDDLKIQLVSKALTAILPIVDNFERARQQLKPEGDEAQTLHRSYQGLYKQLVEVLKQQGVAPMRVVGQQFDPNLHEAVLREPSEEQNEDIIIEELQRGYHLEGKVLRHALVKVSMGPGQQISQESEEKDKVDKDIDSEGSISEEN
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.
A2BTV4
P86622
DRT2_PHAJA
Dermatoxin-J2
Phasmahyla
SLGGFLKGVGKALAGVGKMVADQFGNLLQAGQ
Antimicrobial peptide.
P86622
Q07HB2
COXX_RHOP5
Heme O synthase
Rhodopseudomonas
MSVIESHDLGLIAPRISEAGVADYVALLKPRVMSLVIFTALVGLLLAPGSFHPVLAITSILCIGVGAGAAGALNMWYEDDIDAKMTRTANRPIPRGKITRPEALTFGMTLAFFSVVTLGILVNWIAAALLAFTIFFYVVIYTIWLKRVTAQNIVIGGAAGALPPVVAWAAVTGSVSVEPMLLFAIIFFWTPPHFWALALFRAGDYANAGVPMLPVTAGPDATRLQILLYTIALVAVALAPWPLGYFSAVYGITSLALGGGMLACALRVYRHRTGSAALRASRNLFRFSILYLFALFAVLLLEVVARGVLALFG
Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
Q07HB2
C4LIS3
RISB_CORK4
6,7-dimethyl-8-ribityllumazine synthase
Corynebacterium
MSGEGSPTITIEPGSAHGLRVAIVVSEWNRDITDELASQAQQAGETAGAEVTVIPVVGALEIPVVVKKATQTYDAVVALGCVIQGGTPHFDHVCNAVTYGLTKIAVETETPVGNGVLTCNTHEQAVDRAGGPTAHENKGAEAMIAAIHTAQTLKSMAAD
Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
C4LIS3
P28077
PSB9_RAT
Really interesting new gene 12 protein
Rattus
MLQAGAPTAGSFRTGEVHTGTTIMAVEFDGGVVVGSDSRVSAGAAVVNRVFDKLSPLHQRIYCALSGSAADAQAIADMAAYQLELHGLELEEPPLVLAAANIVKNISYKYREDLLAHLMVAGWDQHEGGQVYGTMGGMLIRQPFAIGGSGSTYIYGYVDAAYKPGMTPEECRRFTTDAITLAMNRDGSSGGVIYLVTITADGVDHRVILGDELPKFYDE
The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processing to generate class I binding peptides.
P28077
P25416
QUTG_EMENI
Protein qutG
Aspergillus subgen. Nidulantes
MDCPIPQTELDEIYAFATDLARKAGQLLLERVNDRNSEQVYAEKENAVDLVTQTDEDVESLIKTAIQTKYPAHKFLGEESYAKGQSREYLIDEQPTWCVDPLDGTVNFTHAFPMFCVSIGFIVNHYPVIGVIYAPMLNQLFSSCLNRGAWLNEMQQLPLIRKPSIPPLPATAPSKCIFACEWGKDRRDIPDGTLQRKIESFVNMAAERGSRGGKGGMVHGVRSLGSATMDLAYTAMGSVDIWWEGGCWEWDVAAGIAILLEAGGLVTAANPPEDIEGPIEPVKLGSRLYLAIRPAGPSETETGRETQERTVREVWRRVRQLDYERPTRQS
Not known. Probably involved in quinate metabolism.
P25416
B5YGE0
EFTS_THEYD
Elongation factor Ts
Thermodesulfovibrio
MAITAQMVKELREKTGAGMMECKKALETSGGDFNKAIDILRQKGLATAQKKASREAKEGIITSYIHMDKIGVMLELNCETDFVARNEEFRQLAKDIAMQIAASNPQYIQREDIPQEVIEKEKEIYKSQIKGNKPPQVIEKIVEGKLEKFFEEMCLLDQPFIKEPEKKIKDLITEKVAKFGENIMVRRFVRFQVGQTQDE
Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.
B5YGE0
B1HMX5
RL22_LYSSC
50S ribosomal protein L22
Lysinibacillus
MTQAKAIARTVRIAPRKVRLVVDLIRGKQVGEAVAILRHTPKAASPVVEKVLKSAVANAEHNYDLDINSLVVSEVFVDEGPTLKRFRPRAQGRASAINKRTSHITLVVSEKKEG
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.
B1HMX5
Q2FZU0
G6PI_STAA8
Phosphohexose isomerase
Staphylococcus
MTHIQLDFSKTLEFFGEHELKQQQEIVKSIHKTIHEGTGAGSDFLGWIDLPVDYDKEEFSRIVEASKRIKENSDVLVVIGIGGSYLGARAAIEMLTSSFRNSNEYPEIVFVGNHLSSTYTKELVDYLADKDFSVNVISKSGTTTEPAVAFRLFKQLVEERYGKEEAQKRIFATTDKEKGALKQLATNEGYETFIVPDDVGGRYSVLTAVGLLPIATAGINIEAMMIGAAKAREELSSDKLEENIAYQYATIRNILYAKGYTTEMLINYEPSMQYFNEWWKQLFGESEGKDFKGIYPSSANYTTDLHSLGQYVQEGRRFLFETVVKVNHPKYDITIEKDSDDLDGLNYLAGKTIDEVNTKAFEGTLLAHTDGGVPNMVVNIPQLDEETFGYVVYFFELACAMSGYQLGVNPFNQPGVEAYKQNMFALLGKPGFEDLKKELEERL
Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
Q2FZU0
P36674
TRER_SALTY
Trehalose operon repressor
Salmonella
MQNRLTIKDIARLSGVGKSTVSRVLNNESGVSERTRERVEAVMNQHGFSPSRSARAMRGQSDKVVAIIVTRLDSLSENLAVQTMLPAFYEQGYDPIMMESQFSPTLVMEHLGMLRRRNIDGVVLFGFTGITEELIAPWKASLVLLARDAQGFASVCYDDEGAIHILMQRLYEQGHRNISFLGVPHSDITTGKRRHDAYLAFCKKHKLHPVAALPGLAMKQGYEHTASVIMPDTTALVCATDTLALGASKYLQEQRIETLQLASVGNTPLIKFLHPEIVTVDPGYAEAGRQAASQLIEQINGRCDPRRIVIPSTLA
Repressor of the treBC operon. It is able to bind trehalose-6-phosphate.
P36674
Q9XVE5
FACE1_CAEEL
Farnesylated proteins-converting enzyme 1
Caenorhabditis
MDASCLFKALLATNWALFLWDQYITFRQYKAHKNAVKRPNEVKELIGEEDYKKARDYKIDNHLFGFFHSWFNQLLLTAQLIGGYYPFLWYATASYPLHVAVFLSINSIIETIIDLPWDLYSTFIIEDAHGFNKQTIGFYFVDKIKKMLVGFALTMPIVYGIEWIIVNGGPYFFVYIWLFVSVVVLLLMTIYPTFIAPLFDKYFPLPDGDLKTKIEQLAASLSYPLTELYVVNGSKRSAHSNAYMYGFWKNKRIVLYDTLLSGAEKEKVHELYVAAGEKIEETENDKKRGMNNDEVVAVLGHELGHWALWHTLINLVITEVNLFFSFAVFGYFYKWEALYQGFGYHDTPPVIGMMLIFQFVLALYNQLASIGMVIHSRSAEFGADEFAANLGHGENLIGALTKLGVDNLSMPINDSLYSWCTHTHPPVVERVAAVRAFQAKNK
Proteolytically removes the C-terminal three residues of farnesylated proteins.
Q9XVE5
C1CKG8
RL21_STRZP
50S ribosomal protein L21
Streptococcus
MSTYAIIKTGGKQVKVEVGQAVYIEKLNVEAGQEVTFNEVVLVGGENTVVGTPLVAGATVVGTVEKQGKQKKVVTYKYKPKKGSHRKQGHRQPYTKVVINAINA
This protein binds to 23S rRNA in the presence of protein L20.
C1CKG8
A0A2I1BSX0
NVFI_ASPN1
Novofumigatonin biosynthesis cluster protein I
Aspergillus
MVGSRTWCESEMLFVQPDAGTKEELYYRVTPKPGQTQANFNWTPHKVRFHDARPQRDSFDLNTHGFTFVEDAISPQLIERIRADDTAAVEGDYFASVAALVKRVTGADHVVCFSPYTRKENSEKGIFGQPARTVHCDHTPAAAIELTHKLCGEDAVRLLQSRFRAFSVWRPLVEPVLDWPLAVVDGRTIAPDDLHPVHWLRYEKKDTEPPFQLSFSETQKWYYLSRQRSDEVSIVKNYDSEVVPSPRSAHCAFKHPFVPKDAPPRESIDVRCLVFGGR
Fe(II)/2-oxoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of novofumigatonin, a heavily oxygenated meroterpenoid containing a unique orthoester moiety . The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase nvfA via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations . DMOA is then converted to farnesyl-DMOA by the farnesyltransferase nvfB . Epoxydation by FAD-dependent monooxygenase nvfK, followed by a protonation-initiated cyclization catalyzed by the terpene cyclase nvfL leads to the production of asnavolin H . The short chain dehydrogenase nvfC then as a 3-OH dehydrogenase of asnovolin H to yield chemesin D . There are two branches to synthesize asnovolin A from chemesin D . In one branch, chemesin D undergoes Baeyer-Villiger oxidation by nvfH, methylation by nvfJ, and enoyl reduction by the nvfM D enoylreductase that reduces the double bond between C-5'and C-6', to form respectively asnovolin I, asnovolin K, and asnovolin A . In the other branch, the methylation precedes the Baeyer-Villiger oxidation and the enoyl reduction to yield asnovolin A via the asnovolin J intermediate . Asnovolin A is further converted to fumigatonoid A by the Fe(II)/2-oxoglutarate-dependent dioxygenase nvfI that catalyzes an endoperoxidation reaction . The alpha/beta hydrolase nvfD then acts as an epimerase that converts fumigatonoid A to its C-5' epimer, which then undergoes spontaneous or nvfD-catalyzed lactonization . The following step utilizes the ketoreductase nvfG to produce fumigatonoid B . The dioxygenase nvfE further converts fumigatonoid B into fumigatonoid C . Finally the Fe(II)/2-oxoglutarate-dependent dioxygenase nvfF catalyzes two rounds of oxidation to transform fumigatonoid C into the end product, novofumigatonin A .
A0A2I1BSX0
B2RQC6
PYR1_MOUSE
Dihydroorotase
Mus
MAALVLEDGSVLQGRPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPSDEEDEFGLSKWFESSEIHVAGLVVGECCPTPSHWSANCTLHEWLQQRGIPGLQGVDTRELTKKLREQGSLLGKLVQKGTEPSALPFVDPNARPLAPEVSIKTPRVFNAGGAPRICALDCGLKYNQIRCLCQLGAEVTVVPWDHELDSQKYDGLFLSNGPGDPASYPGVVSTLSRVLSEPNPRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGTGRCFLTSQNHGFAVDADSLPAGWAPLFTNANDCSNEGIVHDSLPFFSVQFHPEHRAGPSDMELLFDVFLETVREAAAGNIGGQTVRERLAQRLCPPELPIPGSGLPPPRKVLILGSGGLSIGQAGEFDYSGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLPITLHYVTQVIRNERPDGVLLTFGGQTALNCGVELTKAGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASTKEELSALVAPAFAHTSQVLIDKSLKGWKEIEYEVVRDAYGNCVTVCNMENLDPLGIHTGESIVVAPSQTLNDREYQLLRRTAIKVTQHLGIVGECNVQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLPELRNSVTGGTAAFEPSLDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKALRMVDENCVGFDHTVKPVSDMELETPTDKRIFVVAAALWAGYSVERLYELTRIDCWFLHRMKRIVTHAQLLEQHRGQALPQDLLHQAKCLGFSDKQIALAVLSTELAVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTYWGNTHDLDFRAPHVLVLGSGVYRIGSSVEFDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGGQLPNNMAMALHRQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCHTVGYPCVVRPSYVLSGAAMNVAYTDGDLERFLSSAAAVSKEHPVVISKFIQEAKEIDVDAVACDGIVSAIAISEHVENAGVHSGDATLVTPPQDITPKTLERIKAIVHAVGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRIIMGEKVEPVGLMTGSGVVGVKVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPEKNILLTIGSYKNKSELLPTVRLLESLGYSLYASLGTADFYTEHGVKVTAVDWHFEEAVDGECPPQRSILDQLAENHFELVINLSMRGAGGRRLSSFVTKGYRTRRLAADFSVPLIIDIKCTKLFVEALGQIGPAPPLKVHVDCMTSQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFTLFLGASSENAGTLGAVAGSAAGLKLYLNETFSELRLDSVAQWMEHFETWPAHLPIVAHAERQSVAAVLMVAQLTQRPVHICHVARKEEILLIKTAKAQGLPVTCEVAPHHLFLNREDLERLGPGKGEVRPELGSREDMEALWENMAVIDCFASDHAPHTLEEKCGPKPPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPLQEDTYVEVDLEHEWTVPSHMPFSKARWTPFEGQKVKGTVRRVVLRGEVAYIDGQVLVPPGYGQDVRKWPQGVVPQPPPSTPATTEITTTPERPRRVIPGLPDGRFHLPPRIHRASDPGLPAEEPKEKPPRKVVEPELMGTPDGPCYPAPPVPRQASPQNLGSSGLLHPQMSPLLHSLVGQHILSVKQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATSSVQKGESLADSVQTMSCYADVIVLRHPQPGAVELAAKHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGDLKHGRTVHSLACLLTQYRVSLRYVAPPSLRMPPSVRDFVASRGTKQEEFESIEEALPDTDVLYMTRIQKERFGSVQEYEACFGQFILTPHIMTRAKKKMVVMHPMPRVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLGRF
This protein is a 'fusion' protein encoding four enzymatic activities of the pyrimidine pathway (GATase, CPSase, ATCase and DHOase).
B2RQC6
Q0IZS0
NADC_ORYSJ
Quinolinate phosphoribosyltransferase [decarboxylating]
Oryza sativa
MPAAAAAAAPPNPNVLQLAPRLRGLVSFPSSYSSSSPFSNRLRLRLPRAASMSAEARVPVAPPAHPTYDLKAVINLALSEDAGDRGDVSCLATIPSDVKAEATFIAKEDGVVAGISLADMIFKQVDPSLKVEWFESDGNYVHKGLQFGRVYGCARNIIVAERVVLNFMQRMSGIATMTKAMADAAHPACILETRKTAPGLRLVDKWAVLIGGGKNHRIGLFDMVMIKDNHISVAGGITNAMKFVDRFLAKEKLALPVEVETRTLQEVKDLLEYAAENNTSLTRIMLDNMVVPLGNGDIDVSMLKDAVELINGRFETEASGNVTIDTVKKIGETGVTYISSGALTHSVKALDISLKIDTELALQVGRRTNRA
Involved in the catabolism of quinolinic acid (QA).
Q0IZS0
Q83RD2
ASR_SHIFL
Acid shock protein
Shigella
MKKVLALVVAAAMGLSSAAFAAETATTPAPTATTTKAAPAKTTHHKKQHKAAPAQKAQAAKKHHKNTKAEQKAPEQKAQAAKKHAGKHGHQQPAKPAAQPAA
Required for growth and/or survival at acidic conditions.
Q83RD2
Q9QZX8
SO1B2_RAT
Solute carrier family 21 member 10
Rattus
MDHTQQSRKAAEAQPSRSKQTRFCDGFKLFLAALSFSYICKALGGVVMKSSITQIERRFDIPSSISGLIDGGFEIGNLLVIVFVSYFGSKLHRPKLIGIGCFIMGIGSILTALPHFFMGYYKYAKENDIGSLGNSTLTCFINQMTSPTGPSPEIVEKGCEKGLKSHMWIYVLMGNMLRGIGETPIVPLGISYLDDFAKEGHTSMHLGTLHTIAMIGPILGFIMSSVFAKIYVDVGYVDLNSVRITPNDARWVGAWWLSFIVNGLLCITSSIPFFFLPKIPKRSQEERKNSVSLHAPKTDEEKKHMTNLTKQEEQDPSNMTGFLRSLRSILTNEIYVIFLILTLLQVSGFIGSFTYLFKFIEQQFGRTASQANFLLGIITIPTMATAMFLGGYIVKKFKLTSVGIAKFVFFTSSVAYAFQFLYFPLLCENKPFAGLTLTYDGMNPVDSHIDVPLSYCNSDCSCDKNQWEPICGENGVTYISPCLAGCKSFRGDKKPNNTEFYDCSCISNSGNNSAHLGECPRYKCKTNYYFYIILQVTVSFFTAMGSPSLILILMKSVQPELKSLAMGFHSLIIRALGGILAPIYYGAFIDRTCIKWSVTSCGKRGACRLYNSRLFGFSYLGLNLALKTPPLFLYVVLIYFTKRKYKRNDNKTLENGRQFTDEGNPDSVNKNGYYCVPYDEQSNETPL
Mediates the Na(+)-independent uptake of organic anions such as taurochlate, bromosulfophthalein and steroid conjugates such as estrone-3-sulfate, 17-beta-glucuronosyl estradiol, dehydroepiandrosterone sulfate and prostaglandin E2.
Q9QZX8
Q7WF89
AROQ_BORBR
Type II DHQase
Bordetella
MAQRILVLHGPNLNLLGTREPHIYGSLTLAQIDQGLAALAGQLGVALTSWQSNHEGALVERIQAAAADGTDFIIINAAAYTHTSVAIRDALAAVAIPFIEVHLSNLYKRDSFRQHSYLSDLAIGLITGLGADGYEAALRYAARH
Catalyzes a trans-dehydration via an enolate intermediate.
Q7WF89
A1WXI9
BCHN_HALHL
Light-independent protochlorophyllide reductase subunit N
Halorhodospira
MTESASCHGGGVCGGLAQEEGQRQVFCGLTSIVWLHRKMRDAFFLVVGSRTCAHLLQSAAGVMIFAEPRFATAVLGERDLAGMADCNEELDRVVHELLARRPEIRTLFLVGSCPSEVIKLDLGKAAERLTAAHEGRVRVLPYSGSGLETTFTQGEDQFLTTLAHELPASPEGAPSLIVLGTLADVVEDQFRRLFDQLGIGPVHFLPPRTGADLPPVGPGTRVLQAQPFTGEATRALIRRGAERLDAPYPLGVEGTRSWLQAATRSFGVPDEQLEAVIEAPIARAQAALERQRGVLSGKRITFLPDSQLELPLARFLSEECGMQPVEVATPYFDREFHGRERDALGEEVRLVEGQDVDAQLDRLRADRPDLTVCGLGLANPLEAEGLRTKWSIELVFSPIQGFEQAGDLAELFARPLVRHETLKV
Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (BchN-BchB) is the catalytic component of the complex.
A1WXI9
Q810I1
TRI50_RAT
Tripartite motif-containing protein 50
Rattus
MAWQLTVPELQDQLQCPICLEVFKEPLMLQCGHSYCKNCLDSLSEHLDSELRCPVCRQSVDCSSSPPNVSLARVIDALRLPGDTEPTVCVHHRNPLSLFCEKDQEFICGLCGLLGSHQHHRVTPVSTVYSRMKEELAGRLSELKEQHRDVEEHIGKLVNNRTRIINESDVFSWVIRREFQELHHLVDEEKARCLEGVESHTRGLVASLDMQLEQAQGTQERLAQAERVLEQFGNESHHEFIRFHSITSRGEVQQARPLEGVFSPISFKPALHQADIKLTVWKRLFRKVLPAPESLKLDPATAHPLLELSKGNTVVHCGLLAQRRASQPERFDYSTCVLASKGFSWGRHYWEVVVGSKSDWRLGVIKGTASRKGKLSKSPEHGVWLIGLKEGRLYEAFGCPRLPLPVAGHPHRIGVYLHYEQGELTFFDADRPDDLRALYTFQADFQGKLYPILDTCWHERGSNSLPMVLPPPSAPGHLTRAQV
E3 ubiquitin-protein ligase that ubiquitinates Beclin-1/BECN1 in a 'Lys-63'-dependent manner enhancing its binding to ULK1. In turn, promotes starvation-induced autophagy activation. Interacts also with p62/SQSTM1 protein and thereby induces the formation and the autophagy clearance of aggresome-associated polyubiquitinated proteins through HDAC6 interaction.
Q810I1
A1WX11
LPXA_HALHL
Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase
Halorhodospira
MTRIHPNALVDPKARLGEEVEVGPFSVIGPDVEIDEGTWIGPHAVIQGPTRIGRDNRIYQFAALGEAPQHKGYQGEPTELVIGDGNTIREFVTCHRGTAQGRGETRIGDHNWLMAYCHIAHDCRLGNHLLFANSASLAGHVDVGDHATLGGFALVHQFCRIGPYAFCGFGSGINRDVPPFVTVSGQMAVPHGINSVGLRRHGFSRERIRDIKRAYRTIYRQGLRLDDAREALCQQLSHSADVQGMVDFIDNSQRGLLR
Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
A1WX11
A7MWH5
RS5_VIBC1
30S ribosomal protein S5
Vibrio
MAKEQQVQANDLQEKLIAVNRVSKTVKGGRIMSFTALTVVGDGNGRVGFGYGKAREVPAAIQKAMEKARRNMTTIALNEGTLHHPVKGRHSGSKVYMQPAAEGTGVIAGGAMRAVLEVAGVHNVLSKAYGSTNPINIVRATIDALGSMKSPEMVAAKRGLTVEAISE
Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body.
A7MWH5
B0KJ96
LPTD_PSEPG
LPS-assembly protein LptD
Pseudomonas
MALKSPAFRRKFPLLVTGGLLALQPLATSYAVAAEQFDCQVSAAGGWDCKPKAPVNNLPPRPVHEGAAVSSGTEAASEGETADRPMLVTEAKGRALKSRSEDYSHLDWVPREKLTAAQLAETGPYCGGAYVEPTRPGMADTTPKDESPTYINAKVSKYQQEQQIATLAGDVVMRQGSMQAEADEANLYQTENRGELKGNVKIRDNGSLVVGDEAQIQLDTGEAQVDNAEYVMHKSHIRGSALYAKRGENAIIRLKDGTYTTCEPGSNAWQLKGNNITLNPATGFGTATNVTLRVKDFPVFYTPYIYFPIDDRRQSGFLPPSFSTSSDTGFMLVTPYYFNLAPNYDATLYPRYMAKRGLLMEGEFRYLTPSSEGQFGGAYLNDKDDDRKEQTDYKDQRWMVNWQHKGGLDERLMTEVDYTDISDPFYFQDLESDQIGVESRDLLNQQGALTYRGDNYTARLNVHAYEMATISQITPYDRLPQITLNGVLPYNPGGLVMGYESEAVRFDRDLKDDFVRDKDGNPDFSAGAAGRRLDQNVSGIARANGNRFNVAPSISLPMEASYGYLTPKLKYAYTHYDLDLDSQGKAQAIAQSANPAYGSYNSSLNRDVPIFSVDSGLYFDRNTSLFGTNYKQTLEPRLFYLNVPYKDQRDIPIFDSSETLFSYDSLFRDNRFSGTDRIGDENKLSLGVTTRWIEDNGFERQNFSIGQAYYFKDRKVQLPGIYYKDRQSAQSDTSPYALVYNYYFNRDWRFNSDFNWDPDSRSTRSGSAMFHYQPEDNPNKVVNLGYRYRNDTIIYDSTTGTWKEGGSYGNPGDPNYIKDYYKIQQHDFSVIWPIVPQWSVIARWQHDYNRNRTLEAMGGFEYDNCCWKLRLINRYWIDYDDFSQALPANEKGDHGVFLQIVLKGLGGVVGNKVESFLDQGIQGYREREDQAY
Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane.
B0KJ96
A0QQ37
Y614_MYCS2
Putative S-adenosyl-L-methionine-dependent methyltransferase MSMEG_0614/MSMEI_0598
Mycolicibacterium
MRTDNDQWDITISVGQTALFVAASRALEARKPHPLAVDHYAEVFCRAAGGDWVAAVEGTDPEHPLQTEFGVDFVNFQGARTKYFDDYFRRVADAGVRQVVLLAAGLDSRAYRLPWADGTVVYELDVPKVLEFKREVLRRHGATPTAERREVPVDLRDDWPAALRANGFDASQPSAWIAEGLLIYLPADAQELLFAGIDALSAPGSFVAIEESAPMPMDVFEVKRAEALASGDPNSFFALVFNEQCAPGEQWFSERGWTASTTTLNECLHEVGRPAPAPDSEAAQMTGSISLMWARKG
Exhibits S-adenosyl-L-methionine-dependent methyltransferase activity.
A0QQ37
Q5XEZ1
B3GT9_ARATH
Beta-1,3-galactosyltransferase 9
Arabidopsis
MESLPTTVPSKSERRARSSKFSQSSSKPSVIMAFFSCVAWLYVAGRLWQDAENRVVLNNILKKSYDQKPKVLTVDDKLMVLGCKDLERRIVETEMELTLAKSQGYLKNLKSGSSSGKKLLAVIGVYSGFGSHLRRNTFRGSYMPQGDALRKLEERGIVIRFVIGRSPNRGDSLDRKIDEENQARKDFLILENHEEAQEELAKKVKFFFSAAVQNWDAEFYIKVDDNIDLDLEGLIGLLESRRGQDAAYIGCMKSGEVVAEEGGKWYEPEWWKFGDEKSYFRHAAGSLLILSKTLAQYVNINSGSLKTYAFDDTSIGSWMIGVQATYIDDNRLCCSSIRQDKVCSVA
Possesses hydroxyproline O-galactosyltransferase activity. Transfers galactose from UDP-galactose to hydroxyproline residues in the arabinogalactan proteins (AGPs). Is specific for AGPs containing non-contiguous peptidyl hydroxyproline residues. The addition of galactose onto the peptidyl hydroxyproline residues in AGP core proteins represents the first committed step in arabinogalactan polysaccharide addition. AGP glycans play essential roles in both vegetative and reproductive plant growth.
Q5XEZ1
O13008
FABPH_ONCMY
Heart-type fatty acid-binding protein
Oncorhynchus
MAEAFAGTWNLKDSKNFDEYMKALGVGFATRQVGGMTKPTTIIEVAGDTVTLKTQSTFKNTEISFKLGAEFDETTADDRKVKSLITIDGGKMVHVQKWDGKETTLVREVSGNALELTLTLGDVVSTRSYVKAE
FABP are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters.
O13008
O83321
RFUB_TREPA
Probable riboflavin import ATP-binding protein RfuB
Treponema
MMIAERGVRASARGVLSLHHIGKTYPRVMPRSKRGVWGMFGHPGRRAVDDAHTAHGPCSGARETDAAEHSVLSDVNLSFFTGEIHALLGKNGAGKSTLAHILSGFCVPTHGQLRLDGKEQRFSVPFDALRAGIGIVHQQPVFAERATVFENVVMGSAALTGVRWVRRAQVRERIDRIIAQWRMPLKKEEYVACLSADKRFFVSLLCVLFRNPRFIILDEPRCAPAQSRAVFFSHLEEFFVRSSHAPRCGGGVIVVTHRFADALRWAQRISLIEGGKACSFLRTDLLDEYCSAHQVNECIQKVSCALMSASTVTSSAVSSFSSLSDTQSCATVPRTSSARPWVLRVESLQVSKHADVPLTDISFSVAASAIIGIVGTPEDGVHVLEDILCDMHAGASRTHCTGNILLQEHDQVWCLPLQRNTPSLLRAHGVACVPSNCIQRGASMQLTLFDLLVPYTLRTWRTRVRAQMRFVARLLAEEEIYCDPLQPACTLSGGQLQRVILARELATRPRLLILAEPAEGLDSASEQRLLARLRQVAQAGTALVLLAREQHQAQWRALCTERFLLRAGTLCAEVSGTPSPSQDSHT
Probably part of the ABC transporter complex RfuABCD involved in riboflavin import. Probably responsible for energy coupling to the transport system.
O83321
Q99N34
DFFB_RAT
DNA fragmentation factor 40 kDa subunit
Rattus
MCAVLPQPKCVKLRALHSSCKFGVAARSCQELLRKGCIRFQLPVPGSRLCMYEDGTEVTDDCFPSLPNDSELLLLTAGETWHGYVSDITRLLSVFNEPHAGVIQAARQLLSDEQAPLRQKLLADLLHHVSQNITAETREQDPSWFEGLESRFRNKSGYLRYSCESRIRGYLREVSAYISMVDAAAREEYLRVLSSMCHKLKSVQYNGSYFDRGAEASSRLCTPEGWFSCQGPFDLESCLSKHSINPYGNRESRILFSTWNLDHIIEKKRTVVPTLAEAIQDGREVNWEYFYSLLFTAENLKLVHIACHKKTTHKLQCDRSRIYRPQTGSRRKQPPRKQPPRKRPPRKRQ
Nuclease that induces DNA fragmentation and chromatin condensation during apoptosis. Degrades naked DNA and induces apoptotic morphology.
Q99N34
Q2KI13
SGSM3_BOVIN
RUN and TBC1 domain-containing protein 3
Bos
MSGSHVPSANGPFSALTPSMWPQEILAKYAQEEATVEQPEFRYDEFGFRVDKEDADGIPYSGQLLEDPPQRLRWQAHLEFTHNHDVGDLTWDKIAVSLPRSEKLRSLVLAGVPHSMRPQLWMRLSGALQKKRNSELSYREIVKNSSNDETIAAKQIEKDLLRTMPSNACFAHVSGVGVPRLRRVLRALAWLYPEIGYCQGTGMVAACLLLFLEEDDAFWMMCAIIEDLLPASYFSTTLLGVQTDQRVLRHLIVQYLPRLDRLLQEHDIELSLITLHWFLTAFASVVHIRLLLRLWDLFFYEGSLVLFQATLGMLRLKEDELIQSENSASIFNTLSDIPSQLEDADLLLAEAMRLAGSLTAVAVETQRRKHLAYLLADQGQLLGAPATTGLSQVVRRRTQRRKSGITSLLFGEDDLEAMKAKNIKQTELVADLREAILRVARHFQCTDPKNCNVELTPDYSMESHQRDHESYVACSRGHPRRAKALLDFERHDDDELGFRKNDIITIVSQKDEHCWVGELNGLRGWFPAKFVEVLDERSKEYSIAGDDAVTEGVTDLVRGTLCPALKALLEHGLKKPSLLGGACHPWLFIEEAAGREVERDFDSVYSRLVLCKTYRLDEDGKVLTPEELLYRAVQSVNVTHDAAHAQMDVKLRSLICVGLNEQVLHLWLEVLCSSLPTVEKWYQPWSFLRSPGWVQIKCELRVLCCFAFSLSQDWELPAKREEEKKPLKEGVQDMLVKHHLFSWDIDG
May play a cooperative role in NF2-mediated growth suppression of cells.
Q2KI13
Q8DCA1
E4PD_VIBVU
D-erythrose-4-phosphate dehydrogenase
Vibrio
MLKVAINGFGRIGRNVLRAVYESGKHQQIKVVAVNELAQPEAMAHLLQYDTSHGRFGKRISHDQEHLYVHHDACPQGKGEFDSIRILHLSEINLLPWRDLEVDLVLDCTGVFGCQADGLEHIKAGAKKVLFSHPGASDLDNTIIYGVNHETLKAEHNVVSNGSCTTNCIVPIIKVLDEAFGIESGTITTIHSSMNDQQVIDAYHSDLRRTRAASQSIIPVDTKLHKGIERIFPKFSNKFEAISVRVPTVNVTAMDLSVTINTNVKVNDVNQTIVNASQCTLRGIVDYTEAPLVSIDFNHDPHSAIVDGSQTRVSNGHLVKMLVWCDNEWGFANRMLDTALAMQAAQ
Catalyzes the NAD-dependent conversion of D-erythrose 4-phosphate to 4-phosphoerythronate.
Q8DCA1
Q9FDS1
ALD1_ACISP
Aldehyde dehydrogenase 1
Acinetobacter
MHYVDPNQSGSKIHFKDQYENFIGGQWVAPVKGVYFDNISPVDGKSFTRIPRSSAEDIELALDAAHKAKKEWNKSSPTTRSNLLLKIADRMEANLEMLAVAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGGISEIDEDTIAYHFHEPLGVVGQIIPWNFPILMAAWKLAPALAAGNCVVIKPAEQTPVGILLVAELIQDLLPAGVLNIVNGYGAEVGRPLATSPRIAKIAFTGSTQVGQLIMQYATENIIPVTLELGGKSPNVFFADVMDHDDDFLDKTLEGFAMFALNQGEVCTCPSRALIQESIADQFMEKAIERVKRIKLGHPLDTDTMVGAQASLEQQEKILRCIDTGRQEGAEVLLGGHGRQEVGNGYYIEPTIFKGHNNMQVFQEEIFGPVLSVTTFKDFDEAIQIANDTMYGLGAGVWSRSTHTAYRAGRAIEAGRVWTNCYHIYPAHAAFGGYKKSGVGRENHKMMLDHYQQTKNLLVSYSTKAMGFF
Aldehyde dehydrogenase that shows activity toward n-alkanals (C(4) to C(14)), with a preference for longer carbon chains. The best substrate is tetradecanal.
Q9FDS1
P0DP91
ERPG3_HUMAN
Chimeric CSB-PGBD3 protein
Homo
MPNEGIPHSSQTQEQDCLQSQPVSNNEEMAIKQESGGDGEVEEYLSFRSVGDGLSTSAVGCASAAPRRGPALLHIDRHQIQAVEPSAQALELQGLGVDVYDQDVLEQGVLQQVDNAIHEASRASQLVDVEKEYRSVLDDLTSCTTSLRQINKIIEQLSPQAATSRDINRKLDSVKRQKYNKEQQLKKITAKQKHLQAILGGAEVKIELDHASLEEDAEPGPSSLGSMLMPVQETAWEELIRTGQMTPFGTQIPQKQEKKPRKIMLNEASGFEKYLADQAKLSFERKKQGCNKRAARKAPAPVTPPAPVQNKNKPNKKARVLSKKEERLKKHIKKLQKRALQFQGKVGLPKARRPWESDMRPEAEGDSEGEESEYFPTEEEEEEEDDEVEGAEADLSGDGTDYELKPLPKGGKRQKKVPVQEIDDDFFPSSGEEAEAASVGEGGGGGRKVGRYRDDGDEDYYKQRLSPKMPRTLSLHEITDLLETDDSIEASAIVIQPPENATAPVSDEESGDEEGGTINNLPGSLLHTAAYLIQDGSDAESDSDDPSYAPKDDSPDEVPSTFTVQQPPPSRRRKMTKILCKWKKADLTVQPVAGRVTAPPNDFFTVMRTPTEILELFLDDEVIELIVKYSNLYACSKGVHLGLTSSEFKCFLGIIFLSGYVSVPRRRMFWEQRTDVHNVLVSAAMRRDRFETIFSNLHVADNANLDPVDKFSKLRPLISKLNERCMKFVPNETYFSFDEFMVPYFGRHGCKQFIRGKPIRFGYKFWCGATCLGYICWFQPYQGKNPNTKHEEYGVGASLVLQFSEALTEAHPGQYHFVFNNFFTSIALLDKLSSMGHQATGTVRKDHIDRVPLESDVALKKKERGTFDYRIDGKGNIVCRWNDNSVVTVASSGAGIHPLCLVSRYSQKLKKKIQVQQPNMIKVYNQFMGGVDRADENIDKYRASIRGKKWYSSPLLFCFELVLQNAWQLHKTYDEKPVDFLEFRRRVVCHYLETHGHPPEPGQKGRPQKRNIDSRYDGINHVIVKQGKQTRCAECHKNTTFRCEKCDVALHVKCSVEYHTE
Involved in repair of DNA damage following UV irradiation, acting either in the absence of ERCC6 or synergistically with ERCC6. Involved in the regulation of gene expression. In the absence of ERCC6, induces the expression of genes characteristic of interferon-like antiviral responses. This response is almost completely suppressed in the presence of ERCC6. In the presence of ERCC6, regulates the expression of genes involved in metabolism regulation, including IGFBP5 and IGFBP7. In vitro binds to PGBD3-related transposable elements, called MER85s; these non-autonomous 140 bp elements are characterized by the presence of PGBD3 terminal inverted repeats and the absence of internal transposase ORF.
P0DP91
Q93ZX7
GAUT4_ARATH
Like glycosyl transferase 3
Arabidopsis
MMVKLRNLVLFFMLLTVVAHILLYTDPAASFKTPFSKRDFLEDVTALTFNSDENRLNLLPRESPAVLRGGLVGAVYSDKNSRRLDQLSARVLSATDDDTHSHTDISIKQVTHDAASDSHINRENMHVQLTQQTSEKVDEQPEPNAFGAKKDTGNVLMPDAQVRHLKDQLIRAKVYLSLPSAKANAHFVRELRLRIKEVQRALADASKDSDLPKTAIEKLKAMEQTLAKGKQIQDDCSTVVKKLRAMLHSADEQLRVHKKQTMFLTQLTAKTIPKGLHCLPLRLTTDYYALNSSEQQFPNQEKLEDTQLYHYALFSDNVLATSVVVNSTITNAKHPLKHVFHIVTDRLNYAAMRMWFLDNPPGKATIQVQNVEEFTWLNSSYSPVLKQLSSRSMIDYYFRAHHTNSDTNLKFRNPKYLSILNHLRFYLPEIFPKLSKVLFLDDDIVVQKDLSGLWSVDLKGNVNGAVETCGESFHRFDRYLNFSNPLISKNFDPRACGWAYGMNVFDLDEWKRQNITEVYHRWQDLNQDRELWKLGTLPPGLITFWRRTYPLDRKWHILGLGYNPSVNQRDIERAAVIHYNGNLKPWLEIGIPRYRGFWSKHVDYEHVYLRECNINP
May be involved in pectin and/or xylans biosynthesis in cell walls.
Q93ZX7
B3VZU6
TPCE_RANDY
Temporin-CDYe
Rana
MFTLKKSMLLLLFLGTISLTLCEEERDANEEEENGGEVKVEEKRFIGPIISALASLFGG
Antimicrobial peptide.
B3VZU6
A9WNC8
ATPB_RENSM
F-ATPase subunit beta
Renibacterium
MTATATEQGARTAAATGRIARVIGPVVDVEFPADAIPGIYHALTAEITLNGATHAVTFEVSQHLGDNLVRAISLQTTDGLVRGAVVTDTGAPISVPVGDGVKGHIFNVLGQPLDVAESEIQYTERWPIHRKPPSFDQLEGSTEMLETGIKSIDLLTPYIKGGKIGLFGGAGVGKTVLIQEMITRVARNFGGTSVFAGVGERTREGNDLWVEMEESGVLKDTALVFGQMDEPPGTRLRVALSALTMAEYFRDVQNQDVLLFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLADEMGLLQERITSTKGRSITSMQAVYVPADDYTDPAPAATFAHLDATTELSREIASRGLYPAIDPLTSTSRILDPQYIGKDHYDTAVRVKQILQKNKELQDIIAVLGVDELSEEDKIVVSRARRIQQFLSQNTYTAKQFTGVEGSTVSIKDTVEGFTAICNGDVDHIAEQAFFNVGAMDDVERQWAKIQESTK
Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
A9WNC8
Q7Z5J4
RAI1_HUMAN
Retinoic acid-induced protein 1
Homo
MQSFRERCGFHGKQQNYQQTSQETSRLENYRQPSQAGLSCDRQRLLAKDYYNPQPYPSYEGGAGTPSGTAAAVAADKYHRGSKALPTQQGLQGRPAFPGYGVQDSSPYPGRYAGEESLQAWGAPQPPPPQPQPLPAGVAKYDENLMKKTAVPPSRQYAEQGAQVPFRTHSLHVQQPPPPQQPLAYPKLQRQKLQNDIASPLPFPQGTHFPQHSQSFPTSSTYSSSVQGGGQGAHSYKSCTAPTAQPHDRPLTASSSLAPGQRVQNLHAYQSGRLSYDQQQQQQQQQQQQQQALQSRHHAQETLHYQNLAKYQHYGQQGQGYCQPDAAVRTPEQYYQTFSPSSSHSPARSVGRSPSYSSTPSPLMPNLENFPYSQQPLSTGAFPAGITDHSHFMPLLNPSPTDATSSVDTQAGNCKPLQKDKLPENLLSDLSLQSLTALTSQVENISNTVQQLLLSKAAVPQKKGVKNLVSRTPEQHKSQHCSPEGSGYSAEPAGTPLSEPPSSTPQSTHAEPQEADYLSGSEDPLERSFLYCNQARGSPARVNSNSKAKPESVSTCSVTSPDDMSTKSDDSFQSLHGSLPLDSFSKFVAGERDCPRLLLSALAQEDLASEILGLQEAIGEKADKAWAEAPSLVKDSSKPPFSLENHSACLDSVAKSAWPRPGEPEALPDSLQLDKGGNAKDFSPGLFEDPSVAFATPDPKKTTGPLSFGTKPTLGVPAPDPTTAAFDCFPDTTAASSADSANPFAWPEENLGDACPRWGLHPGELTKGLEQGGKASDGISKGDTHEASACLGFQEEDPPGEKVASLPGDFKQEEVGGVKEEAGGLLQCPEVAKADRWLEDSRHCCSTADFGDLPLLPPTSRKEDLEAEEEYSSLCELLGSPEQRPGMQDPLSPKAPLICTKEEVEEVLDSKAGWGSPCHLSGESVILLGPTVGTESKVQSWFESSLSHMKPGEEGPDGERAPGDSTTSDASLAQKPNKPAVPEAPIAKKEPVPRGKSLRSRRVHRGLPEAEDSPCRAPVLPKDLLLPESCTGPPQGQMEGAGAPGRGASEGLPRMCTRSLTALSEPRTPGPPGLTTTPAPPDKLGGKQRAAFKSGKRVGKPSPKAASSPSNPAALPVASDSSPMGSKTKETDSPSTPGKDQRSMILRSRTKTQEIFHSKRRRPSEGRLPNCRATKKLLDNSHLPATFKVSSSPQKEGRVSQRARVPKPGAGSKLSDRPLHALKRKSAFMAPVPTKKRNLVLRSRSSSSSNASGNGGDGKEERPEGSPTLFKRMSSPKKAKPTKGNGEPATKLPPPETPDACLKLASRAAFQGAMKTKVLPPRKGRGLKLEAIVQKITSPSLKKFACKAPGASPGNPLSPSLSDKDRGLKGAGGSPVGVEEGLVNVGTGQKLPTSGADPLCRNPTNRSLKGKLMNSKKLSSTDCFKTEAFTSPEALQPGGTALAPKKRSRKGRAGAHGLSKGPLEKRPYLGPALLLTPRDRASGTQGASEDNSGGGGKKPKMEELGLASQPPEGRPCQPQTRAQKQPGHTNYSSYSKRKRLTRGRAKNTTSSPCKGRAKRRRQQQVLPLDPAEPEIRLKYISSCKRLRSDSRTPAFSPFVRVEKRDAFTTICTVVNSPGDAPKPHRKPSSSASSSSSSSSFSLDAAGASLATLPGGSILQPRPSLPLSSTMHLGPVVSKALSTSCLVCCLCQNPANFKDLGDLCGPYYPEHCLPKKKPKLKEKVRPEGTCEEASLPLERTLKGPECAAAATAGKPPRPDGPADPAKQGPLRTSARGLSRRLQSCYCCDGREDGGEEAAPADKGRKHECSKEAPAEPGGEAQEHWVHEACAVWTGGVYLVAGKLFGLQEAMKVAVDMMCSSCQEAGATIGCCHKGCLHTYHYPCASDAGCIFIEENFSLKCPKHKRLP
Transcriptional regulator of the circadian clock components: CLOCK, ARNTL/BMAL1, ARNTL2/BMAL2, PER1/3, CRY1/2, NR1D1/2 and RORA/C. Positively regulates the transcriptional activity of CLOCK a core component of the circadian clock. Regulates transcription through chromatin remodeling by interacting with other proteins in chromatin as well as proteins in the basic transcriptional machinery. May be important for embryonic and postnatal development. May be involved in neuronal differentiation.
Q7Z5J4
P31350
RIR2_HUMAN
Ribonucleotide reductase small subunit
Homo
MLSLRVPLAPITDPQQLQLSPLKGLSLVDKENTPPALSGTRVLASKTARRIFQEPTEPKTKAAAPGVEDEPLLRENPRRFVIFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWESLKPEERYFISHVLAFFAASDGIVNENLVERFSQEVQITEARCFYGFQIAMENIHSEMYSLLIDTYIKDPKEREFLFNAIETMPCVKKKADWALRWIGDKEATYGERVVAFAAVEGIFFSGSFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLVHKPSEERVREIIINAVRIEQEFLTEALPVKLIGMNCTLMKQYIEFVADRLMLELGFSKVFRVENPFDFMENISLEGKTNFFEKRVGEYQRMGVMSSPTENSFTLDADF
Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. Inhibits Wnt signaling.
P31350
Q32J23
CRL_SHIDS
Sigma factor-binding protein Crl
Shigella
MTLPSGYPKSRLIKKFTALGPYIREGKCEDNRFFFDCLAVCVNVKPAPEVREFWGWWMELEAQESRFTYSYQFGLFDKAGDWKSVPVKDTEVVERLEHTLREFHEKLRELLTTLNLKLEPADDFRDEPVKLTA
Binds to the sigma-S subunit of RNA polymerase, activating expression of sigma-S-regulated genes. Stimulates RNA polymerase holoenzyme formation and may bind to several other sigma factors, such as sigma-70 and sigma-32.
Q32J23
Q9GKY7
JPH2_RABIT
Junctophilin-2 N-terminal fragment
Oryctolagus
MSGGRFDFDDGGAYCGGWEGGKAHGHGLCTGPKGQGEYSGSWNFGFEVAGVYTWPSGNTFEGYWSQGKRHGLGIETKGRWLYKGEWTHGFKGRYGTRQSTSSGAKYEGTWNNGLQDGYGTETYADGGTYQGQFTNGMRHGYGVRQSVPYGMAVVVRSPLRTSLSSLRSEHSNGTVAPDSPASPAADGPALPSPAIPRGGFALSLLANAEAARAPKGGGLFPRGALLGKLRRAESRTSVGSQRSRVSFLKSDLSSGASDAASTASLGEGAEGADDAAPFEADIDATTTETYMGEWKNDKRSGFGVSERSSGLRYEGEWLDNLRHGYGCTTLPDGHREEGKYRHNVLVKGTKRRVLPLKSNKVRQKVEHSVEGAQRAAAIARQKAEIAVSRTSHARAKAEAAEQAALAANQESNIARSLARELAPDFYQPGPEYQKRRLLQEILEHSESLLEPPDRGAAGLPQPPRESPQLHERETPRPEGGPPSPAGTPPQPKRPRPGASKDGLLGPGAWNGEPSGGSGGEGSRPATPAAAGAGRRSPARPASEHMAIEALQAPPAPSREPEVALYRGYHSYAVRTAPPAPPPFEDDPQPEAADPDSAPASPATAPGQAPALGNPEPAPESPAKLEPKPIVPKAKARKTEARGLSKTGAKKKPRKEAAQAAEAEVEVEEVPNTVLICMVILLNIGLAILFVHLLT
Transcription repressor required to safeguard against the deleterious effects of cardiac stress. Generated following cleavage of the Junctophilin-2 chain by calpain in response to cardiac stress in cardiomyocytes. Following cleavage and release from the membrane, translocates to the nucleus, binds DNA and represses expression of genes implicated in cell growth and differentiation, hypertrophy, inflammation and fibrosis. Modifies the transcription profile and thereby attenuates pathological remodeling in response to cardiac stress. Probably acts by competing with MEF2 transcription factors and TATA-binding proteins.
Q9GKY7
C0ZCB6
DER_BREBN
GTP-binding protein EngA
Brevibacillus
MGLPVVAIVGRPNVGKSTIFNRLIGERVAIVEDMPGVTRDRLYGKGEWLTHTFHVIDTGGIEFGETDEILTQMRYQAELAIDEADVIIMIADSRTGVTDADVELSRMLNRTGKPVVLAVNKADNPEMRADIYDFYSLGLGEPFPVSGSHGLGLGDMLEEVCQHFPAEDDEEKRDDVIRVSIIGRPNVGKSSLTNAILGEERVIVSEVAGTTRDAIDTPFERDDQSYVLVDTAGMRKRGKVYETTEKYSVMRAMRSIEDSDVVLVVINGEEGIIEQDKKIAGYAHEAGRGVIIIVNKWDAIEKDDKTMQRFTELIREEFKYLDYAPILYVSAKSKQRVHTILPKVNEVAQAHSMRIPTAVLNDLVTDATIRTPPPSDRGKRLKINYATQATVKPPTFILFVNDPELMHFSYERYIENKIREAFVFEGTPVRIWTRKKT
GTPase that plays an essential role in the late steps of ribosome biogenesis.
C0ZCB6
Q82MN2
TDH_STRAW
L-threonine 3-dehydrogenase
Streptomyces
MKALVKEKAEPGLWLMDVPEPEIGPGDVLIKVLRTGICGTDLHIRSWDGWAQQAVRTPLVLGHEFVGEVVETGRDVVDIKAGDRVSGEGHLVCGKCRNCQAGRRHLCRATVGLGVGRDGAFAEYVALPAANVWVHRVPVDLDVAAIFDPFGNAVHTALSFPLVGEDVLITGAGPIGLMAAAVARHAGARNVMITDVSEERLELARKIGVSLALNVADTTIADGQRALGLREGFDIGLEMSGRPEAMRDMIANMTHGGRIAMLGLPSQEFPVDWARIVTSMITIKGIYGREMFETWYAMSVLLEGGLDLAPVITGRYGYRDYEAAFADAASGRGGKVILDWTL
Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2-amino-3-ketobutyrate.
Q82MN2
B1YFL0
UNG_EXIS2
Uracil-DNA glycosylase
Exiguobacterium
MHTAWQEILKEEKEKDYFIRLWDFVKTAYRETTVYPPKDRIFHAFDAVAPQDVRCVILGQDPYHGPNQANGLSFSVNDGVAIPPSLRNMYKELMSDLGCPAPTTGNLEAWSNQGVFLLNTSLTVEAGKAGSHAKKGWESFTDRVIEVLGQQEQPIVFILWGNHAKSKKSLIDTNRHLVLESVHPSPLSASRGFFGSRPYSQTNDWLQQQNRTPIDWCIS
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.
B1YFL0
A2AIP0
F166B_MOUSE
Protein FAM166B
Mus
MAVVNTSIPGLSGENPHYIPGYTGHCPLLRFSMGQTYGQVTGQLLRGPPGLAWPPAHRTLLPPIQSPRSPVISKGRLPPRRGHERLSSSIIPGYTGFIPRAQFIFAKNCNQVWAEAMSEFTRRHGEQESHQLPDGAKGEREVEEDQLREAEEPPLKQELAHASPYSMDDTDPHKFFMSGFTGYVPRARFLFGSSFPVLTNQALQEFGQMCSRGRAHKDPKPLSPLPRPTFQNLGLLPHYGGYVPGYKFQFGGTFGHLTHDALGLSITQKQLPA
Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating.
A2AIP0
Q6ICY4
MTPC2_ARATH
AtMTP5
Arabidopsis
MERSISFNPRGDNELPDDRSSDVGYAANDRRLAYSRSFQQSHGPRTPAVTEAAKPFLDRTVSSIDMPPDIYSVDGSDVFFGEGKDVDMAKVSVLEMVWEVFGVVTSGNRQMKRLFLLIALNVLYSTTELSIGIFTGRVGLVSDAFHLTFGCGLLTFSLFAMATSRKKPDHAYSYGYKRLEVLSAFTNALFLMFMSFSLAVEALHAFIQDESEHKHYLIVSAVTNLLVNLLGVWFFRNYARVNIAYRKAEDMNYHSVCLHVISDSIRSAGLILASWLLSLGVENAEVLCLGLVSVTVFMLVMPLFKATGGVLLQMAPPNIPSSALSKCLRQITSREDVTEVLQARFWEVVPGHTVGSLRLQVKSGIDERPLLQYVYDVYHDLGVQDLTLQTDYT
Involved in sequestration of excess metal in the cytoplasm into vacuoles to maintain metal homeostasis.
Q6ICY4
A7Z501
HFQ_BACVZ
RNA-binding protein Hfq
Bacillus amyloliquefaciens group
MKPINIQDQFLNQIRKDNTFVTVFLLNGFQLRGQVKGFDNFTVLLETEGKQQLIYKHAISTFAPQKNVQLELE
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.
A7Z501
Q5LY84
PROA_STRT1
Glutamyl-gamma-semialdehyde dehydrogenase
Streptococcus
MTYIDTLGQQAKVASRQIAKLSTAAKNDLLNQVAKALVAESDYIITENAKDMANASENGISKIMQDRLLLTEDRIAGIAEGVRQVADLQDPIGQVVRGYTNLDGLKIVQKRVPMGVIAMIFESRPNVSIDAFSLAFKTNNAIILRGGRDAINSNKALVTVARKALKNAGITADAVQFVEDTSHEVAEELMVATKYVDLLIPRGGARLIQTVKEKAKVPVIETGVGNCHIYVDKYANLDMATQIVINAKTQRPSVCNAAESLVVHADIVEEFLPNLEKAILKIQSVEFRADERALKLMEKAVPASPEDFATEFLDYIMSVKVVDSLDEAINWINTYTTSHSEAIVTQDISRAEQFQDDVDAAAVYVNASTRFTDGFVFGLGAEIGISTQKMHARGPMGLEALTSTKFYINGQGQIRE
Catalyzes the NADPH-dependent reduction of L-glutamate 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate.
Q5LY84
O07669
MURD_ENTHR
null
Enterococcus
MTGNEKNFNHSKTKKVLVLGLAKSGFSAAKLLHELGALVTVNDGKPFDEKPEAQELLSLGVKVIAGSHPIELLDEEFSLMVKNPGIPYSHPFVQKAQELGIPVITEVELAYEVAECPIIGITGTNGKTTTTTMTGLLLNAGDLPGTARLAGNIGYPASSVAQEATADDKIVMELSSFQLMGITDFRPHVAVVTNIYEAHIDYHKTRKEYVKAKWHLQQNMTEKDYLILNWNQEELRELSKKTKATVLPFATEQKLPKGACSLDGSIYYNQEKIMDITELGVPGSHNVENALAAISVAKLYGISNEAIKNALHHFHGVPHRTQYVGEFQGRKFYNDSKATNILATKMALSGFQLDQLVLIAGGLDRGNSFDELIPALKGIKALITFGETQNRLEDAGKKAGIPVIKTAENAEAAVPIALELSEEGDSILLSPANASWDQYPNFEIRGERFMEAVNKLTIQK
Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
O07669
Q8AY43
VKTA_BUNCA
Kunitz inhibitor A
Bungarus
MSSGGLLLLLGLLTLCAELTPVSSKDRPKFCNVPPEPGRCNANVRAFYYNPRLRKCIEFTYGGCGGNANNFKSRGECKRTCAE
Serine protease inhibitor.
Q8AY43
Q9PHQ1
PSTB_CAMJE
Phosphate-transporting ATPase
Campylobacter
MIAKTTNLNLFYGKKQALFDINMQIEQNKITALIGASGCGKSTFLRCFNRMNDKIAKIDGLVEIKGKDVKNQDVVALRKNVGMVFQQPNVFVKSIYENISYAPKLHGMIKNKDEEEALVVDCLQKVGLFEEVKDKLKQNALALSGGQQQRLCIARALAIKPKLLLLDEPTSALDPISSGVIEELLKELSHNLSMIMVTHNMQQGKRVADYTAFFHLGELIEFGESKEFFENPKQEKTKAYLSGAFG
Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system.
Q9PHQ1
Q7L3V2
BOP_HUMAN
Retrotransposon Gag-like protein 10
Homo
MPRGRCRQQGPRIPIWAAANYANAHPWQQMDKASPGVAYTPLVDPWIERPCCGDTVCVRTTMEQKSTASGTCGGKPAERGPLAGHMPSSRPHRVDFCWVPGSDPGTFDGSPWLLDRFLAQLGDYMSFHFEHYQDNISRVCEILRRLTGRAQAWAAPYLDGDLPLPDDYELFCQDLKEVVQDPNSFAEYHAVVTCPLPLASSQLPVAPQLPVVRQYLARFLEGLALDMGTAPRSLPAAMATPAVSGSNSVSRSALFEQQLTKESTPGPKEPPVLPSSTCSSKPGPVEPASSQPEEAAPTPVPRLSESANPPAQRPDPAHPGGPKPQKTEEEVLETEGDQEVSLGTPQEVVEAPETPGEPPLSPGF
Could induce apoptosis in a BH3 domain-dependent manner. The direct interaction network of Bcl-2 family members may play a key role in modulation RTL10/BOP intrinsic apoptotic signaling activity.
Q7L3V2
B2IFY8
RL19_BEII9
50S ribosomal protein L19
Beijerinckia
MNIIETLEAEQAAKLLAKRPIPAFQPGDTVIVNVKVKEGERTRVQAYEGVCIARNGGGLNESFTVRKISYGEGVERVFPIYSPNIDSIKVVRRGKVRRAKLYYLRDRRGKAARIAEKMETPAAKAAREAAKKEAKAAAKAKKAASAAE
This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site.
B2IFY8