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
|
|---|---|---|---|---|---|---|
Q1BYH4
|
UREF_BURCA
|
Urease accessory protein UreF
|
Burkholderia cepacia complex
|
MTTTELVALLHLASPALPIGAYSYSQGLEAALDANLIRDADSARDWIASGLTDVLAHGELPFLAHQLARWQTHDTHALAAENAWFVASRESAELRRETEQMGWSLAQLCASLEWGDAARRATLASLSPIALPTAFAYAAAAHDAGADATLAAYAFGWVENQTSAALKAVPLGQLAGQRIIVALRGAIDAAVRRALATPPDAVNTFAPQLGILSARHETQYSRLFRS
|
Required for maturation of urease via the functional incorporation of the urease nickel metallocenter.
|
Q1BYH4
|
A7INK7
|
TPIS_XANP2
|
Triose-phosphate isomerase
|
Xanthobacter
|
MPASRRVLIAGNWKMNGLKSSLAEIEALAAGYDGDLKAKLDLLVCPPATLLISAAERLAGSGVQLGGQNCHPAPAGAHTGGISAEMLKDAGVTSVIVGHSERRTNLSESDAVVMAKVKAAWCFGLLPIVCVGETAEERDAGEAVGVVTRQVHQSLPEGCTASNLVIAYEPVWAIGTGRTPTPEDVANIHGTIRSVLRSQFGAEADGIRILYGGSVKPDNAATLMAVADVDGALVGGASLKAADFLAIARATPAR
|
Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
|
A7INK7
|
Q2TL60
|
ZN667_MOUSE
|
Myocardial ischemic preconditioning up-regulated protein 1
|
Mus
|
MPAVRGKSKSKAPVTFGDLAIYFSQEEWEWLSPMQKDLYEDVMLENYHNLVSVGLACRRPNIIALLEKGKAPWVIEPSRRRWGPESGSKYETKKLPPNSCHKSGPSICEKPTSSQQKVPTEKAKHNKSSVPSKSKKEHSGKKSLKCNLCGKTFFRSLSLKLHQDFHTGERSYECSTCRHVFRQILSLILHQRVHNWNKSYECDKCGDIFNKKLTLMIHRRIHNGKESFHHEKASDSCPSLSLHRNNHTTDSVHQCRKCGKVFSRMSSLLLHKRSHNRKKIQKYNKYKRGFKKQPVLVHKRVCIGKKTHESKKALIQSARQKTCQSENPFMCGKCGKSFSRISALMLHQRIHTSGNPYKCDKCQKDFGRLSTLILHLRIHSGEKQFKCSKCEKVCSRLSSFIQHQKIHKRKKKLIACKECGKMFGGMKNLKVHLNIHSEEKPFKCNKCSKVFGRQSFLSEHQRIHTGEKPYQCEECGKAFSHRISLTRHKRIHSEDRPYECDLCGKAFSQSAHLAQHERIHTGEKPYACKICKKSFAQRISLILHERSHTGERPYECNECGKAFSSGSDLIRHQRSHSSEKPYECSKCGKAYSRSSSLIRHQSIHSEETP
|
May be involved in transcriptional regulation.
|
Q2TL60
|
Q7VDG6
|
YIDD_PROMA
|
Putative membrane protein insertion efficiency factor
|
Prochlorococcus
|
MIKKINAVISNLFLTLIRFYRSWISPLLGPSCRFVPTCSEYGVEAIEKHGPWKGGWLTLKRLLRCNPLTPCGYDPVPDK
|
Could be involved in insertion of integral membrane proteins into the membrane.
|
Q7VDG6
|
A9MAR7
|
TRMFO_BRUC2
|
Folate-dependent tRNA(M-5-U54)-methyltransferase
|
Brucella
|
MSNNTDLSPVHVIGGGLAGSEAAWQIAQAGVPVVLHEMRPVRGTDAHKTEQLAELVCSNSFRSDDAETNAVGVLHAEMRLAGSLIMACADAHQVPAGGALAVDREGFSQAVTARLEAHPLITIEREEITGLPPTEWGTTIIATGPLTAPSLAEAIAAETDADALAFFDAIAPIIHFDSINMDVCWFQSRYDKVGPGGTGKDYINCPMDEEQYEAFVAALIEGDKTDFKEWEGTPYFDGCLPIEVMAERGPETLRHGPMKPMGLTNAHNPTVKPYAVVQLRQDNALGTLYNMVGFQTKLKYGSQTGIFKMIPGLENAEFARLGGLHRNTYLNSPVLLDNVLRLKSRQTLRFAGQVTGCEGYVESSAIGLLAGRFTAAEKLSQAAVPPPPTTAFGALLGHITGGHIVTDDEPGKRSFQPMNVNFGLFPPVDVPKPEGKRLRGKEKTIAKKRALSARALADCRNWLSLY
|
Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs.
|
A9MAR7
|
Q9BRT2
|
UQCC2_HUMAN
|
Mitochondrial protein M19
|
Homo
|
MAASRYRRFLKLCEEWPVDETKRGRDLGAYLRQRVAQAFREGENTQVAEPEACDQMYESLARLHSNYYKHKYPRPRDTSFSGLSLEEYKLILSTDTLEELKEIDKGMWKKLQEKFAPKGPEEDHKA
|
Required for the assembly of the ubiquinol-cytochrome c reductase complex (mitochondrial respiratory chain complex III or cytochrome b-c1 complex). Plays a role in the modulation of respiratory chain activities such as oxygen consumption and ATP production and via its modulation of the respiratory chain activity can regulate skeletal muscle differentiation and insulin secretion by pancreatic beta-cells. Involved in cytochrome b translation and/or stability.
|
Q9BRT2
|
Q7M722
|
TR114_MOUSE
|
Taste receptor type 2 member 114
|
Mus
|
MLSTMEGVLLSVSTSEAVLGIVGNTFIALVNCMDYNRNKKLSNIGFILTGLAISRICLVLILITEAYIKIFYPQLLSPVNIIELISYLWIIICQLNVWFATSLSIFYFLKIANFSHYIFVWLKRRIDLVFFFLIGCLLISWLFSFPVVAKMVKDNKMLYINTSWQIHMKKSELIINYVFTNGGVFLFFMIMLIVCFLLIISLWRHRRQMESNKLGFRDLNTEVHVRTIKVLLSFIILFILHFMGITINVICLLIPESNLLFMFGLTTAFIYPGCHSLILILANSRLKQCSVMILQLLKCCENGKELRDT
|
Putative taste receptor which may play a role in the perception of bitterness.
|
Q7M722
|
A8QL53
|
VSP1_NAJAT
|
Snake venom serine protease NaSP
|
Naja
|
MVLIRVLASLLILQLSYSKSLDDGAKESAYDDEIQQSSWGNSTVNTTLTETVVIQLIMGGSECYKSKHPFLVYLYNSAGFFCSGTLLNHEWVLTAAHCNRDDIQLKLGVHNVHVHYEDEQIRVPKEKLCCLSTKNCTQWSQDIMLIRLNSSVNNSKHIEPLSLPSRPPSMGSDCTVMGWGTITSPKVTYPKVPHCVDIKILHNPVCQAAYPTMSRKNILCAGVLEGGKDSCKGDSGGPLICDGQIQGIVSWGRFPCAQLLEPGVYTKVFDYIDWIRGIIAGN
|
Snake venom serine protease that may act in the hemostasis system of the prey.
|
A8QL53
|
P30739
|
TNPT_PSEPU
|
Resolvase/recombinase
|
Pseudomonas
|
MRLFGYARVSTSQQSLDVQIKALKAENVRATRIFTDKVSGSHVNREGLRMLRLKVEEGDVVLVKKLDRLGRDTADMIQLIKEFDDMGVAIRFLDDGISTEGTMGKMVVTILSAVAQAERLRILERTNEGRLEAKAKGVKFGRKPTVDKAEVFTLHGQGISAMEIAKRLKIGRSTVYKVLAS
|
Site-specific recombination protein.
|
P30739
|
O95847
|
UCP4_HUMAN
|
Solute carrier family 25 member 27
|
Homo
|
MSVPEEEERLLPLTQRWPRASKFLLSGCAATVAELATFPLDLTKTRLQMQGEAALARLGDGARESAPYRGMVRTALGIIEEEGFLKLWQGVTPAIYRHVVYSGGRMVTYEHLREVVFGKSEDEHYPLWKSVIGGMMAGVIGQFLANPTDLVKVQMQMEGKRKLEGKPLRFRGVHHAFAKILAEGGIRGLWAGWVPNIQRAALVNMGDLTTYDTVKHYLVLNTPLEDNIMTHGLSSLCSGLVASILGTPADVIKSRIMNQPRDKQGRGLLYKSSTDCLIQAVQGEGFMSLYKGFLPSWLRMTPWSMVFWLTYEKIREMSGVSPF
|
UCP are mitochondrial transporter proteins that create proton leaks across the inner mitochondrial membrane, thus uncoupling oxidative phosphorylation from ATP synthesis. As a result, energy is dissipated in the form of heat. May play a role in thermoregulatory heat production and metabolism in brain.
|
O95847
|
Q96PF2
|
TSSK2_HUMAN
|
Serine/threonine-protein kinase 22B
|
Homo
|
MDDATVLRKKGYIVGINLGKGSYAKVKSAYSERLKFNVAVKIIDRKKTPTDFVERFLPREMDILATVNHGSIIKTYEIFETSDGRIYIIMELGVQGDLLEFIKCQGALHEDVARKMFRQLSSAVKYCHDLDIVHRDLKCENLLLDKDFNIKLSDFGFSKRCLRDSNGRIILSKTFCGSAAYAAPEVLQSIPYQPKVYDIWSLGVILYIMVCGSMPYDDSDIRKMLRIQKEHRVDFPRSKNLTCECKDLIYRMLQPDVSQRLHIDEILSHSWLQPPKPKATSSASFKREGEGKYRAECKLDTKTGLRPDHRPDHKLGAKTQHRLLVVPENENRMEDRLAETSRAKDHHISGAEVGKAST
|
Testis-specific serine/threonine-protein kinase required during spermatid development. Phosphorylates TSKS at 'Ser-288' and SPAG16. Involved in the late stages of spermatogenesis, during the reconstruction of the cytoplasm. During spermatogenesis, required for the transformation of a ring-shaped structure around the base of the flagellum originating from the chromatoid body.
|
Q96PF2
|
A9N9F4
|
UBIE_COXBR
|
Demethylmenaquinone methyltransferase
|
Coxiella
|
MNETEKSTHFGYQTVPTDQKTDKVKHVFESVAAKYDLMNDLMSLGIHRCWKDFAITQCRLRTGQRILDLAGGTGDLAKRISPLVGDEGEVVIADINAAMLNVGRRRLLDQGIFRNIQFIQADAEKLPFPNNFFDRIVIGFGLRNVTNQLAALQSMHRVIKPGGFVVILEFSKPTLAPLKAVYDAYSFQLLPRLGKLVAKDEESYRYLVESIRMHPDQEALLSKMTDAGFEDCDYHNLSGGIVAVHRGYKF
|
Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2) and the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2).
|
A9N9F4
|
Q5PI73
|
TREA_SALPA
|
Alpha,alpha-trehalose glucohydrolase
|
Salmonella
|
MIPPEIRRSVLLQKAIKLALAGTLLTFASFSATAADPSSDTETPQPPDILLGPLFNDVQNAKLFPDQKTFADAIPNSDPLMILADYRMQRNQSGFDLRHFVDVNFTLPKAGEKYVPPAGQSLREHIDGLWPVLTRSTKNVEKWDSLLPLPESYVVPGGRFREIYYWDSYFTMLGLAESGHWDKVADMVANFGYEIDAWGHIPNGNRTYYLSRSQPPFFAFMVELLAQHEGDDALKEYLPQLQKEYAYWMEGVETLQPGQQNQRVVKLEDGSVLNRYWDDRDTPRPESWVEDIATAKSNPNRPATEIYRDLRSAAASGWDFSSRWMDNPQQLSTIRTTTIVPVDLNALLYQLEKTLARASAAAGDRAKASQYDALANARQKAIEMHLWNNKEGWYADYDLQNNKIRDQLTAAALFPLYVNAAAKDRAVKVAAAAQAHLLQPGGLATTSVKSGQQWDAPNGWAPLQWVAAEGLQNYGQDDVAMEVTWRFLTNVQHTYDREKKLVEKYDVSSTGTGGGGGEYPLQDGFGWTNGVTLKMLDLICPQEKPCDSVPSTRPASLSATPTKTPSAATQ
|
Provides the cells with the ability to utilize trehalose at high osmolarity by splitting it into glucose molecules that can subsequently be taken up by the phosphotransferase-mediated uptake system.
|
Q5PI73
|
Q9Y397
|
ZDHC9_HUMAN
|
Zinc finger protein 380
|
Homo
|
MSVMVVRKKVTRKWEKLPGRNTFCCDGRVMMARQKGIFYLTLFLILGTCTLFFAFECRYLAVQLSPAIPVFAAMLFLFSMATLLRTSFSDPGVIPRALPDEAAFIEMEIEATNGAVPQGQRPPPRIKNFQINNQIVKLKYCYTCKIFRPPRASHCSICDNCVERFDHHCPWVGNCVGKRNYRYFYLFILSLSLLTIYVFAFNIVYVALKSLKIGFLETLKETPGTVLEVLICFFTLWSVVGLTGFHTFLVALNQTTNEDIKGSWTGKNRVQNPYSHGNIVKNCCEVLCGPLPPSVLDRRGILPLEESGSRPPSTQETSSSLLPQSPAPTEHLNSNEMPEDSSTPEEMPPPEPPEPPQEAAEAEK
|
(Microbial infection) Through a sequential action with ZDHHC20, rapidly and efficiently palmitoylates SARS coronavirus-2/SARS-CoV-2 spike protein following its synthesis in the endoplasmic reticulum (ER). In the infected cell, promotes spike biogenesis by protecting it from premature ER degradation, increases half-life and controls the lipid organization of its immediate membrane environment. Once the virus has formed, spike palmitoylation controls fusion with the target cell.
|
Q9Y397
|
Q1I4H6
|
THIE_PSEE4
|
Thiamine-phosphate pyrophosphorylase
|
Pseudomonas
|
MTLRGLYAITDSQLLAGRFLSHVEAALEGGVCLLQYRDKSDDAGRRLREAEGLKKLCERYGTQLIINDDAELAARLGVGVHLGQTDGPLTPARALLGRQAIIGSTCHASLELAEQAASEGASYVAFGRFFNSVTKPGAPAASLELLEQARARVKLPIAVIGGITLDNAAPLVAHGADLLAVIHGLFGADSAQEVTRRARAFNALFAS
|
Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
|
Q1I4H6
|
A0M672
|
UVRC_GRAFK
|
Excinuclease ABC subunit C
|
Gramella
|
MEKPALEVQLKTLPNSPGVYQYFDKNGKILYVGKAKNLKKRVTSYFNKNHDSHRIGVMVKKICEIKHIVVASETDALLLENNLIKKHQPRFNVMLKDDKTYPWICIKNERFPRVFPTRRLIKDGSEYYGPFTSFKTVNTLLDLIKGLYKLRTCNYDLAEDKIRNGKYKVCLEYHLGNCLGPCEGFQPEEEYNNNIEAIRQIVKGNFKDSLQRFRNQMKQHSEKMEFEDAQRIKNKIDVLENYQAKSTVVNPRINNVDVFSVVSDEGYGYVNFLQLSHGAIIRSHTIEMKKKLDESDRELLELAIVEIRQRFSSNSTEIYVPFKVDVGEELKIVIPKLGDKKKIVELSQRNAKYFRQERFKQMKIVDPDRHVNRVMAQMKEDLRLGKEPRHIECFDNSNIQGTNPVAACVVFKNGKPSKKDYRKFNIKTVEGPDDFASMEEVVFRRYRRLLNEGEDLPELIIVDGGKGQLSSGVKALETLGLRGKIAIIGIAKRLEEIFYPEDSIPLYLDKKSETLKIIQQLRNEAHRFGITFHRNKRSKTALNTELESIQGIGEKTVVELLTHFRSLKRIKEASQKELADVVGSAKAAIICNFYHSE
|
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision.
|
A0M672
|
Q8EBZ8
|
YQGF_SHEON
|
Putative pre-16S rRNA nuclease
|
Shewanella
|
MNAKTVLGFDFGTKSIGVAVGQQITASATPLLSIKAVDGIPNWEEIAKLIQEWQPDLVVVGLPLNMDGTEQEMTHRARKFANRLNAKFGVKIFTQDERLTTTDAKARLFELGGYKALTKGQVDAVSAVLIIESYFENHFGD
|
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
|
Q8EBZ8
|
Q14IB6
|
TDH_FRAT1
|
L-threonine 3-dehydrogenase
|
Francisella
|
MKALAKLKKQPGIWIINDAPIPEYGYNDVLIKIKKTAICGTDLHIYNWDKWSQNTIPVPMITGHEFAGEVVAKGDGVTSVDIGDRVSGEGHLVCGQCRNCRAGKRHLCRKTIGIGVNVQGAFAEYLVMPAVNVFKIPDSISDDIASTFDPMGNAIHTALSFNLTGEDVLITGAGPIGLMAVKIARFCGARRIVITDINEYRLQMARDFGATVALNVAPFKNQDELVKQMRKVMSDIGMTEGFDVGLEMSGINSAISMMLDVMNHGGKLSLLGISAGDISVDWGAILFKGLTLKGIYGREMFETWYLMTSMLQAGMDMNPIITHRLHIDEFQKGFEIMKSGQCGKVILDWSS
|
Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2-amino-3-ketobutyrate.
|
Q14IB6
|
P21609
|
THIO_PEPLI
|
Thioredoxin
|
Peptoclostridium
|
MLMLDKDTFKTEVLEGTGYVLVDYFSDGCVPCKALMPAVEELSKKYEGRVVFAKLNTTGARRLAISQKILGLPTLSLYKDGVKVDEVTKDDATIENIEAMVEEHISK
|
Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions.
|
P21609
|
P76500
|
YFCQ_ECOLI
|
Uncharacterized fimbrial-like protein YfcQ
|
Escherichia
|
MRKTFLTLLCVSSAIAHAADEDITFHGTLLSPPTCSISGGKTIEVEFRDLIIDDINGNYGRKEVPYELTCDSTTRHPDWEMTLTWTGTQTSFNDAAIETDVPGFGIELQHDGQRFKLNTPLAINATDFTQKPKLEAVPVKASDAVLSDTNFSAYATLRVDYQ
|
Part of the yfcOPQRSUV fimbrial operon. Could contribute to adhesion to various surfaces in specific environmental niches. Increases adhesion to eukaryotic T24 bladder epithelial cells in the absence of fim genes.
|
P76500
|
Q8EGF9
|
TILS_SHEON
|
tRNA(Ile)-lysidine synthetase
|
Shewanella
|
MTAQDLSVHIARWLDSLPLQAGSKLVLAYSGGVDSEVLAYGLSEYAKQRPDLRYQLIYVHHGLSPNADNWAKHCQARAAIYGLPVTVERVQLILGPRVSVEAEARKARYQAILPHLNPQDILLTAHHEDDQLETILLALKRGQGPKGLAAMGQIQPLSLADKGSCLQVRPLLDISREMIETFAQTRQLVHIEDESNQDDKYDRNFLRLEIIPRLKARWPSIATTASRSAQLCAEQQAIVETEVSERLPKLLVKAPVTEQTVLKLSELAAQPIEWQGILLRGFIESQEFSLPSYVQLQQMLQQLIHAKEDAKVHIRINDCVLRRFAGMLYLDSGETLSTALHITARDLHQEILTLLTQASAMVEDKIVPFALVTTGPRLRLPKADEVVSLGYGLPGQFRCQPHFRDKGRELKKLWQECAVPPWLRAEVGFLFYNDKLVMAFGLWVEKAFCAQGDEIGLSYLIANP
|
Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
|
Q8EGF9
|
A4IF63
|
TRIM2_BOVIN
|
RING-type E3 ubiquitin transferase TRIM2
|
Bos
|
MASEATNIPSPVVRQIDKQFLICSICLERYKNPKVLPCLHTFCERCLQNYIPAHSLTLSCPVCRQTSILPEKGVAALQNNFFITNLMDVLQRSPGSSAEESSILETVTAVAAGKPLSCPNHDGNVMDFYCQSCETAMCRECTEGEHAEHPTVPLKDVVEQHKASLQVQLDAANRRLPEIDSALQFISEIIHQLTNQKASIVDDIHSTFDELQKTLNVRKSVLLMELEVNYGLKHKVLQSQLDTLLEGQESIKSCSNFTAQALNHGTETEVLLVKKQMSEKLNELADQDFPLHPRENDQLDFIVETEGLKKSIHNLGTILTTNAVASETVATGEGLRQTIIGQPMSVTITTKDKDGELCKTGNAYLTAELSTPDGSVADGEILDNKNGTYEFLYTVQKEGDFTLSLRLYDQHIRGSPFKLKVIRSADVSPTTEGVKRRVKSPGSGHVKQKAVKRPASMYSTGKRKENPIEDDLIFRVGTKGRNKGEFTNLQGVAASTNGKILIADSNNQCVQIFSNDGQFKSRFGIRGRSPGQLQRPTGVAVHPSGDIIIADYDNKWVSIFSSDGKFKTKIGSGKLMGPKGVSVDRNGHIIVVDNKACCVFIFQPNGKIVTRFGSRGNGDRQFAGPHFAAVNSNNEIIVTDFHNHSVKVFNQEGEFMLKFGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDGSGSFLSYINTSADPLYGPQGLALTSDGHVVVADSGNHCFKVYRYLQ
|
E3 ubiquitin-protein ligase that mediates the ubiquitination of phosphorylated BCL2L11. Also mediates the UBE2D1-dependent ubiquitination of NEFL. Plays a neuroprotective function. May play a role in neuronal rapid ischemic tolerance.
|
A4IF63
|
A9W297
|
UREG2_METEP
|
Urease accessory protein UreG 2
|
Methylorubrum
|
MKKITRIGIGGPVGSGKTAVIETITPRLIALGIKPLIITNDVVTTEDAKQVRRTLHGVLIEEKIVGVETGACPHTAVREDPSMNIAAVEELEDKYPDSDVILIESGGDNLTLTFSPALADFYIYVIDVAAGDKIPRKNGAGVCQSDILVINKKDLAPYVGASLEVMARDSKLMRGKKPFLFTNCKTGEGVDDLLQLILDMALFDVRTRPPLAASA
|
Facilitates the functional incorporation of the urease nickel metallocenter. This process requires GTP hydrolysis, probably effectuated by UreG.
|
A9W297
|
Q05589
|
UROK_BOVIN
|
Urokinase-type plasminogen activator chain B
|
Bos
|
MRVLLACLLVCALVVSDSDGSNEVHKESGESNCGCLNGGKCVTYKYFSNIQRCSCPKKFQGEHCEIDTSKTCYQGNGHSYRGKANRDLSGRPCLAWDSPTVLLKMYHAHRSDAIQLGLGKHNYCRNPDNQRRPWCYVQIGLKQFVQFCMVQDCSVGKSPSSPREKEEFQCGQKALRPRFKIVGGQVTNAENQPWFAAIYRRHRGGSITYLCGGSLISPCWVVSATHCFIDHPKKENYIVYLGQSRLNSDTRGEMQFEVEKLILHEDYSAESLAHHNDIALLKIRTSRGQCAQPSRSIQTICLPPEHEDAHSRTRCEITGFGKENPSDYRYSDELKMTFVSLVSHEVCQQPHYYGAEVTDKMLCAADPQWETDSCQGDSGGPLVCTIQGRLTLTGIVSWGRDCAMKYKPGVYTRVSKFLPWINTHTRGEINLVL
|
Specifically cleaves the zymogen plasminogen to form the active enzyme plasmin.
|
Q05589
|
Q9NEZ5
|
UNC95_CAEEL
|
LIM domain-containing protein unc-95
|
Caenorhabditis
|
MTISPQPSHQQFESYQWTTESRSSQQRHGTGTPSQDGRLSAIPDPVERHVARWRSESRNSNKDKVFRNDEEFSQQDEIVNGTLTALKNDVEQTTEIIRRKQEQMRMERRQFQTEMEVNGRISIDPTDDWLAARLKAVSSDDMNQQLVKLKQDQRQNAVTDTLAALVYDVNATTEVLRRGQRGRDGEDGNKKKKEEIEYTLRLTPAPEEQIPQRPKIPEDDNMETDDYSRQYGVQMSEETDSLRRRRARSTTPRRTLHISGSPPPPAAAVCAYCSEEIDGAILTALAPNSERAQKFHTYHFMCTYCQKALNMHGTYREHDLKPYCHDCFYKLYNGLQYAPDDHQASIEKLI
|
Required for the assembly and integrity of muscle dense bodies, which establish the adhesion sites of the muscle cells to the extracellular matrix . Decreased localization of unc-95 to dense bodies and their subsequent dissociation plays an important role in ecdysis during molting . Involved in the organization of the muscle sarcomeric structure and thereby required for locomotion .
|
Q9NEZ5
|
Q1D6I2
|
TRMD_MYXXD
|
tRNA [GM37] methyltransferase
|
Myxococcus
|
MSPPYPVEILTLFPGMVTGYLGASILGKAQEKGLLATTITDIREYAEGKHRVTDDAPYGGGAGMVMKPEPLVAAIEAAKARHPGARVLLMSPRGPTFTQATARELVRHEAGLILVCGRYEGVDERVMAHLDGELSLGDFVLTGGELAAMTVVDAVARLVPGVLGNVDSSVTESFEEGLLEHPQYTRPPVFRGVEVPAALQSGDHARIARWRRWKSLVLTHERRPDLYARVVLSKADQKLLARREEEL
|
Specifically methylates guanosine-37 in various tRNAs.
|
Q1D6I2
|
Q9LUN2
|
YSL5_ARATH
|
Protein YELLOW STRIPE LIKE 5
|
Arabidopsis
|
MRKGVLNPDRDRQIVEHELQETGFSPETEKVKNKNFEEDEEEEDESVEKIFESREVPSWKKQLTVRAFVVSFMLSILFSFIVMKLNLTTGIIPSLNVSAGLLGFFFVKTWTKMLHRSGLLKQPFTRQENTVIQTCVVASSGIAFSGGFGTYLFGMSERIATQSGDVSRGVKDPSLGWIIGFLFVVSFLGLFSVVPLRKIMVIDFKLTYPSGTATAHLINSFHTPQGAKLAKKQVRVLGKFFSLSFFWSFFQWFFTGGENCGFSNFPTFGLKAYQYKFYFDFSATYVGVGMICPYIINISVLLGGILSWGIMWPLIETKKGDWFPDNVPSSSMHGLQAYKVFIAVAIILGDGLYNFCKVLSRTLSGLFVQLRGPTTSISRTSFTLEEDPHASPLSPKQSYDDQRRTRFFLKDQIPTWFAVGGYITIAATSTAILPHMFHQLRWYYILVIYICAPVLAFCNAYGAGLTDWSLASTYGKLAIFTIGAWAGSEHGGMLAGLAACGVMMNIVSTASDLTQDFKTGYLTLSSPKSMFVSQVIGTAMGCVVSPCVFWLFYKAFDDLGLPNTEYPAPFATVYRSMAKLGVEGVASLPRECLVLCYAFFGVAILVNIVKDSLHSNWGRFIPLPMAMAIPFFLGPYFAIDMCVGSLILFIWERVDAAKAEAFGTAVASGLICGDGIWSLPSSVLAIAGVNPPVCMKFLSSATNSKVDNFLKGSI
|
May be involved in the transport of nicotianamine-chelated metals.
|
Q9LUN2
|
P38951
|
XEN2_XENLA
|
Xenoxin-2
|
Xenopus
|
LKCVNLQANGIKMTQECAKEDNKCLTLRSLKKTLKFCASDRICKTMKIMSLPGEKITCCEGNMCNA
|
Lacks alpha-neurotoxic activity, has apparently no antibacterial activity, nor anti-coagulant potency.
|
P38951
|
A9IYI2
|
TILS_BART1
|
tRNA(Ile)-lysidine synthetase
|
Bartonella
|
MCVRLARNLFKTSDFIPCRRVILAVSGGSDSLALMFLVKEYLETLLIPPEIIAVTVDHQLRKESAREAEIVAEICRDHHIKHITVRWEGKKPKTHLAFSARIARYDLLVQEAQKQGASLIMTGHTLNDQVETYQMRCQRLQKRRGALRDEVGAMCDGGAASGFAGALRDKAGARRDEDYVRETRKNIAEKSYGVLYERGLSCIPREALLHRKVRLIRPLLGVQRQTLRNYLRLQGKTWIDDPTNEDRNFERVRVRQSLSSQKLVNIAQKINKAAWQRRQQAQNIADLILALDITVQYGRCFIVKPAPFLQKHSCFPFVVGLFAVLMGGGFYLLSNQKLSMLVQKLCLNSPEKRRFTCAGCVIEYNKEGIALWRERRNMKEALVEPDETLLWDGRYRITNHGSEAIKVGVANLEQLKSLLQNSNSNLEKPHFPSLQSLLMLSNDKGCDIPELISQAIIHKNVIIKRIMAPFDWLSSREDAALVNVVEPFFNLEVKR
|
Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
|
A9IYI2
|
B5L3X1
|
WFED_SHIBO
| null |
Shigella
|
MIDNLIKRTPEINRLLENKRVTGVVTFVNPYSYYKIKEYNKISQLDYIYIDGILLLKLFNFVNGTKIKRHSFDYSSIAKTVFNYSIQNKMKIGLIGSKDYEIEQAVKNIRKKHPGIDISYFHSGYFSSLEEKSSVIDSVIKKSDIIICGLGTPAQEELALDIKIKSNEHLIFTCGGFFTQTASRADFYYPWIKRYNLMWLQRIVLYKHVRKRFFIDYPKFIVRFISENLMKIFTRSN
|
Galactosyltransferase that adds one galactose residue in the beta-1-4 linkage to GlcNAc-alpha-pyrophosphate-lipid in the biosynthesis of the O-polysaccharide repeating unit of the O antigen.
|
B5L3X1
|
O93807
|
TBG_CANAX
|
Gamma-tubulin
|
Candida
|
MPGETITLQVGQCGNQVGLQYWQQLATEHGIQSDGSSTPYPKDINDLQLQELNNSGSSPQSYPQQTKPNGKYRNDHPELFFTLSDSNTYTPRSILIDMEPSVIAKSTSALPMFNPRNVHLSNQGNGAANNWINGYKYGTEEEETLLNLIDREVDKCDNLSNFQLFHSVAGGTGSGVGSKMLEVISDRYGHKKLLNTFSIFPSNEDTSDVVVQPYNTILTLKRLIDYSDATFVFHNDSLNRIENILFNNNSNIQHDDNDLFLGANKLIALVSASVSNPLRFPGYMYSSMESIVSNLIPTPDLKFLTSSIAPFSTQKHNYLNEYDMLLELSNDRYKTNRVGGDTSYISMLNYLIGYNLDQREIRKGILKSQQRISFVPWVARSVLVVHGKKSPYLKNTNLEGIQVTNNTSMIDVFTKILKQFDLLIKRKAYLNRYYSSVEEENEVMEMFNESRESVKSIIDEYKACKEITYLDDDDEDDLEDGDGGGGGNGNGYNNIDDADMGI
|
Tubulin is the major constituent of microtubules. The gamma chain is found at microtubule organizing centers (MTOC) such as the spindle poles or the centrosome, suggesting that it is involved in the minus-end nucleation of microtubule assembly.
|
O93807
|
Q1QWC2
|
YIDD_CHRSD
|
Putative membrane protein insertion efficiency factor
|
Chromohalobacter
|
MRPGKRRPLTRLPFALLSWGMIGLLRVYQYGISPLLGPRCRFWPSCSQYAVEAIQVHGPLKGAWLALKRIVKCHPGHPGGVDPVPPGPHETPRKTSTHDDEPPSR
|
Could be involved in insertion of integral membrane proteins into the membrane.
|
Q1QWC2
|
Q12PE6
|
TOLB_SHEDO
|
Tol-Pal system protein TolB
|
Shewanella
|
MKILAKWLTLATLMLTAQVNAALDIVITEGVDAARPIAVVPFVWEGPGAAPQQISDIVMGDLSRSGTFKPLDIRALPQHGISSVAQFAAASWGKVGAEAVVMGSIKPYGVDQFLVNFELIDLVRAQSQALKGPQNNTELVLESRQTVISANQFRQYGHRISDIVYEKLTGIRGAFLTRTAYVVVKQGQKAPYHLMIADYDGYNEQMLLRSPEPLMSPTWSPDGRRLAYVSFENRKAEIFVQDIYSQTRTLVSSYPGINGAPSFSPDGKKLAVTLSKDGQPEVYVIDIATKAAKRITDHYSIDTEPSWYPDGKSLLFTSERGGKPQIYSVHLDTGKVSRVTFEGEWNLGGSITPDGRSMIFVNRTNGKFHIARMDLATRFLQVLSSTQLDESPSVAPNGTMVIYGTTHQGKQVLAAVSMDGRFKARLPVGQGEVKSPAWSPFL
|
Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity.
|
Q12PE6
|
Q11CR0
|
TRMD_CHESB
|
tRNA [GM37] methyltransferase
|
unclassified Chelativorans
|
MTFRATVLTLYPEMFPGPLDISLAGRARSAGTWSLETVQIRDFATDKHRSVDDTPAGGGAGMVMRADVLARAIDHASPEEDARPRLLMSPRGKPLTQSFVRELATGPGAVIVCGRFEGVDQRVIEARCLLEVSVGDYILSGGEPAAIVLLDAVVRLLPGVMGNESSGAEESFESGLLEHPQYTRPQTFEGREIPEVLTSGNHRKIAEWRSAEAEQLTRERRPDLWLGYHRAKGGT
|
Specifically methylates guanosine-37 in various tRNAs.
|
Q11CR0
|
B7IM77
|
TRPA_BACC2
|
Tryptophan synthase alpha chain
|
Bacillus cereus group
|
MGVEKIKAAFENGKKAFIPYVMGGDGGLEKLKERIRFLDEAGASIVEIGIPFSDPVADGPTIQRAGKRALDSGVTVKGIFQALIEVRKEVQIPFVLMTYLNPVLAFGKERFVEKCLEAGVDGIIVPDLPYEEQNIIAPLLREANIALIPLVTVTSPIERIEKITSESEGFVYAVTVAGVTGVRQNFKEEIHSYLEKVKLHVNLPVVAGFGISTKEHVEEMVTICDGVVVGSKIIELLENEKREEICELIYATKQKEEA
|
The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
|
B7IM77
|
Q9C037
|
TRIM4_HUMAN
|
Tripartite motif-containing protein 4
|
Homo
|
MEAEDIQEELTCPICLDYFQDPVSIECGHNFCRGCLHRNWAPGGGPFPCPECRHPSAPAALRPNWALARLTEKTQRRRLGPVPPGLCGRHWEPLRLFCEDDQRPVCLVCRESQEHQTHAMAPIDEAFESYRTGNFDIHVDEWKRRLIRLLLYHFKQEEKLLKSQRNLVAKMKKVMHLQDVEVKNATQWKDKIKSQRMRISTEFSKLHNFLVEEEDLFLQRLNKEEEETKKKLNENTLKLNQTIASLKKLILEVGEKSQAPTLELLQNPKEVLTRSEIQDVNYSLEAVKVKTVCQIPLMKEMLKRFQVAVNLAEDTAHPKLVFSQEGRYVKNTASASSWPVFSSAWNYFAGWRNPQKTAFVERFQHLPCVLGKNVFTSGKHYWEVESRDSLEVAVGVCREDVMGITDRSKMSPDVGIWAIYWSAAGYWPLIGFPGTPTQQEPALHRVGVYLDRGTGNVSFYSAVDGVHLHTFSCSSVSRLRPFFWLSPLASLVIPPVTDRK
|
E3 ubiquitin-protein ligase. Mediates 'Lys-63'-linked polyubiquitination of the innate immune receptor DDX58, this linkage doesn't lead to proteasomal degradation but seems to enhance IFN induction.
|
Q9C037
|
E7FL12
|
VKT2_PSERS
|
Kunitz serine protease inhibitor Pr-mulgin 2
|
Pseudechis
|
MSSGGLLLLLGLLTLWEGLTPVSSKDRPHFCHLPHDPGPCKGNFQAFYYHPVRRTCLEFIYGGCQGNPNNFKTIDECKRTCAA
|
Serine protease inhibitor that acts against trypsin (EC(50)=10 nM, Ki=5nM), chymotrypsin (EC(50)=100 nM, Ki=40 nM), and plasmin (EC(50)=100 nM, Ki=40 nM).
|
E7FL12
|
O29028
|
TRPB2_ARCFU
|
Tryptophan synthase beta chain 2
|
Archaeoglobus
|
MLSWCMKKIMLDESEMPKEWYNVLPDLPEPLPPPLHPATQEPVKPEDLEPIFPKGLIQQEMSGERWIRIPEDVREIYRIWRPTPLVRAERLEKALKTPARIYFKYEGASPPGSHKPNTAVAQAYYNAKEGVERLTTETGAGQWGSALCFATKLFEMACTVYMVKVSFMQKPYRRVMMETWGGEVIPSPSDRTEVGRKILAENPDTPGSLGIAISEAIEDAAKNENTKYSLGSVLNHVLLHQTVIGLETKAQLEKVDEKPDVLIGCVGGGSNFAGLTYPFVNDAKNGDLEIIAVEPAACPTLTAGEYKYDFGDVAGLTPLLKMYTLGHDFIPPPIHAGGLRYHGDAPTLCMLVKHGVIKARAVKQLPTFEAGLLFARTEGIIPAPETNHAVRAAIDEAIKARENNEEKVIVFGFSGHGLLDLQAYDDYLAGRLADT
|
The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
|
O29028
|
A8GQ89
|
Y6705_RICAH
|
Nucleoid-associated protein A1C_06705
|
spotted fever group
|
MVNFNQFLKQAQSMQKKMQEAQEQMANARYTGKAGGGLVEIIITGKGEVAKISIDESLLKSEEKEMLEDLIKVAFNDAKQKCDEDSQNSLSGALNGMSLPPGFKMPF
|
Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection.
|
A8GQ89
|
C0M8L4
|
TRUA_STRE4
|
tRNA-uridine isomerase I
|
Streptococcus
|
MTRYKAIISYDGTLFSGFQRQSQARTVQEEIEKTLQKLTGGQGIQIHGAGRTDAGVHAYGQVIHFDLEQKRDPEKLRFALDTQTPDDIDVISLEIAADDFHARYHKHFKTYEFLVDIGRPKNPMMRHYATHYPYPLDIAKMQAAIKDLVGTHDFTGFTAAGTSVKNKVRTITAATLTQDPKTGFLVFTFSGNGFLYKQVRNMVGTLLKIGNGRLPIEQIRLVLESKNRQLAGPTAAGNGLYLKEIIYEE
|
Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
|
C0M8L4
|
Q95ZS2
|
TDC1_CAEEL
|
Tyrosine decarboxylase
|
Caenorhabditis
|
MVYGLGEALKNLNSYCQERTTRIRNSLSPSRPSMSEATATGSSSSSRASTTIPSTPNMDVTPTVEDPRQNDNNASGMTRDEFRQYGKETVDYIVDYLENIQKRRVVPAIEPGYLKDLIPSEAPNTPESFESVMEDFEKLIMPGITHWQHPRFHAYFPAGNSFPSIIADMLSDAIGCVGFSWAACPAMTELELIMLDWFGKMIGLPAEFLPLTENGKGGGVIQSSASECNFVTLLAARFEVMKELRQRFPFVEEGLLLSKLIAYCSKEAHSSVEKACMIGMVKLRILETDSKFRLRGDTLRNAIQEDRNLGLIPFFVSTTLGTTSCCSFDVLSEIGPICKENELWLHVDAAYSGSAFICPEFRPLMNGIEYAMSFNTNPNKWLLINFDCSTMWVRDRFKLTQALVVDPLYLQHSWMDKSIDYRHWGIPLSRRFRSLKLWFVIRMYGIDGLQKYIREHVRLAKKMETLLRADAKFEIVNEVIMGLVCFRMKGDDELNQTLLTRLNASGRIHMVPASLGDRFVIRFCVCAENATDKDIEVAYEIIAQATQHVLHDSVKAVIAEEDEEAVALEEMVADLNITETPEKCLTRQNSANAAESGQKLERQLSKEEILAQKQHESLAKKRSFLVRMVSDPKCYNPKIVRHLNMANHRKMSQDLYRDRTLMQTISHSQRPNRLSQSPGSAGSAFFDDDDDRIVADVQTGLQTPI
|
Required for the decarboxylation of tyrosine to tyramine, a precursor of octopamine but probably also itself a neurotransmitter . Involved in the regulation of egg laying, which is inhibited by tyramine . Also involved in controlling locomotion and head movements . Due to its involvement in octopamine biosynthesis, also required for crtc-1-dependent regulation of AMPK-mediated longevity which requires octopamine signaling .
|
Q95ZS2
|
O29322
|
TOP6A_ARCFU
|
Type II DNA topoisomerase VI subunit A
|
Archaeoglobus
|
MKEIERRCLRALIGIVQNIYDQMKAGQVPELHIATRTKYNIEFNEESEVWVYGDRKSVRSAKTVKGAYRILKMTYVIGFLKEQLNLNKSSTLRELYYISEGWGAAKFEEQPESDRLVEDLEILTNFQREHFHIRPEEDGATVIGPLRVREETRRGVREIHCQDDVGEGGYQIPVNVDKIEFVDHDAKFVIAIETGGMRDRLVENGFDEKYDAIIVHLKGQPARSTRRLLRRLNTELNLPVVVFTDGDPWSYRIFASVAYGSIKSAHLSEYLATPAAQFVGIRPTDIVKYDLPADKLTEEDIKALNAILTDPRFDSEFWKKEVNLQLEINKKSEQQALAKYGLDYVTDVYLPERLSELGVI
|
Relaxes both positive and negative superturns and exhibits a strong decatenase activity.
|
O29322
|
Q5X5C5
|
YBEY_LEGPA
|
Endoribonuclease YbeY
|
Legionella
|
MTYHIDIQNATGKLLPLSEDEITKLASLALRDHKQDAELTVRLVDVEEMTYLNHTYRKKNKPTNVLAFPCSLPANIELECPLLGDVVICPEVLLAESAQFNKSLHAHWSLILIHGVLHLLGYDHIKDEEASIMQMLEAKLLAELGYANPYEVEENELE
|
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
|
Q5X5C5
|
Q07H53
|
Y4812_RHOP5
|
Nucleoid-associated protein RPE_4812
|
Rhodopseudomonas
|
MADFLGMMKQAAQLQSKMKEMQSELDRIEVEGISGGGLVNVRMSAKMEVRAVKIDPSLLNPDEVGVLEDLLVSALADAHRKAEAAMQDKMKTLTGGLSLPPGLGL
|
Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection.
|
Q07H53
|
B2T0I5
|
YQGF_PARPJ
|
Putative pre-16S rRNA nuclease
|
Paraburkholderia
|
MSLPAGREATLLAFDYGEKRIGVAVGNSLTRRARPLVIVQNRSREYRFEAVGKLIAEWKPDALVVGLPFHPDGAPHEMTQLAKRFGNQLNGRFNLPVTWVDERYSSVEAKAEIRAGNGRADMLDAEAASIILQQYLDGLSDDHEFH
|
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
|
B2T0I5
|
Q5HL88
|
XYLB_STAEQ
|
Xylulose kinase
|
Staphylococcus
|
MVKEVVLGIDLGTSAIKIIAVDQLGNVIESVSETLKLYQENPGYSEQDPNEWFEATKKGIKELIQSTEMSDKIVKGISFSGQMHGLVIVDDNGIPLRKAILWNDTRNSIQCRQIEDIYGERLNYNPILEGFTLPKMLWVQQHEPEIWNRVDVFMLPKDYLRYCLTQTIHMEYSDACSTLLFNPENYEWTRDVGDTFNIGDIYPPLVKSHSYVGNVTSSLAKELGLSSDVAVYAGGGDNACGAIGAGVIHDKSALCSIGTSGVVLNVEYQRVTSYDSNLHLFNHSVPDTYYAMGVTLAAGYSLNWLKQTFFENESFEEILNLAASSKMGANGLLFTPYLAGERTPHGDAQIRGSFIGISGQHTKADFARAVIEGITYSLYDSIKIMRRAGHEMNSITSIGGGAKSRFWLQLQADIFNVQIKRLKHEEGPSMGAAILAAYGLGWFKTIESCVEAFIKVDEVFEPNNENHDLYEQYYSVYEAIYKQTKQLTADLLTITN
|
Catalyzes the phosphorylation of D-xylulose to D-xylulose 5-phosphate.
|
Q5HL88
|
Q888A0
|
UPP_PSESM
|
UPRTase
|
Pseudomonas
|
MPIREIRHPLIRHKLGLMRRADISTKNFRELAQEVGALLTYEATADLTLESYDIQGWAGTVSVEKIAGKKITVVPILRAGIGMLDGVLSLIPGAKVSAVGVARNEETLQAHTYLEKLVPEIDERLAMIIDPMLATGSSMVATIDLLKKAGCKEIRAMVLVAAPEGIAAVERAHPDVMIYTASIDERLNEHGYIIPGLGDAGDKIFGTKQKDA
|
Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
|
Q888A0
|
Q31C15
|
TAL_PROM9
|
Transaldolase
|
Prochlorococcus
|
MKSILEQLSSMTVVVADTGDLDSIKKFQPRDATTNPSLILAAAKNPDYVKLIDKAIESSENTLPNGFSEIELIKETVDQVSVFFGKEILKIISGRVSTEVDARLSFDTEATVKKARKLINLYKNFGIEKERILIKIAATWEGIKAAEILEKEGIKCNLTLLFNFCQAVTCANANITLISPFVGRILDWHKAKTGKTSFIGAEDPGVISVTQIYKYFKEKGFKTEVMGASFRNLDEIKELAGCDLLTIAPKFLEELKREKGVLIRKLDASTKINNSIDYKFEEKDFRLSMLEDQMASEKLSEGITGFSKAIEELEELLIERLSEMKNHKLISAN
|
Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
|
Q31C15
|
Q9SP55
|
VATG_CITLI
|
Vacuolar proton pump subunit G
|
Citrus
|
MTSNRGQGGIQQLLAAEQEAQHIVAAARNAKMARLKQAKEEAEREIAEYRAQVEREFQRKLAESVGDSGANVKRLEQETEVKIHHLKAGAEKIQYDVVQMFLKHVTTVKN
|
Catalytic subunit of the peripheral V1 complex of vacuolar ATPase (V-ATPase). V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.
|
Q9SP55
|
Q8X884
|
TUSC_ECO57
|
tRNA 2-thiouridine synthesizing protein C
|
Escherichia
|
MKRIAFVFSTVPHGTAAGREGLDALLATSALTDELAVFFIADGVFQLLPGQKPDAVLARDYIATFKLLDLYDIEQCWVCAASLRERGLDPQTPFVVEATPLEADALRRELANYDVILRF
|
Part of a sulfur-relay system required for 2-thiolation of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at tRNA wobble positions.
|
Q8X884
|
Q82TN5
|
Y1849_NITEU
|
Nucleotide-binding protein NE1849
|
Nitrosomonas
|
MQVIIISGLSGSGKSIALKVLEDSGYYCVDNLPASLLVVLINHLQTQQHAYVAVAIDMRSGENITVLPWQLKMIDKSIQIKFIFLEARTETLMQRFSETRRRHPLSDKNITLEEAIRREREALATLTGLGHHIDTSSLRPNVLRAFIKDFIADSRSPSQLTLLFQSFGYKHGIPLDADLVFDIRCLPNPFYDPQLKELTGHDPEVIRFMESQPDASKMLRDISSFLGTWLPAYIRDNRAYLTVAIGCTGGQHRSVYFAEKLALHFHDSAHVLVRHRGLAEYKPHYARR
|
Displays ATPase and GTPase activities.
|
Q82TN5
|
O81123
|
ZIP1_ARATH
|
ZRT/IRT-like protein 1
|
Arabidopsis
|
MSECGCFSATTMLRICVVLIICLHMCCASSDCTSHDDPVSQDEAEKATKLKLGSIALLLVAGGVGVSLPLIGKRIPALQPENDIFFMVKAFAAGVILCTGFVHILPDAFERLSSPCLEDTTAGKFPFAGFVAMLSAMGTLMIDTFATGYYKRQHFSNNHGSKQVNVVVDEEEHAGHVHIHTHASHGHTHGSTELIRRRIVSQVLEIGIVVHSVIIGISLGASQSIDTIKPLMAALSFHQFFEGLGLGGCISLADMKSKSTVLMATFFSVTAPLGIGIGLGMSSGLGYRKESKEAIMVEGMLNAASAGILIYMSLVDLLATDFMNPRLQSNLWLHLAAYLSLVLGAGSMSLLAIWA
|
Mediates zinc uptake from the rhizosphere. May also transport copper and cadmium ions.
|
O81123
|
Q4UGL5
|
TCTP_THEAN
|
Translationally-controlled tumor protein homolog
|
Theileria
|
MKVYRDLYSNDEVCSDAYDHLDPFDNPDLSSVAFEVKTSKVAKGEEDYGIGYNDEEGGDQMNVDPNVEVVVDVVDKFALQSLPLTKKDYSSYIKKYIQRLVATLQEKNPERVEPFKTSVSEFVKHVLANFDDFEFYVGESLDYEAGLVYGYYKGEEVSPRLVFLKDGLVEERY
|
Involved in calcium binding and microtubule stabilization.
|
Q4UGL5
|
A6VW19
|
TIG_MARMS
|
PPIase
|
Marinomonas
|
MQVSVETTSPIERVLTISVPAARVDEKVNSEVAKTAKTIRIDGFRKGKVPVSVVKKRYGQGIRLDAVEQIMRDAYVEAIQKESIQPAGMPSIEPKNFAEGADLEFVVKIEVYPEVTLADNSAIKVDRVVSDVTEADVDTMLETLRKQNAEWSAVERESADGDQVTIDFVGYLGDEAFDGGAAEGHKLVLGSNTMIPGFESGILGAKAGEERTISVTFPEDYQAENLKGKEATFKITVSEVAEQILPELNDAFVEKFGLEEATVAALRAEVRKNMERELNQAIKSKLKNALFEGLSSINEVEVPSALVDQEVDALRKQAAQQFGGQGFDASQLPAELFQEEAKKRAKLGLLISEVIKKDDLKVDDDRVRAFLEDMAQAYQEPQQVIDFYLKNKEQLAQVQSAVLEEQVVDKLLESAQVTEVTLGYEDAIKPNAQAEEAGEEA
|
Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
|
A6VW19
|
A6UC29
|
UREG_SINMW
|
Urease accessory protein UreG
|
Sinorhizobium
|
MPSKNGPLRVGIGGPVGSGKTALTEKLCKAMRERYSLAVVTNDIYTKEDAEALVRMQALPSERIVGVETGGCPHTAIREDASINLQAIADLNRRLPELDLVFIESGGDNLAATFSPDLADLTIYVISVCQGEEIPRKGGPGITKSDLLVINKKDLAPHVGADLEIMERDAARMRGEKPFVFSDMKRGDGVERIVDFLILHGGL
|
Facilitates the functional incorporation of the urease nickel metallocenter. This process requires GTP hydrolysis, probably effectuated by UreG.
|
A6UC29
|
B2UX14
|
TIG_CLOBA
|
PPIase
|
Clostridium
|
MEAKVEKIETNVVKLEIKVEAEKFDAALTKAYNKNKGKYNVPGFRKGKVPMAILKKMYGIEIFYDDAVNIAIDESYNEALKAEDIRPVDYPKVDIVEIGEGKELVYTATVTTYPEVEIGEYKGLDIKKPSYEVSEEEVEKQVKEMQSKNARVETKEEGTIADGNIAIIDFKGFVDGEAFEGGEGTDYPLEIGSGTFIDNFEEQLVGLAIGDKKEVNVTFPENYGKEELNAKPAMFEVTVKGIKVKELPELDDEFAKEVSEFDTLAELKENVKKRLEESNNERAEREFEEAVITSIIETSKIDLPEVMLTKEIDSMMKDLESRLQYQGLSLDQYMEFTGNTIEKMREFMKENAERKVKADIILEAVAKAEEVKATDEQLNERALELGRMYGPKDPKKMANILLKAQKAMIEKDIIIENTLKLIKESCK
|
Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
|
B2UX14
|
Q9V2C0
|
WTPC_PYRAB
|
Molybdate/tungstate import ATP-binding protein WtpC
|
Pyrococcus
|
MLRVESVSKDYKEFKLRDISFDVKKEEHFIILGPSGAGKTVLLEIIAGIIEPDEGRIILNGVDVTSYPPEKRNLAYIPQDYALFPHMTVYDNIAFGLKLRRISRQEIDRKVKEISKVLGIEHLLHRKPRTLSGGEKQRVAIARALVIEPELLLLDEPFANLDVQTKSRFMTEMKVWRKELGFTSLHVTHSFEEAISLGDRVGVMLRGRLVQVGDVKEVFSNPVDEGVARFLGFENIIEGVAKGNILEANGVKITLPISVEGKVRIGVRPEDIILSTEPVKTSARNEFRAEVIGIEELGPLVRVNLKIGGITLKAFITRSSLIELGISEGREVYVSFKTSAIKVF
|
Part of the ABC transporter complex WtpABC involved in molybdate/tungstate import. Responsible for energy coupling to the transport system.
|
Q9V2C0
|
P68423
|
TXH9_CYRSC
|
Huwentoxin-IX
|
Cyriopagopus
|
IICAPEGGPCVAGIGCCAGLRCSGAKLGLAGSCQ
|
Intracisternal injection paralyzes mice.
|
P68423
|
Q8SPP9
|
TSHR_PIG
|
Thyroid-stimulating hormone receptor
|
Sus
|
MSLTPLLQLALLLALPRSLRGKGCPSPPCECHQEDDFRVTCKDIHSIPPLPPNTQTLKFIETHLKTIPSRAFSNLPNISRIYLSIDATLQQLESQSFYNLSKMTHIEIRNTRSLTYINPGALKDLPLLKFLGIFNTGLRIFPDLTKVYSTDVFFILEITDNPYMTSIPANAFQGLCNETLTLKLYNNGFTSVQGHAFNGTKLDAVYLNKNKYLTVIDKDAFGGVFSGPTLLDVSYTSVTALPPKGLEHLKELIARNTWTLKKLPLSLSFLHLTRADLSYPSHCCAFKNQKKIRGILESLMCNESSIRSLRQRKSVNAVNGPFYQEYEEDLGDSSVGNKENSKFQDTHSNSHYYVFFEEQEDEIIGFGQELKNPQEETLQAFDSHYDYTVCGGSEDMVCTPKSDEFNPCEDIMGYRFLRIVVWFVSLLALLGNVFVLVILLTSHYKLTVPRFLMCNLAFADFCMGMYLLLIASVDLYTQSEYYNHAIDWQTGPGCNTAGFFTVFASELSVYTLTVITLERWYAITFAMRLDRKIRLRHAYAIMAGGWVCCFLLALLPLVGISSYAKVSICLPMDTETPLALAYIILVLLLNIVAFTIVCSCYVKIYITVRNPQYNPGDKDTKIAKRMAVLIFTDFMCMAPISFYALSALMNKPLITVTNSKILLVLFYPLNSCANPFLYAIFTKAFQRDVFILLSKFGFCKRQAQAYRGQRVSPKNSTGIQVQKVTQNMRQSLPNMQDDYELLENSHLTHKKHDQISKEYKQPVL
|
Receptor for the thyroid-stimulating hormone (TSH) or thyrotropin. Also acts as a receptor for the heterodimeric glycoprotein hormone (GPHA2:GPHB5) or thyrostimulin. The activity of this receptor is mediated by G proteins which activate adenylate cyclase. Plays a central role in controlling thyroid cell metabolism.
|
Q8SPP9
|
Q1WG82
|
ZGLP1_MOUSE
|
GATA-like protein 1
|
Mus
|
MEAAQAGDLTRRQELLAPPCLDTESLRKSRPPALEPGALRCLTPNIRSLWPTCQDSVSTALPFLQEKEKGLPGSPSPATQVLGSCWELMVIGMSDHLSMARNPRGTQCPNLEISSATSPASLQRRPRKQLNPRMGIEKVDPRFKGVTLEFQIQPDSSLQIVPTYSLPGRSCSQKLPASPSKALASPGSSEALGPRRCASCRTQRTPLWRDAEDGTPLCNACGIRYKKYGTRCSSCWLVPRKSIQPKRLCGRCGMSQDPHLSPTQEL
|
Transcriptional regulator that plays a key role in germ cell development . Determines the oogenic fate by activating key genes for the oogenic program and meiotic prophase entry . Acts downstream of bone morphogenetic protein (BMP) by regulating expression of genes required for the oogenic programs, which are repressed by Polycomb activities in sexually uncommitted germ cells . Regulates expression of STRA8, a central downstream effector for the meiotic program . Acts independently of retinoic acid (RA) . In males, not required for germ-cell sex determination, but required to allow the spermatogonia to efficiently accomplish the meiotic prophase .
|
Q1WG82
|
Q8CX20
|
TRUA_STRA5
|
tRNA-uridine isomerase I
|
Streptococcus
|
MTRYKAQISYDGSAFSGFQRQPNCRTVQEEIERTLKRLNSGNDVIIHGAGRTDVGVHAYGQVIHFDLPQARDVEKLRFGLDTQCPDDIDIVKVEQVSDDFHCRYDKHIKTYEFLVDIGRPKNPMMRNYATHYPYPVIIELMQEAIKDLVGTHDFTGFTASGTSVENKVRTIFDAKIQFEASKNLLIFTFTGNGFLYKQVRNMVGTLLKIGNGRMPISQIKTILQAKNRDLAGPTAAGNGLYLKEIIYEDEECFSNFRK
|
Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
|
Q8CX20
|
B6JFP6
|
TATA_AFIC5
|
Sec-independent protein translocase protein TatA
|
Afipia
|
MGLSFQHILILLVVVLLLFGRNKISDLMGDFAKGIKAFKKGMSDDEVETAKSDSIKTIDNTGKPTNVQANPQRQDSTV
|
Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
|
B6JFP6
|
Q0SPB0
|
TPIS_BORAP
|
Triose-phosphate isomerase
|
Borreliella
|
MRKTFLAGNWKMHYTSAEASIVAKQIATEVKTLNDDFVIMITPPFTALSKVSECIKGSNILLGAQNMSYMESGARTSEISPSMLLEFGVEYVILGHSECRLYLAETDEIINKKIRAGLKHSFKYLILCVGETLDERDSGKTLDVVLSQVKKGLDCVSESDIKRIILAYEPVWAIGTGKTATKEEAEEVHKAIRLEIMKLYSKSASDNIIIQYGGSVNASNIKELMNEPNIDGALIGGASLKAESFLSIINNVR
|
Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
|
Q0SPB0
|
Q9XFH9
|
TRXF2_ARATH
|
Thioredoxin F1
|
Arabidopsis
|
MPLSLRLAPSPTSFRYSPITSTGAGGFSPVKQHCRIPNSGVATKIGFCSGGGGVLDSGRRIGSCVVRCSLETVNVTVGQVTEVDKDTFWPIVKAAGDKIVVLDMYTQWCGPCKVIAPKYKELSEKYQDMVFLKLDCNQDNKPLAKELGIRVVPTFKILKDNKVVKEVTGAKYEDLLAAIEAARSG
|
Probable thiol-disulfide oxidoreductase involved in the redox regulation of enzymes of both reductive pentose phosphate pathway (Calvin-Benson cycle) and oxidative pentose phosphate pathway.
|
Q9XFH9
|
Q8FT12
|
TRPB2_COREF
|
Tryptophan synthase beta chain 2
|
Corynebacterium
|
MTTPATPTRQTLLDAYFGEYGGQFVPEVLLPALDELERAYVEALEDPTFQQELDDLYTNYLGRPTPITECANLPLEGQGRGTARIFLKREDLVHGGAHKGNQTIGQALLAKRLGKTRLIAETGAGQHGTATAMVAALFGMKCTVYMGAKDVARQQPNVYRMRLMGAEVVAVDEQSGNGLSSAIDVAINDWVNNLEDTHYLLGTAAGPHPFPTLVKKFHSVISRESREQMLERTGALPDAVVACVGGGSNAIGAFAQYLEDQPGNEKVRLIGVEPAGYGLDTDLNGAPIHEGRTMHLHGSNSYALLDEDGNLRNSHSVSAGLDYPGVGPEHAHLKDTGRAEYVGATDAEALQAFRMLSRYEGIIPALESSHALAHALKMAAEATEPINILVNLSGRGDKDVAYVRQLLGDHAALDPATDVLTEVDVLGVLEELTPQADTA
|
The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
|
Q8FT12
|
A6SZ08
|
UREE_JANMA
|
Urease accessory protein UreE
|
Janthinobacterium
|
MLTLNTKLEKADQIDGELILPYDQREKSRLRATMVSGEDVAVFTVRGTILRDGDILRGDDGRIVKITAAKEPTYRVEALSPHQLLRCAFHLGNRHTQAQIGNGFLRIRKDAVLKEMLEGLGAKVEEELAAFEPESGAYGGGHHHHGDDGHHPLAPIPLRQKIHRPSDKAE
|
Involved in urease metallocenter assembly. Binds nickel. Probably functions as a nickel donor during metallocenter assembly.
|
A6SZ08
|
Q91242
|
THAB_PAROL
|
Nuclear receptor subfamily 1 group A member 1-B
|
Paralichthys
|
MAQWPEKEEEEQPMFGEEYTGYIPSYLEKDEPCVVCGDKATGYHYRCITCEGCKGFFRRTIQKNLHPSYSCKYDCCCIIDKITRNQCQLCRFKKCIAVGMAMDLVLDDSKRVAKRRLIEENRERRKKEEIVKTLQNRPEPTGAEWELIRMVTEAHRHTNAQGAQWKQKRKFLPDKIGQSPVAPTSDGDKVDLEAFSEFTKIITPAITRVVDFAKKLPMFSEQLPCEDQIILLKGCCMEIMSLRAAMRYDPESETLTLSGEMAVKREQLKNGGLGVVSDAIFDLGKSLAQFNLDDTEVALLQAVLLMSSDRSGLTCMDKIEKCQETYLLAFEHYINYRKHNIPHFWPKLLMKVTDLRMIGACHASRFLHMKVECPNELFPPLFLEVFEDQEV
|
High affinity receptor for triiodothyronine.
|
Q91242
|
Q3K6Y9
|
UPP_PSEPF
|
UPRTase
|
Pseudomonas
|
MSIQEIRHPLIRHKLGLMRRADISTKNFRELAQEVGALLTYEATKDLPLETYDIEGWCGTVSVEKIAGKKITVVPILRAGIGMLEGVLSLIPGAKVSAVGVARNEETLQAHTYLEKLVPEIDERLAMIIDPMLATGSSMVATIDLLKKAGCKDIRAMVLVAAPEGIAAVEQAHPDVIIYTASIDQKLNEHGYIIPGLGDAGDKIFGTKQKDA
|
Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
|
Q3K6Y9
|
A5EJY3
|
UREG2_BRASB
|
Urease accessory protein UreG 2
|
unclassified Bradyrhizobium
|
MSRLALTRADEPMTAARVGIGGPVGSGKTALVERLIPALQTRGIDIAVITNDLVTAEDAERVRRSGLIDPERVSAVEAGACPHTVIREDPTLNIEAADELERRFPGVELILLESGGDNLASTFSRDLTDFWMFVIDVAGGDDIPRKRGPGVIRADLLVINKVDLAPHVGVDLGRMQREATEVRGGRPVLLTNCRRGEGIEAIVDLLEREVLFRK
|
Facilitates the functional incorporation of the urease nickel metallocenter. This process requires GTP hydrolysis, probably effectuated by UreG.
|
A5EJY3
|
Q12GA4
|
UBIA_POLSJ
|
4-HB polyprenyltransferase
|
unclassified Polaromonas
|
MLRRKLGLYLALIRWNRPAGWLLLLWPTLSALWVASHGFPGWHLLTVFTLGTILMRSAGCCVNDVADRDFDRHVKRTAQRPVTSGQVSVREALVLGAVLALLAFGLVLTTNAATIAWSFAALAVTLAYPFAKRYVSMPQAVLGVAFSFGIPMAFAAVQSRVPLLAWVLLLGNLCWVIAYDTEYAMVDRDDDLKIGMKTSAITLGRFDVAGVMLSYLVYLSVWALALADIPQAAIYWMAIGLAGLQALWHGWLIRKRERDDCFKAFRLNHWLGFTVFAGIALSYLAA
|
Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 3-octaprenyl-4-hydroxybenzoate.
|
Q12GA4
|
Q49ZH2
|
TOP3_STAS1
|
DNA topoisomerase III
|
Staphylococcus
|
MKSLIIAEKPSVGRDIANTLNINEKRNGYFENNKYIVTWALGHLVTNATPEQYDASYKEWKLNDLPIIPNKMKTIVISKTRKQFSTVQSLINNNKVKDIIIATDAGREGELVARLILDKAHNKKPTKRLWISSVTNKAIKEGFNKLQDGRKFNNLYHAALARSEADWIVGINATRALTTKYDAQLSLGRVQTPTIQLVQMRQNEINHFKPQTYYTMKLNAAGLTFHCTKPQSHPDKTVLESIKKAIDGQSGHIASISKTHKKAYPQQLYNLTDLQQDAYKRFHLGPKETLNTLQTLYERHKLVTYPRTDSNYLTDDMVDTLKDRLKAIMATSLKDMAKAQMSQTFSSKQRFVNNNKVSDHHAIIPTEVRPDINQLSQRESKIYMMIAQRYLENLMPPHEYEAIAIELKVGQHTFTFKDKVTTKLGFKAIYENKESINTQIDQLQKGTKLNVTKILIEEHETTAPPYFNEGSLLKAMESPQKFFDLSDKKHDKTLKDTGGIGTVATRADIIEKLFNMNAIEARDGKIKVTSKGKQILELAPQKLTSPLLTAEWEEKLLLIEQGKYNASQFISEMKAFTNQVVNEIKESEQNYKHDNLTTTECPTCGKFMIKVKTKNGQMLVCQDPQCKTKKNVQRKTNARCPNCHKKMTLFGRGKDAVYRCVCGHTETQAQMDKRHKNKKSDKVNKKDLKKYMNNDEGIENNPFQDALKGLKF
|
Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone.
|
Q49ZH2
|
Q5UL10
|
UFOG2_FRAAN
|
UDP-glucose flavonoid 3-O-glucosyltransferase 2
|
Fragaria
|
MAPVSNQAGGHVAVLAFPFSTHAAPLLNIVCRLAAAAPSTLFSFFNTKQSNSSILASDTSVLRYTNVCVCEVADGVPEGYVFVGKPQEDIELFMKAAPDNFRKCLEASVAESGREVSCLVTDAFFWFGAHMADDMGGVPWVPFWTAGPASLSAHVHTDLIRNTTSGDCHDEKETITVIAGMSKVRPQDLPEGIIFGNLESLFSRMLHQMGLMLPLATAVFINSFEELDPVITNDLKSKFKRFLNVGPLDLLEPTASAATTTPQTAEAVAGDGCLSWLDKQKAASVVYVSFGSVTRPSPEELMALAEALEASRVPFLWSLRDNLKNPQLDEFLSKGKLNGMVVPWAPQPQVLAHGSVGAFVTHCGWNSVLESVAGGVPLICRPFFGDQKLNARMVEDVWKIGLRLEGGVFTKNGMLKSLDMLLSQDKGTKMKNKIHTLKQLAQQAVEPKGSSTRNFESLLEMATTN
|
In the presence of other necessary color factors, this glycosylation reaction allows the accumulation of anthocyanin pigments . Anthocyanidins are the preferred substrates, while flavonols are only a minor substrate in vitro .
|
Q5UL10
|
Q9XWU8
|
VMP1_CAEEL
|
Ectopic P granules protein 3
|
Caenorhabditis
|
MAKKQKKSTEKSERTVEFKEPPKPANSEERLKPAGRGMKPSPSQNTLNRMERETIVFWRRPHIVIPYALMEIAHLAVELFFKILAHKTVLLLTAISIGLAVYGYHAPGAHQEHVQTIEKHILWWSWWVLLGVLSSIGLGSGLHTFLIYLGPHIAAVTMAAYECQSLDFPQPPYPESIQCPSTKSSIAVTFWQIVAKVRVESLLWGAGTALGELPPYFMARAARISGQEPDDEEYREFLELMNADKESDADQKLSIVERAKSWVEHNIHRLGFPGILLFASIPNPLFDLAGITCGHFLVPFWSFFGATLIGKALVKMHVQMGFVILAFSDHHAENFVKILEKIPAVGPYIRQPISDLLEKQRKALHKTPGEHSEQSTSYLAWGLSLMVTFMILFFFLSIVNSLAKDYHKRLWERKRRQNKDLIDEENQSFEEEEEEAVTPPSSCPLLLSDGFEGVVVKK
|
Involved in autophagy . Thought to act in autophagasome and omegasome formation .
|
Q9XWU8
|
B9E198
|
YQGF_CLOK1
|
Putative pre-16S rRNA nuclease
|
Clostridium
|
MRILGLDIGNKTIGVALSDPLGITAQGITTIKRKGEDRDIEELKAICDKYKVEVIVCGLPKNMNGTLGPQSEKVLKFCNIIEEVINLPIKMWDERLTTVAANKAMLEADLSRAKRKKIVDKMAATYILQGYLDRISK
|
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
|
B9E198
|
Q9R6P9
|
THIO_MYCGA
|
Thioredoxin
|
Mycoplasma
|
MKHITNKAELDQLLSTNKKVVVDFYANWCGPCKILGPIFEEVAQDKKDWTFVKVDVDQANEISSEYEIRSIPTVIFFQDGKMADKRIGFIPKNELKELLK
|
Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions.
|
Q9R6P9
|
Q5FA59
|
TRMD_NEIG1
|
tRNA [GM37] methyltransferase
|
Neisseria
|
MLIQAVTIFPEMFDSITRYGVTGRANRQGIWQFEAVNPRKFADNRLGYIDDRPFGGGPGMIMMAPPLHAAIEHAKAQSSQTAKVIYLSPQGKPLTHQKAAELAELTHLILLCGRYEGIDERLLQSSVDEEISIGDFVVSGGELPAMMLMDAVLRLVPGILGDIQSAEQDSFSSGILDCPHYTKPLEFQGMAVPEVLRSGNHGLIAEWRLEQSLRRTLERRPDLLEKRVLIPKESRLLNKILQEQREIQS
|
Specifically methylates guanosine-37 in various tRNAs.
|
Q5FA59
|
P75804
|
YLII_ECOLI
|
Soluble aldose sugar dehydrogenase YliI
|
Escherichia
|
MHRQSFFLVPLICLSSALWAAPATVNVEVLQDKLDHPWALAFLPDNHGMLITLRGGELRHWQAGKGLSAPLSGVPDVWAHGQGGLLDVVLAPDFAQSRRIWLSYSEVGDDGKAGTAVGYGRLSDDLSKVTDFRTVFRQMPKLSTGNHFGGRLVFDGKGYLFIALGENNQRPTAQDLDKLQGKLVRLTDQGEIPDDNPFIKESGARAEIWSYGIRNPQGMAMNPWSNALWLNEHGPRGGDEINIPQKGKNYGWPLATWGINYSGFKIPEAKGEIVAGTEQPVFYWKDSPAVSGMAFYNSDKFPQWQQKLFIGALKDKDVIVMSVNGDKVTEDGRILTDRGQRIRDVRTGPDGYLYVLTDESSGELLKVSPRN
|
Aldose sugar dehydrogenase with broad substrate specificity. The physiological substrate is unknown. Can oxidize glucose to gluconolactone. Can also utilize D-arabinose, L-arabinose and 2-deoxy-glucose. Has higher activity towards oligomeric sugars, such as maltose, maltotriose or cellobiose. It may function to input sugar-derived electrons into the respiratory network.
|
P75804
|
Q5WI27
|
XPT_ALKCK
|
Xanthine phosphoribosyltransferase
|
Alkalihalobacillus
|
MELLKEAIRKRGSVLSSGVLKVDQFLNHQVDTNLMSAIGEEFARLFADEHVTKVVTIESSGIAPSFMCAHSLQVPLIFARKKKSVTMDKENVYSSRVYSFTKKEYSEVTVSKDWLCPGDRVLIIDDFLANGQAATGLTQIVEEAGATVAGIGIVIEKSFQDGRALLEGKGYRIESLARISSLEGNKVQFVEESAHFAYNKS
|
Converts the preformed base xanthine, a product of nucleic acid breakdown, to xanthosine 5'-monophosphate (XMP), so it can be reused for RNA or DNA synthesis.
|
Q5WI27
|
Q9Y9H2
|
TRPB2_AERPE
|
Tryptophan synthase beta chain 2
|
Aeropyrum
|
MDLARYRFDLSIEEVPTSWYNILPDLPEEVPPPLNPKTGEPVDPSALAKLFPKALIEQEVSRERYIEIPGEVHEAYISFARRPTPLLRAVNLERALNTPAEIYYKYEGVTPTGSHKINTALAQAYYNKLEGVERLVTETGAGQWGSALSAAGAYFGVKVRVYMVRVSYLQKPYRRTLMELYGAEVYPSPSDKTEFGRKLLAENPNHPGSLGIAISEAIEDVINSGGNAKYSLGSVLNHVLLHQTVIGLEAEKQFREAGVYPDIMIGAVGGGSNFAGFTYPFIRHRLKGSSSTRFIAVEPKASPSMTRGVYTYDYGDTAGLTPLLKMHTLGHTYQVPPIHAGGLRYHGVAPTLSVLLKHGIVEARAYHQREVFRAAHMFAKAEGIVPAPESAHAVKAAIDEAIKARDEGRRVVIAFNLSGHGLLDLQGYREYLDGTLEDYEPEEIPASRR
|
The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
|
Q9Y9H2
|
B8F6M2
|
YIDC_GLAP5
|
Membrane protein YidC
|
Glaesserella
|
MNSNRSLLIMGLLLVSFLIFTQWQQDYNPEIQAQKQAMAQAQTQQVANQSSDVPASSNAASINEQSTKGKTITIETDVLRLTVDTLGGDVVDSDLLKYNAELDSNTPFELLQDNGKVLYVAQSGLVGKNGIDTTAGRAQYQATAEKFALAEGQDEIALPLTFEKDGVVYTKTFTLKRGSYNVAVNYHIKNGTAETLEVQPYGQLKHTLVESTGNFAMPTYTGGAYSSSEVNYKKYSFDEMAKANLSVDTKAGWAAVLQHYFVSAWIPNQDAENNLYTRTGNGVGTIGYRGPVTQVAPNGEATITSHLWTGPKDQAAMAQVANNFDLTVDYGWAWFIAKPLFWLLTFIQSIVSNWGLAIIGVTIVVKTILYPLTKAQYTSMAKMRMLQPRIQEMRERFGDDRQRMSQEMMKLYKEEKVNPMGGCLPILLQMPIFIALYWTFMEAVELRHAPFFGWIQDLSAQDPYYIFPLLMGGSMYLLQKMSPTPIADPVQQKVMNFMPVMFTVFFLWFPSGLVLYWLTSNLITIAQQWLIYRNLEKKGLHTRVKK
|
Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins.
|
B8F6M2
|
A3D7K4
|
TRUB_SHEB5
|
tRNA-uridine isomerase
|
Shewanella
|
MARRPKGRFIDGIVLLDKSTGMSSNFALQRVKRFFNANKAGHTGALDPLATGMLPVCLGEGTKFSQHLLDADKRYLVTAKLGERTDTSDSDGEVVQTRAIDFTEAQLLTALDFFRGETQQVPSMYSALKYQGQPLYKYAREGIEVPRESRPITVFELNFIGLEGDELTLDIHCSKGTYIRTIIDDLGEMLGCGAHVIMLRRTQVAQYPYARMVSLEQLEALVAQAHEQQIDPSILLDPLLLPMDTAVADFPEVNVPDAIAPYLMQGQAVRVPVNAGLKTDELVRITLGDIRRFVGIGTMNEDGLLAPKRLIVIHDEPAETD
|
Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
|
A3D7K4
|
P28120
|
WNT52_EPTST
|
Protein Wnt-5(II)
|
Eptatretus
|
SGSCSLKTCWLQLAEFRKVGDHLKECYDGAVAMRLGRRRTLELRNSRLNPPSADDLVYLQTSPDYCTRNARTGSLGTVGRACNKTSAGMDGCELMCCGRGYDQFKATVVERCHCKF
|
Ligand for members of the frizzled family of seven transmembrane receptors. Probable developmental protein. May be a signaling molecule which affects the development of discrete regions of tissues. Is likely to signal over only few cell diameters.
|
P28120
|
Q28RL2
|
TPIS_JANSC
|
Triose-phosphate isomerase
|
unclassified Jannaschia
|
MARKLAAGNWKMNGVEADLAEVDALGEAVAAANCDVLLCPPATLIAPMAKRAGLMDLYVGGQTCHTAASGAHTGDVSAAMLADAGASHVILGHSERRADHGERSEDVAAQVTAAIDANLIAIICVGETEAERDANVTLNVVSSQLAGSIPTGATPAQIVVAYEPVWAIGTGRTPTLEQIAEVHDHIRSELAARRGSAANDIPLLYGGSVKPGNAAEIFAVSNVDGALVGGASLKASDFGGIIAALSAA
|
Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
|
Q28RL2
|
P18735
|
ZG7_XENLA
|
Gastrula zinc finger protein XlCGF7.1
|
Xenopus
|
TREKPFTCTECGKGFSDKSNLRSHQRTHTREKPFTCTECGKSFSQKIGLHNHLKCHTGEKPFMCTECGKSFSNKSNLHTHRKIHTGERPYICTECGKTFPRKKNLQSHQTVHTQEKPFTCSECGKCFSQKKNLHTHQKIHTGEKPFKCNECGQAFLRKRNLLSHERIH
|
May be involved in transcriptional regulation.
|
P18735
|
Q9K9G6
|
THIX_HALH5
|
Formylaminopyrimidine transport permease protein ThiX
|
Halalkalibacterium (ex Joshi et al. 2022)
|
MKRSYQALEPTLFFLMLMVIWEISARMIGQPYLLPSPIQIVMRTIDLSESLFFTHLPATLAIISIGLALSIVLGILLSLLMFWNERVERAVYPLLVASQTIPVIALAPIFVLWFGYSIWSKVAVTVLLTFFPITVNTYDGLKSTNRQYEELFYTMGATKRQLFYRLFVPSTLPSFLTGLRIAVPLAVIGAAVGEWLGANEGLGYFSRRMMTQFDGPGVFAPIFILSLLGILGFAAIKKLENILLPWRKKQ
|
Participates in a thiamine pyrimidine salvage pathway as part of the ABC transporter complex ThiXYZ involved in the import of thiamine degradation products such as the formylaminopyrimidine N-formyl-4-amino-5-aminomethyl-2-methylpyrimidine (FAMP). Is probably responsible for the translocation of the substrate across the membrane.
|
Q9K9G6
|
Q9W552
|
VPS26_DROME
|
VPS26 protein homolog
|
Sophophora
|
MNFLGFGQSADIEIVFDGAEHKTAEVKGEDGKVEKMLLFYDGETVSGKVNVTLKKPGSKLEHQGIKIEFIGQIELYYDRGNHHEFKCLAKALARPGDLIQNNSYPFDFPKVEKQFEVYAGSNVRLRYFLRATIVRRISDITKEVDIAVHTLCSYPEMNNPIKMEVGIEDCLHIEFEYNKSKYHLRDTIIGKIYFLLVRIKIKHMEIAIIKKESTGTGPTMFNENETIAKYEIMDGAPVKGESIPIRVFLAGYNLTPTMRDINKKFSVKYFLNLVLMDTEDRRYFKQQEITLWRKADKPRYHGAQQHQQQQHQHVPLHAPPHLVSGPAAPTVAHSLISSSTDSGEVGGAPTAPGTAGSESKMGLFTRESPNQEFSQQQMDSPPLTPTPSTASVAVAVPTAASSVSEPAPERGIGDGAAAATTSASPVAMLSSSPPPLLPVSPLSRSETEASEQVQPEDEDLDAITPNTKKTGATPLATD
|
Component of the retromer complex which acts in conjunction with wingless (wg) and clathrin-mediated endocytosis to sustain a wntless (wls) traffic loop. This loop encompasses the Golgi, the cell surface, an endocytic compartment and a retrograde route leading back to the Golgi, thereby enabling wls to direct wg secretion. The hh and dpp signaling pathways do not require the retromer complex suggesting that it does not play a general role in exocytosis.
|
Q9W552
|
Q927P1
|
TRUA_LISIN
| null |
Listeria
|
MTRYKAIISYDGSGFFGYQVQPNTRTVQAEIEKALEKMHKGKSVRITASGRTDTGVHAKGQVIHFDSELDITAEKFQKALQVMTPFDISFLTVEEAPADFHARFGTVGKEYRYVIKRTKIFDPFSRNFALHYPYELDIAKMKQASERLIGEHDFTSFCSARTERDSKVRTLYSIDFYEEDAETLVIAFQGNGFLYNMVRILTGTLLDAGQGRISPDDITKALLAHDRQKLISKTAPPQGLYLWRVDYE
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Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
|
Q927P1
|
B4EPB7
|
TYPH_BURCJ
|
TdRPase
|
Burkholderia cepacia complex
|
MFLPQEFIRRKRDGQPLDRDGMAAFVRGVTDGSVTEGQVAAFAMAVYFNDLSTDERVALTLAQRDSGDVLDWRALDLDGPVIDKHSTGGVGDVVSLMLGPMVAACGGYVPMISGRGLGHTGGTLDKLSAIPGYDVMPATDAFRRTVREVGVAIIGQTARLAPADKRIYAIRDVTATVESVAMITASILSKKLAAGLDGLVMDVKVGSGAFMPTAEKSAELARSIVDVGNGAGMKTTAILTDMNQSLAPCAGNALEVACAIDYLTGKSRPARLHDVTMALSAELLVTGGLARDVGHAREKLQQALDSGAAAERFARMVVALGGPADLLDAPARHLARAVVIVPVPAPASGVVQRVDCRALGLAVVALGGGRTRAEDAIDVSVGLSALAEIGQRVEAGEPLGFVHARDEATAAHAADAIRRGYVLGDTGEAPPTLYQRVD
|
The enzymes which catalyze the reversible phosphorolysis of pyrimidine nucleosides are involved in the degradation of these compounds and in their utilization as carbon and energy sources, or in the rescue of pyrimidine bases for nucleotide synthesis.
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B4EPB7
|
Q89AN2
|
XGPT_BUCBP
|
Xanthine phosphoribosyltransferase
|
Buchnera
|
MSKKYIVTWDMLQIYARELAQKLLPVNQWKGIIAVSRGGLIPSALLARELNIRFVDTICVSSYDHNRLRDLKILKYAAGNSSQIIIVDDLVDTGGTGKIIRNLYPKAKFVTIFAKPMGKLLVDEYIIDIPQKVWIEQPWDMGVTYQSPLVRDL
|
Purine salvage pathway enzyme that catalyzes the transfer of the ribosyl-5-phosphate group from 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to the N9 position of the 6-oxopurines guanine and xanthine to form the corresponding ribonucleotides GMP (guanosine 5'-monophosphate) and XMP (xanthosine 5'-monophosphate), with the release of PPi. To a lesser extent, also acts on hypoxanthine.
|
Q89AN2
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A5WBX3
|
UVRC_PSYWF
|
Excinuclease ABC subunit C
|
Psychrobacter
|
MVTPSLTAQADDKQARLKHLIKRLPNLPGVYKMLGKNGDILYVGKAKSLKSRVNSYFAKTIDHPKTRALVSRIHDIETIITRSETEALLLEQNLIKEHRPPYNVLLRDDKSYLYVFISADQPYPRLAYGRGKAKHQKGKFFGPFPSAHAAKETLVLMQKMFQMRQCTNTFFRQRKRPCLEYQIKRCRAPCVGLVSAEEYAADVQNTIRFLKGDSSDIHTTLIEKMEHSAEALDFEKAAFYRDQLSMLREVQSRQAVYTVQGEADIISIASQAGMTCVNVLTVRGGRVLGGKNYFPDVDSNEPINDNLSAFITSFYFQVTDDLPAEIIISHELPDQMALQEALSTYFEAKTVIKTNVREHRAEWLDLAKLNAHNALKTKLGDYLELHARFAALKEVLEPVSQSSIDTIECFDISHTMGEATIASCVVFDQGGARKRDYRQYAIHGVQDGDDYAAMAQAITRRYKKHPLPDVLLIDGGKGQLSMAKNVLTELGLLNDTLLIGVAKGEGRKAGLEVLHFIEHEPLDLPMDSKALHLIMNIRDEAHRFAITAHRKKRDKRRSSSVLEAIPGLGEKRRRDLLNHFGGLQQLLGASQQELEGVNGIGKVMANTIYKVLHE
|
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision.
|
A5WBX3
|
Q7VLH3
|
ZAPB_HAEDU
|
Cell division protein ZapB
|
Haemophilus
|
MSLSIIDQLEEKIKQAVETIQLLQLEVEELKEKNNNLTQERDGLRQEHEQLKVEQQNFQERLRSLLGQIDNV
|
Non-essential, abundant cell division factor that is required for proper Z-ring formation. It is recruited early to the divisome by direct interaction with FtsZ, stimulating Z-ring assembly and thereby promoting cell division earlier in the cell cycle. Its recruitment to the Z-ring requires functional FtsA or ZipA.
|
Q7VLH3
|
A8GIC1
|
TILS_SERP5
|
tRNA(Ile)-lysidine synthetase
|
Serratia
|
MNNNQLSAQLARQLGAHRHLLVAFSGGLDSSVLLHLLVGLRQQLPDLQLRAVHVHHGLSAFADQWVTHCRQQCVAWQLPLVVQHVQVDSQQGGIEAAARAARYSAFASTLAADETLLTAQHLDDQCETFLLALKRGSGPAGLSAMAAQTSLGNNHLLRPLLGHSRQQLEAYAQQHQLSWIEDDSNQDPRFDRNFLRLQVLPLLNQRWPHFAAATARSASLCAEQEQLLDELLAEQLHNLLDEDRALAIDGLLTCSAARRFALLRRWIALFGVTMPSREQLQRLWEEVALSREDAEPQLQLGQYQFRRFRRRLYLLPLMADLREISLSWSLDDSLMLPDGLGELVSGEGDICLRAPQSQQKVSIRFSAQGKHRILGRAHSRPIKKLWQELGIPPWQRERIPLIYYDDQLIAALGIFVSEAGQTPEGQQPWRLHWRKK
|
Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
|
A8GIC1
|
B2RHI2
|
YIDD_PORG3
|
Putative membrane protein insertion efficiency factor
|
Porphyromonas
|
MRLIKAFLVQLLLLPIFFYKRFISPLTPPSCRFTPSCSSYAIEALRKYGPGKGLLLSIKRILRCHPWGGSGYDPVP
|
Could be involved in insertion of integral membrane proteins into the membrane.
|
B2RHI2
|
A3N0N5
|
YACG_ACTP2
|
DNA gyrase inhibitor YacG
|
Actinobacillus
|
MSETIVNCPTCNQDVIWKPESKYRPFCSERCQLIDLGEWANEEKRIAAVENDVMTSDLEGHY
|
Inhibits all the catalytic activities of DNA gyrase by preventing its interaction with DNA. Acts by binding directly to the C-terminal domain of GyrB, which probably disrupts DNA binding by the gyrase.
|
A3N0N5
|
Q8NIH3
|
TRI5_FUSBO
|
Sesquiterpene cyclase
|
Fusarium
|
MENFPTEYFLNTSVRLLEYIRYRDSNYTREERIENLHYAYNKAAHHFAQPRQQQMLKVDPKRLQASLQTIVGMVVYSWAKVSKECMADLSIHYTYTLVLDDSSDDPHPAMLNYFDDLQAGREQAHPWWALVNEHFPNVLRHFGPFCSLNLIRSTMDFFEGCWIEQYNFGGFPGSDDYPQFLRRMNGLGHCVGASLWPKELFDERKNFLEITTAVAQMENWMVWVNDLMSFYKEFDDERDQISLVKNFVTCHEITLDEALEKLTQETLHSSKQMVAVFADKDPQVMDTIECFMHGYVTWHLCDARYRLHEIYKKVKDQDTEDAKKFCKFFEQAANVGAVAPSEWAYPQVAQLANVRAKGDVKEAQKPILSSIELVE
|
TS is a member of the terpene cyclase group of enzymes. It catalyzes the isomerization and cyclization of farnesyl pyro-phosphate to form trichodiene, the first cyclic intermediate in the biosynthetic pathway for trichothecenes. It serves to branch trichothecene biosynthesis from the isoprenoid pathway.
|
Q8NIH3
|
Q0TQZ9
|
XPT2_CLOP1
|
Xanthine phosphoribosyltransferase 2
|
Clostridium
|
MELLKDKIKKEGRVTEDNILMVDSFLNHQMDVEFFNEVGKEFKDRFKNDQIDKILTIESTGIGLGIITAQYFDNVPVVFGKKIERLPRNKREEVFNSEVYSFTKKTIYNVVVDKKFIKPGEKILIVDDFLANACAVFGLIDVVKQAGAEVVGVGIVIEKGFQSGRAHLEDKGIRVESLVTIDKIEDGEVYFK
|
Converts the preformed base xanthine, a product of nucleic acid breakdown, to xanthosine 5'-monophosphate (XMP), so it can be reused for RNA or DNA synthesis.
|
Q0TQZ9
|
Q56254
|
TFS_THECE
|
Transcription elongation factor IIS/RNA polymerase subunit homolog
|
Thermococcus
|
MKFCPKCGNLMLPDRKRKVWVCRSCGYEEPFDEEKDREKTVIKQEVKHKPDEGIVVIEQDLKTLPTTKITCPKCGNDTAYWWEMQTRAGDEPSTIFYKCTKCGHTWRSYE
|
Induces RNA cleavage activity in the RNA polymerase. In its presence, the cleavage activity of the RNA polymerase truncates the RNA back to position +15 in a stepwise manner by releasing mainly dinucleotides from the 3'-end of the nascent RNA. The truncated RNAs are able to continue elongation. Involved in transcriptional proofreading and fidelity. Misincorporation of nucleotides during elongation of transcription leads to arrested elongation complexes which are rescued by TFS-promoted removal of a dinucleotide from the 3'-end. TFS is able to induce a cleavage resynthesis cycle in stalled elongation complexes (resulting from the next missing nucleotide or a reduced incorporation rate of a wrong nucleotide) preventing misincorporation and enabling proofreading in a post-incorporation manner. Pausing of elongation complexes is the main determinant of TFS-induced RNA cleavage.
|
Q56254
|
Q96ME7
|
ZN512_HUMAN
|
Zinc finger protein 512
|
Homo
|
MSSRLGAVPATSGPTTFKQQRSTRIVGAKNSRTQCSIKDNSFQYTIPHDDSLSGSSSASSCEPVSDFPASFRKSTYWMKMRRIKPAATSHVEGSGGVSAKGKRKPRQEEDEDYREFPQKKHKLYGRKQRPKTQPNPKSQARRIRKEPPVYAAGSLEEQWYLEIVDKGSVSCPTCQAVGRKTIEGLKKHMENCKQEMFTCHHCGKQLRSLAGMKYHVMANHNSLPILKAGDEIDEPSERERLRTVLKRLGKLRCMRESCSSSFTSIMGYLYHVRKCGKGAAELEKMTLKCHHCGKPYRSKAGLAYHLRSEHGPISFFPESGQPECLKEMNLESKSGGRVQRRSAKIAVYHLQELASAELAKEWPKRKVLQDLVPDDRKLKYTRPGLPTFSQEVLHKWKTDIKKYHRIQCPNQGCEAVYSSVSGLKAHLGSCTLGNFVAGKYKCLLCQKEFVSESGVKYHINSVHAEDWFVVNPTTTKSFEKLMKIKQRQQEEEKRRQQHRSRRSLRRRQQPGIELPETELSLRVGKDQRRNNEELVVSASCKEPEQEPVPAQFQKVKPPKTNHKRGRK
|
May be involved in transcriptional regulation.
|
Q96ME7
|
A6VMV1
|
Y930_ACTSZ
|
Nucleotide-binding protein Asuc_0930
|
Actinobacillus
|
MELIIISGRSGAGKSVALRALEDIGYYCVDNLPIDLLPQLADILSQSQASAAISLDIRNLPNSSQHLDEILTELENKHQIKIIFLDADRSTLIRRYSDSRRLHPLSVQNQDLSLEAAIDAEQIQLDPLIQHANLIIDTAVLSTHELAERLREFLRGNSDKELKIVVESFGFKYGLPLDADYVFDVRFLPNPHWNPSLRPMTGLEQPVIDFLSKYEDVANFIYTTRNYIETWLPMLERNNRSYLTIAIGCTGGKHRSVYIAQQLGEYFQDKGKHVKIQHKSLEKHKNR
|
Displays ATPase and GTPase activities.
|
A6VMV1
|
P01224
|
TSHB_PIG
|
Thyrotropin beta chain
|
Sus
|
MTAIFLMSMLFGLACGQAMSFCIPTEYMMHVERKECAYCLTINTTICAGYCMTRDFNGKLFLPKYALSQDVCTYRDFMYKTVEIPGCPHHVTPYFSYPVAISCKCGKCNTDYSDCIHEAIKTNYCTKPQKSYVLEFSI
|
Indispensable for the control of thyroid structure and metabolism.
|
P01224
|
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