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2.75k
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5.51k
AlphaFoldDB
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Q3B8E5
AP15B_XENLA
Anaphase-promoting complex subunit 15B
Xenopus
MSTLFPSLLPQVTDSLWFNLDRPCVDENELQQQEQQHQAWLLSIAEKDSSLVPIGKPASEPYDEEEEEDDEDDEDSEEDSEDDEDMQDMDEMNDYNESPDDGEIEADMEGAEQDQDQWMI
Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle.
Q3B8E5
Q6LYM1
DNLI_METMP
Polydeoxyribonucleotide synthase [ATP]
Methanococcus
MLFSDFCKILDKIEKTTKRLEKTDYFVELIDFIKTSEKPENLKQVSQITIGRVFAEFENKEIGIGPNLLLEAVKTTGIPEKDLKSKIKETGDIGTAVENLSSNIKQVSLFSQALTLEEVYSTLKKLSEIEGNSSQKKKTRIISNLLILADPVESRYISRLILEDMRIGMNIPTILASFSNYFNVNKESVEKIYAVTNDIGLLGEKLISGSDIENDPELKLKVFRPIKPMLAQLTPSIEDAMIETKMPQFETKYDGARVQVHKSNGDVKIYSRRLENITNSVPELVEEIKKLDIDNIILEGECVAMDLDSGKPRPFQDILRRFRRKYNIDKMAEKIALRIYFFDVLYYNRGLIDTPLKTRREILEKLFGTNNWDSELEKIKKEIFSSKMLFSSFKLNSGDPNLVKEFFNWSLSIGHEGIMIKNPDAPYTPGSRVKTMYKVKPTLENLDVVVTRAKIGMGKRKDWYGSYELSVKDNDGNLHVIGNVGSGLTEDDLEKLTKIVNEIKIEDLGEEVILEPKIVLEVTYEEIQTSEKYEMGYALRFPRVVQIREDKSINDINTLDDVKKIYEIERNRK
DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.
Q6LYM1
B4EWD2
TATA_PROMH
Sec-independent protein translocase protein TatA
Proteus
MGGISIWQLLIIAVIVVLLFGTNKLRTLGSDLGASVKGFKKAMGDENQKETNNAEKTTNDADFDTKNLAQKTSTEEKSTTESKNKEQV
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.
B4EWD2
O01422
CSN2_CAEEL
COP9 signalosome complex subunit 2
Caenorhabditis
MGDEYMDDDEDYGFEYEDDSGSEPDVDMENQYYTAKGLRSDGKLDEAIKSFEKVLELEGEKGEWGFKALKQMIKITFGQNRLEKMLEYYRQLLTYIKSAVTKNYSEKSINAILDYISTSRQMDLLQHFYETTLDALKDAKNERLWFKTNTKLGKLFFDLHEFTKLEKIVKQLKVSCKNEQGEEDQRKGTQLLEIYALEIQMYTEQKNNKALKWVYELATQAIHTKSAIPHPLILGTIRECGGKMHLRDGRFLDAHTDFFEAFKNYDESGSPRRTTCLKYLVLANMLIKSDINPFDSQEAKPFKNEPEIVAMTQMVQAYQDNDIQAFEQIMAAHQDSIMADPFIREHTEELMNNIRTQVLLRLIRPYTNVRISYLSQKLKVSQKEVIHLLVDAILDDGLEAKINEESGMIEMPKNKKKMMVTSLVVPNAGDQGTTKSDSKPGTSSEPSTTTSVTSSILQGPPATSSCHQELSMDGLRVWAERIDSIQSNIGTRIKF
Essential component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of the SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF. The CSN complex plays an essential role in embryogenesis and oogenesis and is required to regulate microtubule stability in the early embryo. Mediates mei-3/katanin targeting for degradation at the meiosis to mitosis transition via deneddylation of cul-3.
O01422
P46701
PURK_MYCLE
5-(carboxyamino)imidazole ribonucleotide synthetase
Mycobacterium
MMAVPSRCSLGVAPLVAMVGGGQLARMTHQAAIALGQTLRVLATAADEPAAQVTPDVVIGSHTDLEDLRRVALGADALTFDHEHVPTELLDKLVAEGINVAPSPQALVHAQDKLVMRRRLAALGAAMPRFMALDSVDDLAEIDAFAQRLTGSKDAPMVVKAVRGGYDGRGVQMVRDSAHAREVASGYLVDGMPVLVEERVELRRELSALVARSPFGQGAAWPVVETVQRDGICVLVVAPALALADDLASAAQQLALRLAAELGVVGVFAVELFETADGALLVNELAMRPHNSGHWTMDGARTSQFEQHLRAVLDYPLGETDAVAPVTVMVNVLGAPQPPTLSVVTMDERLHHLFARMPDARVHLYDKVERPGRKVGHINFRGTDKDRKNPTKLRERAELAAHWLSHGQWTDGWDPHRAGDDVVEISLACGGRNDAQRQR
Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5-carboxyaminoimidazole ribonucleotide (N5-CAIR).
P46701
O48668
LGB2_PEA
Leghemoglobin Lb5-10
Pisum
MGFTDKQEALVNSSWESFKQNLSGNSILFYTIILEKAPAAKGLFSFLKDTAGVEDSPKLQAHAEQVFGLVRDSAAQLRTKGEVVLGNATLGAIHVQRGVTDPHFVVVKEALLQTIKKASGNNWSEELNTAWEVAYDGLATAIKKAMT
Provides oxygen to the bacteroids. This role is essential for symbiotic nitrogen fixation.
O48668
Q9M336
UPP_ARATH
UMP pyrophosphorylase
Arabidopsis
MACSIGNAFRCSSDTLRFAPRQQCSSRLNPNPSSFLSFNSSPILAQNLGASSSSLSRRTIRARTKMAASEASINGSNRMLVFVPPHPLIKHWISVLRNEQTPCPVFRNAIAELGRLLMYEASREWLPTVVGEIMSPMGPASVEFIDPREPIAVVPILRAGLALAEHASSVLPANKIYHLGVSRDEKTLLPSVYLNKLPDEFPKNSRVFLVDPVLATGGTIMAAMDLLKERGLSVQQIKVICAIAAPPALSKLNEKFPGLHVYAGIIDPEVNEKGYIIPGLGDAGDRSFGTETHWVK
Uracil phosphoribosyltransferase (UPRT) that catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate. Is probably the only functional UPRT, since the dual-domain proteins of the UKL family seem to lack this activity.
Q9M336
B6IV67
SYT_RHOCS
Threonyl-tRNA synthetase
Rhodospirillum
MVSITLPDGGVRTFPRGTTGGQIASAIAKSLGKAALAVKIDGKQRDLALPVEQDCRLEILTRESPEALELIRHDAAHIMAEAVQALYPGTQVTIGPAIATGFYYDFARSEPFTPDDLVKIEAKMHEIVNADAPFTREVWKRDDAIEHFRSIGEKYKAQIIEDLPATETITIYRQGRWYDLCRGPHLPSTGKVGHAFKLMKVAGAYWRGDARNEMLQRIYGTAWRTEKELADHLHQIEEAEKRDHRKLGREMDLFHVQEEAVGSVFWHPKGWALYRTLENYIRTKLDAAGYVEVRTPQLYDSSLFKASGHWDMYGDNMFKIRESVAEDGTEKFLGVKPMNCPAHVQIFRQGLKSYRDLPLRMAEFGNCHRNEPSGALHGILRVRNFTQDDAHIFCTEDQVGQEAKEYFALQLGVYKDLGFDKIAVKLALRPDVRLGTDETWDKAEESLRVALRANDLEFEELPGEGAFYGPKVEFHLTDAIGRSWQCGTLQLDFQLPERLDASYIGQDGARHRPVMLHRAILGSLERFIGMMIEHYAGKFPLWLAPVQVVVATIVSEADAYAQTVAETLRRAGLRVEADVRNEKINLKVREHSLAKVPVMLVVGAREAEQGTVAVRRLGGKDQEVLALGDAVARLKDEARSPAGAETVSPAF
Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr).
B6IV67
Q61333
TNAP2_MOUSE
Primary response gene B94 protein
Mus
MLKMVTFFQGFPGQQSVPGTLNFAVSPQKPRSTSEAESETSMSEASSEDLMPSPEAPDGEEESAKKKEKKSKGLANMFSVFTKGKKKKKDQPRLSDLEVQPKPRPELDGPLPTVEELKEALEHGRLEVAWQVLALERQLEAAAAAGGMSNEELVWRQSKVEALYVLLCDQVLGVLRRPLEAAPERLSQALAVVSQEELEDRRASGGPLAAALEATRPRRWLQRWRGVVAEVAAERLDAQPATAPEGRSEAESRFLHMGRTMKEDLEVVVERLKPLFPDEFNVVRTYAESYHYHFASHLCALAQFELCERDTYLLLLWVQNLYPNDILNSPKLAQELQGVGLGSLLPPKQIRLLEAMFLSNEVTSVKQLMARALELESQRWTQDVAPQSLDGHCHSELAIDILQIISQGQTKAENITSDVGMQIKQLLLVELAALLRSYQRAFDEFLEKSKLLRNYRVNIMANINNCLFFWTSVEQKWQISHDSLNRLLEPLKDLKAHGFDTLLQSLFLDLKPLFKKFTQTRWANPVETLEEIITTVSSSLPEFSELQDCFREELMETVHLHLVKEYIIRLCKRRLVLKTAEQQQQLARHILANADAIQGFCTENGSTATWLHRALPMIAEIIRLQDSSAIKIEVATYATWYPDFSKGHLNAILAIKGNLPSSEVRSIRNILDINTGVQEPPRPLFSLIKVT
May play a role as a mediator of inflammation and angiogenesis.
Q61333
B1HTW9
GATA_LYSSC
Glutamyl-tRNA(Gln) amidotransferase subunit A
Lysinibacillus
MTLFERSAKELQAEIKAGNLSIADLTKEAYERIAKLDGDVQAFLASNEEKATAQAAEMDKVPFEERGPLFGLPIGVKDNIVTEGLETTCASKILEGFMPIYDATVVNKLREAGMITVGKLNMDEFAMGSSNENSYYKTTKNPWNLNHVPGGSSGASAASVAAGEVPFSLGSDTGGSIRQPAAYCGVVGMKPTYGRVSRFGLVAFASSLDQIGPITRNVEDNALLLEAIAGLDPNDSTSADVEVPNYAAALTGDVKGLRIAVPKEFLGEGVGEAARQSVLAALEVLKGLGATVEEVSLPHSKYALAAYYILSSSEASSNLSRFDGIRYGFRAENVTNLMDLYKETRAQGFGDEVKRRIMLGTYSLSAGTYDAYYKKAQQARTLIKADYDKVFEDFDVIIGPTSPTPAFKIGENVDDPMTMYANDILTIPMNLAGVPAISIPCGFDNGLPLGLQIIGKYFDEATIYRVAHAFEQATEFHKQVPQMWEGK
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).
B1HTW9
Q8UGK4
ACPS_AGRFC
4'-phosphopantetheinyl transferase AcpS
Agrobacterium tumefaciens complex
MIIGLGSDLIDIRRVEKSIERFGERFTHRCFTDIERAKSDGRKNRAASYAKRFAAKEACSKALGTGLANGVFWKDMGVVNLPGGKPTMILTNGAGARLAAMLPAGHRANIHLTITDDFPYAQAFVIIEALPVNG
Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Q8UGK4
C3P3T7
TRPD_BACAA
Anthranilate phosphoribosyltransferase
Bacillus cereus group
MNNYLRKLVEGQHLTEEEMYKAGLLLLNENILESEIAAFLVLLKAKGETAEEIYGLVRALREKALPFSNHIQGAMDNCGTGGDGAQTFNISTTSAFVLAGAGVKVAKHGNRAVSSKTGSADLLEELGVNISSTPNEIDYLLEHVGIAFLFAPAMHPALKRIMKIRKELNVPTIFNLIGPLTNPVNLETQFVGIYKRDMLLPVAQVLQKLGRKQALVVNGSGFLDEASLQGENHVVILKDNEIVETSIEPEKYGFSIVKNEEIRGGNSKENAKITLGVLSGEKSVYRDTVLFNAGLALFANGKAKTIEEGITLAAHSIDSGKALAKLNLLIAASNEELERVN
Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
C3P3T7
B0JMD9
YIDD_MICAN
Putative membrane protein insertion efficiency factor
Microcystis
MKGIFIGLIEGYRRFISPLFPPSCRFQPTCSQYAMEAIDRFGVLRGSWLAIKRILRCHPFHPGGYDPVPPCHHKHD
Could be involved in insertion of integral membrane proteins into the membrane.
B0JMD9
Q34572
NU4LM_GORGO
NADH dehydrogenase subunit 4L
Gorilla
MPLIYMNIMLAFTISLLGMLVYRSHLMSSLLCLEGMMLSLFIMATLMTLNTHFLLANIVPITMLVFAACEAAVGLALLVSISNTYGLDYVQNLNLLQC
Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor.
Q34572
Q9DB07
IFT46_MOUSE
Intraflagellar transport protein 46 homolog
Mus
MADNSSDEYEEDNKEKKKPSQLTPQQGFSENDDDDDDDSSETDSDDDDDDEEHGAPLEGAYDPADYEHLPVSAEIKELFEYISRYTPQLIDLDHKLKPFIPDFIPAVGDIDAFLKVPRPDGKPDHLGLLVLDEPSTKQSDPTVLSLWLTENSKQHNITQHMKVKSLEDAEKNPKAIDTWIESISELHRSKPPATVHYTRPMPDIDTLMQEWSPEFEELLGKVSLPTVEIDCSLAEYIDMICAILDIPFYKSRIQSLHLLFSLYSEFKNSQHFKALAEGKKVFTPPPNSASQAGDAETLTFI
Forms part of a complex involved in intraflagellar transport (IFT), the bi-directional movement of particles required for the assembly, maintenance and functioning of primary cilia. May play a role in chondrocyte maturation and skeletogenesis.
Q9DB07
Q9M812
CUT1C_ARATH
Protein CURVATURE THYLAKOID 1C, chloroplastic
Arabidopsis
MASISATLPSPLLLTQRKSNLTSIQKLPFSLTRGTNDLSPLSLTRNPSSISLMVKASGESSDSSTDLDVVSTIQNVWDKSEDRLGLIGLGFAGIVALWASLNLITAIDKLPVISSGFELVGILFSTWFTYRYLLFKPDRQELSKIVKKSVADILGQ
Determines thylakoid architecture by inducing membrane curvature.
Q9M812
Q9PPB4
DAPA_CAMJE
4-hydroxy-tetrahydrodipicolinate synthase
Campylobacter
MDKNIIIGAMTALITPFKNGKVDEQSYARLIKRQIENGIDAVVPVGTTGESATLTHEEHRTCIEIAVETCKGTKVKVLAGAGSNATHEAVGLAKFAKEHGADGILSVAPYYNKPTQQGLYEHYKAIAQSVDIPVLLYNVPGRTGCEISTDTIIKLFRDCENIYGVKEASGNIDKCVDLLAHEPRMMLISGEDAINYPILSNGGKGVISVTSNLLPDMISALTHFALDENYKEAKKINDELYNINKILFCESNPIPIKTAMYLAGLIESLEFRLPLCSPSKENFAKIEEVMKKYKIKGF
Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Q9PPB4
P46514
LE10_HELAN
DS10
Helianthus
MASQQGQQTRKIPEQEKKDLDQRAAKGETVVPGGTRGKSLEAQERLAEGRSKGGQTRKDQLGTEGYKEMGKKGGQTTGDKSAGEREEEEEED
LEA proteins are late embryonic proteins abundant in higher plant seed embryos. They may play an essential role in seed survival and in controlling water exchanges during seed desiccation and imbibition.
P46514
A5E2I8
SPB4_LODEL
ATP-dependent rRNA helicase SPB4
Lodderomyces
MQTNKGSLLWENLRVDLEPWLKDAIRSLNYPTMTPVQASTIPLLSGNKDVIVEAVTGSGKTLAFAIPVLQKVSKRLYQVPEGEEKPEPVKRGHMLAIVMAPTRELAKQIQMVFDKVLELLPEEDSYEPRIKTQLLVGFLGNVREDLDSYQENRPQILIATPGRLLDFMSLQIVKTSSLEIVILDEADKLLDMSFETDVIKILKMLPKQRRTGLFSATISAAGDTIFRTGMNNPVKLQVKTKNFLGEQNNAPTSLQLSYMMIEPEHKLTTMLQMLRDNQFKKAIVYFPTCTSVKHFYQMLSKLCKSSANDIDISALLFFSLHGQLTTKSRLNTLEKFTEGNDESKKYILMATDVAARGIDIPDVDLVIQIDPPTDPSVFLHRCGRTGRANKVGRAIVMLNNDTQEEDYVGFMEVKSVFMTKIDPPEDKDNHSFHNKFQKKLRKYMLEDRARHELAVKSYVGFVRYYSKHIASLIFRLASLDYIAIAKMYGLLRLPKMPESRYIENEKMPEDGWLGEVVDMDTYAYLDKSAEKARLENLEKDKLAKAENAKRRKELKVKNEAWSSKTEKRETKLERKEKMKRKREAIEKQLEAEQERGGLDEEEVKEDWKDLVRKNKKKQKSNGGGGGGGVLQGSFDDL
ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits. Binds 90S pre-ribosomal particles and dissociates from pre-60S ribosomal particles after processing of 27SB pre-rRNA. Required for the normal formation of 18S rRNA through the processing of pre-rRNAs at sites A0, A1 and A2, and the normal formation of 25S and 5.8S rRNAs through the processing of pre-rRNAs at sites C1 and C2.
A5E2I8
Q8YNK2
ALF_NOSS1
Fructose-1,6-bisphosphate aldolase
Nostoc
MALVPLRLLLDHAAENGYGIPAFNVNNLEQIQAILKAAAETDSPVILQASRGARNYAGENFLRHLILAAVETYPEIPIVMHQDHGNAPSTCYSAIKNNFTSVMMDGSLEADAKTPASFEYNVNVTREVVNVAHALGVSVEGELGCLGSLETGAGEAEDGHGFEGTLDHSQLLTDPDEAVNFVEATQVDALAVAIGTSHGAYKFTRKPTGEILAISRIEEIHRRLPNTHLVMHGSSSVPEDLIALINEYGGAIPETYGVPVEEIQKGIKSGVRKVNIDTDNRLAITAAVREALAKNPKEFDPRHFLKPSITYMQKVCAERYVQFGTAGNASKIKQVSLETFAAKYAKGELNAISKAAAKV
Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis.
Q8YNK2
C6AKG2
RSMH_AGGAN
rRNA (cytosine-N(4)-)-methyltransferase RsmH
Aggregatibacter
MTHLNAFSSVEHSTVLLHETVDGLALKENGIYIDGTFGRGGHSRLILSKLSANGKLIAIDRDPKAVAEAQKIQDPRFQIEHNTFSEILSICEKRGLVGKIDGILLDLGVSSPQLDDAARGFSFMKDGPLDMRMDDSKGISAAEWLQQVSEQDLAWVLKTFGEERFAKKIAKAIVNYNKSAVQNGSEFLTRTLQLAELIAHTVPFKDKHKHPATRSFQAIRIFINAELDELEKVLQSALTVLAPAGRLSVISFHSLEDRMVKHFMRKQSQGREIPKGLPLREDQIQRNQTLKVIGKAIMPTDAEIAQNPRARSAVLRVAERLN
Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
C6AKG2
P61382
CRCB1_STAAM
Putative fluoride ion transporter CrcB 1
Staphylococcus
MHRQFLSSCCQNLFFKFKLLLFEVNQMQYVYIFIGGALGALLRYLISFLNTDGGFPIGTLIANLTGAFVMGLLTALTIAFFSNHPTLKKAITTGFLGALTTFSTFQLELIHMFDHQQFITLLLYAVTSYVFGILLCYVGIKLGGGLS
Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
P61382
A9VH19
AROK_BACMK
Shikimate kinase
Bacillus cereus group
MKSIYITGYMGAGKTTIGKVLSKELHMDVVDTDQKIEEKQEKAIRDIFAEEGEMAFREYESEMVRSLPVQNVIITTGGGIIERAENRKWMKENGTVVYLYCDPHVIAERLREDTTRPLFQKKDIDAFITKFESRRAYYEEADIHIDTTNKSVKQIMNELKQKINE
Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
A9VH19
A7FMI1
RF3_YERP3
Peptide chain release factor 3
Yersinia
MSPSEYALEVAKRRTFAIISHPDAGKTTITEKVLLFGHAIQTAGTVKGRGSSHHAKSDWMEMEKQRGISITTSVMQFPYGGCLVNLLDTPGHEDFSEDTYRTLTAVDCCLMVIDAAKGVEDRTRKLMEVTRLRDTPILTFMNKLDREIRDPMEVLDEVERELNIACSPITWPIGCGKSFKGVYHLHKDETYLYQSGKGHTIQEVRIVKGLNNPDLDVAVGEDLAKQFRQELELVQGASHEFDHEAFLSGDLTPVFFGTALGNFGVDHMLDGLVEWAPAPMPRKTDTRVVVASEEKFTGFVFKIQANMDPKHRDRVAFMRVVSGRFEKGMKLRQVRTKKDVVISDALTFMAGDRSHVEEAYAGDIIGLHNHGTIQIGDTFTQGEDMKFTGIPNFAPELFRRIRLRDPLKQKQLLKGLVQLSEEGAVQVFRPLSNNDLIVGAVGVLQFEVVSSRLKSEYNVEAVYESVNVSTARWVECNDVKKFEEFKRKNELNLALDGGDNLSYIAPTMVNLNITQERYPDVIFRKTREH
Increases the formation of ribosomal termination complexes and stimulates activities of RF-1 and RF-2. It binds guanine nucleotides and has strong preference for UGA stop codons. It may interact directly with the ribosome. The stimulation of RF-1 and RF-2 is significantly reduced by GTP and GDP, but not by GMP.
A7FMI1
P53136
NSA1_YEAST
NOP7-associated protein 1
Saccharomyces
MRLLVSCVDSGSIKEVLCNIGTDTSVQSALQPFHVAPHLAEGLKAYVDRMWVISEDEAILARNSGVVELVKISKHLKENEALQVDPKGESKNEKSLSDDLPKFDISEFEITSSVSDLFDDAKLESLSSKSVKRTKLVDGFVTLCPIKKDSSNNTFVAATKSGLLHIIKKGEDKKLIKLASLGLKAPVEFLQLYDLEDTDTDKYIFAYGGEENLIKLVEIDSSFQSLKQIWEAKNVKNDRLDMRVPVWPMALRFLEPSPGKTEKGKLNYQFAAITRWSHLTKYSTQHGRKPFAQIDLLPNREPLSQMEVFDAKGENVVSSLGNFQSETFNELNVITTDYKKNVFKFDGNGRMLGKVGRDDITGSSTYIHVHDGKYLLQGGLDRYVRIFDIKTNKMLVKVYVGSRINFIVMLDDVEIEMPLSPSAKAAKGKQKRKVTELEEDADELWNKLEGKVAASKASKKSKI
Involved in the biogenesis of the 60S ribosomal subunit.
P53136
Q8PK11
EUTC_XANAC
Ethanolamine ammonia-lyase small subunit
Xanthomonas
MSVPSTPPRDAWAQLRQLTPARIALGRVGTSLPTDAHLEFQLAHAQARDAVHLAFDPAPLQAALEQRGRSNILLQSAAADRHQYLQRPDLGRRLAEEAAAQLRGLTAVHGGRHDVAVVVADGLSALAVHRHAARMLDQIDALASQEGWSLAPVVLVRQGRVAIGDEVGELLDARTVIVLIGERPGLSSPDSLGLYLTYTPRVGLTDAARNCISNIRAEGLSYAEATHKLGYLLREAFRRKLSGVQLKDEAEQPALLSGPADVAPRTFLLPD
Catalyzes the deamination of various vicinal amino-alcohols to oxo compounds. Allows this organism to utilize ethanolamine as the sole source of nitrogen and carbon in the presence of external vitamin B12.
Q8PK11
Q8PXF0
GUAAA_METMA
Glutamine amidotransferase
Methanosarcina
MRELKILVVNNYGQFCHLIHRTVRDLDMDTKIIPNVTPIEEILAEEPDGLILSGGPEMERAGLCFDYVREIDVPILGICLGHQAIALAYGGHVHAGKKGGYAEIEVEVLEEDDILRGLGPKTTVWASHADEVAILPDGFIHLARSDVCEIEAMRHPTKPIYGVQWHPEVSHTKKGEELLMNFFEVCDLY
Catalyzes the synthesis of GMP from XMP.
Q8PXF0
B1I1J4
RS3_DESAP
30S ribosomal protein S3
Candidatus Desulforudis
MGQKVDPRGLRLGIVRDWDAKWYAGKKDFSNLLLEDVKIRDYIKSKLLAAGISRIHIERTANRVRIAIHTAKPGVVIGRGGTEVEVLRKELEKLTGRQISINIVEIKTPELDAQLVAENVAAQLQRRVAFRRAMKQAVGRAMKLGAKGIRISVAGRLAGAEIARTEWYSEGKVPLHTLRADIDYGFSEAKTTYGKIGVKVWIYRGEILPERAAREGGR
Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation.
B1I1J4
P15276
ALGP_PSEAE
Alginate regulatory protein AlgR3
Pseudomonas
MSANKKPVTTPLHLLQQLSHSLVEHLEGACKQALVDSEKLLAKLEKQRGKAQEKLHKARTKLQDAAKAGKTKAQAKARETISDLEEALDTLKARQADTRTYIVGLKRDVQESLKLAQGVGKVKEAAGKALESRKAKPATKPAAKAAAKPAVKTVAAKPAAKPAAKPAAKPAAKPAAKTAAAKPAAKPTAKPAAKPAAKPAAKTAAAKPAAKPAAKPVAKPAAKPAAKTAAAKPAAKPAAKPVAKPTAKPAAKTAAAKPAAKPAAKPAAKPAAKPVAKSAAAKPAAKPAAKPAAKPAAKPAAKPVAAKPAATKPATAPAAKPAATPSAPAAASSAASATPAAGSNGAAPTSAS
The promoter for a critical alginate biosynthetic gene, AlgD, encoding GDP-mannose dehydrogenase, is activated only under conditions reminiscent of the cystic fibrosis lung (i.e. under high osmolarity), and at least two regulatory genes, AlgP and AlgQ, have been implicated in this activation process.
P15276
A5CXD7
PYRH_VESOH
Uridine monophosphate kinase
Candidatus Vesicomyosocius
MSKYKRILLKLSGEALASTTNIIDPVTLNKIVDIIKSVLSQNIEIAIVIGGGNIFRGETLTKTGINRITSDHIGMLSTIINALAIADTCQKNKVDALVMSGLSIGGGICNSINHIYAKQALKKGKVIIFCAGTGNPCFTTDTGAALRAIEIGADAIFKATKVDGIYTDDPVKNPNAKRYNSLSFDEAIEKNLQIMDVSAFALCRKHDLEICVFSMLENTNTLSDLLKGKLLGTIVRK
Catalyzes the reversible phosphorylation of UMP to UDP.
A5CXD7
D7Y2H5
NUCC_ECOM1
NucC nuclease
Escherichia
MSDWSLSQLFASLHEDIQLRLGTARKAFQHPGAKGDASEGVWIEMLDTYLPKRYQAANAFVVDSLGNFSDQIDVVVFDRQYSPFIFKFNEQIIVPAESVYAVFEAKQSASADLVAYAQRKVASVRRLHRTSLPIPHAGGTYPAKPLIPILGGLLTFESDWSPALGMSFDKALNGDLSDGRLDMGCVASHGHFYFNNIDSKFNFEHGNKPATAFLFRLIAQLQFSGTVPMIDIDAYGKWLAN
Protects E.coli strain JP313 against bacteriophage lambda cI- infection. When the cdnC-cap7-cap6-nucC operon is transformed into a susceptible strain it confers bacteriophage immunity. Mutations in the sensor (Cap7 also called HORMA) or effector proteins (CdnC, NucC) but not the disassembly protein (Cap6 also called Trip13) no longer confer immunity. The presence of the intact operon leads to culture collapse and cell death which occurs before the phage has finished its replication cycle, thus protecting non-infected bacteria by aborting the phage infection and preventing its propagation.
D7Y2H5
A4W6D7
NHAA_ENT38
Sodium/proton antiporter NhaA
Enterobacter
MKLLHRFFSNEASGGIILIIAAAAAMVFANLGATQGLYHAFLETPVELRVGVLEINKNMLLWINDALMAVFFLLVGLEVKRELVQGSLASRQRAAFPVIAAIGGMVVPALLYLAFNYQDPIARQGWAIPAATDIAFALGVLALLGSRVPVALKIFLMALAIIDDLGAIVIIALFYTSDLSILSLSVAAGAIAALALLNIFNVRRTGIYILVGVVLWTAVLKSGVHATLAGVIIGFFIPLKEQDGHSPAQQLEHVLHPWVAFMILPLFAFANAGVSLQGVTLSGLTSMLPMGIIAGLFIGKPLGISLFCWLALKLKLASLPQGTTFRQIMAVGVLCGIGFTMSIFISTLAFASMDPQLIVWAKLGILTGSLLAAFVGYSLLKVKLSGQVQPV
Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons.
A4W6D7
A5GVW9
RS17_SYNR3
30S ribosomal protein S17
unclassified Synechococcus
MAVKERVGTVVSDKMEKTVVVAVENRFPHPIYKKTVSRTTRYKVHDEDNRCQVGDRVRITETRPLSRSKRWAVAEIMTTKSGS
One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.
A5GVW9
P45020
CYOB_HAEIN
Cytochrome oxidase subunit II
Haemophilus
MIDYEFLRFIWWVLVIVLLIGFSVTDGFDMGVTALLPVIGKKEVERRIMINTIAPHWDGNQVWLLTAGGAIFAAWPIVYAVSFSGFYIALVLVLAALFLRPLGFEYRAKIDNPTWRSVWDWGLFAGGFVPALVFGVAFGNLLQGVPFHFNELTQVTYTGSFFELLNPFALLCGVISLSMLVTHGANWLQMKTTEALRDRARTVSQIGSIVTLIAFVLAGVWLYSKDGYVVTSTIDHFAPSSPMNKEVAVETGAWFRNFNEMPILWIFPALAVVAALLNAAFSKANRCGFAFFFSALTMAGVIITAAVSMFPFVMPSSSHPEQSLLMWDSTSSELTLTLMLIFAVVFVVIALAYTIWSYSKMFGRLDANFIDKNKHSLY
Probable cytochrome oxidase subunit.
P45020
P40688
SWA_DROME
Protein swallow
Sophophora
MSLQDESFPTDELFDQLNNLSSSGARNTWFAEHHKPAVFERDTAPFLEICYADPDFDADGDVANKSAKTCVSDPVGRDQEDEDDYDEDVDGDDHKLGCEKAPLGSGRSSKAVSYQDIHSAYTKRRFQHVTSKVGQYIAEIQAQDQKRRNVKFAGFQRVNSMPESLTPTLQQVYVHDGDFKVDKNCQTHSNSDSNYNSNSNNSSSSFDRLLAENESLQQKINSLRVEAKRLQGFNEYVQERLDRKTDDFVKMKCNFETLRTELSECQQKLRRQQDNSQHHFMYHIRSATSAKATQTDFLVDTIPASGNVLVTPHPLGDLTYNSSKGSIELALLSVAPSARVAQNPVQVQRAIHPQSLDFSSVSTEADGSGSGEHRVETSSRALVRRTPAPNNSETSQPSSNDSAIEVEAHEEERPSSRRQWEQQGELISPRQWGQHEGMYYFDKRNNRVIEVMGFNISQGRNQSHDTIHNQSINDSQTRLLVHSMSMSHLEAHDHFRSKRTTLGSRMLRFLGPCVRCRNGDPLNRSNVTYKDGLPAMPEEEFVDQRNQR
Has a role in localizing bicoid mRNA at the anterior margin of the oocyte during oogenesis, and a poorly characterized role in nuclear divisions in early embryogenesis.
P40688
Q52QH4
NAC68_ORYSJ
OsNAC4
Oryza sativa
MEMAAAVGGSGRRDAEAELNLPPGFRFHPTDEELVVHYLCRKVARQPLPVPIIAEVDLYKLDPWDLPEKALFGRKEWYFFTPRDRKYPNGSRPNRAAGRGYWKATGADKPVAPKGSARTVGIKKALVFYSGKAPRGVKTDWIMHEYRLADADRAPGGKKGSQKLDEWVLCRLYNKKNNWEKVKLEQQDVASVAAAAPRNHHHQNGEVMDAAAADTMSDSFQTHDSDIDNASAGLRHGGCGGGGFGDVAPPRNGFVTVKEDNDWFTGLNFDELQPPYMMNLQHMQMQMVNPAAPGHDGGYLQSISSPQMKMWQTILPPF
Probable transcription factor involved in stress response.
Q52QH4
Q130N3
BIOD_RHOPS
Dethiobiotin synthase
Rhodopseudomonas
MTTPIIVTGTDTGVGKTVFSAALAGALEATYWKPVQAGLDEETDRLAVLRLSGLPETRLLAEAYRLTTPASPHLAAEIDGVAIDPEALVLPDTQGPLVVEGAGGLLVPLTRHVTYIDVFATWRAPVVLCARTTLGTINHTLLSIEALRARAIPLLGIAFIGDENAESERIIVELGRARRLGRLPHLAQLTTDALRAAFARNFNTADFLKETA
Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.
Q130N3
Q3KKZ3
SECA_CHLTA
Protein translocase subunit SecA
Chlamydia
MMDFLKRFFGSSQERILKRFQKLVEEVNACDEKFSSLSDDELRKKTPQLKQRYQDGESLDKLLPEAYGVVKNVCRRLAGTPVEVSGYHQQWDMVPYDVQILGAIAMHKGFITEMQTGEGKTLTAVMPLYLNALTGKPVHLVTVNDYLAQRDCEWVGSVLRWLGLTTGVLVSGSPPEKRKAIYQCDVVYGTASEFGFDYLRDNSIATRKEEQVGRGFYFAIIDEIDSVLIDEARTPLIISGPGEKHNPVYFELKDRVAELVYFQREMCNHIAIEARKVLDPFLGTDVLPKDKKVMEAISEACRALWLVSKGMPLNRVLRRVREHPDLRAMIDKWDVFYHAEQNKEQCLEKLSSLYIVVDEHNNDFELTDKGMLQWIEKIGGAAEDFVMMDMGHEYALIEEDATLSPADKLNRKIAVSEKDTQRKARAHGLRQLLRAHLLMEKDIDYIVRDDQIVIIDEHTGRPQSGRRFSEGLHQAIEAKEHVTIRKESQTFATVTLQNFFRLYEKLAGMTGTAITESREFKEIYSLYVLQVPTFKPCLRIDHNDAFYMTEREKYQAIVAEIISAHRSGKPILIGTESVEVSEKLSRILRQNRINHTVLNAKNHAQEAEIIAGAGKVGAVTVATNMAGRGTDIKLDEEAVAAGGLYVIGTSRHQSRRIDRQLRGRCARLGDPGAAKFFLSFEDRLMRLFASPKLNTLIRHFRPPEGEAMSDPMFDRLIETAQKRVEGRNYTIRKHTLEYDDVMNKQRQTIYAFRNDVLHAEDLFVVAKEQIEHVALALAFLILKDAHADHCSLPKIEEWLSYSFPVKLDDQEIRRLGDVDAVADYIGDLLIEAFDVKFSAMLAEFTEIIGSAANAQGICNDILRSVIISHIDEEWKVHLVDMDLLRSEVGLRSVGQKDPLIEFKNESFLLFEGLIRDIRIAIVKHLFALELSLTRSDRPDNAIPTVATAFHNHDNFRPMELTIVGEEEES
Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
Q3KKZ3
Q5RAN9
CASQ2_PONAB
Calsequestrin, cardiac muscle isoform
Pongo
MKRTHLFIVGVYVLSSCRAEEGLNFPTYDGKDRVVSLSEKNFKQVLKKYDLLCLYYHEPVSSDKVAQKQFQLKEIVLELVAQVLEHKAIGFVMVDAKKEAKLAKKLGFDEEGSLYILKGDRTIEFDGEFAADVLVEFLLDLIEDPVEIISSKLEVQAFERIEDYIKLIGFFKSGDSEYYKAFEEAAEHFQPYIKFFATFDKGVAKKLSLKMNEVDFYEPFMDEPIAIPNKPYTEEELVEFVKEHQRPTLRRLRPEEMFETWEDDLNGIHIVAFAEKSDPDGYEFLEILKQVARDNTDNPDLSILWIDPDDFPLLVAYWEKTFKIDLFRPQIGVVNVTDADSVWMEIPDDDDLPTAEELEDWIEDVLSGKINTEDDDDEDDDDDNSDEEDNDDSDDDDDDE
Calsequestrin is a high-capacity, moderate affinity, calcium-binding protein and thus acts as an internal calcium store in muscle. Calcium ions are bound by clusters of acidic residues at the protein surface, especially at the interface between subunits. Can bind around 60 Ca(2+) ions. Regulates the release of lumenal Ca(2+) via the calcium release channel RYR2; this plays an important role in triggering muscle contraction. Plays a role in excitation-contraction coupling in the heart and in regulating the rate of heart beats.
Q5RAN9
Q12I30
ENGB_SHEDO
Probable GTP-binding protein EngB
Shewanella
MSESIMDFRRAKFLISAPDIAHLNQYLPGDVGVEIAFAGRSNAGKSSALNALTEQKSLARTSKTPGRTQLINVFALDDDRRLVDLPGYGFAQVPLALKNKWQQALGEYLQKRACLSGVVVLMDIRHPLKDLDMQMIEWAVASEIPVLALLTKSDKLAQSAKMKTVNEVRSALADFGDWVKVEPFSSLKGTGKPKVLSILNEWCHPQWLMDAMAQESPED
Necessary for normal cell division and for the maintenance of normal septation.
Q12I30
Q01173
TPM1_XENLA
Tropomyosin-1
Xenopus
MDAIKKKMQMLKLDKENALDRAEQAEADKKGAEDKSKQLEDELVALQKKLKGTEDELDKYSEALKDAQEKLELSDKKATDAEGDVASLNRRIQLVEEELDRAQERLSTALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERAEERAELSESKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERTVAKLEKSIDDLEDELYAQKLKYKAISEELDHALNDMTSI
Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments.
Q01173
Q3K5P2
BIOF_PSEPF
8-amino-7-ketopelargonate synthase
Pseudomonas
MSFDLAARLAARRADNLYRQRPLLESPQGPQVVVDGQPLLAFCNNDYLGLANHPQVIEAWRAGASKWGVGGGASHLVIGHSGPHHELEEALADLTGRPRALLFTTGYMANLGAVTALVGQGDTVLEDRLNHASLLDAGLLSGARFNRYLHNDADSLAKRLEKATGNTLVVTDGVFSMDGDLADLPALARETKAKGAWLMVDDAHGFGPLGANGGGIVEHFGLSQEDVPVLVGTLGKAFGTAGAFVAGSEELIESLIQFARPYIYTTSQPPALACATLKSLELLRSEHWRREHLQTLIRQFRHGAEQIGLELMDSFTPIQPILIGDAGRAVRLSQMLRERGLMVTAIRPPTVPAGSARLRVTLTAAHSEAQVQLLLEGLADCFAQLKSEPSHA
Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide.
Q3K5P2
B2XWR3
RK22_FAGEA
50S ribosomal protein L22, chloroplastic
Fagopyrum
MRKKKKSLTEVSALGQYIPMSVHKARRVIDQIRGRSYKETLMILELMPYRACYPIFKIIYSAAANAKHNKGFEKEDLLVWKAEVNKGPTRKKLKPRARGRSYLIKKPTCHISVVLKDISYYEAYETLYNREKYLPSNFRLKSSGAIWDKK
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.
B2XWR3
C5CD93
RL9_KOSOT
50S ribosomal protein L9
Kosmotoga
MKVILLKDVAKLGKKGEIKEVSDGYGRNYLIPRGLAVEATKSELSKLKNIEDQKKKKEERTKANSEELLRKIKQRHFRMKVKAGASGKLFGAVTSADIAELIAKELGTEFSKRYVDLKENIKNTGEYKVNLKLPGNVKGSIIIAIEKSEED
Binds to the 23S rRNA.
C5CD93
Q004B5
KARG0_PENVA
LvAK
Penaeus
MADAAVIEKLEAGFKKLEAATDCKSLLKKYLTKEVFDKLKDKRTSLGATLLDVIQSGVENLDSGVGIYAPDAEAYTLFAPLFDPIIEDYHVGFKQTDKHPNKDFGDVNSFVNVDPEGKFVISTRVRCGRSLQGYPFNPCLTESQYKEMEAKVSSTLSSLEGELKGTYYPLTGMSKEVQQKLIDDHFLFKEGDRFLQAANACRYWPAGRGIYHNDNKTFLVWVNEEDHLRIISMQMGGDLGQVFRRLTSAVNEIEKRIPFSHHDRLGFLTFCPTNLGTTVRASVHIKLPKLAANREKLEEVAGKYNLQVRGTRGEHTEAEGGIYDISNKRRMGLTEFQAVKEMQDGILELIKIEKEM
Catalyzes the reversible transfer of high energy ATP gamma-phosphate group to L-arginine . Has nucleoside diphosphate kinase-like activity toward dTDP. Binds and phosphorylates dTDP using ATP as a phosphate donor. Does not phosphorylate dADP, dCDP, dGDP, dTMP or thymidine .
Q004B5
Q6UEF2
AFLX_ASPPU
Aflatoxin biosynthesis protein X
Aspergillus
MRRYAILGATGNTGQALLNVLLQSPDNQIHAYCRSASKLNRLRPEISQHRQVKVWEGSLEDVSLLSECIRGTRAVFMVVAIPDNMPHCTIAQDCTNAVLNTLKKLQAEGCQSLPKLIVLSSASLEDSLCADVPPLIHRVLNIAAGNLYSDLAKAEKILRAEKHWVSTTFVKPGGLVHDVQRGHTLSTKTAKTPVSFLDVAAGMVEIADMDDKTYDMMNVSVNAIGDGTAFPWKGVYYVLTGLLFHFFPWTYKYFGDSPMPKPRKDL
Oxidoreductase; part of the gene cluster that mediates the biosynthesis of aflatoxins, a group of polyketide-derived furanocoumarins, and part of the most toxic and carcinogenic compounds among the known mycotoxins . The four major aflatoxins produced by A.parasiticus are aflatoxin B1 (AFB1), aflatoxin B2 (AFB2), aflatoxin G1 (AFG1) and aflatoxin G2 (AFG2) . The first step of the pathway is the conversion of acetate to norsolorinic acid (NOR) and requires the fatty acid synthase subunits aflA and aflB, as well as the PKS aflC . AflC combines a hexanoyl starter unit and 7 malonyl-CoA extender units to synthesize the precursor NOR . The hexanoyl starter unit is provided to the acyl-carrier protein (ACP) domain by the fungal fatty acid synthase aflA/aflB . The second step is the conversion of NOR to averantin (AVN) and requires the norsolorinic acid ketoreductase aflD, which catalyzes the dehydration of norsolorinic acid to form (1'S)-averantin . The norsolorinic acid reductases aflE and aflF may also play a role in the conversion of NOR to AVN . The cytochrome P450 monooxygenase aflG then catalyzes the hydroxylation of AVN to 5'hydroxyaverantin (HAVN) . The next step is performed by the 5'-hydroxyaverantin dehydrogenase aflH that transforms HAVN to 5'-oxoaverantin (OAVN) which is further converted to averufin (AVF) by aflK that plays a dual role in the pathway, as a 5'-oxoaverantin cyclase that mediates conversion of 5'-oxoaverantin, as well as a versicolorin B synthase in a later step in the pathway . The averufin oxidase aflI catalyzes the conversion of AVF to versiconal hemiacetal acetate (VHA) . VHA is then the substrate for the versiconal hemiacetal acetate esterase aflJ to yield versiconal (VAL) . Versicolorin B synthase aflK then converts VAL to versicolorin B (VERB) by closing the bisfuran ring of aflatoxin which is required for DNA-binding, thus giving to aflatoxin its activity as a mutagen . Then, the activity of the versicolorin B desaturase aflL leads to versicolorin A (VERA) . A branch point starts from VERB since it can also be converted to dihydrodemethylsterigmatocystin (DMDHST), probably also by aflL, VERA being a precursor for aflatoxins B1 and G1, and DMDHST for aflatoxins B2 and G2 . Next, the versicolorin reductase aflM and the cytochrome P450 monooxygenase aflN are involved in conversion of VERA to demethylsterigmatocystin (DMST) . AflX and aflY seem also involved in this step, through probable aflX-mediated epoxide ring-opening step following versicolorin A oxidation and aflY-mediated Baeyer-Villiger oxidation required for the formation of the xanthone ring . The methyltransferase aflO then leads to the modification of DMST to sterigmatocystin (ST), and of DMDHST to dihydrosterigmatocystin (DHST) . Both ST and DHST are then substrates of the O-methyltransferase aflP to yield O-methylsterigmatocystin (OMST) and dihydro-O-methylsterigmatocystin (DHOMST), respectively . Finally OMST is converted to aflatoxins B1 and G1, and DHOMST to aflatoxins B2 and G2, via the action of several enzymes including O-methylsterigmatocystin oxidoreductase aflQ, the cytochrome P450 monooxygenase aflU, but also the NADH-dependent flavin oxidoreductase nadA which is specifically required for the synthesis of AFG1 .
Q6UEF2
A7FWQ6
VATB_CLOB1
V-ATPase subunit B
Clostridium
MLKEYRTVKEVVGPLMLVDQVDGVSFDELVEIELHNGEKRRGKVLEINKDKAMVQLFEGSAGINLKGAKVKFLGKPLELGVSEDMLGRVFDGLGNPKDGGPKIIPDKKLDINGIPINPVARNYPDEFIQTGVSAIDGLNTLVRGQKLPVFSGSGLPHAELAAQIARQAKVLNSDSKFAVVFAAIGTTFEEAQYFIDDFTKTGAIDRAVLFINLANDPAIERIATPRMALTAAEYLAFEKGMHVLVIMTDITNYCEALREVSAARKEVPGRRGYPGYLYTDLSTLYERAGRILGKEGSITQIPILTMPEDDKTHPIPDLTGYITEGQIILSRELYKKGIMPPIDVLPSLSRLKDKGIGKGKTREDHADTMNQLFSAYAQGKQAKELSVILGESALSDTDKLYAKFADAFEEEYVSQGFTTNRTIEETLNLGWKLLTILPKSELKRIRDEYLEKYLNKAEESK
Produces ATP from ADP in the presence of a proton gradient across the membrane. The V-type beta chain is a regulatory subunit.
A7FWQ6
A1WHC8
RL2_VEREI
50S ribosomal protein L2
Verminephrobacter
MAVIKMKPTSPGRRAVVKVTREHLHKGQPHAPLLEPQFQKAGRNNNGHITTRHKGGGHKHHYRVVDFKRNKDGIAAKVERIEYDPNRTAHIALVCYADGERRYIIAPRNLEVGATLLSGAEAPIRAGNTLPIRNIPVGSTIHCIELKPGAGAQIARSAGASATLLAREGTYAQVRMRSGEVRKIHIECRATIGEVANEEHSLRQLGKAGVKRWMGIRPTVRGVAMNPVDHPHGGGEGRTGEGRHAVDPWGNLTKGYRTRNNKRTQSMIVSRRKK
One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome.
A1WHC8
Q9HVG4
RSMC_PSEAE
rRNA (guanine-N(2)-)-methyltransferase RsmC
Pseudomonas
MDPRSEVLLRQRHLFATPLLLAGLPADDLLAELPQAQGWSWHAGEQAQLDARFPGRSRFDTRAPTGAWTSAVLFLPKSRELTDYLLASLAARLPGGELFLVGEKRGGIERASKQLAAYGKPRKLDSARHCQLWQVRIEQAPAEPDLHALAQRYSLPLADGELQVVSLPGVFSHGRLDRGSALLLGQLQALPGGHLLDFGCGAGVLGAVLKRRYPASRLSLLDVDAFAVESSRLTLAANGLDGEVIAADGIDGAPRELAAIVSNPPFHQGVHTDYQASERLLQRAAEHLAPGGELRLVANSFLKYPPLIERHLGPCRTLAEGDGFRIYSARRS
Specifically methylates the guanine in position 1207 of 16S rRNA in the 30S particle.
Q9HVG4
Q7Z7H3
CATIP_HUMAN
Ciliogenesis-associated TTC17-interacting protein
Homo
MSSKVYSTGSRAKDHQPSGPECLPLPEANAEAIDFLSSLHKEELQMLFFSETLAMVSDTGEPQGELTIEVQRGKYQEKLGMLTYCLFVHASSRGFLDKMLCGNSLLGYLSEKLELMEQHSQDFIKFLILPMERKMSLLKQDDQLAVTRSIKEGEEVKTGVTSFPWSSIKGFISEAANLVLLRVMAWRRMVPSNARFLTLDTEGKLCYLTYQNLGFQTIQVDHQQAEVFIVEQTVHAEEGIPMSCQYYLLSDGHLAKRIQVGSPGCCIITKMPILREEDEIEPRPVFEKKPLVWEEDMELYSKFLDRKEELRLGHASYLRQHPEAHALISDFLLFLLLRQPEDVVTFAAEFFGPFDPWRPSSPALGSSHRPNPFRSLEPEGDARSGAA
Plays a role in primary ciliogenesis by modulating actin polymerization.
Q7Z7H3
C5BC01
SELA_EDWI9
Selenocysteinyl-tRNA(Sec) synthase
Edwardsiella
MSSDSQVLYSQIPAIDTLLRTPACAALQAQYGSQLVTQALRSLQQQARHAIQRQQALPDWCVDWGVACTRRLAETLQPAMRRVFNLTGTVLHTNLGRALLPDTAIAAAAGAMGAPVTLEYDLDDAGRGHRDRAIADRLCALTGAEDACIVNNNAAAVLLMLATLAPGRDVIVSRGELVEIGGAFRIPDVMTQAGCRLREVGTTNRTHLHDYRQAIGEHSALLMKVHTSNYAIAGFTAAVSEAELAALGQEYGLPVISDLGSGSLLDMAHYGLPAEPMPQRMLADGVDLVSFSGDKLLGGPQAGIIVGRRELIHRLQRHPLKRALRCGKMTLAALDATLQLYQQPEKLRQALPTLRHLTREASEIAACGERLLARLRPHYEEAFVLTLEPCLSQIGSGSLPVDRLPSHAITLTPRDGRGGTLTALADRWRALPCPVIGRLQEGKLWLDLRCLDDEQALLQELCQ
Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis.
C5BC01
C5D3R9
RL23_GEOSW
50S ribosomal protein L23
unclassified Geobacillus
MKDPRDIIKRPIITENTMNLTAQKKYTFEVDVKANKTEVKEAVEKIFGVKVEKVNIMNYKGKFKRVGRYSGYTNRRRKAIVTLTPDSKDIELFEV
One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome.
C5D3R9
A5CSN9
PNP_CLAM3
Polynucleotide phosphorylase
Clavibacter
MEGPEIKFAEAVLDNGKYGTRTVRFEAGRLAQQAQGAVAAYLDEDTMLLSATSVGKHPKDNFDFFPLTIDVEERSYAAGKIPGSFFRREGRPSTEAILVCRLIDRPLRPSFITGLRNEVQVVITVLSIAPDEFYDSLAINAASASSMLSGIPFSGPIAGVRLALIGDQWVVFPKHSQLKEAVFDITVAGRVVTDSEGNEDVAIMMVEAEATEGAWDLIQGGATKPDEAIVAQGLEAAKPFIQQLVAAQASLAQQAAKPTVDYPVFLPYAQETYDAVSALALDELGTVYQTADKIERQDADDALKTRTKEAVAAKVEAGELPQSALTEFSAAYKSVTKTVVRGRILRDGVRMDGRGLADIRPLDAEVQVIPRVHGSAIFQRGETQILGVTTLNMLKMEQQIDSLSPITKKRYLHHYNFPPYSTGETGRVGSPKRREIGHGFLAERALVPVLPSREDFPYAIRQVSEALGSNGSTSMGSVCASTLSLLNAGVPLRAPVAGIAMGLVSDTVDGQVRYAALTDILGAEDALGDMDFKVAGTSEFVTAIQLDTKLDGIPTSVLDGALKQAKEARTAILGVLNQAIDGPDEMAPTAPRVISVNIPVDKIGELIGPKGKTINAIQDETGADISIEEDGTVYIGAVDGPSADAARAQVNAIANPTNPEVGESFLGTVVKIATFGAFVSLLPGKDGLLHISEVRKLAGGKRVENVEDVLGVGQKILVEITKIDDRGKLSLAPVLEETADQEGRDAASHGSEAPAEG
Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
A5CSN9
Q4USF8
ERA_XANC8
GTPase Era
Xanthomonas
MSETSPHRSGSVAVIGRPNVGKSTLTNALVGAKVSIVSNRPQTTRHRLLGIATFPEGQLMLVDTPGLHREQKRAMNRVMNRAARGSLEGVDAAVLVIEAGRWDEEDTLAFRVLSDADVPVVLVVNKVDRLKDKTALFPFLAQVSEGRTFAAVHPVSALKRKGLEALVSDLLKLVPEAEAMYGEDEITDRSQRFLAGELVREQLMRQLGEELPYATTVEIERFAEDGALLRIGAVIWVEREGQKAIVIGKGGTRLKDIGGKARLQMERLFGAKVFLETWVRVREGWSDDEAALKAFGYD
An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism.
Q4USF8
B0KGD8
TUSA_PSEPG
Sulfur carrier protein TusA
Pseudomonas
MTDFTPDAVLDATGLNCPEPVMMLHQHVRNLAAGGLLKVIATDPSTRRDIPKFCNFLGHELLQQQEDAGTFLYWIRKKAD
Sulfur carrier protein which probably makes part of a sulfur-relay system.
B0KGD8
Q7M9A7
MDH_WOLSU
Malate dehydrogenase
Wolinella
MGIIGAGHVGSTVAFILATQGICQEIIIKDLNLDTARGIALDMGHAASATKTHTIVRVANEPSDLRGCDVVVFCAGSPRQPGMSRDDLLLANAKVIRTVLSEVKPYIQESVLVMVSNPLDAMVYTAIKESGLSPLQVLGMAGILDSARMASFIFEKLGYGSDQIVASVMGGHGDDMVPLPRYSNVAGVPITELLEPQEIEEIIHRTRNAGAEIVGYLKKGSAYFAPAKSTAIMVEAILKNSHQVFPCSVLLQGEYGYSDVVGGVPVKLGSRGVCEIIELELLHEERERFDQSIQSVKSLIDALYHHAFFVSSRP
Catalyzes the reversible oxidation of malate to oxaloacetate.
Q7M9A7
Q9FYK2
CML25_ARATH
Calmodulin-like protein 25
Arabidopsis
MFNKNQGSNGGSSSNVGIGADSPYLQKARSGKTEIRELEAVFKKFDVNGDGKISSKELGAIMTSLGHEVPEEELEKAITEIDRKGDGYINFEEFVELNTKGMDQNDVLENLKDAFSVYDIDGNGSISAEELHEVLRSLGDECSIAECRKMIGGVDKDGDGTIDFEEFKIMMTMGSRRDNVMGGGPR
Potential calcium sensor.
Q9FYK2
A5V3X2
ATPD_RHIWR
F-type ATPase subunit delta
Rhizorhabdus
MENSGGIQASLSGRYATALFGLARDEKAIDAVSASLQSLKAALTESDDFRRLTTSPLVSRDEAMKAVAATAASLGIDPLTTKFLGVLAQNRRLGQLGAVIRSFGTLSARHRGETTAEVTSAHPLTATQVKALKAKLKTQLDRDVAVDLTVDPSILGGLIVKIGSRQIDGSIRSKLNSLAIAMKG
This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction.
A5V3X2
P92480
ATP6_EQUAS
F-ATPase protein 6
Equus
MNENLFASFATPTMMGLPIVILIIMFPSILFPSSNRLINNRLISIQQWLVQLTSKQMMTIHNNKGQTWTLMLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVFMGFRHKTKAALAHFLPQGTPIFLIPMLVIIETISLFIQPMALAVRLTANITAGHLLIHLIGGATLALMDISPSTALITFIILILLTILEFAVAMIQAYVFTLLVSLYLHDNT
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
P92480
Q3AMJ0
PANCY_SYNSC
Cytidine monophosphate kinase
unclassified Synechococcus
MPTMGGLHQGHGELIRRASEQGPVLVSVFVNPLQFGPAEDFDRYPRTLEADRGLAECCGAHALWAPSVDAIYPSGLPSAVSRSAPAGLQTHLCGASRPGHFDGVVTVVARLLQLVEPSCLWLGEKDWQQLVILRRLVVDLDLGVVVKGVPTVRESDGLALSSRNQYLFPADRARAAALPAALRHADPSDPESSVRQSLAKAGLEVEYVERVDPRTLQPCGPETAISLLAAAVRCGTTRLIDHVFLMTRQPLVAIDGPAGAGKSTVTRAFAERMGLVYLDTGAMYRSVTWLVQQNGVDHQDAVSIAPLLNDLDLQLKSLPGGGQQVLVNGQDVSDAIRSPEVTASVSAVAAHRCVRQALTAQQKAMGAKGGLVAEGRDIGTAVFPDADLKVFLTATVGERARRRALDLEQRGFPVPERSELEAQIAERDHLDSTREEAPLVQADDALELVTDGMSIEAVIDALVGQFRSRVGEEAWPTPAG
Catalyzes the transfer of a phosphate group from ATP to either CMP or dCMP to form CDP or dCDP and ADP, respectively.
Q3AMJ0
Q2JFV4
NB_FRACC
Ferric nitrobindin
Frankia
MSAGKRSAAGSARSDTATSTVDLHASLLPLAFLVGTWRGEGVGGYEGLDGFHYGQEITFAADGRPALGYVSHTWWADEPRDGREPGSPLATETGFWRVQPGEDGKPVVEVMLAHPFGIAEIYVGTVTGTRIDLDHNVLIRTATARDVTRSVRLYGLVEGCDLAYAIDMEAEGKPMQSHLSARLHRVSD
Heme-binding protein able to scavenge peroxynitrite and to protect free L-tyrosine against peroxynitrite-mediated nitration, by acting as a peroxynitrite isomerase that converts peroxynitrite to nitrate. Therefore, this protein likely plays a role in peroxynitrite sensing and in the detoxification of reactive nitrogen and oxygen species (RNS and ROS, respectively). Is able to bind nitric oxide (NO) in vitro, but may act as a sensor of peroxynitrite levels in vivo.
Q2JFV4
B1LLF1
END8_ECOSM
Endonuclease VIII
Escherichia
MPEGPEIRRAADNLEAAIKGKPLTDVWFAFPQLKSYQSRLIGQHVTHVETRGKALLTHFSNDLTLYSHNQLYGVWRVVETGEEPQTTRVLRVKLQTADKTILLYSASDIEMLTPEQLTTHPFLQRVGPDVLDPKLTPEVAKERLLSPRFRNRQFAGLLLDQAFLAGLGNYLRVEILWQVGLTGNHKAKDLNAAQLDALAHALLDIPRLSYATRGQVDENKYHGALFRFKVFHRDGEPCERCGGIIEKTTLSSRPFYWCPGCQH
Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized pyrimidines, such as thymine glycol, 5,6-dihydrouracil and 5,6-dihydrothymine. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.
B1LLF1
Q8EBI5
LSPA_SHEON
Signal peptidase II
Shewanella
MPLTWKDSGLRWYWVVVLVFLADQLSKQWVLANFDLFESVQLLPFFNFTYVRNYGAAFSFLSEAGGWQRWLFTIVAVGFSSLLTVWLRKQSASLLKLNLAYTLVIGGALGNLVDRLMHGFVVDFIDFYWGKSHYPAFNIADSAIFIGAVLIIWDSFFNSQSEQDKTEEVK
This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Q8EBI5
B2UL92
SYP_AKKM8
Prolyl-tRNA synthetase
Akkermansia
MSQQTAITPTRAQDFPEWYQQVIKAADMAENSEVRGCMVIKPWGYAIWELIQKDLDQRFKDTGHTNAYFPLLIPISYLEKEAEHAEGFATECAVVTHHRLEAQKDEATGKTRMIPTGELTEPFVIRPTSETVIGAAFARWTSSYRDLPLKVNQWCNVMRWEMRPRIFLRTAEFLWQEGHTAHETREEAIEETLTMHKVYEEFQRDVLAIPTIPGEKTEAERFPGAEQTYTVEAMVQDRKAIQAGTSHFLGQNFSKSQNICFAGRDNTQQFAWTSSWGVSTRMIGALIMMHSDDDGLVCPPRVAPQQIVIIPVTPKEESRQAVLDHCEELARTLRAKTFHGQPLRVLVDRRDLGGGAKKWEWVKKGVPVRLEIGPRDLEKGSVCLQRRDRPANEKSFVPETELIDTAADILQSIQDTLLQRAIAFRDSHIRPASTLRELEENFSGEGDADWLQVPWDGSPEEEEELAKRLRISIRCIPLGELGRGEPAPCILTGRMTKRRVLWARSY
Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro).
B2UL92
P41443
GSPH_ECOLI
Putative general secretion pathway protein H
Escherichia
MNQQRGFTLLEMMLVLALVAITASVVLFTYGREDVASTRARETAARFTAALELAIDRATLSGQPVGIHFSDSAWRIMVPGKTPSAWRWVPLQEDAADESQNDWDEELSIHLQPFKPDDSNQPQVVILADGQITPFSLLMANAGTGEPLLTLVCSGSWPLDQTLARDTRP
Component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm. Part of the pseudopilus tip complex that is critical for the recognition and binding of secretion substrates.
P41443
Q2XXR4
CRVP1_VARAC
Cysteine-rich secretory protein VAR1
Varanus
MILLKLYLTLAAILCQSRGTTSLDLDDLMTTNPEIQNEIINKHNDLRRTVDPPAKNMLKMSWDNIIAESAKRAALRCNQNEHTPVSGRTIGGCGCAEKIT
Blocks ryanodine receptors, and potassium channels.
Q2XXR4
Q2S158
SYDND_SALRD
Non-discriminating aspartyl-tRNA synthetase
Salinibacter
MERSSRADLISEDSHPARTHTCGDLRAEDNGEAVVLKGWVDTRRDHGGLVFVDLRDRYGLTQVVFSPQDNQTAYEVAGQLRREDVISVQGTVRPRGEEAVNPDLPTGAIEVSADDLAVLNTSETPPFVVSAHEERQMNTNEDLRLAHRYLDLRRPDLQENIELRHRLYQTTHRYFDAHDFLEVETPVLMKSTPEGARDFLVPSRLHPGRFYALPQSPQTYKQLLMVGGLDRYVQIVKCFRDEDLRADRQPEFTQIDVEMTFATEEQVYELTEGLMADLWDTLEDTTLETPFPRMTYDEALRTYGTDKPDLRFDLELHDVSDCFAGSGFRVFDSIVDDGGHIVALRVPGEGDRGRAAMDRLEDHVTDEIGAAGLIYFQLPSDGSGIEQNLSSDALPHEYGRAAAEQVGAEAGDLVLTLAGHSPTVFEQAGALRLHMGEELGLRPPADEGDDAFLWVTDFPLMEYDEEAGRPVSMHHPFTAPHPDDLDRLDEDPTQVQARAYDLVLNGNEIGGGSIRIHNHETQMQVFDVLGIDEEEAQDRFGFLLDALRYGAPPHGGIALGLDRLVMLLAGADSLRDVIAFPKTQSGKEPMVKSPDWVDPEQLETLALRLDLPPDVEPPARIAQRKRLAS
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Q2S158
P41697
BUD6_YEAST
Actin-interacting protein 3
Saccharomyces
MKMAVDDPTYGTPKIKRTASSSSSIETTVTKLLMSTKHLLQVLTQWSKGTTSGRLVSDAYVQLGNDFKVVSKFFMHAKVDMSDVGDVPMALRRVLEVTLREPPSDETLNKHLPKIREIIVTLLDKLKVKQAILKNMQQEHRISVKSHHQQNPSFTSNLSLGSEGTREGTPLSSRKSSIVRDQRQSDSVENSYGEKVNSTSTGTPSAQSAEATLTKPRTNIKQNLKSNNAPNASDDDDALSQLKKGTNLQRRASKRYSAYHMAKLTNQSTTEAAAAAGLMTTPSPSMLHLEETVRKSKLYGNNNNDDDRNINSAENKGKSIDDVSKASPLAKTPLPIENVRASPRRLSSVVTTSPDKAMNGTCPVFLRIGDKTKKCHVQLPTTKNALRLLFIERFAYSPGANSFPDIYIMDPQYGVFYELEELNLLDIKEGFVIELKLEENPNNTIKEFIDTVKMEISNSQNDIIRHLKEMSFGSAISGKQTEVLPQPGLEANKHDLVGQNKKDDDKTIKDIQYELGKIKQVHNINRSNINETIFNILRKVDNFKSLSFSAKNSSNRMYMEKSQTELGDLSDTLLSKVDDLQDVIEIMRKDVAERRSQPAKKKLETVSKDLENAQADVLKLQEFIDTEKPHWKKTWEAELDKVCEEQQFLTLQEELILDLKEDLGKALETFDLIKLCCEEQEKNPSRSKSNPILPIMRPGTFNQVREQVMVAVQSLNPDHDSRVEAIDKAEKMWEMERKLKASNEFDDELENFVGNSNLKKSGGFEEVERIRKQKDEANLRAYFGPGFT
Not essential for mitotic growth but is necessary for normal morphogenesis. Involved in the organization and/or function of the actin cytoskeleton.
P41697
B7LK52
MDTL_ESCF3
Multidrug resistance protein MdtL
Escherichia
MSRFLICSFALVLLYPAGIDMYLVGLPRIAADLNASEAQLHIAFSVYLAGMAAAMLFAGKVADRSGRKPVAIPGAALFIIASVFCSLAETSTLFLAGRFLQGLGAGCCYVVAFAILRDTLDDRRRAKVLSLLNGITCIIPVLAPVLGHLIMLKFPWQSLFWAMATMGIAVLMLSLFILKETRPAAPAASDKPRENRESLLNRFFLSRVVITTLSVSVILTFVNTSPVLLMEIMGFERGEYATIMALTAGVSMTVSFSTPFALGIFKPRTLMITSQVLFLAAGITLAVSPSHAISLFGITLICAGFSIGFGVAMSQALGPFSLRAGVASSTLGIAQVCGSSLWIWLAAVVGIGAWNMLIGILIACSIVSLLLIMFVTPGRPVAAHEEIHHHA
Confers resistance to chloramphenicol.
B7LK52
Q2ITQ2
PURL_RHOP2
Phosphoribosylformylglycinamidine synthase subunit II
Rhodopseudomonas
MSAPEPKITPELIASHGLKPDEYQRILDLIGREPTFTELGIFSAMWNEHCSYKSSRIHLKGLPTKAPWVLQGPGENAGVIDIGDNQAVVFKMESHNHPSYIEPYQGATTGVGGILRDVFTMGARPIACLNALSFGDPSHPKTRHLVSGVVAGVGGYGNSFGVPTVGGQTRFHTRYDGNILVNAMAVGLADSDKIFLAAASGVGMPIVYLGSKTGRDGMGGATMASAEFDEGSEEKRPTVQVGDPFAEKLLLEACLEIMAKDCVIAIQDMGAAGLTCSAVEMGAKGDLGVDLDLDAVPTRETGMTAYEMMLSESQERMLMVLKPEKEKEAEEIFRKWGLDFAIVGYTTPTKRFVVKHGGAVKADLPIKELGDEAPLYDRPHVPSPKLPVIHAREVNAPMPVPEALEKLLATPDLCSKRWVWEQYDHVIGGNTLQRPGGDAAVVRVEDGPKGLALTVDVTPRYCEADPYEGGKQAVAEAYRNITAVGGKPLAITDNLNFGNPERPEIMGQLVGCLKGISEACIALDSPIVSGNVSLYNETSGRGILPTPSIGGVGLLDDFTKSATLAFKAEGEAILLIGETHGWLGQSVYLRDVCGREEGAPPPVDLACEKRHGDVVRGMIHAGTATAVHDLSDGGLLVALAEMAISGNIGASLDAPPDSTVAHAWWFGEDQGRYLVTVKEDDLLTVLSKLKSVGVPCTQIGTTGGHTLKIDGERAIDVKALRHAHEHWLPDYMAGKN
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.
Q2ITQ2
Q6MTU8
UVRC_MYCMS
Excinuclease ABC subunit C
Mycoplasma
MSLKQQVDLLPNKPGCYLFFNKDNDVIYVGKAKNLKKRVSTYFNKAYNIKTTRLVREITDLKYFIVDNEKESLLLEKNLIKKYHPKYNVLLNDDKTYPYIIITNQKDPMYKYVRKYDKKALKNYGPLPIGSNARSILLTLQRLFPLRMCQGNLNKPCLYYHLNQCSGACFKQVDPSYYEYQIKQVDKFFKGEINQVKQTLVKQMQKASDNLQFEQAQRIKDQITSLDFITAKQNVDIVTNKNIDVVNYEINQDKICFVILFYRLGQLTYKDEYIQNYEGQNLSELFNSYLQQIYQKNIYPDVLLIPNEIELLDLDQNLLEFSSYSLNKQDDVFIKLAKQNAIDSLNKSVISHNVNSGDEIEILEQLKQISNASKYLKRIEVFDISNIYSQFITGACIVYINAKPIRNEFRKYNIDPSYTSDFSRMKFMLEKRFLKQIKEKEQLPDLVIVDGGIIQIHAAKEVLNKLNLKIDVIGLSKDDHHKTRYLIDIFEQTIDIKNFKKLYNFLTSLQIRVDEYAKSGFRKKYHNQLNDQILLIKGVGKKTNLKLYKHFKTIDNIKNASFDELNKVINNKKITNLIISNLNK
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.
Q6MTU8
Q7U522
YIDC_PARMW
Membrane protein YidC
Parasynechococcus marenigrum
MIGYISDNLLIPILDFFYGLVPSYGLAIVALTIVIRVALYPLSAGSIRSARRMRIAQPVIQKRQAEIKSRYANNLQKQQEELGKVMKEFGSPLAGCLPLLVQMPILFALFATLRGSPFADVPYTINLKVLPADQIAAVEPKPFNSASHSIFIAETDHVPVIASLPRGTKLGVGDSATVNLHTKDGRGFDDVLTAVDNPSRFAPTWSITKGDDVVNVSDDGTITALTAGDATVEAKIPGLAARSGFLFIKALGQVGFYADGDINWDIAILVGGFGLTLFLSQLLSGMGMPANPQQATANKITPVMITGMFLFFPLPAGVLLYMVIANIFQALQTFLLTREALPENLQKILDQQMTQQTVPVTATSAGGGDARLPFEPKGGK
Probably also aids protein insertion, folding and/or assembly of membrane complexes destined for the thylakoid.
Q7U522
B4U7U4
FTSH_HYDS0
ATP-dependent zinc metalloprotease FtsH
unclassified Hydrogenobaculum
MQTAKNILIWFLIIGFMIVAFNLFEEKGSSSPSATPMSLTTLVDMVKQNKIGEADIKGDKIIAYTKDGQKVETYIPKGYTSIIDEMIKDGVKVKASPSSGGDISSSGNWLVSMLISWFPVLLFAGIWILMMRQMGNGGPTRAFSFGKSKAKVYIEEKPNVKLDNVAGMDEVKEEVAEVIEYLKDPARFRKLGGRPPKGILFYGEPGVGKTLLAKALAGEAHVPFISVSGSDFVEMFVGVGAARMRDTFETARKNAPCIVFIDEIDAVGRSRGAINLGGNDEREQTLNQLLVEMDGFDTSEGILIIAATNRPDILDPALLRPGRFDRQIFIPKPDVKGRYEILKVHAKNKPLAKDVDLELIARATPGFTGADLENILNEAALLAARKRKDLIHMEDLEEAIDRVMMGLERRGMAISPKEKEKIAVHEAGHALMGLMMPDADPLHKVSIIPRGMALGVTTQLPIDDKHIYDKADLLSRIHILMGGRCAEEVFYGKDGITTGAENDLQRATDLAYRIVATWGMSENVGPISVRRNINPFLGGSTVTEGSPDLLKEIDKEVQKLLASAYEETKRVIAENKEALSSVVKRLIEKETIDCKEFVEILSLHGVEVKNACKQEESLEKKENNVEPKIDKNVVNV
Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
B4U7U4
Q03342
ACT3_ECHGR
Actin-3
Echinococcus granulosus group
LKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNCPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTVEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFRCPEALYQPSFLGMEAVGIHETTFNSIMKCDVDIRKDLYANTVLSGGSTMYPGIADRMQKEITALAPSTMKIKIVAPPDGKYSVWIGGSILASLSTFHEMWISKQEYDESGPSIVHRKCF
Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Q03342
Q9ZLY1
MRAY_HELPJ
UDP-MurNAc-pentapeptide phosphotransferase
Helicobacter
MLYSLLYGYFNINLFQYLTFRAGLGFFIAFFLTLFLMPKFILWAKAKKANQPISSFVPSHQNKKDTPTMGGIVFVFATIVASVLCASLSNLYVLLGIIVLVGFSFVGFRDDYTKINQQNNAGMSAKMKFGMLFILSLIVSVLLSLKGLDTFLYAPFLKNPLFEMPTMLAVGFWVLVFLSTSNAVNLTDGLDGLASVPSIFTLLSLSIFVYVAGNAEFSKYLLYPKVIDVGELFVISLALVGSLFGFLWYNCNPASVFMGDSGSLAIGGFIAYNAIVSHNEILLVLMGSIFVIETLSVILQVGSYKTRKKRLFLMAPIHHHFEQKGWAENKVIVRFWIISMLSNLVALLSLKVC
Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
Q9ZLY1
Q5ADX2
HIR3_CANAL
Histone transcription regulator 3 homolog
Candida
MSSFIPLNFLEDTVSKKDLEEEHTRELQVEQAYKLFQSALKLQKQKQYESAYKVYEELFKLDIVSNHYFEELDFIRGLQDGSQNTDTDELTLLSPNVKSLRYLIFRNRGFLYLDMLKSNTENKSAEKVKEMFYPLLDDFCIALLYNEPDEKLLETLHEIFSYIGSERLSRFVLEYSLTSRKESDDLSGLLPIDQTVLSQYKTMLEHLSSGKFPKLDLKHLSFLEPIRLDIFAQQEKLASKKVAVIKSTSTKWVDLLDAINIHLKENQDESKIEDANRPRIRIFEPYVLTEEPLDIVRIEFTKRGVAVPATETEVTKAQPEQIVQERKPEEDNRVQRSSKRLSKVEDEIPAVTLESSHFLNMDYFRNQMNETIPNFEIFDVCSTYVEDGSGAQYIKDFKNIVSDWNDSYARAILSYDTAKSEDDNLKLLDLLSGYGKSEELKEKNIPPLGEIDIEFPELNYVEFKTYIIKHLLSKILTTKWSDKLYEKFTEWIVQFEGYIINDIDVESAIGVLEVLVDISTSLESQIKDSINNKLNKAVVNSMCQDLLRIKDKIIRWINYIETFPINDLQVASRFKWCQIIKEKAETKSWTENHPVKHKLQKLLGDAHFKINYPNYKNFIDFSKDSINSQLTIISVLAIFWRILSTSSTEDNKEAIRLLEDILLDSNTEPSDAILSIRNFLKQGSIDMKLSLWNILLSFYQSSNSGDKLTVGFEECVLFLNDYLVNEYVLLDEESRLVTLSRILGFYGSSISFVVTSLASTNWILMHPIKVQTLRLFFELSLLFEINEEASYISSLATSIKSKSTKSYHHLTNTLIKTIILILASIQKSNPQILHSVIRLFHTQLGLIGICGHAGGSFLEIAQEYLKSLPNSDQDICQIIKCKYHYSISIDGVVPADHGTARLDELNKNDCKELASFVLPLCFSKGGSTLNNVPKHDIKLLIDEIYDVIGDPDFDSNEALGRNKATLNYFLDNTRLTKRLFQEAFHGLVRLELGEAEEDKQFNGLYYIEGLLLFSSYKLRKKNMQSRAVELESAISLFENDIICGSNRFESWFLLGQSYGYLVEDDLIWTADKLTASDRKITTANLQRKSLICYLMAINKSLDESIKDVIKPVVGNLMSLFAKEMFSAVCEPMSMHAFKVQSHPRFINRVNGALFEPVSQFPAVDKTVCLKIIQQSLQLSIKSSCREWSDYYYLAKVQRKLDKPAGLVMETMASACRSAFKNKHADNIIEPHYNLVSFALKYVKSNRLDSKDALKYLIEDPLIKLEVGEETDFIKLIIKALNKIDSSDKKNWQHKAKYRLARLMQEEYHDVKGAIDQMSSFISLKTPNKALVSIWKPEPERPGKHFLYTFQYIHFYIELLKEIDDLDSLVAMLPKLRRSNSVMINLSIAWEILCSSVCKIIRESYGIGDNFEFTENLINTLPYQTFAANVKLLPDMMRRQSVPENLKSVLCFLFTVNDIKKLNNGYGPTSFIDDTLVTLYFMIYLNYFEKSSTEVTTDSPGLKKKIAKRDIFPLTNDILKAFKKDIEDVTKQKSYNELITAQKLKQGLNEDKSLENVPASANVNEIIVIDDDDDDNLSQEPATKKSKTESNS
Has a role in a nucleosome assembly pathway that is required for the integrity of heterochromatin and proper chromosome segregation.
Q5ADX2
Q6DJ00
OSTCN_XENTR
Gamma-carboxyglutamic acid-containing protein
Silurana
MKLAIVLLLLGLAVLCLGGKDSQHSASAGDSRSSEAFISRQDSANFARRHKRSYRYNVARGAAVTSPLESQREVCELNPDCDELADHIGFQEAYRRFYGPV
Binds strongly to apatite and calcium.
Q6DJ00
Q2MF16
DOIS_STRSD
2-deoxy-scyllo-inosose synthase
Streptoalloteichus
MQTTTITMGDVQYPYRLGTGCVDGIVTRLGELEASHYLVLCDATVAELYGHDLAARLRRSAGPASVLTHPAGEEHKGLGTLDTLADAALHAGVDRRGVVVALGGGVTGNIAGLLAALLFRGIRLVHVPTTVVAMLDSVLSLKQAVNAQVGKNLVGTFYPPVEVLADTAMLGTLPVREIRSGLCEVVKNALAIRPSMIDFLAAELRPDGRYADDVLRWMIDESVAAKAQVTEHDKYERREGLVLEYGHTVGHALEHASHGAVSHGAGVGVGMVAAAEVARRLGHVDADLVELHRELVGKVGVATTLPADVPTEEITYRLGFDNKRGYQPLPADHYAMVLLADVGQPLYQDGLPLTPAPRALVDEVVRELADAPSRIGASVGSAGGAS
Catalyzes the intramolecular carbocycle formation from D-glucose-6-phosphate to 2-deoxy-scyllo-inosose (DOI).
Q2MF16
A8G6V2
ATPD_PROM2
F-type ATPase subunit delta
Prochlorococcus
MPLLNSVTTPYAEALLQVVNENLQTEEMVSEVKQLLELINDSPELEKALSSPILETDAKKKIIIEIFSNKVNSSLMNFLKLLADRQRIGILTSILERFLEIYRENSNIALATVTSAVELTDEQKGLITQKIINIAGTEKLELVTKIDPSLIGGFVASVGSKVIDASLASQIRKLGLSLSK
This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction.
A8G6V2
B0S1J2
QUEA_FINM2
Queuosine biosynthesis protein QueA
Finegoldia
MNTDDFDYELDEKFIAQTPLDKRDESKLMVMDRFNGNTEIKKFYNIIDYLNPGDVLVCNNTRVIPARLFGHRPEKEEKIEVLLLQQTEDKWECLVKPGKKMKLNQVIEFSDSVSAKVVDITEDGSRILKFEYEGIFEERLDELGNMPLPPYIKEKLNDKERYQTVYSKHNGSAAAPTAGLHFTNELLEKIKDKGIYVVFLTLHVGLGTFRPVKVDDVKDHHMHSEYYTISQETVDIINRQKSKGHNIIAVGTTSVRTLETVTHNNNSKLVAESGWTDIFIYPGFEFNIVDSLITNFHLPKSTLMMLVSAFSKKEYIFDAYEKAKQNDFRFFSFGDAMFINGGRNV
Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
B0S1J2
F1LVW7
DIAP3_RAT
mDIA2
Rattus
MEKHRARALGRDSKASRRKGLPSAPPAGPYELGEKRPKLHLNIRTLTDDMLDKFASIRIPKGSKKERPPLPQLKTVSGSSDYSSVSSETMENNPKSLSENEVLKLFEKMMEDMNLNEDKKAPLREKDFSIKKEMVMQYINTASKTGSLRSSRQISPQEFIHELKMGYTGERLFTYLESLRVSLTSNPVSWVQNFGHEGLGLLLDILEKLINGQIQEKVVKKTQHKVIQCLRALMNTQYGLERIMSDERSLSLLAKAMDPKQPSMMADVVKLLSAVCIVGEESILEEVLEALTSAGEERKIDRFFSIVEGLRHNSVQLQVACMQLINALVTSPDDLDFRLHLRNEFMRCGLKEILPNLKGIKNDGLDIQLKVFDEHKEEDLSEFSHRFEDIRAEFDEASDVYSVVWDTVKETRAEGHFVSILQHLLLIRNDRFIRQQYFKLIDECVSQIVLHRDGIDPDFTYRKRLDLDLSQFVDVCIDQAKLEEWEEKASEHCKKFEKECTDHQETQAQLQKKEAKINELQAELQAFKSQFGALPPGTKIPLQTSAKGEPGPSAFPPAPPALGAGVPPPPPPPPPPPPPLPGMAMPFGGPVPPPPPLGFLGGQNFIPLNLPFGLKPKKEFKPEISMRRLNWLKIGPNEMSENCFWIKVNENKYENKDLLCKLENTFCCLEKEKRDTNDFDEKKVIKKRMKELKFLDPKIAQNLSIFLSSFRVPYEKIRTMILEVDEAQLSESMIQNLMKHLPDEEQLKSLSQFRSDYNSLCEPEQFAVVMSNVKRLRPRLTAILFKLQFEEQVNNINPDIMAVSTACEEIKKSKSFSKLLELVLLMGNYMNAGSRNAQTFGFDLSSLCKLKDTKSADQKTTLLHFLVDVCEEKHPDILPFVDDLAHLDKASRVSVEMLEKSLKQMGRQLLQLEKNLETFPPPEDLHDKFVIKMSSFIITAKEHYGKLSTLLDNMTQLYQSVMSYYAVDTKKVSVEEFFNDLNNFRTSFMQALKENIRKREAAEKEKRARIAKERAEKERLERQQEKKRLLEMKTEGDETGVMDSLLEALQSGAAFRDRRKRTPKLKDIRQSLSPMSQRPVLKVCNHENQKMQLSEGSRPHHSINCTSTRTPVAKELNCNLDTHTSTGRIKAVEKEACNAESNRKKEMELLGSVSKSESVPEVEALLARLRAL
Actin nucleation and elongation factor required for the assembly of F-actin structures, such as actin cables and stress fibers. Required for cytokinesis, stress fiber formation and transcriptional activation of the serum response factor. Binds to GTP-bound form of Rho and to profilin: acts in a Rho-dependent manner to recruit profilin to the membrane, where it promotes actin polymerization. DFR proteins couple Rho and Src tyrosine kinase during signaling and the regulation of actin dynamics. Also acts as an actin nucleation and elongation factor in the nucleus by promoting nuclear actin polymerization inside the nucleus to drive serum-dependent SRF-MRTFA activity.
F1LVW7
B3QYB6
QUEF_CHLT3
PreQ(0) reductase
Chloroherpeton
MKPELLETFENQYPNRDYTIEIVNPEFTSVCPKTGLPDFGTITLQYIPNKLCVELKSLKYYYLEFRNAGIFYENVTNKILDDLVKAVKPKEMKIISEWKARGGITTTVTASYEAEK
Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1).
B3QYB6
A6WY74
RUVC_BRUA4
Holliday junction resolvase RuvC
Brucella
MKETIRIIGIDPGLRRTGWGIVESLGNSLHFIGSGTVTSNAEMDLASRLCQLHEGLSKVLHEYMPHEAAVEHTFVNKDATATLKLGQARGIALLAPAQAGLPVAEYAPNAVKKAVIGVGHGEKQQIHMMVKVLMPRASFDTSDAADALAIAICHAHHRQSIASARRLQQLIA
Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group.
A6WY74
Q8DHJ2
PSBZ_THEVB
Photosystem II reaction center protein Z
Thermosynechococcus
MTILFQLALAALVILSFVMVIGVPVAYASPQDWDRSKQLIFLGSGLWIALVLVVGVLNFFVV
Controls the interaction of photosystem II (PSII) cores with the light-harvesting antenna. May also aid in binding of PsbK, Ycf12 and the oxygen-evolving complex to PSII, at least in vitro. PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation.
Q8DHJ2
P58779
SCX5_CENSC
Alpha-like toxin CsEv5
Centruroides
KDGYPVDSKGCKLSCVANNYCDNQCKMKKASGGHCYAMSCYCEGLPENAKVSDSATNIC
Binds voltage-independently sodium channels (Nav) and inhibits the inactivation of the activated channels, thereby blocking neuronal transmission. Is highly toxic to insects and barely toxic to mammals. As it does not compete with the classical alpha-toxin AaH2, this toxin is considered as an alpha-like toxin.
P58779
Q979T2
RS10_THEVO
30S ribosomal protein S10
Thermoplasma
MASYKARISLSGTEHKIVDMVCSEIKEIASRTGVEIHGPMPLPTKKLVVPVRKSPDGEGTNTWDHWEMRIHKRLIDVDADERTLRQLMRIPIPDGVQIEIQIKS
Involved in the binding of tRNA to the ribosomes.
Q979T2
Q5RCW7
KLD8B_PONAB
Kelch domain-containing protein 8B
Pongo
MSAGGGRAFAWQVFPPMPTCRVYGTVAHQDEHLLVLGGCGRAGLPLDTAETLDMASHTWLALAPLPTARAGAAAVVLGKQVLVVGGVDEVQSPVAAVEAFLMDEGRWERRATLPQAAMGVATVERDGMVYALGGMGPDTAPQAQVRVYEPRRDCWLSLPSMPTPCYGASTFLHGNKIYVLGGRQGKLPVTAFEAFDLEARTWTRHPSLPSRRAFAGCAMAEGSVFSLGGLQQPGPHNFYSRPHFVNTVEMFDLEHGSWTKLPRSLRMRDKRADFVVGSLGGHIVAIGGLGNQPCPLGSVESFSLARRRWEALPAMPTARCSCSSLQAGPRLFVIGGVAQGPSQAVEALCLRDGV
Involved in pinching off the separated nuclei at the cleavage furrow and in cytokinesis. Required for mitotic integrity and maintenance of chromosomal stability. Protects cells against mitotic errors, centrosomal amplification, micronucleus formation and aneuploidy. Plays a key role of midbody function involving abscission of the daughter cells during cytokinesis and appropriate chromosomal and nuclear segregation into the daughter cells.
Q5RCW7
A5K5W9
ASNA_PLAVS
Arsenite-stimulated ATPase
Plasmodium (Plasmodium)
MSDADSLSCSLTLESDEYDEEEYDTNLSKLLENKTLNWIFVGGKGGVGKTTTSCSIAVQLAKRRESVLLLSTDPAHNTSDAFNQKFTNQPTLINSFDNLYCMEIDTTYSENTAFKLNKTEFFDNIIPELLQSFPGIDEALCFAELMQSIKNMKYSVIVFDTAPTGHTLRLLAFPELLKKALGYLINLREKLKGTLNMLKSFTNNEMELEGIYEKINHLNAMSISIQSNFQNPLKTTFVCVCIPEFLSVYETERLIQELTKKNISCYNIVVNQVVFPLDSMTVDVAHCEGLLKQIKDKQVQESFSSLVQKTKELEDVYISRRKLQSKYLTQIKNLYGNDFHIVCMPQLKSEIRGLQNISNFSEMLLESKEIPIYR
ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors, where the tail-anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane proteins. ATP hydrolysis is required for insertion. Subsequently, the homodimer reverts towards the open dimer state, lowering its affinity for the membrane-bound receptor, and returning it to the cytosol to initiate a new round of targeting.
A5K5W9
P00171
CYB5_BOVIN
Cytochrome b5
Bos
MAEESSKAVKYYTLEEIQKHNNSKSTWLILHYKVYDLTKFLEEHPGGEEVLREQAGGDATENFEDVGHSTDARELSKTFIIGELHPDDRSKITKPSESIITTIDSNPSWWTNWLIPAISALFVALIYHLYTSEN
Cytochrome b5 is a membrane-bound hemoprotein functioning as an electron carrier for several membrane-bound oxygenases.
P00171
Q9Z2I8
SUCB2_MOUSE
Succinyl-CoA synthetase beta-G chain
Mus
MASPVAIAAQAGKLLRERALRPLLAVRSQAGHLTPRRWLNLQEYQSKKLMSEHGVRVQRFFVANTAKEALEAAKRLNAKEIVLKAQILAGGRGKGVFNSGLKGGVHLTKDPKVVGELAQQMIGYNLATKQTPKEGVKVNKVMVAEALDISRETYLAILMDRSHNGPVIVGSPQGGVDIEEVAASSPELIFKEQIDIFEGIKDSQAQRMAENLGFLGSLKNQAADQITKLYHLFLKIDATQVEVNPFGETPEGQVVCFDAKINFDDNAEFRQKDIFAMDDKSENEPIENEAARYDLKYIGLDGNIACFVNGAGLAMATCDIIFLNGGKPANFLDLGGGVKEAQVYEAFKLLTSDPKVEAILVNIFGGIVNCAIIANGITKACRELELKVPLVVRLEGTNVQEAQNILKSSGLPITSAVDLEDAAKKAVASVAKK
GTP-specific succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
Q9Z2I8
P24794
COX1_BETVU
Cytochrome c oxidase polypeptide I
Beta
MTNLVRWLFSTNHKDIGTLYFIFGAIAGVMGTCFSVLIRMELARPGDQILGGNHQLYNVLITAHAFLMIFFMVMPAMIGGFGNWFVPILIGAPDMAFPRLNNISFWLLPPSLLLLLSSALVEVGSGTGWTVYPPLSGITSHSGGAVDLAIFSLHLSGVSSILGSINFITTIFNMRGPGMTMHRLPLFVWSVLVTAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVSTFSGKPVFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWGGSIQYKTPMLFAVGFIFLFTVGGLTGIVLANSGLDIALHDTYYVVAHFHYVLSMGAVFALFAGFYYWVGKIFGRTYPETLGQIHFWITFFGVNLTFFPMHFLGLSGMPRRIPDYPDAYAGWNALSSFGSYISVVGICCFFVVVTITLSSGKNKRCAPSPWAVEENSTTLEWMVQSPPAFHTFGELPAIKETKS
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
P24794
Q9KS43
TSEL_VIBCH
Toxin TseL
Vibrio
MDSFNYCVQCNPEENWLELEFRSENDEPIDGLLVTITNQSAPSNTYTQTTSSGKVLFGKIAAGEWRASVSQASLLTEVEKYASRKEGQESPVKKRAAAELDAADKDTKQYRFTTIGDFWDEAPKDEFLQKQHKGIDVNASAEKAGFRLSHNQTYVFEIKALRSYMPVIIDTDEFNLVNSYTFALLSKLAYATNDFNRDDGKTIDNQGAISTVISQLKRKERPTYSGDLQAKWLLEEIPYSKALSAQYYAEDDVGSEGYIIFNDELAIIGVRGTEPYFQSKKPPVDNTKFKIIKAASGMAAVIADKIESATDSPGMKDLIITDLDAAQIAPEEFGGTYVHRGFYQYTMALLSLMEKDLGLHKIKKFYCCGHSLGGAGALLISALIKDSYHPPVLRLYTYGMPRVGTRSFVERYQNILHYRHVNNHDLVPQIPTVWMNTDVSEGFHVLDVFKSRVDLMRKMLTDDDDDNYQHHGHLSQLLTYNSNNQVLLTPKQTQVTMLDLANLATNDSVAMVDGLSDASIVEHGMEQYIPNLFEQLTALSDESLMVHYQRAISALEQEIATLQQSYLTVKQAWIESIGNGTPTMNIGRLMSEMHSINKLIENRNKIRGELRQIVSDPQRMPATKFLISQQTLPDEIKVQIR
Toxin secreted by the type VI (T6SS) secretion system that acts on prokaryotic as well as eukaryotic target cells.
Q9KS43
A5F5Y6
NQRD_VIBC3
NQR-1 subunit D
Vibrio
MSSAKELKKSVLAPVLDNNPIALQVLGVCSALAVTTKLETAFVMTLAVMFVTALSNFFVSLIRNHIPNSVRIIVQMAIIASLVIVVDQILKAYLYDISKQLSVFVGLIITNCIVMGRAEAFAMKSEPIPSFIDGIGNGLGYGFVLMTVGFFRELLGSGKLFGLEVLPLISNGGWYQPNGLMLLAPSAFFLIGFMIWAIRTFKPEQVEAKE
NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.
A5F5Y6
P20108
PRDX3_MOUSE
Thioredoxin-dependent peroxiredoxin 3
Mus
MAAAAGRLLWSSVARHASAISRSISASTVLRPVASRRTCLTDILWSASAQGKSAFSTSSSFHTPAVTQHAPYFKGTAVVNGEFKELSLDDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSHLAWINTPRKNGGLGHMNITLLSDITKQISRDYGVLLESAGIALRGLFIIDPNGVVKHLSVNDLPVGRSVEETLRLVKAFQFVETHGEVCPANWTPESPTIKPSPTASKEYFEKVHQ
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.
P20108
Q13ES7
UPPP_RHOPS
Undecaprenyl pyrophosphate phosphatase
Rhodopseudomonas
MLFDIFRAVILGVVEGVTEFLPVSSTGHLLLVGRFFNLGEDSFWKSFAVLIQLGAILAILSIYFAKLWRIALGMFSDPAARRFVIGVLVAFLPAAMIGAVAGSYIKLYLFNPWVVCFSLIVGGAILLWVDQLDLNPQQHDATAFPLPMYFYIGCAQCLAMIPGVSRSGASIVAAMLFGADKRSAAEFSFFLAIPTMVGAFVYDFYKNRGEMTTDHLTIVAIGFVVSFITAVIVVKTFLGYVTRHGFELFAWWRVIVGTLGLIALAMGR
Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Q13ES7
P51480
CDN2A_MOUSE
p16-INK4a
Mus
MESAADRLARAAAQGRVHDVRALLEAGVSPNAPNSFGRTPIQVMMMGNVHVAALLLNYGADSNCEDPTTFSRPVHDAAREGFLDTLVVLHGSGARLDVRDAWGRLPLDLAQERGHQDIVRYLRSAGCSLCSAGWSLCTAGNVAQTDGHSFSSSTPRALELRGQSQEQS
Acts as a negative regulator of the proliferation of normal cells by interacting strongly with CDK4 and CDK6. This inhibits their ability to interact with cyclins D and to phosphorylate the retinoblastoma protein.
P51480
A0A1L8GXY6
N4B3A_XENLA
NEDD4-binding protein 3-A
Xenopus
MAAAQTFNSNCDPGNFHKLQSFPSESVTYTCKMGSVSSLIDKQDFPHDGFNLDFKPFPEPNCKRGLHQKELLSYLNITKKEVKSNKKFHSGLGFRREHSVEGGENDYPVFYHKDHRGTEFSKSSLPERGHLDKSRFGPSALRSNVKAFMSIQSLYQSGNKLSKSNGSLNTMSCVSSPPCRGPLQPSNSHSNNQSESGNDEEDDSLSDSRQNSINSLNSYSPGFSVARGQISASLGHINHIGGSLDQASRGTRDTMAGEKGTLSCRSMATLSRLQCSGEPPPPYEYSQSVEDVARQLEERLHEKGMEARQLRRNASDNDDPFTKVFEDKRRLWMEELDELKQMYMSKLQQISQQALRSQRALQLQLYKVQQEKKRLQEELNSLRGESEELRQKQSQSDNSGPKLEDSKWEISQKAGEISLLKQQLRDSQAEINQKLGEVVSLKSQLREAKVLVKEKEKESAELSTRLQALENAKSQAPVDLPRDNSDTIDLERLRAELMLERRQNEAQMLTFETERKVWKEEKDKVLRYQKEIQSSYREMYHRNQVLERQVLELRQGVGQSPSSPAIWMDTVET
Plays a role in axon and dendrite arborization during cranial nerve development . Also important for neural crest migration and early development of other anterior structures including eye, brain and cranial cartilage .
A0A1L8GXY6
Q5VU43
MYOME_HUMAN
Phosphodiesterase 4D-interacting protein
Homo
MSNGYRTLSQHLNDLKKENFSLKLRIYFLEERMQQKYEASREDIYKRNIELKVEVESLKRELQDKKQHLDKTWADVENLNSQNEAELRRQFEERQQETEHVYELLENKIQLLQEESRLAKNEAARMAALVEAEKECNLELSEKLKGVTKNWEDVPGDQVKPDQYTEALAQRDKRIEELNQSLAAQERLVEQLSREKQQLLHLLEEPTSMEVQPMTEELLKQQKLNSHETTITQQSVSDSHLAELQEKIQQTEATNKILQEKLNEMSYELKCAQESSQKQDGTIQNLKETLKSRERETEELYQVIEGQNDTMAKLREMLHQSQLGQLHSSEGTSPAQQQVALLDLQSALFCSQLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEASWKHNQELRKALQQLQEELQNKSQQLRAWEAEKYNEIRTQEQNIQHLNHSLSHKEQLLQEFRELLQYRDNSDKTLEANEMLLEKLRQRIHDKAVALERAIDEKFSALEEKEKELRQLRLAVRERDHDLERLRDVLSSNEATMQSMESLLRAKGLEVEQLSTTCQNLQWLKEEMETKFSRWQKEQESIIQQLQTSLHDRNKEVEDLSATLLCKLGPGQSEIAEELCQRLQRKERMLQDLLSDRNKQVLEHEMEIQGLLQSVSTREQESQAAAEKLVQALMERNSELQALRQYLGGRDSLMSQAPISNQQAEVTPTGRLGKQTDQGSMQIPSRDDSTSLTAKEDVSIPRSTLGDLDTVAGLEKELSNAKEELELMAKKERESQMELSALQSMMAVQEEELQVQAADMESLTRNIQIKEDLIKDLQMQLVDPEDIPAMERLTQEVLLLREKVASVESQGQEISGNRRQQLLLMLEGLVDERSRLNEALQAERQLYSSLVKFHAHPESSERDRTLQVELEGAQVLRSRLEEVLGRSLERLNRLETLAAIGGAAAGDDTEDTSTEFTDSIEEEAAHHSHQQLVKVALEKSLATVETQNPSFSPPSPMGGDSNRCLQEEMLHLRAEFHQHLEEKRKAEEELKELKAQIEEAGFSSVSHIRNTMLSLCLENAELKEQMGEAMSDGWEIEEDKEKGEVMVETVVTKEGLSESSLQAEFRKLQGKLKNAHNIINLLKEQLVLSSKEGNSKLTPELLVHLTSTIERINTELVGSPGKHQHQEEGNVTVRPFPRPQSLDLGATFTVDAHQLDNQSQPRDPGPQSAFSLPGSTQHLRSQLSQCKQRYQDLQEKLLLSEATVFAQANELEKYRVMLTGESLVKQDSKQIQVDLQDLGYETCGRSENEAEREETTSPECEEHNSLKEMVLMEGLCSEQGRRGSTLASSSERKPLENQLGKQEEFRVYGKSENILVLRKDIKDLKAQLQNANKVIQNLKSRVRSLSVTSDYSSSLERPRKLRAVGTLEGSSPHSVPDEDEGWLSDGTGAFYSPGLQAKKDLESLIQRVSQLEAQLPKNGLEEKLAEELRSASWPGKYDSLIQDQARELSYLRQKIREGRGICYLITRHAKDTVKSFEDLLRSNDIDYYLGQSFREQLAQGSQLTERLTSKLSTKDHKSEKDQAGLEPLALRLSRELQEKEKVIEVLQAKLDARSLTPSSSHALSDSHRSPSSTSFLSDELEACSDMDIVSEYTHYEEKKASPSHSDSIHHSSHSAVLSSKPSSTSASQGAKAESNSNPISLPTPQNTPKEANQAHSGFHFHSIPKLASLPQAPLPSAPSSFLPFSPTGPLLLGCCETPVVSLAEAQQELQMLQKQLGESASTVPPASTATLLSNDLEADSSYYLNSAQPHSPPRGTIELGRILEPGYLGSSGKWDVMRPQKGSVSGDLSSGSSVYQLNSKPTGADLLEEHLGEIRNLRQRLEESICINDRLREQLEHRLTSTARGRGSTSNFYSQGLESIPQLCNENRVLREDNRRLQAQLSHVSREHSQETESLREALLSSRSHLQELEKELEHQKVERQQLLEDLREKQQEVLHFREERLSLQENDSRLQHKLVLLQQQCEEKQQLFESLQSELQIYEALYGNSKKGLKAYSLDACHQIPLSSDLSHLVAEVRALRGQLEQSIQGNNCLRLQLQQQLESGAGKASLSPSSINQNFPASTDPGNKQLLLQDSAVSPPVRDVGMNSPALVFPSSASSTPGSETPIINRANGLGLDTSPVMKTPPKLEGDATDGSFANKHGRHVIGHIDDYSALRQQIAEGKLLVKKIVSLVRSACSFPGLEAQGTEVLGSKGIHELRSSTSALHHALEESASLLTMFWRAALPSTHIPVLPGKVGESTERELLELRTKVSKQERLLQSTTEHLKNANQQKESMEQFIVSQLTRTHDVLKKARTNLEVKSLRALPCTPAL
Participates in microtubule dynamics, promoting microtubule assembly. Depending upon the cell context, may act at the level of the Golgi apparatus or that of the centrosome . In complex with AKAP9, recruits CAMSAP2 to the Golgi apparatus and tethers non-centrosomal minus-end microtubules to the Golgi, an important step for polarized cell movement . In complex with AKAP9, EB1/MAPRE1 and CDK5RAP2, contributes to microtubules nucleation and extension from the centrosome to the cell periphery, a crucial process for directed cell migration, mitotic spindle orientation and cell-cycle progression .
Q5VU43
Q6YPW4
PYRG_ONYPE
UTP--ammonia ligase
Candidatus Phytoplasma asteris
MNNKDLKTKFIFITGGVVSSLGKGITAASIGQILKNRGLKVSIQKLDPYINIDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDENMSKKSNVTAGQIYQSVINKEREGKYLGKTVQVIPHITEEIKQKLIDVALFHKSDVVIVEIGGTVGDIESSPFLEAIRQVRFDFGYHNVLYLHTTLVPYLKKAQEIKTKPTQHSVKELRALGIQPQILVLRSEVPINPETKNKIAALCDINPQAIFEALDVDILYQMILNLHHQGIDDFILQHFKLTNFSNADLQSWKQLITRIQNLEKKVVIALVGKYIVLHDAYLSIIEALKHASYQYNCKLEIKWIDAEKVTPDNISSLLEDYDGILVPYGFGNRAIEGKILAINYARTNNIPFFGICLGMQLAVIEYARNVLHLQGANSLEVDEKTPHPVITKKIVDSNLGGTLRLGSYPCHLKANTKSKAIYNQEIIYERHRHRFEMNPHYVALFEKNNDFVVSGINQEQKLCEIVELKSHPWFIAVQFHPEFLSRPLKPHPLFKGFVEASLLNQKNK
Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.
Q6YPW4
A8ESW0
RS5_ALIB4
30S ribosomal protein S5
Aliarcobacter
MAVNREDFQEAIVKIGRVTKVVKGGRRFRFTALVVVGDKNGTVGFGTGKAKEVPDAIKKALDDAFKSLVTVSIKGTTIAHDIEHKYNASKILLRPASEGTGLIAGGAARPVLELSGVKDIIAKSLGSNNPNNLVQATVEALAKIKG
Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body.
A8ESW0