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
|
|---|---|---|---|---|---|---|
Q9A8S9
|
RPOA_CAUVC
|
Transcriptase subunit alpha
|
Caulobacter
|
MIERNWNELIRPEKPQIETGADATRKARIVAEPLERGFGVTLGNALRRVLLSSLQGAAVTAIQIDGVVHEFSSLEGVREDVVDIVLNIKQLAVRMHAEGPKRMTLRATGPGPVTAGQIETPADIEILNPDHVLCTLDDGASVRMEFTVNNGKGYVPADRNRPEDAPIGLIAVDALYSPVKRVAYRVEPTRQGQSLDYDKLILEVETNGAVTPVDAVAYAARILQDQLQIFITFEEPKAKSADESKPELPFNPALLKKVDELELSVRSANCLKNDNIVYIGDLIQKTEAEMLRTPNFGRKSLNEIKEVLAGMGLHLGMDVPNWPPENIEDLAKKFEDQI
|
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
|
Q9A8S9
|
Q8NFY9
|
KBTB8_HUMAN
|
T-cell activation kelch repeat protein
|
Homo
|
MAASADLSKSSPTPNGIPSSDPASDAMDPFHACSILKQLKTMYDEGQLTDIVVEVDHGKTFSCHRNVLAAISPYFRSMFTSGLTESTQKEVRIVGVEAESMDLVLNYAYTSRVILTEANVQALFTAASIFQIPSIQDQCAKYMISHLDPQNSIGVFIFADHYGHQELGDRSKEYIRKKFLCVTKEQEFLQLTKDQLISILDSDDLNVDREEHVYESIIRWFEHEQNEREVHLPEIFAKCIRFPLMEDTFIEKIPPQFAQAIAKSCVEKGPSNTNGCTQRLGMTASEMIICFDAAHKHSGKKQTVPCLDIVTGRVFKLCKPPNDLREVGILVSPDNDIYIAGGYRPSSSEVSIDHKAENDFWMYDHSTNRWLSKPSLLRARIGCKLVYCCGKMYAIGGRVYEGDGRNSLKSVECYDSRENCWTTVCAMPVAMEFHNAVEYKEKIYVLQGEFFLFYEPQKDYWGFLTPMTVPRIQGLAAVYKDSIYYIAGTCGNHQRMFTVEAYDIELNKWTRKKDFPCDQSINPYLKLVLFQNKLHLFVRATQVTVEEHVFRTSRKNSLYQYDDIADQWMKVYETPDRLWDLGRHFECAVAKLYPQCLQKVL
|
Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a regulator of neural crest specification . The BCR(KBTBD8) complex acts by mediating monoubiquitination of NOLC1 and TCOF1: monoubiquitination promotes the formation of a NOLC1-TCOF1 complex that acts as a platform to connect RNA polymerase I with enzymes responsible for ribosomal processing and modification, leading to remodel the translational program of differentiating cells in favor of neural crest specification .
|
Q8NFY9
|
Q4WI89
|
ATRR_ASPFU
|
ABC-transporter-regulating transcription factor
|
Aspergillus subgen. Fumigati
|
MDGIGDGTESMGFDMPMLMNQQPHLFGSYGHDGSPVAPIFSNPTFQDEPSIGAADDNSDAKRRRIARACDMCRKKKIKCDGKMPKCSHCTNYKTDCVFTQVEKKRNPPKGAKYIEGLENRLGRMESLLRLSGLLSEDDGGKTDLGTLEKRLADRYHASGSNTPHNPQKINIPSQSQIAMSQQNSSSHYSTPRLESQSSPRTAATSPESQKESETEVEGLSDMMCSLVTNNCGETRYIGSSSGFSIFSPKGIQWVNEKTGDNSFQEMISSAYVDDNKWMYWKPEIFSDIFARRVFKPLPPKDEAMSLFKDFFDNFNCMFPLYHEPTFMHLVERQYSRDPYEGSGWWASINVVLAIAHRLRVMSNLVPQEEDRKAWLYLKNAMGVLTELTMRNTDLLSVQALLGMSLFLQGTPNPQPSFFLVAAAIRLSHSIGLHKRGSGFGLNPVEVEQRKRVFWIAYLLDKDICLRSGRPPVQDDDDMNVELPSDDPPDNIGNVPLSDGRSKFNLFRSMCRFATIESKVYKRLYSAKASKQSDGELLNTIGELDKELEDWKDSIPLDFRPEHEIKASHTPLILHVVVLHFAYYNCLTTIHRMSVHHGYWTSRLSNYAIQGLNARPLNPRVFLSAVLCVTAARASINLIKYIPQGDFACVWLILYYPVSALVTLFANILQNPSDARARSDVKLMNVVVNFLSTLVSDESNGSIKRMLGLCGEFERIAKVVLDKAEKESYSKKKRKSPEEPVNLQQSTPEEHPAPSPSTTQPTQAPSRNVPMSSPLFAENPGDPGGNTMADDAGGFASSREIPGTTGVSTNIPPNIQAMPGIAQDYQDMLSPDPLEGVSFADQPPYSATANTPLSSFQQPFVPQDLWQMPMTIEWDWADMSTNFPVFDTNGPPHGGL
|
Transcription factor that regulates expression of the genes related to ergosterol biosynthesis, including erg3B, erg24A, erg25A, as well as cyp51A that encodes a target protein of azoles . Responsible for the expression of the ABC transporter abcC/cdr1B/abcG1 related to azole resistance . Directly binds both the cyp51A and abcC/cdr1B/abcG1 promoters at a conserved 34 bp region called the atrR response element (ATRE) . AtrR also binds to the promoter regions of both the sterol response transcription factor srbA and atrR genes themselves, the latter suggesting the possibility that atrR is autoregulated . AtrR is necessary for hypoxia adaptation and virulence .
|
Q4WI89
|
P48624
|
FAD3E_BRANA
|
Omega-3 fatty acid desaturase 3, endoplasmic reticulum
|
Brassica
|
MVVAMDQRSNVNGDSGARKEEGFDPSAQPPFKIGDIRAAIPKHCWVKSPLRSMSYVTRDIFAVAALAMAAVYFDSWFLWPLYWVAQGTLFWAIFVLGHDCGHGSFSDIPLLNSVVGHILHSFILVPYHGWRISHRTHHQNHGHVENDESWVPLPEKLYKNLPHSTRMLRYTVPLPMLAYPIYLWYRSPGKEGSHFNPYSSLFAPSERKLIATSTTCWSIMLATLVYLSFLVDPVTVLKVYGVPYIIFVMWLDAVTYLHHHGHDEKLPWYRGKEWSYLRGGLTTIDRDYGIFNNIHHDIGTHVIHHLFPQIPHYHLVDATRAAKHVLGRYYREPKTSGAIPIHLVESLVASIKKDHYVSDTGDIVFYETDPDLYVYASDKSKIN
|
ER (microsomal) omega-3 fatty acid desaturase introduces the third double bond in the biosynthesis of 18:3 fatty acids, important constituents of plant membranes. It is thought to use cytochrome b5 as an electron donor and to act on fatty acids esterified to phosphatidylcholine and, possibly, other phospholipids.
|
P48624
|
C3PKP0
|
RS7_CORA7
|
30S ribosomal protein S7
|
Corynebacterium
|
MRKNAAPKRPVVKDPVYNSEQVTMLVNKILRDGKKSTAERIVYGALEVCREKTGTDPVGTLEKALGNIRPDLEVRSRRVGGATYQVPVEVKPARSNTLALRWLVTFTRQRRENSMIERLANEILDASNGLGASVKRREDTHKMAEANRAFAHYRW
|
One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA.
|
C3PKP0
|
Q50186
|
RODA_MYCLE
|
Non-canonical transglycosylase RodA
|
Mycobacterium
|
MTTQLQPVVTVTPPLPTRRNAELLLLGFAAVITVAALAIVEANQERNFRWYLAGYGLIFWSLFASAHLAIRRFAPYTDPLLLPIVALLNGLGLVMIHRLDLVDNDVTGHHHTSAAQQMLWTLVGVAAFVLVMTVLKDHRQLARYGYISGLTGLVFLAIPAPLPEQNGAKIWIRFPGFSIQPAEFSKILLLIFFAAVLVAKRSLFTSAGKHLIGMTLPRPRDLAPLLAAWVISVSVMVFEKDLGTSLLLYASFLVVVYLATQRLSWVIIGLVLFTAGSTIAYFTFEHIRVRMQVWWDPFTNLDVGGYQIVQSLFSFATGGIFGTGLGNGQPDAIPAASTDFIIAVFGEELGLVGLAALLMLYTIVIVRGLRTAIATRDSFGKLLAAGLASTLAIQLFIVSGGVTTLIPLTGLTTPWMSYGGSSLLANYVLLAILARISHSARHPLRSRPHNTSPIAVASTEVIERV
|
Transglycosylase involved in peptidoglycan cell wall formation. Required for the regulation of cell length.
|
Q50186
|
Q8BMT4
|
LRC33_MOUSE
|
Negative regulator of reactive oxygen species
|
Mus
|
MEFPPLWLCLGFHFLIVEWRSGPGTATAASQGGCKVVDGVADCRGLNLASVPSSLPPHSRMLILDANPLKDLWNHSLQAYPRLENLSLHSCHLDRISHYAFREQGHLRNLVLADNRLSENYKESAAALHTLLGLRRLDLSGNSLTEDMAALMLQNLSSLEVVSLARNTLMRLDDSIFEGLEHLVELDLQRNYIFEIEGGAFDGLTELRRLNLAYNNLPCIVDFSLTQLRFLNVSYNILEWFLAAREEVAFELEILDLSHNQLLFFPLLPQCGKLHTLLLQDNNMGFYRELYNTSSPQEMVAQFLLVDGNVTNITTVNLWEEFSSSDLSALRFLDMSQNQFRHLPDGFLKKTPSLSHLNLNQNCLKMLHIREHEPPGALTELDLSHNQLAELHLAPGLTGSLRNLRVFNLSSNQLLGVPTGLFDNASSITTIDMSHNQISLCPQMVPVDWEGPPSCVDFRNMGSLRSLSLDGCGLKALQDCPFQGTSLTHLDLSSNWGVLNGSISPLWAVAPTLQVLSLRDVGLGSGAAEMDFSAFGNLRALDLSGNSLTSFPKFKGSLALRTLDLRRNSLTALPQRVVSEQPLRGLQTIYLSQNPYDCCGVEGWGALQQHFKTVADLSMVTCNLSSKIVRVVELPEGLPQGCKWEQVDTGLFYLVLILPSCLTLLVACTVVFLTFKKPLLQVIKSRCHWSSIY
|
Key regulator of transforming growth factor beta-1 (TGFB1) specifically required for microglia function in the nervous system . Required for activation of latent TGF-beta-1 in macrophages and microglia: associates specifically via disulfide bonds with the Latency-associated peptide (LAP), which is the regulatory chain of TGFB1, and regulates integrin-dependent activation of TGF-beta-1 . TGF-beta-1 activation mediated by LRRC33/NRROS is highly localized: there is little spreading of TGF-beta-1 activated from one microglial cell to neighboring microglia, suggesting the existence of localized and selective activation of TGF-beta-1 by LRRC33/NRROS . Indirectly plays a role in Toll-like receptor (TLR) signaling: ability to inhibit TLR-mediated NF-kappa-B activation and cytokine production is probably a consequence of its role in TGF-beta-1 signaling (Probable).
|
Q8BMT4
|
B3PPF4
|
ACCA_RHIE6
|
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha
|
Rhizobium
|
MHNYLDFEKPISDLEGKIIELKKLATEDESIDTTDEIGRLEVRVREAILEIYSKLNAWQKTQVARHPQRPHFVDYAKTLFQEFTPLAGDRKFSEDAAIQAGLARFRGQPVAVIGQEKGNDTKSRLKHNFGSPRPEGYRKAIRILEMADRFGLPVISLVDTAGAYPGVGAEERGQAEAIARSTEMCLGVKVPLVSVVIGEGGSGGAIAIATGNRVYMLEHSIYSVISPEGAASILWRDSTRAREAATNMKITAEDLKSLGVIDGIISEPLGGAHRDPDSVIAATGDVIANALAEMSSRSGEQLRNERRQKFLNMGRNL
|
Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA.
|
B3PPF4
|
A2S5U5
|
MURG_BURM9
|
Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase
|
pseudomallei group
|
MTSTQRTLMVMAGGTGGHVFPGLAVAHRMQAQGWRVVWLGNPAGMEATLVPRHGIPMEYVRFGGLRGKGLATKFALPFNLLRACAQSLRALRRVKPDVVLGMGGYITFPAGLVTVLTGRPLVLHEQNSIAGLTNKVLAKLAKRVLVAFPGALPNAEWTGNPIRTELARTEPPQARYAARSGKLRLLVVGGSLGAAALNEVVPRALALLAPDERPQVVHQAGAKHIDTLKENYEAAGLSCGSDVALVPFIDDMASAYANADLVICRSGAMTVAEIAAVGVAALFVPFPHAVDDHQTTNAEFLAEQGAAVLVQQRDLSAELLADWLRGQSRDSLAAMAERSRSLAKPDATDEVARVCAAVAGANLEGKQ
|
Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
|
A2S5U5
|
B8DW26
|
RS14Z_BIFA0
|
30S ribosomal protein S14 type Z
|
Bifidobacterium
|
MAKTCLKVKALRKPKFKVRAYTRCMVCGRPHSVYRKFGLCRICLREKAHRGELPGVTKSSW
|
Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site.
|
B8DW26
|
Q4WC50
|
MFSA_ASPFU
|
Major facilitator superfamily transporter mfsA
|
Aspergillus subgen. Fumigati
|
MWTTTSGLSGRSLRLSITFAAVVGFSLFGYNQGMMAGLLNGDEFVNSFPILKMPDNPTAGEKHYIDVIRGAVTSCYELGCFFGALFSMFCGNRLGRTRLIFMGASILIVGALLTTVCYTGKWEVGQFVIGRVVSGIGNGMNTATIPVWQSECSGAHNRGFLVCFEGAMIAGGTFIAYWVVFGISHAADSVQWRFPVALQIFFALVVATGALMLPDSPSWFVSRGLDNEACEVLGKIKGTSPDSDQVLHDFNLIKTDMESTKSEQSNWKTVFTFGKTQEFQRLLIGCSGQFFQQFTGCNAAIYYSTLLFQENLHMEKYLSLIMGGVFASVYALATIPSFFMIERVGRRKLYLIGFLGQGLSFVITFACLIKETEENSKGAAVGIFLFITFFAFTLLPLPWIYPPEINPLRTRTVGASASTCTNWMCNFAVVMFTPLFAGQSPWGVYLFFALFNFVGLIFGYFFYVETAGRELEEVDIIYAKAHVEGKMPFRVAHDLPKLSFEEIVQQSRELGLDTNDHVMLEKKELGLSSDSAQETEEVYEKQ
|
Major facilitator superfamily transporter that may be involved in A.fumigatus adaptation to azoles such as vorizonazole.
|
Q4WC50
|
Q87J41
|
NADE_VIBPA
|
NH(3)-dependent NAD(+) synthetase
|
Vibrio
|
MEQSIRDEMRVLPSIDPHFEIERRIAFIKRKLQEAGCKSLVLGISGGVDSTTLGRLAQLAVDQLNEETGSNDYQFIAVRLPYGEQKDEDEAQLALSFIKPTHSISVNIKQGVDGMHAASNIALEGTGLMPEDAAKVDFVKGNVKARARMIAQYEIAGYVGGLVLGTDHSAENITGFYTKFGDGACDLAPLFGLNKRQVREVAATLGAPEVLVKKVPTADLEELAPQKADEDALNLTYEQIDDFLEGKPVSQQVVDRLVSIYKATQHKRQPIPTIYD
|
Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
|
Q87J41
|
Q9Y2D4
|
EXC6B_HUMAN
|
SEC15-like protein 2
|
Homo
|
MERGKMAEAESLETAAEHERILREIESTDTACIGPTLRSVYDGEEHGRFMEKLETRIRNHDREIEKMCNFHYQGFVDSITELLKVRGEAQKLKNQVTDTNRKLQHEGKELVIAMEELKQCRLQQRNISATVDKLMLCLPVLEMYSKLRDQMKTKRHYPALKTLEHLEHTYLPQVSHYRFCKVMVDNIPKLREEIKDVSMSDLKDFLESIRKHSDKIGETAMKQAQQQRNLDNIVLQQPRIGSKRKSKKDAYIIFDTEIESTSPKSEQDSGILDVEDEEDDEEVPGAQDLVDFSPVYRCLHIYSVLGARETFENYYRKQRRKQARLVLQPPSNMHETLDGYRKYFNQIVGFFVVEDHILHTTQGLVNRAYIDELWEMALSKTIAALRTHSSYCSDPNLVLDLKNLIVLFADTLQVYGFPVNQLFDMLLEIRDQYSETLLKKWAGIFRNILDSDNYSPIPVTSEEMYKKVVGQFPFQDIELEKQPFPKKFPFSEFVPKVYNQIKEFIYACLKFSEDLHLSSTEVDDMIRKSTNLLLTRTLSNSLQNVIKRKNIGLTELVQIIINTTHLEKSCKYLEEFITNITNVLPETVHTTKLYGTTTFKDARHAAEEEIYTNLNQKIDQFLQLADYDWMTGDLGNKASDYLVDLIAFLRSTFAVFTHLPGKVAQTACMSACKHLATSLMQLLLEAEVRQLTLGALQQFNLDVRECEQFARSGPVPGFQEDTLQLAFIDLRQLLDLFIQWDWSTYLADYGQPNCKYLRVNPVTALTLLEKMKDTSRKNNMFAQFRKNERDKQKLIDTVAKQLRGLISSHHS
|
Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
|
Q9Y2D4
|
B9LRD9
|
RS10_HALLT
|
30S ribosomal protein S10
|
Halorubrum
|
MQQARVRLAGTSPEDLDDICADVREIADSTGVALSGPIPLPTKTLEIPSRKSPDGEGTATWEHWEMRVHKRLIDIDADERALRQLMRVQVPNDVSIEIVLED
|
Involved in the binding of tRNA to the ribosomes.
|
B9LRD9
|
Q96LW1
|
Z354B_HUMAN
|
Zinc finger protein 354B
|
Homo
|
MAAGQREARPQVSLTFEDVAVLFTWDEWRKLAPSQRNLYRDVMLENYRNLVSLGLSFTKPKVISLLQQGEDPWEVEKDSSGVSSLGCKSTPKMTKSTQTQDSFQEQIRKRLKRDEPWNFISERSCIYEEKLKKQQDKNENLQIISVAHTKILTVDRSHKNVEFGQNFYLKSVFIKQQRFAKEKTPSKCEIQRNSFKQNSNLLNQSKIKTAEKRYKCSTCEKAFIHNSSLRKHQKNHTGEKLFKCKECLKAFSQSSALIQHQRTHTGEKPYICKECGKAFSHSASLCKHLRTHTVEKCYRCKECGKSFSRRSGLFIHQKIHAQENPHKYNPGRKASSYSTSLSGSQKIHLRKKSYLCNECGNTFKSSSSLRYHQRIHTGEKPFKCSECGRAFSQSASLIQHERIHTGEKPYRCNECGKGFTSISRLNRHRIIHTGEKLYNCNECGKALSSHSTLIIHERIHTGEKPCKCKVCGKAFRQSSALIQHQRMHTGERPYKCNECDKTFRCNSSLSNHQRIHTGEKPYRCLECGMSFGQSAALIQHQRIHTGEKPFKCNTCGKTFRQSSSLIAHQRIHTGEKPYECNACGKLFSQRSSLTNHYKIHIEEDSLKADLHV
|
May be involved in transcriptional regulation.
|
Q96LW1
|
B3EMI1
|
RECX_CHLPB
|
Regulatory protein RecX
|
Chlorobium
|
MADTDDKKAFDLAIRLLGEREHSRKEIITKLERRKFSEAAIDKTLERLDQLGLIDDRSFAEHFVGSRSRKKPSGKYKLRYELFQKGISETIIDEILSDYDSSAHCLDAAMKKFPFLKGDDHYKRKKLYAFLANRGFDSHSIRETLDQIFRS
|
Modulates RecA activity.
|
B3EMI1
|
Q9HCJ3
|
RAVR2_HUMAN
|
Protein raver-2
|
Homo
|
MAAAAGDGGGEGGAGLGSAAGLGPGPGLRGQGPSAEAHEGAPDPMPAALHPEEVAARLQRMQRELSNRRKILVKNLPQDSNCQEVHDLLKDYDLKYCYVDRNKRTAFVTLLNGEQAQNAIQMFHQYSFRGKDLIVQLQPTDALLCITNVPISFTSEEFEELVRAYGNIERCFLVYSEVTGHSKGYGFVEYMKKDFAAKARLELLGRQLGASALFAQWMDVNLLASELIHSKCLCIDKLPSDYRDSEELLQIFSSVHKPVFCQLAQDEGSYVGGFAVVEYSTAEQAEEVQQAADGMTIKGSKVQVSFCAPGAPGRSTLAALIAAQRVMHSNQKGLLPEPNPVQIMKSLNNPAMLQVLLQPQLCGRAVKPAVLGTPHSLPHLMNPSISPAFLHLNKAHQSSVMGNTSNLFLQNLSHIPLAQQQLMKFENIHTNNKPGLLGEPPAVVLQTALGIGSVLPLKKELGHHHGEAHKTSSLIPTQTTITAGMGMLPFFPNQHIAGQAGPGHSNTQEKQPATVGMAEGNFSGSQPYLQSFPNLAAGSLLVGHHKQQQSQPKGTEISSGAASKNQTSLLGEPPKEIRLSKNPYLNLASVLPSVCLSSPASKTTLHKTGIASSILDAISQGSESQHALEKCIAYSPPFGDYAQVSSLRNEKRGSSYLISAPEGGSVECVDQHSQGTGAYYMETYLKKKRVY
|
May bind single-stranded nucleic acids.
|
Q9HCJ3
|
A1AR94
|
PDXJ_PELPD
|
Pyridoxine 5'-phosphate synthase
|
Pelobacter
|
MAKLGLNVDHVATVRQARGGMEPDPVTAAALGELAGAEGITIHLREDRRHIQDRDLEILRRTVKTKLNLEMAATQEMVRIALRTKPEQVTLVPEKRQELTTEGGLDVILNLKAITDAVKRLRDGGIVVSLFVDPDQEQIKAANKSGADYIEIHTGAYADAPDWPSQKRQLEEIDAAIKLASKVGMGVNAGHGINYVNIKPLAALGGIEEYNIGHSIMARAILVGMDRAVKDMVELIKYA
|
Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
|
A1AR94
|
A5F7R1
|
NHAA_VIBC3
|
Sodium/proton antiporter NhaA
|
Vibrio
|
MSDMIRDFFKMESAGGILLVIAAAIAMVIANSAMGEGYQAFLHTYVFGMSVSHWINDGLMAVFFLLIGLEVKRELLEGALKSRETAIFPAIAAVGGMLAPALIYVAFNFNDPAAIQGWAIPAATDIAFALGIMALLGKRVPVSLKVFLLALAIIDDLGVVVIIALFYSSDLSTIALTIGFIMTGVLFMLNAKHVTKLSIYLVAGLILWIAVLKSGVHATLAGVVIGFAIPLKGNKGEHSPLKHLEHALHPYVAFAILPVFAFANAGISLQGVSLAGLTSMLPLGVALGLFLGKPLGIFSFSWAAVKLGVAKLPEGINFKHIFAVSVLCGIGFTMSIFISSLAFGQANEAYDTYARLGILMGSTTAALLGYSLLRLSLPLKKA
|
Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons.
|
A5F7R1
|
P16169
|
GUNA_RUMFL
|
Cellodextrinase A
|
Ruminococcus
|
MLKSRGIIKGINLGGWMSQCDYSRERLDNFVKENDIKQIADWGFDHVRLPIDYNIVQNNDGSVIEDGYNRIDKVVELCRKYGLKLVIDLHKTAGFSFDFGEPESGFFDNKEYQERFYILWEEIARRYGHDTDNIVFELLNEVTDEAFIGKWNEISDICIGRIRKIAPEVIILLGSYHNNAADTVQFLNAPHDDRVVYNFHCYEPLKFTHQGATWTPDIIPGERMKFEDSETSEAYFEELFSTAISTAEKYGTTLYCGEYGVIDVVSAEDSLKWFKVINKVFSKHGISRECGITRKWTSAFPTASTTATVRDTEVSVIKTRKAHNCCTLTEVFTRVY
|
Crystalline cellulose degradation.
|
P16169
|
A0RJ47
|
OBG_BACAH
|
GTP-binding protein Obg
|
Bacillus cereus group
|
MFVDQVKIYVKGGDGGNGMVAYRREKYVPKGGPAGGDGGKGADVVFIVEEGLRTLMDFRYQRHFKADRGQHGMSKGQHGRKSEDLLVKVPPGTVVKDEKTGQILADLVTHGQTAVIAKGGRGGRGNSRFATATNPAPEIAENGEPGQERDVILELKVLADVGLVGFPSVGKSTLLSVVSSARPKIAEYHFTTIVPNLGVVETGDNRSFVMADLPGLIEGAHAGVGLGHQFLRHIERTRVIVHVIDMSGLEGRDPYEDYVTINNELKEYNLRLTERPQVVVANKMDMPDAEENLQAFKEKVGDEVKIFPISAVTKQGVRDLLFEVANLIETTPEFPIHEVVDESDTSVMYKFETEGVKFDITRESDGTFVISGYDIEKTFKMTDFSRDESVRRFARQMRGMGIDEALRARGAKDGDIVKILEYEFEFID
|
An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control.
|
A0RJ47
|
Q03F74
|
PFKA_PEDPA
|
Phosphohexokinase
|
Pediococcus
|
MKRIGIMTSGGDAPGMNLAIRAVARKALSSGLEAYGINYGFAGLVAGDIHEFKAADLDDMVSQGGTMLYSARYPEFAQEESQLKGIEQLKKFGIDALVVIGGDGSYHGALRLTEHGYNTIGLPGTIDNDIPFTDFTIGFDTALNTAVDAIDKIRDTAKSHQRVFAVQVMGRNAADIALWAGVASGADAVIAPGFDYDVEAIANKLKKNRANGKDYGIIVIAEGDANSDAAPEFIDQLKQYGDFDARATVIGHVQRGGVPSAKDRVLASKMGAYAVELLLEGKGGLAVGILENKVQAHNMLDLFDAKHQADDSLYQLSEDLSF
|
Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
|
Q03F74
|
P19371
|
IPYR_DESVH
|
Pyrophosphate phospho-hydrolase
|
Desulfovibrio
|
NYTIGNDNVLTEPLSEIKTAGLMYKMGVQ
|
Inorganic pyrophosphatase is an essential enzyme for the activation of sulfate by sulfate reducing bacteria. This is a high activity pyrophosphatase.
|
P19371
|
A5CXM1
|
RS5_VESOH
|
30S ribosomal protein S5
|
Candidatus Vesicomyosocius
|
MAGYKENNNIDNNYIEKLVNIRRVVKVVKGGRIFGFSALVVVGDGNGKVGYGTGKAREVPVAIQKAMDKARKAMKNVPLVNGTLHYSIISNVGAAKVYMQPASEGTGVIAGGPMRSVLEAVGVHNILAKCNGTRNPISVVRATVEGLTSMLSPQLVATKRGMTVDQITGEE
|
Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body.
|
A5CXM1
|
B5FRC1
|
ACPS_SALDC
|
4'-phosphopantetheinyl transferase AcpS
|
Salmonella
|
MAILGLGTDIVEIARIEAVISRSGERLARRVLSDNEWAIWETHQQPVRFLAKRFAVKEAAAKAFGTGIRNGLAFNQFEVFNDELGKPRLRLWGEALTLAEKLGVAHMHVTLADERHYACATVILES
|
Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
|
B5FRC1
|
Q8E7X6
|
RECO_STRA3
|
Recombination protein O
|
Streptococcus
|
MRVSQTYGLVLYNRNYREDDKLVKIFTETEGKRMFFVKHASKSKFNAVLQPLTIAHFILKINDNGLSYIDDYKEVLAFQETNSDLFKLSYASYITSLADVAISDNVADAQLFIFLKKTLELIEDGLDYEILTNIFEVQLLERFGVALNFHDCVFCHRVGLPFDFSHKYSGLLCPNHYYKDERRNHLDPNMLYLINRFQSIQFDDLQTISVKPEMKLKIRQFLDMIYDEYVGIHLKSKKFIDDLSSWGSIMKSD
|
Involved in DNA repair and RecF pathway recombination.
|
Q8E7X6
|
Q4KC13
|
UPPP_PSEF5
|
Undecaprenyl pyrophosphate phosphatase
|
Pseudomonas
|
MDLWTAAQALILGIVEGLTEFLPISSTGHQIIVADLLDFGGERAMAFNIIIQLGAILAVVWEFRRKILDVVIGLPTQPKAQRFTINLLIAFLPAVVLGVIFADLIHAYLFNPITVATALVVGGLIMLWAERRQHQVHAETVDDITWKDALKVGCAQCLAMIPGTSRSGSTIIGGLLFGLSRKTATEFSFFLAMPTMVGAAVYSGYKYRHLFQPDDFPVFAIGFVTAFVFAMIAVKGLLKFIASHSYAAFAWYRIAFGLLILATWQFGWVDWTAAKP
|
Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
|
Q4KC13
|
Q057V1
|
RNT_BUCCC
|
Exoribonuclease T
|
Buchnera
|
MFIYKDINYAINNRFRGFYPVVIDIESAGFQADTDALLEIAIVTLKMNKSGWLKIDDRLHFHIIPFKGSIIKAESVAFNKIDPFNPLRGAVSEKNALKNIFKLVRKKININKCRKGILVAHNANFDHNFLMAASKRVGNLNNPFHPFTTFDTAALSGLIFGQTVLAKACKLAGIPFDTNQAHSALYDTIQTAYLFCELVNRWKRLGGWPPNSSHRKKTDEI
|
Trims short 3' overhangs of a variety of RNA species, leaving a one or two nucleotide 3' overhang. Responsible for the end-turnover of tRNA: specifically removes the terminal AMP residue from uncharged tRNA (tRNA-C-C-A). Also appears to be involved in tRNA biosynthesis.
|
Q057V1
|
Q5LY40
|
MUTS2_STRT1
|
Endonuclease MutS2
|
Streptococcus
|
MNTKILDQLEFNKVKDQFTEYLQTEQAQAELCDLVPMTNPERIQNQFTEIQEMSEIFVEHHGFAIGSLRDISEPLRRLELDADLNIQELIAIKKVLQASADLSRFYADLENVELIALKRLFEKIEAFPSLQGSLQSINDGGFIEHFASPELQNIRRQLKACDDAIRQTLQDILKKSGHMLAENLIASRNGRSVLPVKNTYRNRIAGVVHDISSSGNTVYIEPRAVIQLNEKITQLRADERHEMARILHELSDQLRPHTAAIANNAWILGHMDFIRGKYLYLHDKKAIIPEISDNQTLQLLNVRHPLLINPVANDLRFDEDLTVIVITGPNTGGKTVMLKTLGLAQLMAQSGLPILADKGSRVAIFQEIFADIGDEQSIEQSLSTFSSHMTHIVEILNTADSNSLVLVDELGAGTDPQEGASLAMAILEHLRLSQIKTMATTHYPELKAYGIETQHVENASMEFDTATLRPTYRFMQGVPGRSNAFEIARRLGLNEIIVKEAENLTDTDSDVNRIIEQLEAQTVETQKRLEHIKDVEQENLKFNRAVKKLYNEFSHEYDKELEKAQKEIQEMVDTALAESDSILKNLHDKSQLKPHEVIDAKGKLKKLAAQVDLSKNKVLRKAKKEKAARAPRVGDDIIVTAYGQRGTLTSQAKNGNWEAQVGLIKMSLKADEFTLVRTQAEAQQPKKKQINVVKKAKKTSSDGPRARLDLRGKRYEEAMQELDAFIDQALLNNMSQVEIIHGIGTGVIRDAVTKYLRRHRHVKNFEYAPQSAGGSGCTIATLG
|
Endonuclease that is involved in the suppression of homologous recombination and may therefore have a key role in the control of bacterial genetic diversity.
|
Q5LY40
|
P49660
|
SSR4_MOUSE
|
Somatostatin receptor type 4
|
Mus
|
MNAPATLPPGVEDTTWTPGINASWAPDEEEEDAMGSDGTGTAGMVTIQCIYALVCLVGLVGNALVIFVILRYAKMKTATNIYLLNLAVADELFMLSVPFARSAAALRHWPFGAVLCRAVLSVDGLNMFTSVFCLTVLSVDRYVAVVHPLATATYRRPSVAKLINLGVWLASLLVTLPIAVFADTRPARGGEAVACNLHWPHPAWSAVFVIYTFLLGFLPPVLAIGLCYLLIVGKMRAVALAGGWQQRRRSEKKITRLVLMVVTVFVLCWMPFYVVQLLNLFVTSLDATVNHVSLILSYANSCANPILYGFLSDNFRRSFQRVLCLRCCLLETTGGAEEEPLDYYATALKSRGGAGCICPPLPCQQEPVQAEPGCKQVPFTKTTTF
|
Receptor for somatostatin-14. The activity of this receptor is mediated by G proteins which inhibits adenylyl cyclase. It is functionally coupled not only to inhibition of adenylate cyclase, but also to activation of both arachidonate release and mitogen-activated protein (MAP) kinase cascade.
|
P49660
|
Q46AR1
|
THI4_METBF
|
Thiamine thiazole synthase
|
Methanosarcina
|
MELDEVIITRAIFDEYSKTFLDYTEVDVALIGGGPANLVAARYLAEAGAKVAIYEQKLSLGGGMWAGGMMFPRIVVQEEACRILDDFGIRYKEYQPGYYVANSVESVGKLISGATSAGAEVFNLVSFEDVMIRENDRVTGIVVNWGPVTVQRLHVDPLMIRTKLVIDGTGHEAVVCNTILRKIPNAKIGNLGKLGEKPMWSEVGEQLVVDATKEIYPGLIVAGMAANAATCSPRMGPVFGGMLLSGEKAAKLALEKLKEL
|
Involved in the biosynthesis of the thiazole moiety of thiamine. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylate (ADT), an adenylated thiazole intermediate, using free sulfide as a source of sulfur.
|
Q46AR1
|
P43429
|
GATA1_RAT
|
NF-E1 DNA-binding protein
|
Rattus
|
MDFPGLGALGTSEPLPQFVDSALVSSTSDSAGFFSSGPESLDTASSSTSPNAATAAATALAYYREAEAYRHSPVFQVYPLLNSMEGIPGSSPYASWAYSKTALYPASTVCPSHEDAPSQTLEDPDGKNNNTFLETLKTERLSPDLLTLGTALPTSLPVTSSAYGGADFPSPFFSPTGSPLSSAAYSSPKFHGSLPLAPCEARECVNCGATATPLWRRDRTGHYLCNACGLYHKMNGQNRPLIRPKKRMIVSKRAGTQCTNCQTTTTTLWRRNASGDPVCNACGLYYKLHQVNRPLTMRKDGIQTRNRKASGKGKKKRGSSLAGAGAAEGPAGGFMVVAGGSSSGNCGEVAPGLTLGTAGTAHLYQGLGPVVLSGPVSHLMSFPGPLLGSPTASFPTGPVPTTTSTSVVSPLSS
|
Transcriptional activator or repressor which probably serves as a general switch factor for erythroid development. It binds to DNA sites with the consensus sequence 5'-[AT]GATA[AG]-3' within regulatory regions of globin genes and of other genes expressed in erythroid cells. Activates the transcription of genes involved in erythroid differentiation of K562 erythroleukemia cells, including HBB, HBG1/2, ALAS2 and HMBS.
|
P43429
|
B4RBX8
|
SYE_PHEZH
|
Glutamyl-tRNA synthetase
|
Phenylobacterium
|
MPDRPVRTRIAPSPTGMMHIGTARTALFNWLYARHTGGKFLLRIEDTDRERSTDEAVKVIFDGLKWLGLDADEPPVFQFARADRHREAAETLLARGGAYRDYMTPEELEAEREVARAEGRVVRSPWRDASPNDAPDRPFVVRLKAPQEGETVIQDAVKGEVRFQNKQLDDLILLRTDGTPTYNLAVVVDDHDMGVTHVIRGDDHLNNAARQTLIYQGLGWEVPVWAHLPLIHGPDGAKLSKRHGAQAVSEFDSMGYLPETMRNYLAKLGWGHGDDEIFSDEQAIAWFDINDVVSAPARLDWAKLNHLNNHYIRQAEPARLAELVKTVLASRDWPLEAGDMAVIERTIPFVRDGAKTTLELADNVVFALKRRPLELPEKTRTQMTEELRGRLSRLREALAAVEYWDVPSLEAALRAFAEAEGVGLGKFGPQLRAVLSGGAPAPDLAGAMVALTRDESLGRLDDALSPSA
|
Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
|
B4RBX8
|
P45062
|
MRAY_HAEIN
|
UDP-MurNAc-pentapeptide phosphotransferase
|
Haemophilus
|
MLVWLAEYLVRYETAFNAISYITVRANLALLTALFISLWIGPKVIKRLQILKFGQEVRNDGPESHFAKKGTPTMGGVMILFSIGVSTLLWANLANPYIWVCLFVLFGYGAIGFVDDFRKITRKNTDGLIARWKYFWMSVVALVAILWLYWLGHDTDATRLVIPFFKDIMPQLGLFYIVLSYFVIVGTGNAVNLTDGLDGLAIMPTALVAGAFALIAWATGNVNFAEYLHIPYIKYSSEVVVFCTAIVGASLGFLWFNTYPAQVFMGDVGSLALGGALGVVAILVRQEFLLVIMGGVFVVEALSVILQVGSYKLRKQRIFRMAPIHHHFELKGWPEPRVIIRFWIISLMLVLMGLVTLKLR
|
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.
|
P45062
|
Q747Q5
|
NADD_GEOSL
|
Nicotinate mononucleotide adenylyltransferase
|
Geobacter
|
MKTGILGGTFNPVHVAHLRIAEEVRDTFALDRVLFIPAASPPHKAMEGEVPFETRCAMVRLATADNHAFAVSDMEGGRPGKSYSVDTIRALKEEYPGDEFFFIIGSDSFLDIGSWYDYEAIFASCNLVVAARPGAEAADLLAALPVAITAQFCYYPAEKRLAHRSGYSVYWLAGVPLDISSRSIRGLARLGRSIRYLVPEAVERYINEQRIYAHDG
|
Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
|
Q747Q5
|
Q04RD6
|
MTNA_LEPBJ
|
S-methyl-5-thioribose-1-phosphate isomerase
|
Leptospira
|
MQESGLKPILWTNKELILLDQRVLPGTTSYLKAKTLEDCIFAIREMVVRGAPAIAITGAFGIALYLNGLSSQPTFSQLKTKLDELLESRPTAVNLRLVIEEFFSRFPEADYSSANLEKMQKSAEEFALFMLEEDLENNLTLSKNALSLFPKSPSSLNIITHCNTGALATAGHGTALGVIRSLRDAGHSLTVFADETRPYLQGARLTAWELKEEGIPSYLITDNMAGWVMSSRKIHAVIVGADRIASNGDTANKIGTYPLAIIAKHHGVPFYVAATSKSMDFRIPDGSHIPIEMRKENEVTSFGFLKDATGKPLLNEGVLAPNGIKALNPSFDVTPASLISGIITERGIISPVTEENLRKTFS
|
Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
|
Q04RD6
|
B7MAV5
|
ASTE_ECO45
|
Succinylglutamate desuccinylase
|
Escherichia
|
MDNFLALTLTGKKPVITEREINGVRWRWLGDGVLELTPLTPPQGVLVISAGIHGNETAPVEMLDALLGAISHGEIPLRWRLLVILGNPPALKQGKRYCHSDMNRMFGGRWQLFAESGETCRARELEQCLEDFYDQGKESVRWHLDLHTAIRGSLHPQFGVLPQRDIPWDEKFLTWLGAAGLEALVFHQEPGGTFTHFSARHFGALACTLELGKALPFGQNDLRQFAVTASAIAALLSGESVGIVRTPPLRYRVVSQITRHSPSFEMHMANDTLNFMPFEKGTLLAQDGEERFTVTHDVEYVLFPNPLVALGLRAGLMLEKIS
|
Transforms N(2)-succinylglutamate into succinate and glutamate.
|
B7MAV5
|
P21988
|
FLA1_TREPH
|
Class B
|
Treponema
|
MIINHNMSAMFAQRTLGVTNNAIGKDME
|
Component of the core of the flagella.
|
P21988
|
Q90679
|
THYN1_CHICK
|
Thymocyte protein Thy28
|
Gallus
|
MPWPSRKRDKGAVADKKEPDAKIAKTEEETEDKEEEEKSTKPPAGSSKSGLKNWKKAKESDSGGEESKITYCHWLLKSEPESRLEKGVDVKFSIEDLKAQPNQTTFWEGVRNYQARNFLRAMKLGQQAFFYHSNCKEPGIVGIVKIVKEAYPDHTQFDQKDPHYDSSSRKENPKWSMVDVQFVRMTKRFIPLSEIKTHHLAHKADGGPLKNMMLFSRQRLSIQPLTQEEFDFVLSLEEEKPH
|
Specifically binds 5-hydroxymethylcytosine (5hmC), suggesting that it acts as a specific reader of 5hmC.
|
Q90679
|
P83572
|
ARALA_ARAEL
|
rRNA N-glycosidase
|
Aralia
|
ANFPTVSLNTVGITRQIPQDFMNAV
|
Toxic type II ribosome-inactivating protein (RIP). Induces apoptosis. Has cytotoxic activity against several human cancer cell lines. Is less cytotoxic to normal human cells.
|
P83572
|
B2IN14
|
DAPEL_STRPS
|
N-acetyldiaminopimelate deacetylase
|
Streptococcus
|
MLDLIQTRRALHQIPEIGLEEFKTQAYLLDVIEKLTTGKDFVQIRTWRTGILVYLQGSQPERTIGWRTDIDGLPIVEQTGLPFASQHQGRMHACGHDFHMTIALGCLERALEEQPKNNLLFLFQPAEENEAGGMLMYEDGAFGDWLPNQFYGLHVRPDLKVGQIATNTHTLFAGTCEVKIRFKGKGGHAAFPHEANDALVAASYFVTQVQSVVSRNVNPIEGAVVTFGVFQAGTTNNVITDTAFLHGTIRALTQDMSLLVQKRVKTVAEGVAAAFDMEVEVELKQGGYLPVENNPALARELMDFFDEKDGIELIDIEPAMTGEDFGYLLSKVDGVMFWLGIDSPYALHHPQMSPKEEVLAIGVAAVSSFLKKKAAE
|
Catalyzes the conversion of N-acetyl-diaminopimelate to diaminopimelate and acetate.
|
B2IN14
|
A0AVF1
|
IFT56_HUMAN
|
Tetratricopeptide repeat protein 26
|
Homo
|
MMLSRAKPAVGRGVQHTDKRKKKGRKIPKLEELLSKRDFTGAITLLEFKRHVGEEEEDTNLWIGYCAFHLGDYKRALEEYENATKEENCNSEVWVNLACTYFFLGMYKQAEAAGFKASKSRLQNRLLFHLAHKFNDEKKLMSFHQNLQDVTEDQLSLASIHYMRSHYQEAIDIYKRILLDNREYLALNVYVALCYYKLDYYDVSQEVLAVYLQQIPDSTIALNLKACNHFRLYNGRAAEAELKSLMDNASSSFEFAKELIRHNLVVFRGGEGALQVLPPLVDVIPEARLNLVIYYLRQDDVQEAYNLIKDLEPTTPQEYILKGVVNAALGQEMGSRDHMKIAQQFFQLVGGSASECDTIPGRQCMASCFFLLKQFDDVLIYLNSFKSYFYNDDIFNFNYAQAKAATGNTSEGEEAFLLIQSEKMKNDYIYLSWLARCYIMNKKPRLAWELYLKMETSGESFSLLQLIANDCYKMGQFYYSAKAFDVLERLDPNPEYWEGKRGACVGIFQMIIAGREPKETLREVLHLLRSTGNTQVEYMIRIMKKWAKENRVSI
|
Component of the intraflagellar transport (IFT) complex B required for transport of proteins in the motile cilium. Required for transport of specific ciliary cargo proteins related to motility, while it is neither required for IFT complex B assembly or motion nor for cilium assembly. Required for efficient coupling between the accumulation of GLI2 and GLI3 at the ciliary tips and their dissociation from the negative regulator SUFU. Plays a key role in maintaining the integrity of the IFT complex B and the proper ciliary localization of the IFT complex B components. Not required for IFT complex A ciliary localization or function. Essential for maintaining proper microtubule organization within the ciliary axoneme.
|
A0AVF1
|
O57864
|
CDC6_PYRHO
|
ORC1-type DNA replication protein
|
Pyrococcus
|
MNEGEQLHLDQLFEKLLKARKIFKNKEVLRHSYTPKDLPHRHEQIETLAQILVPVLKGETPSNIFVYGKTGTGKTVTVKFVTEELKKVSHKYNIPVDVIYINCEIVDTHYRVLANIVNHFKHETGIEVPLVGWPTDEVYAKLKQVIDMRERFVIIVLDEIDKLVKKSGDEVLYSLTRINTELKRAKVSVIGISNDLKFKEYLDPRVLSSLSEEEVVFPPYDANQLRDILMQRAEEAFYPGVLDDGVIPLCAALAAREHGDARKALDLLRVAGEIAEREGASKVTEKHVWKAQEKIEQDMMEEVIKTLPLQSKVLLYAIVLLDENGELPANTGEVYSVYRDLCEYLDLEPLTQRRISDLINELDMLGIINAKVVSKGRYGRTKEIRLNVTPYKIRNVFRYDYTIQPLLAISLKDSQRRLV
|
Involved in regulation of DNA replication.
|
O57864
|
A3D9I1
|
YACG_SHEB5
|
DNA gyrase inhibitor YacG
|
Shewanella
|
MPLTVKCPICKAPVEWVPQSAFKPFCSERCKLIDLGDWASEKHVIPVKAEFDPEAFDEFDLDEGDFFKE
|
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.
|
A3D9I1
|
A1JML7
|
TUS_YERE8
|
DNA replication terminus site-binding protein
|
Yersinia
|
MNKYDLIERLNNRFTALEAGLQALHQQLEDLPLLAARVFSLPEIEKGTEHQPIMHIPVNATVGAAARDLAIQHYQRLFIHHQGQNVSSKAALRLPGVLCFSVTESQLATCQKSIQHINQLKTELEHIITVESGLPSEQRFEFVHTHLHGLITLNTYRTITPLINPSSVRFGWANKHIIKNVTREDVLAQLNKSLNAGRAVPPFSREQWVELISQEINDVQRLPEQARLKIKRPVKVQPIARVWYQEQQKQVQHPCPMPLIAFCQLQSAAELPKLGELTDYDANQIKHKYKPDAKPLQLLVPRLHLYLEI
|
Trans-acting protein required for termination of DNA replication. Binds to DNA replication terminator sequences (terA to terF) to prevent the passage of replication forks. The termination efficiency will be affected by the affinity of this protein for the terminator sequence.
|
A1JML7
|
Q8TQR2
|
DNAK_METAC
|
Heat shock protein 70
|
Methanosarcina
|
MAKILGIDLGTTNSCMAVMEGGDAVVLPNAEGSRTTPSVVGFSKKGEKLVGQVAKRQAISNPENTVYSIKRHMGEANYKVTLNGKTYTPQEISAMILQKLKTEAEAYLGETIKQAVITVPAYFNDAQRQATKDAGSIAGLEVLRIINEPTAASLAYGLDKGDVDQKILVYDLGGGTFDVSILELGGGVFEVKSTSGDTHLGGDDFDQRVIDHLLAEFKKTEGIDLSKDKAILQRLKDAAEKAKIELSGVTVTNINLPFLTVGPDGEPKHMDIDLTRAQFQKMTEDLLEKTLVSMRRALSDSKLTPNDLDKVILVGGATRMPAVVELVENFTGKKPYKNINPDEAVAIGAAIQAGVLGGEVKDVLLLDVTPLTLGIETLGGIATPLIQRNTTIPTKKSQIFSTAADNQPSVEIHVLQGERGIASENKTLGRFTLDGIPPAPRGIPQIEVAFDIDANGILHVNAKDLGTGKEQSISIQKPGGLSDAEIERMVKDAELHAEEDKKRKEEVETRNNAEALINAAEKTIKEAGDVATEDQKSKVNAAIEDLKKALEGKDTEEVKAKTEALQEAVYPISTAMYQKAQQEAQQASGEAGSADARGPDETVVDADYEVVDDEKRK
|
Acts as a chaperone.
|
Q8TQR2
|
A0A0B5ABE6
|
INS1A_CONQU
|
Con-Ins Q1 A chain
|
Lividoconus
|
MTTSSYFLLVALGLLLYLCQSSFGTEHTCEPGASPHPQGKCRPELAEFHETMCEVEESLQGGTDDARKKRGRASLLRKRRGFLSMLKARAKRNEASPLPRAGRGIVCECCKNSCTYEEITEYCPPVTEGSG
|
This venom insulin facilitates prey capture by rapidly inducing hypoglycemic shock. Intraperitoneal injection of this peptide into zebrafish lowers blood glucose with the same potency than human insulin. In vivo, when applied to water, this peptide reduces overall locomotor activity of zebrafish larvae, observed as a significant decrease in the percentage of time spent swimming and movement frequency.
|
A0A0B5ABE6
|
P11983
|
TCPA_MOUSE
|
Tailless complex polypeptide 1B
|
Mus
|
MEGPLSVFGDRSTGEAVRSQNVMAAASIANIVKSSFGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYINENLIINTDELGRDCLINAAKTSMSSKIIGINGDYFANMVVDAVLAVKYTDARGQPRYPVNSVNILKAHGRSQIESMLINGYALNCVVGSQGMPKRIVNAKIACLDFSLQKTKMKLGVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGIDDMYLKYFVEAGAMAVRRVLKRDLKHVAKASGASILSTLANLEGEETFEVTMLGQAEEVVQERICDDELILIKNTKARTSASIILRGANDFMCDEMERSLHDALCVVKRVLELKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNEAQVNPERKNLKWIGLDLVHGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLIKLHPESKDDKHGSYENAVHSGALDD
|
Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin.
|
P11983
|
A4SUY4
|
RS11_POLAQ
|
30S ribosomal protein S11
|
Polynucleobacter
|
MAKQQSASAASQRARKKVKKNVADGIAHVHASFNNTIITITDRQGNALSWATSGGQGFKGSRKSTPFAAQVAAEVAGKAAVECGIKNLEVQIKGPGPGRESAVRALNSLGIKITEIQDVTPVPHNGCRPPKRRRI
|
Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome.
|
A4SUY4
|
Q9NS56
|
TOPRS_HUMAN
|
Tumor suppressor p53-binding protein 3
|
Homo
|
MGSQPPLGSPLSREEGEAPPPAPASEGRRRSRRVRLRGSCRHRPSFLGCRELAASAPARPAPASSEIMASAAKEFKMDNFSPKAGTSKLQQTVPADASPDSKCPICLDRFDNVSYLDRCLHKFCFRCVQEWSKNKAECPLCKQPFDSIFHSVRAEDDFKEYVLRPSYNGSFVTPDRRFRYRTTLTRERNASVYSPSGPVNRRTTTPPDSGVLFEGLGISTRPRDVEIPQFMRQIAVRRPTTADERSLRKIQEQDIINFRRTLYRAGARVRNIEDGGRYRDISAEFFRRNPACLHRLVPWLKRELTVLFGAHGSLVNIVQHIIMSNVTRYDLESQAFVSDLRPFLLNRTEHFIHEFISFARSPFNMAAFDQHANYDCPAPSYEEGSHSDSSVITISPDEAETQELDINVATVSQAPWDDETPGPSYSSSEQVHVTMSSLLNTSDSSDEELVTGGATSQIQGVQTNDDLNNDSDDSSDNCVIVGFVKPLAERTPELVELSSDSEDLGSYEKMETVKTQEQEQSYSSGDSDVSRCSSPHSVLGKDEQINKGHCDSSTRIKSKKEEKRSTSLSSPRNLNSSVRGDRVYSPYNHRHRKRGRSRSSDSRSQSRSGHDQKNHRKHHGKKRMKSKRSRSRESSRPRGRRDKKRSRTRDSSWSRRSQTLSLSSESTSRSRSRSSDHGKRRSRSRNRDRYYLRNNYGSRYKWEYTYYSRNKDRDGYESSYRRRTLSRAHYSRQSSSPEFRVQSFSERTNARKKNNHSERKYYYYERHRSRSLSSNRSRTASTGTDRVRNEKPGGKRKYKTRHLEGTNEVAQPSREFASKAKDSHYQKSSSKLDGNYKNESDTFSDSRSSDRETKHKRRKRKTRSLSVEIVYEGKATDTTKHHKKKKKKHKKKHKKHHGDNASRSPVVITIDSDSDKDSEVKEDTECDNSGPQDPLQNEFLAPSLEPFETKDVVTIEAEFGVLDKECDIATLSNNLNNANKTVDNIPPLAASVEQTLDVREESTFVSDLENQPSNIVSLQTEPSRQLPSPRTSLMSVCLGRDCDMS
|
Functions as an E3 ubiquitin-protein ligase and as an E3 SUMO1-protein ligase. Probable tumor suppressor involved in cell growth, cell proliferation and apoptosis that regulates p53/TP53 stability through ubiquitin-dependent degradation. May regulate chromatin modification through sumoylation of several chromatin modification-associated proteins. May be involved in DNA damage-induced cell death through IKBKE sumoylation.
|
Q9NS56
|
P27589
|
PETD_SYNY3
|
17 kDa polypeptide
|
unclassified Synechocystis
|
MSIIKKPDLSDPDLRAKLAKGMGHNYYGEPAWPNDILYMFPICILGALGLIAGLAILDPAMIGEPADPFATPLEILPEWYLYPTFQILRILPNKLLGIAGMAAIPLGLMLVPFIESVNKFQNPFRRPIAMTVFLFGTAAALWLGAGATFPIDKSLTLGLF
|
Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
|
P27589
|
Q8DGC6
|
CHLB_THEVB
|
Light-independent protochlorophyllide reductase subunit B
|
Thermosynechococcus
|
MKLAYWMYAGPAHIGTLRIASSFKNVHGIMHAPLGDDYFNVMRSMLERERDFTPVTASIVDRHVLARGSQEKVVDNIIRKDTEEHPDLIVLTPTCTSSILQEDLQNFVRRASLSTTADVLLADVNHYRVNELQAADRTLEQIVQFYIDKARRQGTLGTSKTPTPSVNIIGITTLGFHNQHDCRELKQLMADLGIQVNLVIPAAATVHDLQRLPQAWFNLVPYREIGGLTAQYLEREFGQPSVRITPMGVVETARCIRAIQGVLNAQGAGVNYEAFIEQQTREVSQAAWFSRSIDCQNLTGKKAVVFGDNTHAAAMTKILSREMGIHVVWAGTYCKYDADWFRAEVAGFCDEVLITDDHTVVGDAIARVEPAAIFGTQMERHVGKRLNIPCGVIAAPIHIQDFPVGYRPFLGYEGTNQLVDLIYNSFTLGMEDHLLEIFGGHDTKAVIHKGLSADSDLTWTAAGLAELNKIPGFVRGKVKRNTEKFAREQGISEITVEVLYAAKEAVGA
|
Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex.
|
Q8DGC6
|
Q8DTE5
|
CAS2_STRMU
|
CRISPR-associated endoribonuclease Cas2
|
Streptococcus
|
MRMILMFDMPTDTAEERKAYRKFRKFLLSEGFIMHQFSVYSKLLLNNSANTAMIARLKENNPKKGNITLLTVTEKQFARMIYLNGERDTSIANSDSRLVFLGEAFPDET
|
CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease. Involved in the integration of spacer DNA into the CRISPR cassette.
|
Q8DTE5
|
Q07Y78
|
HLDE_SHEFN
|
D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase
|
Shewanella
|
MKVSLPAFENARVLVIGDVMLDRYWVGPTGRISPEAPVPVVKINQIEDRPGGAANVALNIATLGGHVQLAGIVGQDETAQALTQGVKVFGVEPQWLTVADKPTITKLRVLSRNQQLIRLDFEEQFDKATSQALFAQSEAILDNVDVLVLSDYAKGAIDEPKDFIAKARAKGVKVLVDPKGHDFARYHGASLITPNMSEFEAVVGTVTSEDDLIEKAQKLIKLHDFEAILVTRSEKGMTLVSQNQPELHIPTVAREVHDVTGAGDTVISALATSIAAGASLAQACAIANTAAGVVVGKLGTSTVSRIELIQALALNHGESGFGVMTEDQLAYAMDQARLRGERIVMTNGCFDILHAGHVSYLQQAKALGDRLIVAVNDDSSVTRLKGPGRPVNPVDRRMAVLAGLASVDWVVPFTEDTPQRIITRLLPDSLVKGGDYKVEDIAGGAEVIAAGGKVEVLGFEDGVSTTAIIQNIMSQK
|
Catalyzes the ADP transfer from ATP to D-glycero-beta-D-manno-heptose 1-phosphate, yielding ADP-D-glycero-beta-D-manno-heptose.
|
Q07Y78
|
A7GD48
|
MURQ_CLOBL
|
N-acetylmuramic acid 6-phosphate lyase
|
Clostridium
|
MTNISLDKLVTESRNENTKDIDRVETLEMLKMINDEDKKVAEAVEKELIHIAKAVDKIGESFLNGGRLIYVGAGTSGRLGVLDASECPPTYGVSYDLVRGIIAGGESAMFKAREGAEDSKKLCIKDLKNINFGKNDILVGIAASGRTPYVIGGLEYANGIGATTISVTCNPESEMSKIANISIAPVVGPEAITGSTRMKAGTAQKMVLNMLSTGAMVKTGKVYGNLMVDLKATNEKLVERAKRIVMQATGSKREQVEKILKETNFDVKLSIFMIESSLDKIKAKEILDKNKGYIVEAIKEIS
|
Specifically catalyzes the cleavage of the D-lactyl ether substituent of MurNAc 6-phosphate, producing GlcNAc 6-phosphate and D-lactate.
|
A7GD48
|
Q8WVJ2
|
NUDC2_HUMAN
|
NudC domain-containing protein 2
|
Homo
|
MSAPFEERSGVVPCGTPWGQWYQTLEEVFIEVQVPPGTRAQDIQCGLQSRHVALSVGGREILKGKLFDSTIADEGTWTLEDRKMVRIVLTKTKRDAANCWTSLLESEYAADPWVQDQMQRKLTLERFQKENPGFDFSGAEISGNYTKGGPDFSNLEK
|
May regulate the LIS1/dynein pathway by stabilizing LIS1 with Hsp90 chaperone.
|
Q8WVJ2
|
Q6F880
|
TILS_ACIAD
|
tRNA(Ile)-lysidine synthetase
|
Acinetobacter
|
MRSALPTFDEIWQRKFRHRLLIQAQQFPADTVFLIGCSGGMDSMLLLHLMSELFPHKVRAIYIDHQLQSSSRAWGVFVQNFAQQSHIPFTIQPVIVDTGNLENQAREARYAAFESHLKSNEVLVLAHHQQDQTETVLLRLLSGSGVKGLGAMKEIEQKKNICCWRPMLSVSRQQIEHWVEHLKIPYIQDLTNFDTTYDRAWCRETVWPVLQKRFPKMQEAISRTSILMQDADEILHEVLQQDLNQCGDLNHLDLSRLQQLSLARQRQLLSFWMKGKAIYRPAFEMVERVQQEVICAKADAKAALHWNHHYYVRYQNILYRVEKNKYLQKDLVSNVVSTIELQMDASLQLASGVFQIQPMQMGLSPQLFEQPLQLLPRQGGEKIHLYGRVGHWPLKKAIQEAQILPWLRHTIQILALDNVMLGVFTPKGFWLAQSSYCEAGGWQPNLISDVNYLRVEQNS
|
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.
|
Q6F880
|
Q17ZB7
|
RS13_HELAH
|
30S ribosomal protein S13
|
Helicobacter
|
MARIAGVDLPKKKRVEYALTYIYGIGLKSSREILEAVGISFDKRVHELSEDEASSIAKKIQQSYLVEGDLRKKVQMDIKSLMDLGNYRGIRHRKGLPVRGQTTKNNARTRKGKKKTVGSK
|
Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites.
|
Q17ZB7
|
Q97QN5
|
NORM_STRPN
|
Multidrug-efflux transporter
|
Streptococcus
|
MYKTKCLREKLVLFLKIFFPILIYQFANYSASFVDTAMTGQYNTMDLAGVSMATSIWNPFFTFLTGIVSALVPIIGHHLGRGKKEEVASDFYQFIYLALGLSVVLLGMVLFLAPIILNHIGLEAAVAAVAVRYLWFLSIGIIPLLLFSVIRSLLDSLGLTKLSMYLMLLLLPLNSGFNYLLIYGAFGVPELGGAGAGLGTSLAYWVLLGISVLVLFKQEKLKALHLEKRIPLNMDKIKEGVRLGLPIGGTVFAEVAIFSVVGLIMAKFSPLIIASHQSAMNFSSLMYAFPMSISSAMAIVVSYEVGAKRFDDAKTYIGLGRWTALIFAAFTLTFLYIFRGNVASLYGNDPKFIDLTVRFLTYSLFFQLADTFAAPLQGILRGYKDTVIPFYLGLLGYWGVAIPVRTLFDSLTDFGAYSYWIGLIISLIVSGALYRWRLTVIMKRFESLAKSKC
|
Multidrug efflux pump.
|
Q97QN5
|
Q8YP49
|
DXR_NOSS1
|
2-C-methyl-D-erythritol 4-phosphate synthase
|
Nostoc
|
MVKSITLVGSTGSIGTQTLDIVSQYPDQFRIVGLAAGSNVEMLAEQIRQFRPQIAAISAAEKLPALQAAIKDLDPQPILLGGEAGVIEVARYGDAETVVTGIVGCAGLLPTIAAIEAGKDIALANKETLIAGGPVVLPLVEKHGVKLLPADSEHSAIFQCLQGVPKGGLKKILLTASGGAFRDWDVERLAEVTVSDALKHPNWSMGRKITVDSATLMNKGLEVIEAHFLFGLDYQDIEIVIHPQSIIHSLIELQDTSVLAQLGWPDMRLPLLYALSWPERIYTDWERLNLVKAGNLTFREPDHQKYPCMQLAYAAGRAGGSMPAVLNAANEQVVALFLDEKIKFLDIPRCIELVCDRHQNDNCANPSLDDILAADQWARQEVLTATKNLASQPQIISVN
|
Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).
|
Q8YP49
|
Q8CRP5
|
DDL_STAES
|
D-alanylalanine synthetase
|
Staphylococcus
|
MTKENICIVFGGKSAEHDVSILTAQNVLNAIDKERYQVDIIYITNDGEWKKKDNITQEIKNTDELVINDVETGEISQLLSKGSLGKSYDAVFPLLHGPNGEDGTIQGLFEVLDIPYVGNGVLAASSSMDKLVMKQLFEHRGLPQLPYISFLRSEYEKYENNIIKLVNDKLTYPVFVKPANLGSSVGISKCNNEEELKSGITEAFQFDRKLVIEQGINAREIEVAVLGNDYPETTWPGEVVKDVAFYDYKSKYKDGKIRLDIPADLDQDVQMTLRNMALEAFKATDCSGLVRADFFVTDDNQIYINETNAMPGFTAYSMYPNLWKNMGLSYPDLIAKLIDLAKERYEDKKKNKYKIDY
|
Cell wall formation.
|
Q8CRP5
|
Q9UBD6
|
RHCG_HUMAN
|
Tumor-related protein DRC2
|
Homo
|
MAWNTNLRWRLPLTCLLLQVIMVILFGVFVRYDFEADAHWWSERTHKNLSDMENEFYYRYPSFQDVHVMVFVGFGFLMTFLQRYGFSAVGFNFLLAAFGIQWALLMQGWFHFLQDRYIVVGVENLINADFCVASVCVAFGAVLGKVSPIQLLIMTFFQVTLFAVNEFILLNLLKVKDAGGSMTIHTFGAYFGLTVTRILYRRNLEQSKERQNSVYQSDLFAMIGTLFLWMYWPSFNSAISYHGDSQHRAAINTYCSLAACVLTSVAISSALHKKGKLDMVHIQNATLAGGVAVGTAAEMMLMPYGALIIGFVCGIISTLGFVYLTPFLESRLHIQDTCGINNLHGIPGIIGGIVGAVTAASASLEVYGKEGLVHSFDFQGFNGDWTARTQGKFQIYGLLVTLAMALMGGIIVGLILRLPFWGQPSDENCFEDAVYWEMPEGNSTVYIPEDPTFKPSGPSVPSVPMVSPLPMASSVPLVP
|
Functions as an electroneutral and bidirectional ammonium transporter. May regulate transepithelial ammonia secretion.
|
Q9UBD6
|
A0A075B6H7
|
KV37_HUMAN
|
Probable non-functional immunoglobulin kappa variable 3-7
|
Homo
|
MEAPAQLLFLLLLWLPDTTREIVMTQSPPTLSLSPGERVTLSCRASQSVSSSYLTWYQQKPGQAPRLLIYGASTRATSIPARFSGSGSGTDFTLTISSLQPEDFAVYYCQQDYNLP
|
Probable non-functional open reading frame (ORF) of V region of the variable domain of immunoglobulin light chains . Non-functional ORF generally cannot participate in the synthesis of a productive immunoglobulin chain due to altered V-(D)-J or switch recombination and/or splicing site (at mRNA level) and/or conserved amino acid change (protein level) . Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens . The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen .
|
A0A075B6H7
|
Q14149
|
MORC3_HUMAN
|
Zinc finger CW-type coiled-coil domain protein 3
|
Homo
|
MAAQPPRGIRLSALCPKFLHTNSTSHTWPFSAVAELIDNAYDPDVNAKQIWIDKTVINDHICLTFTDNGNGMTSDKLHKMLSFGFSDKVTMNGHVPVGLYGNGFKSGSMRLGKDAIVFTKNGESMSVGLLSQTYLEVIKAEHVVVPIVAFNKHRQMINLAESKASLAAILEHSLFSTEQKLLAELDAIIGKKGTRIIIWNLRSYKNATEFDFEKDKYDIRIPEDLDEITGKKGYKKQERMDQIAPESDYSLRAYCSILYLKPRMQIILRGQKVKTQLVSKSLAYIERDVYRPKFLSKTVRITFGFNCRNKDHYGIMMYHRNRLIKAYEKVGCQLRANNMGVGVVGIIECNFLKPTHNKQDFDYTNEYRLTITALGEKLNDYWNEMKVKKNTEYPLNLPVEDIQKRPDQTWVQCDACLKWRKLPDGMDQLPEKWYCSNNPDPQFRNCEVPEEPEDEDLVHPTYEKTYKKTNKEKFRIRQPEMIPRINAELLFRPTALSTPSFSSPKESVPRRHLSEGTNSYATRLLNNHQVPPQSEPESNSLKRRLSTRSSILNAKNRRLSSQFENSVYKGDDDDEDVIILEENSTPKPAVDHDIDMKSEQSHVEQGGVQVEFVGDSEPCGQTGSTSTSSSRCDQGNTAATQTEVPSLVVKKEETVEDEIDVRNDAVILPSCVEAEAKIHETQETTDKSADDAGCQLQELRNQLLLVTEEKENYKRQCHMFTDQIKVLQQRILEMNDKYVKKETCHQSTETDAVFLLESINGKSESPDHMVSQYQQALEEIERLKKQCSALQHVKAECSQCSNNESKSEMDEMAVQLDDVFRQLDKCSIERDQYKSEVELLEMEKSQIRSQCEELKTEVEQLKSTNQQTATDVSTSSNIEESVNHMDGESLKLRSLRVNVGQLLAMIVPDLDLQQVNYDVDVVDEILGQVVEQMSEISST
|
(Microbial infection) May be required for influenza A transcription during viral infection .
|
Q14149
|
A0JPW5
|
HIP19_ARATH
|
Heavy metal-associated isoprenylated plant protein 19
|
Arabidopsis
|
MTKDKKKKDNVRYMDVEFNVSMHCNDCERKIARVISKFKGVETFVTDMINHKVVVRGKIDPNKLLKKLKKKTGKRVKIVVKEEKGEESSKENENVLEIDMESICLGDQSMFGFCDWEMEKFMVFSDENVKAICSIS
|
Heavy-metal-binding protein.
|
A0JPW5
|
A0A1D8PQN0
|
RS28B_CANAL
|
40S ribosomal protein S28B
|
Candida
|
MDAKTPVTLAKVIKVLGRTGSRGGVTQVRVEFLEDASRTIVRNVKGPVRENDILCLMESEREARRLR
|
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
|
A0A1D8PQN0
|
Q8U158
|
RL24E_PYRFU
|
Large ribosomal subunit protein eL24
|
Pyrococcus
|
MARWNVCSYCGKPFEPGTGKMYVRNDGRVLFFCSRKCERYYFMGRNPRKLKWTKAYQEARLQRGGE
|
Binds to the 23S rRNA.
|
Q8U158
|
O66478
|
TATA2_AQUAE
|
Sec-independent protein translocase protein TatA 2
|
Aquifex
|
MFPGGISMTELIIILAVILLLFGAGRLPEAGRALGEGIRNFRKALSGETEVKEVKAEDVKTEERKEEKKEEKEKVEA
|
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.
|
O66478
|
Q2NTJ0
|
RUVC_SODGM
|
Holliday junction resolvase RuvC
|
Sodalis
|
MTVILGIDPGSRITGYGIVRQEGCKLTYLGSGCIRTKVDDLPARLKLIYAGVSEIITQFQPDCLAIEQVFMAKNADSALKLGQARGVAIVVAMNLDLPVFEYAARQVKQTVVGSGAAEKSQVQHMVRTLLKLPANPQADAADALAIAITHCHVSQNALRMGSGGLNLARGRLR
|
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.
|
Q2NTJ0
|
A5W9N5
|
CBPM_PSEP1
|
Chaperone modulatory protein CbpM
|
Pseudomonas
|
MSSTLIVQLDMRTLCQEADVTAECVIEIVEHGIVEPSGRTPEDWLFDDQAPLVTKRAVKLHQELELEWEGVALALELLQEVQQLRSENNMLKQRLGRFIQM
|
Interacts with CbpA and inhibits both the DnaJ-like co-chaperone activity and the DNA binding activity of CbpA. Together with CbpA, modulates the activity of the DnaK chaperone system. Does not inhibit the co-chaperone activity of DnaJ.
|
A5W9N5
|
Q57849
|
NK_METJA
|
Guanosine-inosine kinase
|
Methanocaldococcus
|
MGGKMEKITCVGHTALDYIFNVEKFPEPNTSIQIPSARKYYGGAAANTAVGIKKLGVNSELLSCVGYDFKNSGYERYLKNLDINISKLYYSEEEETPKAWIFTDKDNNQITFFLWGAAKHYKELNPPNFNTEIVHIATGDPEFNLKCAKKAYGNNLVSFDPGQDLPQYSKEMLLEIIEHTNFLFMNKHEFERASNLLNFEIDDYLERVDALIVTKGSKGSVIYTKDKKIEIPCIKAGKVIDPTGAGDSYRAGFLSAYVKGYDLEKCGLIGAATASFVVEAKGCQTNLPTWDKVVERLEKHRI
|
Catalyzes the phosphorylation of a wide range of nucleosides to yield nucleoside monophosphates. Shows the highest activity for inosine, guanosine and cytidine, but very poor kinase activity with adenosine, thymidine, uridine and xanthosine. ATP is the best phosphate donor, but can also use ITP and GTP. Shows extremely low activity with fructose-6-phosphate.
|
Q57849
|
Q7ZUH5
|
RM14_DANRE
|
39S ribosomal protein L14, mitochondrial
|
Danio
|
MALSLSGLILPKLMQQRAFSVSSAVSAIQKLTRVRVVDNSTLGNAHHHRPPKVIHVYNKNGVGKVGDRVLLAIKGQKKKAIIVGHKMPGARMTPRFDSNNVVLIEDNGNPTGTRIKAPLPTHLRKLEGEYSKLLAIAQRFV
|
May form part of 2 intersubunit bridges in the assembled ribosome. Upon binding to MALSU1, intersubunit bridge formation is blocked, preventing ribosome formation and repressing translation.
|
Q7ZUH5
|
Q93HU4
|
NHAP_APHHA
|
Sodium/proton antiporter ApNhaP
|
Aphanothece
|
MTIEAAMGEEAIKENLEQFLIVLSVSLGVATLSQISSFFRQIPYTLLLVIVGLGLAFVDIRLVNLSPELILEIFLPPLLFEAAWNIRWRNLKKNLFPVVLLAIIGVVISVVGIGFSLNYFSGLSLPIALLVGAILAATDPVSVIALFRELGVGERLTVLMEGESLFNDGVAVVAFSLLVGIPLGTQEFSVTNTLIQFVTLQGIGIGCGGVIGFGISYLTQRFDLPLVEQSLTLVSAYGTYLITEELGGSGVIGVVTVGLILGNFGSRIGMNPRTRLLVSEFWEFIAFFVNSIVFLLIGDQINIRGLADNGQLILITIIALVIIRAISIYGLGTISNLITKQDISWQEETVLWWGGLRGSVSIALALSVPVMLDGRQDIIEAVFGVVLFTLLVQGLTMQTVIEKLGLIGDRAQRRTYSELIARRSALERVLAHLNAVPPSPSIRMKSLKTTKEASKGQLESRQTKKLRSYNNSYPQLRSLEQEQLRELTFKVEADTYAELIRAGKLNNNLSPLLQEVLAKPE
|
Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons. Shows also high Ca(2+)/H(+) antiporter activity at alkaline pH. Does not catalyze exchange between Li(+) and H(+).
|
Q93HU4
|
B7GUP8
|
FMT_BIFLS
|
Methionyl-tRNA formyltransferase
|
Bifidobacterium
|
MLKLVFAGTPDVAVPSLKAFATDPRFDVVGVITRPDAPTGRGRKLTPSPVKAKALELGLPVIDLKPRSPEFMEALNDLHADIAAVIAYGNILPKNVLDAVPMGWYNLHFSNLPKWRGAAPAQRAIWAGDPTTGADVFKVGEGLDDGPIVASLTIELTGRETSGELLDRLAEEGAPMYVDALAAVGEGTATFTAQPAECLEYAHKITVEDARISWTDEAGAIDRQIRACTPHPGAWTELFAEGPIADNDGSTAKSLTLHILAAQPADQSNPNTPADLKPGELKVGKKNVWVGTGSTPLELIQVKAQGKKAMRAADWARGARLSPAACVR
|
Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
|
B7GUP8
|
Q8ZDH1
|
TATE_YERPE
|
Probable Sec-independent protein translocase protein TatE
|
Yersinia
|
MEGLSITKLLVVGILIVLLFGTSKLRTLGADLGAALKGFKKAMRNDDEVSTSVLGETKMSAETKTVAETKAASDSQAAASVERKD
|
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. TatE shares overlapping functions with TatA.
|
Q8ZDH1
|
Q0IIM8
|
TBC8B_HUMAN
| null |
Homo
|
MWLKPEEVLLKNALKLWLMERSNDYFVLQRRRGYGEEGGGGLTGLLVGTLDSVLDSTAKVAPFRILHQTPDSQVYLSIACGANREEITKHWDWLEQNIMKTLSVFDSNEDITNFVQGKIRGLIAEEGKHCFAKEDDPEKFREALLKFEKCFGLPEKEKLVTYYSCSYWKGRVPCQGWLYLSTNFLSFYSFLLGSEIKLIISWDEVSKLEKTSNVILTESIHVCSQGENHYFSMFLHINQTYLLMEQLANYAIRRLFDKETFDNDPVLYNPLQITKRGLENRAHSEQFNAFFRLPKGESLKEVHECFLWVPFSHFNTHGKMCISENYICFASQDGNQCSVIIPLREVLAIDKTNDSSKSVIISIKGKTAFRFHEVKDFEQLVAKLRLRCGAASTQYHDISTELAISSESTEPSDNFEVQSLTSQRECSKTVNTEALMTVFHPQNLETLNSKMLKEKMKEQSWKILFAECGRGVSMFRTKKTRDLVVRGIPETLRGELWMLFSGAVNDMATNPDYYTEVVEQSLGTCNLATEEIERDLRRSLPEHPAFQSDTGISALRRVLTAYAYRNPKIGYCQAMNILTSVLLLYAKEEEAFWLLVAVCERMLPDYFNRRIIGALVDQAVFEELIRDHLPQLTEHMTDMTFFSSVSLSWFLTLFISVLPIESAVNVVDCFFYDGIKAILQLGLAILDYNLDKLLTCKDDAEAVTALNRFFDNVTNKDSPLPSNVQQGSNVSDEKTSHTRVDITDLIRESNEKYGNIRYEDIHSMRCRNRLYVIQTLEETTKQNVLRVVSQDVKLSLQELDELYVIFKKELFLSCYWCLGCPVLKHHDPSLPYLEQYQIDCQQFRALYHLLSPWAHSANKDSLALWTFRLLDENSDCLINFKEFSSAIDIMYNGSFTEKLKLLFKLHIPPAYTEVKSKDASKGDELSKEELLYFSQLHVSKPANEKEAESAKHSPEKGKGKIDIQAYLSQWQDELFKKEENIKDLPRMNQSQFIQFSKTLYNLFHEDPEEESLYQAIAVVTSLLLRMEEVGRKLHSPTSSAKGFSGTVCGSGGPSEEKTGSHLEKDPCSFREEPQWSFAFEQILASLLNEPALVRFFEKPIDVKAKLENARISQLRSRTKM
|
Involved in vesicular recycling, probably as a RAB11B GTPase-activating protein.
|
Q0IIM8
|
C8NA81
|
METAS_CARH6
|
Homoserine transsuccinylase
|
Cardiobacterium
|
MPLVAHRELESLDRLRAEGQEILDVRRASQQDIRELHIGLLNLMPDGALKATERQFLRLIGNSNRIAQFYVHIFTVPGVPRSADMQAYIDSHYENFDDLAHDGLDAIIFTGTNPLHADLAQEAYWPHVQRVFDWADKNVTSVLCSCLASHLALQHFHGIARKRRDEKLFGVFSHRVLDRSHPMLANINTRFDMPHSRWNGISAAQLEARGLPVLVAGEESGVAMASSPDGFRQIYFQGHPEYDRSSLLKEFRRDLALYQDGKLPQPPKLPTHYFTPAGQRLIRDYIESGRPISDFPEAQLADEVDVTWRDTAKALFANWLGLVYQLTHKERHLQYMDGIDPADPLGRLRR
|
Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine.
|
C8NA81
|
P22136
|
AEP2_YEAST
|
ATPase expression protein 2, mitochondrial
|
Saccharomyces
|
MWINRLVKHPSYSVLRFYTKRLCTVSVKSLREFGVLPNSTICHSVYPRRTYVMGRAVINDILIKKSYSTHTVCAIDRSKDENNGSAYDKFEAKGIPIDVHTLKRIISSSGMDESEFSKSISYLFAKTVDPEPKDVLSLEDLSFLLSKLYTQRFQIRRICRDINAKYSEFWFKLFSLYAEKVDAKRNQVNLRNTKLDACEIFDANLMIKNFIELGQLGKAQKILSFILDRNPDILLSPKNADISTIVHFLQLRCGALAPYWKIPDNSEQKQGFLRKMVRLGAKNTSIRLSSTYKAMDHQTLLKIADLALQEKKLLNSEDLLSTLIQSFGHLGQTQILERCIEHIWQISPQEFPSHVVIKHRGCYPSSKILVSILVSFYFNDHDLHRGLSILDSFIKHYPDVKLDALFWRRLFQLSHFAWTPANDKKATSVVRCWHLMKQWYASKRLRPSVDYETLRQLYDIMKKTGNFPLGIDVLRSFKPGIERTRAENAGKVNNIIIKYQKCIIKELVNRGRFSAVREFIDSYGFDRKMTKDLNIFCANRMFLRSKKMKNKIENKKEREKVRLDSFDDDEDDGMIIGSLW
|
Required for translation of the mitochondrial OLI1 transcript coding for the mitochondrial ATP synthase subunit 9.
|
P22136
|
B1HW99
|
RNH3_LYSSC
|
Ribonuclease HIII
|
Lysinibacillus
|
MSNIVLSISTNIQKEVMAYYAANYIERKAAGVIFAAKLPDTSITMYKSGKLMFQGGGAEREAARWGTIEKTPNSKSAIIGAKGDTLPDQFALMSVLGSDETGTGDYFGPMTVAAVYVPSSKIELINELGVKDSKMLSDDYMRKIAPDLRAACVHSVLILRNEKYNSLQAKGYSQGKMKAMMHNKALHNTLAKMAPETPEYILIDQFAERGVYYNYLKNEREIVQESVYFSTKAEQLHVAVATASILARAAFLKEMDRLSDIAGLELMKGASNKVDVQAARIWRKQGEEFLRSITKWHFANTEKARKMI
|
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
|
B1HW99
|
Q2SDI1
|
NADK_HAHCH
|
ATP-dependent NAD kinase
|
Hahella
|
MEQFRNIGLLGRMGSVQVVETLKRLKNYLVGEGYAVILEEATAAVLPGHNVQVSSKKMLGEICDLVIVVGGDGSLLGAARALAGCNVPVLGVNRGRLGFLTDITPTEMEPQLAEVLSGKYVEESRFLLDAYVKRNGEPVGYGCGLNDIVLHPGKSTRMIGFDLYIEGQFVNSQRSDGLIVSTPTGSTAYALSAGGPIMHPRLDAIVLVPMFPHTLSSRPIVVDGNSEIKIIIGDYNQTYPHVSCDGQTHVTCAPGDTVTICKKPQKLRLIHPMNHNFYQICRDKLGWSSSRDQGGQ
|
Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
|
Q2SDI1
|
Q3ZC48
|
DRAM2_BOVIN
|
Transmembrane protein 77
|
Bos
|
MWWFQQGLSFLPSALVIWTAAAFIFSYITAITLHHVDPVLPYISDTGTVAPEKCLFGAMLNIAAVLCVATIYVRYKQVHALNPEENRIIRLNKAGLVLGLLSCLGLSLVANFQKTTFFAVHVCGAVLTFGMGSLYMFVQTILSYQMQPKIHGKQVFWIRLLLVIWCGVSAFSMLTCSSLLYNGSFGADIVQKLHWNPEDKGYVLHMITTAAEWSMSLSFFGFFLTYIRDFQKISLRVEATLHGLTLYDTAPCPVNNERTWLLSRDV
|
Plays a role in the initiation of autophagy. In the retina, might be involved in the process of photoreceptor cells renewal and recycling to preserve visual function. Induces apoptotic cell death when coexpressed with DRAM1.
|
Q3ZC48
|
B0JM93
|
PETD_MICAN
|
17 kDa polypeptide
|
Microcystis
|
MSTLKKPDLSDPALRAKLAKGMGHNYYGEPAWPNDLLYVFPVVIFGTIGLCTGLAIMDPTMIGEPADPFATPLEILPEWYLYPVFQILRILPNKLLGIACMAGVPLGLMLVPFIESVNKFQNPFRRPVATAIFLFGTVVTIWLGIGATFPIDISLTLGLF
|
Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
|
B0JM93
|
Q8RU33
|
VA0D_ORYSJ
|
Vacuolar proton pump subunit d
|
Oryza sativa
|
MYGWEMLSFNIHDGFLEAIVRGNRSGLLTAADYNNLCQCENLDDVKMHLTATEYGPYLQNEPSPLHTTTIVEKCTLKLVDEYKHMMCQATEPLSTFLQYITYGHMIDNVVLIVTGTLHERDVNELLEKCHPLGMFDSIASLAVAQNMRELYRLVLVDTPLAPYFSECITSEDLDDMNIEIMRNTLYKAYLEDFYKFCEKLGGATAEIMCDLLSFEADRRAVNITINSIGTELTRDDRRKLYSNFGLLYPYGHEELAVCEDVDQVRGVMEKYPPYQAIFAKISYGESQMLDKAFYEEEVRRLCLSFEQQFHYAVFFAYIRLREQEIRNLMWISECVAQNQKNRVHDSVVFIF
|
Subunit of the integral membrane V0 complex of vacuolar ATPase. Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells, thus providing most of the energy required for transport processes in the vacuolar system.
|
Q8RU33
|
Q8K402
|
TBX22_MOUSE
|
T-box transcription factor TBX22
|
Mus
|
MALSSRAHAFSVEALMGRPSKRKAQDPREEMQPELQEEQFVEEGEEILRSPSRDSQQPEKRLKAESSKTVFSCSDESNSQESLQEESVIQVELQGSDLWKRFHDIGTEMIITKAGRRMFPSVRIKVKGMDPVKQYYVILDVVPVDSKRYRYVYHSSQWMVAGNTDHSCITPRFYVHPDSPCSGENWMRQIISFDRVKLTNNEMDDKGHIILQSMHKYNPRVHVVEQDSRIDLSLIESFPTEGVKTFSFKETEFTTVTAYQNQQITKLKIDRNPFAKGFRDPGRNRGVLDGFLETYPWMPSFSMDFKTFVTDTQSGSSGSSPVTSSGGAPSPLNSLLSPSCSPPMVYIPPSSFGMTYPDAYLHSVNIPFCYRICPTNNWRSQPFVLPTPERLPSFIIPQTLPPLMMEVPVVSSRGIINPNSGLHEDCNGQCLQASHSANQMLYGLQNPGNIFHPNAIAQEAISYPFHPPNGCYRYTISMPPRLENVASHLSENGTSQISFTEGSCDHSHWYPAINHYL
|
Probable transcriptional regulator involved in developmental processes. This is major determinant crucial to palatogenesis.
|
Q8K402
|
Q1QJ95
|
DCUP_NITHX
|
Uroporphyrinogen decarboxylase
|
Nitrobacter
|
MAQDSTIKPFLEVLSGRRQAVPPIWMMRQAGRYLPEYRELRAKAGGFLDLCFTPEFAAEVTLQPIRRFAFDAAIIFSDILVIPYALGRSVRFEVGEGPRLDPLDTPDMAATLSREADMTKLEPVFEALRRVRRELDSKTALIGFCGAPWTVATYMVAGRGTPDQAPARMMAYRHPEAFAKIIDVLVENSVRYLLGQLKAGADVLQIFDTWAGVLPPREFARWSIEPTRRIVEGVRKIVPDAKIIGFPRGAGALLPSYIEATGVDAVSIDWAAEPSLVREKVQSRVAVQGNLDPLALIAGGAALDRAVDDVLANFAGGRLIFNLGHGIQPETPIPHVEQMIRRVRGSGLRE
|
Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
|
Q1QJ95
|
A5EVY3
|
LUXS_DICNV
|
Autoinducer-2 production protein LuxS
|
Dichelobacter
|
MERKHMNVASFNLDHNAVKAPYVRLADKKIGSHGDVIYKYDIRVCQPNREQMLMPALHSLEHLLAELMRNHSDKILDISPMGCQTGFYISLLNEPDYQVMLHLLETTLNDILAAEAVPACCEEQCGFAANHSLSGAQEIARYLLAHRNKWEQVF
|
Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD).
|
A5EVY3
|
P28381
|
RBL_BARCA
|
Ribulose bisphosphate carboxylase large chain
|
Barnadesia
|
MSPQTETKASVGFKAGVKDYKLTYYTPDYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYGIEPVLGEENQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPTAYVKTFQGPPHGIQVDRDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQAETGEIKGHYLNATAGTCEEMMKRAVFARELAVPIVMHDYLTGGCNATTSLAHYCRDNGLLLHIQRAMHAVIDRQKNHGMHFRVLAKALRMSGGDHIHAGTVVGKLEGEREITLGFVDLLRDDFIKKDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGPVANRVALEACVQARNDGRDLAIHGNEIIREACKWSPELAAACEVWKEIKFEFPALDTFV
|
RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.
|
P28381
|
Q6RYS9
|
DOPR3_CAEEL
|
Dopamine D2-like receptor dop-3
|
Caenorhabditis
|
MLAGQHHVTDIESPLMVVLWRVAAGVFLPLVPTMAVFGNVLVIMSVFRERSLQTVTNMLIVSLAVSDFMVAIGVMSFGVYYEWNDFKWGLGSFFCHVYQALDVACSTASILNLLAISLDRYIAIGHPISYAQYGARGGRAMISITIVWGVSVAVALPLLLGVNPMEENDLQECELANPYFNMISSIFSFFIPCIAMIILYTIIFRRLRQRERARSLRQAQRSENDKISSALLGGAQIARQMGKHFKNRTDQILLEISFQTSSFPTMSESSEDASTISPMINSFNNFLPKKTPYPSTSIPAIPECGSMPNLTIIERPEAEKEKEISIMDLRDTVEMLDDKYSSAILTSFQTSRSFGEELEEILPFIDGSNSVKHSREQLHTTRSNTSTTRLLDVKPELRSISVPSIQDEKKLSQKSNDLPFSHQNGTHKQKLLPNPGILMKSKSTTLLKTNGYMDTDSLNRNSHKKSLADLLANDEFSFSDSMRVYKNRLFKSLSRATSGWNKPRPSRHMVKKATKQMRREHKATVTLAVVLAVFLFCWLPFFVLHLSNSICLIIDENSACVGFLPLYLATWLGYLNSSLNPLIYTVFDQRFRNAFRNILSCGIFKKR
|
G-protein coupled receptor which binds to the neurotransmitter dopamine with high affinity leading to the activation of an associated G-protein and downstream signaling pathways . Couples to G-proteins to inhibit adenylate cyclase (AC) activity and cAMP production . Antagonizes the D1-like dopamine receptor dop-1 to negatively regulate the rate of locomotion . In GABAergic, RIC, and SIA neurons, antagonizes the function of dop-1 to play a role in behavioral plasticity and regulate the decision-making process when conflicting alternatives are present . Antagonizes octopamine signaling in response to food by promoting the dopamine-mediated suppression of crh-1/CREB1 transcription factor activation in cholinergic SIA neurons . This is most likely in association with the G(o)-alpha G-protein subunit goa-1 . Promotes male mating behavior by antagonizing acetylcholine signaling to control the protrusion of copulatory spicules from the tail of males during hermaphrodite vulval location .
|
Q6RYS9
|
Q1GAQ0
|
EFTU_LACDA
|
Elongation factor Tu
|
Lactobacillus
|
MAEKEHYVRTKPHVNIGTIGHVDHGKTTLTAAITTVLAKKGLAQAEDYSQIDAAPEEKERGITINTAHVEYETEKRHYAHMDAPGHADYIKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVNSIVVFLNKCDLVDDPELIDLVEMEVRDLLSEYGYPGDDVPVVRGSALKALEGDEEAQKKIEELMDVVDEYIPTPERETDKPFLMPVEDVFTITGRGTVASGRIDRGTVKVGDSVEIVGLVEKVLTSVVTGLEMFHKTLDLGEAGDNVGVLLRGVDRDQIVRGQVLAAPGSIKTHKTFKGQVYILSKDEGGRHTPFFSDYRPQFYFHTTDITGEIELPEGTEMVMPGDNTEFSVTLIKPAAIEVGTKFTIREGGRTVGAGQVTEIDD
|
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
|
Q1GAQ0
|
A1S3S8
|
TSAD_SHEAM
|
tRNA threonylcarbamoyladenosine biosynthesis protein TsaD
|
Shewanella
|
MRVLGIETSCDETGIAIYDEEKGLMAHTLYSQVKLHADYGGVVPELASRDHVRKIIPLIREALKNADTRIEDLDGICYTKGPGLIGALLVGACVGRSLAFSWNLPAVGVHHMEGHLLAPMLEDEVPEFPFVALLVSGGHSMLVKVDGIGQYEVLGESIDDAAGEAFDKTAKLMGLDYPGGPRLAKLAASGQPANYKFPRPMTDRPGLDFSFSGLKTFVANTIAAEPDDEQTRANIARAFEEAVVDTLSIKCRRALEQTGYKRLVIAGGVSANVRLRAGLAELMEKLGGKVYYPRGEFCTDNGAMIAYAGLQRLKAGQLEDLAVKGQPRWPLDTLLPV
|
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
|
A1S3S8
|
P29238
|
LUXA2_PHOLE
|
Bacterial luciferase alpha chain
|
Photobacterium
|
MKISNICFSYQPPGESHQEVMERFIRLGVASEELNFDGFYTLEHHFTEFGITGNLYIACANILGRTKRIQVGTMGIVLPTEHPARHVESLLVLDQLSKGRFNYGTVRGLYHKDFRVFGTSQEDSRKTAENFYSMILDASKTGVLHTDGEVVEFPDVNVYPEAYSKKQPTCMTAESSETITYLAERGLPMVLSWIIPVSEKVSQMELYNEVAAEHGHDINNIEHILTFICSVNEDGEKADSVCRNFLENWYDSYKNATNIFNDSNQTRGYDYLKAQWREWVMKGLADPRRRLDYSNELNPVGTPERCIEIIQSNIDATGIKHITVGFEANGSEQEIRESMELFMEKVAPHLKDPQ
|
Light-emitting reaction in luminous bacteria.
|
P29238
|
D6R3B6
|
PAMT_CAPFR
|
Putative aminotransferase
|
Capsicum
|
MANITNEFMGHDMLAPFTAGWQSDMEPLVIEKSKGSYVYDINGKKYLDTLSGLWCATLGGSETRLVEAANKQLNTLPFYHSFWNRTTKPSLDLAKELLNMFTANKMAKVFFTNSGSEANDTQVKLVWYYNNALGRPQKKKIIARAKAYHGSTYISAGLSGLPPMHQKFDLPPPFVLHTECPHYWAYHLPGETEEEFSTRLANNLESLILNEGPETVAAFIAEPVLGAAGVILPPATYFDKVQAILRKHDILFIADEVVCGFGRLGTMFGSDKYNIKPDLVSVAKALSSGYMPIAAVLVSQKISSVILSESNKIGAFCHGFTYSGHPVACAVALEALKIYKERNITEVVNKISQKFQEGLKAFADSPIIGEIRGTGLALSTEFVDNKSPNDPFPYEWAVGTYFGAQCAKYGMLVSSTGDHVNMAPPFTLSLEELDELIRIYGKALKDTEKRVEELKSQKK
|
Participates in the biosynthesis of capsaicinoids in pungent cultivars of Capsicum frutescens . Capsaicinoids, the alkaloids responsible for the heat or pungency of chili pepper, are synthesized from phenylpropanoid intermediates in the placental tissue of chili peper fruit (Probable). Can transfer an amine from alanine to vanillin, forming vanillylamine and pyruvate .
|
D6R3B6
|
Q1QUS6
|
LOLA_CHRSD
|
Outer-membrane lipoprotein carrier protein
|
Chromohalobacter
|
MRAFKWALAIGATLALPLTAQAQTGGAERLAALLESVTSYSADFDQQILDGGGQRLQEAEGHMWLSRPGKFHWEVEAPYRQVVVSDGDKVYLYDPDLEQVSVRPLDTRVTHTPALLLSGSADALTENYAVESRQGDDEETFTLTPKSPDTLFESLQLTFENERLEGLQMEDSTGQRTAIAFDDIEVNGDIDASRFTFEIPEGADVIREGG
|
Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane).
|
Q1QUS6
|
Q1QYX8
|
TSAD_CHRSD
|
tRNA threonylcarbamoyladenosine biosynthesis protein TsaD
|
Chromohalobacter
|
MRVLGIETSCDETGVAIYDTERGLIADALHSQMAMHAEFGGVVPELASRDHTRKLLPLIRQVLDDAELRGDQLDAIAYTAGPGLVGALMVGASTAHGLARAWDIPALGVHHMEGHLLAPMLEAAPPDFPFVALLVSGGHTQLVEVHGLGRYRLLGESVDDAAGEAFDKAAKMLELPYPGGPHVAQLAERGDPTRFRFPRPMTDRPGLDFSFSGLKTHTLTTANQLKAAGPLSDQDRADIARAFEEAVVDTLVIKCRRALDTTGLKRLVVAGGVSANHRLRERLDRETAKRQAQAFYPRGRFCTDNGAMIAYVGAQRLLAGERDDATMQATPRWPLASLTPPAA
|
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
|
Q1QYX8
|
Q63467
|
TFF1_RAT
|
Protein pS2
|
Rattus
|
MEHKVTCVLAMVLMLALSSLAQNQEETCAVIPRERINCGFPGVTAQQCKEKGCCFDDSVRGFPWCFRPLVIENQQEEECPF
|
Stabilizer of the mucous gel overlying the gastrointestinal mucosa that provides a physical barrier against various noxious agents.
|
Q63467
|
P55291
|
CAD15_HUMAN
|
Muscle cadherin
|
Homo
|
MDAAFLLVLGLLAQSLCLSLGVPGWRRPTTLYPWRRAPALSRVRRAWVIPPISVSENHKRLPYPLVQIKSDKQQLGSVIYSIQGPGVDEEPRGVFSIDKFTGKVFLNAMLDREKTDRFRLRAFALDLGGSTLEDPTDLEIVVVDQNDNRPAFLQEAFTGRVLEGAVPGTYVTRAEATDADDPETDNAALRFSILQQGSPELFSIDELTGEIRTVQVGLDREVVAVYNLTLQVADMSGDGLTATASAIITLDDINDNAPEFTRDEFFMEAIEAVSGVDVGRLEVEDRDLPGSPNWVARFTILEGDPDGQFTIRTDPKTNEGVLSIVKALDYESCEHYELKVSVQNEAPLQAAALRAERGQAKVRVHVQDTNEPPVFQENPLRTSLAEGAPPGTLVATFSARDPDTEQLQRLSYSKDYDPEDWLQVDAATGRIQTQHVLSPASPFLKGGWYRAIVLAQDDASQPRTATGTLSIEILEVNDHAPVLAPPPPGSLCSEPHQGPGLLLGATDEDLPPHGAPFHFQLSPRLPELGRNWSLSQVNVSHARLRPRHQVPEGLHRLSLLLRDSGQPPQQREQPLNVTVCRCGKDGVCLPGAAALLAGGTGLSLGALVIVLASALLLLVLVLLVALRARFWKQSRGKGLLHGPQDDLRDNVLNYDEQGGGEEDQDAYDISQLRHPTALSLPLGPPPLRRDAPQGRLHPQPPRVLPTSPLDIADFINDGLEAADSDPSVPPYDTALIYDYEGDGSVAGTLSSILSSQGDEDQDYDYLRDWGPRFARLADMYGHPCGLEYGARWDHQAREGLSPGALLPRHRGRTA
|
Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. M-cadherin is part of the myogenic program and may provide a trigger for terminal muscle differentiation.
|
P55291
|
C1FNC6
|
GREA_CLOBJ
|
Transcript cleavage factor GreA
|
Clostridium
|
MSEAKKYVMTYEGVKKLEEELEFLKTVKRKEITEKIKVALSFGDLSENSEYDEAKNEQAFVEGRIIQLENMLKNASIVDENEVPKDIVSVGSIVKVKDYEFDEEVEYIIVGSAEADPMNNKISNESPVGHGLIGKKVGDIIEVTVPDGVSKYEILEVNRA
|
Necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by cleavage factors such as GreA or GreB allows the resumption of elongation from the new 3'terminus. GreA releases sequences of 2 to 3 nucleotides.
|
C1FNC6
|
Q03308
|
VPS16_YEAST
|
Vacuolar protein-targeting protein 16
|
Saccharomyces
|
MKNPSFDWERLKDVFYRSRAIGELKWPTQYEEFKCALSLTVIAVEIQDFIQVYNYFGQLLGKINLQRIHEDIIKFEFDKDEKLILVTKSSIKIVKGWSPLTIESVPLQDPTIDTIWDYHNGIMLLAKSRDIYKLNGNEWELLYENKDKKYNLLTKNHWSCNDDSIILLDVDHVYQVSTSNGALLKLITDSSWHKVTISSRGFICLYNMKDNKLQIFRDPARILMEHNLDSTPDDICWCGNDTVACSFEDEIKLYGPDGLYVTFWYPFTVTNLRAEVDGLKVITTEKIYFLSRVQPQTSNIFRIGSTEPGAMLVDSFSLLEDHAPKAIEILKNFVLEKGVLDCIAAAIDEFEPKLQKMLLNAASYGKASLQYKSFDASIFVNACNTIKLLNCFRSFGIFLTVEEYRCISLKGVIDRLLKYHRYYECIQICKLANERFLLGYVFTEWAKDKIKGSPDMEDDELLDKIKSRLSVIDMTDTLQMVAVAKVAYLEGRFQLSRNLALLEKNEEARIEQLYNLDDDSIALKECIKVQNYSLTISLLIALSKKLTNSQLTKLLIIDMFNNPLYLYYMRMDKAYLYDFYRQTDRFIDLAHVLLQQGKEQQSLHSFLPQIKDLYSQVQNSEVVNNTIEQLQRQEKLWIYQESLGKRFAISFTNMTLDQTLSKLIETGQDKQVKEIVKKFKISEKKLYHLKCKTLVEAKKFDELLQFAQSRKSPIGYMPFYTYLKSRGHMDKASPYVNMIPGLSYQEKKKLYVECRGFRDAIQLAGKEKDIPGLKEIYNIIPPNEPELKALANETMSRI
|
Essential for vacuolar protein sorting. Required for vacuole biogenesis, stability and to maintain vacuole morphology. Required for growth at elevated temperatures. Acts as component of the HOPS complex that acts during the docking stage of vacuole fusion. HOPS is an effector for the vacuolar Rab GTPase YPT7 and is required for vacuolar SNARE complex assembly. It remains bound to SNARE complexes after vacuole fusion.
|
Q03308
|
Q69YH5
|
CDCA2_HUMAN
|
Recruits PP1 onto mitotic chromatin at anaphase protein
|
Homo
|
MDANSKDKPPETKESAMNNAGNASFILGTGKIVTPQKHAELPPNPCTPDTFKSPLNFSTVTVEQLGITPESFVRNSAGKSSSYLKKCRRRSAVGARGSPETNHLIRFIARQQNIKNARKSPLAQDSPSQGSPALYRNVNTLRERISAFQSAFHSIKENEKMTGCLEFSEAGKESEMTDLTRKEGLSACQQSGFPAVLSSKRRRISYQRDSDENLTDAEGKVIGLQIFNIDTDRACAVETSVDLSEISSKLGSTQSGFLVEESLPLSELTETSNALKVADCVVGKGSSDAVSPDTFTAEVSSDAVPDVRSPATPACRRDLPTPKTFVLRSVLKKPSVKMCLESLQEHCNNLYDDDGTHPSLISNLPNCCKEKEAEDEENFEAPAFLNMRKRKRVTFGEDLSPEVFDESLPANTPLRKGGTPVCKKDFSGLSSLLLEQSPVPEPLPQPDFDDKGENLENIEPLQVSFAVLSSPNKSSISETLSGTDTFSSSNNHEKISSPKVGRITRTSNRRNQLVSVVEESVCNLLNTEVQPCKEKKINRRKSQETKCTKRALPKKSQVLKSCRKKKGKGKKSVQKSLYGERDIASKKPLLSPIPELPEVPEMTPSIPSIRRLGSGYFSSNGKLEEVKTPKNPVKRKDLLRHDPDLHMHQGYDKYDVSEFCSYIKSSSSLGNATSDEDPNTNIMNINENKNIPKAKNKSESENEPKAGTDSPVSCASVTEERVASDSPKPALTLQQGQEFSAGGQNAENLCQFFKISPDLNIKCERKDDFLGAAEGKLQCNRLMPNSQKDCHCLGDVLIENTKESKSQSEDLGRKPMESSSVVSCRDRKDRRRSMCYSDGRSLHLEKNGNHTPSSSVGSSVEISLENSELFKDLSDAIEQTFQRRNSETKVRRSTRLQKDLENEGLVWISLPLPSTSQKAKRRTICTFDSSGFESMSPIKETVSSRQKPQMAPPVSDPENSQGPAAGSSDEPGKRRKSFCISTLANTKATSQFKGYRRRSSLNGKGESSLTALERIEHNGERKQ
|
Regulator of chromosome structure during mitosis required for condensin-depleted chromosomes to retain their compact architecture through anaphase. Acts by mediating the recruitment of phopsphatase PP1-gamma subunit (PPP1CC) to chromatin at anaphase and into the following interphase. At anaphase onset, its association with chromatin targets a pool of PPP1CC to dephosphorylate substrates.
|
Q69YH5
|
P53559
|
BIOW_BACSU
|
Pimeloyl-CoA synthase
|
Bacillus
|
MMQEETFYSVRMRASMNGSHEDGGKHISGGERLIPFHEMKHTVNALLEKGLSHSRGKPDFMQIQFEEVHESIKTIQPLPVHTNEVSCPEEGQKLARLLLEKEGVSRDVIEKAYEQIPEWSDVRGAVLFDIHTGKRMDQTKEKGVRVSRMDWPDANFEKWALHSHVPAHSRIKEALALASKVSRHPAVVAELCWSDDPDYITGYVAGKKMGYQRITAMKEYGTEEGCRVFFIDGSNDVNTYIHDLEKQPILIEWEEDHDS
|
Catalyzes the transformation of pimelate into pimeloyl-CoA with concomitant hydrolysis of ATP to AMP.
|
P53559
|
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