wanglab/gogpt-training-data huggingface dataset:
Protein: Origin recognition complex subunit 4 (Q6NWF3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR007858}.
Interaction partners:
Sequence:
MSKRRPAALSDVQCVSLVQELLRERLCHQKLPDQPIGLDSQYKHLLELLRRTAVHGESNSVLIVGPRGSGKTMLLGCVLRELMSLKEVQKNVLLVELNGLLQTDDKIALKEITRQLHLENVVGDKVFGSFAENLAFLLEALKKGDKSSSRPVLFLLDEFDLFAHHKNQTLLYNLLDVSQSAQTPVAVVGFTCRLDVLELLEKRVKSRFSHRQIHLFSSLSFSQYVDVVRLQLSLPQDFPDHRFSSQWNQSVTKLCEDKSVLEVLKRSFNSSKDFRSLFSLLFMAVSRVSVSHSTLCEADFLESGRLISADSKANVLHGLSILELCLIIAMKHLNDTYDGEPFNFQMVHNEFKKFIQRKSHSIHKFEKPVVMKAFEHLLQLELVRPVDSGVCKVQREYQLMRLMLEHGQVMEALQRYPQCPTDVKQWALSAFA
Protein: DNA-directed DNA polymerase (EC 2.7.7.7) (Mitochondrial DNA polymerase catalytic subunit) (Q9U208)
Organism: Caenorhabditis elegans
Interaction partners:
- Glycine--tRNA ligase
- Single-stranded DNA-binding protein
- HMG box-containing protein 5
- Cytochrome b
- CYtochrome P450 family
- DNA-directed RNA polymerase
- Ubiquinone biosynthesis O-methyltransferase, mitochondrial
Sequence:
MRPPKIMQIFHVSRRQIATSKTSNFERKTIETVCPRVHNYLFPHVSAPSTSSAAEYTGVLPPLVADNVVDHFGVLAEQQTRKYKELLEKACEFDLETAKNVLEHIDKTDGWHYKTGWTRYPFSTSEPPETIDFPRDSILFFDIELVVRDGTLPTLAIALGRDAWYGWCSDRLIYESEIPEIPTKADLIPIGEIGMEKVIIGHNVGFDRARCREAYQSINGSKIRFMDTMSMSIPMYGMADHQQSLYEMYDVETNDSHSDWMNAWKGRVSKNSLVAVHDHLYPDKAINAEGFSKKTMRASFVKDPIEQIREDFQPLMSYCARDNILCAEIYFRLWPEFIKRFPHPATLSGMLNMGNVYLPINSYWKMFYEKNVQTCEQKKTAATRKIIESARLVAKRLDDEGEEIGPEKNDVWMWHHDWTFNQKQSNFEWFNKLFKARSFVNLSLDEVDSHHIALKSHLIPAIFGFVFGPFPLFKTRSKGWGFLVPNWKPVEKALQDPNFHEIDAKIDFKPDSAVKKFPLRSFYETVQNNVYMLGELPISPDRKGFELDEAGLVRFYQLDHPSGEGNVGDPLTKHFAKDLKELVLRPTRYEEYFDVVLDSIQTTQFWTSYSDRYCSEVAIWSPEATWRTAENLEMIDGAIAAAVVPAGTISRRSVHKLWVTLTNQSTGHVIGTGIKAMVQAPAGYRLVGADVDSQEQWLAALYGDASAEKRLPLEKRVAGKTAFSNMMLAGSKSDNTDLHSVVASQLKISRNHAKVLNYARLYGSGETHAGKHLMRVGGLKQSEAESTASQLFKLTKGDVAKYMKVDVRMNCVVDKYIEEMVENSDVCKILTIDGIYYMPAYTSQFASETVRFEDWLLSHYSSLLNGSSEPDSLIYSIYENPDEPRRLFVGGYESSTFNFLETSAAAHDLRTPILGCQIADSLGKLPEGTPDSAYFDRKYKRSVMNWIVQSSAVDFLHLLLVSMQWLCDTYKIDARFVISIHDEVRYMCKEPDAPRLALALQLSNLLVRAYISQRVGICQLPNTVAFFSQVDCDTVLRKEVDTESINPDGSKIADGVAWTVDDLLKLTGGKLD
Protein: V-type proton ATPase 16 kDa proteolipid subunit c 2 (V-ATPase 16 kDa proteolipid subunit c 2) (Vacuolar proton pump 16 kDa proteolipid subunit c 2) (C0HLB3)
Organism: Caenorhabditis elegans
Function: Proton-conducting pore forming subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity). Involved in necrotic cell death. Required along with other vacuolar ATPase components for the removal of protein aggregates which form in immature oocytes in the distal gonad. This removal occurs as the oocytes mature and move to the proximal gonad, is triggered by the introduction of sperm through mating and occurs before fertilization. The introduction of sperm triggers V-ATPase accumulation in proximal oocytes and induces lysosomal acidification which leads to engulfing of protein aggregates by lysosomes and subsequent clearance of the aggregates. Lysosomal acidification also leads to changes in mitochondrial morphology and function. Mitochondria in distal immature oocytes are fragmented, produce high levels of reactive oxygen species (ROS) and have high membrane potential, indicative of metabolic inactivity. In contrast, mitochondria in proximal mature oocytes are tubular with lower ROS levels and membrane potential, indicative of an active metabolic state required for aggregate mobilization before clearance.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- V-type proton ATPase 21 kDa proteolipid subunit c''
- V-type proton ATPase subunit
- V-type proton ATPase subunit D
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit C
- V-type proton ATPase subunit E
- Probable V-type proton ATPase subunit F
- V-type proton ATPase subunit B 1
- Oligomycin sensitivity conferral protein
- ATP synthase subunit a
Sequence:
MSYDLETAERAAYAPFFGYMGAASAQIFTVLGAAYGTAKSAVGICSMGVMRPELIMKSVIPVIMAGIIGIYGLVVAMVLKGKVTSASAGYDLNKGFAHLAAGLTCGLCGLGAGYAIGIVGDAGVRGTAQQPRLFVGMILILIFSEVLGLYGMIVALILGTS
Protein: Medium-wave-sensitive opsin 1 (Green cone photoreceptor pigment) (Green-sensitive opsin) (GOP) (P04001)
Organism: Homo sapiens (Human)
Function: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20579627}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MAQQWSLQRLAGRHPQDSYEDSTQSSIFTYTNSNSTRGPFEGPNYHIAPRWVYHLTSVWMIFVVIASVFTNGLVLAATMKFKKLRHPLNWILVNLAVADLAETVIASTISVVNQVYGYFVLGHPMCVLEGYTVSLCGITGLWSLAIISWERWMVVCKPFGNVRFDAKLAIVGIAFSWIWAAVWTAPPIFGWSRYWPHGLKTSCGPDVFSGSSYPGVQSYMIVLMVTCCITPLSIIVLCYLQVWLAIRAVAKQQKESESTQKAEKEVTRMVVVMVLAFCFCWGPYAFFACFAAANPGYPFHPLMAALPAFFAKSATIYNPVIYVFMNRQFRNCILQLFGKKVDDGSELSSASKTEVSSVSSVSPA
Protein: GTPase Obg (EC 3.6.5.-) (GTP-binding protein Obg) (P9WMT1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: 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 (By similarity). GTPase activity is not inhibited by ATP or GDP. Overexpression decreases cell growth starting in late log phase and continuing into stationary phase.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01454, ECO:0000269|PubMed:22578863}. Cell membrane {ECO:0000269|PubMed:21352546}. Note=Found to be entirely in cytoplasm (PubMed:22578863). Also found to be 90% associated with cell membrane, 10% in soluble extract. Associated with 30S and 50S ribosome subunits as well as 70S ribosomes (PubMed:21352546). {ECO:0000269|PubMed:21352546, ECO:0000269|PubMed:22578863}.
Interaction partners:
- Large ribosomal subunit protein bL27
- Glutamate 5-kinase
- Large ribosomal subunit protein bL21
- Large ribosomal subunit protein bL20
- Ribosomal silencing factor RsfS
- Large ribosomal subunit protein bL19
- Large ribosomal subunit protein uL11
- Large ribosomal subunit protein uL2
- Large ribosomal subunit protein uL13
- Large ribosomal subunit protein bL17
Sequence:
MPRFVDRVVIHTRAGSGGNGCASVHREKFKPLGGPDGGNGGRGGSIVFVVDPQVHTLLDFHFRPHLTAASGKHGMGNNRDGAAGADLEVKVPEGTVVLDENGRLLADLVGAGTRFEAAAGGRGGLGNAALASRVRKAPGFALLGEKGQSRDLTLELKTVADVGLVGFPSAGKSSLVSAISAAKPKIADYPFTTLVPNLGVVSAGEHAFTVADVPGLIPGASRGRGLGLDFLRHIERCAVLVHVVDCATAEPGRDPISDIDALETELACYTPTLQGDAALGDLAARPRAVVLNKIDVPEARELAEFVRDDIAQRGWPVFCVSTATRENLQPLIFGLSQMISDYNAARPVAVPRRPVIRPIPVDDSGFTVEPDGHGGFVVSGARPERWIDQTNFDNDEAVGYLADRLARLGVEEELLRLGARSGCAVTIGEMTFDWEPQTPAGEPVAMSGRGTDPRLDSNKRVGAAERKAARSRRREHGDG
Protein: Probable L,D-transpeptidase YbiS (EC 2.-.-.-) (P0AAX8)
Organism: Escherichia coli (strain K12)
Function: Responsible, at least in part, for anchoring of the major outer membrane lipoprotein (Lpp, also known as the Braun lipoprotein) to the peptidoglycan via a meso-diaminopimelyl-L-Lys- bond on the terminal residue of Lpp. Can be oxidized in vivo, its reduction depends preferentially on DsbG, although DsbC is able to partially replace DsbG.
Subcellular location: Periplasm.
Interaction partners:
- Probable L,D-transpeptidase YcbB
- Putative L,D-transpeptidase YafK
- Major outer membrane lipoprotein Lpp
Sequence:
MNMKLKTLFAAAFAVVGFCSTASAVTYPLPTDGSRLVGQNQVITIPEGNTQPLEYFAAEYQMGLSNMMEANPGVDTFLPKGGTVLNIPQQLILPDTVHEGIVINSAEMRLYYYPKGTNTVIVLPIGIGQLGKDTPINWTTKVERKKAGPTWTPTAKMHAEYRAAGEPLPAVVPAGPDNPMGLYALYIGRLYAIHGTNANFGIGLRVSHGCVRLRNEDIKFLFEKVPVGTRVQFIDEPVKATTEPDGSRYIEVHNPLSTTEAQFEGQEIVPITLTKSVQTVTGQPDVDQVVLDEAIKNRSGMPVRLN
Protein: Ribosome-inactivating protein PMRIPm [Cleaved into: PMRIPm A chain (rRNA N-glycosidase) (EC 3.2.2.22); Linker peptide; PMRIPm B chain] (Q9M654)
Organism: Polygonatum multiflorum (Solomon's seal) (Convallaria multiflora)
Function: Gal/GalNAc-specific agglutinin. Behaves as a type-2 ribosome-inactivating protein. Inhibits mammalian ribosomes. The A chain is responsible for inhibiting protein synthesis through the catalytic inactivation of 60S ribosomal subunits by removing adenine from position 4,324 of 28S rRNA (Probable). The B chain binds to cell receptors and probably facilitates the entry into the cell of the A chain; B chains are also responsible for cell agglutination (lectin activity) (Probable). Involved in plant defense against insects (By similarity). Has very low cytotoxic activity against the human tumor cell line Molt4, but higher against CEM.
Interaction partners:
Sequence:
MRVVAAILYINVVVALICGLGIQGGALDLQDYPSVSFQGDAMQLQDYPSITFNLKGATWQTYRDFIEKLREIVTRGATTIAGTSIPVLNRVVPDSRRFVYVRLINLDGNVVTIAVDVTSLYVVAFSANNNGYFFSDSTETERTNLFVGIPRGDPLGFTGNYNSLENWAGADRGSIPLGPALLNKAIRNLRSNGRDSKAAKSLIVVIQMVSEAARFRRIEEQVRRSIADQDTFTPGSLMITMEKKWSKMSQQVERSVNDQGIFTGIFTRTVQLIDDNLQTLNIDNFNALSLHTMLAILLFRCRTTTSSHNTLPAASNIVLMGEDYVDKDDEKCTVGEPTRRISGRAGWCVDVKDGRDNDGNPIQVLSCGDGQERKQQWTFHRDGTIRSKLGKCMTAYGFKHGEYVMIYDCDTAIAGANKWVVSIDGTITNPISGLVLTAPRGATGTTLLVEKNVHAARQCWRVGDDVEPIVTKIVGFQEKCLEANYLENTNVSRYTKVFLDDCVLDRQQQRWALYSDGTIRADSDRSLRVTADGHRSLDSIIILACKGWGNQRWVFNTDGTILNPNAKLVMDVKDSDVSLLQIILHQSTGKPNQKWLTVTLPRTS
Protein: WUSCHEL-related homeobox 8 (Protein STIMPY-LIKE) (Q6X7J5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor, which may be involved in embryonic patterning. May be required for basal embryo development after fertilization. Acts partially redundantly with STIP in promoting embryonic cell division and proliferation. Promotes cotyledon boundary formation by maintaining the symmetry in CUC genes expression domains.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
Interaction partners:
- Probable WRKY transcription factor 2
- CLAVATA3/ESR
- Mitogen-activated protein kinase kinase kinase YODA
- Kinesin-like protein KIN-14E
- TPRXL
- Auxin efflux carrier component 7
- Protein CLAVATA 3
- Protein RKD4
- Homeobox-leucine zipper protein MERISTEM L1
Sequence:
MSSSNKNWPSMFKSKPCNNNHHHQHEIDTPSYMHYSNCNLSSSFSSDRIPDPKPRWNPKPEQIRILESIFNSGTINPPREEIQRIRIRLQEYGQIGDANVFYWFQNRKSRAKHKLRVHHKSPKMSKKDKTVIPSTDADHCFGFVNQETGLYPVQNNELVVTEPAGFLFPVHNDPSAAQSAFGFGDFVVPVVTEEGMAFSTVNNGVNLETNENFDKIPAINLYGGDGNGGGNCFPPLTVPLTINQSQEKRDVGLSGGEDVGDNVYPVRMTVFINEMPIEVVSGLFNVKAAFGNDAVLINSFGQPILTDEFGVTYQPLQNGAIYYLI
Protein: FAD-dependent monooxygenase ausM (EC 1.-.-.-) (Austinoid biosynthesis clusters protein M) (C8VQ98)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: FAD-dependent monooxygenase; part of the gene cluster B that mediates the biosynthesis of austinol and dehydroaustinol, two fungal meroterpenoids. The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA. 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN. Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A. Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE. Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4. The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide. Finally, the cytochrome P450 monooxygenase ausG modifies austinolide to austinol. Austinol can be further modified to dehydroaustinol which forms a diffusible complex with diorcinol that initiates conidiation. Due to genetic rearrangements of the clusters and the subsequent loss of some enzymes, the end products of the Emericella nidulans austinoid biosynthesis clusters are austinol and dehydroaustinol, even if additional enzymes, such as the O-acetyltransferase ausQ and the cytochrome P450 monooxygenase ausR are still functional.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cytochrome P450 monooxygenase ausI
- Cytochrome P450 monooxygenase ausG
- Austinoid biosynthesis clusters protein J
- Aldo-keto reductase ausK
- Polyprenyl transferase ausN
- Terpene cyclase ausL
Sequence:
MSDTPTRKTDLRVIIVGGSVAGLTLAHCLANANIDHIVLEKRAEISPQEGAFLGIWPNGGRIFDQLGVYADLEKCTVPIHKMRVRFPDGVSFSSELPRQVQERFGYPIISLDRQKVLEILYNRYPAKSNIHVNKKVTEIRQTEREAQVLTADGAVYKGDLVVGADGIHSAVRAEMWRQAKDLVGRRDRQDVNHEIAAFTVEYACVFGISSPISGLESGEHVNSYSNGLCVITFHGKDGRVFWFILIKLQKRFIYPFTPRFSASDAAKICAEYANVPVWGDICVRDLWGNKTSVSMTALEEGLLETWRFKRVVLLGDSIHKMTPNIGQGANTAAEDAGVLASLLQRLSTSDSSATSCTIDAVLQEYASLRYERVKSTYQRAYFGARLHTRDDALKAFVGRYIFPRFRQQVLERTSQAIAGAPQVDFLPTPKRTGPGWSDYAGSPEVGAPTLPWLVISLPVLASMLCYLVYSSVFVTPIFP
Protein: Meiotically up-regulated gene 96 protein (O94339)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in meiosis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Meiotically up-regulated gene 37 protein
- Probable 6-phosphogluconolactonase
Sequence:
MVIFSSYFSKQMNRFSTPFVFFFKKLNNTLKKSLQFIMRFHSYHPMFICLLRDSSRNENRKKKVSIGLRTIMRAFSFLMQVATCLIRYSLILTCLVAILLSVLWRIQFAALRMHDLIEEELKMFVLQHNCTLADLWSGKCPSSEDE
Protein: AT4g26650/T15N24_100 (RNA-binding (RRM/RBD/RNP motifs) family protein) (Q8W569)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- RNA binding
- Cleavage stimulating factor 64
Sequence:
MNPEEQKMESASDLGKLFIGGISWDTDEERLQEYFGKYGDLVEAVIMRDRTTGRARGFGFIVFADPSVAERVIMDKHIIDGRTVEAKKAVPRDDQQVLKRHASPMHLISPSHGGNGGGARTKKIFVGGLPSSITEAEFKNYFDQFGTIADVVVMYDHNTQRPRGFGFITFDSEESVDMVLHKTFHELNGKMVEVKRAVPKELSSTTPNRSPLIGYGNNYGVVPNRSSANSYFNSFPPGYNNNNLGSAGRFSPIGSGRNAFSSFGLGLNQELNLNSNFDGNTLGYSRIPGNQYFNSASPNRYNSPIGYNRGDSAYNPSNRDLWGNRSDSSGPGWNLGVSVGNNRGNWGLSSVVSDNNGYGRSYGAGSGLSGLSFAGNTNGFDGSIGELYRGSSVYSDSTWQQSMPHHQSSNELDGLSRSYGFGIDNVGSDPSANASEGYSGNYNVGNRQTHRGIEA
Protein: Sporulation-specific cell division protein SsgB (Sporulation of Streptomyces griseus-like protein B) (SsgA-like protein B) (SALP B) (Q9L268)
Organism: Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Function: Involved in sporulation-specific cell division. Required for early stages of sporulation. Important in the process of growth cessation prior to sporulation-specific cell division. Recruits cell division protein FtsZ to the future septum sites and tethers the contractile ring structure (Z ring) to the cytoplasmic membrane during sporulation. Stimulates polymerization and filament length of FtsZ in vitro (By similarity).
Subcellular location: Cell septum {ECO:0000269|PubMed:19567872, ECO:0000269|PubMed:21205868}. Note=Localizes to the divisome in sporogenic aerial hyphae in a ladder-like manner (PubMed:19567872, PubMed:21205868). Temporospatial localization is controlled by SsgA and it colocalizes with SsgA in presporulation foci. Localizes to the septum sites prior to FtsZ and after that colocalizes with FtsZ at the divisome throughout cell division (PubMed:21205868). {ECO:0000269|PubMed:19567872, ECO:0000269|PubMed:21205868}.
Interaction partners:
- Cell division protein FtsZ
- DNA-binding protein
- Membrane protein
- Transcriptional regulator
- Uncharacterized protein
- Zinc finger CGNR domain-containing protein
- Anti-sigma factor
- Aerial mycelium formation
Sequence:
MNTTVSCELHLRLVVSSESSLPVPAGLRYDTADPYAVHATFHTGAEETVEWVFARDLLAEGLHRPTGTGDVRVWPSRSHGQGVVCIALSSPEGEALLEAPARALESFLKRTDAAVPPGTEHRHFDLDQELSHILAES
Protein: F-box protein 2 (F-box protein OCP1) (Q8VD40)
Organism: Cavia porcellus (Guinea pig)
Interaction partners:
- S-phase kinase-associated protein 1
- S-phase kinase-associated protein 1
- Cullin-1
- F-box protein 4
- F-box/WD repeat-containing protein 7
- F-box protein 6
- F-box and WD repeat domain containing 11
- S-phase kinase-associated protein 2
- S-phase kinase-associated protein 2
- Beta-transducin repeat containing E3 ubiquitin protein ligase
Sequence:
MDGDGDPESVGQPEEVSPEEACAEEACAEGDRPGEEEEEEQEELEEAAYLAELPEALLLRVLAQLPAAELVQACRLVCLRWKELVDGAPLWLLKCQQEGLVPEGCGEEEERDHWQRFYFLSKRRRNLLRNPCGEEDLEGWCDVEHGGDGWRVEEIPGDSGVEFPQDDSVRKYFASSFEWCRKAQVVDLQAEGYWEELLDTTQPAIVAKDWYSGRSDAGCLYELSVKLLSEHEDVLAEFNTGQVPVSPDSEEGGWTEISHTFTDYGPGVRFVRFEHGGQDAVYWKGWFGARVTNSSVWVEP
Protein: SIP1b (Zinc finger E-box-binding homeobox 2b) (B0LVF0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MRELIMADGPRCKRRKQANPRRKNAAVLDFENVVETGSETEEEDRLLVSEEDALLNGAGSPASLVNHESEAPPSPTLSHTLLRKTVDDEDDMKDSGIENVWHENDLLNASIDGTDELKADYDTMGTDVSLEPIGNGTVKSVHCDTDFEDFFGKRKLVDTESHVVSIAEYLQRGDTAIIYPEAPEELSRSRLATPEATGHEENDLPPGTPDAFAQLLTCPYCDRGYKRLTSLKEHIKYRHEKNEENFACPLCSYTFAYRTQLERHMATHKPGRDQHQILNQGSGNRKFKCTECGKAFKYKHHLKEHLRIHSGEKPYECPNCKKRFSHSGSYSSHISSKKCIGLIAINGRVRNNLKTGSSPTSASSSPTNNAISQLRHKLENGKPLGLQDQSNHLNIKSEPLDFNDYKLMMASHGYATGSPFLNGGVRGGSPLGIHNSQSPLQHLGMGIEGQMLGYPSLGNNLSEVQKVLQIVDNTVCRQKMDCKPEEISKLKAYMKELGSHIEEQKQGLNSSGGGQGTLPLINHNGATKSIIDYTLEKVNEAKACLQSLTTDSKRQISNIKKEKANHMLDLGMEEKAHENNLMFTPFSCQYCKETFPGPIPLHQHERYLCKMNEEIKAVLQPAQNALTNKPGLFSEKHGLLHPSIIPEKSLNGPISPYKDHKSVLKAYFAMNMEPNSEELLKISIAVGLPQEFVKEWFEQRKVFQYTTSRTPPLDRSPVESIHPVSAHTPTKDSLGIRSPMSLVKGSDRITSPAIPELHNNCDTPLRLSKTPQYSNHKQLGDKMDHSRSNTPSPLNLSSASSKNSHTSSYTPNSFTSEDLQAEPLDLSLPKLMKEPKHILTVKSRLKLNSGPMDHNHVATPREHADEPLNLAYLSKKEFGSPNANSNLDKSSSPMFGLNPFAAKPMYTSLPPQSAFPPPTFMPPVQASLPGLRPYPSLDQISFLPHMAYTYAAGAASFAEMQQRRKYQRKPGFQSELLDGPADYLSSLDDMADPEACLSRKKIKKTESGMYACDLCDKTFQKSSSLLRHKYEHTGKRPHQCQICKKAFKHKHHLIEHSRLHSGEKPYQCDKCGKRFSHSGSYSQHMNHRYSYCKREAEEREAAEREAREKGHLEPTEMLLNRAYLQGIGPAGYPEHPEREPILRDALNGSIRERLQEVEGAFVKMSRREHDFEEEEDESENKSTDGDTMRDEEENGEHSMDESSKSESKSDHEDAMEDGV
Protein: Small ribosomal subunit protein bS16m (28S ribosomal protein S16, mitochondrial) (MRP-S16) (S16mt) (Q9V6Y3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q9Y3D3}.
Interaction partners:
- Small ribosomal subunit protein bS6m
- Mitochondrial ribosomal protein S11
- Small ribosomal subunit protein mS25
- Large ribosomal subunit protein bL9m
- Ribosomal protein
- Small ribosomal subunit protein uS15m
- Large ribosomal subunit protein bL32m
- Large ribosomal subunit protein bL27m
- Small ribosomal subunit protein mS29
- Large ribosomal subunit protein bL17m
Sequence:
MSLSPASGIGRFYAKSAKIIRFVRLGCTNRPFYHIVVMERRKNQHQPVIEQVGSFDPLPNDYNERLVALNTERIRYWLGKGAHLSTPAAELLGIAGLLPIHPRTYMTAWRNRRTAAEAEASPEKAESTA
Protein: Inwardly rectifying potassium channel 3, isoform C (X2JAW9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MQSDASPLGAAATDSLTMHRSTSMPVKPKPLEQKPLLRSSEKETVNASDYYPESPGFVRRRRSKAAGDHLETRSEQNFPYAHDWAGSTIELTPDLGSGPRTSSSDGLRRSLNRVMEKNGKENVVFRRIPEKSWRYMRDLVTTLVRSWFGHRKTSTPRADQSRSDVYSITPSIQRRLDELANEPPHLSPHFSKSNPNQNERVTFSI
Protein: Nuclear factor of activated T-cells c3 isoform IB-Xa (Nuclear factor of activated T-cells, cytoplasmic, calcineurin-dependent 3, isoform CRA_a) (B5B2S0)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MTTANCGAHDELDFKLVFGEDGAPAPPPPGSRPADLEPDDCASIYIFNVDPPPSTLTTPLCLPHHGLPSHSSVLSPSFQLQSHKNYEGTCEIPESKYSPLGGPKPFECPSIQITSISPNCHQELDAHEDDLQINDPEREFLERPSRDHLYLPLEPSYRESSLSPSPASSISSRSWFSDASSCESLSHIYDDVDSELNEAAARFTLGSPLTSPGGSPGGCPGEETWHQQYGLGHSLSPRQSPCHSPRSSVTDENWLSPRPASGPSSRPTSPCGKRRHSSAEVCYAGSLSPHHSPVPSPGHSPRGSVTEDTWLNASVHGGSGLGPAVFPFQYCVETDIPLKTRKTSEDQAAILPGKLELCSDDQGSLSPARETSIDDGLGSQYPLKKDSCGDQFLSVPSPFTWSKPKPGHTPIFRTSSLPPLDWPLPAHFGQCELKIEVQPKTHHRAHYETEGSRGAVKASTGGHPVVKLLGYNEKPINLQMFIGTADDRYLRPHAFYQVHRITGKTVATASQEIIIASTKVLEIPLLPENNMSASIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHIPQPSGKVLSLQIASIPVECSQRSAQELPHIEKYSINSCSVNGGHEMVVTGSNFLPESKIIFLEKGQDGRPQWEVEGKIIREKCQGAHIVLEVPPYHNPAVTAAVQVHFYLCNGKRKKSQSQRFTYTPVLMKQEHREEIDLSSVPSLPVPHPAQTQRPSSDSGCSHDSVLSGQRSLICSIPQTYASMVTSSHLPQLQCRDESVSKEQHMIPSPIVHQPFQVTPTPPVGSSYQPMQTNVVYNGPTCLPINAASSQEFDSVLFQQDATLSGLVNLGCQPLSSIPFHSSNSGSTGHLLAHTPHSVHTLPHLQSMGYHCSNTGQRSLSSPVADQITGQPSSQLQPITYGPSHSGSATTASPAASHPLASSPLSGPPSPQLQPMPYQSPSSGTASSPSPATRMHSGQHSTQAQSTGQGGLSAPSSLICHSLCDPASFPPDGATVSIKPEPEDREPNFATIGLQDITLDDDQFISDLEHQPSGSAEKWPNHSVLSCPAPFWRI
Protein: Esterase EstA (EC 3.1.1.1) (Autotransporter esterase EstA) (O33407)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Esterase whose enzymatic activity is required for rhamnolipid production, all kinds of cell motility (swimming, swarming, and twitching), and biofilm formation; the exact role of EstA in these processes is unclear. In vitro, has pronounced esterase activities towards p-nitrophenyl esters of short acyl chain length (C4-C6) and Tween detergents. Also shows relatively high activity towards beta-naphthyl butyrate, whereas its activities towards triacylglycerols and acyls-CoA are negligible.
Subcellular location: Cell outer membrane {ECO:0000269|PubMed:10559163, ECO:0000269|PubMed:17631636}; Multi-pass membrane protein {ECO:0000269|PubMed:10559163, ECO:0000269|PubMed:17631636}.
Interaction partners:
- DUF1302 domain-containing protein
- Esterase TesA
- Probable lipase
- Triacylglycerol lipase
- Polyhydroxyalkanoate synthesis protein PhaF
- Probable transcriptional regulator
- Probable serine protease
- Lipase LipC
- ChoE
- DUF3999 domain-containing protein
Sequence:
MIRMALKPLVAACLLASLSTAPQAAPSPYSTLVVFGDSLSDAGQFPDPAGPAGSTSRFTNRVGPTYQNGSGEIFGPTAPMLLGNQLGIAPGDLAASTSPVNAQQGIADGNNWAVGGYRTDQIYDSITAANGSLIERDNTLLRSRDGYLVDRARQGLGADPNALYYITGGGNDFLQGRILNDVQAQQAAGRLVDSVQALQQAGARYIVVWLLPDLGLTPATFGGPLQPFASQLSGTFNAELTAQLSQAGANVIPLNIPLLLKEGMANPASFGLAADQNLIGTCFSGNGCTMNPTYGINGSTPDPSKLLFNDSVHPTITGQRLIADYTYSLLSAPWELTLLPEMAHGTLRAYQDELRSQWQADWENWQNVGQWRGFVGGGGQRLDFDSQDSAASGDGNGYNLTLGGSYRIDEAWRAGVAAGFYRQKLEAGAKDSDYRMNSYMASAFVQYQENRWWADAALTGGYLDYDDLKRKFALGGGERSEKGDTNGHLWAFSARLGYDIAQQADSPWHLSPFVSADYARVEVDGYSEKGASATALDYDDQKRSSKRLGAGLQGKYAFGSDTQLFAEYAHEREYEDDTQDLTMSLNSLPGNRFTLEGYTPQDHLNRVSLGFSQKLAPELSLRGGYNWRKGEDDTQQSVSLALSLDF