lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Component of the cullin-RING ubiquitin ligases (CRL), or CUL3-RBX1-BTB protein E3 ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The functional specificity of the CRL complex depends on the BTB domain-containing protein as the substrate recognition component. Involved in embryo pattern formation and endosperm development. Required for the normal division and organization of the root stem cells and columella root cap cells. Regulates primary root growth by an unknown pathway, but in an ethylene-dependent manner. Functions in distal root patterning, by an ethylene-independent mechanism. Functionally redundant with CUL3B.
Sequence:
MSNQKKRNFQIEAFKHRVVVDPKYADKTWQILERAIHQIYNQDASGLSFEELYRNAYNMVLHKFGEKLYTGFIATMTSHLKEKSKLIEAAQGGSFLEELNKKWNEHNKALEMIRDILMYMDRTYIESTKKTHVHPMGLNLWRDNVVHFTKIHTRLLNTLLDLVQKERIGEVIDRGLMRNVIKMFMDLGESVYQEDFEKPFLDASSEFYKVESQEFIESCDCGDYLKKSEKRLTEEIERVAHYLDAKSEEKITSVVEKEMIANHMQRLVHMENSGLVNMLLNDKYEDLGRMYNLFRRVTNGLVTVRDVMTSHLREMGKQLVTDPEKSKDPVEFVQRLLDERDKYDKIINTAFGNDKTFQNALNSSFEYFINLNARSPEFISLFVDDKLRKGLKGITDVDVEVILDKVMMLFRYLQEKDVFEKYYKQHLAKRLLSGKTVSDDAERSLIVKLKTECGYQFTSKLEGMFTDMKTSEDTMRGFYGSHPELSEGPTLIVQVLTTGSWPTQPAVPCNLPAEVSVLCEKFRSYYLGTHTGRRLSWQTNMGTADIKAIFGKGQKHELNVSTFQMCVLMLFNNSDRLSYKEIEQATEIPAADLKRCLQSLACVKGKNVIKKEPMSKDIGEEDLFVVNDKFTSKFYKVKIGTVVAQKETEPEKQETRQRVEEDRKPQIEAAIVRIMKSRKILDHNNIIAEVTKQLQPRFLANPTEIKKRIESLIERDFLERDSTDRKLYRYLA
The following text describes a protein:
Function:
Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. It elongates telomeres. It is a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme.
Subcellular Localization:
Nucleus. Chromosome, telomere.
Sequence:
MTESGFDILKKVFAGRQVISLADLKDDGENNKKLPQLFRNAVAIHVQHQCKPRAAPQVGAEQQLDWYQLIESCDSNLFMRGLKDKWYLPCVTTSSVCECPFVPHATKSDWEALHAEIGTQKMKCLLIHCNIFVLVGSRALLQICGSLDKGDLEKSYPPIFKYRAAPKATKRKRKEIENVVAILPKTSTLSVLDRPSVKRPLKKIRLASSDGQSQNVEFLVDTSKSIPPIVDKIPDKPPTSLVPVLKKIRFQQSDSLSLPIPLSIEAKVPTNETEHPSSWKEMGKKKTRRWRNKLIAKQNVDNRRAIDGSIKIAHDEILYSSSGWTHFPITHPISHSSPNPTVLAILRAAVGTECNESEDQLRSNLPRLGQLIEVMMKNHRRCRYNPIVRRMLANSDYDPKKSFVDAGRVYLFIRCVIKKVVPIELLGGQTNQQIFLSNVRRFVEAGRGTSFTLNDLIQSMQTSKCHWFSHFSSLPVQISLLARLITWLFVGFVKPLIRQHFYATETSYGRNRIFFYSKDVWQRIHHRMLRSICSVSLRQPLPVLEKSTAPDPAAELQNLLLFARLRFVPKKNGSRPIMSTKFRNTSRKEVNTARLLLSTIAGLYAEGMDAKSTHSLHRKWVHFVENRDKEQPVYFVNADVEDAFGSIDHQKMVALLKGYGRTLPKELQIRTLCTVRPDGRRSKPFQVIPYFHKTNPEGWVQQMSPGTVVFHSGTRTEKLDIVKILQFAIKSVREVHVVHHDKTHYRLKRGIPQGSQLSSALCHIYYGHLVREHLFEFLNHPEDLLIRVVDDFLYLTTNGERARAFHHRIHQGFTDYNAYVNINKSATNLDLTEPRDETKDKPVRKPVWFSFCGLQFHTKTLEIRGDYTKYEGTDIIHCITPTSGEPGKLLLKRLKGISTLKIETIYLDARVNRKPTITRSMFNACLMAAFRFHAIVKHVLMRSTRRHHWCDKALDARYLAHTVIKECCSKMVGHVSSVHRRRKDVKIILSRTETAWLCYEAFHRKLNQHEKLYSNVLLAIRMLQNEYEKKLPEAKLRNIRSWIGRRIPRSFRRMKDRVT
The following text describes a protein:
Function:
Functions in the anterograde transport of storage protein precursors from the endoplasmic reticulum (ER) to the Golgi complex and in the retrograde transport from the Golgi complex to the ER. Forms a complex with ZW10/MIP1, MIP2 and MIP3 on the ER that may be responsible for efficient transport of seed storage proteins. Required for the responses to environmental stresses during seed germination and vegetative growth. Probably not involved in the retrograde transport from the ER to the apoplast.
Subcellular Localization:
Endoplasmic reticulum membrane; Peripheral membrane protein.
Sequence:
MEAIKPLPQVSSFSASVFSFLDGRFKESTDLSHSTGLVSELQTEISELDQRLAGLNRQLESGLAAYASFSDRVGGLFFEVNAKLADLSSSTSVTRSASDSGKEEEATEHVAGEDLPSLAKEVAQVESVRAYAETALKLDTLVGDIEDAVMSSLNKNLRTSRSSGFEEVRLHAIKTLKTTEEILSSVAKRHPRWARLVSAVDHRVDRALAMMRPQAIADYRALLSSLRWPPQLSTLTSASLDSKSENVQNPLFNMEGSLKSQYCGSFHALCSLQGLQLQRKSRQLGIHKGENVLFHQPLWAIEELVNPLTVASQRHFTKWSEKPEFIFALVYKITRDYVDSMDELLQPLVDEAKLAGYSCREEWVSAMVSSLSLYLVKEIFPIYVGQLDEANETDLRSEAKVSWLHLIDLMISFDKRVQSLVSQSGILSLQEDGNLLRISSLSVFCDRPDWLDLWAEIELDERLVKFKEEIDNDRNWTAKVQDELISSSNVYRPPIISSIFLQHLSSIIERSKSVPALYLRARFLRLAASPTIHKFLDCLLLRCQDADGLTALTENNDLIKVSNSINAGHYIESVLEEWSEDVFFLEMGTGQHDPQEVPGLENFTEPSEGIFGEEFEKLEKFRLEWINKLSVVILRGFDARIREYIKNRKQWQEKKDKEWTVSRALVGALDYLQGKTSIIEENLNKADFTAMWRTLASEIDKLFFNSILMANVKFTNDGVERLKVDMEVLYGVFRTWCVRPEGFFPKLSEGLTLLKMEEKQVKDGLSRGDKWLRENRIRYLSEAEAKKVAKSRVFS
The following text describes a protein:
Function:
Major component of the virus occlusion bodies which are large proteinaceous structures termed polyhedra. These structures serve as the protective package for the virus particles outside the infected host and allow natural transmission of virus between insect hosts, assisting persistence in the environment. Forms the paracrystalline lattice of polyhedra and interacts with enveloped virions as well as other accessory molecules and structures to form a mature viral occlusion body.
Subcellular Localization:
Host nucleus.
Sequence:
MPDYSYRPTIGRTYVYDNKYYKNLGAVIKNAKRKKHFAEHEIEEATLDPLDNYLVAEDPFLGPGKNQKLTLFKEIRNVKPDTMKLVVGWKGKEFYRETWTRFMEDSFPIVNDQEVMDVFLVVNMRPTRPNRCYKFLAQHALRCDPDYVPHDVIRIVEPSWVGSNNEYRISLAKKGGGCPIMNLHSEYTNSFEQFIDRVIWENFYKPIVYIGTDSAEEEEILLEVSLVFKVKEFAPDAPLFTGPAY
The following text describes a protein:
Function:
Acyl-CoA ligase; part of the siderophore biosynthetic pathway. Aspergillus fumigatus produces 4 types of siderophores, low-molecular-mass iron chelators, including excreted fusarinine C (FsC) and triacetylfusarinine C (TAFC) for iron uptake and intacellular ferricrocin (FC) for hyphal and hydroxyferricrocin (HFC) for conidial iron distribution and storage. TAFC consists of 3 N(2)-acetyl-N(5)-anhydromevalonyl-N(5)-hydroxyornithine residues cyclically linked by ester bonds; FC is a cyclic hexapeptide with the structure Gly-Ser-Gly-(N(5)-acetyl-N(5)-hydroxyornithine)x3. The biosynthesis of all four siderophores depends on the hydroxylation of ornithine, catalyzed by the monooxygenase sidA. Subsequently, the pathways for biosynthesis of extra- and intracellular siderophores split. For biosynthesis of extracellular siderophores, the transacylase sidF transfers anhydromevalonyl to N(5)-hydroxyornithine. The required anhydromevalonyl-CoA moiety is derived from mevalonate by CoA ligation and dehydration catalyzed by sidI and sidH respectively. The acetylation of N(5)-hydroxyornithine for FC biosynthesis involves the constitutively expressed sidL. FC is hydroxylated to HFC by an as yet uncharacterized enzyme during conidiation. Assembly of fusarinine C (FsC) and FC is catalyzed by two different nonribosomal peptide synthetases (NRPS), sidD and sidC respectively. Subsequently, sidG catalyzes N2-acetylation of FsC for forming TAFC. Both extra- and intracellular siderophores are crucial for growth during iron limitation and virulence.
Subcellular Localization:
Peroxisome. Note=Targeted to peroxisomes via its PTS2-type peroxisomal targeting signal and the corresponding receptor pexG.
Sequence:
MATIRRLQQTLSHLRPPKAPQLLSIVEGPTQPELLDITLGELLTLQSLQYGDYECLVFPWTGARWTYTDLKDEADRVARGLLAMGIQKGDRIGIMAGNCEQYISVFFAAARVGAILVVLNNTYTPSELYYALGHTDCRLLFLTPRIGRHSLEEVLAKLGPRPKEQGTSSALEEIIILRGQYSGFSTYEHVIQRGLPLPSHALQDREAELHSTDVCNLQFTSGSTGNPKAAMLTHHNLVNNSRFIGDRMNLTSFDILCCPPPLFHCFGLVLGMLAVVTHGSKIIFPSETFDPTAVLHAISDEKCTALHGVPTMFEAILSLPKPPNFDCSNLRTGIIAGAPVPRPLMKRLLEELNMTEYTSSYGLTEASPTCFNALTTDSIERRLTTVGKVMPHAKAKIIDTQGHIVPIGQRGELCIAGYQLTKGYWNNPEKTAEALITDSDGVTWLKTGDEAIFDEEGYCSITGRFKDIIIRGGENIYPLEIEERLAAHPAIEVASVIGIPDQKYGEVVGAFLALAADVSARPSDEELRAWTRETLGRHKAPQYFFVFGEEGVDRTIPVTGSGKVRKVDLRKIAASVLERRLAKTAAIKEK
The following text describes a protein:
Function:
Confers resistance to late blight (Phytophthora infestans) races carrying the avirulence gene Avr1. Resistance proteins guard the plant against pathogens that contain an appropriate avirulence protein via an indirect interaction with this avirulence protein. That triggers a defense system including the hypersensitive response, which restricts the pathogen growth.
Subcellular Localization:
Membrane; Peripheral membrane protein. Plastid, chloroplast.
Sequence:
MAFLRSIVTAKTTAIAAAIPAAAFAVSSISSSSSQFERPSKNLKFGSISSSNPILQLSFAKNLQKTSPPSALHMETPSSNHQTSSDNGVVLPELLTEFMVDMSCQGCVNAVKSKLQTVEGVKNVDVDLDNQVVRILGSSPVKTMTEALEQTGRKARLIGQGVPDDFLISAAVAEFKGPDIFGVVRLAQVNMELTRIEANFSGLSPGKHAWSINEFGDLTRGAASTGKLYSPPLGDLVTLEVDEKGEAFYTGPKEKLRVADLIGRAIAVYATEDKTDPGLTAAVIARSAGVGENYKKICACDGTTIWEATNKL
The following text describes a protein:
Function:
Component of the telomerase complex involved in telomere replication. Stimulates RNA/DNA heteroduplex unwinding which favors the telomere replication by the telomerase.
Miscellaneous:
MISCELLANEOUS: [Isoform 1]: Produced by ribosomal frameshifting between codon Leu-92 and Val-93; MISCELLANEOUS: [Isoform 2]: Produced from conventional translation of the YIL009C-A ORF. There is no apparent role for isoform 2 in the cell.
Subcellular Localization:
Nucleus. Chromosome, telomere.
Sequence:
MPKVILESHSKPTDSVFLQPWIKALIEDNSEHDQYHPSGHVIPSLTKQDLALPHMSPTILTNPCHFAKITKFYNVCDYKVYASIRDSSHQILVEFSQECVSNFERTHNCRITSETTNCLMIIGDADLVYVTNSRAMSHFKICLSNISSKEIVPVLNVNQATIFDIDQVGSLSTFPFVYKYL
The following text describes a protein:
Function:
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 unsing 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix (By similarity). NDUFA4 is required for complex IV maintenance (By similarity).
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MLRQIIGQAKRHPSLIPLFIFIGAGGTGAALYVTRLALFNPDVSWDRKNNPEPWNKLGPNDQYKFYSVNVDYSKLKKEGPDF
The following text describes a protein:
Function:
Functions as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Arp2/3 complex plays a critical role in the control of cell morphogenesis via the modulation of cell polarity development.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MAMKDLDALFSSLDPEYYNILMKYLYRGLSTGDRPTCDQCLRIHERLTERAGLGCILRSLADTTNTV
The following text describes a protein:
Function:
Catalyzes the conversion of 2 pyruvate molecules into acetolactate in the first common step of the biosynthetic pathway of the branched-amino acids such as leucine, isoleucine, and valine.
Sequence:
MTVGDHLVARMRAAGISVVCGLPTSRLDSLLVRLSRDAGFQIVLARHEGGAGYLADGFARASGKSAAVFVAGPGATNVISAVANASVNQVPMLILTGEVAVGEFGLHSQQDTSDDGLGLGATFRRFCRCSVSIESIANARSKIDSAFRALASIPRGPVHIALPRDLVDERLPAHQLGTAAAGLGGLRTLAPCGPDVADEVIGRLDRSRAPMLVLGNGCRLDGIGEQIVAFCEKAGLPFATTPNGRGIVAETHPLSLGVLGIFGDGRADEYLFDTPCDLLIAVGVSFGGLVTRSFSPRWRGLKADVVHVDPDPSAVGRFVATSLGITTSGRAFVNALNCGRPPRFCRRVGVRPPAPAALPGTPQARGESIHPLELMHELDRELAPNATICADVGTCISWTFRGIPVRRPGRFFATVDFSPMGCGIAGAIGVALARPEEHVICIAGDGAFLMHGTEISTAVAHGIRVTWAVLNDGQMSASAGPVSGRMDPSPVARIGANDLAAMARALGAEGIRVDTRCELRAGVQKALAATGPCVLDIAIDPEINKPDIGLGR
The following text describes a protein:
Function:
The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. The coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins.
Subcellular Localization:
Cytoplasmic vesicle, COPI-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side.
Sequence:
MAEPDELYTLRAQYWLGHYTLALDEGRQAARRPMPPHLKSEREELVLRCQLALGQYDLVIAEGSGGGKSPSMQALALHARYLSASPEARPSVVDSLKVLLSQPDAPSNTSLQLTACHVFLHSNLLREALQCVHMGLTMEHLSMCVQIYIKIDRLDLANDALNLLKQADEDSVLAQLGSAQVAIASGRSRSEDAVHLLSGLSEQYGPSIMLLNCLAVANMVGGRYEAAEGNLREAMGEEFGGERDADTLVNMVVCGTHLGRKGEEVEKYLELLRGGFGDHPFVQGLVQVEGAFERESHKYQVRA
The following text describes a protein:
Function:
Acts in a DNA repair pathway for removal of UV-induced DNA damage that is distinct from classical nucleotide excision repair and in repair of ionizing radiation damage. Functions in homologous recombination repair of DNA double strand breaks and in recovery of stalled replication forks. Probably plays a role in structure.
Miscellaneous:
MISCELLANEOUS: Present with 339 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus. Chromosome.
Domain:
The flexible hinge domain, which separates the large intramolecular coiled coil regions, allows the heterotypic interaction with the corresponding domain of SMC5, forming a V-shaped heterodimer.
Sequence:
MISTTISGKRPIEQVDDELLSLTAQQENEEQQQQRKRRRHQFAPMTQFNSNTLDEDSGFRSSSDVATADQDNFLEESPSGYIKKVILRNFMCHEHFELELGSRLNFIVGNNGSGKSAILTAITIGLGAKASETNRGSSLKDLIREGCYSAKIILHLDNSKYGAYQQGIFGNEIIVERIIKRDGPASFSLRSENGKEISNKKKDIQTVVDYFSVPVSNPMCFLSQDAARSFLTASTSQDKYSHFMKGTLLQEITENLLYASAIHDSAQENMALHLENLKSLKAEYEDAKKLLRELNQTSDLNERKMLLQAKSLWIDVAHNTDACKNLENEISGIQQKVDEVTEKIRNRQEKIERYTSDGTTIEAQIDAKVIYVNEKDSEHQNARELLRDVKSRFEKEKSNQAEAQSNIDQGRKKVDALNKTIAHLEEELTKEMGGDKDQMRQELEQLEKANEKLREVNNSLVVSLQDVKNEERDIQHERESELRTISRSIQNKKVELQNIAKGNDTFLMNFDRNMDRLLRTIEQRKNEFETPAIGPLGSLVTIRKGFEKWTRSIQRAISSSLNAFVVSNPKDNRLFRDIMRSCGIRSNIPIVTYCLSQFDYSKGRAHGNYPTIVDALEFSKPEIECLFVDLSRIERIVLIEDKNEARNFLQRNPVNVNMALSLRDRRSGFQLSGGYRLDTVTYQDKIRLKVNSSSDNGTQYLKDLIEQETKELQNIRDRYEEKLSEVRSRLKEIDGRLKSTKNEMRKTNFRMTELKMNVGKVVDTGILNSKINERKNQEQAIASYEAAKEELGLKIEQIAQEAQPIKEQYDSTKLALVEAQDELQQLKEDINSRQSKIQKYKDDTIYYEDKKKVYLENIKKIEVNVAALKEGIQRQIQNACAFCSKERIENVDLPDTQEEIKRELDKVSRMIQKAEKSLGLSQEEVIALFEKCRNKYKEGQKKYMEIDEALNRLHNSLKARDQNYKNAEKGTCFDADMDFRASLKVRKFSGNLSFIKDTKSLEIYILTTNDEKARNVDTLSGGEKSFSQMALLLATWKPMRSRIIALDEFDVFMDQVNRKIGTTLIVKKLKDIARTQTIIITPQDIGKIADIDSSGVSIHRMRDPERQNNSNFYN
The following text describes a protein:
Function:
Is involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
Subcellular Localization:
Cytoplasm, cytosol.
Sequence:
MAEVKLHGFWYNLFTLRVVWTLKLKGIPYLNIEKDRYNKSLQLLEYNPVYRKTPVLVHNGKPLCESMLIVEYIDEIWPHNSLLPADTYERALARFWIKYADEIFPAVSAFFSSNNDEEREKSIEKIWEHLRVVENQCFGDQKKFFGGDIINIVEIDFGSIFKFLVAEDILKRRSWKMRNSLTCTHGIIISRMFQLLKKTSQTMRKWWLLLSLLEKNVWHLPKKVIYIRSSMNESLCICLNRFFMRVC
The following text describes a protein:
Function:
[GLV11p]: Acts as a peptide hormone recognized by receptors (e.g. RGI1 and RGI2) to trigger signaling events including the regulation of RITF1 expression and leading to the production of reactive oxygen species (ROS) in roots to modulate meristem size. Signaling peptide (root growth factor) that maintains the postembryonic root stem cell niche in a PIN2-traffic dependent manner by regulating the expression levels and patterns of the transcription factor PLETHORA (PLT), mainly at the post-transcriptional level. Maintains the postembryonic root stem cell niche by regulating the expression levels and patterns of the transcription factor PLETHORA (e.g. PLT1 and PLT2), mainly at the post-transcriptional level. Influences circumferential cell number in the root meristem in response to Pi-deprivation. Regulates the pattern of root growth and lateral root development by modulating the length and the number of cortical cells in the root apical meristem (RAM), and the anticlinal asymmetric cell divisions in lateral root initiation cells.
Miscellaneous:
MISCELLANEOUS: Diffuses into the meristematic region; MISCELLANEOUS: 'Golven' means irregular waves in Dutch.
Subcellular Localization:
[GLV11p]: Secreted.
Sequence:
MVSIRVICYLLVFSVLQVHAKVSNANFNSQAPQMKNSEGLGASNGTQIAKKHAEDVIENRKTLKHVNVKVEANEKNGLEIESKEMVKKRKNKKRLTKTESLTADYSNPGHHPPRHN
The following text describes a protein:
Function:
The PDCD1-mediated inhibitory pathway is exploited by tumors to attenuate anti-tumor immunity and escape destruction by the immune system, thereby facilitating tumor survival. The interaction with PDCD1/PD-1 inhibits cytotoxic T lymphocytes (CTLs) effector function. The blockage of the PDCD1-mediated pathway results in the reversal of the exhausted T-cell phenotype and the normalization of the anti-tumor response, providing a rationale for cancer immunotherapy.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein. Early endosome membrane; Single-pass type I membrane protein. Recycling endosome membrane; Single-pass type I membrane protein.
Sequence:
MRICSIFTFMAYCCLLEAFTITVPKDMYEVEYGSNVTLECRFPVDKQLNLLALVVYWEMKDKKIIQFVNGEEDLNVQHSSYSQRAQLLKDQLFLGKASLQITDVKLQDAGVYCCLISYGGADYKRITLKVNAPYRKINQRMSLDPVTSEHELTCQAEGYPEAEVIWTSSDYQILSGKTTITSSQREEKLFNVTSTLRVNATTNEIFYCTFRRLGPEENSTAVLVIPEPYVDPARKRTHWVILGALLLLIAVTAIFCLKRNVRMMDVEKCGSRDMKSEKQNDTQFEET
The following text describes a protein:
Function:
Has antibacterial activity.
Subcellular Localization:
Secreted.
Sequence:
MKTFLFLFAVFFFLDPAKNAFFDEKCSRINGRCTESCLKNEELIALCQKNLKCCVTVQPCGRDKGDELDEDSGYNRTRG
The following text describes a protein:
Function:
May act as a general Rab protein regulator.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MSSSSSIKLQPWNDFIEWGRYSIPGSQNAITRMEDNLNFYSGNYIAIVAVVLLITLFTNMNLLVAILLLGAIGYYLFFVQKGDKNIGFAVLTPMIQMVILGVVSVIVIYKLSGLTLFYTTLVSLLFVLAHSALKMRNLKNKASNFVSGIKNDLKNELK
The following text describes a protein:
Function:
Multifunctional regulatory protein whose primary function is to antagonize members of the transforming growth factor beta (TGF-beta) superfamily including activin, myostatin, GDF11 or bone morphogenetic proteins (BMPs). Mechanistically, binds to these ligands in the extracellular space, blocking their type II receptor-binding site to inhibit downstream signaling. Plays an essential role in muscle fiber formation and growth both by preventing the repressive effects of myostatin and through SMAD3/AKT/mTOR signaling independently of myostatin. Also promotes neural differentiation by antagonizing the action BMP4. Acts as a specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (FSH) by sequestering activin A/INHBA. On the other hand, translocates into the nucleus where it down-regulates rRNA synthesis and ribosome biogenesis to maintain cellular energy homeostasis by binding to rDNA.
Subcellular Localization:
Secreted.
Sequence:
MVRARHQPGGLCLLLLLLCQFMEDRSAQAGNCWLRQAKNGRCQVLYKTELSKEECCSTGRLSTSWTEEDVNDNTLFKWMIFNGGAPNCIPCKETCENVDCGPGKKCRMNKKNKPRCVCAPDCSNITWKGPVCGLDGKTYRNECALLKARCKEQPELEVQYQGRCKKTCRDVFCPGSSTCVVDQTNNAYCVTCNRICPEPASSEQYLCGNDGVTYSSACHLRKATCLLGRSIGLAYEGKCIKAKSCEDIQCTGGKKCLWDFKVGRGRCSLCDELCPDSKSDEPVCASDNATYASECAMKEAACSSGVLLEVKHSGSCNSISEDTEEEEEDEDQDYSFPISSILEW
The following text describes a protein:
Function:
Central protein that confers the ability to take up biotin on E.coli; while biotin transport requires BioM at very low (pM) concentrations at higher (nM) concentrations expression of BioY alone suffices for uptake.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MERNVTLIGLFAALIVALGFVPAIPLGFGVPITLQSLGVMLAGAVLGSWRGALAVLLVQALVAIGLPVLAGGRGGLGIFVGPTAGFLIGWLPAAFVTGLIVERLRRVPVALAAGIGATLGGIIIMYALGILGFWLVKNAGLKPEDAPISLWAATAIMAPFIPGDLVKVVVTGLVARTIAQYRPSALLARG
The following text describes a protein:
Function:
RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. This subunit can bind 18S rRNA. Binds to GC-rich 5'UTRs in cholinergic motor neurons, thereby may play a role in translational regulation of mRNAs involved in neuropeptide signaling and stress response, including hlh-30 isoform d and ncs-2.
Subcellular Localization:
Cytoplasm.
Sequence:
MTGINAMAPAPEVVSWAEAVEQDNAPHIQEGADGTRTETAFTEVDGVRWKVVTQFKVINKRVPKVVADRKKWVKFGSCKGEPAGPQVATTYVAEEVDMQFTRNRAGEQILDVQEDKQTAKTTSREHCRHCKGNDHWSTHCPYKVMYQLDEEADADKDTEKDRMAMGMRPDGRQIDRNRSDENTCRVTNLPQEMNEDELRDLFGKIGRVIRIFIARDKVTGLPKGFAFVTFESRDDAARAIAELNDIRMYHMVLKVEWTRPSN
The following text describes a protein:
Function:
6'-oxoglucosaminyl:L-glutamate aminotransferase that catalyzes pyridoxal-5'-phosphate-mediated transamination for the conversion of paromamine to neamine in the biosynthetic pathway of neomycin. Also able to catalyze deamination at C-6''' of neomycin.
Sequence:
MTKNSSLLAEFPTCPRDEKDRPRVFTAASGAWLTDESGFRWIDFDNARGSILLGHGDPVVAEAVARAATGADGTATGWSRRVDAVLERLHALCGGEVVGLFRSGTAAVRAAVLAVREATGRPLLLSAGYHGYDPMWYPSEAPLEPNADGVVDFFFDLGLLRELLRAPERVAAVVVSPDHMHLSPGWYRELRRLCSAAGVVLVADEVKVGLRYAPGLSTAELLAPDVWVVAKGMANGHAVSAVGGSRRLLKPLKEVSFTSFFEPTILAAADAALARVATGEPQRAVREAGDRFLRHARKALDDASLPVEIAGDGTFFQFVPATEELEEALYGAANAEGLLFYAGDNQGVSAAFDEAVLGEAERRFARVCERLAPYAGGEPVGDAARYRVAWNVMDGLRQAPRDREETTGLLARLLDD
The following text describes a protein:
Function:
Central component of cohesin, a complex required for chromosome cohesion during the cell cycle. The cohesin complex may form a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. Cohesion is coupled to DNA replication and is involved in DNA repair. The cohesin complex also plays an important role in spindle pole assembly during mitosis and in chromosomes movement.
Subcellular Localization:
Chromosome, centromere. Nucleus.
Sequence:
MYIKQVIIQGFKSYREQTVVEPFHPGHNVVVGRNGSGKSNFFYAIQFVLSDEFNHLRPEQRQALLHEGTGPRVISAYVEIIFDNTDNRLPIDKKEVSLRRVIGSKKDQYFLSKKMVTKADVVNLLESAGFSRSNPYYIVKQGKINQMATAPDSHRLKLLREVAGTRVYDERKAESETIMKETQGKREKIEEFLRTIEDRLKTLEEEKEELKEYQKWDKIRRAVEYTIHDRELKETRKKLDDMENTRKDSGDRQDKLRQQLERAQENSKSASRELRDLKHRAQAAREERDTLNAEQQQLLKEKSKLELTIKDLSDEVQGDNQSKERAERELQRLHETIAQKDGELERIKPQYEEMKRREEECTRELALKEQKRKELYAKQGRGSQFTSRDQRDTWIQNELKSLSKAIKEKNEQIERLQEDLKRDSRKRVELEKKIEEMTSEMENHRLSIDDHNKVFYDMKKRKDLLQTERSGLWRNETLVQQNLASSKEELAKSDQVLRSLAGKPILNGRDSVRQVLDNMRSKGGRMAEIADSYHGLVIENFDCDKSIFTAVEVTAGNRMFHHIVESDRVGTEILKQMNHEKLPGEVTFMPLNRLNVRETNYPPTEDALPMVTKLQYSDRFDKAMRYIFGKTMICRNLEVASVLARTTGLDCVTLDGDQVSSKGSLTGGYVNTSRCRLEVYKTRSTLNAQVAEKEKELADCRSKLQQVESEVNQLLSEIQRTETKNSKSKDVFEKVKADIRLMREELNNIERSKQPKERSLAQLRSSLEAMQSTKEGLESELHQELMTQLSVTDQLEVDRLNDDIRRLTQENKDAFIQRMRLEADKNKLENLLTNNLIRRRDELQQALQEISVEDRNRKLDHCRSELGTVERRLDDVSDALKDVEKKVSDLSRKQKEAQTDLEKLRFKEKDIDERLAESAKDFDKMASRQTALQQKITECTEKIRDLGSLPSDSFDKYQSMATKLLFKQLEKANSELKKYSHVNKKALDQFISFSEEKSKLLERKEELDHGYDKIKELMSTLEYRKYEALQFTFKQVSKYFSEVFQRLVPNGHAYLKVSNSEDASASFGDTEGTDQFTGVAIKVSFSGQNAEMKDMNQLSGGQKSLVALALIFSIQKCDPAPFYLFDEIDQALDAQHRKGVADMIHEHSKNAQFITTTFRPELLEHSDKYYGVKFRNKVSHVECVTREEAYDFVEDDQTHG