lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
N-alpha-acetyltransferase that specifically mediates the acetylation of N-terminal residues of the transmembrane proteins, with a strong preference for N-termini facing the cytosol. Displays N-terminal acetyltransferase activity towards a range of N-terminal sequences including those starting with Met-Lys, Met-Val, Met-Ala and Met-Met. Required for normal chromosomal segregation during anaphase. May also show histone acetyltransferase activity; such results are however unclear in vivo and would require additional experimental evidences.
Subcellular Localization:
Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. Note=Probably forms a intramembrane hairpin-like structure in the membrane.
Sequence:
MTEVVPSSALSEVSLRLLCHDDIDTVKHLCGDWFPIEYPDSWYRDITSNKKFFSLAATYRGAIVGMIVAEIKNRTKIHKEDGDILASSFSVDTQVAYILSLGVVKEFRKHGIGSLLLESLKDHISTTAQDHCKAIYLHVLTTNNTAINFYENRDFRQHHYLPYYYSIRGVLKDGFTYVLYINGGHPPWTILDYIQHLGSALANLSPCSIPHRIYRQAHSLLCSFLPWSSISSKGGIEYSRTM
The following text describes a protein:
Function:
Plays a role in the cellular response to DNA damage and the maintenance of genome stability through its association with the MRN damage-sensing complex. Promotes chromatin loading and activity of the MRN complex to facilitate subsequent ATM-mediated DNA damage response signaling and DNA repair.
Subcellular Localization:
Nucleus. Nucleus, nucleoplasm. Note=Recruited to sites of DNA damage. Phosphorylation on Ser-115 induces its nuclear localization and promotes genome stability.
Sequence:
MASLQRSRVLRCCSCRLFQAHQVKKSVKWTCKACGEKQSFLQAYGEGSGADCRRHVQKLNLLQGQVSELPLRSLEETVSASEEENVGHQQAGNVKQQEKSQPSESRWLKYLEKDSQELELEGTGVCFSKQPSSKMEEPGPRFSQDLPRKRKWSRSTVQPPCSRGVQDSGGSEVAWGPQKGQAGLTWKVKQGSSPCLQENSADCSAGELRGPGKELWSPIQQVTATSSKWAQFVLPPRKSSHVDSEQPRSLQRDPRPAGPAQAKQGTPRAQASREGLSRPTAAVQLPRATHPVTSGSERPCGKTSWDARTPWAEGGPLVLEAQNPRPTRLCDLFITGEDFDDDV
The following text describes a protein:
Function:
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Subcellular Localization:
Nucleus.
Sequence:
MSVLLETTIGDLVVDLDYKTCSAESYNFLKLCKTRFYDCQCIYDLHPEGSARLGDPQVGFAFRTDLPVHNTSIEGLRDTRAVTPKLIEASVAAQPAERFGQVAFVLKPGTRLLGSNILLALNPEPRPHINTVRFAQVIDESLAVLQQLSDVPRDLHHLPRTDIRIRRAHILYDPFPDNRPLPVFLPPVTAARVRLPSADKGSPETLTGAKELTLEILGDIRRAGIAPAENVLFVCKLNPLTRAADLATVFAQFGHVNSVEIIRDRDSGRSLGYGFVEFATKAACELAYTKMDGALIDDRRVHVDFSQSLK
The following text describes a protein:
Function:
Glycosyltransferase that generates the core 1 O-glycan Gal-beta1-3GalNAc-alpha1-Ser/Thr (T antigen), which is a precursor for many extended O-glycans in glycoproteins.
Subcellular Localization:
Membrane; Single-pass type II membrane protein.
Sequence:
MTSPNHHQTKALAVKETWGKRCNILLFMSSAYDSKLPTVQLGVKEGRNRLWGKTRESFRYAWNRYQDKVDWFLKADDDTYVVLENLRYFLTPYNTSKPLWFGHKYKSDVKSGYFSGGAGYVLSKEATRRFVKDGYYNALICRHDHQGAEDLEMGKCMENLNVSTMDTRDSKGRGRFFPFSPELHYFPNEIPQDSWYWRNIYYSTNKGSDCCSDSAISFHYVSARQMRILDYLIYQLRPFGIPADGRPAMPDPPPDSNLTATPWFASNNETTATDPTTNNTSSMEYDDNDGTSQTDEISQEDSKLTAETRLLHNPVRAIASMFGLPRRLFPPASKTAKRL
The following text describes a protein:
Function:
Functions within a multiprotein E3 ubiquitin ligase complex, catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins.
Subcellular Localization:
Cytoplasm, cytosol. Endoplasmic reticulum. Mitochondrion outer membrane. Nucleus. Postsynaptic density. Presynapse.
Sequence:
MIVFVRFNSSHGFPVEVDSDTSIFQLKEVVAKRQGVPTDQLRVIFAGKELRNDWTVQNCDLDQQSIVHIVQRPRRKGQEMNATGGDNARNTAGGCEREPQSLTRVDLSSSVLPGDSVGLAVILHTDSRNDSPPAGSPADRPIYNSFYVYCKGPCQRVQPGKLRVQCSTCRQATLTLTQGPSCWDDVLIPNRMSGECQSPHCPGTTAEFFFKCGAHPTSDKETSVALHLIATNSRNITCITCTDVRSPVLVFQCNSRHVICLDCFHLYCVTRLNDRQFVHDPQLGYSLPCVAGCPNSLIKELHHFRILGEEQYNRYQQYGAEECVLQMGGVLCPRPGCGAGLLPESDQRKVTCEGGNSLGCGFAFCRECKEAYHEGECSALFEASGTTTQAYRVDERAAEQARWEEASKETIKKTTKPCPRCHVPVEKNGGCMHMKCPQPQCRLEWCWNCGCEWNRVCMGDHWFDV
The following text describes a protein:
Function:
Methyltransferase that adds a 2'-O-methyl group at the 3'-end of PIWI-interacting RNAs (piRNAs) and small interfering RNAs (siRNAs) which are classes of regulatory RNAs that are involved in gene silencing in endogenous RNA interference (RNAi) pathways. Methylation protects the 3'-end of small RNAs from tailing and trimming and could constitute a recognition signal for appropriate argonaute machineries (Probable). Methylates and stabilizes 26G-siRNAs (a class of 26 nucleotide siRNAs that possess a monophosphorylated guanine residue at the 5'-end) when they are bound by argonaute protein ergo-1. This occurs in the female germline and embryo, but not in the male germline. Does not methylate 26G-siRNAs bound by argonaute proteins alg-3 or alg-4. Methylates and stabilizes 21U-piRNAs, which are a class of 21 nucleotide piRNAs that possess a uracil residue at the 5'-end, in the male and female germline. In addition, may play a role in exogenous RNAi (exoRNAi) pathways in the germline.
Subcellular Localization:
Cytoplasm. Nucleus, nucleoplasm. Cytoplasmic granule. Note=Nucleoplasm localization ceases following fertilization. In embryos, diffusely localized in the cytoplasm. In cells of the P-lineage (germ cell progenitor cells) in embryos, localizes to granules and at later postembryonic stages of development, localizes to perinuclear granules in the germ cells.
Sequence:
MAHTSDGWGAPYDNQTYVEAYEQLEIALLEPLDRILETANVEEFRPKFKNHQDPNDRKNKKNNDEEWRDSIYNIATDESDTDDHEQRKNFFQPPLQVQRNSFVKNTLMEFKRSSQIDISRLAVMGCGEMSLEKGICEYLGSFGTINVLSVDIDEPSLSIGQQLLGKHLERNAEILAVETGLPVLMRSYVGDILEPDHRFADVDAIVSMEVVEHIPLPNAKKFVENVLGTLMPRIFIFSTPNHEYNAVFGMEPGEFRHGDHKFEMNRKEFSNWLEELSIRFPHYQIDPPHYIGMTRGYENLSGASQAAVCRLQVDLNTTLPQEVTPYEMVGHLPCRLGSRLIAYNLVKEAFLDWLEKIELQEHEPRTDGYSPYWIFNVQNILHHLKAPVSFALTIDEKVAIKYIQGMTSRKVHAEYSHGFNGIVILQMHSKEELIKTVQDNTL
The following text describes a protein:
Function:
Regulates clathrin-mediated endocytosis by phosphorylating the AP2M1/mu2 subunit of the adaptor protein complex 2 (AP-2) which ensures high affinity binding of AP-2 to cargo membrane proteins during the initial stages of endocytosis. Preferentially, may phosphorylate substrates on threonine residues. Regulates phosphorylation of other AP-2 subunits as well as AP-2 localization and AP-2-mediated internalization of ligand complexes. Phosphorylates NUMB and regulates its cellular localization, promoting NUMB localization to endosomes. Binds to and stabilizes the activated form of NOTCH1, increases its localization in endosomes and regulates its transcriptional activity.
Subcellular Localization:
Membrane, clathrin-coated pit. Presynapse.
Sequence:
MKKFSRMPKSEGGGGGGGAAGGGAGGAGAGSSSVGVRVFAVGRYQVTLEESLAEGGFSTVFVVRTHGGHRYALKRMYVNNTTDLNICKREITIMKELSGHKNIVGYLDCAVNSISDNVWEVLILMEYCRAGQVVNQMNKKLQTGFTEAEVLQIFCDTCEAVARLHQCKTPIIHRDLKVENILLNDGGNYVLCDFGSATNKFLNPQKDGVNTVEEEIKKYTTLSYRAPEMINLYGGKPITTKADIWALGCLLYKLCFFTLPFGESQVAICDGSFTIPDNSRYSHNIHCLIRFMLEPDPERRPDIFQVSYFAFKFAKKDCPVSNINNSPIPSTLPEPMTASEAASRKSQIKARITDTIGPTETSIAPRQRPKANSTTATPSVLTIQSSATPVKVPAPDEFGNHRPKGPLKPGNGPEILLGQGPTQQPPQQHRVLQQLQQGDWRLQQLHLQHRHPHQQQQLLQDAYMQQYQHAVQQQQMLQQQLLVHSVYQPQPSASQYPAMMQQYQQAFLQQQMLAQHPQSQPQASPEYLTSPQEFSPALVSYSSSLPAQVGPMMDSSYSANRSIAGKEAVANMTNQKNISNPPDMSGWNPFGEDNFSKLTEEELLDREFDLLRSNRLEERAASDKNVEPLSAPYNHPPEDPFGSVPFISHSGSPEKKIEHPSMNQENGTANPIKNTKGSPVSKDHRTGKKTSENSLVRAQVQKGNDESESDFESDPPSPKSSEEEEQEDEEVLQGEQGDFNDDDTEPENLGHRPLLMDSEDEEEEEKHSSDSDYEQAKTKYSDTSPGYRDSGGGAVQGPSAALLTPAWAPSDVGAGTPRPEFDVFGAVPFFAAQAQLPRQGEQKDLSPHSRLPATGLEPEEFDVFTKAPFSKKVMARDAHAAPAGPPSVDVFGSTPFQPFPPSASKSDSGEDLFGLVPFEEITGSPQQKVKQRSLQKLSSRQRRTKQDAAKSNGKRHHGTPTGAKKPAKPAFRTPERARRHRRVGRRDSQSSNEFLTISDSKENISVALTDGKDRGHVLQAEEGLLDPFGAKPFHPPDLPWHSPHQGLSTDHNPVLPGRPRPNSLHGSFHGAEALKMDDFGAVPFTELVVQSITSHQPQQPQPVELDPFGAAPFPSKQ
The following text describes a protein:
Function:
Cell wall formation.
Subcellular Localization:
Cytoplasm.
Sequence:
MKIFTNQEMKNYSNMRVGGKAKKLIILEPKEEIIDVYNDKENTDIFILGNGTNILFTDEYMDKIFVCTKKLNKIEDLGKNLVKVETGANLKDLTDFMKDKNYTGIESLFGIPGSIGGLVYMNGGAFGTEIFDKIVSIEVFDENHQIREIKKEDLKVAYRKTEIQDKNWLVLSATFKFDNGFDAARVKEIKELRESKHPLDKPSLGSTFKNPEGDFAARLISECGLKGTIIGNAQIAEKHPNFVLNLGNATFKDIIDILTLVKKSVLEKFGIKLEEEIIIVR
The following text describes a protein:
Function:
Involved in pollen mitosis II (PMII) regulation during male gametogenesis.
Subcellular Localization:
Endomembrane system; Multi-pass membrane protein. Vacuole membrane; Multi-pass membrane protein. Note=Associated with intracellular membranes and in the tonoplast and endosomes in the germinating pollen tubes.
Sequence:
MDSAPSPSSLDFELSPPVLVTMTSTSSSASDNVEGADDDANTHGIFNWRDFSSCWRVSESNLYCFSLALLIWFFASFILIENLYGPKNVWLGPSSSILVEPSSIFVKSIKVKVLDYSEPGLQLYGFYRTPALDCFVNWSESRVLSISHESYKGWPYYLNSGSLLNITYTVKPQGSAVQLVVDEGHQGVPQSVLNDPAYRYNVWSWNLIEGSGMIQLEIRKSSSYYLAVANLKSKDVEVELNIDVKAVLYDTKQSFYNCNFSNGECTFNAMSLVGNSVVVTSPAASQGVSIEDEWYIRFSYQPREIAYVIGTGVVICFMLVAIQFCNRFQCSGGEGHLTEDDSARTRLLADKDDDGSSMGSCDDSYANDDADLEEFMGNDGEASNRSRRLCAICFDVPRDCFFLPCGHSVSCYECGTTMQEADGSCPICRRKMKKVKRIYTV
The following text describes a protein:
Function:
Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. Catalyzes Na(+) transport, most probably coupled to electron transfer from reduced ferredoxin to methanophenazine and heterodisulfide reductase. Involved in heterodisulfide reduction during methanogenesis from acetate.
Subcellular Localization:
Cell membrane; Single-pass membrane protein.
Sequence:
MSDSKEITKVIVTMVVISAVAAALLALTYTPTQAQLKLLQAEQQKEAMKEILPQAADFEPVTGSEVDDDGNPVVLYYKGVDSSGNVVGYVVERNQVGAQGMIQLLAGISSDFSTITGFQVMKHSETPGLGALITTPEFQGQFVDLPVADTSLTKNGGQVDAISGATISSQAVVDALHSAVDYVSAQEG
The following text describes a protein:
Function:
Secretory calcium-dependent phospholipase A2 that primarily targets dietary phospholipids in the intestinal tract. Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity) with preference for phosphatidylethanolamines and phosphatidylglycerols over phosphatidylcholines. May play a role in the biosynthesis of N-acyl ethanolamines that regulate energy metabolism and inflammation in the intestinal tract. Hydrolyzes N-acyl phosphatidylethanolamines to N-acyl lysophosphatidylethanolamines, which are further cleaved by a lysophospholipase D to release N-acyl ethanolamines (By similarity). May act in an autocrine and paracrine manner. Upon binding to the PLA2R1 receptor can regulate podocyte survival and glomerular homeostasis. Has anti-helminth activity in a process regulated by gut microbiota. Upon helminth infection of intestinal epithelia, directly affects phosphatidylethanolamine contents in the membrane of helminth larvae, likely controlling an array of phospholipid-mediated cellular processes such as membrane fusion and cell division while providing for better immune recognition, ultimately reducing larvae integrity and infectivity (By similarity).
Subcellular Localization:
Secreted. Note=Secreted from pancreatic acinar cells in its inactive form.
Sequence:
MKLLVLAVLLTVAAADSGISPRAVWQFRKMIKCVIPGSDPFLEYNNYGCYCGLGGSGTPVDELDKCCQTHDNCYDQAKKLDSCKFLLDNPYTHTYSYSCSGSAITCSSKNKECEAFICNCDRNAAICFSKAPYNKAHKNLDTKKYCQS
The following text describes a protein:
Function:
Ionotropic glutamate receptor (By similarity). Activation by glutamate requires additional verification. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist (By similarity); Independent of its ionotropic glutamate receptor activity, acts as a thermoreceptor in the ASER neuron where it triggers a calcium response to activate cold avoidance behavior in response to temperatures below 19 degrees Celsius. Possibly functions as a metabotropic cold receptor and acts upstream of the G(o) G protein goa-1 in the ASER neuron. Also functions in cold sensing in the intestine.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Postsynaptic cell membrane; Multi-pass membrane protein.
Sequence:
MFWIAKTLIAFLILLKTDCYKIAIPANLIDEVNPVLEFVDFRVQVIPYETKPLWRIKQESFKIVGISIENGLFSVCNCLILGASAIILPEQYDGHLAAAAIVQSIADNTNVPCVSLHLSPPTRPSTHLHPHLNAKSLAVAAFIKREKWKDVVVVFEEPDELLEITDMITAGHFDPDSFSSQLVRLKHGDDYGNELKHIKNKLDRYRIVINIPLQKALHFLEQAANMSMCGVLYHYVVMDMDLVTVDIDSIRGIEDCNITSFGVHDVNSEYIEDIRQEIVHKSSIRLPKKGVPYTTSIWIDTLRLLIRSMKSIQIWDEPRCGSSWKSGSDIKKRFFENPLAGISGDLHWAPSGERSNYTLHVYRRTLSFQKFAEWSSRTRRIASSEAVVIANSSEKLTLEGKHLKISVYLEAPFVMITSNGSYEGYCIDLLHKIANILKFTYTIQKVRDNAYGSKESNGKWSGMVGELQRGDADLAVASLTISYGRSEVIDFTVPYMHLGISILFKKPRIRDSDWFKFMDPLSTQVWIMTFASYFVVSVAIWIIAKISPYEQFERDEDNGQYKPVDNQFSLRNSFWFTVCSLMQQGSELCPRAASTRLLTGIWWFFALILISSYTANLAAVLTTRRMETPIENADDLAAQTKIKYGTLGRGSTMSFFNESKIETYERMWQLMSSSPGLFVQSSKEGIARVKSSDYAYLMESSMLEYAVERDCELMQIGGLIDQKGYGIGLPKGSPYRELISTAILRLQEKTELTELKEKWWKDKSVVCEQPKRKDQDDGESIGGIFIILVVGLVLTAVLVIFELITTRKPSPAQSQVIRHVNVIPSFKLGFFRWNVN
The following text describes a protein:
Function:
Required for nuclear membrane fusion during karyogamy.
Miscellaneous:
MISCELLANEOUS: Has a similar domain organization and 27% homology to yeast kar5.
Subcellular Localization:
Nucleus membrane; Multi-pass membrane protein. Note=During metaphase, localizes near the mitotic spindle region, and its localization shifts to the chromosomes as they reach the end of the spindle. During karyomere fusion, detected in prominent puncta, mainly at karyomere-karyomere interfaces corresponding to putative fusion sites.
Sequence:
MALWFVLLWVSSLQYAEVEAFFDWLKKADPAPTPPPAESIVPILLHGEAPAFEMSVVDEKFLAEAKQMELSPLDSCHFRVVAQLKATCSGLSEEQLAKLGVALFNCQSEVEGRRTYPCTEEMSIKECTADMDSDTWNAYHIVSNRARSVCYATRQQHFRKRAELTVNALISTATSQLDAMKDLKEGQKELRDMTAASLDKLLEGHGALQIQQGALKEGQEQLDASISENLQRLAQEKALISTGQQLVAQLIQGITQRMENVSGQLKDQTAEVQEGHQAILEDLAVVRGSAQDIYEKMELNLNGFLQQQNTTAHFYTELMRKLELMNGTLGYMLTYLDNMQTRLEDRLHMIQGYLGWAGLSLRALWTCVMHAGYFLLCAVLLSFLQCTTFSRVTLLLSVPINAIAEINQQAALDLISLTLLLFTLSLGRWFVLQLLWALSKIKGRTCSRPPHLSIYPPKEKTPEKQHEFGEKCPASSSTPVQSDPVCDLEVESFMMGDPCVLGVSPSRCPPKFSHHHLGGTPNHSTPRLKSRHSIAATELDNIPQRNLGVFLETVNRSRSSSPNQSLASSSSFSGRSLCSGITRLGQPCKKRAVVGQDYCRVHEGGHTSYSRL
The following text describes a protein:
Function:
Binds non-specifically to DNA and forms static foci which grow by recruiting other morc-1 molecules, and thereby stimulates conformational changes and compaction of DNA, which appears to be enhanced by ATP-binding, but does not require ATP activity. Preferentially binds to long DNAs. Compacts and entraps segments of DNA by sequentially forming loops along the DNA, beginning at the free ends of single- and double-tethered DNA. Does not extrude the DNA loops on compacted double-tethered DNA. Involved in gene silencing. Plays a role in germline RNA interference (RNAi), and in particular, the silencing of endogenous small interfering RNA (endo-siRNA) target genes. May play a role in heterochromatin localization and condensation, and the siRNAi-directed trimethylation of 'Lys-9' of histone H3 in hermaphrodite X chromosomes. Promotes transgenerational epigenetic inheritance and germline immortality.
Subcellular Localization:
Nucleus. Nucleus, nuclear body. Note=Localizes to punctate nuclear bodies in germline stem cells and gonadal meiotic nuclei.
Sequence:
MPNDTNGDDYKKLEKASVNLNFLKSNSHTHIGPLSAIAELVDNAYDADARDLHIDFLDINNEQFLELRDDGLGMAREEALHAITFGHSAKCSYKIGRYGNGLKSGAFHLGRELLLVTKKDGIITALLISHRFHEDQGLTNSVFVPCPSFDLDGIPICQTESEKDRFNLEMKIIGKYAPLGSRTLAELADKITGSTGTIIIIGNLRRSVTGELAINTTKDPTDIIVDSGEENKPWRESLRKYLEFIYLKPRMRIHVRGEQVLPKRISENWIAKKQQLISGDQFTAAYNKILDEKNETVKKCEEEKALVMSEIGGTNYTSVRREDRANQKSLRLRVDTSQKNLDSAIADRDAFKKEGKSEKSFHLNMGIETKDRSNNGIHFYINNRLILWGNKEAKFFSKFANSIGISMFLSLDYSLFSAAQNKQGFDHVKDFQVLVRKCNDALRDYSMYLEKSWIPTHLKNTWNVRIYEGDDVWAVLWGVYGYNNTTSTTCVQTHDSARDQVMWTTCGIWKLCQMCRTWIKASRPNEIVGSNDDFFCCENVNHHGCRTIVAEDNDFSKLPEKYDHILPQKRLTNSAPSSSDSQNSIRSASSCSSSSRLLNVAKIESHERIHSSTGGHRLGESFSTTSVKMEPIPNNAHDSHIAEVQRRHSTGRAISPAVSEISRRAGTAPSSQLDMIMGEESDESQEALTIRAPRQRAKRPIERVSRRNRRDQSDDDSDSENEERYATAPKKSKVKGKAVVRAPKMTREKWLEEMLNQFLTAHGEQPLPKNGQRDFDPTNIVEQTSRRNFKNNQRIVDAQQAIMRQIGSVLDHLKRNPTHNFKIPASGTVEEKLKNIEHQIKGKKK
The following text describes a protein:
Function:
Severs microtubules in an ATP-dependent manner. Microtubule severing may promote rapid reorganization of cellular microtubule arrays.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MANPLAGLQDHLKHARDYALEGLYDTSIIFFDGAIAQINKHLANLDDTFIRTKWMNCKKAISEEVEIVRQLDAQLKSFKEAPGTMRSSSPPIRSNNKSFLFQPLDEYPTSSPSTFDDPDVWAPPRDTNTPNRRSARGQSSARKSSQDGAWARGPSKTGTPSRGAKPSGSKASSAVRSSTASSTGGRKGKSSSSKADSASSDAEEGKSKKAQYEGPDGDLAAMLERDVLDSTPGVRWDDVAGLSEAKRLLEEAVVLPLWMPEYFQGIRRPWKGVLMFGPPGTGKTLLAKAVATECGTTFFNVSSATLASKWRGESERMVRCLFELARAYAPSTIFIDEIDSLCTSRGASGEHESSRRVKSELLVQIDGVNNSSTNEDGQPKIVMVLAATNFPWDIDEALRRRLEKRIYIPLPSFESRKSLISINLRTVEVATDVNIDEVARRTEGYSGDDLTNVCRDASMNGMRRKIAGKTRDEIKNMSKDDISKDPVAMCDFEEALVKVQKSVSPSDIERHEKWMAEFGSA
The following text describes a protein:
Function:
The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Domain:
The EIIB domain is phosphorylated by phospho-EIIA on a cysteinyl or histidyl residue, depending on the transported sugar. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the EIIC domain; The EIIC domain forms the PTS system translocation channel and contains the specific substrate-binding site.
Sequence:
MSKENNYHHLAQKILELCGGKSNISSYTHCMTRLRITPYDESKADAQALRKLDGVLGVVEAETLQIILGTGVVNHVTAAFSKLVSAEEGADVKEAAAKKKADINRKNATPFKLFLRKIASIFIPLIPALVASGLITGITKAIIQAGWLSADSQIAIILTVIGSGLFTYLGILVGINASKEFGGTPALGALAGILIINPEIAKISLFGEELLPGRGGLIGVLFAAIFIAYTEQFIRRFIPQSLDIIVTPTVSLLITGIVTYVVFMPLGGFISDAITSGLLSILDIGGIAAGFILGATFLPLVVTGLHQGLTPVHMELINSIGNDPLLPILAMGGAGQVGAAFAVFVKTKKTTLRKAIAGGLPSGLLGIGEPLIFGVTLPLGRPFLTACLGAGIGGAFQAYFQVATIAIGVSGLPLSFLVLPSQIILYIVGLFISYAAGFLLTYAFGYKDEMASQFD
The following text describes a protein:
Function:
May hydrolyze collagen type IV, fibronectin, fibrinogen, beta-casein, type I gelatin and alpha-1 proteinase inhibitor. Is also able to activate progelatinase B.
Subcellular Localization:
Secreted, extracellular space, extracellular matrix.
Domain:
The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
Sequence:
MQLVILRVTIFLPWCFAVPVPPAADHKGWDFVEGYFHQFFLTKKESPLLTQETQTQLLQQFHRNGTDLLDMQMHALLHQPHCGVPDGSDTSISPGRCKWNKHTLTYRIINYPHDMKPSAVKDSIYNAVSIWSNVTPLIFQQVQNGDADIKVSFWQWAHEDGWPFDGPGGILGHAFLPNSGNPGVVHFDKNEHWSASDTGYNLFLVATHEIGHSLGLQHSGNQSSIMYPTYWYHDPRTFQLSADDIQRIQHLYGEKCSSDIP
The following text describes a protein:
Function:
Involved in the uptake of iron in complex with vulnibactin, a catecholate siderophore synthesized by V.vulnificus. Binds and transports ferric vulnibactin across the outer membrane. The energy source is provided by the inner membrane TonB system (Probable).
Subcellular Localization:
Cell outer membrane; Multi-pass membrane protein.
Sequence:
MAALRPARTSVAEKKTFKLHALSAVVMGLCASGQAYAQTESTNSNKKEEMPVVVVIGEKTERTIYDTSSSVQVFDQETIDNTPGATEIDDLLQLIPNMVDSGQGNSMPTVRGIDGSGPSIGGLASFAGTSPRLNMSIDGRSLTYSEIAFGPRSLWDMQQVEVYLGPQSYIQGRNASAGAIVMKTNDPTHHFESAVKAGVGERNYSQTAAMISAPIIQDELAFRLSFDQQKRDSFVDLASYEPAGDAKKIEMNSVRGKLLYEPSALAGFKTTLGVSHMDSRGPQSESTNVVGNEAFRPVYETKSLSTAWDISWQLNEVLTFENNLVYSKFAFDRYTNPLQKGDYTAEGKEFHVEPLLRYLSLGGRVNALVGARYYKSSQDDEYVDATSANPMSGSTKTQSAFAELTYALTQSIDVTVAGRYEKERVKRKVSDPRFKLDHDDTLSVFLPKFDIAFKPDMAQTFGFKVAKGYNSGGAGLAFNPILGGGFSPYQFEEEYIWNYEFYTRHRLGNSVELMTNTFYNDFDSMQMTQTLSNGDVLIANLDNAKTYGAEIGTRWYATDSLELFANLGLLKTEYKEVNGTSKELERAPNMTGNLGGQYSFFDGFELSANAAYTGDYFSDRSNTEIVKIDAYWVANAQLAYVFENGRAALFATNLFDSDKTTLYARGSLNEPLKQQPRMIGASLQLNF
The following text describes a protein:
Function:
RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Sequence:
MGLPKTLRLKHWQDFQTVYQQGKRHRHSNLLMRVLGDRQADHSRFGITVSQKVSKKATVRNRLKRQIRAVINHFQPQIKPGFDVVIIVLPQGIGCNYERFLRELEQLFSQAGIIDHGHSRNHLL
The following text describes a protein:
Function:
May play a role in male fertility. May act as a retinoid carrier protein within the epididymis.
Subcellular Localization:
Secreted.
Sequence:
MKLEMALSIALALAVVSWTQEFFPKEAQTLNWSKFSGFWYIIAIATDTQGFLPARDKRKLGASVVKVHKTGQLRVVIAFSRPRGCQSREVTLKKDRKRPVFRNTLKGVKGFHVLSTDYTYGLVYLRLGRGGSNYKSLLLFNRQNISSFLSLREFLDTCHILQLTKQATILPKDDSCAHTILP
The following text describes a protein:
Function:
This protein catalyzes the committed step to the synthesis of the acidic phospholipids.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MNIKTFNLPTTLTIIRILIVPIFIIEAPANPQLGAFLFLIASITDFLDGYLARKFKQITKLGIILDPIADKLLVITALIILVDLVRVPAWIATIIILREFIITTLRFYALSRGVIIPAEKAGKAKTVLQMIAILFLFIAEEIYGLDLYDVGLILIYIATFVAVYSAIKYLFYFWRNIK
The following text describes a protein:
Function:
NodD regulates the expression of the nodABCFE genes which encode other nodulation proteins. NodD is also a negative regulator of its own expression. Binds flavonoids as inducers.
Sequence:
MELSDIQTFAAVARTGGITRAAEELNTVQSNVTQRVKALEAEIGTPLFERHSRGMTLTGAGKRLLPYAQRMAALSREAVLAARDDGEPKGPLAIGSMETTAAVRLPPLLADFHRRFPAVRLSLRTATTADLVAGVLEGTLDGAFVAGPIAHADLTATSAFREELVLVSARRWSSLAELRAGTPESGPTALVFRTGCTYRQRLEQIFVEFGWPSAARFELGTLDGMIGCVAADMGVTLLPRAVVERSAMNGSVSIHPLSASHARVETLFIQRSAGHQYSALQGFAACLKKDDDVIAA
The following text describes a protein:
Function:
May be involved in the biogenesis of curli organelles.
Subcellular Localization:
Cell membrane; Lipid-anchor.
Sequence:
MQRLFLLVAVMLLSGCLTAPPKEAARPTLMPRAQSYKDLTHLPAPTGKIFVSVYNIQDETGQFKPYPASNFSTAVPQSATAMLVTALKDSRWFIPLERQGLQNLLNERKIIRAAQENGTVAINNRIPLQSLTAANIMVEGSIIGYESNVKSGGVGARYFGIGADTQYQLDQIAVNLRVVNVSTGEILSSVNTSKTILSYEVQAGVFRFIDYQRLLEGEVGYTSNEPVMLCLMSAIETGVIFLINDGIDRGLWDLQNKAERQNDILVKYRHMSVPPES
The following text describes a protein:
Function:
Methyltransferase that can methylate proteins and, to a lower extent, arsenic. Catalytic subunit of a heterodimer with TRMT112, which monomethylates 'Lys-12' of histone H4 (H4K12me1), a modification present at the promoters of numerous genes encoding cell cycle regulators. Catalytic subunit of a heterodimer with TRMT112, which catalyzes N5-methylation of Glu residue of proteins with a Gly-Gln-Xaa-Xaa-Xaa-Arg motif. Methylates ETF1 on 'Gln-185'; ETF1 needs to be complexed to ERF3 in its GTP-bound form to be efficiently methylated. May also play a role in the modulation of arsenic-induced toxicity by mediating the conversion of monomethylarsonous acid (3+) into the less toxic dimethylarsonic acid. It however only plays a limited role in arsenic metabolism compared with AS3MT.
Subcellular Localization:
Nucleus.
Sequence:
METPVYKFEPHDYDTVYEPAEDTFLLLDALEAELDTIKARQPSLCVEIGPGSGVVIVALSKHLPAGQTHCIGFDLNPNACRMTQKTAHLNGSRVDVVNMDLLAGLRPTSVDLLVFNPPYVPTQPATTAHAAASLEEHIDEFRSSVDVGQTLVHAWAGGADGRVVTDRVLADLPRVLSPTGLFYLLLLKENKPEEVLEQIRGMNLRGSIIKERRIRGEHLYVVRIERSERK
The following text describes a protein:
Function:
Glucanases play a role in cell expansion during growth, in cell-cell fusion during mating, and in spore release during sporulation. This enzyme may be involved in beta-glucan degradation. Active on laminarin and lichenan.
Subcellular Localization:
Cell membrane; Single-pass type II membrane protein. Secreted, cell wall.
Sequence:
MYGTFKALASLLAVAVGVQAQESSVTRSFYGMAYSPDGALLPQCGADQASVTRDMGKLAQLTPRIRLYGADCNQTELVLEGIKQAGNVDLSVWLGIFIDGNDTVYERQLNAVTTAIQKYGTEHIAGITVGNEFLLLSYGDGGSATDPKGVAARTTLLNYIQKTNQTLKAMKLDKAIPLGTADAGSAVTKELCAGADYVMANVHPWFGHVPVEQSAGWTWQFFQDFDVNVCAQAPNKPVMYIAETGWPTASDNASITTNGPSKASVQGLQTFMDSFVCQANKNNTNYFFFELKDEEWKKKYGGVEPYWGLYDFNMKYKDGLKVPNCPVTSPTGRAVGPASSSPGGRNAQGGAKKSAAPSSANPVASTFVLALIATGLFAIL