wanglab/gogpt-training-data huggingface dataset:
Protein: Ypt/Rab-type GTPase avaA (Aspergillus vacuolar morphology protein A) (YPT7 homolog avaA) (C8VQY7)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Ypt/Rab-type GTPases are key regulators of membrane trafficking and intracellular vesicular transport. They act as molecular switches that convert between GTP-bound and GDP-bound states, and regulate virtually all steps of membrane traffic from the formation of the transport vesicle at the donor membrane to its fusion at the target membrane. In the GDP-bound state, Ypt proteins are predominantly cytosolic, solubilized through the interaction with a GDP dissociation inhibitor (GDI). In the GTP-bound state, the proteins are membrane bound and interact with specific effector proteins that select cargo, promote vesicle movement, or verify the correct site of fusion (By similarity). AvaA functions in vacuolar biogenesis.
Interaction partners:
- Rab GDP dissociation inhibitor
- AvaB protein
- GTPase-activating protein GYP7
- Pep3/Vps18/deep orange beta-propeller domain-containing protein
- Vacuolar protein sorting protein
- Probable vacuolar protein sorting-associated protein 16 homolog
- Vacuolar assembly protein, putative
- Vacuolar sorting protein
- Putative lipase atg15
- Vacuolar fusion protein mon1
Sequence:
MSSRKKVMLKVIILGDSGVGKTSLMNQYVNKKFSGSYKATIGADFLTKEVLVDDRLVTMQIWDTAGQERFQSLGVAFYRGADCCVLVYDVNNSKSFEALDSWRDEFLIQASPRDPESFPFVVIGNKIDMEESKRMISSKRAMTFCQSKGNIPYFETSAKEAVNVEQAFEVIARSALAQEEAEEYGGDYTDPINIHDTTERDGCAC
Protein: Phosphate-binding protein PstS 2 (PBP 2) (PstS-2) (P9WGT9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Functions in inorganic phosphate uptake, although probably not the main uptake protein under phosphate starvation. Part of the ABC transporter complex PstSACB involved in phosphate import (Probable).
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
Interaction partners:
- Phosphate transport system permease protein PstC 1
- Phosphate transport system permease protein PstC 2
- Phosphate transport system permease protein PstA 1
- Phosphate transport system permease protein PstA 2
- Phosphate import ATP-binding protein PstB 2
- Phosphate-binding protein PstS 1
- Phosphate import ATP-binding protein PstB 1
- Phosphate-binding protein PstS 3
- Serine/threonine-protein kinase PknD
- Lipoprotein LprA
Sequence:
MKFARSGAAVSLLAAGTLVLTACGGGTNSSSSGAGGTSGSVHCGGKKELHSSGSTAQENAMEQFVYAYVRSCPGYTLDYNANGSGAGVTQFLNNETDFAGSDVPLNPSTGQPDRSAERCGSPAWDLPTVFGPIAITYNIKGVSTLNLDGPTTAKIFNGTITVWNDPQIQALNSGTDLPPTPISVIFRSDKSGTSDNFQKYLDGASNGAWGKGASETFNGGVGVGASGNNGTSALLQTTDGSITYNEWSFAVGKQLNMAQIITSAGPDPVAITTESVGKTIAGAKIMGQGNDLVLDTSSFYRPTQPGSYPIVLATYEIVCSKYPDATTGTAVRAFMQAAIGPGQEGLDQYGSIPLPKSFQAKLAAAVNAIS
Protein: Large ribosomal subunit protein uL14my (50S ribosomal protein HLL, mitochondrial) (Protein HUELLENLOS) (Q84JG5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds to 23S rRNA in mitochondrion (By similarity). Required for the formation of the proximal region of the ovule primordium during floral organogenesis, thus participating in patterning and growth of ovule. Also regulates the initiation and/or maintenance of integument and embryo sac ontogenesis. Prevents inappropriate cell death in the young ovule.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:11752383}.
Interaction partners:
- Large ribosomal subunit protein uL18y
- At1g01640
- Short integuments 2, mitochondrial
- At1g43860
- Large ribosomal subunit protein uL13x
- Large ribosomal subunit protein uL13z
- At5g64650
- At5g09770
- Large ribosomal subunit protein uL13w
- Translation elongation factor EF1B/ribosomal protein S6 family protein
Sequence:
MATALASKLSKGRSLLGGLCNAFSGLMNSSSNGMMNGSILSQQQHRTFIQMGTILKCVDNSCAKEVMCIQSLRGKKGARLGDIIVGSVKEANPIVQKKVKKDAIPKGKVKKGMVVYGVVVRAAMPKGRADGSQVKFDDNAIVVVGIKEKKGQNNSHGSKRKMEYNQPTGTRVFGPVPHEMRLRKQLKILSLAQHIV
Protein: DNA topoisomerase 3-alpha (EC 5.6.2.1) (DNA topoisomerase III alpha) (O70157)
Organism: Mus musculus (Mouse)
Function: Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone. As an essential component of the RMI complex it is involved in chromosome separation and the processing of homologous recombination intermediates to limit DNA crossover formation in cells. Has DNA decatenation activity. It is required for mtDNA decatenation and segregation after completion of replication, in a process that does not require BLM, RMI1 and RMI2.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:Q13472}.
Interaction partners:
- Fanconi anemia group M protein homolog
- RecQ-mediated genome instability protein 2
- RecQ-mediated genome instability protein 1
- RecQ-like DNA helicase BLM
- Replication protein A 70 kDa DNA-binding subunit
- Replication protein A 14 kDa subunit
- Bifunctional 3'-5' exonuclease/ATP-dependent helicase WRN
- Replication protein A 32 kDa subunit
- Structure-specific endonuclease subunit MUS81
- Fanconi anemia group G protein homolog
Sequence:
MIFPVTLLAFQWHRRPGGRALSRAAMEVAFRGVRKVLCVAEKNDAAKGIADLLSNGRMRRKEGLSKFNKIYEFDYHLYGQNVTMIMTSVSGHLLAHDFQMQFRKWQSCNPLVLFEAEIEKYCPENFIDIKKTLERETHHCQALVIWTDCDREGENIGFEIIHVCKAVKPNLRVLRARFSEITPHAVRTACENLTEPDQRVSDAVDVRQELDLRIGAAFTRFQTLRLQRIFPEVLAEQLISYGSCQFPTLGFVVERFKAIQAFVPEVFHKIKVTHDHKDGTVEFNWKRYRLFNHTACLVLYQLCMEDPMATVVEVRSKPKSKWRPQALDTVELEKLASRKLRINAKETMRIAEKLYTQGYISYPRTETNIFPKDLNLVALVEQQTVDPHWGAFAQTILERGGPTPRNGSKSDQAHPPIHPTKYTSGLQGDDRRLYEFIVRHFLACCSQDAQGQETTVEIDIAQERFVAHGLIILARNYLDVYPYDHWSDKLLPVYEQGSHFQPSTVEMVDGETSPPQLLTEADLIALMEKHGIGTDATHAEHIETIKARMYVGLTSDKRFLPGHLGMGLVEGYDSMGYEMSKPDLRAELEADLKLICEGKKDKFQVLRQQVQKYKQVFIEAVAKAKKLDEALSQYLGERTEMAQQEEIYPAMPEPVRKCPQCNKDMVLKTKKSGGFYLSCMGFPECRSAVWFPDSVLEASRDNSVCSVCQPPPVYRLKLKFKRGSLPPAMPLEFVGCIGGCDETLKEIFGLRFPRALPRASQPSGHLQASQALNRMDSSQHNLSQPLVNRHTRPSKTVAQALLPPTTAGESNSVTCNCGREAVLLTVRKQGPNQGRHFYKCSNGDCNFFLWADSSHSTGGGTPTSASGPPGSSVGCPSSVGSHMDGFGSLGSDSDGGTPCLCGQPAVTRTVQKDGPNKGRQFHTCAKPREQQCGFFQWVDENVAPGSFAAPAWPGGRGKAQRPEAASKRPRAGSSDAGSTVKKPRKCSLCHQPGHTRTFCPQNR
Protein: Ribonuclease H2 subunit B (Ribonuclease HI subunit B) (A0A2R8YGP2)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAAGVDCGDGVGARQHVFLVSEYLKDASKKMKNGLMFVKLVNPCSGEGAIYLFNMCLQQLFEVKVFKEKHHSWFINQSVQSGGLLHFATPVDPLFLLLHYLIKADKEGKFQPLDQVVVDNVFPNCILLLKLPGLEKLLHHVTEEKEIDNKKYYKYSKEKTLKWLEKKVNQTVAALKTNNVNVSSRVQSTAFFSGDQASTDKEEDYIRYAHGLISDYIPKELSDDLSKYLKLPEPSASLPNPPSKKIKLSDEPVEAKEDYTKFNTKDLKTEKKNSKMTAAQKALAKVDKSGMKSIDTFFGVKNKKKIGKV
Protein: Dixin (Coiled-coil protein DIX1) (Coiled-coil-DIX1) (DIX domain-containing protein 1) (Q2VUH7)
Organism: Rattus norvegicus (Rat)
Function: Positive effector of the Wnt signaling pathway; activates WNT3A signaling via DVL2. Regulates JNK activation by AXIN1 and DVL2.
Subcellular location: Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q155Q3}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:Q155Q3}. Cytoplasm {ECO:0000250|UniProtKB:Q155Q3}. Note=Colocalizes with gamma-tubulin at the centrosome, both during interphase and mitosis. Associated with actin stress fiber at the filament ends. {ECO:0000250|UniProtKB:Q155Q3}.
Interaction partners:
- Disrupted in schizophrenia 1 homolog
- Nuclear distribution protein nudE-like 1
- G protein-coupled receptor associated sorting protein 3
Sequence:
MLACLTRGNLLDVLQEGFNEQQLQAYVAWVNAQLKKRPSVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPSNQQEMKSNVERVLQFVASKNIRMHQTSAKDIVEGNLKSIMRLVLALAAHFKPGSSRTVSQGRDSRTSVQSHQPHCATAVAQGAAAALADVCHDVSRSGRDVFRYRQRNASVDEEIENPYWSVRALVQQYEGQQRSPSESSCSSLTSPSPIHSAKSESIITQSEEKADFVIIPSEGIENRTDETGSPLSRDWRPGSPGTYLEATWEEQLLEQQEHLEKEMEEAKKMISGLQALLLNGSLPEDEQERPVALCEPGVNPEEQLIIIRSRLDQSMEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYKKDLGQKDRLLQQQQAKLEDALRKLSDASYQQVDLERELEQKDVLLAHRVKGDTDEVTNYNSHSSQRNGFVLPVAGRAATTATHRGPQSSDLQLVRDALRSLRNSFSGHDPQHHTIDSLEQGISSLIERLHVIETQKKQERKVRGRSPRNQASSEYRASWPPNSTLPHSQSSPAVSNTCTKVLYFTDRSLTPFMVNIPKRLGEVTLKDFKAAIDREGSHRYHFKALDPEFGTVKEEVFHDDDAIPGWEGKIVAWVEDHREN
Protein: Peptidase S1 domain-containing protein (Q9VT23)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- GH14734p
- trypsin
- RH54371p
- trypsin
- RH26557p
- trypsin
Sequence:
MSKKLVLLLLFVATVCAHRNRNRTAHHGGGPKDIIVNGYPAYEGKAPYAVGLRMNNGAVGGGSVIGNNWVLTAAHCLTTDSVTIHYGSNRAWNGQLQHTVNKNNFFRHPGYPNSAGHDIGLIRTPYVSFTNLINKVSLPKFSQKGERFENWWCVACGWGGMANGGLADWLQCMDVQVISNGECARSYGSVASTDMCTRATDGKSVCGGDSGGALVTHDNPIQVGVITFASIGCKSGPSGYTRVSDHLDWIREKSGIAYY
Protein: ORF K11 (P88948)
Organism: Human herpesvirus 8 type M
Interaction partners:
Sequence:
MHSLFFEEPEPSGFGSSGQSSSLLAPDSPRPSTSQVQGPLHVHTPTDLCLPTGGLPSPVIFPHETQGLLAPPAGQSQTPFSPEGPVPSHVSGLDDCLPMVDHIEGCLLDLLSDVGQELPDLGDLGELLCETASPQGPMQSEGGEEGSTESVSVLPATHPLESSAPGASVMGSGQELPDLGDLSELLCETASPQGPMQSEGGEEGSTESVSVLPATHPLESSAPGASVMGSSFQASDNVDDFIDCIPPLCRDDRDVEDQEKADQTFYWYGSDMRPKVLTATQSVAAYLSKKQAIYKVGDKLVPLVVEVYYFGEKVKTHFDLTGGIVICSQVPEASPEHICQTVPPYKCLLPRTAHCSVDANRTLEQTLDRFSMGVVAIGTNMGIFLKGLLEYPAYFVGNASRRRIGKCRPLSHRHEIQQAFDVERHNREPEGSRYASLFLGRRPSPEYDSDHYPVILHIYLAPFYHRD
Protein: Mitochondrial thiamine pyrophosphate carrier 1 (Q5AP79)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004448}.
Interaction partners:
- ATP synthase subunit alpha
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome b-c1 complex subunit 2, mitochondrial
- ADP/ATP translocase
- ATP synthase subunit 4
- Isocitrate dehydrogenase subunit 2, mitochondrial
Sequence:
MSTPSEYKLPEYTVKDYASFALAGAIGCGATHGAMTPIDVVKTRIQLEPTVYNKGMLGSFKQVIKSEGAGALLTGLGPTILGYSLQGAFKFGGYELFKKTFIEYLGYDTAKQYKDSIYIGSSALAEFFADIALCPLEATRIRLVSQPTFANGLIGGFSRILKEEGVGSFYNGFTPILFKQIPYNIAKFLVFERANEAIYNAIPTPKVDLSTAAHTAVNLGAGIIAGCAAAIVSQPADTLLSKVNKTKKAPGQSTVGLLIQLAKQLGVSGSFAGLPTRLVMVGTLTSLQFTIYGSLKKALNCPPAVAL
Protein: Transmembrane protein 188 (Q5LJU1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus membrane {ECO:0000256|ARBA:ARBA00004232}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004232}.
Interaction partners:
- CTD nuclear envelope phosphatase 1 homolog
Sequence:
MEDTDQEDLLAFERRLAEVVNTEKRSSLRWRFVLGAIFACSAISACHWVRDAKESESVVFQILSSQSAFAFSLATICLLIFYGFNHATKQDPSILRDTQEMLSPFRLNIDNQGRLILLPRQTE
Protein: Tropomodulin-2 (Neuronal tropomodulin) (N-Tmod) (Q9JKK7)
Organism: Mus musculus (Mouse)
Function: Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- Beta-adducin
- Alpha-adducin
- Gamma-adducin
- Dematin
- Nebulin
- Tropomyosin alpha-3 chain
- Gelsolin
- Troponin T, slow skeletal muscle
- Tropomyosin alpha-1 chain
- Tropomyosin beta chain
Sequence:
MALPFQKGLEKYKNIDEDELLGKLSEEELKQLENVLDDLDPESATLPAGFRQKDQTQKAATGPFDREHLLMYLEKEALEQKDREDFVPFTGEKKGRVFIPKEKPVETRKEEKVTLDPELEEALASASDTELYDLAAVLGVHNLLNNPKFDEETTNGEGRKGPVRNVVKGEKAKPVFEEPPNPTNVEASLQQMKANDPSLQEVNLNNIKNIPIPTLKEFAKSLETNTHVKKFSLAATRSNDPVALAFAEMLKVNKTLKSLNVESNFITGTGILALVEALRENDTLTEIKIDNQRQQLGTAVEMEIAQMLEENSRILKFGYQFTKQGPRTRVAAAITKNNDLVRKKRVEGDRR
Protein: DNA-directed RNA polymerase subunit Rpo1N (EC 2.7.7.6) (DNA-directed RNA polymerase subunit A') [Cleaved into: Mja rpo1N intein (Mja rpoA' intein) (Mja rpoA1 intein)] (Q58445)
Organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Function: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Forms the clamp head domain.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00863}.
Interaction partners:
- DNA-directed RNA polymerase subunit Rpo2C
- DNA-directed RNA polymerase subunit Rpo2N
- DNA-directed RNA polymerase subunit Rpo1C
- DNA-directed RNA polymerase subunit Rpo5
- DNA-directed RNA polymerase subunit Rpo3
- DNA-directed RNA polymerase subunit Rpo11
- DNA-directed RNA polymerase subunit Rpo6
- DNA-directed RNA polymerase subunit Rpo10
- Probable transcription termination protein NusA
- DNA-directed RNA polymerase subunit Rpo7
Sequence:
MERYEIPKEIGEIMFGLLSPDYIRQMSVAKIVTPDTYDEDGYPIDGGLMDTRLGVIDPGLVCKTCGGRIGECPGHFGHIELAKPVIHIGFAKTIYKILKAVCPHCGRVAISETKRKEILEKMEKLERDGGNKWEVCEEVYKEASKVTICPHCGEIKYDIKFEKPTTYYRIDGNEEKTLTPSDVREILEKIPDEDCILLGLNPEVARPEWMVLTVLPVPPVTVRPSITLETGERSEDDLTHKLVDIIRINNRLEENIEGGAPNLIIEDLWNLLQYHVNTYFDNEAPGIPPAKHRSGRPLKTLAQRLKGKEGRFRYNLAGKRVNFSSRTVISPDPCLSINEVGVPEVVAKELTVPEKVTKYNIERIRQLLRNGSEKHPGVNYVIRKMIGRDGTEQEYKVKITESNKDFWAENIREGDIVERHLMDGDIVLYNRQPSLHRMSIMAHRVRVLPYRTFRHNLCVCVDGDTTVLLDGKLIKIKDLEDKWKDVKVLTSDDLNPKLTSLSKYWKLNADEYGKKIYKIKTELGREIIATEDHPFYTTNGRKRCGELKVGDEVIIYPNDFPMFEDDNRVIVDEEKIKKVINNIGGTYKNKIINELKDRKLIPLTYNDQKASILARIVGHVMGDGSLIINNKNSRVVFRGDIEDLKTIKEDLKELGYDGEEIKLHEGETEITDYNGKKRIIKGKGYSFEVRKKSLCILLKALGCVGGDKTKKMYGIPNWIKTAPKYIKKEFLSAYFGSELTTPKIRNHGTSFKELSFKIAKIEEIFDEDRFIKDIKEMLKEFGIELKVRVEEGNLRKDGYKTKVYVASIYNHKEFFGRIGYTYANKKETLARYAYEYLLTKEKYLKDRNIKKLENNTKFITFDKFIKEKCLKNGFVKEKIVSIEETKVDYVYDITTISETHNFIANGFLTGNCPPYNADFDGDEMNLHVPQSEEARAEAEALMLVEKHILSPRFGGPIIGAIHDFISGAYLLTSNYFTKDEATLILRSGGIKDELWEPDKVENGVPLYSGKKIFSKALPKGLNLRYKAKICRKCDVCKKEECEYDAYVVIKDGELIKGVIDKNGYGAEAGLILHTIVKEFGPEAGRKFLDSATKMAIRAVMLRGFTTGIDDEDLPEEALKEIEKVLDEAEEKVKEIIEKYERGELELLPGLNLEESREAYISNVLREARDKAGAIAERYLGLDNHAVIMAVTGARGNILNLTQMAACLGQQSVRGKRIFRGYRGRVLPHFEKGDLGARSHGFVRSSYKKGLSPTEFFFHAMGGREGLVDQAVRTAQSGYMQRRLINALQDLKTEFDGTVRDSRGIMIQFKYGEDGIDPMLADRGKAVNIDRIIDKVKMKYNQ
Protein: Class 10 plant pathogenesis-related protein 2B (LlPR10.2b) (Ypr-10.2b) (EC 3.1.27.-) (allergen Lup l 4) (Q9LLQ2)
Organism: Lupinus luteus (European yellow lupine)
Function: Class II ribonuclease (RNase) (By similarity). Binds to several cytokinins including natural adenine-type (e.g. trans-zeatin and kinetin) and artificial urea-type (e.g. N,N'-diphenylurea and N-phenyl-N'-(2-chloro-4-pyridyl)urea) hormones. Interacts with melatonin.
Subcellular location: Cytoplasm, cytosol {ECO:0000305|PubMed:18406424}.
Interaction partners:
Sequence:
MGVFTFQDEYTSTIAPAKLYKALVTDADIIIPKAVETIQSVEIVEGNGGPGTIKKLTFIEGGESKYVLHKIEAIDEANLGYNYSIVGGVGLPDTIEKISFETKLVEGANGGSIGKVTIKIETKGDAQPNEEEGKAAKARGDAFFKAIESYLSAHPDYN
Protein: Unconventional myosin-Ia (Brush border myosin I) (BBM-I) (BBMI) (Myosin I heavy chain) (MIHC) (Q62774)
Organism: Rattus norvegicus (Rat)
Function: Involved in directing the movement of organelles along actin filaments.
Interaction partners:
- Espin
- Actin, cytoplasmic 2
- Unconventional myosin-Ic
- Unconventional myosin-VI
- Myosin-IIIa
- PDZ and LIM domain protein 4
- Myosin IF
- Actin-related protein 2/3 complex subunit 3
- Capping protein regulator and myosin 1 linker 1
- Myosin XVIIIb
Sequence:
GVEDLILLEPLDEESLIKNLQLRYEKKEIYTYIGNVVISMNPYQQLPIYGPEFIAKYRDYTFYELKPHIYALANVAYQSLKDRDRDQCILITGESGAGKTEASKLVMSYVAAVCGKGEQVNSVKEQLLQSNPVLEAFGNAKTIRNDNSSRFGKYMDIEFDFKGSPLGGVITNYLLEKSRVVKQLKGERNFHIFYQLLAGADTQLLKALKLEEDARGYAYLNGEVSRVNGMDDASNFRAVQNAMAVIGFSEEEIRQVLEVTALVLKLGNVKLAGEFQANGLPASGVCDGKGIQEIGEMMGLNSVELEKALSSRTMETGKEKVVTVLNVIQAQYARDALAKNIYSRLFDWIVNRINESIKVGTGEKRKVMGVLDIYGFEILEDNSFEQFVINYCNEKLQQVFIELTLKEEQEEYKREGIPWTKVEYFDNGIICDLIEHSQRGILAMLDEECLRPGVVSDTTFLAKLNQLFSKHSHYESKVTQNAQRQYDRTMGLSCFRICHYAGKVTYDVTSFIDKNNDLLFRDLSQTMWKAQHPLLHSLFPRGNPKEASPKRPPTAGTQFKNSVAILMKNLYSKNPNYIRCIKPNDQQQQGRFTSELVMVQARYLGLLENVRVRRAGYAFRQAYKPFLERYRLLSRSTWPRWNGEDREGVEKVLGSLILSSEELAYGRTKIFIRSPKTLFYLEEQRRLRLQQLATLIQKVYRGWRCRTHYQQMRKSQILLSAWFRGNKQKKHYGKIRSSVLLIQAFVRGWKARKNYRKYFRSGARITLANFIYQSITQKFLLNLKKNLPSTKVLDNTWPAAPYRCFNTANQELQHLFYQWKCKKYRDQLSPKQVQTLREKLCA
Protein: 60S ribosomal protein L24, putative (Q385D3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Eukaryotic translation initiation factor 6
- Nucleolar GTP-binding protein 1
- 60S ribosomal protein L7a
- 60S ribosomal protein L5, putative
- 60S ribosomal subunit protein L31, putative
- Large ribosomal subunit protein eL18
- 60S ribosomal protein L6, putative
- Nucleolar GTP-binding protein 2
- Ribosome biogenesis protein NSA2 homolog
- 60S ribosomal protein L35, putative
Sequence:
MRIEQCSFCGAPIYPGHGQMFVRNDCKIFRFCASKCRKNFGMKRNPMKLKWTKTFRKANGKELAVDSTMDFEQRRHVPVKYNRELLHNTLKVMKRVERIKQSRQEALWERRMERAHLQERRDAASALKHNIDWIEDTEVKHKARDDLVAVQQEAEVKKQQRREAARKRAQKRREMERAAGAPTNTSVKSRH
Protein: Glutathione peroxidase-like peroxiredoxin gpx1 (EC 1.11.1.24) (Glutathione peroxidase homolog) (GPx) (Thioredoxin peroxidase gpx1) (O59858)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Glutathione peroxidase-like protein that protects cells during oxidative stress. Has peroxidase activity reducing hydrogen peroxide, alkyl and phospholipid hydroperoxides using preferentially thioredoxin as a reducing power. May act as a scavenger of H(2)O(2).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18162174}. Mitochondrion {ECO:0000269|PubMed:18162174}.
Interaction partners:
- Catalase
- Peroxiredoxin tpx1
- Glutathione reductase
- Peroxisomal membrane associated protein 20
- Chromatin modification-related protein eaf3
- Glutaredoxin-1
- Sulfiredoxin
- Thioredoxin-1
- AP-1-like transcription factor
- Superoxide dismutase
Sequence:
MSHFYDLAPKDKDGNPFPFSNLKGKVVLVVNTASKCGFTPQYKGLEALYQKYKDRGFIILGFPCNQFGNQEPGSDEEIAQFCQKNYGVTFPVLAKINVNGDNVDPVYQFLKSQKKQLGLERIKWNFEKFLVNRQGQVIERYSSISKPEHLENDIESVL
Protein: Putative eukaryotic translation initiation factor 4 gamma (Q1MSJ1)
Organism: Oryza glaberrima (African rice)
Interaction partners:
- eIF-4F 25 kDa subunit
- RNA helicase
- RNA helicase
- eIF-
- Eukaryotic translation initiation factor NCBP
- RNA helicase
- Nuclear cap-binding protein subunit 1
- Nuclear cap-binding protein subunit 1
- Nuclear cap-binding protein subunit 2
- Cellulose synthase
Sequence:
MEKDHQPVISLRPGGGGGGPRPGRLFSPAFAAAASGSGDLLRSHVGGASKIGDPNFEVRERVRYTRDQLLELREIVDIPEAILRIKQEIDIELHGEDQIWGRPESDVQVQTQTQAQPHNRYGETDNRDWRARTVQPPAANEEKSWDNIREAKAAHASSGRQQEQVNRQDQLNHQFASKAQVGPTPALIKAEVPWSARRGNLSEKDRVLKTVKGILNKLTPEKFDLLKGQLMESGITTADILKDVISLIFEKAVFEPTFCPMYAQLCSDLNEKLPSFPSEEPGGKEITFKRVLLNNCQEAFEGDESLRAEIAKLTGPDQEMERRDKERIVKLRTLGNIRLIGELLKQKMVPEKIVHHIVQELLGSGPDKKACPEEENVEAICQFFNTIGKQLDENPKSRRINDTYFIQMKELTTNLQLAPRLRFMVRDVVDLRSNNWVPRREEIKAKTISEIHDEAMKTLGLRPGATGLTRNGRNAPGGPLSPGGFPMNRPGTGGMMPGMPGTPGMPGSRKMPGMPGLDNDNWEVPRSKSMPRGDSLRNQGPLLNKPSSINKPSSINSRLLPHGSGALIGKSALLGSGGPPTRPSSLMASPTHTPAQTAPSPKPVSAAPAVVPVTDKAAGSSHEMPAAVQKKTVSLLEEYFGIRILDEAQQCIEELQCPEYYSEIVKEAINLALDKGPNFIDPLVRLLEHLHTKKIFKTEDLKTGCLLYAALLEDIGIDLPLAPALFGEVVARLSLSCGLSFEVVEEILKAVEDTYFRKGIFDAVMKTMGGNSSGQAILSSHAVVIDACNKLLK
Protein: Cell cycle regulator CcrZ (EC 2.7.1.15) (EC 2.7.1.229) (Cell cycle regulator protein interacting with FtsZ) (A0A0H2ZQL5)
Organism: Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466)
Function: Plays a role in cell cycle regulation and chromosome integrity. Activates DnaA-dependent chromosomal DNA replication initiation ensuring that the chromosome is replicated at the right time during the cell cycle. May regulate replication initiation through phosphorylation of a possible second messenger or metabolite, and by interacting with replication initiation proteins. Has ATPase activity with D-ribose and 2-deoxy-D-ribose in vitro, but not with choline. Involved in DNA damage response (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:34373624}. Note=Localizes at mid-cell, forming a patchy ring. Disassembles from the old septum to assemble at the newly formed division site. Colocalizes with FtsZ during the full cell cycle. Colocalizes with DnaA in newborn cells. {ECO:0000269|PubMed:34373624}.
Interaction partners:
Sequence:
MDLGDNELTLTPIPGKSGKAYMGSYPDGKRIFVKMNTSPILPGLAREQIAPQLLWSRRLADGRDMCAQEWLTGKILTPYDMNRKQIVNILTRLHRSRPLMTQLSRLGYAMETPVDLLQSWQETAPDALRKNHFISEVMADLRQTIPGFREDHATIVHGDVRHSNWIETDSGLIYLVDWDSVRLTDRMFDVAHMLCHYISEHQWKEWLTYYGYKYNQTVLSKLYWYGQLSYLSQISKYYMNQDLENVNREIHGLRHFRDKYGKRR
Protein: IMP-specific 5'-nucleotidase 1 (EC 3.1.3.99) (Q99312)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: IMP-specific 5'-nucleotidase involved in IMP (inosine 5'-phosphate) degradation.
Interaction partners:
- Uridine nucleosidase
- Suppressor of disruption of TFIIS
- Purine nucleoside phosphorylase
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2
- AMP deaminase
- Nicotinamide mononucleotide adenylyltransferase
- Hypoxanthine-guanine phosphoribosyltransferase
- Inosine-5'-monophosphate dehydrogenase 3
- Nicotinate-nucleotide pyrophosphorylase [carboxylating]
Sequence:
MSSRYRVEYHLKSHRKDEFIDWVKGLLASPFVLHAVSHEGDYNDDLATTQRVRSQYADIFKDIEGLIKDKIEFDSRNMSQDEIEDGASSQSLNILGQSRLNLLVPSIGTFFTELPLEQAFLWEDSQRAISARRMVAPSFNDIRHILNTAQIFHFKKQENLHNGKVLRLVTFDGDVTLYEDGGSLVYTNPVIPYILKLLRCGINVGIVTAAGYDEAGTYENRLKGLIVALHDSTDIPVSQKQNLTIMGGESSYLFRYYEDPEEDNFGFRQIDKEEWLLPRMKAWSLEDVEKTLDFAERTLNRLRKRLNLPSEISIIRKVRAVGIVPGERYDEASKRQVPVKLDREQLEEIVLTLQNTLESFAPSRRIQFSCFDGGSDVWCDIGGKDLGVRSLQQFYNPESPIQPSETLHVGDQFAPVGSANDFKARLAGCTLWIASPQETVNYLHRLLETD
Protein: Synaptotagmin-13 (Synaptotagmin XIII) (SytXIII) (Q9EQT6)
Organism: Mus musculus (Mouse)
Function: May be involved in transport vesicle docking to the plasma membrane.
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:11171101}; Single-pass membrane protein {ECO:0000269|PubMed:11171101}.
Interaction partners:
Sequence:
MVLSVPVIALGATLGTATSILALCGVTCLCRHMHPKKGLLPRDREPDPEKARPGVLQAAQQFNIKKSTEPVQPRPLLKFPDIYGPRPAVTAPEVINYADYTLETTEESAAPASPQAQSDSRLKRQVTEELSIRPQNGVVEDVCVMETWNPEKAASWNQAPKLHFRLDYDQKKAELFVTSLEAVTSDHEGGCDCYIQGSVAVKTGSVEAQTALKKRQLHTTWEEGLALPLGEEELPTATLTLTLRTCDRFSRHSVIGELRLGLDGASVPLGAAQWGELKTTAKEPSAGAGEVLLSISYLPAANRLLVVLIKAKNLHSNQSKELLGKDVSVKVTLKHQAQKLKKKQTKRAKHKINPVWNEMIMFELPDDLLRASSVELEVLGQGEEGPSCELGHCSLGLHASGSERSHWEEMLKNPRRQIAMWHQLHL
Protein: Phosphotransferase (EC 2.7.1.-) (Q9GQS3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVHELCQQLLLTDEQVQELCYRILHELRRGLAKDTHPKANVKCFVTYVQDLPNGNERGKFLALDLGGTNFRVLLIHLQENNDFQMESRIYAIPQHIMIGSGTQLFDHIAECLSNFMAEHNVYKERLPLGFTFSFPLRQLGLTKGLLETWTKGFNCAGVVNEDVVQLLKDAIARRGDVQIDVCAILNDTTGTLMSCAWKNHNCKIGLIVGTGANACYMERVEEAELFAAEDPRKKHVLINTEWGAFGDNGALDFV
Protein: Thioredoxin superfamily protein (O65541)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Anamorsin homolog
- Protein BOLA2
- SufE-like protein 1, chloroplastic/mitochondrial
- Protein BOLA1
- Protein BOLA4, chloroplastic/mitochondrial
Sequence:
MSGTVKDIVSKEELDNLRHSGAPLVLHFWASWCDASKQMDQVFSHLATDFPRAHFFRVEAEEHPEISEAYSVALVPYFVFFKDGKTVDTLEGADPSSLANKVGKVAGSITPASLGLAAGPTILETVKKNAKASGQDRAQPVSTADALKNRLEKLTLLCYS