wanglab/gogpt-training-data huggingface dataset:
Protein: T. brucei spp.-specific protein (Q4GYH5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MHFIILMCSRLLFTHFPLRVSLHVCVFFILLFCFASFYSRMHFSLVLLSVSSVLVSELLLLPPSLPFSFLPSLLPSLRFYFNSLFAFTPIFVYFPLPIFFSFFFFSLFYIVGPLPVATVTVGPSPPLSSSSHFFFLFILLCICTSKRASRIFFEHVPSLRVLSVCLYEFFFFLSGLEV
Protein: Monodehydroascorbate reductase 4, peroxisomal (AtMDAR4) (EC 1.6.5.4) (Q9LK94)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the conversion of monodehydroascorbate to ascorbate, oxidizing NADH in the process. Involved in the detoxification of H(2)O(2) that escapes the peroxisome and causes oxidative damage to oil bodies.
Subcellular location: Peroxisome membrane {ECO:0000269|PubMed:16146528}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- L-galactono-1,4-lactone dehydrogenase, mitochondrial
- Glutathione S-transferase DHAR2
- Glutathione S-transferase DHAR1, mitochondrial
- Stress-response A/B barrel domain-containing protein UP3
- Glutathione S-transferase DHAR3, chloroplastic
- Rieske
- L-ascorbate peroxidase 3
- F18O14.31
- Glutathione reductase, chloroplastic
- L-ascorbate peroxidase 1, cytosolic
Sequence:
MGRAFVYVILGGGVAAGYAALEFTRRGVSDGELCIISEEPVAPYERPALSKGFLLPEAPARLPSFHTCVGANDEKLTPKWYKDHGIELVLGTRVKSVDVRRKTLLSSTGETISYKFLIIATGARALKLEEFGVEGSDAENVCYLRDLADANRLATVIQSSSNGNAVVIGGGYIGMECAASLVINKINVTMVFPEAHCMARLFTPKIASLYEDYYRAKGVKFIKGTVLTSFEFDSNKKVTAVNLKDGSHLPADLVVVGIGIRPNTSLFEGQLTIEKGGIKVNSRMQSSDSSVYAIGDVATFPVKLFGEMRRLEHVDSARKSARHAVSAIMDPIKTGDFDYLPFFYSRVFAFSWQFYGDPTGDVVHFGEYEDGKSFGAYWVKKGHLVGSFLEGGTKEEYETISKATQLKPAVTIDLEELEREGLGFAHTVVSQQKVPEVKDIPSAEMVKQSASVVMIKKPLYVWHAATGVVVAASVAAFAFWYGRRRRRW
Protein: Myc protein (Q14901)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRGSGRLRTPELVCSRPPPPGPGRPWLPSCLEKGRASQRLGGKKNGGRDRAEYKSRFSGLYLTRCSNSSERQRERAGGRLGWKSRASRAALRASWEGRSGANRGLRLWPSPPADPPASRPQPLPHPRNFAHSSGRALCTGTYNTRARTRLSRRGEAILPIWGHFPAAARTRFSERLSLQLLRRWIFFG
Protein: Diphosphomevalonate decarboxylase (EC 4.1.1.33) (Q6FWQ9)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Isopentenyl-diphosphate Delta-isomerase
- Farnesyl pyrophosphate synthase
- Mevalonate kinase
- Phosphomevalonate kinase
- Candida glabrata strain CBS138 chromosome H complete sequence
- Hydroxymethylglutaryl-CoA synthase
- L-lactate dehydrogenase
- Candida glabrata strain CBS138 chromosome C complete sequence
- Terpene cyclase/mutase family member
- Acetyl-CoA acetyltransferase
Sequence:
MTYVASTTAPVNIATLKYWGKRDAKLNLPTNSSISVTLAQEDLRTLTSAATSSEFKEDKLWLNGKEESLSSERTQNCLADLRALRRQLEEKDSSLPPMSQWKLHIVSENNFPTAAGLASSAAGFAALVMAIAKLYELPQSASDISKIARKGSGSACRSLFGGYVAWEMGEKADGSDSKAVEVAPLEHWPNMKAAVLVVSADKKDTPSTSGMQLTVNTSDLFKERITNVVPKRFEAMKKAILDKDFPTFAELTMKDSNSFHATCLDSFPPIFYINDTSKKIIKLCHLINEFYGETIVAYTYDAGPNSVLYYLEENEEKLFAFIYTLFSKVDGWQSKYNSEELSKFTSTFNNQVKGKFQFDLDDTIQENVSRVILTRVGPGPQDTKECLINEETGLPK
Protein: GH14591p (Q95SM1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MYNRAAAMGFPKDFAKDNSCQLQQQQQQQQSPQVTTNKQQANQQTQQQPQQQSQQSQPHLTQLQTALSQNYQQQQQQTQAQKLPQQQQQQPPQQLNYQQQQAQLNHNYTAQQQATAVPDKPPAAQSTVAAAVSESSSNMMNLPSTAHQHHLSQTHHLAAYNKPTPPPPQTYSNPLMQSMLGYAGNYFDKTMPPAAHMYSASSSAASAYGNPAQQLPGNYVPGNNNPAHQQQQQPQQQQQQQQQAPAVPPAEVKAPAKRGRKKKAATIAAEAAAAAAKQQQQQQQQQQQQAQQQQQVAAQQQHQQQQVSAQQQQQQHQQVAAQQQQHQAMPQYNMPQSMASAAAATNNQLQAHAQALQQVSQLYAGLKSGGVSSPVGSSAATPVNSGGSTTNQTAADAAAISLKTSTGGMVPGSAFNFAPTPGTLGLYGDQAAAASSYLDQFRDAPNPYYMPPAPAHSGTAANPSGNAADKGQNPLNTAAGSYPFLAAAHPSSRAAAAAAAYPFADPNSQLYQQYLRRDDFHTRMIFNQSLLGGPAAAAAAAGYGQPPPPPSAYQRAALGMPKPYDINRQSWF
Protein: Thyroid hormone receptor interactor 11 (D4ABD7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004395}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004395}.
Interaction partners:
- Intraflagellar transport 20
- Coiled-coil domain containing 27
- NHS actin remodeling regulator
Sequence:
MSSWLGGLGSGLGQSLGQVGGSLASLTGQISNFTKDMLMEGTEDVPDLPNSGREENGATHSVLRSENERLKKLYTDLEEKHEASELQIKQQSSSYRSQLQQKEEEINHLKARQTALQDELLRLQVAAQSAHSGAATAPAATAPASFSYGISHPVSAFHEDDMDFGDVISSQQEINRLSNEVSRLESELGHWRHIAQVQGAQSSDQTEICKLQNIIKELKQNRSQEIDDHQHEMSVLQNAHQQKLTEISRRHREELRDYEERIEELENLLQQGGSGVTVTDHSKVYEMQNTIQSLQMERVESSRKIEDLENKIKEIHKRLSSAEHDREVCKKEQERLEMEKRQMAEQCERLKLDCREAQQSALRLTDAVTEDERSLSQSASVAEVLRLQQALTDAENEVKRLSSLNQDTNLAEDNQKLQMCVQTLEKEKSLLSQEKEELQTSLSRLSHEYEVIKSTATRDSDLSSQVHDLKHNLEAKEQELNQSIHENEILMAELEELDKQNQEATKHVILIKEQLSKQQSEGDSVIKRLKEELDDEKKRTHQLEDDKMNIIKELNVQKEKLTHSEQVLSDLQLTKQKLEGKVEDLVDQLSKSEKNNFDIQKENRELREHIRQNEEELSTVRSELTQSQTQGSNSNLKDDLLREKETEVQSLKQNLSEIEQLNEHLKQVAFDLRIENEKLVVACEDVRNQLEESVAGNNQISLEKAAILEWEKAQLEAEPCRAEKRLLEEGRKYRQTVQGPSSTHSPDASALQLEQERLIQLNQEKDFEIAELKKSIEQMDTDHKQTKETLSSSLEEQKQLAQLINEKEICIVKLKEKSSELQRELDRCSQALRKNETLRQTIEEKDRSLGSMKEENNHLQEELERLREQQSRAVPVPEPRTLDSTTELESELSQLHTIKDHLEEEIKHHQKMIEDQNQNKMQLLQSLQEQKKAMDEFKYQHEQMSITHSRLFLEKDEEIKNLQKTIEQIKAQLQEERQDSQTENSDIFQETKVQSLNIEIGSEKHDLSKAETERLVKGIKERELEIKLLNEKNISLTKQIDQLSKDEVGKLTQIIQQKDVEIQALHARISSASYSQDVVYLQQQVQAYAMEREKVMVVLSEKTRENSKLKSEYHKMIDILSAKEAALIKLQDENKKMSTRFESSGQDMFKETIQNLSRIIREKDIEIDALSQKCQTLLTVLQTSGTGSEVGGVNSNQFEELLQERDKLKQQVKKMEEWKQQVMTTVQNMQHESAQLQEELHQLQAQVSVDSDNNTKLQVNYTGLIQSYEQNETKLKNFGQELAQVQHSIGQLCTTKDLLLGKLDSMSPQLSPGSSLTTQAAEPLKASQCSGPHESSHLLQQEVDDLRKSLQEKDATIRTLQENNHRLSDSMAASSEGERKEHEQTDSEVKQLKEKQEVLQNLLKEKDLLIKAKSDQLHSSNENFANKVSENELLRQAVTNLKERILILEMDISKLKGENEKVIEASKGKETEYQALQETNMKFSMMLREKEFECHSMREKALAFEQLLKEKEQGKAGELNQLLNAVKSMQEKTVTFQQERDQVMLALKQKQMETSTLQNEVQRLRDKEARLNQELQRLRDHLLESEDSHTREALAAEDREAKLRKKVSVLEEKLVSSSNAMENASHQASVQVESLQEQLNMVSKQRDETALQLSVSQEQVKQYAMSLTNLQMVLEHFQQEEKAMYSAELEKQNQLLTEWKKKAESLEGKVLSLQERLDEANAALDSASRLTEQLDLKEEQIEELKKQNELHQEMLDDAQKKLMSLVNSTEGKVDKVLMRNLFIGHFHTPKNQRHEVLRLMGSILGVKREEMEQLFAEDQGGVTRWMAGWLGGGSKSVPNTPLRPNQQSVFNSSFSELFVKFLETESHPSVPPPKLSVHDLKPLDSPGRRKVDTGTAEGFRDTAESRAGRRTDMNPFLAPRSAAVPLINPAGHGPGGPGHLLLKPISDVLPTFTPLPVSPDNSAGVVLKDLLKQ
Protein: Mortality factor 4 like 1 (H0YMJ0)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEVTGPRFQCTFFSGSSSQGEKNGERVLCFHGPLLYEAKCVKVAIKDKQVKYFIHYSGWNKNWDEWVPESRVLKYVDTNLQKQRELQKANQEQYAEGKMRGAAPGKKTSGLQQKNVEVKTKKNKQKTPGNGDGGSTSETPQPPRKKRARVDPTVENEETFMNRVEVKVKIPEELKPWLVDDWDLITRQKQLFYLPAKKNVDSILEDYANYKKSRGNTDNKEYAVNEVVAGIKEYFNVMLGTQLLY
Protein: Nhs protein (B2RXX7)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MPFAKRIVEPQWLCRQRRPAPGPDEDTSGGSVEPPPPLQPPGRREEAEAPEPEEPPRVPPAPLPLPPLPPSLPAPAEQDQQPPSEAREAGEESVAGVSEAASAPGETSEASAEAVLLMLDLCAVSNAALARVLRQLSDVARHACSLFQELESDIQLTHRRVWALQGKLGSVQRVLSTLDPKQEAVPVSNLDIESKLSVYYRAPWHQQRNIFLPATRPPCVEELHRHARQSLQALRREHRSRSDRREQRAAAPLPIAAPPLPAYPPAHSQRRREAKDRHFLTFNSTRSPSPTECCHMAPWSRKSHSPEDEDTDAMLGQRPKNPIHNVPSTLDKQTNWNKALPLPTPEEKMKQDAQVISSCIIPINVTGVGFDREASIRCSLVHSQSVLQRRRKLRRRKTISGIPRRVQQEIDSDESPVARERNVIVHTNPDPSNTVNRRSGTRDSECQTEDILIAAPSRRRIRAQRGQSIAASLSHSAGNISALADKGDTMFTPVVSSRTRSRSLPREGNRGGDAEPKVGAKPSAFEEGERFVGDHERTPNDCSEAPSSPSTQEHQPALGLACSQHLHSPQQKLSERGRSRLSRMAADSGSCDISSNSDTFGSPVHCISTASVLLSSHMDQKEDHQSSSGNWSGSSSTCPSQTSETIPPAASPPLTGSSHCDSELSLNTAPNANEDASVFVTEQYNDHLDKVRGHRTNSFTSTVADLLDDPNNSNTSDSEWNYLHHHHDASCRQDFSPERPKADSLGCPSFTSMGTYDSFLEKSPSDKADTSSHFSVDTEGYYTSMHFDCGLKGNKTYVCHYAGLGPENGQGVGVPPALPDCAWQEYLDHRRQGRPSISFRKPKAKPTPPKRSSSLRKSDGNADISEKKEPKISSGQHLPHSSREMKLPLDFSNTPSRVENANLPAKLDSSWINQSEHAIKEPQLDTPDISPFKDEGAESTHYADLWLLNDLKTNDPYRSLSNSSTATGTTVIECIKSPESSESQTSQSESRATTPSLPSVDNEYKLASPEKLAGLASPSSGYSSQSETPTSSFPTAFFSGPLSPGGSKRKPKVPERKSSLQQPSLKDGALSLSKDFELPIIPPSHLDLSALHVLNKPFHHRHPLHVFTHKQNTVGDMPRSNPAPSLAITPTVLKSVNLRSISKSEEVRQKEGNNTDLPYLEENAATAASVASLSPSKARPHTAKKSISRQYSAEDTLLPFLDSSVAEMGPEKHLEKNPNFDGKSHGDPETATSASSNLPDSNVMKEQIQMESELISENILRKNCGFSTGFQRVSASRPSDLGSKMIQYGASPDGTVQQGQKAPSGVREEGGKPESVDGITLQANSSTRVTDISSQYKHQRVISRHHDKVPVTIRHESEMSTVNSFPEKCSEQENIASGISPQSASDNSRAEETQGSMDETSLKESSPSDDSITSPLSEDSQAGAEGVFVSPNKPRTTEDLFAVIHRSKRKVLGRKDSGDMSVRSKSRVPLGSSSSSANSVTSPSSNVTAGTSQRSPGLIYRNAKKSNTSNEEFKLLLLKKGSRSDSSYRMSATEILKSPVLPKPPGEFTAESPQSPDDTHQGTPGTEALSPLSPCSPRVNAEGFSSKNFATSASARVGRSRVPPVASSSRYSVRCRLYNTPMQAISEGETENSDGSPHDDRSSQSST
Protein: Lysine--tRNA ligase (EC 6.1.1.6) (Lysyl-tRNA synthetase) (Q9W327)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Probable glutamine--tRNA ligase
- Methionine--tRNA ligase, cytoplasmic
- Isoleucine--tRNA ligase, cytoplasmic
- Bifunctional glutamate/proline--tRNA ligase
- leucine--tRNA ligase
- Probable arginine--tRNA ligase, cytoplasmic
- Probable aminoacyl tRNA synthase complex-interacting multifunctional protein 2
- leucine--tRNA ligase
- Tyrosine--tRNA ligase
- Aspartate--tRNA ligase, cytoplasmic
Sequence:
MFARCALRTVQGSWPRCRYTGIQPLAAGFHVSAPQMEPSKQTKLELKRRLKAEQKAKEKAEKAAAAPAENTAGKKKSSAAEEEEISPNEYFKLRSAAVQELKRSPATDPYPHKFHVSSSLEDFIAKYENSLKEGETLENVKLSVAGRVHAIRESGAKLIFYDLRGEGVKVQVMASAKSYKSEADFEIDTSKLRRGDIIGVVGHPGKTKKGELSVMPSEIKLLSPCLHMLPHLHFGLKDKETRYRQRYLDLILNNNVREKFQIRAKIISYVRQFLDRLGFLEIETPMMNMIAGGATAKPFVTHHNDLKMDLFMRIAPELYHKMLVVGGLDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYADIMDITEQLVSGMVKAIRGSYKVIYHPEGPEGPEQELDFTPPFKRVSMIKTLEEKLQVKFPAADTFNSPETNQFLSQLCAKHQVECPAPRTTARLLDKLVGEFIEEFCVNPTFICEHPQIMSPLAKYHRSIPGLTERFELFVAKKEICNAYTELNDPVVQRERFEQQASDKAAGDDEAQLVDENFCTSLEYGLPPTGGFGMGIDRLAMFLTDSNNIKEVLLFPAMKPEDANRTAAETAPTAQQ
Protein: Probable U6 snRNA-associated Sm-like protein LSm3 (Q9Y7M4)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Binds specifically to the 3'-terminal U-tract of U6 snRNA.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- LSM complex subunit lsm6
- LSM2-LSM8 complex subunit lsm8
- LSM complex subunit lsm7
- LSM complex subunit lsm5
- LSM complex subunit lsm4
- LSM complex subunit lsm2
- LSM1-LSM7 complex subunit lsm1
- Small nuclear ribonucleoprotein-associated protein B
- Small nuclear ribonucleoprotein Sm D2
- Small nuclear ribonucleoprotein Sm D1
Sequence:
MESAQAVAEPLDLVRLSLDEIVYVKLRGDRELNGRLHAYDEHLNMVLGDAEEIVTIFDDEETDKDKALKTIRKHYEMLFVRGDSVILIAPPRN
Protein: Dirigent protein (PhDPO) (Q1ZZU9)
Organism: Sinopodophyllum hexandrum (Himalayan may apple) (Podophyllum hexandrum)
Function: Dirigent proteins impart stereoselectivity on the phenoxy radical-coupling reaction, yielding optically active lignans from two molecules of coniferyl alcohol in the biosynthesis of lignans, flavonolignans, and alkaloids and thus plays a central role in plant secondary metabolism (By similarity). Also involved in the biosynthesis of etoposide, a chemotherapeutic compound of the topoisomerase inhibitor family.
Subcellular location: Secreted, extracellular space, apoplast {ECO:0000250|UniProtKB:Q9SUQ8}.
Interaction partners:
Sequence:
MGGEKAFSFIFLLFLCFFLANLSASSAHPPRQKLKQRIPCKQLVLYFHDVVYNGHNKANATASIVGAPQGADLVKLAGENHFGNVVVFDDPITLDNNFHSPPVGRAQGLYVYDKKDTFHSWLSFSFTLNTTMHQGTLIFMGADPILIKNRDITVVGGTGDFFMARGIATIATDSYEGEVYFRLKVDIKLYECW
Protein: Insulin receptor substrate 2 (F1MAL5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Growth factor receptor-bound protein 2
- Insulin-like growth factor 1 receptor
- Insulin receptor substrate 1
- Insulin-2
- Insulin-1
- Insulin receptor
- Tyrosine-protein kinase JAK2
- Suppressor of cytokine signaling 3
- Phosphatidylinositol 3-kinase regulatory subunit alpha
- Insulin receptor substrate 3
Sequence:
MASAPLPGPPASAGGDGPNLNNNNNNNNNHSVRKCGYLRKQKHGHKRFFVLRGPGTGGEEAAAAGGSPPQPPRLEYYESEKKWKSKAGAPKRVIALDCCLNINKRADAKHKYLIALYTKDEYFAVAAENEQEQEGWYRALTDLVSEGRSGDGGSGTTGGSCSASLPGALGGSAGAAGCDDNYGLVTPATAVYREVWQVNLKPKGLGQSKNLTGVYRLCLSARTIGFVKLNCEQPSVTLQLMNIRRCGHSDSFFFIEVGRSAVTGPGELWMQADDSVVAQNIHETILEAMKALKELFEFRPRSKSQSSGSSATHPISVPGARRHHHLVNLPPSQTGLVRRSRTDSLAATPPAAKCTSCRVRTASEGDGGAAGGAGTAGGRPMSVAGSPLSPGPVRAPLSRSHTLSAGCGGRPSKVALAPAGGALQHSRSMSMPVAHSPPAATSPGSLSSSSGHGSGSYPLPPGSHPHLPHPLHHPQCQRPSSGSASASGSPSDPGFMSLDEYGSSPGDLRAFSSHRSNTPESIAETPPARDGSGGELYGYMSMDRPLSHCGRPYRRVSGDGAQDLDRGLRKRTYSLTTPARQRQVPQPSSASLDEYTLMRATFSGSSGRLCPSLPASSPKVAYNPYPEDYGDIEIGSHKSSSSNLGADDGYMPMTPGAALRSGGPNSCKSDDYMPMSPTSVSAPKQILQPRSAAALPPSGAAVPAPPSGAGRTFPVNGGGYKASSPAESSPEDSGYMRMWCGSKLSMENPDPKLLPNGDYLNMSPSEAGTAGTPPDFFSAALRPGGEALKGVPGHCYSSLPRSYKAPCTCGGGDNDQYVLMSSPVGRILEEERLEPQATPGAGTFGAAGGSHTQPHHSAVPSSMRPSGIVGRPEGFLGQRCRAVRPTRLSLEGLQTLPSMQEYPLPTEPKSPGEYINIDFGEGGTRLSPPAPPLLASAASSSSLLSASSPASSLGSGTPGTSSDSRQRSPLSDYMNLDFSSPKSPKPSTRSGDTVGSIDGLLSPEASSPYPPLPPRPSASPSSLQQPLPPAPGDLYRLPPATAATSQGPTAGSSMSSEPGDNGDYTEMAFGVAATPPQPIAAPPKPEGARVTSPTSGLKRLSLMDQVSGVEAFLQVSQPPDPHRGAKVIRADPQGGRRRHSSETFSSTTTVTPVSPSFAHNSKRHNSASVENVSLRKSSEGNSILGGSDEPSTSPGQAQPSAGVPPAPQARPWNPGQPGALIGCPGGSSSPMRRETSVGFQNGLNYIAIDVRGEQGSLAQSQPQHPQPGDKNSWGRTRSLGGLLGTVGGSGTSGVCGGPGTGALPSASTYASIDFLSHHLKEATVVKE
Protein: Inner capsid protein VP2 (P17462)
Organism: Rotavirus A (strain RVA/Cow/United Kingdom/UK/1975/G6P7[5]) (RV-A)
Function: Inner capsid protein that self-assembles to form an icosahedral capsid with a T=2 symmetry, which consists of 120 copies of VP2, with channels at each of its five-fold vertices. This capsid constitutes the innermost concentric layer of the viral mature particle. It encapsidates the polymerase VP1, the capping enzyme VP3 and the genomic dsRNA, thereby defining the core. The innermost VP2 capsid and the intermediate VP6 capsid remain intact following cell entry to protect the dsRNA from degradation and to prevent unfavorable antiviral responses in the host cell during all the replication cycle of the virus. Nascent transcripts are transcribed within the structural confines of this double-layered particle (DLP) and are extruded through the channels formed by VP2 N-termini. VP2 is required for the replicase activity of VP1 polymerase (By similarity). Probably recruits a copy of a VP1-VP3 complex, potentially along with a segment of plus-strand RNA, as a decamer of VP2 assembles. May activate the autoinhibited VP1/RNA complex to coordinate packaging and genome replication (By similarity).
Subcellular location: Virion {ECO:0000255|HAMAP-Rule:MF_04127, ECO:0000269|PubMed:20122940}. Note=Inner capsid protein. Also found in spherical cytoplasmic structures, called virus factories, that appear early after infection and are the site of viral replication and packaging (Potential). {ECO:0000255|HAMAP-Rule:MF_04127, ECO:0000269|PubMed:20122940}.
Interaction partners:
Sequence:
MAYRKRGATVEADINNNDRMQEKDDEKQDQNNRMQLSDKVLSKKEEVVTDSQEEIKIRDEVKKSTKEESKQLLEVLKTKEEHQKEIQYEILQKTIPTFEPKESILKKLEDIKPEQAKKQTKLFRIFEPRQLPIYRANGEKELRNRWYWKLKKDTLPDGDYDVREYFLNLYDQVLTEMPDYLLLKDMAVENKNSRDAGKVVDSETASICDAIFQDEETEGAVRRFIAEMRQRVQADRNVVNYPSILHPIDYAFNEYFLQHQLVEPLNNDIIFNYIPERIRNDVNYILNMDRNLPSTARYIRPNLLQDRLNLHDNFESLWDTITTSNYILARSVVPDLKELVSTEAQIQKMSQDLQLEALTIQSETQFLTGINSQAANDCFKTLIAAMLSQRTMSLDFVTTNYMSLISGMWLLTVVPNDMFIRESLVACQLAIVNTIIYPAFGMQRMHYRNGDPQTPFQIAEQQIRKFSGSGIGWHFVNNNQFRQVVIDGVLNQVLNDNIRNVHVIKQLMQALMQLSRQQFPTMPVDYKRSIQRGILLLSNRLGQLVDLTRLLAYNYETLMACVTMNMQHVQTLTTEKLQLTSVTSLCMLIGNATVIPSPQTLFHYYNVNVNFHSNYNERINDAVAIITAANRLNLYQKKMKAIVEDFLKRLHIFDVARVPDDQMYRLRDRLRLLPVEVRRLDIFNLILMNMDQIERASDKIAQGVIIAYRDMQLERDEMYGYVNIARNLDGFQQINLEELMRTGDYAQITNMLLNNQPVALVGALPFVTDSSVISLIAKLDATVFAQIVKLRKVDTLKPILYKINSDSNDFYLVANYDWVPTSTTKVYKQVPQQFDFRNSMHMLTSNLTFTVYSDLLAFVSADTVEPINAVAFDNMRIMNEL
Protein: Cell division protein FtsZ homolog 2-2, chloroplastic (AtFtsZ2-2) (Plastid division protein FTSZ2-2) (Q9LXJ0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Exhibits GTPase activity (By similarity). Component of the plastid division machinery that forms a contractile ring at the division site. Contributes to plastid division in the vegetative shoot apex, at the shoot apical meristem (SAM) where the proplastid-to-chloroplast transition takes place.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:18431481, ECO:0000269|PubMed:22823492}. Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:18431481}; Peripheral membrane protein. Note=Forms a contractile ring at the chloroplast midpoint (PubMed:22823492, PubMed:25731613). Exhibits a dynamic trunover in FtsZ ring facilitated by ARC3-mediated destabilization (PubMed:25731613). {ECO:0000269|PubMed:22823492, ECO:0000269|PubMed:25731613}.
Interaction partners:
- Protein ACCUMULATION AND REPLICATION OF CHLOROPLASTS 6, chloroplastic
- Dynamin-like protein ARC5
- Protein ACCUMULATION AND REPLICATION OF CHLOROPLASTS 3
- Plastid division protein PDV2
- Plastid division protein CDP1, chloroplastic
- Plastid division protein PDV1
- Probable transmembrane GTPase FZO-like, chloroplastic
- Dynamin
Sequence:
MAAYVSPCLTPPDSRVLTVLRKSVLPDHHLGTRVGCLRMSEGTTKRYRVVASHKYESSSIRNSLNSHSTSHFQSQDSFLNLHPEISMLNPRKETSSVPITEDLDELSTPNTYNEARIKVIGVGGGGSNAVNRMIESEMIGVEFWIVNTDIQAMRISPVFPDNRLQIGKELTRGLGAGGNPEIGMNAATESKEAIQEALYGSDMVFVTAGMGGGTGTGGAPIIAGVAKAMGILTVGIVTTPFSFEGRRRALQAQEGIAALRDNVDTLIVIPNDKLLAAVSQSTPVTEAFNLADDILRQGVRGISDIITIPGLVNVDFADVRAIMANAGSSLMGIGTATGKTRARDAALNAIQSPLLDIGIERATGIVWNITGGSDLTLFEVNAAAEVIYDLVDPTANLIFGAVVDPSYSGQISITLIATGFKRQEEGEGRPLQATQADASMGATRRPSSSFTEGSSIEIPEFLKKKGRSRYPRL
Protein: Immunoglobulin kappa variable 2-30 (Ig kappa chain V-II region RPMI 6410) (P06310)
Organism: Homo sapiens (Human)
Function: V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen.
Subcellular location: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
Interaction partners:
Sequence:
MRLPAQLLGLLMLWVPGSSGDVVMTQSPLSLPVTLGQPASISCRSSQSLVYSDGNTYLNWFQQRPGQSPRRLIYKVSNRDSGVPDRFSGSGSGTDFTLKISRVEAEDVGVYYCMQGTHWP
Protein: TATA-box-binding protein (TATA sequence-binding protein) (TATA-binding factor) (TATA-box factor) (Transcription initiation factor TFIID TBP subunit) (P20227)
Organism: Drosophila melanogaster (Fruit fly)
Function: General transcription factor that functions at the core of the DNA-binding multiprotein factor TFIID. Binding of TFIID to the TATA box is the initial transcriptional step of the pre-initiation complex (PIC), playing a role in the activation of eukaryotic genes transcribed by RNA polymerase II.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P20226}.
Interaction partners:
- B-related factor 1
- Transcription initiation factor TFIID subunit 5
- Transcription initiation factor TFIID subunit 6
- Transcription initiation factor TFIID subunit 9
- Transcription initiation factor TFIID subunit 2
- Transcription initiation factor TFIID subunit 12
- Transcription initiation factor TFIID subunit 11
- Transcription initiation factor TFIID subunit 4
- Transcription initiation factor TFIID subunit 1
- Transcription initiation factor IIB
Sequence:
MDQMLSPNFSIPSIGTPLHQMEADQQIVANPVYHPPAVSQPDSLMPAPGSSSVQHQQQQQQSDASGGSGLFGHEPSLPLAHKQMQSYQPSASYQQQQQQQQLQSQAPGGGGSTPQSMMQPQTPQSMMAHMMPMSERSVGGSGAGGGGDALSNIHQTMGPSTPMTPATPGSADPGIVPQLQNIVSTVNLCCKLDLKKIALHARNAEYNPKRFAAVIMRIREPRTTALIFSSGKMVCTGAKSEDDSRLAARKYARIIQKLGFPAKFLDFKIQNMVGSCDVKFPIRLEGLVLTHCNFSSYEPELFPGLIYRMVRPRIVLLIFVSGKVVLTGAKVRQEIYDAFDKIFPILKKFKKQS
Protein: Probable GTP-binding protein EngB (P0A6P7)
Organism: Escherichia coli (strain K12)
Function: Necessary for normal cell division and for the maintenance of normal septation. Depletion of this protein leads to a severe reduction in growth rate and to extensive filamentation, with a block beyond the stage of segregation. Essential for bacteria survival.
Interaction partners:
- GTPase Der
- tRNA modification GTPase MnmE
- Ribosome-binding ATPase YchF
- GTPase ObgE/CgtA
- GTPase HflX
- Ribosomal silencing factor RsfS
- Large ribosomal subunit protein bL17
- Large ribosomal subunit protein uL15
- Large ribosomal subunit protein bL21
- 23S rRNA
Sequence:
MTNLNYQQTHFVMSAPDIRHLPSDTGIEVAFAGRSNAGKSSALNTLTNQKSLARTSKTPGRTQLINLFEVADGKRLVDLPGYGYAEVPEEMKRKWQRALGEYLEKRQSLQGLVVLMDIRHPLKDLDQQMIEWAVDSNIAVLVLLTKADKLASGARKAQLNMVREAVLAFNGDVQVETFSSLKKQGVDKLRQKLDTWFSEMQPVEETQDGE
Protein: Carotenoid cleavage dioxygenase 7, chloroplastic (OsCCD7) (Beta,beta-carotene 9',10'-oxygenase) (EC 1.13.11.68) (Protein DWARF-17) (Protein HIGH-TILLERING DWARF 1) (Protein MAX3 homolog) (Q7XU29)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Involved in strigolactones biosynthesis by cleaving asymmetrically a variety of linear and cyclic carotenoids at the 9-10 double bond. Produces one C(13) beta-ionone and the C(27) 10'-apo-beta-carotenal. Strigolactones are hormones that inhibit tillering and shoot branching through the MAX-dependent pathway, contribute to the regulation of shoot architectural response to phosphate-limiting conditions and function as rhizosphere signal that stimulates hyphal branching of arbuscular mycorrhizal fungi and trigger seed germination of root parasitic weeds. Can rescue the phenotype in the Arabidopsis max3 mutant.
Subcellular location: Plastid, chloroplast {ECO:0000250}.
Interaction partners:
- Beta-carotene isomerase D27, chloroplastic
- Carotenoid cleavage dioxygenase 8 homolog B, chloroplastic
- Carotenoid cleavage dioxygenase 8 homolog A, chloroplastic
- Strigolactone esterase D14
Sequence:
MATQAIAPMHAAVVHRHHVLPPRRCVRRRGVFVRASAAAAAAAAETDTLSAAFWDYNLLFRSQRDECLDSIPLRVTEGAIPPDFPAGTYYLAGPGIFSDDHGSTVHPLDGHGYLRSFRFRPGDRTIHYSARFVETAAKREESRDGASWRFTHRGPFSVLQGGKKVGNVKVMKNVANTSVLRWGGRLLCLWEGGQPYEVDPRTLETVGPFDLLGLAAADDNKATNASAARRPWLQEAGLDAAARLLRPVLSGVFDMPGKRLLAHYKIDPRRGRLLMVACNAEDMLLPRSHFTFYEFDAHFDLVQKREFVVPDHLMIHDWAFTDTHYILLGNRIKLDIPGSLLALTGTHPMIAALAVDPRRQSTPVYLLPRSPETEAGGRDWSVPIEAPSQMWSVHVGNAFEEANRRGGLDVRLHMSSCSYQWFHFHRMFGYNWHHKKLDPSFMNAAKGKEWLPRLVQVAIELDRTGECRRCSVRRLSDQHARPADFPAINPSYANQRNRFVYAGAASGSRRFLPYFPFDSVVKVDVSDGSARWWSTDGRKFVGEPVFVPTGGGEDGGYVLLVEYAVSKHRCHLVVLDAKKIGTENALVAKLEVPKNLTFPMGFHGFWGDE
Protein: Probable esterase LipO (O06832)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Long-chain-fatty-acid--CoA ligase FadD13
- Phospholipid/glycerol acyltransferase domain-containing protein
- Medium/long-chain-fatty-acid--CoA ligase FadD8
Sequence:
MRFRRMARPRPLTRAAVELLNAANGLRPLSGSGYSTVLAFWLGWPTSEVPGVYLGASVLDALRRGRRGDFGGLKGKAALALTAAAWVILAVIRYRGATTPGPVLEAGLTEQLGPDYAKELATLPTEPMRSRGRNLPLRTAMARRRYVETTNVVCYGPYGRANLADIWRRRDLPRDAKAPVLVQVPGGAWVLGWRRPQAYPLMSHLAARGWVCVSLNYRVSPRHTWPDHIVDVKRALAWVKENIAAYGGDPNFVAISGGSAGGHLCALAALTPNDPRFQPGFEQVDTSVAAAVPVYGRYDWFTTDAPGRREFVGLLETFVVKRKFSTHRDIFVDASPIHHVRADAPPFFVLHGRHDSLIPVAEAHAFVEELRAVSKSPVAYADLPHAQHAFDVFGSPRAHHTAEAVARFLSWVYATNPPAT
Protein: Vacuolar protein sorting-associated protein 54 (D7SFN0)
Organism: Caenorhabditis elegans
Subcellular location: Golgi apparatus, trans-Golgi network {ECO:0000256|ARBA:ARBA00004601}.
Interaction partners:
Sequence:
MMHDVVDGRLAGKLVAKTDDFWQVVRSYSGLQEQLANALQCVMVVRKNLKRVDELVCDQSKKIVEVHERYEQKKKLLAKLHDISCLREAQSTVQMMLSQGDYPKAIECIETSLDVLSKELNGVTCFRHLASQLRELYTVIGRMMNEDFASLIQKELGVKPEAGTMIQAEGELSAVLLGLMRMRKYSFIAVLREEIIEGVKSVMRQVIKNQILNNGVDLNDFDPSLTQLGEPVRRMKHADFLKTVKAVMDEEFYFCKRLEALQDILLETVERANPLHRHGSEDIIVERIEEAKDIHESESDDEVGTTFSKSASSGGFSVGGSALSSNASATTLLSIEVRSEAFLRHVLPLIAEFGHQCAQQRISRLLIARAKNASVTEATTPTQLSECIKLVKEFQSKCDKEGWYSTQNQKVGGLGRSVNKLSMDYIEKFHAARKIRIGNMLDTELWKATDVSIVDQNIVDMAMETGQLRNTKRIDDGPIKKSFKRTESAVTIDSTTSTSNQIQGVIVDEENYVVVGSSITMIQLLSDYCEAISEMPSFSQDWNSRVVELLKTFNSRCCQLILGAGALQLVGLKTISVRNLALAGRSLELVCRFIPMVHDEMDRVLPENRKSLLRYFKQVESEYRDHVNEIAAKLISVIAHYTTNCLGMWDVKGVIPSPEFQQICRHMLKFHNGLVGIMPRDQIEALFRQVHENFKANLREHVTGMGITPHDPLKYGYVTKDYMFYQQNVKNMESCRNLELESLNDIMFE