wanglab/gogpt-training-data huggingface dataset:
Protein: Multicilin (Multiciliate differentiation and DNA synthesis-associated cell cycle protein) (McIdas protein) (Protein Idas) (Q3UZ45)
Organism: Mus musculus (Mouse)
Function: Transcription regulator specifically required for multiciliate cell differentiation. Acts in a multiprotein complex containing E2F4 and E2F5 that binds and activates genes required for centriole biogenesis. Required for the deuterosome-mediated acentriolar pathway. Plays a role in mitotic cell cycle progression by promoting cell cycle exit. Modulates GMNN activity by reducing its affinity for CDT1.
Subcellular location: Nucleus {ECO:0000269|PubMed:21543332}. Note=Excluded from the nucleolus. {ECO:0000250|UniProtKB:D6RGH6}.
Interaction partners:
- Transcription factor E2F4
- Geminin coiled-coil domain-containing protein 1
- Transcription factor E2F5
- Cyclin-O
- Geminin
- Forkhead box protein J1
- DNA-binding protein RFX2
- Deuterosome assembly protein 1
Sequence:
MQACEGSAAGRRAFDSICPNRMLDLSRRTLGKPGKPERKFVPSWKSFSGCGGGSPVAVYEDPPDAEPAPLPALTTIDLQDLADCTSLLGTEASPSGDSSASQNPSLQTEEDFNLQNFRDAMDDLIADSSSLMSPPLTNSDFPFSPCDVSSFGSCLSPSLDPPALGSPDLPPPPTEQYWKEVADQNQRALGTALIENNQLHVTLTQKQEEIASLRERNVQLKELASRTRHLASVLDKLMITQSPAEPFQIKATTKRSLEELFCAAGQAGQGCAEVDAILRDISQRCEEALHNRDPKRPRLQPEPDSKDCSSRNLHGAFRGLRTDCSASSVNLSHSELEEGGSFSTPIRSHSTIRTLAFPQGKAFTIRTVTGGYKFRWVPS
Protein: Neuromedin-S (Q5H8A2)
Organism: Rattus norvegicus (Rat)
Function: Implicated in the regulation of circadian rhythms through autocrine and/or paracrine actions. Stimulates the contraction of rectum and elevation of blood pressure.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Neuromedin-U receptor 2
- Neuromedin-U receptor 1
- Neuromedin-U
Sequence:
MKHPFPQFPPILVIYCFCMLQIPSSGASPPLAGPPDGLDAVDPERLAHFLNQRETCSNQPKESRDVYKRFLFHYSRAWKSTHPVNSEFAPVHPLMRLAAKLPSRRMKRLPRLLHTDSRMATIDFPKKDPTTSLGRPFFLFRPRNGRYTDKVQ
Protein: Iron(III) enterobactin esterase (EC 3.1.1.108) (Enterochelin esterase) (Ferric enterobactin esterase) (P13039)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the hydrolysis of ferric enterobactin (Fe-Ent). Is responsible for the release of iron from ferric enterobactin. Also catalyzes the hydrolysis of iron-free enterobactin (Ent). Cleavage of ferric enterobactin results in a mixture of three hydrolysis products, 2,3-dihydroxybenzoylserine (DHBS), the linear dimer (DHBS)2 and the linear trimer (DHBS)3, while cleavage of iron-free enterobactin yields only the monomer. Hydrolysis of ferric enterobactin is less efficient than hydrolysis of unliganded enterobactin. It also cleaves the aluminum (III) complex at a rate similar to the ferric complex.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:1534808}.
Interaction partners:
- Enterobactin synthase component F
- Ferric enterobactin-binding periplasmic protein FepB
- Isochorismate synthase EntC
- Enterobactin biosynthesis protein YbdZ
- Ferrienterobactin receptor
- Enterobactin exporter EntS
- Enterobactin synthase component E
- Enterobactin synthase component B
- 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase
- Ferric enterobactin transport system permease protein FepG
Sequence:
MTALKVGSESWWQSKHGPEWQRLNDEMFEVTFWWRDPQGSEEYSTIKRVWVYITGVTDHHQNSQPQSMQRIAGTNVWQWTTQLNANWRGSYCFIPTERDDIFSVPSPDRLELREGWRKLLPQAIADPLNLQSWKGGRGHAVSALEMPQAPLQPGWDCPQAPEIPAKEIIWKSERLKKSRRVWIFTTGDATAEERPLAVLLDGEFWAQSMPVWPVLTSLTHRQQLPPAVYVLIDAIDTTHRAHELPCNADFWLAVQQELLPLVKAIAPFSDRADRTVVAGQSFGGLSALYAGLHWPERFGCVLSQSGSYWWPHRGGQQEGVLLEKLKAGEVSAEGLRIVLEAGIREPMIMRANQALYAQLHPIKESIFWRQVDGGHDALCWRGGLMQGLIDLWQPLFHDRS
Protein: Lividin-3 (Q2UXR2)
Organism: Odorrana livida (Green mountain frog) (Polypedates lividus)
Function: Antimicrobial peptide.
Subcellular location: Secreted {ECO:0000255, ECO:0000269|PubMed:16713657}.
Interaction partners:
Sequence:
MFTLKKSLLLLFFLGTISLSLCEEERDADEDEGEMTEEEVKRSVLGTVKDLLIGAGKSAAQSVLTALSCKLSNSC
Protein: GTPase Der (GTP-binding protein EngA) (P9WNL3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: GTPase that plays an essential role in the late steps of ribosome biogenesis.
Interaction partners:
- Cytidylate kinase
- Uncharacterized RNA pseudouridine synthase Rv1711
- Possible segregation and condensation protein ScpB
- GTPase HflX
- Segregation and condensation protein A
- Peptide chain release factor 1
- Uncharacterized protein Rv1708
- DNA primase
- Glycerol-3-phosphate dehydrogenase [NAD
- Glycerol-3-phosphate dehydrogenase [NAD
Sequence:
MTQDGTWVDESDWQLDDSEIAESGAAPVVAVVGRPNVGKSTLVNRILGRREAVVQDIPGVTRDRVCYDALWTGRRFVVQDTGGWEPNAKGLQRLVAEQASVAMRTADAVILVVDAGVGATAADEAAARILLRSGKPVFLAANKVDSEKGESDAAALWSLGLGEPHAISAMHGRGVADLLDGVLAALPEVGESASASGGPRRVALVGKPNVGKSSLLNKLAGDQRSVVHEAAGTTVDPVDSLIELGGDVWRFVDTAGLRRKVGQASGHEFYASVRTHAAIDSAEVAIVLIDASQPLTEQDLRVISMVIEAGRALVLAYNKWDLVDEDRRELLQREIDRELVQVRWAQRVNISAKTGRAVHKLVPAMEDALASWDTRIATGPLNTWLTEVTAATPPPVRGGKQPRILFATQATARPPTFVLFTTGFLEAGYRRFLERRLRETFGFDGSPIRVNVRVREKRAGKRR
Protein: Myosin heavy chain-like, isoform D (Q8INC1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPPLSPANEATAEIAASGEENAGPVESDRLEKEKFLARVLAAMNGGPRSGNLASNNSSGSSLNSTLSGSAPLARPPKPPASQARKQLRLLPKQREQSPVLSNGHTTRSTLSHQHTTNKYTLKSTGGNAGSSTLSSSLLGNKDSEIPYEVSLKLPLNPPTGADSDRHRLVNRSPSPALSVSSRCSTQSQSSISNFTSNSRLQTPPRRVFPQSYTRGSGGVDPYEMRQLESSPVVFDGNLSFVLGCQRQPVYQSMRASPSFEDPRTSSAYLSEKIQNFLKRTDHVQEEWTAMSRRTRRINSNSGRAGGSESRCTTPGSTCSGYDDYDTISLIERQRERNSMERCGSVGRTRSSQNILTKAFQLAKQLPHTPTSRGNSVARDRESSVATISLTTGDNDDDDDRTIREEDDELSELTVDLAEERSTAHIATERLEAETAERLKLEKELGDQTNKVKNLQETTEKLEMELICAKSDLNGISEDEDAENEDGVGGGVYKLKYERVARELEFTKRRLHTQHEHDLEQLVALKKHLEMKLSDAYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAECQSLQDAVRQERQAKERYGREKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEMTFGGGTEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEARRESQQRDEELEEVRGNGYKKIKALECQLETEHEERTLLLREKHELERRLSSMEDRDRVDRDAEEALNQKLRRDLRKYKALLKDAQTQLERLKADTPGKTLIRQLRNQLEDAESARSLAMKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIEENEEELGELMKKYSATVKQLNTEQINVSEAEFKLNEMEAERNNLKEQVAELQHRLDNVENLGDPSMAMMSKRLELRTKELESRLELEQATRARLEVQVNRHKEALEKLQNEVTQSKMREMQAQDVIKKSQKSLRDMREEFHAVSSREQESLTRRKDLEKKVEQMESEGAALKNDLRLALQRIADLQQAMEEEGEEELSESDESLSSVGSISDLEDRLRPVHVKRSSQQSLNGSIGGGGGSVVSSTRTVVFEKDDNSPRNNAK
Protein: Probable RNA-directed DNA polymerase from transposon BS (EC 2.7.7.49) (Reverse transcriptase) (Q95SX7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNPLKILIWNANGISRKAKDVELFAHNKKVDILLVTELRLKRGETVKIYGYAYYPAYRPSLNNNSVGGVAVFVRTTLRHFPQRVIETRHIQLSSVKVATGLGDLQFSAIYCSPSTRIEERHFTDIIRACGQRYLVGGDWNARHWLWGDTCNSPRGRELAEALSVTGAKILATGSPTRYPYVPSHTPSCIDFAVYHGIPDHLATITQSWDLDSDHLPLIISIETDSTHVNPSPRLVTKHTDLLAFSRQLESLISLNTTLNSGEEIEMAVDNLTESIHRAAAVSTSPVPRIGTTYGIVLTREARELLTQKRRLRRRAIRSQDPWDRLLWNRAAKQLRNVLRELRSNFFEQKLASMDYTVDAGYSLWKCTKSLKRQPFRQVPIRCPGGELAKNEEEQANCFANHLETRFTHFQFATTEQYQETLDSLETPLQMSLPIKPIRVEEIVEAIKSLPLKKSPGIDNVCNATLKALPVRAILYLALIYNAILRVQFFPKQWKMAAILMIHKPGKPEESPESYRPISLLSSLSKLWERLIANRLNDIMTERRILPDHQFGFRQGHSTVEQVHRLTKHILQAFDDKEYCNAVFIDMQQAFDRVWHDGLISKVKKLFPAPYYGVLKSYLEDRRFMVRVRNSYSIPRVMRAGVPQGSVLGPLLYSVFTADLPCPNAYHMADPRKALLATYADDIALLYSSNCCNEAARGLQEYLTTLAAWCKRWILKVNPQKTINPCFTLKTLSPVTAPIELEGVILDQPSQAKYLGITLDKRLTFGPHLKATTRRCYQRMQQLRWLLNRKSTMTLRAKRAVYVHCVAPIWLYGIQIWGIAAKSNYNRIQVLQNRAMRAITDCPYYVRGTTLHRDLNLHTVEEQISRHTSRYSDRLRRHHSILARRLLPARPLRRLKRKGFAKTLGQP
Protein: Epoxyqueuosine reductase (EC 1.17.99.6) (Queuosine biosynthesis protein QueG) (P39288)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00916}.
Interaction partners:
- S-adenosylmethionine:tRNA ribosyltransferase-isomerase
- NADPH-dependent 7-cyano-7-deazaguanine reductase
- 7-carboxy-7-deazaguanine synthase
- 7-cyano-7-deazaguanine synthase
- 6-carboxy-5,6,7,8-tetrahydropterin synthase
- Methionine synthase
- Queuine tRNA-ribosyltransferase
- GTP cyclohydrolase 1
Sequence:
MSEPLDLNQLAQKIKQWGLELGFQQVGITDTDLSESEPKLQAWLDKQYHGEMDWMARHGMLRARPHELLPGTLRVISVRMNYLPANAAFASTLKNPKLGYVSRYALGRDYHKLLRNRLKKLGEMIQQHCVSLNFRPFVDSAPILERPLAEKAGLGWTGKHSLILNREAGSFFFLGELLVDIPLPVDQPVEEGCGKCVACMTICPTGAIVEPYTVDARRCISYLTIELEGAIPEELRPLMGNRIYGCDDCQLICPWNRYSQLTTEEDFSPRKPLHAPELIELFAWSEEKFLKVTEGSAIRRIGHLRWLRNIAVALGNAPWDETILTALESRKGEHPLLDEHIAWAIAQQIERRNACIVEVQLPKKQRLVRVIEKGLPRDA
Protein: Probable serine protease HtrA1 (EC 3.4.21.107) (High-temperature requirement A protease) (O06291)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Essential protein that may act as a regulatory protease that is conditionally activated upon appropriate environmental triggers.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15952732}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Sec-independent protein translocase protein TatB
- Proteasome-associated ATPase
- Anti-sigma-E factor RseA
- Glycerol kinase
- CysO-cysteine peptidase
Sequence:
MDTRVDTDNAMPARFSAQIQNEDEVTSDQGNNGGPNGGGRLAPRPVFRPPVDPASRQAFGRPSGVQGSFVAERVRPQKYQDQSDFTPNDQLADPVLQEAFGRPFAGAESLQRHPIDAGALAAEKDGAGPDEPDDPWRDPAAAAALGTPALAAPAPHGALAGSGKLGVRDVLFGGKVSYLALGILVAIALVIGGIGGVIGRKTAEVVDAFTTSKVTLSTTGNAQEPAGRFTKVAAAVADSVVTIESVSDQEGMQGSGVIVDGRGYIVTNNHVISEAANNPSQFKTTVVFNDGKEVPANLVGRDPKTDLAVLKVDNVDNLTVARLGDSSKVRVGDEVLAVGAPLGLRSTVTQGIVSALHRPVPLSGEGSDTDTVIDAIQTDASINHGNSGGPLIDMDAQVIGINTAGKSLSDSASGLGFAIPVNEMKLVANSLIKDGKIVHPTLGISTRSVSNAIASGAQVANVKAGSPAQKGGILENDVIVKVGNRAVADSDEFVVAVRQLAIGQDAPIEVVREGRHVTLTVKPDPDST
Protein: 28S rRNA (cytosine-C(5))-methyltransferase (EC 2.1.1.-) (NOL1/NOP2/Sun domain family member 5) (Q9VDZ4)
Organism: Drosophila melanogaster (Fruit fly)
Function: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the C(5) position of a cytosine in 28S rRNA.
Interaction partners:
- tRNA
- tRNA
- GH27195p
- 60S ribosome subunit biogenesis protein NIP7 homolog
- Nucleolar complex protein 2
- Methionyl-tRNA formyltransferase, mitochondrial
- Probable rRNA-processing protein EBP2 homolog
- Ribosome biogenesis protein BOP1 homolog
- RRM domain-containing protein
- LD47540p
Sequence:
MSKKPHSIKVPTQYRATAKILKAALEQQKCIKTLIFAEKHARTRSLHTVLKKFSENRVALEKAIEETGLLRDNPSFDPSLAKILVTELLFGRKELNGESKPVQTVRSYKDRLLNSIRDFGVQRKEPNPRYVRINTNLYSLAEALDYLHKSDWRRKELPADASYADFLTAIKSLAENEFMTDLHVEGVLIFPAKWSNYWVRHPLVHSKRFILQNKATCLAAELLAPPSGATVLDMCAAPGMKTVHICNVMQNKGCIYSVEQDHVRYNTLCEITKDAGCDIVKPILGDALNLTPERFPDVEYILVDPSCSGSGMQNRMTVCDEPKEDKRLQKLQGLQIKILSHAMGAFPNVKRIAYCTCSLWKEENEQVVQRCLQLNPSFKLLSCKKALRNKWHNVGDKDYPNIGKNVLYCQPDSDLTDGIFLALFEKRREGEKD
Protein: Uncharacterized RNA-binding protein C23A1.09 (O42847)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- ATP-dependent RNA helicase fal1
- Protein mago nashi homolog
- Uncharacterized protein C19C7.01
- Nonsense-mediated mRNA decay protein 2
- Nuclear cap-binding protein subunit 2
- Nonsense-mediated mRNA decay protein 3
- ATP-dependent RNA helicase uap56
- Uncharacterized RNA-binding protein C106.12c
- RNA-binding protein with serine-rich domain 1 homolog
- Importin beta-like protein kap111
Sequence:
MRPAKSVEGYIIIVTGVHPEATEEQVEDLFADFGPVKNLHLNLDRRTGYVKGYALIEYATLEQAQKAVDEKNLSLLDEKLEVDFAFLEPPERAPRPSISTRSRSQSPEVQHRDRDVAMAEP
Protein: S-adenosylmethionine permease GAP4 (SAM permease) (Amino-acid permease GAP4) (Q59WB3)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Amino-acid permease involved in S-adenosylmethionine (SAM) transport and required for SAM-induced morphogenesis. GAP4 is also able to transport arginine and thialysine, and thus probably also lysine.
Subcellular location: Cell membrane {ECO:0000269|PubMed:21764911, ECO:0000269|PubMed:28028545}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MSYKGNDIEKQQSASTATGFNDKQIASTSEDATDRSHNIHGDTSSLDSRYTYETVDQEKNYFKRVYNSFKPMNLEEQGIDTSQLTPVERTIIASAKHPLARRLKARHLQMIAIGGSIGTGLFVGSGYALANGGPGAVLIGYVIVGYALLTVVNALGELSVQFPVSGSFNAFFSRFLEPSFGGTFGILYAASWCISLPSELIAAAMTIQYWNTEVNPAVWVAVFWVVIVVINLFGVKGYGEMEYFLSIIKVLAVVGFIILGICITCGVGDQGYIGGKYWHNPGAFNHGLKGVTSVFISAAFSFGGIELVALAASETANPRISLPAAVKSTFWRIFIFYILTAIIIGCLVPYTNDDLLNGTGIAASPFVIAVSQGGIRVVPHIMNAVVVIAVISVGNSSVYGCSRTLASLAVQGLLPKSMGYIDRGGRPLIAILFTSAIGLLGFLVVVDNEGDVFTWFFSICSLSSFFTWGAINVVHLRWRFALAAQGRSTDEIIFRSPLGTFGSWTGILVLILIVIGEVWVSIWPIGSPADVQQFWKNCLSLPLMIVMWAGFKTYHRSWNMLWVKLEDIDLDTGRREIDVELLKQELAEERQIIKSKPFVYRIYKFFF
Protein: L-lactate dehydrogenase (EC 1.1.1.27) (Q5U077)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MATLKEKLIAPVAEEEATVPNNKITVVGVGQVGMACAISILGKSLADELALVDVLEDKLKGEMMDLQHGSLFLQTPKIVADKDYSVTANSKIVVVTAGVRQQEGESRLNLVQRNVNVFKFIIPQIVKYSPDCIIIVVSNPVDILTYVTWKLSGLPKHRVIGSGCNLDSARFRYLMAEKLGIHPSSCHGWILGEHGDSSVAVWSGVNVAGVSLQELNPEMGTDNDSENWKEVHKMVVESAYEVIKLKGYTNWAIGLSVADLIESMLKNLSRIHPVSTMVKGMYGIENEVFLSLPCILNARGLTSVINQKLKDDEVAQLKKSADTLWDIQKDLKDL
Protein: Protein argonaute-2 (Q86B39)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MPGDSLTSSSFMPDGGAETSSSSQLGGSAHGAIGTKPDAGVQFQCPVRPNHGVEGRSILLRANHFAVRIPGGSVQHYQIDVFPDKCPRRVNREVIGCLISSFSKYFTNIRPVYDGKRNMYTREPLPIGTEPMNFEVTLPGDSAVERKFSVTMKWIGQVCLSALDDAMEGRVRQVPHEAVQSIDVILRHLPSLKYTPVGRSFFTPPGVMKPGMQMHQESKLGGGREVWFGFHQSVRPSQWKMMLNIDVSATAFYRAMPVIEFVAEVLELPVQALAERRALSDAQRVKFTKEIRGLKIEITHCGAVRRKYRVCNVTRRPAQTQTFPLQLETGQTIECTVAKYFFDKYRIQLKYPHLPCLQVGQEQKHTYLPPEVCDIVPGQRCLKKLTDVQTSTMIKATARSAPEREREICKLVSKAELSADPFAHEFGITINPAMTEVKGRVLSAPKLLYGGRHRATTALPNQGVWDMRGKQFHTGMEVRTWAIACFAQQSHVKENDLRMFTTQLQRISTDAGMPIIGTPMFCKYASGVEQVEPMFKYLKQTYSAIQLIVVVLPGKTPIYAEVKRVGDTVLGIATQCVQAKNAIRTTPQTLSNLCLKMNVKLGGVNSILLPNVRPRIFNEPVIFLGCDITHPAAGDTRKPSIAAVVGSMDAHPSRYAATVRVQQHRQEIITDLTYMVRELLVQFYRNTRFKPARIVVYRDGVSEGQLFNVLQYELRAIREACVMLESGYQPGITFIAVQKRHHTRLFAADKADQVGKAFNIPPGTTVDVGITHPTEFDFFLCSHAGIQGTSRPSHYHVLWDDNDLTADELQQLTYQMCHTYVRCTRSVSIPAPAYYAHLVAFRARYHLVDRDHGSGEEGSQPSGTSSEDTTLSSMAKAVQVHPDSNNVMYFA
Protein: RING finger protein 113 homolog (Q55G16)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Cell division cycle 5-like protein
- Activating signal cointegrator 1 complex subunit 3-like
- Pre-mRNA-processing factor 19
- PSP proline-rich domain-containing protein
- Cyclophilin-type peptidylprolyl cis-trans isomerase
- Pre-mRNA-splicing factor CWC26
- Initiation factor eIF-4 gamma middle domain-containing protein
- Putative pre-mRNA-splicing factor ATP-dependent RNA helicase DHX16
- Splicing factor 3A subunit 2
- Protein BUD31 homolog
Sequence:
MEKEESTNKNNENIQSENEINKIDNKSNTENPTIKCIFKKPNKQRNIRKRSDDLILNTSNNADEEDEDGNEEKDKKKLKSKINQYTTKQDKKNEFSYDSSGNAGSSINSAELSSTQYMNEEEEFKKEVVLSSSRNNNNNNNNNNNNNNDNISNSEGSGGSDNNDDGIYRGMKSYSTFVEKKSDLTYKGGGVKAGPMKTSTTFKLSNRIDHQPDVCKDYKQTGQCTFGDACKFLHDRSDYKSGWQIDKEYEEEQKQKRLNNINGIKNNNNDNKNNDDDKEQQQFPFACFICKKQYVDPVQTKCKHFFCEDCALTHNRKNKKCALCGEPTLGTFITPPKKILDQLMEISKSHFKNQS
Protein: Arginine decarboxylase 1, chloroplastic (ADC 1) (ADC-O) (ARGDC 1) (AtADC1) (EC 4.1.1.19) (Q9SI64)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for the biosynthesis of putrescine. Catalyzes the first step of polyamine (PA) biosynthesis to produce putrescine from arginine. Is a minor contributor to basal arginine decarboxylase (ADC) activity and putrescine biosynthesis. Accumulation of putrescine plays a positive role in freezing tolerance. Production of polyamines is essential for normal seed development. Controls PA homeostasis which is crucial for normal plant growth and development.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:28109885}. Cytoplasm, cytosol {ECO:0000269|PubMed:28109885}. Note=Localizes mainly in the chloroplast. {ECO:0000269|PubMed:28109885}.
Interaction partners:
- Agmatine deiminase
- Arginase 1, mitochondrial
- Arginase 2, chloroplastic/mitochondrial
- Spermidine synthase 2
- Spermine synthase
- Spermidine synthase 1
- Argininosuccinate lyase, chloroplastic
- Thermospermine synthase ACAULIS5
- S-adenosylmethionine decarboxylase proenzyme 1
- NO-associated protein 1, chloroplastic/mitochondrial
Sequence:
MPALAFVDTPIDTFSSIFTPSSVSTAVVDGSCHWSPSLSSSLYRIDGWGAPYFAANSSGNISVRPHGSNTLPHQDIDLMKVVKKVTDPSGLGLQLPLIVRFPDVLKNRLECLQSAFDYAIQSQGYDSHYQGVYPVKCNQDRFIIEDIVEFGSGFRFGLEAGSKPEILLAMSCLCKGNPEAFLVCNGFKDSEYISLALFGRKLELNTVIVLEQEEELDLVIDLSQKMNVRPVIGLRAKLRTKHSGHFGSTSGEKGKFGLTTVQILRVVRKLSQVGMLDCLQLLHFHIGSQIPSTALLSDGVAEAAQLYCELVRLGAHMKVIDIGGGLGIDYDGSKSGESDLSVAYSLEEYAAAVVASVRFVCDQKSVKHPVICSESGRAIVSHHSVLIFEAVSAGQQHETPTDHQFMLEGYSEEVRGDYENLYGAAMRGDRESCLLYVDQLKQRCVEGFKEGSLGIEQLAGVDGLCEWVIKAIGASDPVLTYHVNLSVFTSIPDFWGIDQLFPIVPIHKLDQRPAARGILSDLTCDSDGKINKFIGGESSLPLHEMDNNGCSGGRYYLGMFLGGAYEEALGGVHNLFGGPSVVRVLQSDGPHGFAVTRAVMGQSSADVLRAMQHEPELMFQTLKHRAEEPRNNNNKACGDKGNDKLVVASCLAKSFNNMPYLSMETSTNALTAAVNNLGVYYCDEAAAGGGGKGKDENWSYFG
Protein: Bidirectional sugar transporter SWEET17 (AtSWEET17) (Protein SUGARS WILL EVENTUALLY BE EXPORTED TRANSPORTERS 17) (Q84WN3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as a vacuolar hexose transporter. Regulates fructose (Fru) homeostasis in leaves and roots by exporting/importing Fru through the tonoplast regarding metabolic demand.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:23583552, ECO:0000269|PubMed:24381066, ECO:0000303|PubMed:25988582}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8L9J7}.
Interaction partners:
- Sucrose transport protein SUC4
- At2g39500/F12L6.16
- Monosaccharide-sensing protein 2
- Sugar transporter ERD6-like 7
- Sugar transporter ESL1
Sequence:
MAEASFYIGVIGNVISVLVFLSPVETFWKIVKRRSTEEYKSLPYICTLLGSSLWTYYGIVTPGEYLVSTVNGFGALVETIYVSLFLFYAPRHLKLKTVDVDAMLNVFFPIAAIVATRSAFEDEKMRSQSIGFISAGLNIIMYGSPLSAMKTVVTTKSVKYMPFWLSFFLFLNGAIWAVYALLQHDVFLLVPNGVGFVFGTMQLILYGIYRNAKPVGLSNGLSEIAQDEEEGLTSRVEPLLS
Protein: NADH-quinone oxidoreductase subunit N (EC 7.1.1.-) (NADH dehydrogenase I subunit N) (NDH-1 subunit N) (NUO14) (P0AFF0)
Organism: Escherichia coli (strain K12)
Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- NADH-quinone oxidoreductase subunit J
- NADH-quinone oxidoreductase subunit G
- NADH-quinone oxidoreductase subunit B
- NADH-quinone oxidoreductase subunit K
- NADH-quinone oxidoreductase subunit L
- NADH-quinone oxidoreductase subunit M
- NADH-quinone oxidoreductase subunit A
- NADH-quinone oxidoreductase subunit H
- NADH-quinone oxidoreductase subunit F
- NADH-quinone oxidoreductase subunit E
Sequence:
MTITPQNLIALLPLLIVGLTVVVVMLSIAWRRNHFLNATLSVIGLNAALVSLWFVGQAGAMDVTPLMRVDGFAMLYTGLVLLASLATCTFAYPWLEGYNDNKDEFYLLVLIAALGGILLANANHLASLFLGIELISLPLFGLVGYAFRQKRSLEASIKYTILSAAASSFLLFGMALVYAQSGDLSFVALGKNLGDGMLNEPLLLAGFGLMIVGLGFKLSLVPFHLWTPDVYQGAPAPVSTFLATASKIAIFGVVMRLFLYAPVGDSEAIRVVLAIIAFASIIFGNLMALSQTNIKRLLGYSSISHLGYLLVALIALQTGEMSMEAVGVYLAGYLFSSLGAFGVVSLMSSPYRGPDADSLFSYRGLFWHRPILAAVMTVMMLSLAGIPMTLGFIGKFYVLAVGVQAHLWWLVGAVVVGSAIGLYYYLRVAVSLYLHAPEQPGRDAPSNWQYSAGGIVVLISALLVLVLGVWPQPLISIVRLAMPLM
Protein: Threonine--tRNA ligase catalytic subunit (EC 6.1.1.3) (Threonyl-tRNA synthetase catalytic subunit) (ThrRS-cat) (Q97VW8)
Organism: Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus)
Function: Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also activates L-serine and transfers it to tRNA(Thr); unlike most archaea the editing function is found in a freestanding protein (ACQ980D1). In vitro when both subunits are present, or if the 2 subunits are fused, L-seryl-tRNA(Thr) is no longer produced, the 2 subunits edit incorrectly charged L-seryl-tRNA(Thr). Has no activity on correctly acylated L-seryl-tRNA(Ser) or L-threonyl-tRNA(Thr).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00184}.
Interaction partners:
- Valine--tRNA ligase
- Threonine--tRNA ligase editing subunit
- Probable translation initiation factor IF-2
- Arginine--tRNA ligase
- Isoleucine--tRNA ligase
- Serine--tRNA ligase
- Elongation factor 2
- Large ribosomal subunit protein uL11
- Large ribosomal subunit protein uL2
- Small ribosomal subunit protein uS12
Sequence:
MESYKPVWLKGAVILAINLIDKGYKPVAVGLGERDFYIDVKSDTSITLDEVKKAINENVLANVSIENNQIVYKGNKVSIIEDKVSISTNLNPKYFEILNISTHHPNPNEQYVRIRGVAFETEEQLKDYLSWLEKAEETDHRLIGEKLDLFSFHEEAGSGLVLFHPKGQTIRNELIAFMREINDSMGYQEVYTSHVFKTDIWKISGHYTLYRDKLIVFNMEGDEYGVKPMNCPAHILIYKSKPRTYRDLPIRFSEFGHVYRWEKKGELYGLLRVRGFVQDDGHIFLREDQLREEIKMLISKTVEVWHKFGFKDDDIKPYLSTRPDESIGSDELWEKATNALISALQESGLKFGIKEKEGAFYGPKIDFEIRDSLGRWWQLSTIQVDFNLPERFKLEYIDKDGIKKRPVMVHRAIYGSIDRFVAILLEHFKGKLPTWLSSVQVRVLPITDEVNEYAEKVLNDMRKRRIRAEIDYAGETLSKRIKNAYDQGVPYILIVGKKEASEGTVTVRARGNIEVRNVKFEKFLELLITEIAQRDVEQTTVKALK
Protein: Ethylene-responsive transcription factor ERF110 (Q70II3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probably acts as a transcriptional activator. Binds to the GCC-box pathogenesis-related promoter element. May be involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MSAMVSALTQVVSARSQTEAEGAHSSSSSAGHKRGWLGIDSAPIPSSFARVDSSHNPIEESMSKAFPEEAREKKRRYRGVRQRPWGKWAAEIRDPHRAARVWLGTFDTAEAAARAYDEAALRFRGNKAKLNFPEDVRILPPPPPLLRSPADTVANKAEEDLINYWSYTKLLQSSGQRSFLERGQEESSNIFEHSPMEQPLPPSSSGPSSSNFPAPSLPNT
Protein: Os05g0421900 protein (Q6L4Y3)
Organism: Oryza sativa subsp. japonica (Rice)
Interaction partners:
Sequence:
MVYISNAQDASKLIVTAKGGGGEADDAAASSAAVVLDLWRQPAKIPAPFVWPRADVALPPSSPPTGELDVPVVDLAAALRDAAGMRRAVAQVAAACASHGFFQVSGHGVPPSLARAALDGAAGFFRLPPAAKQRARRAPGTVTGYTAAHADRFVDNLPWKETLSFGHRHANAAGNNSSTVADYFSTLGDDFKHLGEVYQEYCEAMEEVTKAIMAVLGESLGVGGGYYREFFEDSSSIMRCNYYPPCPEPERTLGTGPHCDPSALTVLLQDGDVDGLQVLVAGAWRPVRPLPGAFVVNIGDTFMALTNGRYKSCLHRAVVHREQERRSLAFFLCPREDRVVRPPAGAGAGERRLYPDFTWADFMRFTQRHYRADTRTLDAFARWLRPPACSGAAPVVGPPTTATQAATV
Protein: HTH LytTR-type domain-containing protein (A0A0H2URK9)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Interaction partners:
Sequence:
MMKLRIEIDGNLEETEIVIKTPTLTDEIADLQRLLQESKAPRLTFYKGTGEYYLDLSEILFFETEGSKIYAHNQKEAYEVRLKLYELESILPRYFNRVSKSTIANIRQIYSVDKSFSGTGTISFYQTHKEVHVSRHYQSLLKENLRNMR
Protein: CCAAT-binding factor complex subunit php4 (O14318)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the transcription regulatory CCAAT-binding complex. Required for the reprogramming of the cell for iron use. Down-regulates pcl1, sdh4, and isa1 underlow-iron conditions.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19502236}. Nucleus {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:19502236}. Cytoplasm, cytoskeleton, spindle pole. Note=Iron starvation induces nuclear accumulation and iron induces relocalization to the cytoplasm, in association with exportin crm1. {ECO:0000269|PubMed:19502236}.
Interaction partners:
- Transcriptional activator hap5
- Transcriptional activator hap2
- Iron-sensing transcriptional repressor
- Transcriptional activator hap3
- Monothiol glutaredoxin-4
- Uncharacterized bolA-like protein C8C9.11
- Iron-sulfur assembly protein 1
- Fe
- Monothiol glutaredoxin-3
- Succinate dehydrogenase cytochrome b small subunit, mitochondrial
Sequence:
MESSKSPSEVEKSSSASPAPQKPMIRVSKQWVVPPRPKPGRKPALDALGRRKAPIKPRPGPTSALSVEEAKFRVREKQYQDTIGKLQKENNELLEQLEMLQAQLKNSTLDSPKEVEVNSEVVKPDSATTENENRYVNQYNYPVEPPCAKNAVYTEIPIELDPHAFLGDSAKRIRVDSDSKDAKSVPSENGRIRVSMSPQNEINFTPENPAVMEKIRKRGVCNSVEGCLYSGSPKSVKRVRESEETKVYAQLLIDLHKSSKSAPMLKAGPSIAFKLPTMEPNFNDVRPVTSISSSS