wanglab/gogpt-training-data huggingface dataset:
Protein: Penicillin-binding protein 1A (PBP-1a) (PBP1a) [Includes: Penicillin-insensitive transglycosylase (EC 2.4.99.28) (Peptidoglycan TGase); Penicillin-sensitive transpeptidase (EC 3.4.16.4) (DD-transpeptidase)] (P02918)
Organism: Escherichia coli (strain K12)
Function: Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits).
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:7006606}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
- Peptidoglycan D,D-transpeptidase MrdA
- Peptidoglycan glycosyltransferase MrdB
- Penicillin-binding protein activator LpoA
- D-alanyl-D-alanine carboxypeptidase DacA
- Penicillin-binding protein 1B
- Peptidoglycan D,D-transpeptidase FtsI
- D-alanyl-D-alanine carboxypeptidase DacC
- D-alanyl-D-alanine carboxypeptidase DacD
- D-alanyl-D-alanine carboxypeptidase DacB
- Probable peptidoglycan glycosyltransferase FtsW
Sequence:
MKFVKYFLILAVCCILLGAGSIYGLYRYIEPQLPDVATLKDVRLQIPMQIYSADGELIAQYGEKRRIPVTLDQIPPEMVKAFIATEDSRFYEHHGVDPVGIFRAASVALFSGHASQGASTITQQLARNFFLSPERTLMRKIKEVFLAIRIEQLLTKDEILELYLNKIYLGYRAYGVGAAAQVYFGKTVDQLTLNEMAVIAGLPKAPSTFNPLYSMDRAVARRNVVLSRMLDEGYITQQQFDQTRTEAINANYHAPEIAFSAPYLSEMVRQEMYNRYGESAYEDGYRIYTTITRKVQQAAQQAVRNNVLDYDMRHGYRGPANVLWKVGESAWDNNKITDTLKALPTYGPLLPAAVTSANPQQATAMLADGSTVALSMEGVRWARPYRSDTQQGPTPRKVTDVLQTGQQIWVRQVGDAWWLAQVPEVNSALVSINPQNGAVMALVGGFDFNQSKFNRATQALRQVGSNIKPFLYTAAMDKGLTLASMLNDVPISRWDASAGSDWQPKNSPPQYAGPIRLRQGLGQSKNVVMVRAMRAMGVDYAAEYLQRFGFPAQNIVHTESLALGSASFTPMQVARGYAVMANGGFLVDPWFISKIENDQGGVIFEAKPKVACPECDIPVIYGDTQKSNVLENNDVEDVAISREQQNVSVPMPQLEQANQALVAKTGAQEYAPHVINTPLAFLIKSALNTNIFGEPGWQGTGWRAGRDLQRRDIGGKTGTTNSSKDAWFSGYGPGVVTSVWIGFDDHRRNLGHTTASGAIKDQISGYEGGAKSAQPAWDAYMKAVLEGVPEQPLTPPPGIVTVNIDRSTGQLANGGNSREEYFIEGTQPTQQAVHEVGTTIIDNGEAQELF
Protein: Protein odd-skipped (P23803)
Organism: Drosophila melanogaster (Fruit fly)
Function: Pair-rule protein that determines both the size and polarity of even-numbered as well as odd-numbered parasegments during embryogenesis. DNA-binding transcription factor that acts primarily as a transcriptional repressor but can also function as a transcriptional activator, depending on the stage of development and spatial restrictions. May function redundantly with odd and drm in leg joint formation during the larval stages, acting downstream of Notch activation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Segmentation protein even-skipped
- Segmentation protein fushi tarazu
- Segmentation protein paired
Sequence:
MSSTSASPISNITVDDELNLSREQDFAEEDFIVIKEERETSLSPMLTPPHTPTEEPLRRVHPAISEEAVATQLHMRHMAHYQQQQQQQQQQQQHRLWLQMQQQQQQHQAPQQYPVYPTASADPVAVHQQLMNHWIRNAAIYQQQQQQQQHPHHHHHHGHPHHPHPHPHHVRPYPAGLHSLHAAVMGRHFGAMPTLKLGGAGGASGVPSGATGSSRPKKQFICKYCNRQFTKSYNLLIHERTHTDERPYSCDICGKAFRRQDHLRDHRYIHSKDKPFKCSDCGKGFCQSRTLAVHKVTHLEEGPHKCPICQRSFNQRANLKSHLQSHSEQSTKEVVVTTSPATSHSVPNQALSSPQPENLAQHLPVLDLSSSSSSSEKPKRMLGFTIDEIMSR
Protein: Branched-chain amino acid aminotransferase 5 / branched-chain amino acid transaminase 5 (BCAT5) (F4JXK3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus lamina {ECO:0000256|ARBA:ARBA00024186}.
Interaction partners:
Sequence:
MATSSRSERFPITPSTAATNRLTITPNSRVLKSPLTEEIMWKRLKDAGFDEQSIKNRDKAALIAYIAKLESEVYDYQHNMGLLLLEKNELSSQYEEIKASVDESDLTHMREKSAYVSALAEAKKREESLKKDVGIAKDLFIDFVLFFFSQLEKTLHEMRAECAETKVSAGSTMSEAHVMIEDALKKLADAEAKMRAAEALQAEANRYHRIAERKLKEVESREDDLTRRLASFKSECETKENEMVIERQTLNERRKSLQQEHERLLDAQVSLNQREDHIFARSQELAELEKGLDTAKTTFEEERKAFEDKKSNLEIALALCAKREEAVSERESSLLKKEQELLVAEEKIASKESELIQNVLANQEVILRKRKSDVEAELECKSKSVEVEIESKRRAWELREVDIKQREDLVGEKEHDLEVQSRALAEKEKDITEKSFNLDEKEKNLVATEEDINRKTTMLEDEKERLRKLDLELQQSLTSLEDKRKRVDSATQKLEALKSETSELSTLEMKLKEELDDLRAQKLEMLAEADRLKVEKAKFEAEWEHIDVKREELRKEAEYITRQREAFSMYLKDERDNIKEERDALRNQHKNDVESLNREREEFMNKMVEEHSEWLSKIQRERADFLLGIEMQKRELEYCIENKREELENSSRDREKAFEQEKKLEEERIQSLKEMAEKELEHVQVELKRLDAERLEIKLDRERREREWAELKDSVEELKVQREKLETQRHMLRAERDEIRHEIEELKKLENLKVALDDMSMAKMQLSNLERSWEKVSALKQKVVSRDDELDLQNGVSTVSNSEDGYNSSMERQNGLTPSSATPFSWIKRCTNLIFKTSPEKSTLMHHYEEEGGVPSEKLKLESSRREEKAYTEGLSIAVERLEAGRKRRGNTSGDETSEPSNNKKRKHDVTQKYSDEADTQSVISSPQNVPEDKHELPSSQTQTPSGMVVISETVKITRVTCETEVTNKVTTLDCSESPSEAGRKMGEETEDGDCNQTGINASETVIHNEAATEDICT
Protein: Robo2 (Q9QZI3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MTPLMFTLLLLFGFLRIRTDGXRLRQEDFPPKXVEQPSEVIVSKGKPNTPNWKQKGRPFPTIGKVQRMVKPGWDKTKDDSKVTQGCLLPSGSLFFLRIVHGRRSKPDEGTYVCVARNYLGEAVSRNASLEVALLRDDFRQNPTDVVVAAGEPAILECQPPRGHPEPTIYWKKDKVRIDEKEERISIRGGKLMISNTRKSDAGMYTCVGTNMVGERDSDPAELTVFERPTFLRRPINQVVLEDEPAEFRCQVQGDPQPTVRWKKDDADLPRGRYDIKDDYTLRIKKAISADEGTYVCIAENRVGKVEASATLTVRAPPQFVVRPRDQIVAQGRTVTFPCETKGNPQPAVFWQKEGSQNLLFPNQPQQPNSRCSVSPTGDLTITNIQRSDAGYYICQALTVAGSILAKAQLEVTDVLTDRPPPIILQGPINQTLAVDGTALLKCKATGPLPVISWLKEGFTFLGRDPRATIQDQGTLQIKNLRISDTGTYTCVATSSSGETSWSAVLDVTESGATISKNYDTNDLPGPPSKPQVTDVTKNSVTLSWQTGTPGVLPASAYIIEAFSQSVSNSWQTVANHVKTTLYTVRGLRPNTIYLFMVRAINPQGLSDPSPMSDPVRTQDISPPAQGVDHRQVQKELGDVTVRLHNPVVLTPTTVQVTWTVDRQPQFIQGYRVMYRQTSGLQASTVWQNLDAKVPTERSAVLVNLKKGVTYEIKVRPYFNEFQGMDSESKTIRTTEEAPSAPPQSVTVLTVGSHNSTSISVSWDPPPADHQNGIIQEYKIWCLGNETRFHINKTVDATIRSVVIGGLFPGIQYRVEVAASTSAGVGVKSEPQPIIIGGRNEVVITENNNSITEQITDVVKQPAFIAGIGGACWVILMGFSIWLYWRRKKRKGLSNYAVTFQRGDGGLMSNGSRPGLLNTGDPNYPWLADSWPATSLPVNNSNSGPNEIGNFGRGDVLPPVPGQGDKTATMLSDGAIYSSIDFTTKTTYNSSSQITQATPYATTQILHSNSIHELAVDLPDPQWKSSVQQKSDLMGFAYSLPDQNKGNNAYFTSLTTDWLRD
Protein: Ammonium transporter (G5EB09)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Cell membrane {ECO:0000256|RuleBase:RU362002}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU362002}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Histone H3
- Nitrate transporter
Sequence:
MASEGMAPFTPEYASYNWTGAPSDYSSLATNELGGNSRVENLNKWYQSGDQAYIIVASAMVMLMVPGLGFLYSGLARRKSALSMIWACMGSMCVVTFQWYFWGYSLAFSPTATNGYIGNLRNFGLMKVLADPSPGSPLVPNLLYAFYQMQFCAVTAAIIMGAVAERGRLLPAMVFTFVWATIVYCPIACWVWNVNGWAFNYGVLDYAGGGPVEICSGLSALAYSMVLGRRQERMMLNFRPHNVSLILLGTVFLWFGWLGFNGGSSFGANMRATMACWNTNLTAAFGAITWVILDWRLARKWSMVGWCSGTISGLVAATPASGFLPPWASVVLGIVTGIVCNYSTKVKYWIRIDDSMDVFAEHGVAGIVGLIFNAFFADDAIVGLDGVNTGSEMGGWLIHNWKQLYIQIAFIVAASAYSFVVSAIVAYAINAIPGLKLRASEEAELLGMDDDQLGEFAYDYVEVRRDYLAWTPQKHDQHADGHEVPAAARYGIGEHSEMMLDGEAPTGATNSRGSEVSGVQEINVKEESQRPAPPTDAEKAAQGL
Protein: Nociceptin receptor (Kappa-type 3 opioid receptor) (KOR-3) (Orphanin FQ receptor) (ROR-C) (XOR1) (P35370)
Organism: Rattus norvegicus (Rat)
Function: G-protein coupled opioid receptor that functions as receptor for the endogenous neuropeptide nociceptin. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Signaling via G proteins mediates inhibition of adenylate cyclase activity and calcium channel activity. Arrestins modulate signaling via G proteins and mediate the activation of alternative signaling pathways that lead to the activation of MAP kinases. Plays a role in modulating nociception and the perception of pain. Plays a role in the regulation of locomotor activity by the neuropeptide nociceptin.
Subcellular location: Cell membrane; Multi-pass membrane protein. Cytoplasmic vesicle {ECO:0000250}. Note=Ligand binding leads to receptor internalization into cytoplasmic vesicles, decreasing the amount of available receptor at the cell surface (By similarity). Internalization requires phosphorylation at Ser-360. Can recycle to the cell membrane. {ECO:0000250}.
Interaction partners:
- Prepronociceptin
- Proenkephalin-A
- Pro-opiomelanocortin
- Proenkephalin-B
- Prolactin
- Prolactin-6A1
Sequence:
MESLFPAPYWEVLYGSHFQGNLSLLNETVPHHLLLNASHSAFLPLGLKVTIVGLYLAVCIGGLLGNCLVMYVILRHTKMKTATNIYIFNLALADTLVLLTLPFQGTDILLGFWPFGNALCKTVIAIDYYNMFTSTFTLTAMSVDRYVAICHPIRALDVRTSSKAQAVNVAIWALASVVGVPVAIMGSAQVEDEEIECLVEIPAPQDYWGPVFAICIFLFSFIIPVLIISVCYSLMIRRLRGVRLLSGSREKDRNLRRITRLVLVVVAVFVGCWTPVQVFVLVQGLGVQPGSETAVAILRFCTALGYVNSCLNPILYAFLDENFKACFRKFCCASSLHREMQVSDRVRSIAKDVGLGCKTSETVPRPA
Protein: E3 ubiquitin-protein ligase MYLIP-A (EC 2.3.2.27) (Myosin regulatory light chain-interacting protein A) (MIR-A) (RING-type E3 ubiquitin transferase MYLIP-A) (Q6TEM9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of myosin regulatory light chain (MRLC) (By similarity). Regulates cell movements during gastrulation by acting downstream of fz7 to antagonize the frizzled-signaling pathway.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:14651927}.
Interaction partners:
- Stathmin domain-containing 1.
- Microtubule-associated tumor suppressor 1 homolog A
- Histone-lysine N-methyltransferase SETDB1-A
Sequence:
MLCHVTRPDAVVMEIEVDAKANGEDCLNKVCRKLGIIEVDYFGLQFSGSKGENLWLNLRNRISQQMDNLTPCRLRLRVKFFVEPHLILQEQTRHLFFMHVKEDLHRGHLRMCSEQAQELSALLAQAEFGDYNQNTAKYWYTELCGSEPNQTTINSIIAKHKALEGLSQASVEYQALQLVSSLEHYGVEWHWARDAEAQRLAIGVGPEGIAICRDDFSLVNRISYPIIQIATQSGKSVYLTVTKESSDSVVLLFKLISNRAASGLYRAITETHAFYRCDTVTNAVMMQYSRDFKGHLASLFLNENINLGKKYVFDIRRTSKEVYDYARRALYNAGIVDMMSRPGERTPSNRSPSREQEGALDCGGCQQSRLLQEKLQKLREALLCMLCCEEEIDAAFCPCGHMVCCQNCAAQLQSCPVCRSEVEHVQHVYLPTCTSLLNLTIGENSPEPIHRGMAAHTCTTNDYSTSEKIYQN
Protein: Anaphase-promoting complex subunit 2 (Q9W1E5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Shattered
- Anaphase-promoting complex subunit 5
- Cell division cycle protein 27 homolog
- Cell division cycle 16
- Anaphase-promoting complex subunit 4
- Anaphase-promoting complex subunit 10
- Anaphase promoting complex subunit 7, isoform A
- Cyclosome subunit 8
- Fizzy-related protein homolog
- Ubiquitin-conjugating enzyme E2 C
Sequence:
MCDFDALWADVLRIFPVLGGANAVSNDPVEENVFQNVRQHLMVLGSIDTFAAVVDLEIQSTIRNVLVPKFWKHIHDGLVSSKLQGWINDQALAIEALPDKNGLFTQFIDAINELHDSFQSLMQVKPRLIQLVGAETKPTAKTVKLMQEEGIKNCLRDCLLAQLPPNFSVVVGAFYWVHFKLFTKASNLALTTVDSDVFDELLCVGCNFEAEQCCCQRLTDMVNKTNMKLFEMNLIDRLTGSALTALIKLKIKEHISDTCMGIFDRSHLKQLETWLSDVIMSWLTNIFTEWKSKDSISDIEVPESVKSFKVKLTYFMYETFAQSVIGQFFSIIIDYPDSIPAIDDLKICMEKIDMRVYLTESLRNSLEARILHPGVNTMDILTGYVAAIKAIRHLDSTGVILEMVTAPIKDYLRKRNDTVRRVVTGLTEEGPTDLSEELAKGETIKECKDSGTDEFSNWENWQPDPFGIDASIMQYNSSRKMRSADIISMVVDIYGSKELFMTEYRNLMADRLLAQLDFNSEKEIRNLELLKIRFGESLLHSCEVMLKDVTDSKRINAHIHSDGDRTENQLFDISSLIVSAQFWPSFNKESLQLPEEIENEFKKYTKAYEAYKGNRTLNWRTVTGRVNIEIEIGDRTMEMVVSPILAVIIYHFQTKNEWTIEDLSSITKVPASALRRRLSFWQNHGLISETTPGIFTLLEKESEKSQYEDMSLAEADEEDLESAMASASDQREEELQVFWSYIVGMLTNLDSMPIDRIHQMLKLFASHSGGVEFTQDELKHFLQRKVREHKLIFSGGVYQLAK
Protein: T-complex protein 1 subunit gamma (TCP-1-gamma) (CCT-gamma) (Matricin) (mTRiC-P5) (P80318)
Organism: Mus musculus (Mouse)
Function: Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- T-complex protein 1 subunit eta
- T-complex protein 1 subunit alpha
- T-complex protein 1 subunit beta
- T-complex protein 1 subunit zeta
- T-complex protein 1 subunit theta
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit zeta-2
- Stress-induced-phosphoprotein 1
- Cell division cycle protein 20 homolog
Sequence:
MMGHRPVLVLSQNTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISRTQDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVDVNNREMMLSIINSSITTKVISRWSSLACNIALDAVKTVQFEENGRKEIDIKKYARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSLEYKKGESQTDIEITREEDFTRILQMEEEYIHQLCEDIIQLKPDVVITEKGISDLAQHYLMRANVTAIRRVRKTDNNRIARACGARIVSRPEELREDDVGTGAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLDPQLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQESCETWGVNGETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVSGHKKKGDDQNRQTGAPDAGQE
Protein: Basonuclin zinc finger protein homolog (Q1ZXU0)
Organism: Caenorhabditis elegans
Function: Probable transcription factor. Involved in motor neuron fate determination and maintenance, acting as a transcriptional repressor to counteract gene activation by transcription factor unc-3 in a subset of motor neurons. Required throughout development to repress transcription by unc-3, probably acting by binding to specific promoter elements. Represses expression of DA and DB motor neuron-specific effector genes, such as unc-129 and unc-53, in VA and VB motor neurons.
Subcellular location: Nucleus {ECO:0000269|PubMed:28056346}.
Interaction partners:
- T-box protein 12
- C2H2-type domain-containing protein
Sequence:
MDVRFPPYIFSMPHLIYNSWLSLNAPKLAQLQLQSIKLVGQDKSINQSELPVNSENISIRVETETNIDSLAKEEKLSEHVHDEKADKIEKTSEDNDTSTLLKLKRRVACDICSKSFCDKGALKIHTSAVHLREMHTCTVTGCGKQFSSRRSRNRHSSNNNPKLHMPESLTLTGSGLSMKTSLDTFWPTRFLLGKDHPLDLSLNLV
Protein: cAMP-dependent protein kinase catalytic subunit beta (PKA C-beta) (EC 2.7.11.11) (P68181)
Organism: Mus musculus (Mouse)
Function: Mediates cAMP-dependent signaling triggered by receptor binding to GPCRs. PKA activation regulates diverse cellular processes such as cell proliferation, the cell cycle, differentiation and regulation of microtubule dynamics, chromatin condensation and decondensation, nuclear envelope disassembly and reassembly, as well as regulation of intracellular transport mechanisms and ion flux. Regulates the abundance of compartmentalized pools of its regulatory subunits through phosphorylation of PJA2 which binds and ubiquitinates these subunits, leading to their subsequent proteolysis. Phosphorylates GPKOW which regulates its ability to bind RNA (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P22694}. Cell membrane {ECO:0000250|UniProtKB:P22694}. Membrane {ECO:0000250|UniProtKB:P22694}; Lipid-anchor {ECO:0000250|UniProtKB:P22694}. Nucleus {ECO:0000250|UniProtKB:P05131}. Note=Translocates into the nucleus (monomeric catalytic subunit). The inactive holoenzyme is found in the cytoplasm. {ECO:0000250|UniProtKB:P05131}.
Interaction partners:
- cAMP-dependent protein kinase type I-alpha regulatory subunit
- cAMP-dependent protein kinase type I-beta regulatory subunit
- Ezrin
- cAMP-dependent protein kinase type II-beta regulatory subunit
- Cyclic AMP-responsive element-binding protein 1
- A-kinase anchor protein 1, mitochondrial
- A-kinase anchor protein 5
- Adenylate cyclase type 5
- Glycogen synthase kinase-3 beta
- Phosphodiesterase
Sequence:
MGNTAIAKKGSEVESVKEFLAKAKEDFLRKWENPPPSNAGLEDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVSDIKTHKWFATTDWIAIYQRKVEAPFIPKFRGSGDTSNFDDYEEEEIRVSITEKCGKEFCEF
Protein: Synaptophysin-like 1 (Q66H18)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MASKAYLIRQRFSRLSQRMSTFQINLNPLKEPLGFIKILEWFASIFAFATCGGFKGKTEIQVNCLSAPGENKTITATFGYPFRLNQASFHSAPNVNVCKVNWEKHVLIGDYSSSAQFYVTFAVLVFLYCIAALLLYVGYTNLYRDSRKLPMIDFIVTLVATFLWLVSSSAWAKALTDIKVATGHRIVEELDPCKSEVSCYFVSVTSMGSLNVSVIFGFLNMILWGGNAWFVYKETSLHSPSNTSASHGQGGVPPTSGM
Protein: Nitroreductase NfnB (NR NfnB) (EC 1.-.-.-) (FMN-dependent NAD(P)H nitroreductase) (A0R6D0)
Organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis)
Function: Confers resistance to antitubercular drugs benzothiazinone (BTZ) and dinitrobenzamide (DNB). Inactivates BTZ and DNB by reducing an essential nitro group of these compounds to amino group or to hydroxyl amine, respectively, using NADH or NADPH as source of reducing equivalents; two electrons are transferred. Able to reduce the nitro group of bicyclic nitroimidazole PA-824, but not of quinone menadione, nitrofurazone, methyl-4-nitrobenzoate, 4-nitrobenzene methyl sulfonate or 4-nitroacetophenone.
Interaction partners:
- Transcriptional regulator, TetR family protein
- Decaprenylphosphoryl-beta-D-ribose oxidase
- nicotinamidase
- Decaprenylphosphoryl-2-keto-beta-D-erythro-pentose reductase
Sequence:
MSVPTLPTGPTVDLAQAAERLIKGRRAVRAFRPDEVPEETMRAVFELAGHAPSNSNTQPWHVEVVSGAARDRLAEALVTAHAEERVTVDFPYREGLFQGVLQERRADFGSRLYAALGIARDQTDLLQGYNTESLRFYGAPHVAMLFAPNNTEARIAGDMGIYAQTLMLAMTAHGIASCPQALLSFYADTVRAELGVENRKLLMGISFGYADDTAAVNGVRIPRAGLSETTRFSR
Protein: Phospholipid-transporting ATPase (EC 7.6.2.1) (Q2KG18)
Organism: Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Magnaporthe oryzae)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}. Membrane {ECO:0000256|RuleBase:RU362033}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU362033}.
Interaction partners:
Sequence:
MTIKSSGLKRLSLLGRAQNRGSSTEKKRASMGKGGESLQQSSEGDNEDQDQGEHDDQPEGPGPRTLYFNLPLPPEKLNDKGELVDTYPRNKIRTAKYTPLSFIPKNLWLQFHNIANIYFLFLVILAFFPIFGSVNPGLGAVPLIFIVTVTAIKDAIEDSRRTQSDIELNDSTVHRLCGWNNINVKEDNISLWRRFKKGNTKVFGGLWRFMETLWSKEARVKRREKAAQVADTPRISIDTRRTGRPESVISPHTHRTSFISAREDIPMTPVTSPLPRAEGQQNLEVVPQQEGLASGRPSSNFSFRGDSAELAHIKTDLINRTIPAEGKARFRRDKWKNLQVGDFVRIYSDDELPADIIILATSDPEGACYIETKNLDGETNLKFRQALKCGRNMKNSRDCERAQFIVESEPPQPNLYKYNGAIKWNQPIEGDASGSWREMTEPITIDNTLLRGCNLRNTDWVLGVVLFTGHHTKIMMNSGITPSKRPRIARELNYNVLYNFFILFGMCLLSAIVNGFAFGTSDNSIALFEYGSIGPTPAMNGFITFWAAIILFQNLVPISLFISLELVRLLQAFFIYSDVDMYYEPIDQPCIPKSWNISDDLGQIEYIFSDKTGTLTQNVMEFKKATINGQPYGEAYTEALAGLHRRMGIDVEKEAAEARVQIAADKEKALAALRKIHDNPYLHDDDLQFIAPDFVEDLMGANGQEQQQACERFMLALALCHTVIPERQPGEKATMLYKAQSPDEAALVSTARDMGFTVLSSNSDGVRLNVMGEEKYYPILNTIEFNSSRKRMSAIVRMTDGQTVLFCKGADSIIYSRLKKGEQKQLRTDTAQHLEMFAREGLRTLCIAERVLGEQEYQAWSKEYAVAAAAVENREDKMEAIADQIEQDLTLLGGTAIEDRLQDGVPQTIAVLAEAGIKLWVLTGDKVETAINIGFSCNLLNNDMELLNLKVDEDETGLTTREQFMAKLEAELDKYLKIFNLTGSDEDLAAARKIHEAPQATHAVVIDGFTLRWVLEDTLKQKFLLLCKQCKSVLCCRVSPAQKAAVCAMVKNGLDVMTLSIGDGANDVAMIQEADVGVGIAGVEGRQAVMSSDYAIAQFSFLQRLVLVHGRWSYRRLAESISNFFYKNLVWAMPLFLFQIYCDFDMTYLFDYTYILMFNLLFTSVPVILMGVLDQDVSDTVSLAVPQLYRRGIERLEWTQTKFWLYMLDGTYQGVMSFFIPYLVVVGSPFVTTNGLDVTDRVRFGAYIAHPAVVTINLYILINSYQWDWLIVLVVVLSDLFVFFWTGVFTSNTYSQWFYEAAPQIYAQPSFWAVFIITPVMCMFPRFSIKALQKVYWPYDVDIIREQVQQGKFDRLQPAPVGQTLPGGRSTAGSSPSLAKGNPGTFSGQDDERPIYPPSVATHTRTQTGSDGTNYTGHRMSMEQQQLEHQPLDQLTPMEHIPTRPSIDRARPSYDRVRASMDRVRPSYEASNDFTSAARLSRVESSRSRGGPPPSSHNLFAGRLRGLSIISAKSRHGPDSRGGQ
Protein: Complex 1 LYR protein (Q57WX7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRISCSCLNKSLVSTAIPSDIIERAGTNLPGIPHKYRVCRAYRQWLKLAVLCPHSLLCELNEHAQMNERFVIIVRQKFREGEELRDPEEIAVAVQSCERSLAMFRFLAADGARRRFPEAKPRLNLHKMGFMEMAKINYTQMAKEYWNTYIMRRW
Protein: Ceramide glucosyltransferase (EC 2.4.1.80) (GLCT-1) (Glucosylceramide synthase) (GCS) (Glycosylceramide synthase) (UDP-glucose ceramide glucosyltransferase) (UDP-glucose:N-acylsphingosine D-glucosyltransferase) (Q9R0E0)
Organism: Rattus norvegicus (Rat)
Function: Participates in the initial step of the glucosylceramide-based glycosphingolipid/GSL synthetic pathway at the cytosolic surface of the Golgi. Catalyzes the transfer of glucose from UDP-glucose to ceramide to produce glucosylceramide/GlcCer (such as beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine). Glucosylceramide is the core component of glycosphingolipids/GSLs, amphipathic molecules consisting of a ceramide lipid moiety embedded in the outer leaflet of the membrane, linked to one of hundreds of different externally oriented oligosaccharide structures (By similarity). Glycosphingolipids are essential components of membrane microdomains that mediate membrane trafficking and signal transduction (By similarity). They are implicated in many fundamental cellular processes, including growth, differentiation, migration, morphogenesis, cell-to-cell and cell-to-matrix interactions (By similarity). They are required for instance in the proper development and functioning of the nervous system. As an example of their role in signal transduction, they regulate the leptin receptor/LEPR in the leptin-mediated signaling pathway (By similarity). They also play an important role in the establishment of the skin barrier regulating keratinocyte differentiation and the proper assembly of the cornified envelope (By similarity). The biosynthesis of GSLs is also required for the proper intestinal endocytic uptake of nutritional lipids (By similarity). Catalyzes the synthesis of xylosylceramide/XylCer (such as beta-D-xylosyl-(1<->1')-N-acylsphing-4-enine) using UDP-Xyl as xylose donor (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:1532799, ECO:0000269|PubMed:9867864}; Multi-pass membrane protein {ECO:0000269|PubMed:9867864}.
Interaction partners:
- Sphingomyelin phosphodiesterase 2
- Ceramide kinase
- Non-lysosomal glucosylceramidase
- Acid ceramidase
- Ceramide synthase 2
- Glucosylceramidase
- Ceramide synthase 3
- 2-hydroxyacylsphingosine 1-beta-galactosyltransferase
- Ceramide synthase 5
- Ceramide synthase 4
Sequence:
MALLDLAQEGMALFGFVLFVVLWLMHFMSIIYTRLHLNKKATDKQPYSKLPGVSLLKPLKGVDPNLINNLETFFELDYPKYEVLLCVQDHDDPAIEVCKKLLGKYPNVDARLFIGGKKVGINPKINNLMPAYEVAKYDLIWICDSGIRVIPDTLTDMVNQMTERVGLVHGLPYVADRQGFAATLEQVYFGTSHPRSYISANVTGFKCVTGMSCLMRKDVLDQAGGLIAFAQYIAEDYFMAKAIADRGWKFSMSTQVAMQNSGSYSISQFQSRMIRWTKLRINMLPATIICEPISECFVASLIIGWAAHHVFRWDIMVFFMCHCLAWFIFDYIQLRGVQGGTLCFSKLDYAVAWFIRESMTIYIFLSALWDPTISWRAGRYRLRCGGTAEEILDV
Protein: Serine/threonine-protein kinase hal4 (EC 2.7.11.1) (Halotolerance protein 4) (Serine/threonine-protein kinase ppk10) (O14019)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Promotes K(+) uptake, by the potassium transporter trk1-trk2, which leads to the subsequent cellular resistance to toxic cations such as Na(+), Li(+) and Ca(2+).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Guanine nucleotide exchange factor subunit ric1
- Protein sat1
- Potassium transport protein 1
- Potassium transport protein 2
- GTP-binding protein ryh1
Sequence:
MGEKDKLHEISSKFASLGLGSLKSTPKARETTEPPPPSSQQPPSTPNGKEAASPSALKQNVRPSLNSVQQTPASIDAVASSSNVSLQSQQPLSKPVVSSKPNQTTAMPPPSNNPSRHVSSTSNKPAAVSPNPAAHHAELPSGSVPPSASVSRANSTATTTPHKAGVVSNPAAANVHVLSVAASPNPSTPSNGPAPVSTTATPSRNPVTRLQRIFSQNSVSRQNSRTGRGAAVANTEETNSTGGSETGGAANSSSTSNPSSAKWSRFTVYDDASHTHQLRPARRQEKLGKMLKDFLAGNSKKREEERIAKEAADAQHQLSLVQSWINGYGQEKLADKKDPAKVSASFVEKYGRCQEVIGRGAFGVVRIAHKVDPQNSGSETLYAVKEFRRKPAESQKKYTKRLTSEFCISSSLRHPNVIHTLDLIQDGKGDYCEVMELCSGGDLYTLIMAAGRLEPMEADCFFKQLMRGVDYLHDMGVAHRDLKPENLLLTVSGSLKITDFGNGECFRMAWEKEAHMTCGLCGSAPYIAPEEYTESEFDPRAVDVWACGVIYMAMRTGRHLWRVAKKSEDEYYSRYLMDRKNESGYEPIEMLERSRCRNTLYNILHPNPTYRLTAKQIMKSEWVRSITLCEAGNAGL
Protein: DNA-3-methyladenine glycosylase II (EC 3.2.2.21) (P96819)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Uncharacterized protein Rv0102
- Probable exodeoxyribonuclease III protein XthA
Sequence:
MRSIDVVVEAVVTFAGAAGFAHTLAPLRRGQQDPCFRVPGDGTIWRTSLLPTGPVTARISRAGRDAARCVAWGSGAEEFVDMAPAMLGAADDASDFVPLHPAVAAAHRRLPNLRLGRTGQVLEALIPAVIEQRVPGADAFRSWRLLVSKYGTQAPGPAPPGMRVPPSAEVWRHIPSWEFHRANVDPGRARAVVGCAQRAASLERLVSLPAARAAEALTSLPGVGVWTAAETTQRVFGDADAVSVGDYHIPKMIGWTLVGRPVDDAGMLELLEPMRPHRHRVVRLLEASGLAREPRRGPRLPVQNIRAL