wanglab/gogpt-training-data huggingface dataset:
Protein: Ribonuclease BN (RNase BN) (EC 3.1.-.-) (Ribonuclease Z homolog) (RNase Z homolog) (P0A8V0)
Organism: Escherichia coli (strain K12)
Function: Zinc phosphodiesterase, which has both exoribonuclease and endoribonuclease activities, depending on the nature of the substrate and of the added divalent cation, and on its 3'-terminal structure. Can process the 3' termini of both CCA-less and CCA-containing tRNA precursors. CCA-less tRNAs are cleaved endonucleolytically after the discriminator base, whereas residues following the CCA sequence can be removed exonucleolytically or endonucleolytically in CCA-containing molecules. Does not remove the CCA sequence. May also be involved in the degradation of mRNAs. In vitro, hydrolyzes bis(p-nitrophenyl)phosphate and thymidine-5'-p-nitrophenyl phosphate.
Interaction partners:
- Ribonuclease E
- Ribonuclease T
- Ribonuclease D
- Ribonuclease R
- Ribonuclease G
- Exoribonuclease 2
- Polyribonucleotide nucleotidyltransferase
- Oligoribonuclease
Sequence:
MELIFLGTSAGVPTRTRNVTAILLNLQHPTQSGLWLFDCGEGTQHQLLHTAFNPGKLDKIFISHLHGDHLFGLPGLLCSRSMSGIIQPLTIYGPQGIREFVETALRISGSWTDYPLEIVEIGAGEILDDGLRKVTAYPLEHPLECYGYRIEEHDKPGALNAQALKAAGVPPGPLFQELKAGKTITLEDGRQINGADYLAAPVPGKALAIFGDTGPCDAALDLAKGVDVMVHEATLDITMEAKANSRGHSSTRQAATLAREAGVGKLIITHVSSRYDDKGCQHLLRECRSIFPATELANDFTVFNV
Protein: [histone H4]-N-methyl-L-lysine20 N-methyltransferase KMT5B (EC 2.1.1.361) (EC 2.1.1.362) ([histone H4]-lysine20 N-methyltransferase KMT5B) (A0A0D9SF94)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
METNGAKIVSTRAWKKNEKLELLVGCIAELREADEGLLRAGENDFSIMYSTRKRSAQLWLGPAAFINHDCKPNCKFVPADGNAACVKVLRDIEPGDEVTCFYGEGFFGEKNEHCECHTCERKGEGAFRTRPREPALPPRPLDKYQLRETKRRLQQGLDSGSRQGLLGPRACVHPSPLRRDPFCAACQPLRLPACSARPDTSPLWLQWLPQPQPRVRPRKRRRPRPRRAPVLSTHHAARVSLHRWGGCGPHCRLRGEALVALGQPPHARWAPQQDWHWARRYGLPYVVRVDLRRLAPAPPATPAPAGTPGPILIPKQALAFAPFSPPKRLRLVVSHGSIDLDVGGEEL
Protein: Glycoprotein H (Q8JLV0)
Organism: Gallid alphaherpesvirus 2
Subcellular location: Virion membrane {ECO:0000256|ARBA:ARBA00004563}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004563}.
Interaction partners:
Sequence:
MGLPGSIVFLIMIHAFCAKKTPTNTLPSLLSLLGITDLPSLRLNILSLDGSANNQGSWVRDNTTFVYIGASSPANGVLFYMPTSHVQQMTFYKRPVSKLLASNNLIKFLNTGSYINHSFMTAMPPYRRNVQTPSDRSGLKLDDKDDAQPTGTNPPTELKNLKPIDVVNPEHRFILTSELTGTYVKHVCFVDPMDMLIPVDYAHIRTIIFGSDGAEVIMKIGITFASITISMKSAPPVELILSERARNISLIWPALKPYEPVDKFTRRPYLIYLLGPHMNASDMEIKSYINVIESVEESSNYDFQIAQTHAQLFIFAATPISDINDIYCFRVVTTRLFMSLVASVRNAFQSGYISFDEIIKTEANIKMITETLSTFALHSNPGTYFLLPGMHLRNENADIIKSLIRKTIINASKNTASLSILQHLYVLRSAYAFNISQESGNLGEHVSSISLELIIALHEESVRDTIAWNTSARHALYYAFASIFQRPPNEWDASRTARKALLFASSMCTEEHIVATELVIQEMYIKINVKNSPVHILDVYTPCVTALRMDISEHHHRLYAMSDVILHPVIEKYLENDSRGIDAEEELETKAELVITKLKTPLRRRLTIYASEVVTCSDAGILEATALLVLPISGLGSYVVTRQLGIRGIVYNVDGVDVNNQLYITYVRLPCTTTAGNIVPMVLPRPLGSDCPYCGCVLLRYSTNGNLRHTIYISSQDLQRELIAGGNSSIRYFNPTIAQIYGTSLLLYPNGTIVRILAFESERVTIISATYVATATAGASIAISIAIITVRMIINNFRYNYHRYKKLSLYDDL
Protein: Intraflagellar transport protein 122 homolog (WD repeat-containing protein 10) (Q6NWV3)
Organism: Mus musculus (Mouse)
Function: As a component of the IFT complex A (IFT-A), a complex required for retrograde ciliary transport and entry into cilia of G protein-coupled receptors (GPCRs), it is required in ciliogenesis and ciliary protein trafficking (By similarity). Involved in cilia formation during neuronal patterning. Acts as a negative regulator of Shh signaling. Required to recruit TULP3 to primary cilia.
Subcellular location: Cell projection, cilium {ECO:0000269|PubMed:21209331}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:21209331}. Note=Localizes to photoreceptor connecting cilia. {ECO:0000269|PubMed:21209331}.
Interaction partners:
- WD repeat-containing protein 35
- Intraflagellar transport protein 43 homolog
- WD repeat-containing protein 19
- Tetratricopeptide repeat protein 21B
- Intraflagellar transport protein 140 homolog
- Intraflagellar transport protein 88 homolog
- Intraflagellar transport protein 81 homolog
- Intraflagellar transport protein 52 homolog
- Intraflagellar transport protein 57 homolog
- Intraflagellar transport protein 46 homolog
Sequence:
MRAVLTWRDKAEQCIYDLAFKPDGTQLILAAGNRLLVYDTSDGTLLQPLKGHKDTVYCVAYAKDGKRFASGSADKSIIIWTSKLEGILKYTHNDSIQCVSYNPVTHQLASCSSSDFGLWSPEQKSVSKHKSSSKITCCSWTNDGQYLALGMANGIISIRNKNGEEKVKIERPGGSLSPIWSICWNPSREEHNDILAVADWGQKLSFYQLSGKQIGKDRPLNFDPCCISYFTKGEYILVGGSDKQVSLFTKDGVRLGTVGEQNSWVWTCRVKPDSNYVVVGCQDGTISFYQLIFSTVHGLYKDRYAYRDSMTDVIVQHLITEQKVRIKCRELVKKIAIYKNRLAIQLPEKILIYELYSEDSTDMHYRVKEKIVKKFECNLLVVCADHIILCQEKRLQCLSFSGVKEREWQMESLIRYIKVIGGPAGREGLLVGLKNGQILKIFVDNLFAIVLLKQATAVRCLDMSASRNKLAVVDENDTCLVYDIHTKELLFQEPNANSVAWNTQCEDMLCFSGGGYLNIKASTFPVHQQKLQGFVVGYNGSKIFCLHVFSMSAVEVPQSAPMYQYLDRKMFKEAYQIACLGVTDADWRELAMEALEGLEFETARKAFTRVQDLRYLELISSIEERKKRGETNNDLFLADVFSYQGKFHEAAKLYKRSGHENLALDMYTDLCMFEYAKDFLGSGDPKETKMLITKQADWARNINEPKAAVEMYISAGEHAKAIEISGSHGWVDMLIDIARKLDKAEREPLLMCACYFKKLDSPGYAAETYLKIGDLKSLVQLYVDTKRWDEAFALGEKHPEFKDDVYVPYAQWLAENDRFEEAQKAFHKAGRQGEAVRVLEQLTHNAVVESRFNDAAYYYWMLSMQCLDMAQDPAQKDAMLDKFHHFQHLAELYHGYQTIHRYTEEPFSFDLPETLFNISKFLLHSLTKATPLGISKVNTLFTLAKQSKALGAYKLARHAYDKLRGLQIPARIQKSIELGTLTIRSKPFHDSEELVPLCYRCSTNNPLLNNLGNVCINCRQPFIFSASSYEVLHLVEFYLEEGITDEEAVALIDLEAPRHKREGKWRETSSNNSQTLKLDETMDSIGEDDPFTAKLSFEQGSSEFVPVVVNRSVLRSMSRRDVLIKRWPPPLQWQYFRSLLPDASITMCPSCFQMFHSEDYELLVLQHACCPYCRRRIDDTGP
Protein: Large neutral amino acids transporter small subunit 4 (L-type amino acid transporter 4) (Solute carrier family 43 member 2) (Q8CGA3)
Organism: Mus musculus (Mouse)
Function: Uniporter that mediates the transport of the stereospecific L-phenylalanine, L-methionine and L-branched-chain amino acids, between the extracellular space and the cytoplasm and may control the transepithelial (re)absorption of neutral amino acid in kidney and small intestine. Transport activity is mediated through facilitated diffusion and is sodium ions-, chloride ions- and pH-independent.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15659399}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000269|PubMed:25480797, ECO:0000269|PubMed:30379325}. Note=Located at the basolateral membrane in the small intestine enterocytes, kidney proximal tubule, thick ascending limb and, to a minor extent, of distal convoluted tubule epithelial cells. {ECO:0000269|PubMed:25480797, ECO:0000269|PubMed:30379325}.
Interaction partners:
- Large neutral amino acids transporter small subunit 2
- Y+L amino acid transporter 2
- Large neutral amino acids transporter small subunit 1
- Amino acid transporter heavy chain SLC3A2
Sequence:
MAPTLATAHRRRWWMACTAVLENLLFSAVLLGWGSLLIMLKSEGFYSYLCTKPENVTNSTVGGSAEPEPEELSLVNGWLSCKAQDEILNLAFTVGSFLLSAITLPLGIIMDKYGPRKLRLLGSACFAVSCLLIAYGASNPDSLSVLIFIALALNGFGGMCMTFTSLTLPNMFGDLRSTFIALMIGSYASSAVTFPGIKLIYDAGASFIGILVVWAGCSGLVFFNCFFNWPLEPFPGPEDMDYSVKIKFSWLGFDHKITGKQFYKQVTTVGRRLSVGSSMRTAKEQAALQEGHKLCLSTVDLEVKCQPDAAAAPSFMHSVFSPLLVLSLVTMCVTQLRLIFYMGAMNSILEFLVRGDQKTVALYTSIFGALQLLCLLTAPVIGYIMDWKLKECEDTSEEPEEKEGTQGEKKQKRDRQIQKVTNAMRAFAFTNVLLVGFGVTCLIPNLPLQIFSFVLHTIVRGFIHSAVGGLYAAVYPSTQFGSLTGLQSLVSALFALLQQPLYLAMMGPLGGDPLWVNVGLLAMSMLGFCLPLYLICYRRQLERQLQQKREDSKLFLKINGSSNREAFV
Protein: Thioredoxin reductase (EC 1.8.1.9) (C8V4E8)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Thioredoxin
- Glutathione reductase
- cystathionine gamma-lyase
- Metallo-beta-lactamase family protein
- Mitochondrial peroxiredoxin
- 1-Cys peroxiredoxin
- Thioredoxin reductase, putative
- Glycine cleavage system P protein
- Molybdopterin synthase catalytic subunit
- Glutathione peroxidase
Sequence:
MVHSKVVIIGSGPAAHTAAIYLSRAELKPVLYEGMLANGTAAGGQLTTTTDVENFPGFPDGIGGSELMDAMRKQSIRFGTEVITETISRVDLSQRPFKLWTEWNDGPDNEPARTADAVIIATGANARRLNLPGEDVYWQNGISACAVCDGAVPIFRNKPLFVIGGGDSAAEEAIFLTKYGSSVTVLVRRDKLRASKAMASRLLANPKVTVRFNTVATEVLGEKKLNGLMTHLRVKNVLTGEEETLEANGLFYAVGHDPATALVKGQVELDEDGYIATKPGTSFTSVEGVFACGDVQDKRYRQAITSAGSGCIAALEAERFIGESESNEEIPPAHANPAL
Protein: Candida glabrata strain CBS138 chromosome C complete sequence (Q6FWT2)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Candida glabrata strain CBS138 chromosome L complete sequence
Sequence:
MASKAQDKVSTMAESEDFSTLIERFQFVKVLDSNPQTKVISLLGTIDGKDAIITAEKTHFVFDETVHKTASDENATPIFYHCENEYSCVNGIEELKQITNNDIYYWGLSVLRQSMDYNPTAKLNLIWPATPVHVKKYEQQNFHLIKETPEAYKRIVEPYIEEMHNKGRLAWVNNILYGEAEADRVVYKDYQEDNKKDSFIVLPDMKWDGNNLESLYLVAISYRDDIRSLRDLKMEDRDWLKNIYNKIRSIIPACYNYAVHPDELRVFIHYQPSYYHFHIHIVNIKHPGLGNGISTGKAILLDEIIDMLQYLGPEGYMRKTITYVIGENHDLWKRGLEEEVSKQLEADGIPKLPNIVEGF
Protein: Keratin, type I cytoskeletal 19 (Cytokeratin-19) (CK-19) (Keratin-19) (K19) (P08727)
Organism: Homo sapiens (Human)
Function: Involved in the organization of myofibers. Together with KRT8, helps to link the contractile apparatus to dystrophin at the costameres of striated muscle.
Interaction partners:
- Keratin, type I cytoskeletal 18
- Epithelial cell adhesion molecule
- Cell adhesion molecule CEACAM5
- Protein LIAT1
- Alpha-fetoprotein
- Desmoplakin
- Prominin-1
- Keratin, type II cytoskeletal 8
- Gamma-enolase
- Glypican-3
Sequence:
MTSYSYRQSSATSSFGGLGGGSVRFGPGVAFRAPSIHGGSGGRGVSVSSARFVSSSSSGAYGGGYGGVLTASDGLLAGNEKLTMQNLNDRLASYLDKVRALEAANGELEVKIRDWYQKQGPGPSRDYSHYYTTIQDLRDKILGATIENSRIVLQIDNARLAADDFRTKFETEQALRMSVEADINGLRRVLDELTLARTDLEMQIEGLKEELAYLKKNHEEEISTLRGQVGGQVSVEVDSAPGTDLAKILSDMRSQYEVMAEQNRKDAEAWFTSRTEELNREVAGHTEQLQMSRSEVTDLRRTLQGLEIELQSQLSMKAALEDTLAETEARFGAQLAHIQALISGIEAQLGDVRADSERQNQEYQRLMDIKSRLEQEIATYRSLLEGQEDHYNNLSASKVL
Protein: LD06023 isoform (LD06023p) (Zyxin, isoform A) (Q8T0F5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MESVAQQLRELSLPKGDTGSPLVCIGHGKVAKLVAKISNNQNASVKRRLDIPPKPPIKYNEMPQVPSSRQVLCSREPLYSQPLIGVEKTMRGHMPFRKYLSSEFGVADTQINRKTTLDNPAILEQQLEALAYHKLQMEKKGLLGVQAKPTQPLNSFTKPLSKTLSKSLIYSNLGSVRKEIETLELLTDETKISASTYSNVNETDNEKDELPPPPSPESAVSSSYSELRHATLEFNKPIDYLQNNQTTNPLQIYANQYAMQHDATGKSSSTYDSIYEPINPRPCVADTLPRESYNLHNSYVNDNNPNISHEYNISNSIEANQTLYIHGNARTTFYDVNSIHRNDKEGLKNYISIPTEPVQELENYGRCVKCNSRVLGESSGCTAMDQIYHIFCFTCTDCQINLQGKPFYALDGKPYCEYDYLQTLEKCSVCMEPILERILRATGKPYHPQCFTCVVCGKSLDGLLFTVDATNQNYCITDFHKKFAPRCCVCKQPIMPDPGQEETIRVVALDRSFHLECYKCEDCGLLLSSEAEGRGCYPLDDHVLCKSCNAKRVQALTNRMTSEH
Protein: Vacuolar protein sorting-associated protein 52 homolog (G5EFV8)
Organism: Caenorhabditis elegans
Function: Acts as component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN). The GARP complex facilitates tethering as well as SNARE complex assembly at the Golgi. Plays a role in the trafficking of cargo to dense-core vesicles, probably through association with the EARP-interacting protein eipr-1. Important for neuronal function.
Subcellular location: Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:21613545}. Perikaryon {ECO:0000269|PubMed:27191843}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:27191843}. Note=Co-localizes with rab-2 to perinuclear puncta in the perikaryon. Co-localizes with the small GTPases rab-6.1 and rab-6.2 at Golgi structures (PubMed:21613545). {ECO:0000269|PubMed:21613545, ECO:0000269|PubMed:27191843}.
Interaction partners:
- Vacuolar protein sorting-associated protein 51 homolog
- Vacuolar protein sorting-associated protein 54
- Vacuolar protein sorting-associated protein 53 homolog
- Vps54_N domain-containing protein
- Putative syntaxin 6
- EARP-interacting protein 1
- t-SNARE coiled-coil homology domain-containing protein
- Exocyst complex component 3
- Exocyst complex component 1
- Ras-related protein rab-6.2
Sequence:
MPRTRVNLQKSEANDRSFTISSLEFCLSQLRKADPNLVKKAIASGDGLTESKNDVSTRLSEAHRYSVQQCLDNSEQLAQLHNQLVHCDNVFERLQATLYSFQDNLGSIGQDMKNLQLQSHHIHQELENRQKVRVELSQFVDDIAVSQTMMKTINDTDANDRGFLEALHELHHKITLILQRGNGDAVAVNDTMPILEGLKLKAVVKVREWLLQKMFQFRKPLSNYQVFQHQLLKCRFFYEFLLHHDLISAKELQDEYIDTISKMFFTYFKAYATRLFKLAMKDVATKEDALGSIDFAKPAGLGAIFSSKQHVVRNKATVFSIGQRHQILSDDFLGALIVPHAATQNHQSYQFEALFRSIQLAFVDHYSHEYLFITDFFLVSNDEAIELHNKAMARAMSVVLKSCEEQIALSWDAISLHLCICLCDKFTEVLAEREVPEVSDYWNTVTSFLWTRLNLVMSQHYESVKSVDLKKLMHSGSLDARPHFIVRRYAELTSAHLMIAKASGKEMGAKMEAVLENSEDSIEQLLTRMSAMQQTQKNKHVFLINNYDLILSIIDNEESKHTKIYAIVHELEQKSIDDFVEEMLEPHIGYMIKFVNECESLIVQGHTQLLVRYNDKVGTVVANFNAKWRPAVDSINSECIQLFTNFSLGTTILQTIFTKYVQYINRFTKILSHDVFAKNPVCSQLVNVHQVMLEIKRFKPAY
Protein: Disco-interacting protein 2 (Q9W0S9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for precise axonal bifurcation in mushroom body neurons by suppressing ectopic bifurcation and regulating the guidance of sister axons. Acts downstream of the serine/threonine-protein kinase Bsk to modulate the direction of axon projection. May play a role in fatty acid metabolism.
Subcellular location: Cell membrane {ECO:0000269|PubMed:27908785, ECO:0000269|PubMed:28396149}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- DNA methyltransferase 1-associated protein 1
Sequence:
MEHTASLPGYVREKLAELDLELSEGDITQKGYEKKRAKLLQPFLKKPEGDKVKSTPPPPYYNVKNANNSTNHGNINNDGVIVSSEGYSYVTEVPSLSSSQQRHSKKIDFHQQAAMSLSSAPQSGNAGAPGYENMRPQGGAVGDPGYQNTREPSAFQNQQSTNNSQHRQRRTQRKVTHNEKRYHSEVRQEAVQQALAALKGRPKPSLPMPSKRTSVLNRSPGCNDELDSSTDDESIPEETISPDKEYNYPRDHISNSILPPEPIIKPPIRESSMGSQQHARTDVKQNQITNQKYTAPNSAPERRPPQNLPPLPTSEPLSSDYPPIAYKRENDFSDKAFKQKQYNAPDITQFNNAHRAADRVTRYVNVSQNELNETDANGKWKVSAKIQQLLNTLKRPKRRPLPEFYEDNDIELEIAANTKDPNAPKPEGSTMTPVQGEQLSIPAGLPRTLECALQRYGTNSFKSPMATVLDPNGKVTTTLTYGKLLSRAQKIAHALSTKIFSKGPEQVTLKPGDRVALVYPNNDPLSFITAWYGCMFRGLVPLPIELPLSSSDTPPQQVGFLLSSCGITVALTSEACLKGLPKSTTTGEIAKLKGWPRLQWFVTEHLPKPPKEFNVGNLRADDSAAAYIEYTTDKEGSVMGVTVTRAAMINHCRALTMACHYTEGETIVCVLDFKREVGLWHSVLTSVLNGMHVIFIPYALMKLRPSSWMQLITKHRASCCLVKSRDLHWGLLATKDHKDISLSSLRMLLVADGANPWSLSSCDQFLSVFQAKGLRSDAICPCASSSEVFTVSLRRPGRGSCGFSPSATGRGVLSMAALSHGVVRVDSEDSLTSLTLQDCGQVMPAAQMVVVRSEGPPVLCKTDQVGEICVTSGSTSASYFGLDGMTNSTFKVQPLLEELEQPKDGNGTVNIISKPIGEDFYVRSGLLGFLGPGGLVFVCGSRDGLMTVTGRKHNADDIIATVLAVEPMRFIYRGRIAVFSIKVLRDERVCVIAEQRPDCSEEESFQWMSRVLQAVDSIHQVGIYCLALVPPNHLPKTPLGGIHLCEARRRFLEGSLHPANVLMCPHTCVTNLPKPRELHQGVQTAAKLSSSSGCGITDTGVGPASVMVGNLVQGNRLAEAHGRDVGLAEDCERKPQLITGVLRWRANTSPDHIIFTLLNSKGAIAKTLTCSELHKRAEKIAALLQERGRIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPITIRPPHPQNLNTTLPTVRMIVDVSKSGIVLSIQPIIKLLKSREAATSIDPKTWPPILDIDDNPKRKYAGIATVSFDSSAYLDFSVSTCGRLSGVNITHRSLSSLCASLKLACELYPSRHVALCLDPYCGLGFVMWTLIGVYSGHHSILIAPYEVEANPSLWLSTLSQHRVRDTFCSYGVIELCTKALSNSIPSLKQRNIDLRCVRTCVVVAEERPRVQLTQQFCKLFQALGLNTRCVSTSFGCRVNPAICVQGASSAESAQVYVDMRALRNNRVALVERGAPNSLCVIESGKLLPGVKVIIANPETKGHCGDSHLGEIWVQAPHNANGYFTIYGDETDYNDHFNAKLVTGATSELYARTGYLGFLRRTECSQSASLLDETTPSVASRDSDTESLNSISQLQLNFSNVSLGGNSEHSLVGGASNANDQELHDAVYVVGAVDEVISLRGMNYHPIDIENSVMRCHKKIAECAVFTWTNLLVVVVELDGNESEALDLVPLVTNTVLEDHQLIVGVVVVVDPGVVPINSRGEKQRMHLRDGFLADQLDPIYVAYNM
Protein: Terminase, large subunit (DNA-packaging protein) (Gene product 17) (gp17) [Includes: ATPase (EC 3.6.4.-); Endonuclease (EC 3.1.21.-)] (P17312)
Organism: Enterobacteria phage T4 (Bacteriophage T4)
Function: The terminase large subunit acts as an ATP driven molecular motor necessary for viral DNA translocation into empty capsids and as an endonuclease that cuts the viral genome to initiate and to end a packaging reaction. The terminase lies at a unique vertex of the procapsid and is composed of two subunits, a small terminase subunit involved in viral DNA recognition (packaging sequence), and a large terminase subunit possessing endonucleolytic and ATPase activities. Both terminase subunits heterooligomerize and are docked on the portal protein to form the packaging machine. The terminase large subunit exhibits endonuclease activity and cleaves the viral genome concatemer once the capsid is full (headful packaging). Once the capsid is packaged with the DNA, the terminase complex is substituted by the tail.
Interaction partners:
Sequence:
MEQPINVLNDFHPLNEAGKILIKHPSLAERKDEDGIHWIKSQWDGKWYPEKFSDYLRLHKIVKIPNNSDKPELFQTYKDKNNKRSRYMGLPNLKRANIKTQWTREMVEEWKKCRDDIVYFAETYCAITHIDYGVIKVQLRDYQRDMLKIMSSKRMTVCNLSRQLGKTTVVAIFLAHFVCFNKDKAVGILAHKGSMSAEVLDRTKQAIELLPDFLQPGIVEWNKGSIELDNGSSIGAYASSPDAVRGNSFAMIYIDECAFIPNFHDSWLAIQPVISSGRRSKIIITTTPNGLNHFYDIWTAAVEGKSGFEPYTAIWNSVKERLYNDEDIFDDGWQWSIQTINGSSLAQFRQEHTAAFEGTSGTLISGMKLAVMDFIEVTPDDHGFHQFKKPEPDRKYIATLDCSEGRGQDYHALHIIDVTDDVWEQVGVLHSNTISHLILPDIVMRYLVEYNECPVYIELNSTGVSVAKSLYMDLEYEGVICDSYTDLGMKQTKRTKAVGCSTLKDLIEKDKLIIHHRATIQEFRTFSEKGVSWAAEEGYHDDLVMSLVIFGWLSTQSKFIDYADKDDMRLASEVFSKELQDMSDDYAPVIFVDSVHSAEYVPVSHGMSMV
Protein: Nucleoporin_N domain-containing protein (Q95Y15)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Nuclear pore protein
- Nucleoporin NUP35
- Nuclear Pore complex Protein
- Nsp1_C domain-containing protein
- Nuclear pore complex protein 15
- Nucleoporin SEH1
- Protein SEC13 homolog
- WD_REPEATS_REGION domain-containing protein
- Nuclear pore complex protein Nup85
- Nuclear pore complex protein 5
Sequence:
MSVSFMELGSADSAEAAANKVAHHVEQMMETSDFFDRLTQHGTTPVSGLGEKFYVKGAPEFVSTRRIPIPGELQMQMSNIHSEFSMGFFTQISRVWVVIDNNLYMWNYETNDDLAFFDSSDAAILKVSLVNIKPGVFEPEIQYGLVVGTISDICLYPVFDFVENGASSISIDSKRCFKIALDGATVNDISYTSNGRVFYTADDQLFEFVYEKQNGWFGSTNHKCRGVNQTASILGTLISLPFFGSSKEPLDQITIDKSRNIMYLLGRAGTVSVWDLGADGAACAKFLSVPISKIAHEAHILTQFGHDETSFHSITSIKALEASQSAALNLVATTAKGVRLYFSVSTGPQSTMAMFNNSGTPNERNRPQTSVRPQCLRVAHVRFAPGVTPASIYGDGPNGVSVVYADESICAMATANRNTIFAFSNFFYPSSQFFVESTTECDISGHVWEIETVSRCKVKSRPPPRHLVDRVHPHSYFRSQLESGNQKLLVCSNEGVFEFTHVNAVDALREALFDGGVEGNATLQLWQKLGSTEMLCLAFRILTSDAPIDERIRGKAEQILYSLKEAPEIVENEQQRMLDQSTTTSWSPNDSSMAEWRHRMKTPLLSSTPRTDGRNGNAGGAPPQAHFSSPFSPMLDMSMASGHHNGNMRMSPSRRHDALFYYFSRLVAPVWNDTICEVLNGKQLTITFEPESIQSLKEEIQKLARLMDDYRLVPMMEFNGYSSNMTDRLNHEATSLERHSLIGLRKLIDATLETLSLWLLAYEYNLTAISSGMNPQLLPNFSSRKLAHLVSDGSNLNAELIRAMIKYFLGDEAGTKILSESLRQLCPNLYSEDDACVTFAMEQLEAARKQGPGAARRRLVQSAVEMFKQSIGKVVLASTCQQLAESVEDYEPIVELCLLRAAKDDPKQLALLAYKHGRSGSDAEMLGAEKKREDCYRVITDVLDKLEDEATSEVPRDTAVNRDLMINAVLNSDDQLAHAAVFRWLLTKNKTNVILQSKSPFIEFFLVQEINAGRGQKYFDLLWRFYEKSGNYDKAARLLSKLAENDNWKMGLTQRCAYLSHAILCAQSCKDSTVTTNIDELRDRLDVANVQMRIKDALGCSASASARNQEFVRKLDGPILSLQELLLQYVVPFKLHKIKLSLLHCAGMYVEKHIFETWEDIIQDEFTTAQDEGTLCEQLSNTIGELFSVYRDTKYFPREFVIRRILEIGSGGVIGESVQQQRHILPPSFYPLLCKKINLSNCEFLRTASDEFRAGGDAWWTHNSRGQEYITKVVLKMARTVVRELENMPTAHSRRSTARDCLTHILPFIRRSCDVSASLSLQNLGTELTALQNRLSEFSN
Protein: Probable transcription repressor protein RGM1 (Q00453)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Nucleus.
Interaction partners:
Sequence:
MRGKQPKRNKDNASVKRNYRCVGYPDCNMSFNRTEHLARHIRKHTGEKPFQCNICLKFFSRIDNLRQHQSSVHSDVDLMSLRRLQQSANSTANDPNATRMFPQLRPYGIVVQPAPVPYNLPISTPASPQDTISLYAPPYFPHPMPSAPIPLPHQPPPLPIYSYMQPLFLNHTPIQNHNIVELPPDSSDTPASPSKVQSFDQAKDASPNAKK
Protein: Cysteine protease (EC 3.4.22.-) (Q4Q4N3)
Organism: Leishmania major
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU363115}.
Interaction partners:
- Autophagy-related protein
- Autophagy-related protein
- Autophagy-related protein
- Autophagy-related protein
- Autophagy-related protein
- Autophagy-related protein
- Autophagy-related protein
- Autophagy-related protein
- Protein kinase domain-containing protein
- Protein kinase domain-containing protein
Sequence:
MGTNAKVAEKTPCVDSGSLFKWWLNPSKIFRTPNRKLKNTTPVVVVGSGSHSGDGTTEFVKVATKKLLYFSYRNCFPPLPSGSTTDTHWGCLVRTTQMLVGTCLLRYHCKGAYVLPEADNAELKERISRLFMDVPSAPLGIHKAEDEAHKNSVKYASMLSPTEAGMAIAAALIAFRAQGGDVPFTFCCESRHIDEPAVMAKLLEGQHVVLIIPVVLGIAPMSDQYELVMLKILDVKACCGIAGGFKQASLYMFGHQGRSVFFMDPHYVQNAYTSSRTVGTLEGSRGELRARRFDPCMVLGFYLHTPEDYRVFAEELAVANSLVVFPLISFGRRPREGTTLSEDRVVSVAESAESITLHEKEKPQRSRNPLAADGEHARSSNSISSPPS
Protein: Dead end protein 1 (Q7T1H5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: RNA-binding factor that positively regulates gene expression by prohibiting miRNA-mediated gene suppression. Relieves miRNA repression in germline cells. Prohibits the function of several miRNAs by blocking the accessibility of target mRNAs (By similarity). Sequence-specific RNA-binding factor that binds to U-rich regions (URRs) in the 3'untranslated region (3'-UTR) of several mRNAs (By similarity). Does not bind to miRNAs (By similarity). Germline-specific protein required for the primordial germ cell (PGC) survival and migration during early embryonic development.
Subcellular location: Nucleus. Cytoplasm. Note=Perinuclear germ granules, also called germ plasm or chromatoid body.
Interaction partners:
- Nanos homolog 3
- Deleted in azoospermia-like
- Nanos homolog 1
- Tudor domain-containing protein 7A
- RNA binding protein
- Piwi-like protein 1
- DEAD
- Nanos homolog 1
- Regulator of G protein-signaling 14a.
- Piwi-like protein 2
Sequence:
MVGDMDAQQQELQQILNPQKLKSLQEWMQRNSITLTQVNGQRKYGGPPPGWQGPAPGSGCEVFISQIPNDVYEDRLIPLFQSIGTIYEFRLMMNFSGQTRGFAYAKYGDPLTASAAVTTLHQYRLPEGGCLTVRRSTEKRQLRLGDLPVSMNESKLLMVLQMLSDGVEDVLLKPPGPKGKEVVALVNYTSHYAASMAKKVLVEAFRNRYGISITVRWTSFSKSKRVEDTPQEDSCVTPLVLKPLSKPSLLHYDVPAHQSLLPLFRAVGGPTTSEQRDEMIPQPTIMSRNELIPQSSIRQRDEMVPQLPIRPRDGMAPQSPISLDAVSHLQWMCEVNRLGSPQYEVHFHHAAPDGFLYFAFKVLIPGLPLPLYGFVQILPGTSARAMKSEVYRAAAEQVIQTLCRVSNLRPF
Protein: Cell wall mannoprotein PIR1 (Protein with internal repeats 1) (Q59SF7)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Component of the outer cell wall layer required for stability of the cell wall and specifically for cell wall rigidity.
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:10672182, ECO:0000269|PubMed:10802178, ECO:0000269|PubMed:15302828, ECO:0000269|PubMed:15470096, ECO:0000269|PubMed:18227255, ECO:0000269|PubMed:20641015}. Note=Covalently attached to the cell wall.
Interaction partners:
Sequence:
MKYSTLVSIAAFISTSLAATVPDEHYSTLSPSAKIPSGASTDFSGTFGIQVVTVESASALSTDTATSTLTRNDNKKEATPVAQITDGQVQHQTTGGVSAIKQISDGQVQHQTNAAQPIAQISDGQIQHQTTAKATATPVQQINDGQIQHQTTVQPVAQISDGQIQHQTAKATATPVQQIGDGQIQHQTTVQPVAQISDGQIQHQTVKASATPVQQIGDGQIQHQTTAAAATTASAVKQINDGQIQHQTTTAENVAKAQSDGQAIATGSPSSNSTLSDDDDLSSTIPKACSSANNLEMTLHDSVLKDTHERWGAIVANHQFQFDGPIPQAGTIYSAGWSIKDGYLYLGDSNIFYQCLSGDFYNLYDENVAKQCSAVKLSVIEFVNC
Protein: Meiotic recombination protein spo-11 (EC 5.6.2.2) (Q22236)
Organism: Caenorhabditis elegans
Function: Required for meiotic recombination. Mediates DNA cleavage that forms the double-strand breaks (DSB) that initiate meiotic recombination.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- MutS protein homolog him-14
- DNA repair protein RAD51 homolog
- Crossover junction endonuclease MUS81
- Exonuclease 1
- MutS protein homolog 5
- DNA repair and recombination protein RAD54-like
- Zip homologous protein 3
- Structural maintenance of chromosomes protein 3
- Biogenesis of lysosome-related organelles complex 1 subunit 1
- HORMA domain-containing protein
Sequence:
MYEYSFNPNIDHEPGSVESQQSTIYSDSDDSDDSFLDDEVIPPKEQAMRKIEFALADIKRQMDNKEKSLTLRISTSKSHFCLRYTAKRKGKLDRDLHCLHQVYDLLENDKRSTKRELYYEHKAVYGNQKYLDSSIKSICELLNESRANLNILSCGRGIIRGAITFLVENVGVIDARVQEVLITDALLFSNIISEADFILVVEKDTTFQKLMDENFQAMFPRGILATSKGYPDIATRNVLKMLSEKRKFPIYGLFDADPHGIEIYLTYKYGPTKEFAEGRGAFVPTIEWIGLFPTDFHRFTIDQSQCLPLVRTDFVKIEKMIPRSIQLGEIVVTRELDWMIQNKFKMELESINMCGQEYMARFLIAPRVMSIEKEIPIQPETIINEYHEDSQCSLSTDDDREAKDDDYIDSDAEEKFQNMIDNDSD
Protein: Usher syndrome 1C (Autosomal recessive, severe), isoform CRA_d (Usher syndrome 1C isoform 2) (A0A0S2Z4U9)
Organism: Homo sapiens (Human)
Subcellular location: Cell projection {ECO:0000256|ARBA:ARBA00004316}.
Interaction partners:
Sequence:
MDRKVAREFRHKVDFLIENDAEKDYLYDVLRMYHQTMDVAVLVGDLKLVINEPSRLPLFDAIRPLIPLKHQVEYDQLTPRRSRKLKEVRLDRLHPEGLGLSVRGGLEFGCGLFISHLIKGGQADSVGLQVGDEIVRINGYSISSCTHEEVINLIRTKKTVSIKVRHIGLIPVKSSPDEPLTWQYVDQFVSESGGVRGSLGSPGNRENKEKKVFISLVGSRGLGCSISSGPIQKPGIFISHVKPGSLSAEVGLEIGDQIVEVNGVDFSNLDHKEAVNVLKSSRSLTISIVAAAGRELFMTDRERLAEARQRELQRQELLMQKRLAMESNKILQEQQEMERQRRKEIAQKAAEENERYRKEMEQIVEEEEKFKKQWEEDWGSKEQLLLPKTITAEVHPVPLRKPKYDQGVEPELEPADDLDGGTEEQGEQDFRKYEEGFDPYSMFTPEQIMGKDVRLLRIKKEGSLDLALEGGVDSPIGKVVVSAVYERGAAERHGGIVKGDEIMAINGKIVTDYTLAEAEAALQKAWNQGGDWIDLVVAVCPPKEYDDELTFF