wanglab/gogpt-training-data huggingface dataset:
Protein: rRNA processing protein RCL1 (RNA 3'-terminal phosphate cyclase-like protein 1) (Q08096)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Does not have cyclase activity. Plays a role in 40S-ribosomal-subunit biogenesis in the early pre-rRNA processing steps at sites A0, A1 and A2 that are required for proper maturation of the 18S RNA. Essential for viability.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:25064857}.
Interaction partners:
- Pre-rRNA-processing protein PNO1
- U3 small nucleolar RNA-associated protein 4
- U3 small nucleolar RNA-associated protein 15
- Ribosome biogenesis protein BMS1
- Nucleolar protein 56
- U3 small nucleolar ribonucleoprotein protein LCP5
- Protein BFR2
- U3 small nucleolar ribonucleoprotein protein IMP3
- U3 small nucleolar RNA-associated protein 21
- Nucleolar complex protein 4
Sequence:
MSSSAPKYTTFQGSQNFRLRIVLATLSGKPIKIEKIRSGDLNPGLKDYEVSFLRLIESVTNGSVIEISYTGTTVIYRPGIIVGGASTHICPSSKPVGYFVEPMLYLAPFSKKKFSILFKGITASHNDAGIEAIKWGLMPVMEKFGVRECALHTLKRGSPPLGGGEVHLVVDSLIAQPITMHEIDRPIISSITGVAYSTRVSPSLVNRMIDGAKKVLKNLQCEVNITADVWRGENSGKSPGWGITLVAQSKQKGWSYFAEDIGDAGSIPEELGEKVACQLLEEISKSAAVGRNQLPLAIVYMVIGKEDIGRLRINKEQIDERFIILLRDIKKIFNTEVFLKPVDEADNEDMIATIKGIGFTNTSKKIA
Protein: Proteasome subunit beta type-11 (EC 3.4.25.1) (Proteasome subunit beta-5t) (A5LHX3)
Organism: Homo sapiens (Human)
Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. Incorporated instead of PSMB5 or PSMB8, this unit reduces the chymotrypsin-like activity of the proteasome (By similarity). Plays a pivotal role in development of CD8-positive T cells (By similarity).
Subcellular location: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}. Nucleus {ECO:0000250}.
Interaction partners:
- Proteasome subunit beta type-10
- Proteasome subunit beta type-9
- Proteasome subunit alpha-type 8
- Proteasome subunit beta type-4
- Proteasome subunit alpha type-5
- Proteasome subunit alpha type-7
- Proteasome subunit alpha type-3
- Proteasome subunit beta type-3
- Proteasome subunit beta type-1
- Proteasome subunit beta type-2
Sequence:
MALQDVCKWQSPDTQGPSPHLPRAGGWAVPRGCDPQTFLQIHGPRLAHGTTTLAFRFRHGVIAAADTRSSCGSYVACPASCKVIPVHQHLLGTTSGTSADCATWYRVLQRELRLRELREGQLPSVASAAKLLSAMMSQYRGLDLCVATALCGWDRSGPELFYVYSDGTRLQGDIFSVGSGSPYAYGVLDRGYRYDMSTQEAYALARCAVAHATHRDAYSGGSVDLFHVRESGWEHVSRSDACVLYVELQKLLEPEPEEDASHAHPEPATAHRAAEDRELSVGPGEVTPGDSRMPAGTETV
Protein: Protein apnoia (Q9VFX3)
Organism: Drosophila melanogaster (Fruit fly)
Function: Transmembrane protein that plays a key role in trachea development by regulating crb localization and maintenance at the apical cell membrane. Required for anisotropic apical surface expansion important for tracheal tube elongation and lumen stability at larval stages.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:30645584}; Multi-pass membrane protein {ECO:0000255}. Note=In tracheal cells, colocalizes with crb in the subapical region, a small region of the apical membrane apical to the adherens junctions. {ECO:0000269|PubMed:30645584}.
Interaction partners:
- Osiris 20
- FI01546p
- Osiris 15
- Osiris 18
- Osiris 19, isoform A
Sequence:
MAANQKIVFALVCLFLACDLVLGQQQAANSSDSDSDVAESRTFGHHFLRRISFALVPGAFVVGVITTLLAALTVVSIKGLGVGVILLVLAIGQMLSRALPVQAAAAYAAAPVPVQAPVPVVYSHSHTQQPVWLEKEW
Protein: Coiled-coil domain-containing protein 62 (E9PVD1)
Organism: Mus musculus (Mouse)
Function: Nuclear receptor coactivator that can enhance preferentially estrogen receptors ESR1 and ESR2 transactivation. Modulates also progesterone/PGR, glucocorticoid/NR3C1 and androgen/AR receptors transactivation, although at lower level; little effect on vitamin D receptor/VDR (By similarity). Required for normal spermiogenesis. It probably plays a role in acrosome formation.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:28339613}. Note=Mainly nuclear. {ECO:0000250}.
Interaction partners:
- Huntingtin-interacting protein 1-related protein
- Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial
- 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase
Sequence:
MRSSEGAPSWAVALPPPLRPCAYGVSEVTRCWHQLSLGAGESSMNPSATLYRRQNIGSEVETSTIEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQKVLTLEERCSKLEGELHKRTDIIKSLMKKVKTLESNQAECQTALQKTQQQLQEMAQKATHSTLLSEDLEARNENLSSTLVDLSAQVGQLQAREQALTTMIKLKDKDIIEAVNHISDCSGKFKLLEHALRDAKMAETCVVREKQDYKQKLKALRIEVNKLKEDLNEKTTENNEQREEIIRLKQEKSCLHDELIFTVEREKRKDELLDIAKSKQDRTNSELQNLRQIYVKQQSDLQFLNFNIESSQELIQIHGLKMEEPKALECSKDMCLSDLDNNYPKIDIKRERNQKSLVKDQTFEVMLAQHNGSDKSSCDACREKKLQVNTALGEKSVIALSSLFTKDLLDKQKSWSLGGKIQTEPENKVTLCKVHAKSPKCDGVGLPTEEKQLSETSVSLSDEKQWHDINVYLGLSSCSKQPDRLDGDGHDRTGTSEVSCCTPNVVCIGDNDLSESKCCHPSNIIIEAPGHMTDTEWMNIFKPSRAQRIVRHKTMCTCSRSVSAMKYNSSASELIGMQPSQCVGSLKSAEREEESAALPDRRTSANEKDDFSPTSKLQRLLAESRQMVTDLELSTLLPISCENLNRSKLEVSEEPDEKTTLVSH
Protein: Pentatricopeptide repeat-containing protein At1g20300, mitochondrial (Q9LN22)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Mitochondrion {ECO:0000305}.
Interaction partners:
- RNA-binding
- KH domain-containing protein At3g08620
- At2g37400
- RNA-binding
- Tetratricopeptide repeat
- U4/U6 small nuclear ribonucleoprotein Prp31 homolog
- Outer envelope pore protein 16-1, chloroplastic
- Glycine-rich RNA-binding protein 2, mitochondrial
- Probable plastid-lipid-associated protein 1, chloroplastic
- Proline-rich protein 1
Sequence:
MALLRSKLHLSRTLSFISPLLPKTFSTSATSLLSDHENDESAATITAAVSVPISPLLTPEDTQTVEKFHSIIKDHYRKNPTSPNDAILNPSLTLHALSLDFSQIETSQVSPSVVRCVIEKCGSVRHGIPLHQSLAFFNWATSRDDYDHKSPHPYNEMIDLSGKVRQFDLAWHLIDLMKSRNVEISIETFTILIRRYVRAGLASEAVHCFNRMEDYGCVPDKIAFSIVISNLSRKRRASEAQSFFDSLKDRFEPDVIVYTNLVRGWCRAGEISEAEKVFKEMKLAGIEPNVYTYSIVIDALCRCGQISRAHDVFADMLDSGCAPNAITFNNLMRVHVKAGRTEKVLQVYNQMKKLGCEPDTITYNFLIEAHCRDENLENAVKVLNTMIKKKCEVNASTFNTIFRYIEKKRDVNGAHRMYSKMMEAKCEPNTVTYNILMRMFVGSKSTDMVLKMKKEMDDKEVEPNVNTYRLLVTMFCGMGHWNNAYKLFKEMVEEKCLTPSLSLYEMVLAQLRRAGQLKKHEELVEKMIQKGLVARPL
Protein: Outer membrane porin C (Outer membrane protein 1B) (Outer membrane protein C) (Porin OmpC) (P06996)
Organism: Escherichia coli (strain K12)
Function: Forms pores that allow passive diffusion of small molecules across the outer membrane.
Subcellular location: Cell outer membrane {ECO:0000269|PubMed:2464593}; Multi-pass membrane protein {ECO:0000269|PubMed:16949612}.
Interaction partners:
- Outer membrane protein A
- Periplasmic serine endoprotease DegP
- Outer membrane porin F
- Maltoporin
- Nucleoside-specific channel-forming protein Tsx
- Intermembrane phospholipid transport system lipoprotein MlaA
- Outer membrane protein assembly factor BamA
- Tol-Pal system protein TolB
- Outer membrane porin PhoE
- Outer membrane protein X
Sequence:
MKVKVLSLLVPALLVAGAANAAEVYNKDGNKLDLYGKVDGLHYFSDNKDVDGDQTYMRLGFKGETQVTDQLTGYGQWEYQIQGNSAENENNSWTRVAFAGLKFQDVGSFDYGRNYGVVYDVTSWTDVLPEFGGDTYGSDNFMQQRGNGFATYRNTDFFGLVDGLNFAVQYQGKNGNPSGEGFTSGVTNNGRDALRQNGDGVGGSITYDYEGFGIGGAISSSKRTDAQNTAAYIGNGDRAETYTGGLKYDANNIYLAAQYTQTYNATRVGSLGWANKAQNFEAVAQYQFDFGLRPSLAYLQSKGKNLGRGYDDEDILKYVDVGATYYFNKNMSTYVDYKINLLDDNQFTRDAGINTDNIVALGLVYQF
Protein: Probable autotransporter YfaL [Cleaved into: Probable secreted autotransporter protein YfaL; Probable autotransporter YfaL translocator] (P45508)
Organism: Escherichia coli (strain K12)
Function: Probably an autotransporter.
Subcellular location: [Probable autotransporter YfaL]: Periplasm.; SUBCELLULAR LOCATION: [Probable secreted autotransporter protein YfaL]: Secreted. Cell surface.; SUBCELLULAR LOCATION: [Probable autotransporter YfaL translocator]: Cell outer membrane {ECO:0000269|PubMed:16522795}.
Interaction partners:
- Type 1 fimbrin D-mannose specific adhesin
- Uncharacterized fimbrial-like protein SfmH
- Chaperone protein FimC
- Type-1 fimbrial protein, A chain
- Uncharacterized fimbrial-like protein SfmA
- Protein FimF
- Uncharacterized fimbrial-like protein SfmF
- Probable fimbrial chaperone SfmC
- ATP synthase epsilon chain
- ATP synthase gamma chain
Sequence:
MRIIFLRKEYLSLLPSMIASLFSANGVAAVTDSCQGYDVKASCQASRQSLSGITQDWSIADGQWLVFSDMTNNASGGAVFLQQGAEFSLLPENETGMTLFANNTVTGEYNNGGAIFAKENSTLNLTDVIFSGNVAGGYGGAIYSSGTNDTGAVDLRVTNAMFRNNIANDGKGGAIYTINNDVYLSDVIFDNNQAYTSTSYSDGDGGAIDVTDNNSDSKHPSGYTIVNNTAFTNNTAEGYGGAIYTNSVTAPYLIDISVDDSYSQNGGVLVDENNSAAGYGDGPSSAAGGFMYLGLSEVTFDIADGKTLVIGNTENDGAVDSIAGTGLITKTGSGDLVLNADNNDFTGEMQIENGEVTLGRSNSLMNVGDTHCQDDPQDCYGLTIGSIDQYQNQAELNVGSTQQTFVHALTGFQNGTLNIDAGGNVTVNQGSFAGIIEGAGQLTIAQNGSYVLAGAQSMALTGDIVVDDGAVLSLEGDAADLTALQDDPQSIVLNGGVLDLSDFSTWQSGTSYNDGLEVSGSSGTVIGSQDVVDLAGGDNLHIGGDGKDGVYVVVDASDGQVSLANNNSYLGTTQIASGTLMVSDNSQLGDTHYNRQVIFTDKQQESVMEITSDVDTRSDAAGHGRDIEMRADGEVAVDAGVDTQWGALMADSSGQHQDEGSTLTKTGAGTLELTASGTTQSAVRVEEGTLKGDVADILPYASSLWVGDGATFVTGADQDIQSIDAISSGTIDISDGTVLRLTGQDTSVALNASLFNGDGTLVNATDGVTLTGELNTNLETDSLTYLSNVTVNGNLTNTSGAVSLQNGVAGDTLTVNGDYTGGGTLLLDSELNGDDSVSDQLVMNGNTAGNTTVVVNSITGIGEPTSTGIKVVDFAADPTQFQNNAQFSLAGSGYVNMGAYDYTLVEDNNDWYLRSQEVTPPSPPDPDPTPDPDPTPDPDPTPDPEPTPAYQPVLNAKVGGYLNNLRAANQAFMMERRDHAGGDGQTLNLRVIGGDYHYTAAGQLAQHEDTSTVQLSGDLFSGRWGTDGEWMLGIVGGYSDNQGDSRSNMTGTRADNQNHGYAVGLTSSWFQHGNQKQGAWLDSWLQYAWFSNDVSEQEDGTDHYHSSGIIASLEAGYQWLPGRGVVIEPQAQVIYQGVQQDDFTAANRARVSQSQGDDIQTRLGLHSEWRTAVHVIPTLDLNYYHDPHSTEIEEDGSTISDDAVKQRGEIKVGVTGNISQRVSLRGSVAWQKGSDDFAQTAGFLSMTVKW
Protein: Erythrocyte membrane protein band 4.1 like 3 (cDNA FLJ77757) (A8K968)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MQCKVILLDGSEYTCDVEKRSRGQVLFDKVCEHLNLLEKDYFGLTYRDAENQKNWLDPAKEIKKQVRSGAWHFSFNVKFYPPDPAQLSEDITRYYLCLQLRDDIVSGRLPCSFVTLALLGSYTVQSELGDYDPDECGSDYISEFRFAPNHTKELEDKVIELHKSHRGMTPAEAEMHFLENAKKLSMYGVDLHHAKDSEGVEIMLGVCASGLLIYRDRLRINRFAWPKVLKISYKRNNFYIKIRPGEFEQFESTIGFKLPNHRAAKRLWKVCVEHHTFFRLLLPEAPPKKFLTLGSKFRYSGRTQAQTRRASALIDRPAPYFERSSSKRYTMSRSLDGASVNENHEIYMKDSMSAAEVGTGQYATTKGISQTNLITTVTPEKKAEEERDEEEDKRRKGEEVTPISAIRHEGKTDSERTDTAADGETTATEELEKTQDDLMKHQTNISELKRTFLETSTDTAVTNEWEKRLSTSPVRLAARQEDAPMIEPLVPEEKMETKTESSGIETEPTVHHLPLSTEKVVQETVLVEERRVVHASGDASYSAGDSGDAAAQPAFTGIKGKEGSALTEGAKEEGGEEVAKAVLEQEETAAASRERQEEQSAAIHISETLEQKPHFESSTVKTETISFGSVSPGGVKLEISTKEVPVVHTETKTITYESSQVDPGTDLEPGVLMSAQTITSETTSTTTTTHITKTVKGGISETRIEKRIVITGDADIDHDQALAQAIKEAKEQHPDMSVTKVVVHKETEITPEDGED
Protein: Probable U3 small nucleolar RNA-associated protein 7 (U3 snoRNA-associated protein 7) (U three protein 7) (Q9P4X3)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in nucleolar processing of pre-18S ribosomal RNA.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Uncharacterized WD repeat-containing protein C2E1P5.05
- U3 small nucleolar RNA-associated protein 4
- U3 small nucleolar RNA-associated protein 6
- KRR1 small subunit processome component homolog
- Uncharacterized WD repeat-containing protein C3D6.12
- Uncharacterized protein C3B8.09
- U3 small nucleolar RNA-associated protein 10
- rRNA biogenesis protein rrp5
- Probable U3 small nucleolar RNA-associated protein 11
- U3 small nucleolar RNA-associated protein 22
Sequence:
MSAQKLNLEDVNASTKKYSRGRKLNPKKIKDKKLRSNIQKIEERIENVESSLAKTEILHEDNPGLLEAEGLERTYKFRQDQLAPNVALETATKSFSLDLDKFGGYSFDYTRDGRMILLGGRKGHISAFDWRTGKLLTELHLRETVRDVKWFHNHQYFAVAQKKYVYVYDNMGTEIHCLKRHIEVNALDFLPYHLLLTSIGNAGYLKYQDVSTGQLVAEHRTGMGASHVLHQNPHNAVEHVGHANGQVTLWSPSSTTPLVKMLTHRGPVRDLAVNRDGRYMVTAGADSLLKVWDLRTYKELHSYYTPTPAQRLTLSDRGLLAVGWGPHATIWKDALRTKQNFPYMNHLLPSSSVVDLHYCPYEDILGIGHAKGFESIIVPGSGEPNYDSYENDPFASRKQRQETEVRQLLEKLRPEMISLNADFIGNVDRAAPSLRKAEAEEEKPPEEKWVPKAKARGKNSALRRYLRKHARNVVDQRRLKVEKSLEIEKKMRAQRVRREQKLPEEREKWGYALSRFVSKK
Protein: RNA-binding protein NOB1 (EC 3.1.-.-) (Q8BW10)
Organism: Mus musculus (Mouse)
Function: May play a role in mRNA degradation (By similarity). Endonuclease required for processing of 20S pre-rRNA precursor and biogenesis of 40S ribosomal subunits (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9ULX3}.
Interaction partners:
- Serine/threonine-protein kinase RIO2
- Protein LTV1 homolog
- Pre-rRNA-processing protein TSR1 homolog
- Bystin
- RNA-binding protein PNO1
- Serine/threonine-protein kinase RIO1
- Small ribosomal subunit protein uS7
- Ubiquitin-like protein FUBI
- Small ribosomal subunit protein uS2
- Small ribosomal subunit protein eS1
Sequence:
MAPVEHVVADAGAFLRDAPLQDIGKNIYTIREVVREIRDKATRRRLAVLPYQLRFKEPLPEYVRLVTEFSKKTGDYPSLSATDIQVLALTYQLEAEFVGVSHLKKEPEKAKVSSSIQHPETALHISGFHLPSKSKPLQEAVDRGHAADGPENLEFSSFMFWRTPLPNIDRELQELLIDGREEEEEEEECEDSDDDGGGWITPSNIKQIQQELEQCDTPEDVQVGCVTTDFAMQNVLLQMGLHVLAVNGMLVREARSYILRCHGCFKTTSDMNRVFCGHCGNKTLKKVSVTINDDGTLHMHFSRNPKVLNPRGLRYSLPTPKGGKYAINPHLTEDQRFPQLRLSQKARQKTDVFAPDYIAGVSPFAENDISSRSAILQVRDGMLGAGRRRLNPNASRKKFVKKR
Protein: Casein kinase I homolog 2 (EC 2.7.11.1) (P40234)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. May contribute to the regulation of morphology.
Subcellular location: Cytoplasm.
Interaction partners:
- Pheromone P-factor receptor
- Casein kinase I homolog 1
- Casein kinase I homolog 3
- Pheromone M-factor receptor
- Meiotic recombination protein rec8
- Meiotic recombination protein rec11
- Separin
- Linear element protein rec10
Sequence:
MNSQTSVVGVHYRVGRKIGEGSFGVIFDGMNLLNNQLIAIKFEPKKSEAPQLRDEYRTYKLLVGNAGIPNVYYFGQEGLHNILVIDLLGPSLEDLFEWCGRRFSVKTVAMTAKQMLSRVQTIHEKNLVYRDIKPDNFLIGRPSSRNANMVYMVDFGMAKYYRDPKTKQHIPYSERKSLSGTARYMSINTHLGREQSRRDDLESLGHVFMYFLRGSLPWQGLKAANNKHKYEKISEKKQSTSISELCAGFPNEFSKYMTYVRSLEFDEEPDYAFLQELFDDVLRANGDTNDGVYDWMLLNDGKGWESSSSHFSVVAMKRRKNYLGLNVVQNDDSRKKNSTLQTQNMRFKSSYGVRGPRNYSSFDALPSKNAPLVRQEQSASKKTIYAHSSRGYDRVRPMYVSQPSNNAVGVNHPNDNSDSEAKGGFFDMICCRCFS
Protein: Nucleoporin NUP53 (Nuclear pore protein NUP53) (G0S156)
Organism: Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (Thermochaetoides thermophila)
Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm).
Subcellular location: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q03790}. Nucleus membrane {ECO:0000250|UniProtKB:Q03790}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q03790}; Cytoplasmic side {ECO:0000250|UniProtKB:Q03790}. Nucleus membrane {ECO:0000250|UniProtKB:Q03790}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q03790}; Nucleoplasmic side {ECO:0000250|UniProtKB:Q03790}. Note=Symmetric distribution. {ECO:0000250|UniProtKB:Q03790}.
Interaction partners:
- Nascent polypeptide-associated complex subunit alpha
- Nucleoporin NIC96
- Nucleoporin NUP192
- Nucleoporin NUP170
- Putative 60S ribosomal protein
- 60S ribosomal protein L25-like protein
- Nucleoporin NUP145
- Nucleoporin NUP188
- Nucleoporin NSP1
- Nucleoporin NUP49
Sequence:
MPPLILHNVPDDELYVGDDGIQRPFAMVFPQQDGSLRSRKANLETGAFGKSTRRTRSKAATPAKREDPTIAAADKIFSNWLASQNQSAPQTSVPAPAQRKPNLIPSSSSQNLAQGHDESSAPSQTRFFRKQEPTEVILRGYRNAQHQYAAINHYEQIAGRICEDYPREPPVESRRYKSELRDPAFTHRRALTPEERAKVNRAMSGEHWVKVTFESAEAADKAVYSSPQLIQGHLVYAEYYKGVPPAQDEAIPDPSVAAFGAALSRTQTLRQRNRGSFSLSGTQEAGGPDASPTSSLTADTGTLASGVEISTSTSNTLNGGAAAGGAEKSQDDEFCRVIPTVRKAKLLPMEEALLPAPTFTQRIANHIPFLRWFNGAMIGSEVPRTETGEFDWVRASLFWKLMWWLDFLLGLFGGDIRDAEKDDKED
Protein: D-alanyl-L-alanine endopeptidase (EC 3.4.22.-) (1,4-N-acetylmuramidase) (EC 3.2.1.17) (B30 lysin) (Endoysin) (Glycosidase) (Q8HA43)
Organism: Streptococcus phage B30 (Streptococcus agalactiae bacteriophage B30)
Function: The endopeptidase activity cleaves the bacterial peptidoglycan between D-alanine and L-alanine. The N-acetyl-muramidase activity cleaves between N-acetylmuramic acid and N-acetylglucosamine bonds.
Interaction partners:
Sequence:
MATYQEYKSRSNGNAYDIDGSFGAQCWDGYADYCKYLGLPYANCTNTGYARDIWEQRHENGILNYFDEVEVMQAGDVAIFMVVDGVTPYSHVAIFDSDAGGGYGWFLGQNQGGANGAYNLVKIPYSATYPTAFRPKSFKNAVTVTDNTGLNKGDYFIDVSAYQQADLTTTCQQAGTTKTIIKVSESIAWLSDRHQQQANTSDPIGYYHFGRFGGDSALAQREADLFLSNLPSKKVSYLVIDYEDSASADKQANTNAVIAFMDKIASAGYKPIYYSYKPFTLNNIDYQKIIAKYPNSIWIAGYPDYEVRTEPLWEFFPSMDGVRWWQFTSVGVAGGLDKNIVLLADDSSKMDIPKVDKPQELTFYQKLATNTKLDNSNVPYYEATLSTDYYVESKPNASSADKEFIKAGTRVRVYEKVNGWSRINHPESAQWVEDNYLVNATDM
Protein: GDP-mannose 4,6 dehydratase (EC 4.2.1.47) (GDP-D-mannose dehydratase) (Dm-gmd) (GDP-mannose dehydratase) (Q9VMW9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Catalyzes the conversion of GDP-D-mannose to GDP-4-dehydro-6-deoxy-D-mannose (also known as GDP-4-keto-6-deoxy-D-mannose or GDP-4-dehydro-alpha-D-rhamnose), an essential step in the synthesis of GDP-fucose from GDP-mannose.
Interaction partners:
- Probable GDP-L-fucose synthase
- Mannose-1-phosphate guanylyltransferase catalytic subunit beta
- Mannose-1-phosphate guanylyltransferase regulatory subunit alpha
- ALG1, chitobiosyldiphosphodolichol beta-mannosyltransferase
- Dolichol-phosphate mannosyltransferase subunit 1
- mannose-6-phosphate isomerase
- UDP-glucose 4-epimerase
- Dolichol phosphate-mannose biosynthesis regulatory protein
- Dolichol-phosphate mannosyltransferase subunit 3
- GDP-fucose transporter, Golgi
Sequence:
MLNTRLIAMSTSDGAPETKKQRPESSSNGSKDQNGTEAGAEGDSRDKVALITGITGQDGSYLAEFLLKKDYEVHGIIRRASTFNTTRIEHLYADPKAHKGGRMKLHYGDMTDSSSLVKIINMVKPTEIYNLAAQSHVKVSFDLSEYTAEVDAVGTLRILDAIRTCGMEKNVRFYQASTSELYGKVVETPQNEQTPFYPRSPYACAKMYGFWIVINYREAYNMYACNGILFNHESPRRGENFVTRKITRSVAKIYHKQMEYFELGNLDSKRDWGHASDYVEAMWMMLQRESPSDYVIATGETHSVREFVEAAFKHIDREITWKGKGVDEVGVENGTGIVRVRINPKYFRPTEVDLLQGDASKANRELNWTPKVTFVELVSDMMKADIELMRKNPIA
Protein: Probable NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5 (Q18359)
Organism: Caenorhabditis elegans
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Matrix side {ECO:0000250}.
Interaction partners:
- NADH dehydrogenase 1 alpha subcomplex subunit 8
- NADH-ubiquinone oxidoreductase chain 1
- Complex I-49kD
- NADH dehydrogenase 1 beta subcomplex subunit 3
- NADH dehydrogenase 1 beta subcomplex subunit 5, mitochondrial
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH dehydrogenase iron-sulfur protein 4
- NADH dehydrogenase 1 alpha subcomplex subunit 2
- Cytochrome b-c1 complex subunit 7
- NADH dehydrogenase 1 beta subcomplex subunit 10
Sequence:
MSSRFLRTAVARATQQRSMYENPYINRFKARSKVSEDFHKKTTGITGLFVNEHPHRALTVVYGRILRALEQIPRDAAYRKYTEAVVKQRLALVQAENDIKKLEEKIGMGQIEEVIEQAEYELETTRAIVDSKAWEPLVESAPKGQWSWPV
Protein: Golgin subfamily A member 5 (Golgin-84) (Q3ZU82)
Organism: Rattus norvegicus (Rat)
Function: Involved in maintaining Golgi structure. Stimulates the formation of Golgi stacks and ribbons. Involved in intra-Golgi retrograde transport.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:12656988}; Single-pass type IV membrane protein {ECO:0000269|PubMed:12656988}. Note=Found throughout the Golgi.
Interaction partners:
- Conserved oligomeric Golgi complex subunit 7
- Golgi reassembly-stacking protein 1
- Golgin-45
- Golgi reassembly-stacking protein 2
- Golgi SNAP receptor complex member 1
- small monomeric GTPase
Sequence:
MSWFADLAGRAEDLLNRVDQGAATALRKESTSNTFYSKNTDYPELHQQNTDSTYHTGQKANYISSAADNIRHQKATIIAGTANVKVGSRTGGDASHPTEHASVPRPSSHFVRRKKSEPDDELLFDFLNSSQKEPTGRVEIKKEKGKAPVLPSSQSSAVSSVTTSVTTIKATEENSGSQSPEVSSSDSMPEGHKKSTEESTVSNAISVEHSSVPSDGSMSHELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNEARVRVEKWNVDNSKSDRITRELRAQVDDLTEAVAAKDSQLAVLKVRLQEADQVLSSRTEALEALQSEKSRIMQDHNEGSSLQNQALQTLQERHEADATLKREQESYKQMQSEFATRLNKMEVERQNLAEAVTLAERKYSEERKKVDDLQQQVKLHRSSLESAKQELVDYKQKATRILQSKEKLINSLKEGSSFEGLDSSTASSMELEELRHERELQKEEIQKLMGQIHQLRSELQDMEAQQVSEAESAREQLQDLQDQIAKQRASKQELETELDRMKQEFHYVEEDLHRTKNTLQSRIKDREEEIQKLRNQLTNKTLSNSSQSELESRLHQLTETLIQKQTLLESLSTEKNSLVFQLERLEQQLHSAATGPSSGSSINMSGVDSGEGTRLRNVPVLFNDTETNLAGMYGKVRKAASSIDQFSIRLGIFLRRYPIARVFVIIYMALLHLWVMIVLLTYSPEMHHDQPYGK
Protein: rRNA methyltransferase 1, mitochondrial (EC 2.1.1.-) (21S rRNA (guanosine(2270)-2'-O)-methyltransferase) (21S rRNA [Gm2270] 2'-O-methyltransferase) (Mitochondrial large ribosomal RNA ribose methylase) (Petite colonies protein 56) (P25270)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of 2'-O-methylguanosine at position 2270 (Gm2270) in the 21S mitochondrial large subunit ribosomal RNA (mtLSU rRNA), a universally conserved modification in the peptidyl transferase domain of the mtLSU rRNA. This modification seems to be important for the normal accumulation of the mitochondrial large ribosomal subunit.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Mitochondrial GTPase 1
- rRNA methyltransferase 2, mitochondrial
- Large ribosomal subunit protein uL29m
- Large ribosomal subunit protein bL17m
- tRNA modification GTPase MSS1
- Large ribosomal subunit protein mL43
- Acyl carrier protein, mitochondrial
- MIOREX complex component 8
- Large ribosomal subunit protein uL15m
- Multisubstrate pseudouridine synthase 7
Sequence:
MTSLTNAVFKRYLAVTPSAHQALKTRIKKKSSSFDKFFPQQSNSRKKQWETLNEDKASWFKRKYAHVHAREQDRAADPYGKKKAHVEKLKEIKNQAKLNQKSHKSKFQNKDIALKLMNDNPIFEYVYGTNSVYAALLNPSRNCHSRLLYHGTIPSKFLQIVDELKVTTELVDKHRLNLLTNYGVHNNIALETKPLQPVEIAYLGDMDTSSAALSIHELGFNNENIPHELPYGTKTDAKKFPLGLYLDEITDPHNIGAIIRSAYFLGVDFIVMSRRNCSPLTPVVSKTSSGALELLPIFYVDKPLEFFTKSQEMGGWTFITSHLANATSEKYTVGKTISMHDLNGLCNELPVVLVVGNESQGVRTNLKMRSDFFVEIPFGGIEKGNRAPEPIVDSLNVSVATALLIDNILTCK