ids
stringlengths 6
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stringlengths 11
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stringlengths 108
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Q9PLV4 | MRYGEKEIKEFDVENMEIWPNDAKNDYIIKITLPEFMCCCPRSGYPDFATIYLEYMPDKFVVELKAIKLYINTFMYRNVSHEASINEIYNTLKDKLKPKWIKVVGDFNPRGNVHTVIECRSDMVVPK | Function: Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1).
Catalytic Activity: 7-aminomethyl-7-carbaguanine + 2 NADP(+) = 7-cyano-7-deazaguanine + 3 H(+) + 2 NADPH
Sequence Mass (Da): 15040
Sequence Length: 127
Pathway: tRNA modification; tRNA-queuosine biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.7.1.13
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B9KE89 | MRYGEKEIKEFDVENMEVWPNDAKNDYVIKITLPEFMCCCPRSGYPDFATIYLEYIPNKLVVELKAIKLYINTFMYRNVSHEASINEIYNTLKEKLDPKWIKVVGDFNPRGNVHTVIECRSDLVVPQ | Function: Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1).
Catalytic Activity: 7-aminomethyl-7-carbaguanine + 2 NADP(+) = 7-cyano-7-deazaguanine + 3 H(+) + 2 NADPH
Sequence Mass (Da): 14941
Sequence Length: 127
Pathway: tRNA modification; tRNA-queuosine biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.7.1.13
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Q9ZE74 | MPLSTSLLGKKNTYKDSYDATLLFKIPRINNRNVLGIDSNHLPFYGVDIWNTYEISCLNKNGKPLVGIGTFYIPADSENIVESKSFKLYLNSFNNFIIESIEELERIILQDLSNVTYAKVTGRIFPINTKIEFGIPSGKNIDNLDIVCNNYGPPDNSLIEYEDVLVEEEIYSNLFKSNCLVTGQPDWGTIVIKYKGKKLKYDSFLRYLISFRNFNEFAEQCAERIFIDIKNSINLDFLSIYIVYTRRGGIDICPYRSTDKSYTLPNDKRLIRQ | Function: Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1).
Catalytic Activity: 7-aminomethyl-7-carbaguanine + 2 NADP(+) = 7-cyano-7-deazaguanine + 3 H(+) + 2 NADPH
Sequence Mass (Da): 31481
Sequence Length: 273
Pathway: tRNA modification; tRNA-queuosine biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.7.1.13
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B5A5T4 | MWTQRNAVGNWLLVLTAVIGFLTFIWIPQTSAECQTRSIYCYECDSWTDARCKDPFNYTALPRDQPPLMTCNGCCVKMVRHQRSPYEVVRRMCTSQLQINLFMVDHVCMMESSGNGHMCFCEEDMCNSSKNLHTNGCQLHLIPIAVAVSWLMGQLLSR | Function: Required for homeostatic regulation of sleep under normal conditions and after sleep deprivation. Important regulator of the Sh K(+) channel, acting as a signaling molecule that connects sleep drive to lowered membrane excitability, possibly by enhancing K(+) channel activity and thus reducing neuronal excitability.
PTM: N-glycosylated.
Location Topology: Lipid-anchor
Sequence Mass (Da): 18124
Sequence Length: 158
Subcellular Location: Cell membrane
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B4MQJ1 | MSLPAGNAVGNWLLILTAIFGFLTLIWIPQASAECQTRSIYCYECDSWTDARCKDPFNYTALPRDQPPLMTCNGCCVKMVRHQRSRYEVVRRMCTSQLQINLFMVDHVCMMESSGNGHMCFCEEDMCNSSKNLYTKNGYQHLINIMIIWLIGILLNQLSNR | Function: Required for homeostatic regulation of sleep under normal conditions and after sleep deprivation. Important regulator of the Sh K(+) channel, acting as a signaling molecule that connects sleep drive to lowered membrane excitability, possibly by enhancing K(+) channel activity and thus reducing neuronal excitability (By similarity).
PTM: N-glycosylated.
Location Topology: Lipid-anchor
Sequence Mass (Da): 18520
Sequence Length: 161
Subcellular Location: Cell membrane
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P34140 | MNPEYDYLFKLLLIGDSGVGKSCLLLRFADDTYTESYISTIGVDFKIRTINLDGKIIKLQIWDTAGQERFRTITSSYYRGAHGIIVVYDVTDHVSFNNVKQWMQEIQRYACDSVTRLLVGNKCDLIEKKIVDTSTAREYADSVGIPFLETSAKSSANVEQAFMIMASEIKKLQGGIQPNNNSTYNAHVVKPTGFTPIGKKKKCSII | Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. Rab1B regulates vesicular transport between the endoplasmic reticulum and successive Golgi compartments. Plays a role in the initial events of the autophagic vacuole development which take place at specialized regions of the endoplasmic reticulum.
Location Topology: Lipid-anchor
Sequence Mass (Da): 23126
Sequence Length: 206
Subcellular Location: Cytoplasm
|
Q9H0U4 | MNPEYDYLFKLLLIGDSGVGKSCLLLRFADDTYTESYISTIGVDFKIRTIELDGKTIKLQIWDTAGQERFRTITSSYYRGAHGIIVVYDVTDQESYANVKQWLQEIDRYASENVNKLLVGNKSDLTTKKVVDNTTAKEFADSLGIPFLETSAKNATNVEQAFMTMAAEIKKRMGPGAASGGERPNLKIDSTPVKPAGGGCC | Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes . Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion . Plays a role in the initial events of the autophagic vacuole development which take place at specialized regions of the endoplasmic reticulum . Regulates vesicular transport between the endoplasmic reticulum and successive Golgi compartments (By similarity). Required to modulate the compacted morphology of the Golgi . Promotes the recruitment of lipid phosphatase MTMR6 to the endoplasmic reticulum-Golgi intermediate compartment (By similarity).
PTM: Prenylated; by GGTase II, only after interaction of the substrate with Rab escort protein 1 (REP1).
Location Topology: Lipid-anchor
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 22171
Sequence Length: 201
Subcellular Location: Cytoplasm
EC: 3.6.5.2
|
P10536 | MNPEYDYLFKLLLIGDSGVGKSCLLLRFADDTYTESYISTIGVDFKIRTIELDGKTIKLQIWDTAGQERFRTVTSSYYRGAHGIIVVYDVTDQESYANVKQWLQEIDRYASENVNKLLVGNKSDLTTKKVVDNTTAKEFADSLGVPFLETSAKNATNVEQAFMTMAAEIKKRMGPGAASGGERPNLKIDSTPVKSASGGCC | Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (By similarity). Plays a role in the initial events of the autophagic vacuole development which take place at specialized regions of the endoplasmic reticulum (By similarity). Regulates vesicular transport between the endoplasmic reticulum and successive Golgi compartments . Required to modulate the compacted morphology of the Golgi. Promotes the recruitment of lipid phosphatase MTMR6 to the endoplasmic reticulum-Golgi intermediate compartment .
PTM: Prenylated; by GGTase II, only after interaction of the substrate with Rab escort protein 1 (REP1).
Location Topology: Lipid-anchor
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 22163
Sequence Length: 201
Subcellular Location: Cytoplasm
EC: 3.6.5.2
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Q92928 | MNPGYDCLFKLLLIGDSGVGKSCLLLRFADDPYTESYISTIGVDFKIQTIELDGKTIKLQIWDTAGQERFWTITSSYYRGAHGFLVVYDVTDQESYANVKQWLQEIDRHASENVNKLLVGNKSDLTTKKVVDNTTAKEFADSLGIPFLETSAKNATNVEQAFMTMAAEIKKQMGPGAASGGERPNLKIDSTPVKPAGGGCC | Function: Protein transport. Probably involved in vesicular traffic (By similarity).
PTM: (Microbial infection) Phosphocholinated at Ser-76 by L.pneumophila AnkX, leading to displace GDP dissociation inhibitors (GDI) . Both GDP-bound and GTP-bound forms can be phosphocholinated. Dephosphocholinated by L.pneumophila Lem3, restoring accessibility to L.pneumophila GTPase effector LepB .
Location Topology: Lipid-anchor
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 22017
Sequence Length: 201
Subcellular Location: Membrane
EC: 3.6.5.2
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Q9TVU5 | MKEYDYLFKIIVIGDSGTGKSSLLLRFADNTYSESYMSTIGVDFKIKTVKIDNTTIKLQIWDTAGQERFRTITSTYYRGAHGIICVYDVTNKLSFDHITETWLQDIDKYATSNVCKLLIGNKIDLAESRVVSADEAKHVAEQNNMNYIEASAKTDSNVEKAFTTIAKALKDKVTQYPSNAPASTVSLNTASKVPTNRGLTDSCQESSVFKKMNFSSGKCT | Function: Protein transport. Probably involved in vesicular traffic from ER to Golgi (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 24470
Sequence Length: 220
Subcellular Location: Cell membrane
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Q9NX57 | MRKPDSKIVLLGDMNVGKTSLLQRYMERRFPDTVSTVGGAFYLKQWRSYNISIWDTAGREQFHGLGSMYCRGAAAIILTYDVNHRQSLVELEDRFLGLTDTASKDCLFAIVGNKVDLTEEGALAGQEKEECSPNMDAGDRVSPRAPKQVQLEDAVALYKKILKYKMLDEQDVPAAEQMCFETSAKTGYNVDLLFETLFDLVVPMILQQRAERPSHTVDISSHKPPKRTRSGCCA | Function: Plays a role in apical endocytosis/recycling. Plays a role in the maturation and acidification of phagosomes that engulf pathogens, such as S.aureus and M.tuberculosis. Plays a role in the fusion of phagosomes with lysosomes.
Location Topology: Lipid-anchor
Sequence Mass (Da): 26277
Sequence Length: 234
Subcellular Location: Golgi apparatus
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P35295 | MRKPDGKIVLLGDMNVGKTSLLQRYMERRFPDTVSTVGGAFYLKQWRSFNISIWDTAGREQFHGLGSLYCRGAAAIILTYDVNHPQSLFELEDRFLGLTETANNDCLFAIVGNKVDLTSERDTEGGEKEGPASGKVGSCVSTKVPKQVQPEDAVALYKKILKYKMLDEREMPAAEQMCFETSAKTGYNVDLLFETLFDLVVPMIMRQRAEESDQTVDIASCKTPKQTRSGCCA | Function: Plays a role in apical endocytosis/recycling. Plays a role in the maturation and acidification of phagosomes that engulf pathogens, such as S.aureus and Mycobacterium. Plays a role in the fusion of phagosomes with lysosomes (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 25989
Sequence Length: 233
Subcellular Location: Cytoplasmic vesicle
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Q17R06 | MAAAGGGGAAAGRTYSFKVVLLGEGCVGKTSLVLRYCENKFNDKHITTLQASFLTKKLNIGGKRVNLAIWDTAGQERFHALGPIYYRDSNGAILVYDITDEDSFQKVKNWVKELRKMLGNEICLCIVGNKVDLEKERHVSIQEAESYAESVGAKHYHTSAKQNKGIEELFLDLCKRMIETAQVDERAKGNGSSQPGAARRGVQIIDDEPQAQSVGGGCCSSG | Function: Small GTPase involved in membrane trafficking control (By similarity). Regulates integrin internalization and recycling, but does not influence the traffic of endosomally translocated receptors in general (By similarity). As a result, may regulate cell adhesion and migration (By similarity). During the mitosis of adherent cells, controls the endosomal trafficking of integrins which is required for the successful completion of cytokinesis (By similarity). Involved in neurite growth (By similarity). Following SBF2/MTMT13-mediated activation in response to starvation-induced autophagy, binds to and regulates SNARE protein VAMP8 endolysosomal transport required for SNARE-mediated autophagosome-lysosome fusion (By similarity). Modulates protein levels of the cargo receptors TMED2 and TMED10, and required for appropriate Golgi localization of TMED10 (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 24146
Sequence Length: 222
Subcellular Location: Endoplasmic reticulum membrane
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Q00578 | MTDVEGYQPKSKGKIFPDMGESFFSSDEDSPATDAEIDENYDDNRETSEGRGERDTGAMVTGLKKPRKKTKSSRHTAADSSMNQMDAKDKALLQDTNSDIPADFVPDSVSGMFRSHDFSYLRLRPDHASRPLWISPSDGRIILESFSPLAEQAQDFLVTIAEPISRPSHIHEYKITAYSLYAAVSVGLETDDIISVLDRLSKVPVAESIINFIKGATISYGKVKLVIKHNRYFVETTQADILQMLLNDSVIGPLRIDSDHQVQPPEDVLQQQLQQTAGKPATNVNPNDVEAVFSAVIGGDNEREEEDDDIDAVHSFEIANESVEVVKKRCQEIDYPVLEEYDFRNDHRNPDLDIDLKPSTQIRPYQEKSLSKMFGNGRARSGIIVLPCGAGKTLVGITAACTIKKSVIVLCTSSVSVMQWRQQFLQWCTLQPENCAVFTSDNKEMFQTESGLVVSTYSMVANTRNRSHDSQKVMDFLTGREWGFIILDEVHVVPAAMFRRVVSTIAAHAKLGLTATLVREDDKIGDLNFLIGPKLYEANWMELSQKGHIANVQCAEVWCPMTAEFYQEYLRETARKRMLLYIMNPTKFQACQFLIQYHERRGDKIIVFSDNVYALQEYALKMGKPFIYGSTPQQERMNILQNFQYNDQINTIFLSKVGDTSIDLPEATCLIQISSHYGSRRQEAQRLGRILRAKRRNDEGFNAFFYSLVSKDTQEMYYSTKRQAFLVDQGYAFKVITHLHGMENIPNLAYASPRERRELLQEVLLKNEEAAGIEVGDDADNSVGRGSNGHKRFKSKAVRGEGSLSGLAGGEDMAYMEYSTNKNKELKEHHPLIRKMYYKNLKK | Function: ATP-dependent 3'-5' DNA helicase, component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to TFIIK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. The ATPase activity of XPB/SSL2, but not its helicase activity, is required for DNA opening. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. The ATP-dependent helicase activity of XPB/SSL2 is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module TFIIK controls the initiation of transcription . XPB/SSL2 acts as a double-stranded DNA translocase promoting DNA opening by tracking along the nontemplate promoter strand, rotating and inserting DNA into the Pol II active site cleft, leading to DNA unwinding. May also use this translocase mechanism during DNA repair rather than physically wedging open damaged DNA .
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 95341
Sequence Length: 843
Subcellular Location: Nucleus
EC: 3.6.4.12
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P28188 | MNPEYDYLFKLLLIGDSGVGKSCLLLRFSDDSYVESYISTIGVDFKIRTVEQDGKTIKLQIWDTAGQERFRTITSSYYRGAHGIIIVYDVTDEESFNNVKQWLSEIDRYASDNVNKLLVGNKSDLTENRAIPYETAKAFADEIGIPFMETSAKDATNVEQAFMAMSASIKERMASQPAGNNARPPTVQIRGQPVAQKNGCCST | Function: Protein transport. Regulator of membrane traffic from the Golgi apparatus towards the endoplasmic reticulum (ER).
Location Topology: Lipid-anchor
Sequence Mass (Da): 22648
Sequence Length: 203
Subcellular Location: Golgi apparatus
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Q9SEH3 | MNPEYDYLFKLLLIGDSGVGKSCLLLRFADDSYLDSYISTIGVDFKIRTVEQDGKTIKLQIWDTAGQERFRTITSSYYRGAHGIIVTYDVTDLESFNNVKQWLNEIDRYASENVNKLLVGNKCDLTSQKVVSTETAKAFADELGIPFLETSAKNATNVEEAFMAMTAAIKTRMASQPAGGSKPPTVQIRGQPVNQQSGCCSS | Function: Protein transport. Regulator of membrane traffic from the Golgi apparatus towards the endoplasmic reticulum (ER) (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 22318
Sequence Length: 202
Subcellular Location: Cell membrane
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P06839 | MKFYIDDLPVLFPYPKIYPEQYNYMCDIKKTLDVGGNSILEMPSGTGKTVSLLSLTIAYQMHYPEHRKIIYCSRTMSEIEKALVELENLMDYRTKELGYQEDFRGLGLTSRKNLCLHPEVSKERKGTVVDEKCRRMTNGQAKRKLEEDPEANVELCEYHENLYNIEVEDYLPKGVFSFEKLLKYCEEKTLCPYFIVRRMISLCNIIIYSYHYLLDPKIAERVSNEVSKDSIVIFDEAHNIDNVCIESLSLDLTTDALRRATRGANALDERISEVRKVDSQKLQDEYEKLVQGLHSADILTDQEEPFVETPVLPQDLLTEAIPGNIRRAEHFVSFLKRLIEYLKTRMKVLHVISETPKSFLQHLKQLTFIERKPLRFCSERLSLLVRTLEVTEVEDFTALKDIATFATLISTYEEGFLLIIEPYEIENAAVPNPIMRFTCLDASIAIKPVFERFSSVIITSGTISPLDMYPRMLNFKTVLQKSYAMTLAKKSFLPMIITKGSDQVAISSRFEIRNDPSIVRNYGSMLVEFAKITPDGMVVFFPSYLYMESIVSMWQTMGILDEVWKHKLILVETPDAQETSLALETYRKACSNGRGAILLSVARGKVSEGIDFDHQYGRTVLMIGIPFQYTESRILKARLEFMRENYRIRENDFLSFDAMRHAAQCLGRVLRGKDDYGVMVLADRRFSRKRSQLPKWIAQGLSDADLNLSTDMAISNTKQFLRTMAQPTDPKDQEGVSVWSYEDLIKHQNSRKDQGGFIENENKEGEQDEDEDEDIEMQ | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: ATP-dependent 5'-3' DNA helicase, component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to TFIIK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. The ATP-dependent helicase activity of XPD/RAD3 is required for DNA opening. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module TFIIK controls the initiation of transcription. XPD/RAD3 acts by forming a bridge between TFIIK and the core-TFIIH complex. Involved in the maintenance of the fidelity of DNA replication.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 89786
Sequence Length: 778
Subcellular Location: Nucleus
EC: 3.6.4.12
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O12944 | LAKRKAGGEEEDGEWRPPATQKRQKAGSEAESADCYRSPFRKPLTQLTNRPLCLDSSQHEAFIRSILSKPFKVPIPNYKGPTGLRALGIKRAGLRSPLHDPFEEGALVLYEPPLLSAHEQLKIDKDKVPVHVVVDPVLSRVLRPHQREGVKFLWDCVTSRRIPGSHGCIMADEMGLGKTLQCITLMWTLLRQSPDCKPEIEKAMVVSPSSLVRNWYNEVEKWLGGRIQPLAIDGGSKEEIDRKLVGSMNQRGLRVPSPILIISYETFRLHAEALQKGSVGLVICDEGHRLKNSENQTYQALNSLNTPRRVLISGTPIQNDLLEYFSLVHFVNSGILGTAQEFKRHFELPILKGRDADASEAERQKGEERLKELISIVNRCLIRRTSDILSKYLPVKIEQVVCCRLTPLQAELYKNFLKQAKPVEELKEGKINVSSLSSITSLKKLCNHPALIYDKCVEEEEGFMGALDLFPAGYSTKSVEPQLSGKMLVLDYILAVTKSTSNDKVVLVSNYTQTLDLFEKLCRNRRYLYVRLDGTMSIKKRAKVVERFNSPSSPEFIFMLSSKAGGCGLNLIGANRLVMFDPDWNPANDEQAMARVWRDGQKKTCYIYRLLSTGTIEEKIFQRQTHKKALSSCVVDEEQDVERHFSLGELKELFSLNETTISDTHDKIKCRRCVNGHQVRPPPEGSDCTSDLSQWNHCADKRGLQDSVLKAAWDAAVTFTFHHHSHEEQRGIP | Function: Plays an essential role in homologous recombination (HR) which is a major pathway for repairing DNA double-strand breaks (DSBs), single-stranded DNA (ssDNA) gaps, and stalled or collapsed replication forks. Acts as a molecular motor during the homology search and guides RAD51 ssDNA along a donor dsDNA thereby changing the homology search from the diffusion-based mechanism to a motor-guided mechanism. Plays also an essential role in RAD51-mediated synaptic complex formation which consists of three strands encased in a protein filament formed once homology is recognized. Once DNA strand exchange occured, dissociates RAD51 from nucleoprotein filaments formed on dsDNA.
PTM: Acetylated. Acetylation promotes interaction with BRD9, and subsequently with RAD54, which is essential for homologous recombination (HR).
Sequence Mass (Da): 82765
Sequence Length: 733
Subcellular Location: Nucleus
EC: 3.6.4.-
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F1Q8K0 | MRRSLAPSQVAKRKQGPDSDDEEDWEPDMEPQCKRDCREKYISPYRKPLTPLTNRPFCADGNEHEAFIRKILSKPFKIPIPNYTGVLGLRALGLRRAGVRKALHDPFEDGALVLYEPPVISAHDLIKADKEKLPVHVVVDPVLSKVLRPHQREGVKFLWDCVTGRRIENSYGCIMADEMGLGKTLQCITLIWTLLKQSPDCKPEIDKVIVVSPSSLVRNWYNEVGKWLGGRVQPVAIDGGSKDEIDSKLVNFISQQGMRIPTPILIISYETFRLHAEVLHKGKVGLVICDEGHRLKNSDNQTYLALNSMNAQRRVLISGTPIQNDLLEYFSLVHFVNSGILGTAQEFKKRFEIPILKGRDADASDKDRAAGEQKLQELISIVNRCLIRRTSDILSKYLPVKIEQVVCCNLTPLQKELYKLFLKQAKPVESLQTGKISVSSLSSITSLKKLCNHPALIYEKCLTGEEGFDGALDLFPQNYSTKAVEPQLSGKMLVLDYILAMTRTTTSDKVVLVSNYTQTLDLFEKLCRNRRYLYVRLDGTMSIKKRAKIVERFNNPSSPEFIFMLSSKAGGCGLNLIGANRLVMFDPDWNPANDEQAMARVWRDGQKKTCYIYRLLSTGTIEEKILQRQAHKKALSSCVVDEEQDVERHFSLGELRELFSLNEKTLSDTHDRFRCRRCVNGRQVRPPPDDSDCTCDLSNWHHCADKRGLRDPVLQASWDAAVSFVFHQRSHEDQRGVV | Function: Plays an essential role in homologous recombination (HR) which is a major pathway for repairing DNA double-strand breaks (DSBs), single-stranded DNA (ssDNA) gaps, and stalled or collapsed replication forks . Acts as a molecular motor during the homology search and guides RAD51 ssDNA along a donor dsDNA thereby changing the homology search from the diffusion-based mechanism to a motor-guided mechanism. Also plays an essential role in RAD51-mediated synaptic complex formation which consists of three strands encased in a protein filament formed once homology is recognized. Once DNA strand exchange occured, dissociates RAD51 from nucleoprotein filaments formed on dsDNA (By similarity).
PTM: Phosphorylated. Phosphorylations at Ser-566 and Ser-567 allow efficient removal of RAD51 filaments from DNA.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 83737
Sequence Length: 738
EC: 3.6.4.12
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O76460 | MRRSLAPSQRGPLRPESRHSFTPPLLKKNKRSCQQELEREQELDRRRLGALRDASNTSELPLPIRFTANSEYELAIAKVLARKFKVPMDNYVPDYGGKRVLGVRRCISRRPLHDPMACNALVLFHPPAYTEHERMGMDPTKVLVHVVVDPLLSNILRPHQREGVRFMYECVEGKRGNFNGCIMADEMGLGKTLQCVTLVWTLLRQGPECKPTINKAIVVSPSSLVKNWEKEFTKWLHGRLLCLPMEGGTKENTIRALEQFSMTSARLGTPVLLISYETFRIYAEILCKYEVGMVICDEGHRLKNSDNLTYQALMGLKTKRRVLLSGTPIQNDLTEYYSLVNFVNPEMLGTAAVFKRNFESAILRGQNTDSTEQERQRAIEKTQELIGLVDQCIIRRTNQILTKYLPVKFEMVICAKLTAIQLELYTNFLKSDQVRRSLADCNEKASLTALADITTLKKICSHPDLIYEKLTAREKGFENSQNVLPSNYKPKDLNPELSGKFMLLDFMLAAIRAEGNDKVVLISNYTQTLDLFEQLARKRKYGFVRLDGTMSIKKRSKVVDRFNDPESDSFLFMLSSKAGGCGLNLIGANRLFMFDPDWNPANDEQAMARVWRDGQKKPCYIYRLVASGSIEEKILQRQTHKKSLSSTIIDNNESAEKHFTRDDLKDLFTFDANILSDTHDKLKCKRCVQNIQMKPPPEDTDCTSHLSQWYHCSNNRGLPDNILAQAWMDCKCVSFVFHHRSQAQEIVPSAEEEATDQPEEKPESRKRSSTPASDDSADEDFRGF | Function: Involved in mitotic DNA repair and meiotic recombination. Functions in the recombinational DNA repair pathway. Essential for interhomolog gene conversion (GC), but may have a less important role in intersister GC than spn-A/Rad51. In the presence of DNA, spn-A/Rad51 enhances the ATPase activity of okr/Rad54.
Sequence Mass (Da): 89534
Sequence Length: 784
Subcellular Location: Nucleus
EC: 3.6.4.-
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Q92698 | MRRSLAPSQLAKRKPEGRSCDDEDWQPGLVTPRKRKSSSETQIQECFLSPFRKPLSQLTNQPPCLDSSQHEAFIRSILSKPFKVPIPNYQGPLGSRALGLKRAGVRRALHDPLEKDALVLYEPPPLSAHDQLKLDKEKLPVHVVVDPILSKVLRPHQREGVKFLWECVTSRRIPGSHGCIMADEMGLGKTLQCITLMWTLLRQSPECKPEIDKAVVVSPSSLVKNWYNEVGKWLGGRIQPLAIDGGSKDEIDQKLEGFMNQRGARVSSPILIISYETFRLHVGVLQKGSVGLVICDEGHRLKNSENQTYQALDSLNTSRRVLISGTPIQNDLLEYFSLVHFVNSGILGTAHEFKKHFELPILKGRDAAASEADRQLGEERLRELTSIVNRCLIRRTSDILSKYLPVKIEQVVCCRLTPLQTELYKRFLRQAKPAEELLEGKMSVSSLSSITSLKKLCNHPALIYDKCVEEEDGFVGALDLFPPGYSSKALEPQLSGKMLVLDYILAVTRSRSSDKVVLVSNYTQTLDLFEKLCRARRYLYVRLDGTMSIKKRAKVVERFNSPSSPDFVFMLSSKAGGCGLNLIGANRLVMFDPDWNPANDEQAMARVWRDGQKKTCYIYRLLSAGTIEEKIFQRQSHKKALSSCVVDEEQDVERHFSLGELKELFILDEASLSDTHDRLHCRRCVNSRQIRPPPDGSDCTSDLAGWNHCTDKWGLRDEVLQAAWDAASTAITFVFHQRSHEEQRGLR | Function: Plays an essential role in homologous recombination (HR) which is a major pathway for repairing DNA double-strand breaks (DSBs), single-stranded DNA (ssDNA) gaps, and stalled or collapsed replication forks . Acts as a molecular motor during the homology search and guides RAD51 ssDNA along a donor dsDNA thereby changing the homology search from the diffusion-based mechanism to a motor-guided mechanism. Also plays an essential role in RAD51-mediated synaptic complex formation which consists of three strands encased in a protein filament formed once homology is recognized. Once DNA strand exchange occured, dissociates RAD51 from nucleoprotein filaments formed on dsDNA (By similarity).
PTM: Acetylated. Acetylation promotes interaction with BRD9, and subsequently with RAD54, which is essential for homologous recombination (HR).
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 84352
Sequence Length: 747
Subcellular Location: Nucleus
EC: 3.6.4.12
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P41410 | MIQQPTTAKPRISTSSKLNTVLSKNKENVPGKLFKKFKCPSLVISEKRKELPLRKKPRVNYSEYGSVDGKYDSAYVSENVSGLATIKEANRLILNHERRDPSTVIKKQFSVPKPIKGHEDISKLCAHRPPPTLGMKRKVDFIPRPLYDPADEFAIVLYDPTTDADEIIPDIKEVLAEKRKKDELLKNRKGKKEISDSEPESDHDSCVSTDTVASCSTEQSLITSNTSKHRRPNKSLKDLLGIQKEKPPPPPVAVVIDPKLARILRPHQIEGVKFLYKCVTGRIDRCANGCIMADEMGLGKTLQCIALLWTLLKQSPQAGKPTIEKAIITCPSSLVKNWANELVKWLGKDAITPFILDGKSSKQELIMALQQWASVHGRQVTRPVLIASYETLRSYVEHLNNAEIGMLLCDEGHRLKNSDSLTFTALDKLNVQRRVILSGTPIQNDLSEYFSLLNFANPGLLGSRQEFRKNYEIPILKGRDADGTEKDKENGDAKLAELAKIVNRFIIRRTNDILSKYLPVKYEHVVFCNLSEFQLSLYKHFITSPEINKILRGTGSQPLKAIGLLKKICNHPDLLNLTEDLEGCEALFPPGFIPRELRGRDRNIDSSLSGKMLVLERMLYQIKQETDDKIVLISNYTSTLDLFEQLCRARGYKALRLDGTMNVNKRQRLVDTFNDPEKDAFVFLLSSKAGGCGINLIGANRLILFDPDWNPAADQQALARVWRDGQKKDCFVYRFIATGTIEEKIFQRQSHKQSLSSCVVDEAQDVERHFSLDNLRQLFQLNDHTVCETHETYKCKRCRDGKQFIRAPAMLYGDTSTWNHFTNPTLDRIEDHLLKREAGKQQVSTVFQYKSH | Function: Plays an essential role in homologous recombination (HR) which is a major pathway for repairing DNA double-strand breaks (DSBs), single-stranded DNA (ssDNA) gaps, and stalled or collapsed replication forks. Acts as a molecular motor during the homology search and guides RAD51 ssDNA along a donor dsDNA thereby changing the homology search from the diffusion-based mechanism to a motor-guided mechanism. Plays also an essential role in RAD51-mediated synaptic complex formation which consists of three strands encased in a protein filament formed once homology is recognized. Once DNA strand exchange occured, dissociates RAD51 from nucleoprotein filaments formed on dsDNA.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 96654
Sequence Length: 852
Subcellular Location: Nucleus
EC: 3.6.4.12
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P32863 | MARRRLPDRPPNGIGAGERPRLVPRPINVQDSVNRLTKPFRVPYKNTHIPPAAGRIATGSDNIVGGRSLRKRSATVCYSGLDINADEAEYNSQDISFSQLTKRRKDALSAQRLAKDPTRLSHIQYTLRRSFTVPIKGYVQRHSLPLTLGMKKKITPEPRPLHDPTDEFAIVLYDPSVDGEMIVHDTSMDNKEEESKKMIKSTQEKDNINKEKNSQEERPTQRIGRHPALMTNGVRNKPLRELLGDSENSAENKKKFASVPVVIDPKLAKILRPHQVEGVRFLYRCVTGLVMKDYLEAEAFNTSSEDPLKSDEKALTESQKTEQNNRGAYGCIMADEMGLGKTLQCIALMWTLLRQGPQGKRLIDKCIIVCPSSLVNNWANELIKWLGPNTLTPLAVDGKKSSMGGGNTTVSQAIHAWAQAQGRNIVKPVLIISYETLRRNVDQLKNCNVGLMLADEGHRLKNGDSLTFTALDSISCPRRVILSGTPIQNDLSEYFALLSFSNPGLLGSRAEFRKNFENPILRGRDADATDKEITKGEAQLQKLSTIVSKFIIRRTNDILAKYLPCKYEHVIFVNLKPLQNELYNKLIKSREVKKVVKGVGGSQPLRAIGILKKLCNHPNLLNFEDEFDDEDDLELPDDYNMPGSKARDVQTKYSAKFSILERFLHKIKTESDDKIVLISNYTQTLDLIEKMCRYKHYSAVRLDGTMSINKRQKLVDRFNDPEGQEFIFLLSSKAGGCGINLIGANRLILMDPDWNPAADQQALARVWRDGQKKDCFIYRFISTGTIEEKIFQRQSMKMSLSSCVVDAKEDVERLFSSDNLRQLFQKNENTICETHETYHCKRCNAQGKQLKRAPAMLYGDATTWNHLNHDALEKTNDHLLKNEHHYNDISFAFQYISH | Function: Plays an essential role in homologous recombination (HR) which is a major pathway for repairing DNA double-strand breaks (DSBs), single-stranded DNA (ssDNA) gaps, and stalled or collapsed replication forks . Acts as a molecular motor during the homology search and guides RAD51 ssDNA along a donor dsDNA thereby changing the homology search from the diffusion-based mechanism to a motor-guided mechanism . Also plays an essential role in RAD51-mediated synaptic complex formation which consists of three strands encased in a protein filament formed once homology is recognized . Once DNA strand exchange occured, dissociates RAD51 from nucleoprotein filaments formed on dsDNA .
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 101754
Sequence Length: 898
Subcellular Location: Nucleus
EC: 3.6.4.12
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Q2YMH5 | MAKTRVQFICQNCGAVHSRWAGKCDSCGEWNTLIEEGTNSGIGSGPAAMLSKRKGRAVALTSLSGEIEDAPRIVSGISELDRVTGGGFVRGSALLIGGDPGIGKSTLLTQAAAALSNRGHRIVYVSGEEAVAQIRLRAQRLGVAASAVELAAETNVEDIIATISSDNSGSKRPDLVIIDSIQTLWTDMADSAPGTVTQVRSSAQAMIRYAKQTGAAVVLVGHVTKDGQIAGPRVVEHMVDGVLYFEGEGGHHYRILRTVKNRFGPTDEIGVFEMSDGGLREVSNPSELFLGERNEKSPGAAVFAGMEGTRPVLVEIQALVAPSSLGTPRRAVVGWDGGRLAMILAVLESHCGVRFGQHDVYLNVAGGYRISEPAADIAVAAALVSSMAGIALPPDCVYFGEISLSGAVRAVSHAVQRLKEAEKLGFRQAEVPNGSGELWKDRNFRLMETAALADLVARIAASGAGKK | Function: DNA-dependent ATPase involved in processing of recombination intermediates, plays a role in repairing DNA breaks. Stimulates the branch migration of RecA-mediated strand transfer reactions, allowing the 3' invading strand to extend heteroduplex DNA faster. Binds ssDNA in the presence of ADP but not other nucleotides, has ATPase activity that is stimulated by ssDNA and various branched DNA structures, but inhibited by SSB. Does not have RecA's homology-searching function.
Sequence Mass (Da): 49024
Sequence Length: 467
Domain: Has a putative N-terminal zinc-finger, a middle region with homology to RecA with ATPase motifs including the RadA KNRFG motif, while the C-terminus is homologous to Lon protease.
EC: 3.6.4.-
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Q9PK96 | MTTTKIKTQWACSECGSYSPKWLGQCPGCFQWNTLVEEIHSSKLKTSSYPLSSTTPVPLNTVKFQEEIRISTRSKGWNRLLGGGTVCGSLTLLGGEPGIGKSTLLLQISSQFAEQGYKVLYVCGEESVSQTSLRAQRLQISSSNIFLFPETNLEDIKQQISDLAPDILIIDSIQIIFSPSLSSAPGSVAQVRETTAELMHIAKQKQITTFIIGHVTKSGEIAGPRILEHLVDTVLYFEGNAHTNYRMIRSVKNRFGPTNELLILSMQTDGLHEVENPSGFFLQEKVVETTGSTIIPIVEGSETLLVEVQALVSSSPFSNPVRKTSGFDPNRFSLLLAVLEKRANVKLYTSDVFLSIAGGLKITQPSADLGAVLSVVSSLYNRYLPKNYTYTGEIGLGGEIRHVTHIEHRIKESIIMGFKGIVMPSGQIKGLPKEYLDQIDIIGVKTIKDAVRLLQ | Function: DNA-dependent ATPase involved in processing of recombination intermediates, plays a role in repairing DNA breaks. Stimulates the branch migration of RecA-mediated strand transfer reactions, allowing the 3' invading strand to extend heteroduplex DNA faster. Binds ssDNA in the presence of ADP but not other nucleotides, has ATPase activity that is stimulated by ssDNA and various branched DNA structures, but inhibited by SSB. Does not have RecA's homology-searching function.
Sequence Mass (Da): 49951
Sequence Length: 455
Domain: Has a putative N-terminal zinc-finger, a middle region with homology to RecA with ATPase motifs including the RadA KNRFG motif, while the C-terminus is homologous to Lon protease.
EC: 3.6.4.-
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Q9RVC4 | MERVAVLFRRTCNSENCSKGRRPLRERPLAGLFFCSLPAPLSIPCLSLPGSNPGDFVPKVKTNYICNSCGYQSAKPLGRCPNCQAWNSFEEEVPTASTSGKSGRGGLGGYGGVKGGKLTPLSTVGRREEPRTPSGIPELDRVLGGGLVAGGVTLIGGEPGIGKSTLLLQVADKVASRGGTVLYVAGEESLEQIRLRADRLGVAADLQMTRDTRAEHIAALLEEHKPALCIVDSIQTVTVEGEGAPGGVAQVRDGTAMLTRAAKETGTATVLVGHVTKDGTVAGPKVMEHIVDTTVFLETVGAFRLLRSVKNRFGQAGELGVFEMRGEGLIAVDNPSAAFLAERPLDVPGSVVAATVDGQRPMLLEVQALASKTPYPNARRVVVGLDPRRVDVVLAVLERRLDLTLGGLDVYVNLAGGLKVPDPGLDLAVALAVYSAVVGRALPQNVAVFGEVGLAGEVRSTQMALRRAEEAGRAGYKRLVVPPGLDGQAGVKSVEEAVKAVWR | Function: DNA-dependent ATPase involved in processing of recombination intermediates, plays a role in repairing DNA breaks. Stimulates the branch migration of RecA-mediated strand transfer reactions, allowing the 3' invading strand to extend heteroduplex DNA faster. Binds ssDNA in the presence of ADP but not other nucleotides, has ATPase activity that is stimulated by ssDNA and various branched DNA structures, but inhibited by SSB. Does not have RecA's homology-searching function.
Sequence Mass (Da): 52758
Sequence Length: 503
Domain: Has a putative N-terminal zinc-finger, a middle region with homology to RecA with ATPase motifs including the RadA KNRFG motif, while the C-terminus is homologous to Lon protease (By similarity). Absence of the zinc-finger domain gives a slight increase in sensitivity to gamma and UV irradiation, absence of the Lon protease domain gives slightly increased resistance to gamma and UV irradiation.
EC: 3.6.4.-
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P24554 | MAKAPKRAFVCNECGADYPRWQGQCSACHAWNTITEVRLAASPMVARNERLSGYAGSAGVAKVQKLSDISLEELPRFSTGFKEFDRVLGGGVVPGSAILIGGNPGAGKSTLLLQTLCKLAQQMKTLYVTGEESLQQVAMRAHRLGLPTDNLNMLSETSIEQICLIAEEEQPKLMVIDSIQVMHMADVQSSPGSVAQVRETAAYLTRFAKTRGVAIVMVGHVTKDGSLAGPKVLEHCIDCSVLLDGDADSRFRTLRSHKNRFGAVNELGVFAMTEQGLREVSNPSAIFLSRGDEVTSGSSVMVVWEGTRPLLVEIQALVDHSMMANPRRVAVGLEQNRLAILLAVLHRHGGLQMADQDVFVNVVGGVKVTETSADLALLLAMVSSLRDRPLPQDLVVFGEVGLAGEIRPVPSGQERISEAAKHGFRRAIVPAANVPKKAPEGMQIFGVKKLSDALSVFDDL | Function: DNA-dependent ATPase involved in processing of recombination intermediates, plays a role in repairing DNA breaks. Stimulates the branch migration of RecA-mediated strand transfer reactions, allowing the 3' invading strand to extend heteroduplex DNA faster. Binds ssDNA in the presence of ADP but not other nucleotides, has ATPase activity that is stimulated by ssDNA and various branched DNA structures, but inhibited by SSB. Does not have RecA's homology-searching function . Genetic experiments involving combination of radA mutations with mutations in recA, recB, recG, recJ, recQ, ruvA and ruvC show it plays a role in recombination and recombinational repair, probably involving stabilizing or processing branched DNA or blocked replication forks. Is genetically synergistic to RecG and RuvABC . May be involved in recovery of genetic rearrangements during replication fork breakdown . In combination with RadD is important in recovery from double-strand DNA breaks (DSB) .
Sequence Mass (Da): 49472
Sequence Length: 460
Domain: Has a putative N-terminal zinc-finger, a region with homology to RecA with ATPase motifs including the RadA KNRFG motif (approximately residues 60-290), while the C-terminus is homologous to Lon protease (from about residue 290 to the end, the ribosomal S5 domain). In this organism the Lon protease active site Ser-372 is conserved, but not all other bacteria encode Ser at this position . Mutation of Ser-372 has no discernible effect on RadA function, suggesting RadA is not a protease .
EC: 3.6.4.-
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P56148 | MAKKTSLFECQHCGFTSPKWLGKCVQCNAWESFIELNQAQKEVLNTLKKPIPQAQKSVSIAAIEHEEVIKFSSTQSELDIVLGGGIAKGGLYLVGGSPGVGKSTLLLKVASGLAKNQQKVLYVSGEESLSQIKMRAIRLDCIEKELYLLNEINWPVIKANIESENYFACVIDSIQTLYSPEISSAPGSISQVREITFELMRLAKTRDIAIFIIGHITKEGSIAGPRVLEHMVDSVLYFEGDPSRELRILRSFKNRFGPTSEIGLFEMKEQGLVSAKEASSLFFSKEEPMEGSAITITLEGSRALILEIQALVSECSFGSPKRLANGFDTNRLNMLIALLEKKLEIPLNRHDVFINVSGGIKISEPACDLAVIASILSSFKNRKIDNKTAFLGEVSLNGRILEAPNLNARLKEMENYGFLKAILPKKPSQKTSIKCYEANAVGKIVEWM | Function: DNA-dependent ATPase involved in processing of recombination intermediates, plays a role in repairing DNA breaks. Stimulates the branch migration of RecA-mediated strand transfer reactions, allowing the 3' invading strand to extend heteroduplex DNA faster. Binds ssDNA in the presence of ADP but not other nucleotides, has ATPase activity that is stimulated by ssDNA and various branched DNA structures, but inhibited by SSB. Does not have RecA's homology-searching function.
Sequence Mass (Da): 49451
Sequence Length: 448
Domain: Has a putative N-terminal zinc-finger, a middle region with homology to RecA with ATPase motifs including the RadA KNRFG motif, while the C-terminus is homologous to Lon protease.
EC: 3.6.4.-
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O13034 | MSLQPLTAVNCGSLVQPGFSLLDLEGDVYLFGQKGWPKRSCPTGIFGVRIKKGELKLRAISFSNNSSYLPPLRCPAIAHFEAQDGKPECYLIHGGRTPNNELSSSLYMLSVDSRGCNRKVTLRCEEKELVGDVPSARYGHTLSVINSRGKTACVLFGGRSYMPPTERTTQNWNSVGDCPPQVYLIDLEFGCCTAHTLPELTDGQSFHVALARQDCVYFLGGHILSSDCRPSRLIRLHVELLLGSPVLTCTILHEGLTITSAIASPIGYHEYIIFGGYQSETQKRMECTYVGLDDVGVHMESREPPQWTSEISHSRTWFGGSLGKGTALVAIPSEGNPTPPEAYHFYQVSFQKEQDGEATAQGCSQESTDFEDSAPLEDSEELYFGREPHELEYSSDVEGDTYNEEDEEDESQTGYWIKCCLSCQVDPNIWEPYYSTELTRPAMIFCSRGEGGHWVHAQCMELPESLLLQLSQDNSKYFCLDHGGLPKQEMTPPKQMLPVKRVPMKMTHRKAPVSLKMTPAKKTFLRRLFD | Function: Core component of the RAG complex, a multiprotein complex that mediates the DNA cleavage phase during V(D)J recombination. V(D)J recombination assembles a diverse repertoire of immunoglobulin and T-cell receptor genes in developing B and T lymphocytes through rearrangement of different V (variable), in some cases D (diversity), and J (joining) gene segments. DNA cleavage by the RAG complex occurs in 2 steps: a first nick is introduced in the top strand immediately upstream of the heptamer, generating a 3'-hydroxyl group that can attack the phosphodiester bond on the opposite strand in a direct transesterification reaction, thereby creating 4 DNA ends: 2 hairpin coding ends and 2 blunt, 5'-phosphorylated ends. In the RAG complex, rag2 is not the catalytic component but is required for all known catalytic activities mediated by RAG1. It probably acts as a sensor of chromatin state that recruits the RAG complex to H3K4me3 (By similarity).
Sequence Mass (Da): 59174
Sequence Length: 530
Domain: The atypical PHD-type zinc finger recognizes and binds histone H3 trimethylated on 'Lys-4' (H3K4me3). The atypical PHD-type zinc finger also binds various phosphoinositides (By similarity).
Subcellular Location: Nucleus
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P21784 | MSLQMVTVGHNIALIQPGFSLMNFDGQVFFFGQKGWPKRSCPTGVFHFDIKQNHLKLKPAIFSKDSCYLPPLRYPATCSYKGSIDSDKHQYIIHGGKTPNNELSDKIYIMSVACKNNKKVTFRCTEKDLVGDVPEPRYGHSIDVVYSRGKSMGVLFGGRSYMPSTQRTTEKWNSVADCLPHVFLIDFEFGCATSYILPELQDGLSFHVSIARNDTVYILGGHSLASNIRPANLYRIRVDLPLGTPAVNCTVLPGGISVSSAILTQTNNDEFVIVGGYQLENQKRMVCSLVSLGDNTIEISEMETPDWTSDIKHSKIWFGSNMGNGTIFLGIPGDNKQAMSEAFYFYTLRCSEEDLSEDQKIVSNSQTSTEDPGDSTPFEDSEEFCFSAEATSFDGDDEFDTYNEDDEDDESVTGYWITCCPTCDVDINTWVPFYSTELNKPAMIYCSHGDGHWVHAQCMDLEERTLIHLSEGSNKYYCNEHVQIARALQTPKRNPPLQKPPMKSLHKKGSGKVLTPAKKSFLRRLFD | Function: Core component of the RAG complex, a multiprotein complex that mediates the DNA cleavage phase during V(D)J recombination. V(D)J recombination assembles a diverse repertoire of immunoglobulin and T-cell receptor genes in developing B and T-lymphocytes through rearrangement of different V (variable), in some cases D (diversity), and J (joining) gene segments. DNA cleavage by the RAG complex occurs in 2 steps: a first nick is introduced in the top strand immediately upstream of the heptamer, generating a 3'-hydroxyl group that can attack the phosphodiester bond on the opposite strand in a direct transesterification reaction, thereby creating 4 DNA ends: 2 hairpin coding ends and 2 blunt, 5'-phosphorylated ends. The chromatin structure plays an essential role in the V(D)J recombination reactions and the presence of histone H3 trimethylated at 'Lys-4' (H3K4me3) stimulates both the nicking and haipinning steps. The RAG complex also plays a role in pre-B cell allelic exclusion, a process leading to expression of a single immunoglobulin heavy chain allele to enforce clonality and monospecific recognition by the B-cell antigen receptor (BCR) expressed on individual B-lymphocytes. The introduction of DNA breaks by the RAG complex on one immunoglobulin allele induces ATM-dependent repositioning of the other allele to pericentromeric heterochromatin, preventing accessibility to the RAG complex and recombination of the second allele. In the RAG complex, RAG2 is not the catalytic component but is required for all known catalytic activities mediated by RAG1. It probably acts as a sensor of chromatin state that recruits the RAG complex to H3K4me3.
Sequence Mass (Da): 59074
Sequence Length: 527
Domain: The atypical PHD-type zinc finger recognizes and binds histone H3 trimethylated on 'Lys-4' (H3K4me3). The presence Tyr-445 instead of a carboxylate in classical PHD-type zinc fingers results in an enhanced binding to H3K4me3 in presence of dimethylated on 'Arg-2' (H3R2me2) rather than inhibited. The atypical PHD-type zinc finger also binds various phosphoinositides, such as phosphatidylinositol 3,4-bisphosphate binding (PtdIns(3,4)P2), phosphatidylinositol 3,5-bisphosphate binding (PtdIns(3,5)P2), phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) and phosphatidylinositol 3,4,5-trisphosphate binding (PtdIns(3,4,5)P3).
Subcellular Location: Nucleus
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O04157 | MSTRRRTLLKVIILGDSGVGKTSLMNQYVNNKFSQQYKATIGADFVTKELQIDDRLVTLQIWDTAGQERFQSLGVAFYRGADCCVLVYDVNHLKSFESLDNWHNEFLTRASPRDPMAFPFILLGNKVDIDGGNSRVVSEKKAREWCAEKGNIVYFETSAKEDYNVDDSFLCITKLALANERDQDIYFQPDTGSVPEQRGGCAC | Function: Intracellular vesicle trafficking and protein transport. Functions in autophagy. Involved in xylem and tracheary element differentiation.
Location Topology: Lipid-anchor
Sequence Mass (Da): 22945
Sequence Length: 203
Subcellular Location: Cell membrane
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Q9LW76 | MASRRRVLLKVIILGDSGVGKTSLMNQFVNRKFSNQYKATIGADFLTKEVQIDDRIFTLQIWDTAGQERFQSLGVAFYRGADCCVLVNDVNVMKSFENLNNWREEFLIQASPSDPENFPFVVLGNKTDVDGGKSRVVTEKKAKSWCASKGNIPYFETSAKDGVNVDAAFECIAKNALKNEPEEEVYLPDTIDVAGARQQRSTGCEC | Function: Intracellular vesicle trafficking and protein transport.
Location Topology: Lipid-anchor
Sequence Mass (Da): 22966
Sequence Length: 206
Subcellular Location: Cell membrane
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Q9XI98 | MPSRRRTLLKVIILGDSGVGKTSLMNQYVNKKFSNQYKATIGADFLTKEVQFEDRLFTLQIWDTAGQERFQSLGVAFYRGADCCVLVYDVNSAKSFEDLNNWREEFLIQASPSDPENFPFVVIGNKIDVDGGSSRVVSEKKARAWCASKGNIPYYETSAKVGTNVEDAFLCITTNAMKSGEEEEMYLPDTIDVGTSNPQRSTGCEC | Function: Intracellular vesicle trafficking and protein transport. May play a role in adaptation to stress by recylcing macromolecules in specific cellular compartments.
Location Topology: Lipid-anchor
Sequence Mass (Da): 22980
Sequence Length: 206
Subcellular Location: Cell membrane
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Q9LS94 | MPSRRRTLLKVIILGDSGVGKTSLMNQYVNKKFSNQYKATIGADFLTKEVQFEDRLFTLQIWDTAGQERFQSLGVAFYRGADCCVLVYDVNSMKSFENLNNWREEFLIQASPSDPENFPFVLIGNKVDVDDGNSRVVSEKKAKAWCASKGNIPYFETSAKVGTNVEEAFQCIAKDALKSGEEEELYLPDTIDVGTSNQQRSTGCEC | Function: Essential for trafficking from prevacuolar compartments to vacuoles. Involved in the trafficking of newly synthesized protein to vacuoles. Essential for plant growth . Participates in the recruitment of the core retromer components to the endosomal membrane by interacting with VPS35A .
Location Topology: Lipid-anchor
Sequence Mass (Da): 23102
Sequence Length: 206
Subcellular Location: Endosome membrane
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O74824 | MRKKVLLMGRSGSGKSSMRSIVFSNYVAKDTRRLGATIDIEHSHVRFLGNLVLNLWDCGGQEAFMENYLSAQRDHIFRNVQVLIYVFDVESREFERDLVTFRNCLEATVANSPQARVFCLIHKMDLVQEDLRDLVFEERKAILLETSKDLETTCLATSIWDETLFKAWSAIVYTLIPNTPTLESHLREFAKAAEAAEVILFERTTFLVISSYSSESNPATDAHRFEKISNIVKQFKLSCSKMQAQFTTFELRGGNFSAFIVPYTEDTYILVVIADPEIESAVTLMNIQSARRFIEASKSASDGIQLQP | Function: GTPase involved in activation of the TORC1 signaling pathway, which promotes growth and represses autophagy in nutrient-rich conditions (By similarity). Also required for TORC1 inactivation during nitrogen starvation (By similarity).
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 35010
Sequence Length: 308
Subcellular Location: Vacuole membrane
EC: 3.6.5.-
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Q00582 | MSSNNRKKLLLMGRSGSGKSSMRSIIFSNYSAFDTRRLGATIDVEHSHLRFLGNMTLNLWDCGGQDVFMENYFTKQKDHIFQMVQVLIHVFDVESTEVLKDIEIFAKALKQLRKYSPDAKIFVLLHKMDLVQLDKREELFQIMMKNLSETSSEFGFPNLIGFPTSIWDESLYKAWSQIVCSLIPNMSNHQSNLKKFKEIMNALEIILFERTTFLVICSSNGENSNENHDSSDNNNVLLDPKRFEKISNIMKNFKQSCTKLKSGFKTLILNNNIYVSELSSNMVCFIVLKDMNIPQELVLENIKKAKEFFQ | Function: GTPase involved in activation of the TORC1 signaling pathway, which promotes growth and represses autophagy in nutrient-rich conditions . Also required for TORC1 inactivation during nitrogen starvation . Required for intracellular sorting of GAP1 out of the endosome . Functionally associated with the inorganic phosphate transporter PHO84, and may be involved in regulating its function or localization .
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 35847
Sequence Length: 310
Subcellular Location: Vacuole membrane
EC: 3.6.5.-
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O74544 | MKPRKIILMGLRRSGKSSIQKVVFYKMPPNETLFLESTSKLTQDHISSFIDFSVWDFPGQVDVFDAAFDFESIFTQVGALIFVIDAQDDYLDALARLHVTVARVVTINPNICIEVFIHKVDGLSDEFKIDTQRDIQQRTQDELADIGLENVPISFHLTSIFDHSIFEAFSRVIQKLIPQLPTLENLLNIFCSNSLVEKAYLFDVLSKIYVATDSSPVDVQSYEICSDFIDVILDIGSIYGRSSQLKPGHSPEILDETSSVIRLSNDLVLFLREMNQYLALICIVRADNFEKSGLIEYNVQCLQTAIQSIFSPRT | Function: GTPase involved in activation of the TORC1 signaling pathway, which promotes growth and represses autophagy in nutrient-rich conditions (By similarity). Also required for TORC1 inactivation during nitrogen starvation (By similarity).
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 35592
Sequence Length: 314
Subcellular Location: Vacuole membrane
EC: 3.6.5.-
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Q9VZ23 | MAQEGQDIPTFKCVLVGDGGTGKTTFVKRHMTGEFEKKYVATLGVEVHPLIFHTNRGAIRFNVWDTAGQEKFGGLRDGYYIQGQCAVIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLVGDPNLEFVAMPALLPPEVKMDKDWQAQIERDLQEAQATALPDEDEEL | Cofactor: Mg(2+) interacts primarily with the phosphate groups of the bound guanine nucleotide.
Function: GTPase involved in nucleocytoplasmic transport, participating both to the import and the export from the nucleus of proteins and RNAs. Switches between a cytoplasmic GDP- and a nuclear GTP-bound state by nucleotide exchange and GTP hydrolysis. Nuclear import receptors such as importin beta bind their substrates only in the absence of GTP-bound RAN and release them upon direct interaction with GTP-bound RAN, while export receptors behave in the opposite way. Thereby, RAN controls cargo loading and release by transport receptors in the proper compartment and ensures the directionality of the transport. Interaction with RANBP1 induces a conformation change in the complex formed by XPO1 and RAN that triggers the release of the nuclear export signal of cargo proteins. RAN (GTP-bound form) triggers microtubule assembly at mitotic chromosomes and is required for normal mitotic spindle assembly and chromosome segregation. Required for normal progress through mitosis (By similarity). GTP-bound Ran modulates both spindle and nuclear envelope assembly, supporting a role during mitosis . During oogenesis, modulates formation of Nup358-containing granules and biogenesis of the nuclear pore complex probably by mediating the transport of their components along microtubules .
Sequence Mass (Da): 24708
Sequence Length: 216
Subcellular Location: Nucleus
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P62826 | MAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIKFNVWDTAGQEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFVAMPALAPPEVVMDPALAAQYEHDLEVAQTTALPDEDDDL | Cofactor: Mg(2+) interacts primarily with the phosphate groups of the bound guanine nucleotide.
Function: GTPase involved in nucleocytoplasmic transport, participating both to the import and the export from the nucleus of proteins and RNAs . Switches between a cytoplasmic GDP- and a nuclear GTP-bound state by nucleotide exchange and GTP hydrolysis . Nuclear import receptors such as importin beta bind their substrates only in the absence of GTP-bound RAN and release them upon direct interaction with GTP-bound RAN, while export receptors behave in the opposite way. Thereby, RAN controls cargo loading and release by transport receptors in the proper compartment and ensures the directionality of the transport . Interaction with RANBP1 induces a conformation change in the complex formed by XPO1 and RAN that triggers the release of the nuclear export signal of cargo proteins . RAN (GTP-bound form) triggers microtubule assembly at mitotic chromosomes and is required for normal mitotic spindle assembly and chromosome segregation . Required for normal progress through mitosis . The complex with BIRC5/survivin plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules . Acts as a negative regulator of the kinase activity of VRK1 and VRK2 . Enhances AR-mediated transactivation. Transactivation decreases as the poly-Gln length within AR increases .
PTM: Acetylation by KAT5 at Lys-134 is increased during mitosis, impairs RANGRF binding and enhances RCC1 binding . Acetylation at Lys-37 enhances the association with nuclear export components . Deacetylation of Lys-37 by SIRT7 regulates the nuclear export of NF-kappa-B subunit RELA/p65 .
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 24423
Sequence Length: 216
Subcellular Location: Nucleus
EC: 3.6.5.-
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P62834 | MREYKLVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEVDCQQCMLEILDTAGTEQFTAMRDLYMKNGQGFALVYSITAQSTFNDLQDLREQILRVKDTEDVPMILVGNKCDLEDERVVGKEQGQNLARQWCNCAFLESSAKSKINVNEIFYDLVRQINRKTPVEKKKPKKKSCLLL | Function: Induces morphological reversion of a cell line transformed by a Ras oncogene. Counteracts the mitogenic function of Ras, at least partly because it can interact with Ras GAPs and RAF in a competitive manner. Together with ITGB1BP1, regulates KRIT1 localization to microtubules and membranes. Plays a role in nerve growth factor (NGF)-induced neurite outgrowth. Plays a role in the regulation of embryonic blood vessel formation. Involved in the establishment of basal endothelial barrier function. May be involved in the regulation of the vascular endothelial growth factor receptor KDR expression at endothelial cell-cell junctions.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Location Topology: Lipid-anchor
Sequence Mass (Da): 20987
Sequence Length: 184
Subcellular Location: Cell membrane
EC: 3.6.5.2
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P32253 | MSKLLKLVIVGDGGVGKSALTIQLTQNQFIAEYDPTIENSYRKQVNIDEEVYMLDILDTAGQEEYSAMRDQYIRSGRGFLIVYSIISRASFEAVTTFREQILRVKDLSTYPIVIIGNKADLPDKDRKVPPMEGKELAKSFGAPFLETSAKSRVNVEEAFFTLVREIKRWNQNPQNEEMLPPKKRGCIIL | Function: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Location Topology: Lipid-anchor
Sequence Mass (Da): 21496
Sequence Length: 189
Subcellular Location: Cell membrane
EC: 3.6.5.2
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Q9Y272 | MKLAAMIKKMCPSDSELSIPAKNCYRMVILGSSKVGKTAIVSRFLTGRFEDAYTPTIEDFHRKFYSIRGEVYQLDILDTSGNHPFPAMRRLSILTGDVFILVFSLDNRDSFEEVQRLRQQILDTKSCLKNKTKENVDVPLVICGNKGDRDFYREVDQREIEQLVGDDPQRCAYFEISAKKNSSLDQMFRALFAMAKLPSEMSPDLHRKVSVQYCDVLHKKALRNKKLLRAGSGGGGGDPGDAFGIVAPFARRPSVHSDLMYIREKASAGSQAKDKERCVIS | Function: Small GTPase. Negatively regulates the transcription regulation activity of the APBB1/FE65-APP complex via its interaction with APBB1/FE65 (By similarity).
PTM: S-nitrosylation stimulates guanine-nucleotide exchange activity.
Location Topology: Lipid-anchor
Sequence Mass (Da): 31642
Sequence Length: 281
Subcellular Location: Cell membrane
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P03967 | MTEYKLVIVGGGGVGKSALTIQLIQNHFIDEYDPTIEDSYRKQVSIDDETCLLDILDTAGQEEYSAMRDQYMRTGQGFLCVYSITSRSSYDEIASFREQILRVKDKDRVPLILVGNKADLDHERQVSVNEGQELAKGFNCPFMESSAKSRINVEEAFYSLVREIRKELKGDQSSGKAQKKKKQCLIL | Function: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Location Topology: Lipid-anchor
Sequence Mass (Da): 21202
Sequence Length: 187
Subcellular Location: Cell membrane
EC: 3.6.5.2
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Q8THK1 | MSLNKAVLEIRQRIKVKPSPTNEPAASWTGTDLVNGVQTKTLTVIFKSAGCRWGKAGGCTMCGYVYDCASEPPSLEDYMAQLEKAMRKAEKFPEFMVKIFTSGSFLDEQEVLPEARDAILKNLTEDPRVTKVLVETRPNYVTEENVQACLSILKNKPFELAFGLETSSDKIRRDSINKGFTFQDFVHAAETAKKYGVTVKVYLMLKPLFLSERQAMEDIIRSIDDAAPYADTISINLCNVQKGTLVEALWEKGQYRPPWLWSIIEILRQAKAAHPELPLMSDPVGAGSKRGPHNCKICSSEVADSLRTFSLTQNPADLSTADCECKELWKKVLEIEDFTYGTPILD | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Radical SAM enzyme involved in the synthesis of archaeosine, a modified nucleoside present in the dihydrouridine loop (D-loop) of archaeal tRNAs. Catalyzes the cleavage of the C(epsilon)-N bond of the lysine moiety of q0kN15-tRNA, leading to the formation of archaeosine at position 15 in tRNAs.
Catalytic Activity: 7-N-[(5S)-5-amino-5-carboxypentyl]formamidino-7-deazaguanosine(15) in tRNA + S-adenosyl-L-methionine = 5'-deoxyadenosine + archaeosine(15) in tRNA + 2 H(+) + L-1-piperideine-6-carboxylate + L-methionine
Sequence Mass (Da): 38704
Sequence Length: 346
Pathway: tRNA modification; archaeosine-tRNA biosynthesis.
EC: 4.3.2.-
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Q5JE80 | MTYWTSEDNVAGKPGTALFIILPTIGCYRYRIGQACYMCSYPTAAPKVKWTQEAIVNYVKEALEKIEGTEGPFAVRMFTSGSFLDNGELKPETRRKIFEILAEMDNVEEIVIESRSELVRYEAVKELAEIVPDKHFEVAIGLETANDDVADVSINKGNTFADFVKAAEITHKAGAKVKTYLLLKPIFLSERDGVEDAKESIIKAEPYTDTFSINITDIQKGTLYERLWEKKEYRPPWLWSAVEVLIWAKRKFPNKRILSDPVGAGSKRGPHNCLTDYDRVIGKAIKKFSATQDLSYIENLKPECRDRWEYIVENGLLDWQLVTW | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Radical SAM enzyme involved in the synthesis of archaeosine, a modified nucleoside present in the dihydrouridine loop (D-loop) of archaeal tRNAs. Catalyzes the cleavage of the C(epsilon)-N bond of the lysine moiety of q0kN15-tRNA, leading to the formation of archaeosine at position 15 in tRNAs.
Catalytic Activity: 7-N-[(5S)-5-amino-5-carboxypentyl]formamidino-7-deazaguanosine(15) in tRNA + S-adenosyl-L-methionine = 5'-deoxyadenosine + archaeosine(15) in tRNA + 2 H(+) + L-1-piperideine-6-carboxylate + L-methionine
Sequence Mass (Da): 36996
Sequence Length: 324
Pathway: tRNA modification; archaeosine-tRNA biosynthesis.
EC: 4.3.2.-
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Q7Z444 | MELPTKPGTFDLGLATWSPSFQGETHRAQARRRDVGRQLPEYKAVVVGASGVGKSALTIQLNHQCFVEDHDPTIQDSYWKELTLDSGDCILNVLDTAGQAIHRALRDQCLAVCDGVLGVFALDDPSSLIQLQQIWATWGPHPAQPLVLVGNKCDLVTTAGDAHAAAAALAHSWGAHFVETSAKTRQGVEEAFSLLVHEIQRVQEAMAKEPMARSCREKTRHQKATCHCGCSVA | Function: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. Plays an important role in the tumor-like growth properties of embryonic stem cells (By similarity).
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Location Topology: Lipid-anchor
Sequence Mass (Da): 25287
Sequence Length: 233
Subcellular Location: Cell membrane
EC: 3.6.5.2
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Q7TN89 | MALPTKSSILDLSSGTPCTRSPEESHEAWAQCKDAGRQLPEYKAVVVGASGVGKSALTIQMTHQCFVKDHDPTIQDSYWKEVARDNGGYILNVLDTSGQDIHRALRDQCLASGDGVLGVFALDDPSSLDQLQQIWSTWTPHHKQPLVLVGNKCDLVTTAGDAHAAAALLAHKLGAPLVKTSAKTRQGVEEAFALLVHEIQRAQEAVAESSKKTRHQKAVCSCGCSVA | Function: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. Plays an important role in the tumor-like growth properties of embryonic stem cells.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Location Topology: Lipid-anchor
Sequence Mass (Da): 24321
Sequence Length: 227
Subcellular Location: Cell membrane
EC: 3.6.5.2
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Q15907 | MGTRDDEYDYLFKVVLIGDSGVGKSNLLSRFTRNEFNLESKSTIGVEFATRSIQVDGKTIKAQIWDTAGQERYRAITSAYYRGAVGALLVYDIAKHLTYENVERWLKELRDHADSNIVIMLVGNKSDLRHLRAVPTDEARAFAEKNNLSFIETSALDSTNVEEAFKNILTEIYRIVSQKQIADRAAHDESPGNNVVDISVPPTTDGQKPNKLQCCQNL | Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. The small Rab GTPase RAB11B plays a role in endocytic recycling, regulating apical recycling of several transmembrane proteins including cystic fibrosis transmembrane conductance regulator/CFTR, epithelial sodium channel/ENaC, potassium voltage-gated channel, and voltage-dependent L-type calcium channel. May also regulate constitutive and regulated secretion, like insulin granule exocytosis. Required for melanosome transport and release from melanocytes. Also regulates V-ATPase intracellular transport in response to extracellular acidosis.
PTM: Citrullinated by PADI4.
Location Topology: Lipid-anchor
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 24489
Sequence Length: 218
Subcellular Location: Recycling endosome membrane
EC: 3.6.5.2
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P46638 | MGTRDDEYDYLFKVVLIGDSGVGKSNLLSRFTRNEFNLESKSTIGVEFATRSIQVDGKTIKAQIWDTAGQERYRAITSAYYRGAVGALLVYDIAKHLTYENVERWLKELRDHADSNIVIMLVGNKSDLRHLRAVPTDEARAFAEKNNLSFIETSALDSTNVEEAFKNILTEIYRIVSQKQIADRAAHDESPGNNVVDISVPPTTDGQRPNKLQCCQSL | Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. The small Rab GTPase RAB11B plays a role in endocytic recycling, regulating apical recycling of several transmembrane proteins including cystic fibrosis transmembrane conductance regulator/CFTR, epithelial sodium channel/ENaC, potassium voltage-gated channel, and voltage-dependent L-type calcium channel. May also regulate constitutive and regulated secretion, like insulin granule exocytosis. Required for melanosome transport and release from melanocytes. Also regulates V-ATPase intracellular transport in response to extracellular acidosis.
PTM: Citrullinated by PADI4.
Location Topology: Lipid-anchor
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 24489
Sequence Length: 218
Subcellular Location: Recycling endosome membrane
EC: 3.6.5.2
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Q9LET3 | MNGGPSGFHNAPVTKAFVITSALFTVFFGIQGRSSKLGLSYQDIFEKFRIWKLIMSTFAFSSTPELMFGLYLLYYFRVFERQIGSNKYSVFILFSGTVSLLLEVILLSLLKDTTANLLTSGPYGLIFASFIPFYLDIPVSTRFRVFGVNFSDKSFIYLAGVQLLLSSWKRSIFPGICGIIAGSLYRLNILGIRKAKFPEFVASFFSRLSFPSFGNSPPPAPSRNIVGTISPNTGRRAERSQPAPLPSSVEPSEEAITTLVSMGFDRNAARQALVHARNDVNAATNILLEAQSH | Function: Probable rhomboid-type serine protease that catalyzes intramembrane proteolysis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32378
Sequence Length: 293
Subcellular Location: Membrane
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Q9CAN1 | MANRDVERVGKKNRGANNNYFYEESSGETHWTSWLIPAIVVANLAVFIAVMFVNDCPKKITGPNKECVARFLGRFSFQPLKENPLFGPSSSTLEKMGALEWRKVVHEHQGWRLLSCMWLHAGIIHLLTNMLSLIFIGIRLEQQFGFIRVGLIYLISGLGGSILSSLFLQESISVGASGALFGLLGAMLSELLTNWTIYANKAAALITLLFIIAINLALGMLPRVDNFAHIGGFLTGFCLGFVLLVRPQYGWEASRTNTSRTKRKYSMYQYVLFVVSVVLLVVGLTVALVMLFKGENGNKHCKWCHYLSCFPTSKWTC | Function: Rhomboid-type serine protease that catalyzes intramembrane proteolysis. Can cleave the Drosophila proteins Spitz and Keren . May function in pollen elongation .
Catalytic Activity: Cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35413
Sequence Length: 317
Subcellular Location: Golgi apparatus membrane
EC: 3.4.21.105
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O58677 | MMVLRMKVEWYLDFVDLNYEPGRDELIVEYYFEPNGVSPEEAAGRIASESSIGTWTTLWKLPEMAKRSMAKVFYLEKHGEGYIAKIAYPLTLFEEGSLVQLFSAVAGNVFGMKALKNLRLLDFHPPYEYLRHFKGPQFGVQGIREFMGVKDRPLTATVPKPKMGWSVEEYAEIAYELWSGGIDLLKDDENFTSFPFNRFEERVRKLYRVRDRVEAETGETKEYLINITGPVNIMEKRAEMVANEGGQYVMIDIVVAGWSALQYMREVTEDLGLAIHAHRAMHAAFTRNPRHGITMLALAKAARMIGVDQIHTGTAVGKMAGNYEEIKRINDFLLSKWEHIRPVFPVASGGLHPGLMPELIRLFGKDLVIQAGGGVMGHPDGPRAGAKALRDAIDAAIEGVDLDEKAKSSPELKKSLREVGLSKAKVGVQH | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the addition of molecular CO(2) and H(2)O to ribulose 1,5-bisphosphate (RuBP), generating two molecules of 3-phosphoglycerate (3-PGA). Functions in an archaeal AMP degradation pathway, together with AMP phosphorylase and R15P isomerase.
Catalytic Activity: 2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O
Sequence Mass (Da): 48247
Sequence Length: 430
EC: 4.1.1.39
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P31200 | MSPQTETKASVGFKAGVKDYKLTYYTPEYETKDTDILAAFRVTPQPGVPPEEAGQAVA | Function: RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site (By similarity).
Catalytic Activity: 2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O
Sequence Mass (Da): 6294
Sequence Length: 58
Subcellular Location: Plastid
EC: 4.1.1.39
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Q96T37 | MRTAGRDPVPRRSPRWRRAVPLCETSAGRRVTQLRGDDLRRPATMKGKERSPVKAKRSRGGEDSTSRGERSKKLGGSGGSNGSSSGKTDSGGGSRRSLHLDKSSSRGGSREYDTGGGSSSSRLHSYSSPSTKNSSGGGESRSSSRGGGGESRSSGAASSAPGGGDGAEYKTLKISELGSQLSDEAVEDGLFHEFKRFGDVSVKISHLSGSGSGDERVAFVNFRRPEDARAAKHARGRLVLYDRPLKIEAVYVSRRRSRSPLDKDTYPPSASVVGASVGGHRHPPGGGGGQRSLSPGGAALGYRDYRLQQLALGRLPPPPPPPLPRDLERERDYPFYERVRPAYSLEPRVGAGAGAAPFREVDEISPEDDQRANRTLFLGNLDITVTESDLRRAFDRFGVITEVDIKRPSRGQTSTYGFLKFENLDMSHRAKLAMSGKIIIRNPIKIGYGKATPTTRLWVGGLGPWVPLAALAREFDRFGTIRTIDYRKGDSWAYIQYESLDAAHAAWTHMRGFPLGGPDRRLRVDFADTEHRYQQQYLQPLPLTHYELVTDAFGHRAPDPLRGARDRTPPLLYRDRDRDLYPDSDWVPPPPPVRERSTRTAATSVPAYEPLDSLDRRRDGWSLDRDRGDRDLPSSRDQPRKRRLPEESGGRHLDRSPESDRPRKRHCAPSPDRSPELSSSRDRYNSDNDRSSRLLLERPSPIRDRRGSLEKSQGDKRDRKNSASAERDRKHRTTAPTEGKSPLKKEDRSDGSAPSTSTASSKLKSPSQKQDGGTAPVASASPKLCLAWQGMLLLKNSNFPSNMHLLQGDLQVASSLLVEGSTGGKVAQLKITQRLRLDQPKLDEVTRRIKVAGPNGYAILLAVPGSSDSRSSSSSAASDTATSTQRPLRNLVSYLKQKQAAGVISLPVGGNKDKENTGVLHAFPPCEFSQQFLDSPAKALAKSEEDYLVMIIVRGFGFQIGVRYENKKRENLALTLL | Function: RNA-binding protein that acts as a key regulator of N6-methyladenosine (m6A) methylation of RNAs, thereby regulating different processes, such as hematopoietic cell homeostasis, alternative splicing of mRNAs and X chromosome inactivation mediated by Xist RNA . Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing (By similarity). Plays a key role in m6A methylation, possibly by binding target RNAs and recruiting the WMM complex . Involved in random X inactivation mediated by Xist RNA: acts by binding Xist RNA and recruiting the WMM complex, which mediates m6A methylation, leading to target YTHDC1 reader on Xist RNA and promoting transcription repression activity of Xist . Required for the development of multiple tissues, such as the maintenance of the homeostasis of long-term hematopoietic stem cells and for megakaryocyte (MK) and B-cell differentiation (By similarity). Regulates megakaryocyte differentiation by regulating alternative splicing of genes important for megakaryocyte differentiation; probably regulates alternative splicing via m6A regulation . Required for placental vascular branching morphogenesis and embryonic development of the heart and spleen (By similarity). Acts as a regulator of thrombopoietin response in hematopoietic stem cells by regulating alternative splicing of MPL (By similarity). May also function as an mRNA export factor, stimulating export and expression of RTE-containing mRNAs which are present in many retrotransposons that require to be exported prior to splicing . High affinity binding of pre-mRNA to RBM15 may allow targeting of the mRNP to the export helicase DBP5 in a manner that is independent of splicing-mediated NXF1 deposition, resulting in export prior to splicing . May be implicated in HOX gene regulation .
PTM: Methylated at Arg-578 by PRMT1, leading to promote ubiquitination by CNOT4 and subsequent degradation by the proteasome.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 107189
Sequence Length: 977
Subcellular Location: Nucleus speckle
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Q0VBL3 | MRSAGREPLPRRSPRWRRASPLCETSAGWRVSQLRRDDLRRPSTMKGKERSPVKPKRSRGGEDSSSRGERSKKLGGSGGSNGSSSGKTDSGGSRRSLHLDKSSSRGGSREYETGGGSSSSRLHSYSSPSTKNSSGGGESRSSSRGGGGESRSSGAASSAPGGGDGVEYKTLKISELGSQLSDEAVEDGLFHEFKRFGDVSVKISHLSGSGSGDERVAFVNFRRPEDARAAKHARGRLVLYDRPLKIEAVYVSRRRSRSPLDKDAYAPSSSVVGTSVGSHRHAPGGGGGQRSLSPGGAALGYRDYRLQQLALGRLPPPPPPPLPRELERERDYPFYDRVRPAYSLEPRVGAGAGAAPFREVDEISPEDDQRANRTLFLGNLDITVTENDLRRAFDRFGVITEVDIKRPSRGQTSTYGFLKFENLDMSHRAKLAMSGKIIIRNPIKIGYGKATPTTRLWVGGLGPWVPLAALAREFDRFGTIRTIDYRKGDSWAYIQYESLDAAHAAWTHMRGFPLGGPDRRLRVDFADTEHRYQQQYLQPLPLTHYELVTDTFGHRAPDPLRSARDRTPPLLYRDRDRDLYTDSDWVPPPPPVRERSARAATSAVTAYEPLDSLDRRRDGWSLDRDRGDRDLPSSRDQPRKRRLPEESGGRHLDRSPESERPRKQRHCTPSPDRSPELSSNRDRYNSDNDRSSRLLLLERSSPVRDRRGSLEKSQSDKRDRKNSASAERDRKHRTAAPTEGKNPLKKEDRSDGNAPSASTSSSKQKPPSQKQDGGTAPVAASSPKLCLAWQGMLLLKNSNFPSNMHLLQGDLQVASSLLVEGSTGGKVAQLKITQRLRLDQPKLDEVTRRIKVAGPNGYAILLAVPGSSDSRSSSSSATSDTAASTQRPLRNLVSYLKQKQAAGVISLPVGGNKDKENTGVLHAFPPCEFSQQFLDSPAKALAKSEEDYLVMIIVRAKLVNSG | Function: RNA-binding protein that acts as a key regulator of N6-methyladenosine (m6A) methylation of RNAs, thereby regulating different processes, such as hematopoietic cell homeostasis, alternative splicing of mRNAs and X chromosome inactivation mediated by Xist RNA . Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing . Plays a key role in m6A methylation, possibly by binding target RNAs and recruiting the WMM complex . Involved in random X inactivation mediated by Xist RNA: acts by binding Xist RNA and recruiting the WMM complex, which mediates m6A methylation, leading to target YTHDC1 reader on Xist RNA and promoting transcription repression activity of Xist (By similarity). Required for the development of multiple tissues, such as the maintenance of the homeostasis of long-term hematopoietic stem cells and for megakaryocyte (MK) and B-cell differentiation . Regulates megakaryocyte differentiation by regulating alternative splicing of genes important for megakaryocyte differentiation; probably regulates alternative splicing via m6A regulation (By similarity). Required for placental vascular branching morphogenesis and embryonic development of the heart and spleen . Acts as a regulator of thrombopoietin response in hematopoietic stem cells by regulating alternative splicing of MPL . May also function as an mRNA export factor, stimulating export and expression of RTE-containing mRNAs which are present in many retrotransposons that require to be exported prior to splicing (By similarity). High affinity binding of pre-mRNA to RBM15 may allow targeting of the mRNP to the export helicase DBP5 in a manner that is independent of splicing-mediated NXF1 deposition, resulting in export prior to splicing (By similarity). May be implicated in HOX gene regulation (By similarity).
PTM: Methylated at Arg-577 by PRMT1, leading to promote ubiquitination by CNOT4 and subsequent degradation by the proteasome.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 105722
Sequence Length: 962
Subcellular Location: Nucleus speckle
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A7GLA2 | MKKHGVLNSEIAAILAALGHTDTIVIADCGLPIPDSVKRIDLAVELGKPSFLDVLQVVIEDMAIEKVTVAEEITTNNREIYKEIETRLKEANFEYVLHEEFKEKTKQAKAIIRTGEATPYANIILHAGVIF | Function: Catalyzes the interconversion of beta-pyran and beta-furan forms of D-ribose.
Catalytic Activity: beta-D-ribopyranose = beta-D-ribofuranose
Sequence Mass (Da): 14542
Sequence Length: 131
Pathway: Carbohydrate metabolism; D-ribose degradation; D-ribose 5-phosphate from beta-D-ribopyranose: step 1/2.
Subcellular Location: Cytoplasm
EC: 5.4.99.62
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P36946 | MKKHGILNSHLAKILADLGHTDKIVIADAGLPVPDGVLKIDLSLKPGLPAFQDTAAVLAEEMAVEKVIAAAEIKASNQENAKFLENLFSEQEIEYLSHEEFKLLTKDAKAVIRTGEFTPYANCILQAGVLF | Function: Catalyzes the interconversion of beta-pyran and beta-furan forms of D-ribose.
Catalytic Activity: beta-D-ribopyranose = beta-D-ribofuranose
Sequence Mass (Da): 14227
Sequence Length: 131
Pathway: Carbohydrate metabolism; D-ribose degradation; D-ribose 5-phosphate from beta-D-ribopyranose: step 1/2.
Subcellular Location: Cytoplasm
EC: 5.4.99.62
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Q7NTN5 | MKKHGHLNRDIARILASMGHTDSLVIADCGLPIPPGVECVDLSLKLGQPGFIETLDSILADFQCERAVFAIECRQHNPAVQDKAERMAQAGAALDFVSHEEFKQRCQAARAVIRTGECTPYANVILHSGVIF | Function: Catalyzes the interconversion of beta-pyran and beta-furan forms of D-ribose.
Catalytic Activity: beta-D-ribopyranose = beta-D-ribofuranose
Sequence Mass (Da): 14412
Sequence Length: 132
Pathway: Carbohydrate metabolism; D-ribose degradation; D-ribose 5-phosphate from beta-D-ribopyranose: step 1/2.
Subcellular Location: Cytoplasm
EC: 5.4.99.62
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Q88RZ3 | MNTTALLIGLGPLLGWGLYPTIASKIGGRPVNQILGSTIGTLIFALIYAWVQGIAFPSGMNLWFSILSGIGWASAQIVTFKVFTMVGSSRAMPITTAFQLLGASLWGVFALGDWPGAMDKVLGGLALVGIIIGAWLTVWSEHKDAGNARTLRQAVIWLAVGEIGYWAYSAAPQATNIGGEEAFVPQAIGMVIVSIVYALFLASRGEKLALVEGVSYTHIISGFFFAFAALTYLISAQPNMNGLATGFILSQTSVVLATLTGIWFLGQKKTTKEMWVTIGGLILIIAAAAVTVTI | Function: Could be involved in the uptake of ribose.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31049
Sequence Length: 294
Subcellular Location: Cell membrane
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Q9X4M3 | MNAVNILIGLMPMIGWGIFPVIVGKIGGKPASQILGTTFGTLILAIVVAIFRGTPIPETKTFIFCLISGACWALAQIITFHVFETMGVSRTMPITTGFQLVGASLWGVFVLGNWSSSQSKLIGFTAIALIIIGVYLTAWSEDKSSASKSGAVKGILLLLVGELGYLGYSAFPQAVSADGFQGFLPQAIGMTIVGIIFGLTQTKKDYKPFKEATSYKNIFSGFFFAFAALTYLISAQPSVNGLATGFVLSQTSVIFATIGGIYILKEKKSKKEMIAVMVGLLLVLVAGSVTAFIK | Function: Could be involved in the uptake of ribose.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31169
Sequence Length: 294
Subcellular Location: Cell membrane
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O00559 | MAITQFRLFKFCTCLATVFSFLKRLICRSGRGRKLSGDQITLPTTVDYSSVPKQTDVEEWTSWDEDAPTSVKIEGGNGNVATQQNSLEQLEPDYFKDMTPTIRKTQKIVIKKREPLNFGIPDGSTGFSSRLAATQDLPFIHQSSELGDLDTWQENTNAWEEEEDAAWQAEEVLRQQKLADREKRAAEQQRKKMEKEAQRLMKKEQNKIGVKLS | Function: May participate in suppression of cell proliferation and induces apoptotic cell death through activation of interleukin-1-beta converting enzyme (ICE)-like proteases.
Location Topology: Single-pass type III membrane protein
Sequence Mass (Da): 24377
Sequence Length: 213
Domain: The coiled coil domain is necessary for the homodimerization.
Subcellular Location: Golgi apparatus membrane
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Q5PQP2 | MAITQFRLFKVCTCLATVLSFLKRLICRSGRGRKLSGDQITLPTTVDYSSVPKQTDVEEWTSWDEDAPTSVKIEGGTGNAAAQQNSLEQLEPDYFKDMTPTIRKTQKIVIKKREPLSFGVPDGSTGFSSRLAATQDMPFIHQSSELGDLDTWQENSNAWEEEEDAAWQAEEVLRQQKIADREKRAAEQQRKKMEKEAQRLLKKEQNKMGVKLS | Function: May participate in suppression of cell proliferation and induces apoptotic cell death through activation of interleukin-1-beta converting enzyme (ICE)-like proteases.
Location Topology: Single-pass type III membrane protein
Sequence Mass (Da): 24187
Sequence Length: 213
Domain: The coiled coil domain is necessary for the homodimerization.
Subcellular Location: Golgi apparatus membrane
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P10896 | MAAAVSTVGAINRAPLSLNGSGSGAVSAPASTFLGKKVVTVSRFAQSNKKSNGSFKVLAVKEDKQTDGDRWRGLAYDTSDDQQDITRGKGMVDSVFQAPMGTGTHHAVLSSYEYVSQGLRQYNLDNMMDGFYIAPAFMDKLVVHITKNFLTLPNIKVPLILGIWGGKGQGKSFQCELVMAKMGINPIMMSAGELESGNAGEPAKLIRQRYREAADLIKKGKMCCLFINDLDAGAGRMGGTTQYTVNNQMVNATLMNIADNPTNVQLPGMYNKEENARVPIICTGNDFSTLYAPLIRDGRMEKFYWAPTREDRIGVCKGIFRTDKIKDEDIVTLVDQFPGQSIDFFGALRARVYDDEVRKFVESLGVEKIGKRLVNSREGPPVFEQPEMTYEKLMEYGNMLVMEQENVKRVQLAETYLSQAALGDANADAIGRGTFYGKGAQQVNLPVPEGCTDPVAENFDPTARSDDGTCVYNF | Function: Activation of RuBisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase; EC 4.1.1.39) involves the ATP-dependent carboxylation of the epsilon-amino group of lysine leading to a carbamate structure.
PTM: Phosphorylated at Thr-78 by CK2.
Sequence Mass (Da): 51981
Sequence Length: 474
Subcellular Location: Plastid
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P38623 | MLKIKALFSKKKPDQADLSQESKKPFKGKTRSSGTNNKDVSQITSSPKKSFQDKNIVQYPSVVADDHHMKSLTDELVTTIDSDSSPSDNITTENVETVTSVPAIDVHESSEGQLSSDPLISDESLSEQSEIISDIQDDSTDDDNMEDEIPEKSFLEQKELIGYKLINKIGEGAFSKVFRAIPAKNSSNEFLTKNYKAVAIKVIKKADLSSINGDHRKKDKGKDSTKTSSRDQVLKEVALHKTVSAGCSQIVAFIDFQETDSYYYIIQELLTGGEIFGEIVRLTYFSEDLSRHVIKQLALAVKHMHSLGVVHRDIKPENLLFEPIEFTRSIKPKLRKSDDPQTKADEGIFTPGVGGGGIGIVKLADFGLSKQIFSKNTKTPCGTVGYTAPEVVKDEHYSMKVDMWGIGCVLYTMLCGFPPFYDEKIDTLTEKISRGEYTFLKPWWDEISAGAKNAVAKLLELEPSKRYDIDQFLDDPWLNTFDCLPKEGESSQKKAGTSERRHPHKKQFQLFQRDSSLLFSPAAVAMRDAFDIGNAVKRTEEDRMGTRGGLGSLAEDEELEDSYSGAQGDEQLEQNMFQLTLDTSTILQRRKKVQENDVGPTIPISATIRE | Function: Serine/threonine-protein kinase involved in a signal transduction pathway that is activated by changes in the osmolarity of the extracellular environment.
PTM: Autophosphorylated. Phosphorylated by HOG1 at Ser-520 after osmotic stress.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 68062
Sequence Length: 610
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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P75685 | MEKYLHLLSRGDKIGLTLIRLSIAIVFMWIGLLKFVPYEADSITPFVANSPLMSFFYEHPEDYKQYLTHEGEYKPEARAWQTANNTYGFSNGLGVVEVIIALLVLANPVNRWLGLLGGLMAFTTPLVTLSFLITTPEAWVPALGDAHHGFPYLSGAGRLVLKDTLMLAGAVMIMADSAREILKQRSNESSSTLKTEY | Function: Probably involved in reactive chlorine species (RCS) stress resistance.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21899
Sequence Length: 197
Subcellular Location: Cell inner membrane
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O14039 | MDFYNHAANILSDLSKKKGSIKQLAFNSKKHDPKRTYALVCETLKYKPVLDEIIARSELLVLEKKLKENLARVLVHDLLMSKRGLSISNGPIKECILRHKTRLNAEFVKLKVKKGVKSHEELALKNPVSLPRWLRINTIKSTKDEVLQGLGLDKVSSIEELGPDKFYIDDCVENLIAIDPSFPIVENSLYKEGKVIIQDKASCFPAAVLAGLTGHVGDIIDGCAAPGNKTTHLAACFPKSHIFAFERDAKRVQTLRKMVGISGANNVTIEHQDFTLTDPKSDLYRNVTHILLDPSCSGSGIVSRQDYLLGNEQDVTEDTERLENLCSFQSTILKHALQFPNCRHVTYSTCSVHRLENEQVVCEVLSQEPDWKCNSLTKTLPNWKTRGIPEYCAQPSMAEGMIRCKPGAGGTIGFFVANLYHPQREQETFKMYKNDDDTKKRKRKKKKKEVKKKARIQGEE | Function: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the C(5) position of a cytosine in 25S rRNA.
Catalytic Activity: a cytidine in 25S rRNA + S-adenosyl-L-methionine = a 5-methylcytidine in 25S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 51877
Sequence Length: 460
Subcellular Location: Nucleus
EC: 2.1.1.-
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P53972 | MNFYRDATWVLEDIEKEAAKERISGSMQTLVLKSCKRYKLKSNPKHIYAVLDSCWKYKPYLEKVMKKAHILEDIPKKKGKPLFSRLTLLLLCHDLLLSKQKRIQMGKHPIKDYVLKFKSPLHSEMVKLKLKLKVRELSELVLSEDISNDLPPVRWIRINPLKCHPNGETEPVLAELRKKFTLKVDKWSELVPGSIYYDEFIPNLFGIHPSDKITAHELYKHGKIIIQDRASCFPAHILNPGPSDIVIDSCSAPGNKTTHTASYIYPEPPKDNNTRIYAFEKDPERAKVLQKMIKIAGCSPNISVNVGDFTKLATPEKYKDVTCFIVDPSCSGSGIFGRKFFDSFNRRKIDDKDDDGGIVPDEQEEFIAKEELQTRLAKLSSFQFQMVKHAMSFPAAKKIVYSTCSIHAEENERVVIDLLLDKSVREWGWKVAPKREVIPSWPRRGKVEEFEEVFRDGVTYDPQQLAEGCIRALPKSDGGIGFFAVCFERD | Function: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the C(5) position of cytosine 2278 (m5C2278) in 25S rRNA . Loss of m5C2278 in 25S rRNA results in anisomycin hypersensitivity .
Catalytic Activity: cytidine(2278) in 25S rRNA + S-adenosyl-L-methionine = 5-methylcytidine(2278) in 25S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 56177
Sequence Length: 490
Subcellular Location: Nucleus
EC: 2.1.1.311
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Q92781 | MWLPLLLGALLWAVLWLLRDRQSLPASNAFVFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQRVASSRLHTTLLDITDPQSVQQAAKWVEMHVKEAGLFGLVNNAGVAGIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQARGRVINITSVLGRLAANGGGYCVSKFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRTPVTNLESLEKTLQACWARLPPATQAHYGGAFLTKYLKMQQRIMNLICDPDLTKVSRCLEHALTARHPRTRYSPGWDAKLLWLPASYLPASLVDAVLTWVLPKPAQAVY | Function: Catalyzes the oxidation of cis-isomers of retinol, including 11-cis-, 9-cis-, and 13-cis-retinol in an NAD-dependent manner . Has no activity towards all-trans retinal (By similarity). Plays a significant role in 11-cis retinol oxidation in the retinal pigment epithelium cells (RPE). Also recognizes steroids (androsterone, androstanediol) as its substrates .
Catalytic Activity: 11-cis-retinol + NAD(+) = 11-cis-retinal + H(+) + NADH
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34979
Sequence Length: 318
Domain: The last 8 amino acids of the C-terminal tail are important for a proper localization as well as for the in vivo enzymatic activity.
Pathway: Cofactor metabolism; retinol metabolism.
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.1.1.209
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O55240 | MWLPLLLGALLWAVLWLLRDRQSLPASDAFIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGETGLFGLVNNAGVAGIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQARGRVVNITSVLGRIAANGGGYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVTNLESLESTLKACWARLPPAIQAHYGEAFLDTYLRVQRRIMNLICDPELTKVTSCLEHALTARHPRTRYSPGWDAKLLWLPASYLPARVVDAVLTWILPRPAQSVS | Function: Catalyzes the oxidation of cis-isomers of retinol, including 11-cis-, 9-cis-, and 13-cis-retinol in an NAD-dependent manner . Has no activity towards all-trans retinal (By similarity). Plays a significant role in 11-cis retinol oxidation in the retinal pigment epithelium cells (RPE). Also recognizes steroids (androsterone, androstanediol) as its substrates (By similarity).
Catalytic Activity: 11-cis-retinol + NAD(+) = 11-cis-retinal + H(+) + NADH
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34826
Sequence Length: 318
Domain: The last 8 amino acids of the C-terminal tail are important for a proper localization as well as for the in vivo enzymatic activity.
Pathway: Cofactor metabolism; retinol metabolism.
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.1.1.209
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Q9N126 | MADAPRTVLISGCSSGIGLELAVQLAHDPRQRYQVVATMRDLGKKGTLETAAGEALGQTLTVAQLDVCSDESVAQCLNCIQGGEVDVLVNNAGVGLVGPLEGLSLAAMQNVFDTNFFGAVRLVKAVLPSMKRRRQGHIVVVSSVMGLQGVVFNEVYAASKFAMEGFFESLAVQLLQFNIFISLVEPGPVVTEFEGKLLEQVSTAEFPGTDPDTLSYFRDLYLPASRELFHNVGQSPQDVAKVIVKVIGSARPPLRRRTNTRYTPLIALKAMDPSGSLYVRTSHCLLFRWPRLLNLGLRCLACSCFRTPVWPR | Function: Retinol dehydrogenase with a clear preference for NADP. Converts all-trans-retinal to all-trans-retinol. May play a role in the regeneration of visual pigment at high light intensity.
Catalytic Activity: all-trans-retinol + NADP(+) = all-trans-retinal + H(+) + NADPH
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33956
Sequence Length: 312
Subcellular Location: Membrane
EC: 1.1.1.300
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Q9NYR8 | MAAAPRTVLISGCSSGIGLELAVQLAHDPKKRYQVVATMRDLGKKETLEAAAGEALGQTLTVAQLDVCSDESVAQCLSCIQGEVDVLVNNAGMGLVGPLEGLSLAAMQNVFDTNFFGAVRLVKAVLPGMKRRRQGHIVVISSVMGLQGVIFNDVYAASKFALEGFFESLAIQLLQFNIFISLVEPGPVVTEFEGKLLAQVSMAEFPGTDPETLHYFRDLYLPASRKLFCSVGQNPQDVVQAIVNVISSTRPPLRRQTNIRYSPLTTLKTVDSSGSLYVRTTHRLLFRCPRLLNLGLQCLSCGCLPTRVRPR | Function: Retinol dehydrogenase with a clear preference for NADP. Converts all-trans-retinal to all-trans-retinol. May play a role in the regeneration of visual pigment at high light intensity (By similarity).
Catalytic Activity: all-trans-retinol + NADP(+) = all-trans-retinal + H(+) + NADPH
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33755
Sequence Length: 311
Subcellular Location: Membrane
EC: 1.1.1.300
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Q8N3Y7 | MSFNLQSSKKLFIFLGKSLFSLLEAMIFALLPKPRKNVAGEIVLITGAGSGLGRLLALQFARLGSVLVLWDINKEGNEETCKMAREAGATRVHAYTCDCSQKEGVYRVADQVKKEVGDVSILINNAGIVTGKKFLDCPDELMEKSFDVNFKAHLWTYKAFLPAMIANDHGHLVCISSSAGLSGVNGLADYCASKFAAFGFAESVFVETFVQKQKGIKTTIVCPFFIKTGMFEGCTTGCPSLLPILEPKYAVEKIVEAILQEKMYLYMPKLLYFMMFLKSFLPLKTGLLIADYLGILHAMDGFVDQKKKL | Function: Oxidoreductase with strong preference for NAD . Active in both the oxidative and reductive directions . Oxidizes all-trans-retinol in all-trans-retinaldehyde . No activity was detected with 11-cis-retinol or 11-cis-retinaldehyde as substrates with either NAD(+)/NADH or NADP(+)/NADPH .
Catalytic Activity: all-trans-retinol--[retinol-binding protein] + NAD(+) = all-trans-retinal--[retinol-binding protein] + H(+) + NADH
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34095
Sequence Length: 309
Pathway: Cofactor metabolism; retinol metabolism.
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.1.1.105
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Q12305 | MWKAVMNAWNGTESQSKNVSNIQSYSFEDMKRIVGKHDPNVVLVDVREPSEYSIVHIPASINVPYRSHPDAFALDPLEFEKQIGIPKPDSAKELIFYCASGKRGGEAQKVASSHGYSNTSLYPGSMNDWVSHGGDKLDL | Function: Thiosulfate:glutathione sulfurtransferase (TST) required to produce S-sulfanylglutathione (GSS(-)), a central intermediate in hydrogen sulfide metabolism . Provides the link between the first step in H(2)S metabolism performed by the sulfide:quinone oxidoreductase (SQOR) which catalyzes the conversion of H(2)S to thiosulfate, and the sulfur dioxygenase (SDO) which uses GSS(-) as substrate . The thermodynamic coupling of the irreversible SDO and reversible TST reactions provides a model for the physiologically relevant reaction with thiosulfate as the sulfane donor .
Catalytic Activity: glutathione + thiosulfate = H(+) + S-sulfanylglutathione + sulfite
Sequence Mass (Da): 15413
Sequence Length: 139
Subcellular Location: Mitochondrion
EC: 2.8.1.-
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Q08742 | MFKHSTGILSRTVSARSPTLVLRTFTTKAPKIYTFDQVRNLVEHPNDKKLLVDVREPKEVKDYKMPTTINIPVNSAPGALGLPEKEFHKVFQFAKPPHDKELIFLCAKGVRAKTAEELARSYGYENTGIYPGSITEWLAKGGADVKPKK | Function: Thiosulfate sulfurtransferase which catalyzes the transfer of sulfane sulfur from thiosulfate to cyanide.
Catalytic Activity: hydrogen cyanide + thiosulfate = 2 H(+) + sulfite + thiocyanate
Sequence Mass (Da): 16697
Sequence Length: 149
Subcellular Location: Mitochondrion
EC: 2.8.1.1
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Q934F8 | MIKKVVAYAAIAASVMGASAAAAPQAMAIGDDSGPVSANGNGASQYFGNSMTTGNMSPQMALIQGSFNKPCIAVSDIPVSVIGLVPIQDLNVLGDDMNQQCAENSTQAKRDGALAHLLEDVSILSSNGEGGKG | Function: Forms part of the rodlet layer on the spore surface; despite their high similarity both RdlA and RdlB are required for rodlet formation . Plays a role in cell adhesion to polystyrene plates . Forms amyloid-like fibrils in vitro composed of stacked beta-sheets .
Sequence Mass (Da): 13355
Sequence Length: 133
Domain: The mature protein has 2 regions in the N-terminus capable of forming amyloid rods of slightly differing conformation; intact protein makes longer fibrils. Amyloid formation depends on polar residues between amino acids 45 and 70.
Subcellular Location: Secreted
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Q10215 | MFSKTLSVSRLLMTRSFYSSTVVKNVSIFDFEKVYNLSKRPTGDKSTVLIDVREPDEFKQGAIETSYNLPVGKIEEAMKLSDEEFSKTYGFSKPVFEDNVVVYCRSGRRSTTASDILTKLGYKNIGNYTGSWLEWSDKIKSK | Function: Thiosulfate sulfurtransferase which catalyzes the transfer of sulfane sulfur from thiosulfate to cyanide.
Catalytic Activity: hydrogen cyanide + thiosulfate = 2 H(+) + sulfite + thiocyanate
Sequence Mass (Da): 16185
Sequence Length: 142
Subcellular Location: Mitochondrion
EC: 2.8.1.1
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P34057 | MGNSKSGALSKEILEELQLNTKFTEEELSAWYQSFLKECPSGRITRQEFESIYSKFFPDSDPKAYAQHVFRSFDANSDGTLDFKEYVIALHMTTAGKPTQKLEWAFSLYDVDGNGTISKNEVLEIVMAIFKMIKPEDVKLLPDDENTPEKRAEKIWAFFGKKEDDKLTEEEFIEGTLANKEILRLIQFEPQKVKERIKEKKQ | Function: Acts as a calcium sensor and regulates phototransduction of cone and rod photoreceptor cells (By similarity). Modulates light sensitivity of cone photoreceptor in dark and dim conditions . In response to high Ca(2+) levels induced by low light levels, prolongs RHO/rhodopsin activation in rod photoreceptor cells by binding to and inhibiting GRK1-mediated phosphorylation of RHO/rhodopsin (By similarity). Plays a role in scotopic vision/enhances vision in dim light by enhancing signal transfer between rod photoreceptors and rod bipolar cells . Improves rod photoreceptor sensitivity in dim light and mediates response of rod photoreceptors to facilitate detection of change and motion in bright light .
PTM: The N-terminal glycine is linked to one of four different types of acyl groups. The most abundant is myristoleate (14:1), but 14:0, 14:2, and 12:0 acyl residues are also present (By similarity). The Ca(2+) induced exposure of the myristoyl group, known as the calcium-myristoyl switch, promotes RCVRN binding to the photoreceptor cell membranes only when intracellular Ca(2+) concentration is high (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 23407
Sequence Length: 202
Domain: EF-hand 2 and EF-hand 3 domains are the low-affinity and the high-affinity calcium binding sites, respectively. EF-hand 1 and EF-hand 4 domains do not bind calcium due to substitutions that disrupt their respective Ca(2+) binding loops. The cooperative binding of calcium to the EF-hand 2 domain following EF-hand 3 domain calcium binding requires myristoylation (By similarity). Calcium binding to the 2 EF-hand domains induces exposure of the myristoyl group through a protein conformation change, this process known as the calcium-myristoyl switch facilitates binding to photoreceptor cell membranes (By similarity).
Subcellular Location: Photoreceptor inner segment
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P0AG22 | MVAVRSAHINKAGEFDPEKWIASLGITSQKSCECLAETWAYCLQQTQGHPDASLLLWRGVEMVEILSTLSMDIDTLRAALLFPLADANVVSEDVLRESVGKSVVNLIHGVRDMAAIRQLKATHTDSVSSEQVDNVRRMLLAMVDDFRCVVIKLAERIAHLREVKDAPEDERVLAAKECTNIYAPLANRLGIGQLKWELEDYCFRYLHPTEYKRIAKLLHERRLDREHYIEEFVGHLRAEMKAEGVKAEVYGRPKHIYSIWRKMQKKNLAFDELFDVRAVRIVAERLQDCYAALGIVHTHYRHLPDEFDDYVANPKPNGYQSIHTVVLGPGGKTVEIQIRTKQMHEDAELGVAAHWKYKEGAAAGGARSGHEDRIAWLRKLIAWQEEMADSGEMLDEVRSQVFDDRVYVFTPKGDVVDLPAGSTPLDFAYHIHSDVGHRCIGAKIGGRIVPFTYQLQMGDQIEIITQKQPNPSRDWLNPNLGYVTTSRGRSKIHAWFRKQDRDKNILAGRQILDDELEHLGISLKEAEKHLLPRYNFNDVDELLAAIGGGDIRLNQMVNFLQSQFNKPSAEEQDAAALKQLQQKSYTPQNRSKDNGRVVVEGVGNLMHHIARCCQPIPGDEIVGFITQGRGISVHRADCEQLAELRSHAPERIVDAVWGESYSAGYSLVVRVVANDRSGLLRDITTILANEKVNVLGVASRSDTKQQLATIDMTIEIYNLQVLGRVLGKLNQVPDVIDARRLHGS | Function: In eubacteria ppGpp (guanosine 3'-diphosphate 5'-diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. This enzyme catalyzes the formation of pppGpp which is then hydrolyzed to form ppGpp (By similarity).
Catalytic Activity: ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate
Sequence Mass (Da): 83876
Sequence Length: 744
Pathway: Purine metabolism; ppGpp biosynthesis; ppGpp from GTP: step 1/2.
EC: 2.7.6.5
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P9WHG8 | MTAQRSTTNPVLEPLVAVHREIYPKADLSILQRAYEVADQRHASQLRQSGDPYITHPLAVANILAELGMDTTTLVAALLHDTVEDTGYTLEALTEEFGEEVGHLVDGVTKLDRVVLGSAAEGETIRKMITAMARDPRVLVIKVADRLHNMRTMRFLPPEKQARKARETLEVIAPLAHRLGMASVKWELEDLSFAILHPKKYEEIVRLVAGRAPSRDTYLAKVRAEIVNTLTASKIKATVEGRPKHYWSIYQKMIVKGRDFDDIHDLVGVRILCDEIRDCYAAVGVVHSLWQPMAGRFKDYIAQPRYGVYQSLHTTVVGPEGKPLEVQIRTRDMHRTAEYGIAAHWRYKEAKGRNGVLHPHAAAEIDDMAWMRQLLDWQREAADPGEFLESLRYDLAVQEIFVFTPKGDVITLPTGSTPVDFAYAVHTEVGHRCIGARVNGRLVALERKLENGEVVEVFTSKAPNAGPSRDWQQFVVSPRAKTKIRQWFAKERREEALETGKDAMAREVRRGGLPLQRLVNGESMAAVARELHYADVSALYTAIGEGHVSAKHVVQRLLAELGGIDQAEEELAERSTPATMPRRPRSTDDVGVSVPGAPGVLTKLAKCCTPVPGDVIMGFVTRGGGVSVHRTDCTNAASLQQQAERIIEVLWAPSPSSVFLVAIQVEALDRHRLLSDVTRALADEKVNILSASVTTSGDRVAISRFTFEMGDPKHLGHLLNAVRNVEGVYDVYRVTSAA | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: In eubacteria ppGpp (guanosine 3'-diphosphate 5'-diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. This enzyme catalyzes both the formation of pppGpp, which is then hydrolyzed to form ppGpp, as well as the hydrolysis of ppGpp. RelA is probably a key factor in the pathogenesis of M.tuberculosis as it regulates the intracellular concentrations of (p)ppGpp (By similarity).
Catalytic Activity: guanosine 3',5'-bis(diphosphate) + H2O = diphosphate + GDP + H(+)
Sequence Mass (Da): 81827
Sequence Length: 738
Pathway: Purine metabolism; ppGpp biosynthesis; ppGpp from GDP: step 1/1.
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O52177 | MWGNVAPPLVQSYDCSSFDDSPERHPPTVSQYHPDPDLDIIKKAYVYSAKVHQGQLRKSGEPYLVHPLEVAGILGELKLDEASIVTGLLHDTIEDTLATEEELTELFGSEVAHLVDGVTKLSKFSASASLSQEEKQAENFRKMIIAMAQDIRVILVKLADRTHNMRTLDHMSEEKQARIAQETLDIYAPLANRLGISWIKTELEDLSFRYVKPQEFFALQAKLNKRKKEREKYIEDTCDLIRSKLAERGLKGEVSGRFKHVYSIYKKIKSQGIDFDQIHDIIAFRIIAPTAPSCYEALGLVHEMWKPVPGRFKDFIAIPKPNMYQSLHTTIIGPLSERVEVQIRTSEMHKIAEEGIAAHWKYKEGKAVISKDDEKFAWLRQLMEWQQDLKDPKEFLETVKVDLFTDEVFVFTPKGDVRSLPRGATPVDFAYAIHSDVGNRCVGAKVNGKIVPLRYKMKNGDTVEVLTSPQQHPSKDWLTFVKTSRAQQRIRGFIKQQQREKSLQLGRELADRELKRFQLNFNRLLKSGEMKKAAVDLGFRVEDDMLVAIGYGKVTPQQLSHRLVPQEKLNAAEAGGRADANPAATTSGGAGNSVLPGLSRVTDLAKRLVGRSNRSGVQIGGVDDVLVRFGRCCNPVPGDPIAGFITRGRGVTVHTVGCEKALATDPERRVDVSWDVRGDFKRPVTLRVLTADRPGLLADITNTFSKKGVNISQANCRATGDDRAVNTFEVIISDLKQLTDLMRTIERLQGVYSVERI | Function: In eubacteria ppGpp (guanosine 3'-diphosphate 5'-diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. This enzyme catalyzes the formation of pppGpp which is then hydrolyzed to form ppGpp (By similarity).
Catalytic Activity: ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate
Sequence Mass (Da): 84978
Sequence Length: 757
Pathway: Purine metabolism; ppGpp biosynthesis; ppGpp from GTP: step 1/2.
EC: 2.7.6.5
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P55133 | MVAVRGAHLKENTTFELVSWVESLRQDAKVSSRIEGTYQRCIELAAEQENGPLLLWRGRELVEILVTLSMDADTLIAALLYPLVEGGCYSTDALKEEYSGTILHLVQGVEQMCAISQLKSTAEETAQAAQVDNIRRMLLSMVDDFRCVVIKLAERICNLREVKDQPDEVRRAAAQECANIYAPLANRLGIGQLKWEIEDYAFRYQHPDTYKQIAKQLSERRIDREDYITHFVDDLSDAMKASNIRAEVQGRPKHIYSIWRKMQKKSLEFDELFDVRAVRIVAEELQDCYAALGVVHTKYRHLPKEFDDYVANPKPNGYQSIHTVVLGPEGKTIEIQIRTKQMHEESELGVAAHWKYKEGTASGGAQSAYDEKINWLRKLLAWQEEMSDSGEMLDELRSQVFDDRVYAFTPKGDVVDLPSNATPLDFAYHIHSEVGHRCIGAKVEGRIVPFTYHLQMGDQVEIITQKEPNPSRDWLNPNLGFVTSSRARAKVHAWFRKQDRDKNIIAGKEILEAELVKIHATLKDAQYYAAKRFNVKSPEELYAGIGSGDLRINQVINHINALVNKPTAEEEDQQLLEKLSEASNKQATSHKKPQRDAVVVEGVDNLMTHLARCCQPIPGDDIQGFVTQGRGISVHRMDCEQLEELRHHAPERIIDTVWGGGFVGNYTITVRVTASERNGLLKELTNTLMNEKVKVAGMKSRVDYKKQMSIMDFELELTDLEVLGRVLKRIEQVKDVAEAKRLYG | Function: In eubacteria ppGpp (guanosine 3'-diphosphate 5'-diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. This enzyme catalyzes the formation of pppGpp which is then hydrolyzed to form ppGpp. Also plays a role in the reductive division that occurs during the initial phase of nutrient starvation.
Catalytic Activity: ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate
Sequence Mass (Da): 84546
Sequence Length: 744
Pathway: Purine metabolism; ppGpp biosynthesis; ppGpp from GTP: step 1/2.
EC: 2.7.6.5
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Q9TSZ1 | MDAWRGMPRWGLLLLLWGSCTFGLPTETTTFKRISLKRMPSIRESLKERGVDMARLGPERMALVNITSSVILTNYMDTQYYGEIGIGTPPQTFKVVFDTGSSNVWVPSSKCSRLYTACVYHKLFDASDSSSYKHNGTELTLRYSTGTVSGFLSQDVITVGGITVTQTFGEVTEMPALPFMLAEFDGVVGMGFSEQAIGKVTPLFDNIISQGLLKEDVFSFYYNRDSENSQSLGGQIVLGGSDPQHYEGNFHYINLIRTGLWQIPMKGVSVGSSTLLCEDGCLALVDTGASYISGSTSSIEKLMEALGAKKRLFDYVVKCNEGPTLPDISFHLGGKEYTLTSADYVFQESYSSKKLCTLAIHAMDIPPPTGPTWALGATFIRKFYTEFDRGNNRIGFALAR | Function: Renin is a highly specific endopeptidase, whose only known function is to generate angiotensin I from angiotensinogen in the plasma, initiating a cascade of reactions that produce an elevation of blood pressure and increased sodium retention by the kidney.
Catalytic Activity: Cleavage of Leu-|-Xaa bond in angiotensinogen to generate angiotensin I.
Sequence Mass (Da): 44038
Sequence Length: 400
Subcellular Location: Secreted
EC: 3.4.23.15
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Q6DYE7 | MARCRMPRWGLLLVLWGSCTFGLPADTGAFRRIFLKKMPSIRESLKERGVDVAGLGAEWNQFTKRLSSGNSTSPVVLTNYLDTQYYGEIGIGTPPQTFKVVFDTGSANLWVPSTRCSPLYTACEIHCLYDSSESSSYMENGTTFTIRYGSGKVKGFLSQDMVTVGGITVTQTFGEVTELPLIPFMLAKFDGVLGMGFPAQAVGGVTPVFDHILSQGVLKEEVFSVYYSRNSHLLGGEVVLGGSDPQYYQGNFHYVSISKTGSWQIKMKGVSVRSATLVCEEGCMVVVDTGASYISGPTSSLRLLMDTLGAQELSTNEYVVNCNQVPTLPDISFHLGGRAYTLTSKDYVLQDPYGNEDLCTLALHGLDVPPPTGPVWVLGASFIRKFYTEFDRHNNRIGFALAR | Function: Renin is a highly specific endopeptidase, whose only known function is to generate angiotensin I from angiotensinogen in the plasma, initiating a cascade of reactions that produce an elevation of blood pressure and increased sodium retention by the kidney.
Catalytic Activity: Cleavage of Leu-|-Xaa bond in angiotensinogen to generate angiotensin I.
Sequence Mass (Da): 44099
Sequence Length: 403
Subcellular Location: Secreted
EC: 3.4.23.15
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P00797 | MDGWRRMPRWGLLLLLWGSCTFGLPTDTTTFKRIFLKRMPSIRESLKERGVDMARLGPEWSQPMKRLTLGNTTSSVILTNYMDTQYYGEIGIGTPPQTFKVVFDTGSSNVWVPSSKCSRLYTACVYHKLFDASDSSSYKHNGTELTLRYSTGTVSGFLSQDIITVGGITVTQMFGEVTEMPALPFMLAEFDGVVGMGFIEQAIGRVTPIFDNIISQGVLKEDVFSFYYNRDSENSQSLGGQIVLGGSDPQHYEGNFHYINLIKTGVWQIQMKGVSVGSSTLLCEDGCLALVDTGASYISGSTSSIEKLMEALGAKKRLFDYVVKCNEGPTLPDISFHLGGKEYTLTSADYVFQESYSSKKLCTLAIHAMDIPPPTGPTWALGATFIRKFYTEFDRRNNRIGFALAR | Function: Renin is a highly specific endopeptidase, whose only known function is to generate angiotensin I from angiotensinogen in the plasma, initiating a cascade of reactions that produce an elevation of blood pressure and increased sodium retention by the kidney.
Catalytic Activity: Cleavage of Leu-|-Xaa bond in angiotensinogen to generate angiotensin I.
Sequence Mass (Da): 45057
Sequence Length: 406
Subcellular Location: Secreted
EC: 3.4.23.15
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P08424 | MGGRRMPLWALLLLWTSCSFSLPTDTASFGRILLKKMPSVREILEERGVDMTRISAEWGEFIKKSSFTNVTSPVVLTNYLDTQYYGEIGIGTPSQTFKVIFDTGSANLWVPSTKCGPLYTACEIHNLYDSSESSSYMENGTEFTIHYGSGKVKGFLSQDVVTVGGIIVTQTFGEVTELPLIPFMLAKFDGVLGMGFPAQAVDGVIPVFDHILSQRVLKEEVFSVYYSRESHLLGGEVVLGGSDPQHYQGNFHYVSISKAGSWQITMKGVSVGPATLLCEEGCMAVVDTGTSYISGPTSSLQLIMQALGVKEKRANNYVVNCSQVPTLPDISFYLGGRTYTLSNMDYVQKNPFRNDDLCILALQGLDIPPPTGPVWVLGATFIRKFYTEFDRHNNRIGFALAR | Function: Renin is a highly specific endopeptidase, whose only known function is to generate angiotensin I from angiotensinogen in the plasma, initiating a cascade of reactions that produce an elevation of blood pressure and increased sodium retention by the kidney.
Catalytic Activity: Cleavage of Leu-|-Xaa bond in angiotensinogen to generate angiotensin I.
Sequence Mass (Da): 44276
Sequence Length: 402
Subcellular Location: Secreted
EC: 3.4.23.15
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P81134 | MAVLVVFLSFLVADVFGNEFSILRSPGSVVFRNGNWPIPGERIPDVAALSMGFSVKEDLSWPGLAVGNLFHRPRATVMVMVKGVDKLALPPGSVISYPLENAVPFSLDSVANSIHSLFSEETPVVLQLAPSEERVYMVGKANSVFEDLSVTLRQLRNRLFQENSVLTSLPLNSLSRNNEVDLLFLSELQVLRDISSLLSRHKHLAKDHSPDLYSLELAGLDEIGKHYGEDSEQFRDASKILIDALQKFADDMYNLYGGNAVVELVTVRSFDTSLVRKTRNILETKQVKDPSTTYNLAYKYNFEYPVVFNLVLWIMIGLALTLIVTCYNIWNMDPGYDSIIYRMTNQKIRMD | Function: Multifunctional protein which functions as a renin, prorenin cellular receptor and is involved in the assembly of the lysosomal proton-transporting V-type ATPase (V-ATPase) and the acidification of the endo-lysosomal system (By similarity). May mediate renin-dependent cellular responses by activating ERK1 and ERK2 (By similarity). By increasing the catalytic efficiency of renin in AGT/angiotensinogen conversion to angiotensin I, may also play a role in the renin-angiotensin system (RAS) (By similarity). Through its function in V-type ATPase (v-ATPase) assembly and acidification of the lysosome it regulates protein degradation and may control different signaling pathways important for proper brain development, synapse morphology and synaptic transmission (By similarity).
PTM: Phosphorylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 39491
Sequence Length: 351
Subcellular Location: Endoplasmic reticulum membrane
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Q9VHG4 | MLRVFVIFSLFIAAINASGEFTVLNRPKAISFKGNDALESHYVGDVLYASMGNAVSGDTNWNGLTINDPFNLAKGVILVHVQGIGHVTTAGNVKTYELTGSGTDASLNALAAELEAANEPVCDINFEQFDDGVQAWKSCFGDFEAPAAKPTKHLNPSLHTADKQFLQEVGFINSAADHLAEMAKPSNVLMLRVSVDGVAKAHGEKSVAVEEANKLLSAAISRLLAASQKSSDSVLFVQTTEKDVAASRAKRDTIAASTTNPYNLAVYYGSDYPVIFNIILWFMVVFGLSLLAICYAIAAMDPGRDSIIYRMTSTRIKKDN | Function: Multifunctional protein which functions as transmembrane receptor in the planar cell polarity (PCP) and is involved in the assembly of the proton-transporting vacuolar (V)-ATPase protein pump . As transmembrane receptor mediates fz/PCP signaling through interaction with fz and stabilizes asymmetric PCP domains through its interaction with stan . Also mediates Wnt/beta-cat signaling through interaction with fz/fz2 . Probably by controlling the assembly of the V-ATPase pump and thus the acidification of the endo-lysosomal system, plays a role in many neuronal processes including synapse morphology and synaptic transmission .
PTM: Proteolytically cleaved by a furin-like convertase in the trans-Golgi network to generate N- and C-terminal fragments . Cleavage is reduced in the fat body .
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 34421
Sequence Length: 320
Subcellular Location: Cell membrane
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O75787 | MAVFVVLLALVAGVLGNEFSILKSPGSVVFRNGNWPIPGERIPDVAALSMGFSVKEDLSWPGLAVGNLFHRPRATVMVMVKGVNKLALPPGSVISYPLENAVPFSLDSVANSIHSLFSEETPVVLQLAPSEERVYMVGKANSVFEDLSVTLRQLRNRLFQENSVLSSLPLNSLSRNNEVDLLFLSELQVLHDISSLLSRHKHLAKDHSPDLYSLELAGLDEIGKRYGEDSEQFRDASKILVDALQKFADDMYSLYGGNAVVELVTVKSFDTSLIRKTRTILEAKQAKNPASPYNLAYKYNFEYSVVFNMVLWIMIALALAVIITSYNIWNMDPGYDSIIYRMTNQKIRMD | Function: Multifunctional protein which functions as a renin, prorenin cellular receptor and is involved in the assembly of the lysosomal proton-transporting V-type ATPase (V-ATPase) and the acidification of the endo-lysosomal system . May mediate renin-dependent cellular responses by activating ERK1 and ERK2 . By increasing the catalytic efficiency of renin in AGT/angiotensinogen conversion to angiotensin I, may also play a role in the renin-angiotensin system (RAS) . Through its function in V-type ATPase (v-ATPase) assembly and acidification of the lysosome it regulates protein degradation and may control different signaling pathways important for proper brain development, synapse morphology and synaptic transmission (By similarity).
PTM: Phosphorylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 39008
Sequence Length: 350
Subcellular Location: Endoplasmic reticulum membrane
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Q9CYN9 | MAVLVVLLFFLVAGALGNEFSILRSPGSVVFRNGNWPIPGDRIPDVAALSMGFSVKEDLSWPGLAVGNLFHRPRATIMVMVKGVDKLALPAGSVISYPLENAVPFSLDSVANSIHSLFSEETPVVLQLAPSEERVYMVGKANSVFEDLSVTLRQLRNRLFQENSLLNSLPLNSLSRNNEVDLLFLSELQVLHDISSLLSRHKHLAKDHSPDLYSLELAGLDELGKRYGEDSEQFRDASKILVDALQKFADDMYSLYGGNAVVELVTVKSFDTSLVRKSRTILEAKQENTQSPYNLAYKYNLEYSVVFNLVLWIMIGLALAVIITSYNIWNMDPGYDSIIYRMTNQKIRID | Function: Multifunctional protein which functions as a renin, prorenin cellular receptor and is involved in the assembly of the lysosomal proton-transporting V-type ATPase (V-ATPase) and the acidification of the endo-lysosomal system (By similarity). May mediate renin-dependent cellular responses by activating ERK1 and ERK2 (By similarity). By increasing the catalytic efficiency of renin in AGT/angiotensinogen conversion to angiotensin I, may also play a role in the renin-angiotensin system (RAS) (By similarity). Through its function in V-type ATPase (v-ATPase) assembly and acidification of the lysosome it regulates protein degradation and may control different signaling pathways important for proper brain development, synapse morphology and synaptic transmission .
PTM: Phosphorylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 39092
Sequence Length: 350
Subcellular Location: Endoplasmic reticulum membrane
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Q6AXS4 | MAVLVVLLSSLVSSALANEFSILRSPGSVVFRNGNWPIPGDRIPDVAALSMGFSVKEDLSWPGLAVGNLFHRPRATIMVTVKGVDKLALPTGSVISYPLENAVPFSLDSVANSIHSLFSEETPVVLQLAPSEERVYMVGKANSVFEDLSVTLRQLRNRLFQENSVLNSLPLNSLSRNNEVDLLFLSELQVLHDISSLLSRHKHLAKDHSPDLYSLELAGLDELGKRYGEDSEQFRDASRILVDALQKFADDMYSLYGGNAVVELVTVKSFDTSLVRKSRTILETKQENTQSPYNLAYKYNLEYSVVFNLVLWIMTGLALAVIITSYNIWNMDPGYDSIIYRMTNQKIRMD | Function: Multifunctional protein which functions as a renin, prorenin cellular receptor and is involved in the assembly of the lysosomal proton-transporting V-type ATPase (V-ATPase) and the acidification of the endo-lysosomal system (By similarity). May mediate renin-dependent cellular responses by activating ERK1 and ERK2 (By similarity). By increasing the catalytic efficiency of renin in AGT/angiotensinogen conversion to angiotensin I, may also play a role in the renin-angiotensin system (RAS) (By similarity). Through its function in V-type ATPase (v-ATPase) assembly and acidification of the lysosome it regulates protein degradation and may control different signaling pathways important for proper brain development, synapse morphology and synaptic transmission (By similarity).
PTM: Phosphorylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 39082
Sequence Length: 350
Subcellular Location: Endoplasmic reticulum membrane
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P82708 | MPPNLTGYYRFVSQKNLEDYLQALNVNMALRKIALLLKPDKEIDQRGNHMTVKTLSTFRNYVLEFEVGVEFEEDLRTVDGRKCQTIVTWEEEQLVCVQKGEVPNRGWRLWLEEEMLYQEVTARDAVCQCVFRKVK | Function: Intracellular transport of retinol.
Sequence Mass (Da): 15962
Sequence Length: 135
Domain: Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior.
Subcellular Location: Cytoplasm
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P82980 | MPPNLTGYYRFVSQKNMEDYLQALNISLAVRKIALLLKPDKEIEHQGNHMTVRTLSTFRNYTVQFDVGVEFEEDLRSVDGRKCQTIVTWEEEHLVCVQKGEVPNRGWRHWLEGEMLYLELTARDAVCEQVFRKVR | Function: Intracellular transport of retinol.
Sequence Mass (Da): 15931
Sequence Length: 135
Domain: Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior.
Subcellular Location: Cytoplasm
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Q96R05 | MPADLSGTWTLLSSDNFEGYMLALGIDFATRKIAKLLKPQKVIEQNGDSFTIHTNSSLRNYFVKFKVGEEFDEDNRGLDNRKCKSLVIWDNDRLTCIQKGEKKNRGWTHWIEGDKLHLEMFCEGQVCKQTFQRA | Function: Intracellular transport of retinol.
Sequence Mass (Da): 15536
Sequence Length: 134
Domain: Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior.
Subcellular Location: Cytoplasm
|
Q9EPC5 | MPADLSGTWNLLSSDNFEGYMLALGIDFATRKIAKLLKPQKVIEQNGDSFTIQTCSSLRNYLVKFKVGEEFEEDNKGLDNRKCTSLVTWENDKLTCVQRGEKKNRGWSHWIEGDQLHLEMFCEGQVCKQTFQRA | Function: Intracellular transport of retinol.
Sequence Mass (Da): 15428
Sequence Length: 134
Domain: Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior.
Subcellular Location: Cytoplasm
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B9DFK5 | MAGCAMNLQFSSVVKVRNEISSFGICNRDFVFRDLAKAMKVPVLRIRGGSGRQRSRLFVVNMSQSPIEPQSGGFAATEQIKGEGDNSILGKDNVRNLGTDQLENLDIDGNVGDGFNGSDGNGGGGGGGNGGEGDGEGEDYEEKEFGPILKFEEVMKETEARGATLPSDMLEAAKNYGIRKVLLLRYLDLQSSAGLLGFAIRSWAMLRNRMLADPSFLFKIGAEIVIDSCCATVAEVQKRGKDFWAEFELYVADLLVGTVVNIALVGMLAPYVRFGQPSASPGFLGRMVFAYNALPSSVFEAERPGCRFSAQQRLATYFYKGIMYGAVGFGCGIVGQGIANLIMTAKRNINKSEENIPVPPLIKSAALWGVFLSVSSNTRYQIINGLERVVEASPFAKKFPPAAMAFTVGVRLANNIYGGMQFVDWARLSGCQ | Function: May play a role in leaf development. Required for leaf mesophyll cell division in the early stages of leaf organogenesis . Acts in a developmental pathway that involves PPT1/CUE1 but does not include ASE2/DOV1 .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46629
Sequence Length: 432
Subcellular Location: Plastid
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B2UL99 | MDYTPLIEKRRQRLEELETVIAEPDFFNDQKKASEIMREHRRLKELMETWDSLNATEQQLADNQELAKTDDPELAELAALEIPELEAALEKLRSDVQYSLLPRDTTEDRDAIIEIRAGTGGDEASLFAGDLLRMYQRFAEERGWRFEHLESSPSDVGGFKEVVCRIAGEEVFRFLKYEGGVHRVQRVPATETQGRIHTSTATVAVMPEAEEVDIEIRPEDLRIEVCRSGGAGGQHVNKTESAVQIWHIPTGVYVRCEEERSQMKNREKGMKILRAKLFEAKKREEAEKYSAARRNLIGSGGREEKIRTYNFPQNRLTDHRIGYTSHNLDGILMGQLEDLIMALQHAEMQERLAEAGMS | Function: Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
PTM: Methylated by PrmC. Methylation increases the termination efficiency of RF1.
Sequence Mass (Da): 40973
Sequence Length: 358
Subcellular Location: Cytoplasm
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P56905 | MANMSRLNELVSEFGLVERRLGDPQALADGREYARLTRRHRELLPLVTLVREREQAEADLSGARELLQDPDMRDPDMKELAQLEVGGLQARLAEIEAELEVLLLPTDPDDGKDVILELRAGAGGAEAGLFVMDLLRMYERYAAGLNLKLNVLDAAESDLGGASKVVAEVTGDFAFRALKWERGVHRVQRVPATESQGRIHTSTATVAVLPEAEPGEVNLDLSEVRIDVFRSQGAGGQGVNTTDSAVRAVYRAGTPDEIMVICQDGRSQIKNREKALQVLTARLAERERAAREAQERQERASQVGSGDRSEKIRTYNYPQNRVTDHRLEGEDKNHPLDAVMAGGLAPVVSALARAQREEQLLAMSQEGAEDQHGAA | Function: Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
PTM: Methylated by PrmC. Methylation increases the termination efficiency of RF1 (By similarity).
Sequence Mass (Da): 41126
Sequence Length: 375
Subcellular Location: Cytoplasm
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B8E003 | MLQKLVIDKLEEIEKRFEEIEGLLAKEDVISDFNKYQSLLKERAKIEEIVDKFREYKRLLKEKEDLEEMVKEEQDEDLRSLAETELEDIQEKLEKVEFELKALLLPKDPNDEKNIIMEIRAGTGGEEAALFAADLFRMYLGYAQKKGWKVEIVSSNPTGLGGFKEIIFIVEGKGAYSRLKFESGVHRVQRVPITESSGRIHTSTATVAVLPEMEEIEVEIDPKDLRIETFRSGGAGGQHVNKTESGVRITHIPSGIVVQCQDERSQHQNREKAMKVLRARLYEYYQREKENEIASQRRQQVGTGERSEKIRTYNFPQRRVTDHRINYSSFQLEEVLSGELDEFIDRLILAEKEEQIKKLFEEVGATS | Function: Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
PTM: Methylated by PrmC. Methylation increases the termination efficiency of RF1.
Sequence Mass (Da): 42486
Sequence Length: 367
Subcellular Location: Cytoplasm
|
B1MLV1 | MSETPLIDAMLAEHAELEKQLADPALHADAAAARKAGRRFAMLSPIVATHRKLATARDDLATARELSADDPSFADEVTELESSIAELETQLSDMLAPRDPHDGDDILLEVKSGEGGEESALFAADLARMYIRYAERHGWKVTVLDETESDLGGYKDATLAIASKGDSADGVWSRLKFEGGVHRVQRVPVTESQGRVHTSAAGVLVYPEPEEVEEIQIDESDLRIDVYRSSGKGGQGVNTTDSAVRITHLPTGIVVTCQNERSQLQNKARAMQVLAARLQALAEEQAQADASAGRASQIRTVDRSERIRTYNFPENRITDHRVGFKAHNLDQVLDGDLDALFDALAAADRKARLQEA | Function: Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
PTM: Methylated by PrmC. Methylation increases the termination efficiency of RF1.
Sequence Mass (Da): 38804
Sequence Length: 356
Subcellular Location: Cytoplasm
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A5IZH6 | MEKTMFKSLSEIKQSYLELLKKIDDPEVISNIKEYSAINKEIAKIREISEKFITYENILKDVEQAKIMLESKNEEEVEFAKMIIDENSLKLDELEEKLKILILPQDENDDKNIIVEIRGAAGGDEANIFAGDLFRMYSKFADELGFRLKILSTNSASAGGFSQIVFSIKGEKAYSKFKFESGVHRVQRVPVTESQGRIHTSTTTVTVMPEIDDSVEIEIKPSDLKIDVFRSSGAGGQSVNTTDSAVRITHLPTNIVVTSQDERSQIANRETALTILKSKLYDLEMQKKAEEESGYRKLAGHGDRSEKIRTYNYPQDRVTDHRISFSTSLKPIMEGKLTPIIDALLAEEQNQKIKESGF | Function: Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
PTM: Methylated by PrmC. Methylation increases the termination efficiency of RF1.
Sequence Mass (Da): 40472
Sequence Length: 358
Subcellular Location: Cytoplasm
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