ids
stringlengths 6
10
| seqs
stringlengths 16
1.02k
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stringlengths 117
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A0A1S3KHL3 | MANSMLADVFVAGCRGEVLVPNGLVEGRTHGWRSLFSGHGSRIQLLQQNMLYKILVTERGKNGGQLAVILNTANYEVKKEEWHEIKTSDGKLFAFKFDKNDKQFVVFQAELKRVLQLETRPLRRGGRNREQTNTKCSPGAAKDGNMASGREVADAIPFYSSDSSFSGNTASQQYVDMYVNAIPKEPYDSTEEWKYKGGGGHPRDYSAPTASFSSKAKAARSYSAYAPPPEAHEQPATPLSSRGGAGGVQRREEQVHSRSLSTGLQNLIESLQSAIYKGEGEQAGIVAKSLAIKRANIKMELYQSGDSGKSTEKMISLKVYVEDKSNSGTSIMLKVRLSMTIRDLKRHMFLEHQFPPEVQRWIIGKSRAKDDDHLNKFKQLIHDGSPVYLYLMSAKSVGLPGRQVYEREHNMGQADLIPVDVCDEPAVAAPTTPPHPASQQRAAAPGHQNVPEPRRPSGSEETLRPPQQQQQQRLQQLPQQQQRQQQLPQQQQPVDTAEGWSCPQCTYVNLPLRPGCAMCAADRPADYREPDNYVPTDEELQMMAQQQELDRQALEYQERRRRQEGQQRLENYQQLLHAADQSLVVNTEDFTCPICFDDIAPGDGVVLRDCLHMFCKSCLKAAVTYSEEAAVKCPYQDDNYTCPSFLQDMEIKALVSNEVFQKYLQLSLSQAESQAVNSYHCKTADCRGWCIYEDEVNFFDCPVCGKKNCLTCKAIHEGINCKQYQEDLKIRAGNDKAAKQTNDMLEKLIRDGDAMRCPHCRVIVQKKDGCDWIKCSFCKTEICWVTRGPRWGPAGPGDISGGCMCRVNAQRCHDNCQNCH | Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.31
Catalytic Activity: [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.
Sequence Length: 820
Sequence Mass (Da): 92006
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A0A6G1FWJ7 | MRILSTISLAVLAAAAPVELVERQFGGGGGGSTSNELTQGSCKEVVFIFARGSGEPGNIGMIIGPPLISALKALVPNTAVQGVPYSAGIAGNLQRGGTDQASINTATQIFNQANTKCPDSIIIAGGYSQGAALMHRTIEKLPDNVKNKIAAVVTFGDTQNEEDKGTIPNFPPEKVKIFCNENDGVCGASLSVNAGHMSYSTSMKPAAQFLADGVNKAKQGGGASSGSSSGSSSDGSSGSPTGGPSGLGGLGGISGGGGLGGLSGSGGLSGLSGGLGGLRGGGLGGLMSGGRGGLGGLRGGS | Function: Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants. Degrades cutin, a macromolecule that forms the structure of the plant cuticle.
Catalytic Activity: cutin + H2O = cutin monomers.
EC: 3.1.1.74
Subcellular Location: Secreted
Sequence Length: 301
Sequence Mass (Da): 29126
|
Q8T3U8 | MSRRVFGLSIKSFRLFRRTPIHPPAFQHFSGGVFRTSFRSFCDCQEHRRMDLPEGILMGFGNPLLDITCTVEDNVILEKYGLEANAAIIADEKHDALFDELMNMENVIYSAGGACQNSMRIFQWIVQTPFRAVFIGSVGKDKLGDRIEKRAKSDGLLTLYQLKEELPTGSCAVIINGPNRSLVANLGAASLFSDDWIDEDDNICALDRAEYFYFTGFFLAVCPPAVERVARMCCETNRIMILNFSAVFVLQMQKEALGNILQYVDIIICNKEEAIAFSDTNDWKTKNIFEIGSRLQQMPKENTRPRLVMITDAVCPVLVFQDNDRVLEYPVPPVKQGEIFDTNGCGDAFVGGFLAMYVQRMPLDYCIRTGIFASQQVLHVVGVQIDKLPKFSEKCI | Cofactor: Binds 3 Mg(2+) ions per subunit.
Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenosine: step 1/1.
Function: ATP dependent phosphorylation of adenosine and other related nucleoside analogs to monophosphate derivatives.
EC: 2.7.1.20
Subcellular Location: Nucleus
Catalytic Activity: adenosine + ATP = ADP + AMP + H(+)
Sequence Length: 396
Sequence Mass (Da): 44676
|
A0A7J4JU34 | MLDISFVRQNPLEVRSNLAKRQDKGILERFDSLLSVDKEWRSLKQKVDELRSMRNLISKEIEALVKQGKATQEKINEARAIPEQIKSSEARMRELDEKRLSLLMAIPNLLHESVPFGKDETENKVIRVWGKLSKPDFEIQHHGQLAVRLGGADFEKAVQVSGEGFYFLKNELALMEQALSQYAIHYLVKKGFTFVKPPFLLRRKPLSGALDLSEFESVIYKIEGEDHYLIGTAEHSLNALHFEEILDSNQLPLLYAGFSTNFRKEIGKHGLDERGLFRLHQFDKVEQFVFCKPEDSWKLHERLLKNAEEIVQGLELPYRVVNVCTGDIGTVAAKKYDIECWSPREGKYFETHSLSNCTSYQAVRSGIKYRISQTEKAFVHTLNATAIAAPRALRAILENHQSSDGTVKVPKALQPFMLGVKEIVPLDLQKQKPQIPQPSKKHAHKLLKRKPRRK | Pathway: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1.
Function: Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).
Catalytic Activity: ATP + L-serine + tRNA(Sec) = AMP + diphosphate + H(+) + L-seryl-tRNA(Sec)
EC: 6.1.1.11
Subcellular Location: Cytoplasm
Sequence Length: 454
Domain: Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding.
Sequence Mass (Da): 52044
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A0A8T6MEG4 | MINMDIEKIYKILEKELKEYTIPLAEQIDIKSKNSFYVLIGTMLSARTKDQITAKVCDNLFKEIKNTDDLIKIKIEKLEQLLYPVGFYKTKAKNLKLLAKKLKEDFNNKVPRTIEELITLPGVGRKTANLVIAVSYKIPAICVDTHVHRIFNRIGYIETKNPLETEMVLRNKLPKKFWIDTNYLFVILGQNICFPRNPNCEKCPINKICLKKIK | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.
EC: 4.2.99.18
Catalytic Activity: 2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-2'-deoxyribonucleoside-DNA + H(+)
Sequence Length: 214
Sequence Mass (Da): 24904
|
A0A6J0L7K7 | METSDRISSGVTVIGAEAPSTFHIAPRPSESPNQFLGSSLAPTEAPMPSAGSGDAFGKKKRGRPRKNEANGALLPMQIFSSAPLVKKQRRGKLNGLDMKMHNKRMGFHTCGERLGGVGSNFTPHIITVKAGEDITMRVISFSQQRPRAICILSANGVISSVTLRRPDSCGGTLTYEVCLSHSTLYQI | Function: Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs).
Subcellular Location: Nucleus
Sequence Length: 187
Domain: The PPC domain mediates interactions between AHL proteins.
Sequence Mass (Da): 20069
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A0A2I4GPM5 | MEIMKKPKTKIVCTLGPASRSVPMLEKLLRAGMNVARFNFSHGSHDYHQETLDNLRTAMENTGILCAVMLDTKGPEIRTGFLKDSKPIQLKQGQEITISIDYSIKGDENMICMSYKKLAVDVKPGMVILCADGTISFTVLSCDKESGFVRCRCENSAVLGERKNVNLPGVVVDLPTLTEKDNEDILHWGIPNKIDMIALSFVRKGSDLVEVRKLLGNHAKNILLMSKVENQEGVANFDDILANSDAFMVARGDLGMEIPIEKIFLAQKVMIYKCNIQGKPVVTATQMLESMIKSPRPTRAEATDVANAVLDGTDCVMLSGETAAGAYPELAVRTMAKICLEAEGTLDYGDVFKRLMQHSPVPMSPLESLASSAVRTANSAKAAVILVLTRGGSTAKLVAKYRPGMPILSVVVPEIKTDSFDWSCSDEAPARHSLIFRGLVPVLSAGSARASDAETTEEALEFAIQHAKARDLCKNGDSVVALHRVDNASVIKILTVK | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
EC: 2.7.1.40
Catalytic Activity: ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate
Sequence Length: 497
Sequence Mass (Da): 54011
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A0A1I8MZP5 | MNGLNAAKDIGLSWIRPPESEIAFPDIKKPLPIGFFSIDGDRMFEPSDAQLKYYKSPAPETFPLDLNAGLNRVIHKPESVRNELLDHLLRFLYDHQQRIFVNSPAPEFVSYRGLLRLLMCTPYEHRNDWCIHVTRFKNTIYLVERETEQKRYERSQESQFVKNCCSWGFKFEQYCLSDSPFREPDTSSPVNESEEFSLVFHTRLAGMNLLYGAEMDGIISEQPVQLNYDKPVIENLKFVELKTRQGQGQRINFLKFKSRNWWCQSFLVGIEDLYVGIRNDKGFVRSLEHVETRSLPKNGAQNHWSPSVCANFLSQFLCRLKALTANLNCPYTVYEFYFNSRTGQINYVCLPGKTEHSFLPDWFVESISRLLKNTPR | Function: Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA.
EC: 3.6.1.-
Subcellular Location: Nucleus
Sequence Length: 376
Sequence Mass (Da): 43886
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A0A2I4ENL6 | MKHLALALVLAILIHRQCFHIGVEAGDGFIRTRGIHFLLNGNPYYANGFNAYWLMYVASDPSQRPKVSAAFREASSHGLTVARTWAFSDGGYRPLQYSPGSYNEQMFKGLDFVIAEARRYGIKLILSLANNYDSFGGKKQYVNWARNQGQYLSSEDDFFRNPVVKGYYKNHIKTVLSRYNSYTGIHYKDDPTIMAWELMNEPRCTSDPSGRTIQAWITEMASYVKSIDRNHLLEAGLEGFYGQSTPQRKGLNPSLEIGTDFIANNQIPGIDFATTHSYPDQWLPSSNDQFQLSFLNNWLNAHIQDAQYILRKPILLTEFGKSWKVAGFSTYQRDLLFNTVYYKIYSSAKRGGAAAGGLFWQLLSEGMDSFRDGYEIVLSQSPSTANIIAQQSHKLHQIRKFFERMRNIERWKRAMATRRAQWLARNRGRRIGN | Catalytic Activity: Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.
EC: 3.2.1.78
Subcellular Location: Secreted
Sequence Length: 433
Sequence Mass (Da): 49640
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A0A6G1FXC6 | MKASWIVFLPSLVSAHYTFPVLNKTPDWSHVRQTANDGSAGNFPITDLDSPMMRCFEKSGHEPASTLDVQAGRTLTFTASNGLGHPGPFLLYMAKVPSGQKASSWDPSGNVWFKIQEYGPKVTAQGYQWEINGSTRDVPVTIPKDVPSGEYLLRVEHIAIHIPETPQIYISCGQINVQGGGNGQPKPLVAFPGAYSKNDPGIAVYRQWDSVPSENVPMPGPPVWKG | Function: Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds. Involved in the degradation of complex natural cellulosic substrates.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
EC: 3.2.1.4
Subcellular Location: Secreted
Sequence Length: 226
Domain: Has a modular structure: an endo-beta-1,4-glucanase catalytic module at the N-terminus, a linker rich in serines and threonines, and a C-terminal carbohydrate-binding module (CBM). The genes for catalytic modules and CBMs seem to have evolved separately and have been linked by gene fusion.
Sequence Mass (Da): 24617
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A0A8C4RMP3 | MWEQIWEIAANNPNITVSHVDAHTKGTDAEALFNAVADAQTKTATVTIMEHGTDMAKWAHERGGHLGAAATVKWAHPDAKLPIRGSEGAAGLDLYAIQDETVTERVTIINTGIGVKIPKGHYGHVCPRSSLALKGVTVLAGVIDADYQGTVKVLLQSSMGDPIKLTKGDRIAQLLIIPVHMGKVQESTAPVVKTGRNVGGFGSTDNPHNKTVTCRTNN | Pathway: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2.
Function: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.
EC: 3.6.1.23
Catalytic Activity: dUTP + H2O = diphosphate + dUMP + H(+)
Sequence Length: 218
Sequence Mass (Da): 23156
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B0XJ66 | MLRPYYGLYLVLGMVFRVTEAVIGLLKLDLVARALEAKFGNFIIGLNDSRPKEDAPTDSVSKTELDHLAKMVTFWWNKTGPAKMLHTFYQVRVPLVVEGLAETGRISKADISKPDSLKGVRILEAGCGGGVLAEDLARLGAYVVGVDPGTEMIDLAKRHLETESADLKDRLEYHAITVEEHAKKFAGTYDAIVCSEVMEHVDEKVPILEACVRCLKPGGSLFVTTENQTMLAWFMFIIIPEYILKFIPKGTHFYEKFVSPGQISKILDQYQCKTKRVRGFFYDRMFNSWSFIESDECNYGLHAVKK | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.
Catalytic Activity: 3,4-dihydroxy-5-all-trans-polyprenylbenzoate + S-adenosyl-L-methionine = 3-methoxy,4-hydroxy-5-all-trans-polyprenylbenzoate + H(+) + S-adenosyl-L-homocysteine
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 306
Sequence Mass (Da): 34487
Location Topology: Peripheral membrane protein
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A0A2D6K6U1 | MFDIGFWELAIIGVIALLIIGPERLPKAARTAGFWVGRARRLVSDLKADIDKEIRDSEIDELKEAGEALNEVRSDIEKETETFTDRIVDEEYDSFGDPLSHRDDAEPGKTTPSSPPTEDQNGNLADSAQSRHSGDPSND | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation.
Subcellular Location: Cell membrane
Sequence Length: 139
Sequence Mass (Da): 15370
Location Topology: Single-pass membrane protein
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A0A1I8N4J6 | MSLLLQINDCQLVKLQQNPEYMTRPKLVKIYDINYTRFSPAKKFRYLFKEPSQYPLDLNNVVGDPIEIKHSTQNNLLHPLLNTYFEDHNEKSLLEEDIDDDDNRNANKVEMTDVYSRRGILERIMGFYYEKNDFSALVSRCNGKLFVVELPQSEDAFERNQSGNNTHHRRFCQITSVDTMPELSDCNDDNIFQVAIHEANLGKYNLHYVARAPAIKVTEASKNDLKNLRDVEFVSTKQMWSSIRDKSTKFLKYWLQSYLSNVRELYIAYKDSKGMVSSPIECWKTCDIPKNYLWKPRVCTTFLNEFLNKVEEIMANINSLDIVFEFAFNTSTRSVTYFKKSGVGFIPKEYADRIQEKIV | Function: Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA.
EC: 3.6.1.-
Subcellular Location: Nucleus
Sequence Length: 359
Sequence Mass (Da): 42077
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A0A8H3GZZ1 | MSTNITFHPGAVEKNERTQLLGQKGLTLWLTGLSASGKSTIAVALEQQLLQSKKLAYRLDGDNVRFGLNKDLGFSEKDRNENIRRISEVAKLFNDAAAIAITSFISPYRSDRQFAREIHEKAGLTFVEVYIDAPLSVVEARDPKGLYKKARAGEIKDFTGISAPYEPPEKAEIHIHTDHSSVEDSSYILDTMATTTTRPIVFMDINIGETPAGRLKMELFSDIVPKTAENFRQLCTGEHRRVLCLKPLLLTLRPVTDVRDFMVQGGDFLNGDGTGSFSIYGDKFPDENFEMKHTGPGLLSMANSGPNTNGCQFFITAATCDFLDGKHVVFGKVIDGILTLRKIENVATGPNNRPKLTVKITGEILTTHWQALTAFRAYATDWIDDRMWRDVRS | Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3.
Function: Catalyzes the synthesis of activated sulfate.
EC: 2.7.1.25
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Length: 393
Sequence Mass (Da): 43752
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A0A8T5F405 | MKLIFLGPPGSGKGTQAKILSNNVNIPQISTGDLFRENIKNKTELGIKAQSFMDQGYLVPDEVTNGMAKERLERNDCESGYILDGYPRTIPQAKFLDTVQNIDKVVNFELNEEEVVKRISGRRTCKTCGEMFHLMFKKPQKEGICDKCSNGLIQRPDDAPESVKVRLEVYKKQTEPLIEFYKDQGKILNVSALSSIDEIASKVKEVLEL | Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1.
Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
EC: 2.7.4.3
Subcellular Location: Cytoplasm
Sequence Length: 209
Domain: Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis. Some bacteria have evolved a zinc-coordinating structure that stabilizes the LID domain.
Sequence Mass (Da): 23545
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F9CZJ4 | MFKDFLLVGTGSFLGGGMRLLVSRLLTAWVPTPFPLGTFTVNVLGCLLIGFFSGQPVGSGHLSPAARLLLTTGFCGGFTTFSTFMSEHTALVKDGQYFYVTLYLLGSLALGLVAVLAGHQLAKLV | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell inner membrane
Sequence Length: 125
Sequence Mass (Da): 13206
Location Topology: Multi-pass membrane protein
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A0A336LWH4 | MDYHLLINFVISIGAYFLTVNLIPSLKPMFLKANLFGIDMNKKSSGKVPEAMGVVTGCIFLISLFLFIPVPFSSALVSREGDFPHDEFVELIAALLSICCMILLGFADDVLDLRWRHKLLLPTVASLPLLMVYYVNFGSTTVIMPNFVRSYIGFSLDIGFLYYIFMGMLAVFCTNAINILAGINGLEVGQSLVIAGSIIIFNFIEMQNPVVSEAHRFSLYFMLPYFATTFALWKFNRYVNFYNLPL | Pathway: Protein modification; protein glycosylation.
Function: Catalyzes the initial step of dolichol-linked oligosaccharide biosynthesis in N-linked protein glycosylation pathway: transfers GlcNAc-1-P from UDP-GlcNAc onto the carrier lipid dolichyl phosphate (P-dolichol), yielding GlcNAc-P-P-dolichol.
Catalytic Activity: a dolichyl phosphate + UDP-N-acetyl-alpha-D-glucosamine = N-acetyl-alpha-D-glucosaminyl-diphosphodolichol + UMP
EC: 2.7.8.15
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 246
Sequence Mass (Da): 27704
Location Topology: Multi-pass membrane protein
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A0A2I4E5Q3 | MKRELDPNLHSLADSSITASASSGSSTGKAKMCWEDEVQPDGGMDELLAVLGYQVRSSDMAEVAQKLELLEDLMGNAQGDGLSQLATDTVHYNPSDLSTWLQSMLSELNPPCNDFDPIVPPAAGAPPAPLDDSLLALAESSTITSIDFDKQNNNSHNRVFEESSSSDYDLKAIPGKAMYSQPQSQIEYSPSSRDSKRLKSSSASGSNPDISFSGSSTTVGGGFTVSTESTRPVVLIDSQENGIRLVHALMACAEAVQQNSLGLAEALVKQIGYLAVSQAGAMRKVATYFAEALARRIYKLYPKNPLDHSLSDILQMHFYETCPYLKFAHFTANQAILEAFEGKKRVHVIDFSMNQGMQWPALMQALALRPGGPPAFRLTGIGPPAPDNSDHLQEVGWKLAQLAETIHVEFEYRGFVANSLADLNASMLDLRPREVESVAVNSVFELHKLLARSGAIEKVFSVVKQMKPDIVTVVEQEANHNGPVFLDRFTESLHYYSTMFDSLEGSVSNQDKVMSEVYLGKQICNVVSCEGVDRVERHETSVQWRARLGSAGFEPVHLGSNAFKQASMLLALFAGGEGYRVEENNGCLMLGWHTRPLIATSAWQLAGKATLAH | Function: Transcriptional regulator that acts as a repressor of the gibberellin (GA) signaling pathway. Probably acts by participating in large multiprotein complexes that repress transcription of GA-inducible genes.
Subcellular Location: Nucleus
Sequence Length: 613
Domain: The DELLA motif is required for its GA-induced degradation.
Sequence Mass (Da): 66771
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A0A0J1I6N8 | MKKLSIKLGILFFIIIFGLEAFMFSYLHSSLVNVRIEEELSALQARGNSHRDILEKHFEEDSISHVILMESEALTDVVIVNQKGDILGTSFDNNNYKKYLIQQKKELKSEGKVVEDDWKNKPYIITLSPIMQKNETIGYVYMYQETASIHTLIGRLNEHFVLAGIIALLLTFVVIVLLTRALTKPLVKMREATYQISKGNFLVDLPRTSNDELGELAVSIKELARDLNFLKKERNDFLASISHELRTPLTYIKGYADISLRKNIEEEEKEKYLQIIVEESNRLSSLIEDLFELAKIDKNTFLIQKQQINLNELLGKLQIKMFPAFKEKEIDLTIFCPKTTSFYGDPARMEQILFNLLDNAMKYSPVKSKVDVMVRFRKKETEITIKDNGKGIPEEDLPYIFNRFYRVDKSRTRSLGGYGLGLSIVQELVQAQEGTIRVESKLNIGTTFILTFKNLGGEIK | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 460
Sequence Mass (Da): 52901
Location Topology: Multi-pass membrane protein
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B0W9Y7 | MGSFINSKDFPVEKRDAIIKAFARIDQRVVWKFEDESIPDLPNNVLIQSWLPQNDILAHPNVKVFITHGGLLSGTEALYHGKPIVGIPIFGDQTMNVQRAVKAGYGVELQYKDITKSSIRNALDKVLRDPKYAETARSISRRYHDKPMSTKKTALYWLEYVIRYQGAPQLRSPAMALTLIEYCSIDVYSLVVTISYATGARILGILPMGAKSHNIIGAAYMKALAAAGHEVTVVSPYTLKTPPKNYRDIELTGMLEAMDDQEKNLFNYKGSGIGSFFIMMYVLYGKLPEVVGKLVLQHPNVVKLLNSNEKFDLVIVESFLTESLYGFAQHFDAPLVTYSTFGNSMWTNDLVGTPAPPSHVAHFLLSYADRMAFWERLVNTVVTILDRVVFEWYYLPKQREFYEVGFPNAKISFEDQMKNVSLVFLNQHFSVSSPRPYAPNMVEVGGIQVEKPKALPKMFTEF | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 462
Sequence Mass (Da): 52194
Location Topology: Single-pass membrane protein
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A0A2I4FDC1 | MGIKDLLRFMKPHIEPIHIKKYAGKRVGIDAYSWLHKGAYSCSMELCLNSDSDRKMRYLEYFMHRINLLRHHKVTPVVVFDGGNIPCKAATEEERHRKRKANRDLAMAKLKQGDASAAYELFQRAVSITPSMAHQVIQVLRSENIEYVVAPYEADAQLAYLCSLEAEKGGIISVITEDSDLIAYGCQAIVFKMDKFGNGEEIVLDKIFGSVALTPSFRNFDMDLFTGMCVLAGCDFLSSIPGIGIGKAYALVSKYRNLDRVLSVLKFEKGNQMPDDYSKSFTEAVAVFQHAQIYDIDTKKLKHLKPLPEKLLQSLNGELEFLGPEMPTSIASAIAEGYLDPISMEAFDHFPSSGCHPDSLVIQSSGQLESLEAAAVSTQESCITISSSHKTSKTDVSEKQTSVSNSSKYLKEAAALEKLLLPSEIHGTVEIPTVQNRNSLKAPDNNPFKKRKWDEIQLDPIESITEQVSFATDESLGILCVTPDNTPLKVLDKSPRKRRLSDIQSDQTAGHVSGITDLGYSETMCINLESQESVNSKPKRVANGRRREKIEKSKRGSSKSSENKKSNSILNFFSRV | Cofactor: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.
Function: 5'->3' double-stranded DNA exonuclease which may also possess a cryptic 3'->5' double-stranded DNA exonuclease activity. Functions in DNA mismatch repair.
EC: 3.1.-.-
Subcellular Location: Nucleus
Sequence Length: 576
Sequence Mass (Da): 64065
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A0A2I4GVN3 | MPVVQKLYDACKVSFSTDGPVSEEALRKVRSSLDELKPSNVGLEQEAQLARQWKASVKGSNGKKGRNGPNGCHQWPPPIKYLHLHECAKLSIGIFCMLPGSIIPLHNHPGMTVLSKLLYGSLHVRSYDWLDIPGSGSADLSQARPAKLVRDCEMSAPCGTTILHPSSGGNIHCFKALTPCAIFDILSPPYSSEDGRHCSYFRKSPRGDLPDIDELCGIEPSEVAWLEEIQPPENLVVQRGLYRGPVIRS | Function: Seed storage protein.
EC: 1.13.11.20
Catalytic Activity: L-cysteine + O2 = 3-sulfino-L-alanine + H(+)
Sequence Length: 249
Sequence Mass (Da): 27308
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A0A1C0B9E4 | MTKKQLILYVTIFSSLVITANYTVQFPINEWLTYGAIMFPFTFLLTDILSENFEKKEVLNVIKYGVLIAIIPTILIAGWQIAFASLTCLVVSQYINVRIFKFLKRKFINLWWLRSNGSTLIGQFFDTSIFFILAFSFVMPFETILKLIIGDYLIKVSLALLDMPIFYLIAIKFREKIFHRA | Function: Involved in the import of queuosine (Q) precursors, required for Q precursor salvage.
Subcellular Location: Cell membrane
Sequence Length: 181
Sequence Mass (Da): 21091
Location Topology: Multi-pass membrane protein
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B0XAK2 | MYKLSGLLMPVVLLGLISLGSTLNLNDPCTNPNGEAGRCIFFRECQPLVSIYNKPLISPEESTFVRNSQCGTSNGKALVCCAGIQTANRISTLPRPNQCGLDLSDRIFGGQPTALDEFPWTALIHYRKPNGNFGFHCGGSLITSRYVVTAAHCINAIPRGWQVVGVRLGEYDLKNANNDCDSDGCADVPVDMDVEKITVHENYNAQTKSQYDDIALIRFTRDVGFTDYIKPICLPIGDAERLRNNVGVKAIAAGWGRTEIASASDVKLKVQLDITDPKACGQVYRSSGVTLRDTQLCAGGARGKDTCSGDSGGPLMIRVKTNYFLYGIVSFGPNKCGTKDVPGVYTSVVKYIDWIENNIQ | EC: 3.4.21.-
Subcellular Location: Secreted
Sequence Length: 360
Domain: The clip domain consists of 35-55 residues which are 'knitted' together usually by 3 conserved disulfide bonds forming a clip-like compact structure.
Sequence Mass (Da): 39108
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A0A2S2PX78 | MSEGGRNVEFEIQMTVPVTTRHLYKLPPGLSNNRPTGWIVQQEVARMMDSLLDPFSSFASFSKPVRRTNQASKRSHLYRSSSQQTQTPNVVPNISRANNDNRSNNNQQYYKPKSNGPSEKWAASLRKRDSESLPAIHTKRDRCCSHPGGYRTKPVIPPLIHQVPSTARPADQKKQLQKIKTVVGYESHLVDIIEKDILQRNPNVQWDRIAGLKHAKTLLQEAMVLPMLMPDFFKGIRRPWKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTMTSKYRGESEKLVRLLFEMAKIHSPSTIFIDEVDSLCSLRGSEGEHEASRRFKAELLIHMDGLNSTSDEENNTSIMVLAATNHPWDIDDAFRRRFEKRIYLPLPNDDSRITLLKLCLEGVNLDDSFDHRFVANKLRGYTGSDIANVCRDAAMMGMRRKIVGQTPDQIKNIKRADIDLPVTVQDFNEAIERCRKTVTSQDIEKYQSWIDEFGSF | Function: Catalytic subunit of a complex which severs microtubules in an ATP-dependent manner. Microtubule severing may promote rapid reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation.
Catalytic Activity: n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers.
EC: 5.6.1.1
Subcellular Location: Cytoplasm
Sequence Length: 488
Sequence Mass (Da): 55368
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A0A8T6MDG7 | MLETNIKWLKEISDHEVLEVGYKAHILSEISKANIPLPRGFVVNYKNFFNFVQKDNLKEKINEILKTIDYNNKEDIEKKSIEIRTLFLKQKFDEDFISDVLKMYTKLGESKVGFMNTKVDEYTAIRASVSSEEYPLKELDPIERHTGFLNIKGREEVLNSIKECWADLYAPEILEYKYKKGFEENKIHLSIIIQKMIPGKKSGIMLTSKNDSKDTIVIEAIHGFGGKSLITEVTPDHYEINKKTLTTIKKTQSNQEWMLKRIVGKTTKTNVDVKDSEKQKLNQRDLNELANIGNKLEMIYGTSLEVNWVMDENEEFLIVSVNPIDPNLKKIKKKKKIDITSYQEKLDSYKKNLLLEGIGVSNGLSIGIVKIINNKKDLLRVDENTIFVTKMTTLEMSQTLRKAKGIVTDAGSTICHAALIAKKYDVPCVVHTERSTEILRDGQAVLVNGFNGKVYSVIGYVAPPITKTVTETRRENEVSIEKAQNKDPEYPKTITKIFIKINNLEEVKSINLPDIDGIVLSIDSLFTNYEKGSMLENINLLVPTIKNKLLEITKIFEGKEIFYKVNTHKQNLITENVSSYEIEAIMELKSRINILLENIKSADEIIPVKENTESKIGVLVENIKENIISEYISRGIENITFNLEEIDFVKVKEVIKICKENKIMRIAEINSKNTISNIKTYIDSNINGVIINKEQLEYKDTIYKQERDLLKNLLSV | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Function: Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate.
EC: 2.7.9.2
Catalytic Activity: ATP + H2O + pyruvate = AMP + 2 H(+) + phosphate + phosphoenolpyruvate
Sequence Length: 716
Sequence Mass (Da): 82082
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B0XGU6 | MIRLSNLEVLWTCLNFCVLGRSRCGKRQHKSHSIFVFQRLERLVVTTLSGVISYPFDTVRRRMMMQSGRAKADIMYKNTLDCWVKISKQEGSKAFFKGAFSNVLRGTGGALVLVFYDELKALMG | Function: Catalyzes the exchange of ADP and ATP across the membrane.
Subcellular Location: Membrane
Sequence Length: 124
Sequence Mass (Da): 14161
Location Topology: Multi-pass membrane protein
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A0A2E1KWN4 | MSFSYSLEFILEGIGDSVESVEKTGDYAGSIEGFASLSEAREGDLSFFYSNRYKKDLEESHASVIIVPKGLTIEPKPAQLLLAVENPSLSFAMLCREVEFNLMPRPKPGIHPSAVVHPTAVISPHAYIGPLSVIEAEAEVGAATLVSQVTIGRNARVGDDTLIGAQGVVGAYCIIGNGNRLSEGCVIGSDGYGYLQSDGKHERIPQIGIVETASHVDIGANSTVDRARLGRTFIDEGTKVDNLVQIAHNVQIGKHCLLIAQSGIAGSSQIKDHVILAAKSGIAGHLSVGANSIIGPLSGVYNSLEANSNVIGVPAVSKLLYWRVTALSQKLPKLFERFNAIESLINKN | Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
Function: Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
EC: 2.3.1.191
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine = a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + H(+) + holo-[ACP]
Sequence Length: 348
Sequence Mass (Da): 36931
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A0A1I8NAY0 | MKIVSSLILIFGLSFFGRVVVASNFIEVARNSNASDEELSTASEDLAQKYAEEYLRFVETGKESKDLIDLTAQLRETQGKECLFRNLPQQLDEAQEFFTCTTCRIAVHIIVWVLRTAVSNEQAAELAKKAFIYFCSSVQIQTAPVCEGLFNLNWPILYFILMNSNISPKTICGFLPIQFCRFEQPGFNWILNIDNSKWPLLAPKADVPRKTPFDLNILHLTDIHNDPEYMAGSWADCKEPMCCRASSTVAGKESNQSRAGYWGDYRNCDVPLYMVENALEHIRSENGRIDYIYYTGDIMPHNIWSTTRDGNLELISQIYGLLERRFPGIPVYPCVGNHEMHPVNTFGHENVPSEFHPFWLYEHLWSTWQRWLPADTKETIIKGGYYTVSPRPGFRIISLNNIDCYLLNWWIYYDGGNHTSIPQLNWLHDTLLKAEEAGEFVHILMHIPSGDSQCWTVWAREYNRVVERFSHTIGGIFNGHTHHDEFEVHYSSKGYPMAISWNGGSLTAYTMKNPNYRIYEVEPKTYQVVDHSTWIFNLTEANAYGDQRSPQWFREYQFSEFTENLSPAGIDALLDKMATNPEILRQYWKYKTLSSDPLLDMGCNNTCLLNTICNLATSVYNQKERCKELQAKLKTALSSE | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Converts sphingomyelin to ceramide.
EC: 3.1.4.12
Catalytic Activity: a sphingomyelin + H2O = an N-acylsphing-4-enine + H(+) + phosphocholine
Subcellular Location: Secreted
Sequence Length: 640
Sequence Mass (Da): 73751
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A0A485K8G1 | MADSLSKASTVPLKKYKWAYRVGCPAIKLMLLCLLLEIPGSRLRITRRDKTWEWNWSELHMLLAIVAAATLSYYAVQGSDPGYVTEDMVRSIEGGDSLLNEYEFDDEDDLELSKAREIEYRKKKIQAMEATLAKEQELQDESAETTASVNVEAAKTMEFCTTCNLEPPLRAYHCAFCQRCVATFDHHCFCIGTCVGERNHCRFWWFLLLTSIEIYTCLGIVHSGFHTAPTIQVWLKANCMALVGVVFFWCFAFSAYSLFGFHSTFCSWSECLVYANTIVAFLMLTNSTTRELGKGPEKLAYLRGTRECDLPFSNGLCGNLGGFCCVRAGLRHPKDWTPQQWKPVGRIDRNSDRICDNLWENKYYSCC | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 367
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 41828
Location Topology: Multi-pass membrane protein
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A0A914CT03 | MDTIFFERQEGMLCAQHALNMLLQHPYFTAVDLADIARDLDERERAVMSPSVLANFQSHNYDDSGYFSIQVITEAMKNFELRVIPLDNPSYIEYRMNPERGIAYICNLRLHWFTIRKFGNQWFHLNSLRNGPELISGALLKNFFDDIIQQGYSVFLIEGTLPVSLADNVIDKQPVNHSGILGMPTVINPDEEDEALAIALSLSEAEHKRAVEGKTATTDMEIDDAQLQKVLQESLKEVSLLTENDLNKAIQQSLDETPSTSAASTSRRIPRLTSSYSIDERRNAIEPDQAEVIRQQRSRFLDNLEAQSNTHP | Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
EC: 3.4.19.12
Subcellular Location: Nucleus
Sequence Length: 312
Sequence Mass (Da): 35429
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A0A485LQ81 | MSTVPSSGSAAPATGAATNARRNTNQRRKKQQANATPSSTSTPLVPSATVIQASVLRPHARAFAPQATAESGAATTEDKKPRRKTPRASQRGGPTDTTAAASPTTDTPKDGGGGGRSRRGPRKQQKPVVHVATPVSIENDLDDLDEETKAALDLCLVCAEPFRYHAIGECNHAGICSTCSMRMRMLMKDMNCPICKQPNPRVIVTDTVAPYTSFGIWGDTGGPGVVLDDRSEMFFSQCASHYESLVARRDFVCRRCPKSKRIKYRALEDLQLHMENDHATYFCDLCVQHQHFFIAEHPLYSMKELMAHQTAAVAANSRECHPLCEFCHVRYYSDVELHVHLERDHFKCHLCPDNQHRYYRNYKSLETHFRREHFFCEDPACIAKGFVVFSNDLDFQAHLFTAHGTADNRVRVAFTVRRGMEVDESPYASSHDTWEFVEPPPTTTRQEEFPALPITAAPAPLATPPRPITRAPVPTMRPAAAPAPSVPRDVLSRNAQLAAAFGRGPKTEDALEKELRPQYTQELKEWGRAKYRTLCAVEKKIEDMMSDRSCFSTHLKAMPRDQRRMIHELAVFYGLKSEARDTEPNRFISLYKLATSSLPLVSLSKMLMEESQGPKRQARRARVYMERNVQLPVGRGWEKVQEVQAAPAPKDAWSDEEDEAVEDVSAYVKPQGSSTRLEFLRRNESADASDDERA | Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Length: 694
Sequence Mass (Da): 77732
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A0A485LJK4 | MAMFLANESLGTDDAFPSTFELIMQERMAGGFQPAAQYLLTAICDTYPHLAATLPVQNFQETYALVKLAIERYCLAHYDCLLVERFYGIKRMEMRPDKSLAPLSEASRRRSLLWQIGVPYLKSKADAYYQSLLAADAPPTAPAPPSSPTSSSSPPAPPSRLETFWRHWRHLRVWTDMKRFFVDVYPAVHFGYEGTFLLYQWMYLFGYTPHFTPFLRAMKLVFARITPKDITAFDKQRLRHRTNVLKQLPTNSTWNAVRRWLYKATWVTIDYSQTIVVLAIVGFKFMEWLHSDLNPRRNGAGGSGALGGHGIKMPHAAPPPPPVRPLLTHSAISLSTETQRCGLCQRVRTNPASCISGYVFCYPCIHAYVQAHGECPVTRVRCDVSSVSRIYEEA | Pathway: Protein modification; protein ubiquitination.
Function: Component of a retrotranslocation channel required for peroxisome organization by mediating export of the PEX5 receptor from peroxisomes to the cytosol, thereby promoting PEX5 recycling.
Subcellular Location: Membrane
Sequence Length: 394
Sequence Mass (Da): 44709
Location Topology: Multi-pass membrane protein
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A0A2E1KX30 | MPRFFSPAKINLLLAIHQKLDNGYHALSSIVVACDFGDILTIEPLSDQSDRIECTDPSIPCDSNNLIAKMMQCLRNEINLPNNYHFHLEKNIPSGAGFGGGSSNAITALKGVLSLSGQSLEPSTMNRIAAKIGSDCSFFLNPIPSLIQGQGEKIQPLPSQLARSISGLELVLYKPNFSISTAHAYQKLRHTDFCSVPKTEQIIEDFQESLDISKLLYNSFSHQHEEKYMILNLLLSQFRAKGIPSLISGSGSGCFSLLVGENIDNQRTFIKDCIERALGKQAFLKCTRILSDLNHFGNCDLPIDPPNGFQQ | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6.
Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
EC: 2.7.1.148
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+)
Sequence Length: 311
Sequence Mass (Da): 34273
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A0A2I4EPX8 | MAFARLVQWLDLLACALLLLKTEGFNVGITYVQTAVAKGAVCLDGSPPAYHWDKGFGAGMNNWLVHIEGGGWCNNITTCLSRKNTRLGSSKQMAKEIAFSGIMSKYRMFNPDFYNWNRIKVRYCDGASFTGDVEAVNPATNLHFRGARVWLAVIEDLLSKGMRSAKNAILSGCSAGGLTSILHCDSFRALLPIGAKVKCLSDAGYFINTKDVSGAQHIEAFFSEVVATHGSSKNLPSSCTSKLRAGFCFFPQYMAQQIRTPVFLVNAAYDSWQIKNILAPGVSDPHGYWHSCKLNIKNCSPSQITTMQDFRLQFLRALKALGPSSSRGLFIESCYAHCQTETQETWLSSDSPLLSRTTIARAVGNWFYDRSPFQKIDCPYPCNPTCHNRVFDTKEHPDL | Function: Hydrolyzes acetyl esters in homogalacturonan regions of pectin. In type I primary cell wall, galacturonic acid residues of pectin can be acetylated at the O-2 and O-3 positions. Decreasing the degree of acetylation of pectin gels in vitro alters their physical properties.
EC: 3.1.1.-
Subcellular Location: Secreted
Sequence Length: 399
Sequence Mass (Da): 44211
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A0A485KZ34 | MNKEKLHEREAKEVAQLKERIELETPERGTQVEDIESFDLMPLSISTKNGLKRGKFAKPTKIQIGTIPHALVGRDILAAAKTGSGKTLAFLIPMLEKLYRNRWDTEDGVGALIISPTRELAMQIFEVLRSIGKSHSFSAGLVIGGKNFQEEQYRIIKMNILVATPGRLLQHMEQTPNFELSNLLMLILDEADRILDMGFSAQLTAIVGYLPPDRQTMLFSATQTKSVKDLARLSLNEPEYIAVHEKSTTATPSGLVQNYLVCNAGQKLDVLFSFIKSHLKQKTIVFVSTCRQVRFIHDVFCKMQPGVPLSALHGKYKQGKRVDVYYNFLNKPAGVMFATDVAARGLDFPNVDWVIQLDAPEDTANYIHRVGRTARYNKNGRALMLLNDSEVEGLLAGLEESKIPISKIEVNPAKTQSTHGKVASVVAADKDLKALAQKAFMSYVRSIYLQPSKHIFDATKLDTDQLASSYGLPHAPRMPFLKEIATQTRDVNREKKNVNRKLQALKDKIKAEKLLKKLGKTGAAPPPVERRRRRRRLHVVKQRHNWDKDEDVGELESAVEKKKAKQAKKIRVNAANASKVVFDDDGNTIAPFDQLASADAGEFDDVEAHARKFQATVAKRLLEKDEEDRRLEKERVRAKHTKKRQQKKGEREDEDGPVAMLGRASDDEDDDEGSDEGSDDEGSDDEGEDDVEGDDDDDDDDDEEGTLEDREAQALAMMARKKRRLA | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 726
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence Mass (Da): 81463
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A0A1I8N1Z0 | MTAKRIHGPCVVSYVALSLFLVLLFASHLPVHGEFYSSIDSLKRLDSIESSLLLSFRKYSEGLEDYISIIRRFMERIKFQHEKAEKDVEDYLGNPINAFTLIERVVRDWMDVNDLLKFEDISQELMDSLTQLRKNSSLPDENELKGAVLGLARLQDIYDIDADDMANGKGYGHPLTWRECLEIATTLIDENRMDLALKWLKQTDRKLQNSQDAKEIKDYFATQIKEHFARVHHTLGDKQKAQQHLNGISEKDSQHSSKLTMKMLNRLMDEKQKYIPFKESDRHRNYARLCQGKSLNRTQLSCHLDSSSHPFFILNPLQIEPMLMDPYIRVYHNLLSDEQITNLFNFASKKFYRSEVIRGPNENEVTEKRVSQQAWVSPEDTPTAAYMYRMVHLITGFNMTNVEKMQVANYGIGGLYVPHYDYMNVSRTLAGLVGDRISTNMFYLSDVIQGGYTIFPELNVYLKPIKGSMVMWPNLHRSVQPDIRTLHAGCPVVKGTKRIANIWTHSGYQDVARPCGLTNDALK | Function: Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins.
EC: 1.14.11.2
Subcellular Location: Endoplasmic reticulum lumen
Sequence Length: 523
Sequence Mass (Da): 60330
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A0A1I8NDJ9 | MRNKVLQYSVRHFMQRFSKNKPNFGTCNTVEIGNVSEEREVPEHIVKPDYYYKPMPPGFTLGEPEIKNQQQIECMRNSCKLAAQVLKSCTDIIKVGVTTDEIDEFVHNSIITANAYPSPLRYASFPKSTCTSVNNVACHGIPDDRPLHDGDIINVDITVFLNGYHGDCSKTFMVGDVDERGRYLVEKTEECLHECIQLCRPQVEFKAIGNFIAKFCKQTGLNTIPAFIGHGIGSYFHGPPEILHFKNNVPGTMQTGMTFTIEPILTLGGPDIEIQEDGWTAMSVDGARSAQFEHTILVTDDGCEILTKIDEN | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site.
Function: Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val).
EC: 3.4.11.18
Catalytic Activity: Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
Sequence Length: 312
Sequence Mass (Da): 34913
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A0A1C0B8A9 | MSAEIVLASVIFVAIGFILAGVFLLTKFIGPQNKNSAIKNNVYESGITNPVGTANIRFSIKFYLVAISFLLFDVEVIFMFPWAVNVVELGYAGLIKMFIFMGLLFIGLIYIYKKKALSWD | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.-
Subcellular Location: Cell membrane
Sequence Length: 120
Sequence Mass (Da): 13399
Location Topology: Multi-pass membrane protein
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A0A6L9H6G6 | MPLYSIKMRASAQGRHISGAEKIIPDSRIPTCASRLLQRGLTHPKGSPDLLNIKIECLQDKDILYLDALPVSTVDVFDVHEGMQEIRKFLESLGLANAEKIISLLSGAYSMRGAILLDVDTLERLEPDPGRGVRATYMDQEAGQRSGETPGASPKNHYQEAIVLATKVANAPNVIGEICISDDPGYVTGYVASKSAGYKRITRMKEYGSENGGRIFLYRGGREDVGKTISYLEKQPVIVRNVQPLESKEKAAGKFDFIEKELQAMRDTHLYRTMKTIRSAQSRTVECGGRTMLMMASNNYLDMSSRTDVKQHAAQILEVYGAGSGGSRLTTGNTALHEMLEQKIASFKSTESALVFNSGYTANTAAISALMGKGDTIFSDELNHASIIDGCRLSGANVVVYRHNDMKDLERSISEHPCARGLIVSDAVFSMDGDILHLPEFVQIADKNGLLSMVDEAHSTGVLGKTGRGITEHFYYQCRPDILMGTLSKAIGSEGGFVCGSKNLTEYLKNKARGFIFSTSLSPVAMAASYKAFEVIEEHPELVARLQENVRFFCQCLQEGGLFAHSETAVIPILIGDEKKAMEVSQALFEEGYFTSAIRYPTVKKGSARLRIALMATHEREQLKKAAQAILKHFSDTL | Pathway: Cofactor biosynthesis; biotin biosynthesis.
Function: Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide.
EC: 6.2.1.14
Catalytic Activity: 6-carboxyhexanoyl-[ACP] + H(+) + L-alanine = (8S)-8-amino-7-oxononanoate + CO2 + holo-[ACP]
Sequence Length: 638
Sequence Mass (Da): 69996
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A0A2W6C1U5 | MTGLPCACVIGAGSSGIAAAKALHERGIPFDCFERSDRVGGNWVFANRNGMSSAYRSLHINTSRERMEYSDYPMPRSYPDFPHHTQIAAYFDAYVDRFGLRGQIAFETGVQHAARCADGVWTITLETGERRRYDALLVANGHHWDPRWPEPPFPGRFDGAQMHSHEYIENTAFHDKRVLVVGIGNSAMDIAVESSFVAARTMLSSRRGAHILPKYLFGRPIDQIGVNPLITRLPVTVRSAIAATLYRIGVGRMPDYGLPEPDHKLGEAHPTISPDFLNRVAHGEIVWKPSIASLQGDRVRFADGSAEQVDVIIWCTGYKVSFPFFDPNFVSAPRNDLPLFRRVFKPGIDNLFFIALLQPVGATMPLAEAQGRWVAAYLRGEYQLPPVAEMEADMRRERARMLARYVASERHTMQVDFDSYLHDLGSERRAGAVRARAAGSRLPVPAREKIMGPGAELLPPQPSRPELPDLLA | Catalytic Activity: (2E)-geranial + H(+) + NADPH + O2 = (1E)-2,6-dimethylhepta-1,5-dien-1-yl formate + H2O + NADP(+)
EC: 1.14.13.148
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 472
Sequence Mass (Da): 52589
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B0WHB6 | MISSWKPSRLCFAIKVDEGLDGETFFLYVFLAAVVVQLLVLGQRFLGTSIRLGMRRRTTSKTWPSALKRPKLRSPRSSSTRCFTTRTVGGRQGAIVEKAVRNRVEVHFCPCKEHLYELEGEHGIGGLPKYVIYFKRPNDWRVICVPLETASFVCHKWRGKRDNKLEEVSGTEGANFCHQTGFNGGNRTREGCAADCRGQSEGVRDIEKQRQAQAIADGAQETGTTNPKDVDFRQNVPQADPPAAKSEAGHQRRLNRFSRAQLISSSTVWIKPQHQQLATMQIVLDAFESDPNNVSVKIHRKLAPFRCGNPVNSIGILKQISIRIVYEFRFKCNSRYVNETGRCV | Function: TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins. May be involved in the recycling of the translocation apparatus after completion of the translocation process or may function as a membrane-bound chaperone facilitating folding of translocated proteins.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 344
Sequence Mass (Da): 38798
Location Topology: Single-pass type I membrane protein
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B0X4L9 | MNLLCPSMDQLYRLALSLFRWCGFVPFGLDGSSLRVQNQTHHGGNPFTFKWIILVVCICLVDVVMAAIFHDSVFFLEYAVGWINDMFKFGSLALTVFIIEAEVVAQRKTQLQIFEGLEQLGEHRARVGLLNGAKYKQFIRRFLWKFFGYLVFTFAIEMKLITGIMSYNLQWTYTWLTAISLQTINRMRTLFYIFYIDLIRAQCEVIREELLRLGDMMQLTKTLPQISSQSQTITRQVSKTLIFLKGCYTDLWFISFNVNSSLGWSTCFILTCNFVQVSCDFYWVYLTVHDKASDGYTELLMCIIPATTLFITLLYSAESCLKVSNSFGPILHEMPKNDQEILYKIVYRFTNHVFHQPIRFKAHSLFDVNYKLLKMFLTGVVTYMFIFMPFSTDLPDSPK | Function: Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates.
Subcellular Location: Cell membrane
Sequence Length: 399
Sequence Mass (Da): 46484
Location Topology: Multi-pass membrane protein
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A0A336MXH9 | MADKGAHLTQSSSFLINEPSFFDAVASKSLNSYGVVKKIIDNLCHSGRNNWIRKFFTEIYFSCNILIQTYYLSNYGGSFAETFYGLTRKNKKTKGFYKKDFYFSWLCLAILPYIQIKLNNFKDNISMNIDSVDKTQQKKYKNVCIIFGKLNVILEIAKLIQFLCKLIKYFCNIFN | Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Membrane
Sequence Length: 175
Sequence Mass (Da): 20403
Location Topology: Multi-pass membrane protein
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A0A485KQW3 | MPRKKGVIWSFFNDLPDDESSRLKMSRVECKYCKGNVVKSTSRLRSHLRICPNFDGALMPPMDDDEEDDGLPEFKDPKVVKDEGKETFHPLSRYIDHTLLKPDATPNDIAVLCREAYDHGFFSVCVNSVYAAHARQVLDGFEKKPKRTCMHHVKVCCVVGFPSGASPSEVKAFETNHCLAAGAEEIDMVISLGHMKAGDHAYVLRDISAVVLVCKKFNALCKVILETALLTEAEIETASHLAISAGAEFVKTSTGFAARGASVHDVQLMGRIAHPRNVQVKASGGIRSMEDAQHMIQAGATRLGTSAGLTIVHPTADYNMTI | Pathway: Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2.
EC: 4.1.2.4
Catalytic Activity: 2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate
Sequence Length: 322
Sequence Mass (Da): 35241
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T1PFG2 | MALRVLNMALRRQLAAQLPRTSQVGSVASVHTLDKIGKREIVGYGWNGTACYVDRVDYPMPPVRFREPTNEINNLREKEKGDWKKLSVEEKKALYRASFCQTLAELKAPSGEWKLHLGMGLLFASAAIWVAILMNLFVYDELPASFDEEHQKAQLKRMLDLEINPVAGLSSKWDYENKRWKN | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 182
Sequence Mass (Da): 20866
Location Topology: Single-pass membrane protein
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A0A653B9S6 | MSLQFPTIADCIGNTPLVRLQRLAGETSNTLLVKLEGNNPAGSVKDRPALSMINRAELRGDIQPGDTLIEATSGNTGIALAMAAAIKGYKMILIMPDNSTAERKWAMTAYGAELILVSKEEGMEGARDLAEKLQAEGRGKVLDQFANGDNPEAHYSGTGPEIWRQTGGTITHFISSMGTTGTIMGTSRYLKEQNPAIQIVGLQPQEGSAIPGIRRWPQEYLPKIYQAERVDQVMDMGQAEAEHVMRRLAREEGIFCGVSSGGSVAGMLRLSQQVENAVLVAIICDRGDRYLSTGVYEEPTN | Pathway: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-serine: step 2/2.
EC: 2.5.1.47
Catalytic Activity: hydrogen sulfide + O-acetyl-L-serine = acetate + L-cysteine
Sequence Length: 301
Sequence Mass (Da): 32556
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A0A348B338 | MRLFTALRIPGEPLISILREIEQIPGIKPVDKESLHVTLLFLGEVPESVVPLLKEGLSSMKFKSVEVELKGLGVFPSPFSARVVWVGLAGNLDPVRELRLKQEGLLRELRVHYDKKEFSPHVTLGRVKSRPPKELIELIDIYGSTSFGKVKLESFHLMRSILTPKGPIYDSLIEVRGA | Function: Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester.
EC: 3.1.4.58
Catalytic Activity: a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + H2O = a 3'-end 2'-phospho-ribonucleotide-RNA + H(+)
Sequence Length: 178
Sequence Mass (Da): 19976
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B0W5T6 | MLSPGFLRFVNVLIGMNASERKAFLQFTTGCSSLPPGGLANLHPRLTVVRKVDAGEGSYPSVNTCVHYLKLPDYPNEEILRERLLTATKEKGFHLN | Pathway: Protein modification; protein ubiquitination.
Function: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates.
EC: 2.3.2.26
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Length: 96
Sequence Mass (Da): 10644
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A0A6G1G0H6 | MQTLRQYARFPYRAGLAFATGILINEKLASPLAIEGSSMHPALSPDYHATGRKDRVVFTKWGAAHDLKRGDVIAFWTPHDPEKIGVKRVVAVAGDTVVPRSDKYPLREEVVPFNHVWVEGDNERDTKDSNDYGPISKALIHGKASYIVWPFVRFGPVESIHAKSQSKIRETPTAMVVPEEYL | Function: Catalytic component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum (By similarity). Specifically cleaves N-terminal signal peptides that contain a hydrophobic alpha-helix (h-region) shorter than 18-20 amino acids.
Subcellular Location: Membrane
Sequence Length: 182
Sequence Mass (Da): 20396
Location Topology: Single-pass membrane protein
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A0A1I8MQT6 | MKMKYFILIQVVFSISGPWKIEASDPRLPTAIRPDYYELKIITHLENATNLTFHGDVLICFKVLEDTTNVTLHVRDLVVNEASIQVTNFADDEDFCLFAENVETLPELDFYNIHFDGILVKGRRYELYLEFTGNLNRASRGYFYNSYVDVKTNQTRWISFTDFEPIYARSVFPCLDEPDYKAKFKIWLGHHHSLRALSNMPLQTQIPMDSSDGYVWSVFEESLPMSTYLVAFSINDFAYRESKSGDSNVVFRTWCREEYVSQCSYALDIASKILGYFEKLFGVPFPLPKIDIVAVPKYGSSAMENWGLITFKESILRLEPDSLYEWSKIVIISVMSHELVHQWFGNLVTMKWWNDVWIKEGFATYFHSLAMDYIMPGRDMYLENSIFNAKTVFQYDAEINGHPLSNYVRTSDEIVKLFDSITYQKASSAIRMLHLYMGSEAFFGGLQTYLARHQFGNAQADDLWDSLASAALKYKIIKHKHELKIIMDSWTLQAGYPVVTVKRIEYAGAVEISQQRFSRSSGNLSSPGASSCWWVPITYTTANELNFNDTTPKAWMPCNDDSDRGESLVLYNVITENQWVIFNIQVMAIYRVNYDVYNWKLIANFLKNDNFEQIPLINRIQLLSDVIYCARSGHIGYAIALNVMEYLRRERETMPWLISLHAIRPDLNLVAQLSQHHVPTMAYMHYLLQPIYSYLISQNETEISSTKDLQLKDLKTLVIQYACFFGLQDCVHTALSYFQQWKTNNNNPIPDDWILPVYCTTMRYGDENEWNYLWDFFNNTAPHDILILKSLACTQSRKVLTKFLDIAFNKKLQLPMVFAQIAFESVASNPAGTSLALKYLIENASEIQKDFSVPHLLSNVASFAFAPDDLSNLCIFMDAHPELFEKHSKRKRQILDEVNQKRLWAQRNLEEITTFMTNRLLSLDKERIRNDKEEINYYNYS | Cofactor: Binds 1 zinc ion per subunit.
EC: 3.4.11.-
Subcellular Location: Cell membrane
Sequence Length: 941
Sequence Mass (Da): 109347
Location Topology: Lipid-anchor
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A0A2I4ERQ2 | MPEETTSIDYVMEAASGPHFSGLRLDGLLSSPPASSSSSPAQRSSASASGLSPLAADSNFPKQPFVIGVSGGTASGKTTVCDMIIQQLHDHRVVLINQDSFYRGLTPEESERVYEYNFDHPEAFDTEQLLDCIQKLKSGQSYQVPIYDFKIHRRCSDSFRQVNASDVIILEGILIFHDQHVRNMMNMKIFVDTDADVRLARRIRRDTVERGRDINSVLEQYAKFVKPAFDDFVLPSKKYADVIIPRGGDNHVAIDLIVQHIQTKLGQHNLCKIYPNVYVIQSTFQIRGMHTLIRDTDISKHDFVFYSDRLIRLVVEHGLGHLPFTEKQVVTPTGSVYTGVDFCKKLCGVSIIRSGESMENAMRACCKGIKIGKILIHRDGDNGKQLIYEKLPKDISERHVLLLDPVLATGNSANQAIELLIQKGVPESHIIFLNLISAPEGIHCVCKRFPSLKIVTSEIDVELNEEFRVIPGLGEFGDRYFGTDD | Pathway: Pyrimidine metabolism; CTP biosynthesis via salvage pathway; CTP from cytidine: step 1/3.
EC: 2.7.1.48
Catalytic Activity: ATP + cytidine = ADP + CMP + H(+)
Sequence Length: 485
Sequence Mass (Da): 54279
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A0A485KTH4 | MDPKVLVPSLSYDKHKGQYGKVGIVGGCVEYTGAPYYAGISALKTGADLCHVFCAPDAAIPIKCYSPELIVHPFLSPFLVTNVTSVLGRLDALVVGPGLGRDPDILDAAKTIIGAAKARQLPLVLDGDALFLVSTDLSLVHGYEQAILTPNIMEYTRLCVSLGLLDTLDLTQAATLPPQLVAAKLGHVTVLQKGHVDVVSDGVATTEQASQGCPRRCGGQGDVRAGRQHWNIPRMACRATLVRLIAIHDRDSRSTPRKPPATVAAPVSALCLAALGGSLLTRESARLAFATHGRATTTPDLIASIPTAFGTLFDS | Function: Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ATP, which is converted to ADP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration.
EC: 4.2.1.93
Catalytic Activity: (6S)-NADHX + ATP = ADP + H(+) + NADH + phosphate
Sequence Length: 315
Sequence Mass (Da): 33119
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A0A8T5L4L7 | MSIKETIKHYIRVMRIARKPSKEEFVNTGKVCALGIGIIGVIGFAIFIAFVLLLPWL | Function: Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
Subcellular Location: Cell membrane
Sequence Length: 57
Sequence Mass (Da): 6403
Location Topology: Single-pass membrane protein
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A0A2S2JKI7 | MKLQLAIDLEDIDGAINLIEKTKDSVDVFEYGTPLVINFGLEGLKKIRDRFPDITLLADAKIMDVASYEVGQAFKYGADITTILGVAEDQSIKDAIKTTHEMGKELLVDMIGVQDIAKRAQELDKMGADYISTHTGYDLQALGKTPFEDLHTIKENVKDTKTAVAGGIKVDTAEKIINEQPDLLIVGGGISTVDDPAKAAKEIKAMMK | Pathway: One-carbon metabolism; formaldehyde assimilation via RuMP pathway; D-fructose 6-phosphate from D-ribulose 5-phosphate and formaldehyde: step 1/2.
EC: 4.1.2.43
Catalytic Activity: D-ribulose 5-phosphate + formaldehyde = D-arabino-hex-3-ulose 6-phosphate
Sequence Length: 208
Sequence Mass (Da): 22640
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B0X6M1 | MPIDIFEHLEKYDEGIRSVRNFYQPGQTGWFLQVVVLVVPASGSSVIGKVLNGGGPEASKRHTSKGCFGIVTGVGLGATVDCVIVANDATVKGGSYHPITVKKHLRAHEMAQANNPPCIYLVDSGGLNLPRPDTIQTVPSSAVPRALPGWRPSVEPVLCCLFPRELRDPLPSRMAIPDCLNLLE | Pathway: Amino-acid degradation; L-leucine degradation; (S)-3-hydroxy-3-methylglutaryl-CoA from 3-isovaleryl-CoA: step 2/3.
EC: 6.4.1.4
Catalytic Activity: 3-methyl-(2E)-butenoyl-CoA + ATP + hydrogencarbonate = 3-methyl-(2E)-glutaconyl-CoA + ADP + H(+) + phosphate
Sequence Length: 184
Sequence Mass (Da): 19778
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A0A6G1G2V8 | MAEQATRGSSTINYKDGGMRDNKEYQTRLRQTLEAGEVELLSPEMLISSRDAEHPANLIPSLCEAFYKLGWVTGTGGGISIRKGALAYFAPSGVQKERIKPEDLFVLDLRLGTYLRYPLPLKPSQCTPLFHLSFMKRGAGACIHTHSQWAVLVTLLVEQELQQRTAKGGFATWDDRSMGGITDLTGAERSLSKKRWDATPGRDAVLHRPFRISRLEQIKGIPAGQKHTDGYIDDVDLSKIEPSRPGYLSYYDTLAIPIIENTAHEEDLSASLAAAIEMYPHSSAVLVKRHGVYVWGETWVKAKTVCESLDYIFQLAIEMRKLNAPWTED | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 2/6.
Function: Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P).
EC: 4.2.1.109
Subcellular Location: Cytoplasm
Catalytic Activity: S-methyl-5-thio-D-ribulose 1-phosphate = 5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O
Sequence Length: 329
Sequence Mass (Da): 36770
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A0A183DW40 | MNVQMNEMKRICVVVFLVARWFLAITGVSVSRYTQQIRQVTIQTDGYAPVVDDDYVAVSMAIQPGYIVRFEPFADADRIHHILLFGCDYPAKAMPLWRGLETCRGPSHILYAWARNAPDLRLPEGVAFSVHYAHPFLGRVLDYSGVTVHLIDERPNNLAAVLLNTGADEMCNFYMMFYWDATAPDPFPYGAVCGMQEEQAVVNKEYPIDGVTLLPPHPDWEHKAHQSGKPFGKVYVVLKYFYLFYVVCRIQGAREFLLRVAWTMILA | Cofactor: Binds 2 Cu(2+) ions per subunit.
EC: 1.14.17.3
Catalytic Activity: a [peptide]-C-terminal glycine + 2 L-ascorbate + O2 = a [peptide]-C-terminal (2S)-2-hydroxyglycine + H2O + 2 monodehydro-L-ascorbate radical
Sequence Length: 267
Sequence Mass (Da): 30446
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A0A815WP73 | MVILKVQRTNEPGLENAVVINSNVQELRPYSEIQITKSNGTQHRFRLIMNSYVTNGYILINEKESKLRRLHLNHKYRVEGVKSSVIDKKAQIDYKKLNLAGCTSAIEEIVRRVFRPRKFPSDMCREMKIQYIRGVILHGPPGTGKTSTILALCEYFGLEPKVINGPELIKSVFGKSEQAVRELFEEAIFDQENKGDSSPLHVIVFDEMDALFRKRTSDSGACETRNGIVTQLLTMLDGEKKLNNIIVFGTTNRFDMLEPALLRHGRFDLQIKIDLPNARERLEIMNYHLRGVRKSGNLSSNVLTSHLEELANITNNYSAADIAGIVQEAISEAFARAYDNIITDLGKLKREECNICVEWNDLVTAFHKSEKMRQIGQAQFQTKEIESIIDYNQ | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Required for vesicle-mediated transport. Catalyzes the fusion of transport vesicles within the Golgi cisternae. Is also required for transport from the endoplasmic reticulum to the Golgi stack. Seems to function as a fusion protein required for the delivery of cargo proteins to all compartments of the Golgi stack independent of vesicle origin.
EC: 3.6.4.6
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Subcellular Location: Cytoplasm
Sequence Length: 393
Sequence Mass (Da): 44806
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A8QX31 | MFTTPAKTLFTATLILGTLIATTSTSWLGVWMGLEINLLSFIPLMTDTKNLMSTEASLKYFLVQALASAALLFSIILMFAFSNNPFYMNTEIFSTLMSSALLLKMGAAP | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
EC: 7.1.1.2
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Sequence Length: 109
Sequence Mass (Da): 11901
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A0A815AZL7 | MFVPFTNLPRSATVQPTPFKVSIPQSNLDELKTLIQLSKVAPLTYEGSQEDRKYGVTNKWIRETKEKWEKDFDWRKHEAHINSFPNYIAPVVDDDSKEYKIHFVALFSDKSDAVPLVLLHGWPGSFIEFLPMLTLLSDGHTPSTLPYHLIVPSLPGYAFSSSPPLDKDFRIEDIARIINRLVIGLGFEQGYVVQGGDIGSKVARVMAAEHASCKAIHINFCIMPEPSGVDNTTLNELDREGLIRAAEFMSTGSAYALEHATRTSTIGHVLASNPIALLAWIGEKFLEWTDEKPPLDTILESVTLYWITETLPRALYPYRQLFTPGNIGAHENPKWYIKKPFGFSWFPKEIAPIPQSWAATTGNLVFFRQHTKGGHFAALERPDVLAKDIKDFIEQVWSQAKKA | Catalytic Activity: 1-(4-methoxyphenyl)-N-methyl-N-[(3-methyloxetan-3-yl)methyl]methanamine + H2O = 2-{[(4-methoxybenzyl)(methyl)amino]methyl}-2-methylpropane-1,3-diol
EC: 3.3.2.9
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 403
Sequence Mass (Da): 45451
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I1XMS8 | MSAHLTDTAFSSLPLHPLLQKGLQQAGFEFCTPIQAQSLPLLLANHDVAGQAQTGTGKTIAFLLATFQRLLANQDAQKSTSKQPRALILAPTRELAIQIVKDAELLNSHAGLRIVIAHGGKDYQRQRDAIDDGCDVLIGTPGRLLDFHKQRVFNLNKIEAVVLDEADRMFDLGFIKDVRFFLRRLPSPEKRLGMLFSATLSYKVTELAYEHMNNPEKVQVEPEKMMGDRIEEWVYYPSNEEKIPLLLALIKRIQPVRSIVFVNTKQVAERVWGYLEGNGYKAALLSGDVPQKKRESLLKHFQDGEFPYLVATDVAARGLHIPEVSHVFNFDLPQDAEDYVHRTGRTARAGASGIAISLACEEYAFSLPDIEHYIKHKLPVAQSTDEQLETPQPRIKAERNPAPRHKNKARGDKSHNNRPRDGKRNNGHNKPVTSDANQ | Function: DEAD-box RNA helicase involved in RNA degradation. Has RNA-dependent ATPase activity and unwinds double-stranded RNA.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
EC: 3.6.4.13
Subcellular Location: Cytoplasm
Sequence Length: 438
Sequence Mass (Da): 49165
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A0A183EEG4 | MESLLVPIIFNRSIYDVSLPPGSFIAADDFESPRQLAKYLNYLERNNTVYLRNRYSCSYLEWTKHYQRSTAETSMCDLCRYVHSCRENGTSKTVSDISAWWYRDKQCISDYAMKFLENQRTTKKLPVMEVE | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 131
Sequence Mass (Da): 15522
Location Topology: Single-pass type II membrane protein
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A0A183DH72 | MEDCEVIEPADVIIVEGILIFYDQELRNLFDMKLFVDADSDDRLARRVQRDTRERGRSLSQVLHQYLNLVKPAFEEFCLPTKKYADVVIPRGVDNEVAIDLILHHIHEILRSPSPSSHSSLDGSVASAPDRTPSLTRPH | Pathway: Pyrimidine metabolism; UMP biosynthesis via salvage pathway; UMP from uridine: step 1/1.
EC: 2.7.1.48
Catalytic Activity: ATP + cytidine = ADP + CMP + H(+)
Sequence Length: 139
Sequence Mass (Da): 15818
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A0A834D6W9 | MASTPQKTTASASSFLADDISSSSSSSSIFQDATASASVSASAANAEQDCSVASTDRSNDQLGKKVAMASVIDAVDSLPEPSANTSSKGIPTMLRAQTRHPLDPLSATEISVAVATVRAAGATPEVRDSMRFIEVVLFEPDKHVVALADAYFFPPFQPSLVPKTKGGPVVPSKLPPRRARLIVYNRKSNETSVWVVELSEVHAVTRSGHHRGKVISSRFVPNVQPPMDAVEYAECEAAVKDFPPFREAMKRRGIEDMDLVMVDIWCVGYHGEADAPCRRLSKPLIFCRTESDCPMENGYARPVEGVYVLLICKKWW | PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.
Cofactor: Contains 1 topaquinone per subunit.
EC: 1.4.3.-
Sequence Length: 316
Sequence Mass (Da): 34302
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A0A7S6NMY9 | TLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLTSGMIETGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRAMGITLDRMPLFTWSVVITAVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 219
Sequence Mass (Da): 23476
Location Topology: Multi-pass membrane protein
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A0A183D1E4 | MLRRTMARYLCLTQVLVLRDISIRVRQRFPTYESVIKAGSPLAHLLQLSLSYMTKEEYDKFKDYQLQEDYNSGRYWAPLNWAFSLVMQARKDGKIKTDIWTAKLFDELRKFQNSMQLVCNYDWVQIPLAYPQVTVGMLFYCGFLICVHWLSPFVSPFEPLPAVPVFYGE | Function: Forms chloride channels.
Subcellular Location: Cell membrane
Sequence Length: 169
Sequence Mass (Da): 19956
Location Topology: Multi-pass membrane protein
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A0A7D5QP78 | MTVNTIGSIAEFDTNGVTTNYPFYFKFLANEDLVVTYVNPLGVSSILNLGTHYTANGAGNDQGGSIVTTSALAGPGQLVVARDMEAYQQTSLRNQGKFLAETHEDVFDKLTMLVQQAFATLGRALTRPFGRDYFFAENRRITSVRDPVEPQDATTKHSVEMYVGGLIQAGQGPINSAANVLYVAPNGLTRKVQDLSSKTDANLGAQLIGFKGRTVGDRLNDFVSSLDYATGDGVTDDTTAFIVAMAFADTRGVPLYVVPTPNGYVLGPVDVPCSLIGERSKIIRKAGTTGTWLNVVDNGVKIKGLDPDGGWFAERFIEVDGHSDVEITDNRPTRIGEYFVHFNGADRLRVERNTYKAGTNGISNVMPSGSLTAAISRDVKIRENNISDLDGSGIQLAGKQLVGDSNYFKTNELAVVADISGNILKNITGHGIIAQGRSIKVHGNETDNCGSGPGLQSIVAQATNVSVNGNIVSGGKGVGIDMGWCTNASANGNTLIGCGEVGIELQSCTNLTCTGNNIKDCGRLNPGSGSAGITIAQGYFGPSIINYAVTVTGNTVTNSGIAGKYGISVQANVKNLIISSNHLASSGTLGPMFVDPTAKALSFGNITSNNEEDLFITYGNTPKLVSRNATGNGDLWLAPEGSGKLRLDKNFGTAATPGNFSAQSIIEIKDLSGNTFYMPARTSPW | Pathway: Glycan biosynthesis; alginate biosynthesis.
EC: 5.1.3.37
Catalytic Activity: [(1->4)-beta-D-mannuronosyl](n) = [alginate](n)
Sequence Length: 685
Sequence Mass (Da): 72297
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A0A1B2WSH5 | TLYFMFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALTLLLASSVVENGAGTGWTVYPPLSSVIAHSGASVDLAIFSLHLAGISSILGAVNFITTVINMRSSGITFDRMPLFVWSVMITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 219
Sequence Mass (Da): 23578
Location Topology: Multi-pass membrane protein
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Q9VBY7 | MADNAEPLTLSRDVKRSIELLEKLQASGDFPTTKLAALQKVLNSDFMTSVREVYEHVYETVDIQGSHDVRASATAKATVAAFAASEGHAHPRVVELPKTEEGLGFNVMGGKEQNSPIYISRIIPGGVADRHGGLKRGDQLLSVNGVSVEGENHEKAVELLKQAVGSVKLVVRYTPKVLEEMEMRFDKQRNTRRRQ | Function: Plays a role in establishing and maintaining the asymmetric distribution of channels and receptors at the plasma membrane of polarized cells.
Subcellular Location: Cell junction
Sequence Length: 195
Sequence Mass (Da): 21493
Location Topology: Peripheral membrane protein
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A0A817C9H3 | MINCLCQFYFLSTILSFPFHTFGTEWLSIMLRKIHTTANNESKWFPRVVMCDFMVRHLGSNHHWMAVQCNLPINLFNELMFLIIWAWFMLLSSLTCISLILCFILIYTNIGCTFIYKYLHINLFKSKKEQQDGFIEKYLKYDGILVLRIIAHNTNDIIMAKLVGALFKIYLNSIEKENNDDDNDDERCSNGHYERVDTSSI | Function: Structural component of the gap junctions.
Subcellular Location: Cell membrane
Sequence Length: 201
Sequence Mass (Da): 23705
Location Topology: Multi-pass membrane protein
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A0A5A7TFQ5 | MSPLWVKLKREPTNVPAPCICINLGDTGPQSQVIPAAFKNFSKSHKEKTIAELAQDKWLDCTPEGFVNLGVRSFLDLRSWFRSNDVPSCEVCNEAGVKAELCSSEVCTVRVHRYCLKKMLSNKKSKRACPGCGTRWQSTMSNIESKEEVDEPDTRTQDQPSSHKRKKSKLNVDIDLGPNEDSTAEASQPPPDTRRATRNSTRQR | Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
EC: 2.3.2.27
Subcellular Location: Nucleus
Sequence Length: 204
Sequence Mass (Da): 22894
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A0A183DVZ3 | MYVIVIAVNGITECFAMATMNQQQVFYHGWFLFCICPVHILLCSALSYFIGVYGLIFANIINMLTRITYSWRHIQRFLSGKISFAEALPNSSTVVVLLFCLAVTSLSLLIFGGVGGIMHSAAHAAVGGSLFVFTVSHIYQNDVHVARCVGKLKRLALLNDDDPELKANSAQQDGRPCSTRIRRRLATAHTSSRSFSAVIWRTEWS | Function: May be involved in N-linked oligosaccharide assembly.
Subcellular Location: Membrane
Sequence Length: 205
Sequence Mass (Da): 22751
Location Topology: Multi-pass membrane protein
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A0A817SCE4 | MIDSIDPALYRPGRLDTLIEVGEPDAKGRSDIFNIYTKTLLQNSLLSDDINIERLVQRTHGMTGAHIEQLVRRATHSDSKRDLQSRRTLHITDEETEELQIKNIDFTVALA | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Required for vesicle-mediated transport. Catalyzes the fusion of transport vesicles within the Golgi cisternae. Is also required for transport from the endoplasmic reticulum to the Golgi stack. Seems to function as a fusion protein required for the delivery of cargo proteins to all compartments of the Golgi stack independent of vesicle origin.
EC: 3.6.4.6
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Subcellular Location: Cytoplasm
Sequence Length: 111
Sequence Mass (Da): 12656
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A0A1I7W0Q6 | MECSINRQATSSSNESDSESGEDVVEKLPFNLAMFDFKQCDPKRCTGKKLERYGFVKVLKLGTKFPGLLLSPNGERTISAADLAYIKNGGLAVVDCSWNQVANVDLNRARASHHRLLPYLVAANPVNFGKPCQLSCVEAFAAGLYMIGLKSNAQLLLSKFKWGPNFLKMNEDLLDAYAACENGAEVIARQNAHLRTLAKEASEMKQRPVDMPKSDSETDNDDNGENGDNGELN | Function: Aminocarboxypropyltransferase that catalyzes the aminocarboxypropyl transfer on pseudouridine in 18S rRNA. It constitutes the last step in biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi).
EC: 2.5.1.-
Catalytic Activity: an N(1)-methylpseudouridine in 16S/18S rRNA + S-adenosyl-L-methionine = H(+) + N(1)-methyl-N(3)[(3S)-3-amino-3-carboxypropyl]pseudouridine in 16S/18S rRNA + S-methyl-5'-thioadenosine
Sequence Length: 233
Sequence Mass (Da): 25566
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A0A657BES1 | MIKAILEGHKVLVCRPEPSASELCKVLESVGAETYSLPCIEVRTLALTPQVKNIIYALDQYEKVVVVSQHAATQLIHYVDELWPQAPADQKWFGIGRKTTQLLAEADLSVSIPDQDYSSEGLLDTPELNHVKGQKILIAKGKEGRSKLEQGLRDRGAKVTTIELYERVTPEYSDQTLQESISDFGATSIVTLSAETLDNLHSLAKSISATPTGTRLIVPSERVAKHAQSLGYQKTQVSEQLRPIDIIKALARPA | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 3/4.
Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
EC: 4.2.1.75
Catalytic Activity: hydroxymethylbilane = H2O + uroporphyrinogen III
Sequence Length: 254
Sequence Mass (Da): 27925
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A0A336MLV6 | MTQILTNAYDWYRDLMDNRSDPRVKDWPMMSSPFPTLALCLFYAYFSKTLAPKLMANRKPFDLRNILIVYNLFQTVFSIWIFYEYLQSGWWGHYSFKCQPVDYSNDPMALRVQFVAIFTHQFQLLFRECDYPKGFMVWIGLHGVMFLFLFSDFYKQAYQKRAAAAQKKFDDYQNGKIHANGHTNGKVNGTNEGACMPVLEDEPIVKNGNGIYMNGKYTNGLNGHVNGVCENNNGIPNGNGLKSRKD | Catalytic Activity: a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA
EC: 2.3.1.199
Subcellular Location: Membrane
Sequence Length: 246
Sequence Mass (Da): 28467
Location Topology: Multi-pass membrane protein
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A0A817MTT3 | MAGATGRQFFVGGNWKMNYSKAILKKVNNTLNNKKGANVDIVCTPSSLFIKDFISSKPTHVQVSAQNCYHAKEGIFTGEISPKM | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
EC: 5.3.1.1
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
Sequence Length: 84
Sequence Mass (Da): 9210
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A0A336KIJ5 | MNLKAPALLILIISICVYTVESANRQYQYRESDDEIDDLQREFYDEHLKFMKYGNHSTRLMELYNELKAPSDFMRLNLEEMSQKKIDFGCWGCRIAAPTLFIYRRINKMSDEEIEKAGIDICVNAKISTPHVCEGLIKMNLEPILFVIDNQPKLTGNIFCAFALHGSCGEIKEPEFLYSIKVDPNYPLMDDGFSAISNRNVNQETFKIIHITDVHFDPRYVVGNNAKCDDPTCCRESHGKPNNTANAAGKWGSYDCDVPWESVVDLVQHLKAEHGDAEIIYYTGDTVDHGIWETSFEFNINAMKKFEDYMAEEFNGMKFYPILGNHEAHPVDVFAPEEISKESLSMNYLYGYISKAWRRWLPQSTELTLNRGGYYTTLVRPGFRVVGLNNNVCYNINWWVMYHPQEHTVQLNWLHDVLLQAEKANERVHILLHQPPGGESCYYVWAREYQKLIDRFHHIITGQFNGHTHREEFNVFYKSNDLSRPINVAWNGGSQVTFTNVNPNYRVYHVDKETLEIVDAETYYYNLTEANSGDANPRWQKMYSFKQEYGMEDLSPSSLDRLVTRFANDKDLLTKYWQFRYKLADPMLEKNCDKECLLENLCTIVTNQVFDNRKCDEIKKIFNENH | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Converts sphingomyelin to ceramide.
EC: 3.1.4.12
Catalytic Activity: a sphingomyelin + H2O = an N-acylsphing-4-enine + H(+) + phosphocholine
Subcellular Location: Secreted
Sequence Length: 626
Sequence Mass (Da): 73048
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A0A336KSV3 | MILQQINSIISRVKQKNEKSRSYVCINCGCPVKELIKKYSPTVLKINHCDNCNEIADKYIEFETIIILIDLVLLSKAAYRHVVFNTESKNLWKLAVIIILLESYCLWVETFKVDRSSPQSIHDPFLSEKSFYLSCAQIILGNVLLYIFMVILSAPSRGLLYINHGNHPLYRSKLAFALNLLRGLTLASIGKFFFLPIMIWKENSTETQIAVHLSLVIIYFILSLIHAHSVVANCSRLASIFIVIFSYVSETYIITELSLYAKGHLF | Function: Mediator of sterol homeostasis involved in sterol uptake, trafficking and distribution into membranes.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 266
Sequence Mass (Da): 30414
Location Topology: Multi-pass membrane protein
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A0A183ED94 | MNLIVAVDDSGGIGKNGALPWRLPREMARFAKLTSTTNDRSKRNAVLMGRKVWEEIPAKFRPLKDRLNVLYITRVEGDFSADVFFPSVDYSRFTKNDEPEEVQEEHGIKYRYEIYTNKSGL | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
EC: 1.5.1.3
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH
Sequence Length: 121
Sequence Mass (Da): 13973
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A0A813NLC5 | MPQDLSEMTRKLMNNPVHILLEPNDRTLEGIRQFYINIEREHVNMDAKQYSNAMNEFRIGSSRILIRTDALLNNTDVPQVALVINYELPIHREHYIRRIGRYGAFGRKGTAITFITQNEQQTLRNIEKFYYTSIQEMPLDIADLI | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 145
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence Mass (Da): 17054
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A0A183DN62 | MPQELCTKCENFKEEVRIALIGKYVQIKDAYASVNKALRHAAVQAKRNLVIEYVQSEHLEETQDPLRLPDYNRAWQAVKKADGILVPGGFGGRGTEGKIAACKYARENKIPFLGICLGMQCAAIEFARNVCHIERANSTEFDKALVGKQQVVIDMPEHRGEDKGMGGTMRLGLRDTIFLTKGSVLYQLYGAKKKISERHRHRYEVNPEIVPTLMHNGLMFVGSLGIDHEGAVKTDEKEGSCSPTVSASFPEIDVSSPKIYGIQDSLFYDITNLANAITSHLSKRFDKLSRYYLKFLELQSDLCLEIEQLCKRHPYFVGVQFHPEYLSHPLQPSPPFFGLIAAASGQLENFLRGWKMPTSMNVLKPAEDNITDNTSVVQATHTTVNKGCEMLDENIAEFEQKLDI | Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2.
EC: 6.3.4.2
Catalytic Activity: ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L-glutamate + phosphate
Sequence Length: 404
Sequence Mass (Da): 45343
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A0A3G8EXF4 | MHTRKAITEALQKLGVQTGDLLMVHASLKAIGPVEGGAETVVAALRSAVGPTGTVMGYASWDRSPYEETLNGARLDDEARRTWLPFDPATAGTYRGFGLLNQFLVQAPARGAARTPMHRWSRLVRWLKR | Function: Resistance to antibiotics containing the 2-deoxy-streptamine ring including gentamicin, kanamycin, tobramycin, neomycin and apramycin.
EC: 2.3.1.81
Catalytic Activity: a 2-deoxystreptamine antibiotic + acetyl-CoA = an N(3')-acetyl-2-deoxystreptamine antibiotic + CoA + H(+)
Sequence Length: 129
Sequence Mass (Da): 14144
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A0A3S5XFJ8 | RMNNMSFWLLPPSISLLILSSLVESGTGTGWTVYPPLSSIIAHSGTSVDLSIFSLHIAGISSILGAINFISTMLNMKIKFLNFNQISLFIWSITITTILLLLSLPVLAGAITMLLTDRNLNSSFFDPMGGGDPVLYQHLFWFFGHP | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 146
Sequence Mass (Da): 16019
Location Topology: Multi-pass membrane protein
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A0A183D803 | MQYNRVVAVKQEATFSYAFYPSDQFAGRPLGLVVELHYEDNDGKAFVHSVFNETVTIIEDESNFNTETGFLYVIFAAVVVLILLAGQHFLSKLTRKHGMAKSRQAQPIEMGTGNKNEVDFEWIPREILNHSKSPKGVPRQRKQAQRT | Function: TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins. May be involved in the recycling of the translocation apparatus after completion of the translocation process or may function as a membrane-bound chaperone facilitating folding of translocated proteins.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 147
Sequence Mass (Da): 16731
Location Topology: Single-pass type I membrane protein
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A0A817JFH7 | MSILYKILLCLTLCKLCVSGYPPSYCVRFDTDVNGSKNPIIINITQNWSPIGANHLFDIINSDFYSVPSAFFRVVPNFVVQFGISGDPIQNTIWNEPIQDGFIITFIYLFIYLFYICLDPVKMSNSKGTLSYATAGPNTRTTQLFINYVNNPRLDSLGFSPLGIVTTGFDTALAIFNPTPGSTDGVDQDQYAEKGNKWIIDNYPQINFIEKVSITYNCPFTN | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
EC: 5.2.1.8
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Length: 222
Sequence Mass (Da): 24899
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A0A183CWJ8 | MTISYNLDVASASSLNFFRLVFRWKGSIWKLCLKELCIWTVLFLIITFIYRTPYFLSNDQKVAFENLMNYFNSHLTYIPLTFMLGFFVQIVVRRWSVLFQNMGYVESTSMYIGGYVYGEDDESRLWRRTMARYLCLTQLLVYRDISVRVRKRFPTYDSIIKAGFMLENEREMLDSIHLNFDKYWVPINWIYALIFRARNSGKIVSDSFTNKLCDEIKNFRYNIQMLCNYDWVPIPLAYPQVTLTNFIINTAFYASLLFQSIFTLKSATL | Function: Forms chloride channels.
Subcellular Location: Cell membrane
Sequence Length: 269
Sequence Mass (Da): 32056
Location Topology: Multi-pass membrane protein
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A0A7C2J1D4 | MKEKTWIEVNVEINPSLLDVLSNGIFSLGAEGLEEADNQVKIYFQKNRWDASTLKSLTDMIHKYHPEFDASTIQIKDIPYQDWTENWKDSFKRFHLTENIIVKPDWDDYHPKKDEIVITISPKMAFGTGHHETTQLVMLMLQKYIKNGDHVLDAGAGSGILAVLAAKLGARRITAFDNDPIVLENIRENFSLNEINIQTDIICGTLGDIKKSEYDVITANIDRNVLLELPEKFINYIKPDGILILSGLLSRDEDKILTGYEEYNWQVIEKEQKGAWLALALKHK | Function: Methylates ribosomal protein L11.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 284
Sequence Mass (Da): 32500
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A0A183CW45 | MIVFGFVLLRNCSLFPHCSGFLPSLQYIVLYRGAYYGLFDSAKARFKSDASNDISFTCAFLIGQVVTFTAALISYPLDTVRRRLMMQAGRHDTLYRGVWHCTTKIWHEEGFRAYFSGMWVNTIRGTGAALILAFYNEFSKYV | Function: Catalyzes the exchange of ADP and ATP across the membrane.
Subcellular Location: Membrane
Sequence Length: 142
Sequence Mass (Da): 16257
Location Topology: Multi-pass membrane protein
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A0A085N9H9 | MIGYLNSVKLFFLVGLAATSVAIQLLFNKAVPFPFIDEKFHFDQLHNYCDGNFTYWNAKITTPPGLYVLSLAYVRGLSLLFGSDSCSLPTVRFFNVIATLLLFNVSYAVTKDVSLTRFRRALNALNCTIFPIFYFSTFLYYTDCCSLLLLSCCYVMAKAKQPMYSALFALLSVCVRQSNVVWVVFTAAIYFLESFEGYVKQQRFSYYDGKWSNLLISKLFWHDVILPELNYALVVLLFLSFAYMNGGFALGDRQAHQVCLHISQLFYCVAVILLLGWPVLLSRSRVLSFAKSLYANKALYALVILLMTVCIRSFTFVHPYLLADNRHLTFYIWRRWFAVHYLCRFLFIPVYIFAFYCITCKLRRYGAMWKSVFWICLAACCIPNRLLEMRYFIVPFYTWRIHCPTPRTNKLVLEFFFHALINAALLLIFLLKTFRWADELEPQRIIL | Catalytic Activity: a dolichyl beta-D-glucosyl phosphate + alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol = a dolichyl phosphate + alpha-D-Glc-(1->2)-alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + H(+)
EC: 2.4.1.256
Subcellular Location: Membrane
Sequence Length: 447
Sequence Mass (Da): 52137
Location Topology: Multi-pass membrane protein
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A0A817LDC8 | MLYSHAKDISDKELFELISERRTMSRMLSDYGEQKSTSISTAKRLAEFLGEDIIKDKGLYCRFVIANVPRDASITEHTILLDIFQ | Function: DNA polymerase II participates in chromosomal DNA replication.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
EC: 2.7.7.7
Subcellular Location: Nucleus
Sequence Length: 85
Sequence Mass (Da): 9801
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A0A8H7MZE0 | MAGVSQLENPWGHAPANPTVIRSNVTLLGTVFAAAFGMQLAFDTGSERIWDNINRGRQWKDIKQRYIEAAEDDE | Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Subcellular Location: Membrane
Sequence Length: 74
Sequence Mass (Da): 8276
Location Topology: Single-pass membrane protein
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A0A817IPD3 | MLYAYGRHHPILTSSSSHDQDQESSRSNHRLYRYNHEPVSSNLLSRDISSILILLFFLFLLVISLSQILVVHTSRYGANFSAMQKIQDELKQMDESMEALLRDNVLPIDKWRLLFQIQTYLYRFELLFDSFNNDSDLIINNQVNKNFDQIKTNITIKQLLKPLLNKSDELLLQENNSDHLMNNLKRVQNRLAALVDEDENLHWKYRETKNNYTNNNDNKRKRNYCQEEPRYLYGRYLDENSTFPNVSLYEIETNYTNVRSGGQWSPSHCIARHRVAIIIPYRDRYEHLVTLLYYLHPILQRQELDYKIYVSEQTGNGTYNKAVLMNAAFIYASSEYDFQCFVFHDVDLIPEDDRNMYSCPVFPRHMSVAVDEMNYKLTYEELIGGVFNIRPDHFLTVNGYSNLYWGWGAEDDDLYYRLKELSIKVIRPPATIARYKMLPHTKRVPSIWNKRAKLLYSAAKRYTWDGVSSARYNLTSAIAYPLFTHLLIDVGLPPPGFS | Pathway: Protein modification; protein glycosylation.
Function: Catalyses the transfer of galactose onto proteins or lipids.
EC: 2.4.1.-
Subcellular Location: Membrane
Sequence Length: 498
Sequence Mass (Da): 58684
Location Topology: Single-pass type II membrane protein
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A0A183DLS2 | MLPSFVRAVPNGTERGNFLALDLGGTNFRVLLIKLKETTAEMTGKVYRVPDNIMKGSGVVVNL | Pathway: Carbohydrate metabolism; hexose metabolism.
EC: 2.7.1.-
Catalytic Activity: ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+)
Sequence Length: 63
Sequence Mass (Da): 6850
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A0A183CWR7 | MINEKIVAGEHFTTAEGTSALVNRARRSAWPAVSVDEAARILDGQVSVIDGTRTVSIKNIKSGTHSQKLEFFKIPAADGKGIRRVVSGTTAGVLATTVLQPGTICRVNTGSMVPDGADAVVQIEDTRLVEHNETEEVLVEILNEPEIGQDVREIGCDIKLGELLLSRGCVIGAAEIGILSAAERKFLQLFKQPKVAIVSTGNEVVDSESDQCPVGSVRDTNRPQLIALVKEYSFEPFDAGIVPDESDLIYCFCFKNLFFTKPTRQYFRKENIQEALEAALMLCDVAVCSGGVSMGEKDYLKEVLQRMNFEIKFGRVLMKPGLPTTFAAGNWDGKEKLVFGLPGNPVSTWVTAHLFLLPTLKKMAGWAQCQFTSISVRVS | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes two steps in the biosynthesis of the molybdenum cofactor. In the first step, molybdopterin is adenylated. Subsequently, molybdate is inserted into adenylated molybdopterin and AMP is released.
Catalytic Activity: ATP + H(+) + molybdopterin = adenylyl-molybdopterin + diphosphate
Sequence Length: 379
Sequence Mass (Da): 41329
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W6TIZ4 | MSSFVIICIVSISRLMTHSGMIKDLADGISTLTGTLYPLFSPLIGALGTFLTGSDTVSNVLFGPLQTQIANNIDINPYWLSAANTTGATGGKMISPQNITIATTTAGLIGQEGKLLSKTIIYAIGYILISGILVYFLL | Function: Uptake of L-lactate across the membrane. Can also transport D-lactate and glycolate.
Subcellular Location: Cell membrane
Sequence Length: 138
Sequence Mass (Da): 14503
Location Topology: Multi-pass membrane protein
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A0A0A2FIR4 | MSDLYINLQSIQALYDAEIERLAVQSGKTLLERKKEDKNHVLGWVDTPISMQEEDFLRIERAASTFSGCDFVICIGIGGSYLGGRAVIQALGHSFESYRTTHKHPQVLFAGQNICQDYLYELMMLLQDRSFGIIHISKSGTTTEPAIAFRFLRDLLIGKVGEKEADRLTVVITSPFSGALRTLANQKKLTALDIPDNVGGRFSVLTAVGLLPMAISRIDIRQLLNGAKRMREQCLSVAFDKNPAMRFAAARYALYMSGKKIEILATSTPKLHFFSEWWKQLFAESEGKQQRGLFPAAITLTTDLHSMGQWIQQGERSIFETYVTVDKCRNNLTLPLYAEDTDQLNYIAGYSPNEINRQALIGSQMAHTEGEVPILEVSVPELNAYCMGQLLYFFEFVVAIGGLMLKVNPFDQPGVEAYKVNTFRLLKRPGY | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Function: Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
Catalytic Activity: alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate
EC: 5.3.1.9
Subcellular Location: Cytoplasm
Sequence Length: 431
Sequence Mass (Da): 48380
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A0A257KZZ9 | MNGFLISVVSVLYLGFLFYLAFVAERFKSKKKSLIDNPYVYALSLSVYCTAWTFYGSVGRVKQTGLEFLSVYIGPTLVMLLGWSVLRKIIRISHVHSITSVADFISARYGKYRSLGVWVTIISLLAGIPYIGLQIKAISKSFEILSGMTHGQYFYQEPAFYISMLLVVFTILFGTRKVQANETHEGMIFAIAAEGIFKLLAFLAVGIFVTFWMNDGFAGVFEKHYYQKEIQKAFDFEKQPGYGNWFMHILVSAFSFMFLPRQFQVAVVENQNENNLKQAIWLLPLYMFLIDIFVIPIALTGSSLFAANPSILADNYVIELPLSVSANIIALIAYIGGFSAATGMIIVETIAISTMLTNSLVLPALLENKRFKEKYTFRIINFAVWIRRGAIILTVLLGFFYYKTVASYFSLVSIGLIAFVAIGQFGPIILGGIFWKGATKAGALVGLLSGFTIWLFSLILPSLLTDSSGQYINTFVAGFFEFFAHFKIQGFDDISNTTFWSLLVNSLLYFVVSMCTEVTPSEAKQALLFVDVFKYSTKEGQSVLWKGKARNEHLIELLVSFIGSMQAKEELEDFARKNNIDLKDVTADPKLVSYVENTISSIIGTSTARMLVASITKEEVVSIDEILEVLKRSQKIVEDNQELKNKTHQLEKLSKELKTTNEKLQKSDTIKNEFLTTVTHEIRTPLTSIKALSEIIYDNEDLEFEQKKIFLNTIIEETDRLSRLVNQVLDLEKYESGKHKLIKKNIDIPQLLDNVFLRMEELAKERNVKLKSFTHKEITGFKADEDKLIQLLINLLSNAIKFSRAENGWVLLSVDTSKKKVLFTIEDNGVGIPQEMQSRIFEKFYQADNQGSMKEKGSGLGLSITKKIVEIHKGSVFLESMPDKGTKVIVSFPN | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 894
Sequence Mass (Da): 100886
Location Topology: Multi-pass membrane protein
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