ids
stringlengths 6
10
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stringlengths 16
1.02k
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stringlengths 117
4.4k
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A0A6P4CHB5
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MEDRGNVTAAPPAEEKVFRSTEVFAAESSSKSKGFKTTLALALWLGAIHFNGALMLFALLFLPLSKALLVFALLFVFMVIPIDEKSKFGRKLSRYICKNACSYFPITLHVEDIKAFNSNRAYVFGFEPHSVLPIGVVALADNTGFMPLPKIKVLASSAVFYTPFLRHIWTWLGLTPATKKNFLSLLDNGYSCILIPGGVQETFLMEHGTETAYLKARKGFIRIAMQKGQPLVPVFCFGQSDIYKWWKPGGKLILNFARAIKFTPIYFWGIFGSPIPFKHPMYVVVGRPIELDKNPEPTTEEVATVHSQFVASLQDLFERYKARAGYPNLELRIV
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EC: 2.3.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 334
Sequence Mass (Da): 37502
Location Topology: Multi-pass membrane protein
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A0A2G6HU48
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MGEKTSFESQMQKLEELVRQMSRDELSLEEALACYEEGIVLSRELSQRLEQAQQKVENLSSIIAEQPVGKSE
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Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.11.6
Subcellular Location: Cytoplasm
Sequence Length: 72
Sequence Mass (Da): 8216
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A0A2P5X2I3
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MASSTSKKVTLKSSDGVIFVVDEAVALKSQTIKNMIEDDCADGEIPIPGVTGNTLAKVLEFCTKHVDDKDDELPTKFKDWDANFAKVDQNTLYYLTLAANFLNIKSLLGLMCQTVADMIKGKSPEEIRKTFNIENDFTPEEEEEIRRENAWAFN
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Pathway: Protein modification; protein ubiquitination.
Function: Involved in ubiquitination and subsequent proteasomal degradation of target proteins. Together with CUL1, RBX1 and a F-box protein, it forms a SCF E3 ubiquitin ligase complex. The functional specificity of this complex depends on the type of F-box protein. In the SCF complex, it serves as an adapter that links the F-box protein to CUL1.
Subcellular Location: Nucleus
Sequence Length: 154
Sequence Mass (Da): 17273
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A0A2S1Z0X3
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MTDPVRAPWEAPMRLALEEAARAPLTGDVPVGAVVLAEDGAVLATGRNERELTGDPTGHAEVLALRRAAAARGSWRLTGCTLVVTLEPCTMCAGALVLSRVDRVVYGARDEKAGAAGSLWDVVRDRRLNHRPEVIQGVLEAECARQLTAFFRDARGGAAETLGPRTPGSQDPGRQTPGSQSACPQTPGQRAAGQGPGNGLPER
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Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deamination of adenosine to inosine at the wobble position 34 of tRNA(Arg2).
EC: 3.5.4.33
Catalytic Activity: adenosine(34) in tRNA + H(+) + H2O = inosine(34) in tRNA + NH4(+)
Sequence Length: 203
Sequence Mass (Da): 21277
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A0A0H5BAZ9
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MTATTTAPAPNTTLIADLGGTNARFALFGADKVGPIVRLAVADHASLPAAIASFLAKAAPAHPPTRAVLAIAGPVDDGRAVFTNADWIADAQQLGRTFGFSSVRLVNDFAAQAWALPHLGGGDLFALGGEASVPGAPMVVLGPGTGLGVAALVPTPAGGIVISTEGGHVTLPGTSPREDAIIAVLRAKLGHVSAESVLSGPGLVHLHDAIATLDGACHTARTGPEITAAGLAGSCPVCRSTLDAFCAMLGMVAGNLALSFGARGGVFVAGGIAPRLVDYLKQSAFRAQFEAKGRFRAYLQPIPVHVVLHGDPAFVGLAAIARAG
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Catalytic Activity: ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+)
EC: 2.7.1.2
Subcellular Location: Cytoplasm
Sequence Length: 324
Sequence Mass (Da): 32457
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A0A0R2HLZ4
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MMEKLKERLDAFSDAVIAIIITIMVLELPMPQHDSLSEYLQFGKAIGIFFISFCYIANIWYQHSVLYSDAKTINNKVFVSEFVFLAFLSLIPIFTKLITVDTNRHTVMAYGILTFIVSGLSMLVSFEVVHQEYSEKSDVQRIFRKVYQNHSNFLGIINVVVLILAYFKPTWAVWCYLALPVISFIFNRDDQTDLKEVPSLPQADQNKYLNFSNTDLREYRKKQRQISHKYMKQRQTNPNWQEDMAKEMRDLFKDGGFDQSTMGAGFSRQPFSRQPYERQTDQNKKPDKLNNPNKTNKPKK
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Catalytic Activity: K(+)(in) = K(+)(out)
Subcellular Location: Membrane
Sequence Length: 300
Sequence Mass (Da): 35123
Location Topology: Multi-pass membrane protein
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A0A1Q4H574
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MNTKLLAAELDEPTPVSELGAERVRRACSAMTAGEPVVLSDGTESSLVLLSSAATPAGVSRLIKAGSGLLFVAVEQDRLRQLRIPPMAADHHSSSSRFHVAVDAAVGIGTGISATDRARTVRLISDPACGIDDFVRPGHVIPVAADMTPPHAPGTAELALALARLAADSVPTATYCALTSEGDPSSVAGPEEGAAIARQNGLAYVLREDVLAAFYRAR
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Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1.
Function: Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
EC: 4.1.99.12
Sequence Length: 218
Sequence Mass (Da): 22504
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Q9ST31
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MAVSMRSATVRASGRVQARPAARTVKATASLQKVAQVAGVAVSSLALAFAAGADATVKLGADSGALVFDPATVTIKAGESVSWVNNAGYPHNIVFDEDSIPGGENADALSHEDYLNAPGETVSSKFATAGTYEYYCEPHQGAGMKGKVVVN
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Cofactor: The crystal structure with reduced Cu(1+) has also been determined.
Function: Participates in electron transfer between P700 and the cytochrome b6-f complex in photosystem I.
Subcellular Location: Plastid
Sequence Length: 151
Sequence Mass (Da): 15431
Location Topology: Peripheral membrane protein
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A0A0D1JKU6
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MATVYQHSTLAALMAGLLGGTITVGELKEHGDTGIGTLHGVDGEVIILNGEVYQAESSGKVNHITDMSTLVPFATVHQAHGPESKAITLKDVTLSNVDVINEYNLYNNFSGIGLHGEFSHIKVRIAPKASEPFPSLLEITKQQPVFERENVSGTLVGYYSPELYHGVVAAGWHVHFISDDRQFAGHVLEFQAPELTGSLVAFSDYQLHLPIENTAFREHHLDMNGLREGVTAAEGNTND
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Pathway: Polyol metabolism; (R,R)-butane-2,3-diol biosynthesis; (R,R)-butane-2,3-diol from pyruvate: step 2/3.
EC: 4.1.1.5
Catalytic Activity: (2S)-2-acetolactate + H(+) = (R)-acetoin + CO2
Sequence Length: 239
Sequence Mass (Da): 25943
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A0A8H3YL72
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MPPRVPVRLLRSHQISALRTSFRQQFQQPFRFQRRYAATEAAPVAEQTGFAKFWNSKVGPKTVHFWAPIMKLVIVLAGVADFAKPPETLSLNQNLALLSTGAIWTRWCFIIKPQNLFLAAINFGLGIVGAIQVTRITLYNNSLKKGGITETIKDEVKAEGQAIKDTAAAAKKAVN
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Function: Mediates the uptake of pyruvate into mitochondria.
Subcellular Location: Membrane
Sequence Length: 175
Sequence Mass (Da): 19376
Location Topology: Multi-pass membrane protein
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A0A523D812
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MPELPEVETVRRGLEPHVVGGFIDDIEVGDPKIFQIEPHLLLEQIRGQQILGLTRRGKYLIFELERHYFIFHFGMTGQLTFRDPNRSDSEGFKRHPVTGLQRTRQHAPDRHTHLQVHLRQGGAMLFRDIRKFGKVFLIEKGEVAVFFERLGLEPWTPDYNLKAFLQKFGNRKLAIKSLLLDQSFVAGVGNIYADEALFAAGIHPARKVRSLRKTEKESLFEAIPKVLEEGIEYGGTTLRDFVNSDGNTGHHQERLQVYGRKGESCHRCGTLIQRMVISQRSTCFCPDCQPRGGRSRTGKAPI
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Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.
EC: 3.2.2.23
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: 302
Sequence Mass (Da): 34472
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A0A0P9DB60
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MKDFIWRLRMNYDIKSIKGTDINYYFICKRRAWMSIHTFYIIDKNQFIEHGNFLNNRNRKYGYHGIRIGHNEIDNLEIDTQGNYIVHEFKRGRKALEGDIFQVLHYIELLENEGFKVRYGVLHLLGANKIKIVEKTPELLSKLEKAYENINNLRNDKMPEPVKNYYCSHGCSYAFFCWG
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Cofactor: Mg(2+) or Mn(2+) required for ssDNA cleavage activity.
Function: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA).
EC: 3.1.12.1
Sequence Length: 179
Sequence Mass (Da): 21454
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A0A179ISC8
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MTVTLRTEEMILNVGPQHPSTHGVFRVILKLDGETIVEATPVIGYLHRGTEKLAEDLTYTQIIPYTDRMDYLSAMIGNYALVHAVETLMGLEIPERAEYLRVIAMELNRIASHLVWFGTYLLDIGALTPFLYAFREREKILTLLAELSGARMTYSYMRIGGVKWDVPDDGWLGRVERFVDDFERALEDFHALVTGNEIVQARLQGVGRYDQETAIAYGLTGVNLRSTGVAYDVRKAKPYSIYDRFEFEVPVRTEGDLWARYLLRMEEMEQSRRIVKQAVRQFPSGGEIMARMPKLIRPPAGEVYTSVESPRGELGVAIVSEGKPQPYRIHFRRPSFVNLQLLPKLLVGQNIANMVAILGSIDIVLGEVDA
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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 a menaquinone. 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: 370
Sequence Mass (Da): 41884
Location Topology: Peripheral membrane protein
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A0A4P1S0Y0
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MGGIQLCKELMQIRRIFVDETAIPGARLTLTPSEHHYATRVMRLKQGQGVELISPEGCMDATLESISAHRTVVRVLSSAKIKNEPSVSITLFQGIPDHLEKLELIVQKSVELGISRILTFTSRYTDAKYRKLDLTKKMVRMNKIAKEAVRQCGRTRTPNVEGPVPIEKIDSELVGHDAVFLFFEKEFKEQKTLVSSPENPAIIVGPEGGFSDAEVAGLVEGKCIPIHLPGRILRTETAAMACLTLVQAHFGDYSHVF
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Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.193
Subcellular Location: Cytoplasm
Sequence Length: 257
Sequence Mass (Da): 28508
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A0A0A6Z8M9
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MSLKEWFEERRKISGSIEDLIERTSKDYIVNEMDKNKNIKIDFNNRLWVQCDNCENLLYMKYLRQNKSVCEECGYHLQMSSSDRIELSIDHGTRHPMDEDMAAPDPIQFHFEDEPYIDRITSCQIRTGLTDAVQTGIGRLNGIPIAIGVMDFQFMGGSMGSVVGEKITRLIEYATKESLPVIMVCASGGARMQEGSFSLMQMAKISAALYIHQLEKKLLYVSILTYPTTGGVTASFGMLGDIIIVEPKAYIAFAGRRVIEQTSGQKVPDGLQVAEHLFDHGLFDLIVPRSLLKGVLSELFQLYGSIPCEKERTLGSVSCNDQQLSSSATRNESNSDTVSSRVENRNNQSQRIVPHLSFSQLSILDPIINRNSVLTTK
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Cofactor: Binds 1 zinc ion per subunit.
Pathway: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
Function: Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.
EC: 2.1.3.15
Subcellular Location: Plastid
Catalytic Activity: acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein]
Sequence Length: 377
Sequence Mass (Da): 42280
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F0UIY7
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MRLLATGRILRLASNQGRATAKSTRYYRPARSQLTPLVNSRSNSSTSTGAEAAAADSAPVGALGQSKSQPDRQVSTARPAQEGIKDGDKIHHVDEWTNTPGNILSHIGRRLYLDENHPLSITRQLIESQFTGPEFGNYAEPNPIVSTAQNFDILGFPANHPGRSRTDTYYVNKTTVLRTHTSAHQHSYFQRLGLNEKACPDEEGYTVIADVYRRDAIDRSHYPVFHQMECARLWKRPRGDPLKYSLQTAETIMNDANKIPAHNVKVEDPNPTIHAQRNPLQAEHLSVQETEAIAAHLKRSLEQLVIKIFTAAREGTPESAHTDQELLKVRWVEAYFPFTSPSWELEVFWQGDWLEVLGCGVVKQELLISAGVPHRVGWAFGLGLERIAMLLFNIPDIRLFWSRDPRFLSQFQAGKITRFIPFSKHPACYKDVAFWLPPSAAAAAGSRMPFHENDIMEIVRDVAGDLVEDVQLVDEFSHPKTGRKSLCYRVNYRSLERTLTNEETNKLHEMVRRKLVEKAGVEIR
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Catalytic Activity: ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) + L-phenylalanyl-tRNA(Phe)
EC: 6.1.1.20
Subcellular Location: Mitochondrion matrix
Sequence Length: 524
Sequence Mass (Da): 59217
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A0A2V8HML4
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MALVGRIGRPHGLKGQVVINPETDFIEERFAAGAIVWIKSDGGEQQLTVASMRVQNGRPIVGFAGFNRIEDVERLAGQELRVPEDALQPLGAGTYYEHQLVGCAVETTDGGSVGEVAKVEGGAGGSRLVIDGPRGEILIPLAVDICVDIDVANRKIRINPPEGLLELNEVRHRHHLSADDRSRARGRGR
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Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Subcellular Location: Cytoplasm
Sequence Length: 189
Domain: The PRC barrel domain binds ribosomal protein uS19.
Sequence Mass (Da): 20355
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A0A7W1P8H4
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MSTLTWMDGRLVPESQAVVPFLTAGLHYGMGVFEGIRCYDTALGPAVFRLDDHVERLLASARILGFGPLPYDATALSEAVHETVAANHLRACYIRPLIYLADGGMNLSLDTGRPRVGIAAWAWHDYHGGSATAGIRVNVSSYTRHHPNAMPTHAKVAGNYVNSFLAKTECSRLGFDDAVMLDTEGFVSECTGENLFLVRRGTIFTPPVDSALSGITRDTVMALAGDLSLRVVEERLVRDRLYSADEVFICGTAAEVVGVREIDMRPVGDGAVGPLTAAIQREFREVVSGRHARSAGWLSTAPERPVSGTLESQGVQAPR
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Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4.
Function: Acts on leucine, isoleucine and valine.
EC: 2.6.1.42
Catalytic Activity: 2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate
Sequence Length: 319
Sequence Mass (Da): 34426
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A0A957H910
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MGRFLMVGAGGFIGAILRYAISLWLAPLSERVGFPYGTFVANMLGCFLIGFLSGWVLARELSLEMRLLILTGFLGALTTFSTFGYESLALLRGEGVGYGLLNILLQLTVGLGAIWLGGHLAPALD
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Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 125
Sequence Mass (Da): 13329
Location Topology: Multi-pass membrane protein
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A0A132MQM0
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MRYPPIDELVAQAGSKYRLTMIAARRARQLLEDKRPLIEAPRSSRDVGIALEEFYAGRLEVRPKAEA
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Function: Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
EC: 2.7.7.6
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Length: 67
Sequence Mass (Da): 7641
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A0A3D0J508
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MKTYGLIYNRNRPGAERIVRELAAWLKDHGIAALAEKGFDISQAEMADEAQVAARCDMMLVLGGDGTLLRAVRLMGDAQKPVLGINLGSLGFLTEISQDNIQQSMEQVIRGQYQIEERAIIKARCGDADFFALNDFDIRVPTRLVELSVSIGDELVSRYFADGMLIATPTGSTAYSLSAGGPIVEPDMDAFVLTPICPHTLSLRPMIVSMKKTITVVVHGKNEEAVLVADGQTVARLKDDQKLTITKAERKALLARPAASSFYNILRTKLKWGARGENS
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Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
EC: 2.7.1.23
Subcellular Location: Cytoplasm
Sequence Length: 279
Sequence Mass (Da): 30482
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A0A2V9YPX1
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MLITITVADHFHLVMPGWSPVALWSVAVITGLLFFAALLAHELAHSVLAKARGLRVRAITLFALGGVSQIESEASDAKSEFWIAFVGPLTSLVIGVICLGIARLTGWAPGSEPYTPVPAVLLWLGYINIALAAFNMIPGYPLDGGRVLRAVTWWITGNADRSTRIAAQVGQLVALLFIISGLIQFFSGKGFGALWIAFIGWFLLDASRSSYIHVELMSGLRDRRVADIMERDCGTVESHLSLEDFVDEYMLRSGRRCFVVIQNNYLVGLITPHEVKQVPRDQWPQTSVQSVMRPLRDLKVVTPDTPAVQALELMTREDINQLPVVSHGHLEGVFSRGQVLRFLQTHSELHGH
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Cofactor: Binds 1 zinc ion per subunit.
Subcellular Location: Cell membrane
Sequence Length: 352
Sequence Mass (Da): 38839
Location Topology: Multi-pass membrane protein
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A0A0W0U8H7
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MATIEIDGKTCEAENGKMIIEVADDAGIYIPRFCYHKKLSVAANCRMCLVEVENGRKPVPACATPITNGMKVFTKSEEAIRSQKAVMEFLLINHPLDCPICDQGGECELQDLSMGFGADMSGYDESKRSVDDDNLGKLIATEMTRCIHCTRCVRFGEEIAGVRELGATGRGEKTQIGTFVEHSMTSEISGNIIDLCPVGALTSRPYRFTARSWELQQHESIAPHDCLGSNIYLHVRRNQLMRVVPRECEPLNETWLSDRDRFSYLGVNSEKRAQQPMIKRNGQWESVDWEQALKFAAEGTSRVIEHHGPEQFAAFASPSSSLEEMYLLQKLMRAMGVNNLDHRLHQTDFSDQAQRPVLTKNSAQVADLESASDILVLGSNLVREVPLAAARMRKAVRNGAQLAVINPVDYDLHCDVHMKAIASPQDMPHTLAALVLATAEASNRLDELSDEVRRLTLGVHVSESIREIAASLSKPEAIIITGALFENHPHASLLRALLSEIVRLSGAKDMHLSTGSNAAGAQIAGMVPHRGAAAAVLDAPGLDAQASIEARLKGYWLMGVEPGFDFANPHAARQAMLGAEFVVVMSAFVCDSMKDYANVILPMALSPETSGTWINVNNTWQSVKGALTPPGEARPGWKILRVLGNILQCRDFEYVSSDEILREVQSALDLLVDAAYQPIWPEALPVHTDELVRVGEWPIYRVDATVRHATALQHCASADEACVRMHPETANRLKLQNEATVSQGNIKITLPLKRDERVAPDVVWVPNAMPETVDLGHAFAGITITC
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Cofactor: Binds 1 [2Fe-2S] cluster per subunit.
Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. 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.
EC: 7.1.1.-
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
Sequence Length: 786
Sequence Mass (Da): 86344
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F0US47
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MADEIKIDKATFFNRLSTFYSAWKADKRLSNPVFGGVGSIVILMGKTEDANSFQKNNAMHFWLLGYEFPATLFVFTTEAMYVVTTAKKAKHLEHLKGGKIPVEILVTTKDPEQKAKVFEKCLDVIKSAGKKVGTLPKDMSTGPFVEEWKRLFSEISKEVEEVDIAPALSSVAFAVKGPEELISMRNASRACSGLMSEYFVDEMSQLLDEEKKITHKELATKVDAKMDDAKFFKKLAKLPPEFDPQQIDWAYGPIIQSGGNYDLRFTAVPDSNNLHTGIIIAGFGIRYKTYSSVIARTFLVDPSKSQETNYAFLLSIHDAVMKDIRDGAVAKDLYNKALGMIKAKKPELEKHFLKNIGAGIGIELRDPNMILNGKNNKVLKSGMTLCVMIGFTDVQDPDPKDKKNESYSMVITDTVRVGESSPHIFTKDAGIDMDSISFYFGDEEETEKPKVKSEASKSSAIASKNITKTKLRAERPTQVNEGAEARRREHQKELAAKKLKEGLERFAGTTGDQNGTSQKKFKRFESYKRDNQLPIKVKDLAVYVDHKASTVIVPIMGRPVPFHINTIKNASKSDEGEYAYLRINFLSPGQGVGRKDDQPFEDPSAHFVRNLTLRSRDNDRLAQVAQDITELRKNALRREQEKKEMEDVVEQDKLVEIRNRRPAKLPDVYLRPPLDGKRVPGEVEIHQNGLRYQSPLRSEHVDVLFSNVKHLFFQPCAHEMIVIIHVHLKTPIMIGKRKTKDVQFYREATEMQFDETGNRRRKHRYGDEEEFEAEQEERRRRLALDREFKAFAEKISDAGRDEGVDVDVPFREIGFNGVPNRSNVLIQPTTDAIVQLTEPPFLVVTLSEIEIAHLERVQFGLKNFDMVFVFKDFHRPPVHINTIPVESLEGVKDWLDSVDIAFSEGPLNLNWGAIMKTVTSDPHGFFVDGGWSFLAQDSDSEEEEDEEESAFEMSDSELAASDESSEDDSEFDDEASAEASEAFSGDEDDESAGEDWDELERQAKKKDRESGLDDSEKGKKRKR
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Function: Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides.
Catalytic Activity: Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide.
Subcellular Location: Nucleus
Sequence Length: 1023
Sequence Mass (Da): 115742
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A0A0I9SAI3
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MKLPILVYGQPVLRKTCEKVDMSAPELDRLITDMWEILRDADGCGLAASQVGSSLQLFIVNSRDTFLYMDKQERAQYFEGDTGIQETFINAEILARDDERMHSEEEGCLSLPGMSERVKRPWSITVHYFDRERKEHTRTFRGYTARVIQHEYDHTLGKLYIDRLDSLRRNLIANKLKKFAAGTRRGK
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Cofactor: Binds 1 Fe(2+) ion.
Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
EC: 3.5.1.88
Catalytic Activity: H2O + N-terminal N-formyl-L-methionyl-[peptide] = formate + N-terminal L-methionyl-[peptide]
Sequence Length: 187
Sequence Mass (Da): 21747
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A0A7S3D7J1
|
MGALELINSPKKVFNLLSHPSEIAAIFKLRAYAKKIEQDRDRINRGDENVKYAYDVLTRTSRSFASVILQLGDDLRDSVCIFYLVLRGLDTIEDDMSIPLQEKLEMLYKFPIYLETPGWNTTHGEDAYKDLMKNFDKIIDVYSKLPKPHREVISDITKRMGEGMAHFATREVVTKADWDQYCYYVAGLVGIGLSRLFYVSGLESEKYNQMDSTASLANSMGLFLQKTNITRDYLEDIIEGRIFWPKEVWSKYAEKLEDFRAPANKDKALACLNELITDALGHGLDCVDYMVTLQDKNNFMFCAVPQVMAIATLAECYNNYGVFTGVVKIRKGLAAKLITDCTNMERLYGHYVTFSKIILSKINPADPNARLTKSICEDMIKKCEPHASYAPSFMVNKVLIPAMAVGTIAFAIAPSSFFSSN
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Pathway: Terpene metabolism; lanosterol biosynthesis; lanosterol from farnesyl diphosphate: step 1/3.
Function: Catalyzes the condensation of 2 farnesyl pyrophosphate (FPP) moieties to form squalene.
EC: 2.5.1.21
Catalytic Activity: 2 (2E,6E)-farnesyl diphosphate + H(+) + NADH = 2 diphosphate + NAD(+) + squalene
Sequence Length: 421
Sequence Mass (Da): 47638
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A0A0H3WDF2
|
DMAFPRMNNLSFWLLPPSLLLLVISGMDEMGVGAGWTIYPPLASLEGHSGSSVDFAIFSLHLAGASSIMGAINFISTIVNMRSWGMSMEKVPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNSSFFDPAGGGDPVLFQHLFWFFGHP
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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: 151
Sequence Mass (Da): 16392
Location Topology: Multi-pass membrane protein
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B8N5F2
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MVNLQLTLPAMALSSTVLAASVHSETSVGTLHRERAEALLSQMTWEEKVGQMGGIRRLLNTGPEIDEENYEYRQAEYQNGNIGFGATLNWADDILPLTNEVRQRQINESRLHIPFITVTDSINSLYLSGGTIFPSNLAMAATFNIPLFSEGVAALREEQIAIGVSWVLSPPLDIAWEPRYSRIGELFGEDSYLTGEFGHAYVQTMQDKDDSGNIKVATTVKHFVYGESRGGINAASMYGGINHLYNDQLRPYLRALEADPAAVMVSYASVDLVPMSANKYLVRDILRQRLGFEGIVMSDAGGIAHLYTESRLAGSYAEAALLALEAGLQMELSPQSPAVFPTLVAAAEDSHVGQLIDEAVLNILQLKFATGVFDKPLPDPAKVNETLRTPAHLEISRHVTRESIVLLQNDGILPTTPSKVALLGPFADIRNYGSYAPVNSSDSQYGNSLYQSLQAKLGTSNVTLVQGVDFIDTDTTNIATAVSAAKEAGLAIIVLGSLSVGTTDPLVTKRTDGEFFTHANLGFPGAQQQLLDAVLDASIPTILVLSGGQPFVLNNSTLRSNAILHSFLGGEFTGDALAEIIMGDVNPSGKLPISLPQDTSATPVFYDYLPSDDTGTADSILGFHSTYQFPLLSRSPPMPFGFGLSYTDFTISAPRARASNSSVEVRVNITNVGPIAGKEVVQLYHRPNTTTGIEVPVKRLVRFEKVDLHAGEGREVRFVIPHKDLGYYVDGELRVKRGVYSFWAGTSSRTEDLKGVNVTVL
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Pathway: Glycan metabolism; cellulose degradation.
EC: 3.2.1.21
Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.
Sequence Length: 761
Sequence Mass (Da): 82404
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A0A094ZHS9
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MSENIKDGKQSLHSDHRRSGGHDYRRHTSGHIHSSDSHPRTFSGGATHSEVGEGGVGGLVGDSHGGHSFGGHEQGGVMDATFIWKLTKLGRIGSSRLRFDDDFADRLNYQYTGVLMFLFIGLIGIRQYVAIKITLKTYIFLHNLIGNNFMRFQSKRFMSLLFIIFGNLNTTTTNNNNRSNNHCNEQAYVCKPIQCWIPQEFTRGWEEYAENYCWVSNTYFAPLQHSLPPAPDREMLLIGYYQWAPIVMAIQAMLFYLPCLIWRLFMAQSGFNVRRILQMSCDSNVLLPEHTMKNVRFIARYMEGCIYRQRDYRKRKLSTVLGFSPTSYTGLGQSPHIHVHQHYSPSYPPHLHQQQQPHSHLHHPPPPPPPHSHTQSPPYMPTSQFHQQLTTVNSRQSPIGGDENRYNNDHQIESTLITSPRRDSNTSLFDKIRHSFSIDDNNKKSKKRLPSVTEEANTLVTTMETLNSRNSGDYHPMLGRLKIDDSHTQQNITTNVNTTNSYRSIHTLSPTLYKSQEKSSLNLHKKQHLHYCCTCFCGKRQGNFLVLLYFFTKFLYLTNIIGQLFMMEKFVGNDSTFYGFRVLYDLLKGREWFHSGNFPRVTFCDFEAKKLGKNHK
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Function: Structural component of the gap junctions.
Subcellular Location: Cell membrane
Sequence Length: 616
Sequence Mass (Da): 71074
Location Topology: Multi-pass membrane protein
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C1LH70
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MDFYVNVPPPVHYLDVAVAFKSLSNAEKDYVFSCTQASWVGGLIGLIQTSPESAGIFLFVNRFFKSENVYSFMEKATKNNFSDEEITHLLSYFASVLGNFGNYLSFGDTKFIPAISLERVTDLLSLNNAFSDPKTGLKVLWEKIAPAVYSLNPRRLRLGFGPTEITSYYSGDCIRSDAELVQKYLENIKTEAYNTRLFKSSSSNSKVYSIRFASAEEKVQSVDFSGLPQDTYMQLEYGDYCEIMKLLVDCSMDAEAHSLNKVESEMWQHYAKSFCTGSVDSHKDASRLWVKDKGPVVESYIGFIETYRDPLGVRAEFESFVAVVNKSMSSKFQRLVDNAVELLSNLPWPSTYEKDRFLQPDFTSLDVVTFATSGIPVGINIPNYDDVRQVDGFKNVSLGNVLSARFKDPKSEFLRNEDKKLYIDHAESSFELQVGLHELLGHGSGKLFQRTNDGKLNFDTNSTKDLITGGPILSWYEPGETYDSKFSSLSSAIEECRAECVGIYLCNLPLVLEQFGLNTNCSADTVPDVVYVNWLSMVRSGVISMEFYSPGENPSDIGSWRQAHCCARYAILRVLIEADSSLVLVNEVVGEDGAPDISIFLDRKKLLTVGRPAIGEFLRKLQYYKSTANAKDGCAFFQHYSQLLPEHIKLRKIVIDRKKPRPIFVQPGLRKTPSGVELISYPTTYPGVIQSFVDRYNDLPLGQKALNALEKIWYRELPYFENIPV
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Cofactor: Binds 1 zinc ion per subunit.
EC: 3.4.14.4
Catalytic Activity: Release of an N-terminal dipeptide from a peptide comprising four or more residues, with broad specificity. Also acts on dipeptidyl 2-naphthylamides.
Sequence Length: 725
Sequence Mass (Da): 81692
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A0A0Q2S4R0
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MEKGRLVLIDGEHYPDVTAWAVEKLGDVCCAVFLGGSEKIGSIDEIGRKLGLRVYYGHDYMMSLRRALEENEITEVVDLSDEPVLDYEDRFRIASLCMLYGVPYRGADFYFTPRRLKRTRKPSLAVIGTGKRVGKTAVSGFIARTLKEIARPVIVTMGRGGPEKPELIDGERFEITPEFLLQLAQSGKHAASDHFEDALTARVTTIGCRRCGGGMAGFSFFDVIDEGIRLAESLPNDLIILEGSGATFPAYRADGYILITSAKGKLDFIRGYFGSFRVSLADVVVVTMADSVSEGRLRALKEAVRSINPDADVHLTTLRSRPLGDVSGKRLGLVMTSSDALPRAGEWLEKLGAEVVAVSANLSRRGLLLKDLQAFRGIDAVAVELKAAAVDVVTKWALENGIEVIYLDNEPVNVDGKDLREAILKLGRSILEGGR
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Function: Catalyzes the formation of cyclic 2,3-diphosphoglycerate (cDPG) by formation of an intramolecular phosphoanhydride bond at the expense of ATP.
Catalytic Activity: (2R)-2,3-bisphosphoglycerate + ATP + H(+) = ADP + cyclic (2R)-2,3-bisphosphoglycerate + phosphate
EC: 6.5.1.9
Subcellular Location: Cytoplasm
Sequence Length: 435
Sequence Mass (Da): 47527
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A0A5B8YYD8
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PGSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMNFWLLPPSLTLLISSKIVKNGAGTGWTVYPPLSSNIAHGGSSVDLAIFSLHLAGISSILGAINFITTIINMKLNSLSFDQMPLFIWAVGITAFLLLLSLPVLAGAITMLLTDRNLNTSFFDP
|
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: 179
Sequence Mass (Da): 19347
Location Topology: Multi-pass membrane protein
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A0A5M3YKS1
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MPSIFSATLALCIATAGVLSGICMYPPHGPPPTRFRTDRIRFMTGAFPKLVTHICTVAFLYHALVTLYYPATATDAPVLSTICPYPHHLDANIVSWSPRTMLSLLTIFVGAIVRIAAYGGLGRNFTFELAAPDRLVTGGMYRFVQHPGYTGLGMVVAGGLGICYQWHSAAIACWMPDGLFYDLQWVAELGGLGVGVVGLSVLTIRVRDEERMLRERFGEEWEMWHRRTARFVPGIA
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Catalytic Activity: [protein]-C-terminal S-[(2E,6E)-farnesyl]-L-cysteine + S-adenosyl-L-methionine = [protein]-C-terminal S-[(2E,6E)-farnesyl]-L-cysteine methyl ester + S-adenosyl-L-homocysteine
EC: 2.1.1.100
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 236
Sequence Mass (Da): 26009
Location Topology: Multi-pass membrane protein
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A0A453QMY1
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MMGDTLREGTHLDIESELNLIKHTQMELKANCATDKAQRKTMKELGLKRARRFGWPNTYVFTKAMGEMLLGHLRGDLPVVIIRPSIITSILKEPLPGWMEGVRTIDSVFLGYAKQALKFFLVDPNTIMDVIPGDMVVNSMMVAMLAHSGEQAQTIYHVTSSMSNPASYMTLRESAHRYFVDNPPRGENGEPIRLNKMRFFSTVARLRMYMVIKYKLPLEVRPIFRFEIGVKFDFADENETNVFVL
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Function: Catalyzes the reduction of fatty acyl-CoA to fatty alcohols.
EC: 1.2.1.84
Catalytic Activity: a long-chain fatty acyl-CoA + 2 H(+) + 2 NADPH = a long-chain primary fatty alcohol + CoA + 2 NADP(+)
Sequence Length: 245
Sequence Mass (Da): 28039
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A0A6S8FL82
|
MDCCLCLLTTVYWLTVISSCFAVLGTGTFQRMHAYGKLRVVADQTRADVRPVGPEEKVSLLRQVNKLVLFVEKMTVPKKWFTHFYVVANFWNGLFVVSTFLSYASYTDDQNDKYITIFSLVRILSSPFLGGYCTDITPITLHDVSSKPLPPLVDLFDVLFPLLQVQIHVAFRLYECLYVSKSSLNGRMHIFGYLIGLSFYLAVPWTIVVDTFLWRESEEALATGYGTNEKRSFYFYDICTYLASLCVFVYASHQQKKAHKILAELRAEQNCKSSFLPSSIYIPCHGFLFFEYTIKVNGT
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Pathway: Protein modification; protein glycosylation.
Function: Plays a key role in early steps of protein N-linked glycosylation by being required for the conversion of polyprenol into dolichol. Dolichols are required for the synthesis of dolichol-linked monosaccharides and the oligosaccharide precursor used for N-glycosylation. Acts as a polyprenol reductase that promotes the reduction of the alpha-isoprene unit of polyprenols into dolichols in a NADP-dependent mechanism.
Catalytic Activity: di-trans,poly-cis-dolichol + NADP(+) = di-trans,cis-polyprenol + H(+) + NADPH
EC: 1.3.1.94
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 299
Sequence Mass (Da): 34235
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A0A1W6ESY4
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MISHIISQESGKKETFGALGMIYAMLAIGLLGFVVWAHHMFTVGMNVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYSPSLLWALGFVFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLLTGLTMNEEWLKAQFTIMFLGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNIISTVGSTISLFGILFFLFIIWESMISQRMPIYPLQLNSSIEWYQNLPPAEHSYAE
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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: 255
Sequence Mass (Da): 28705
Location Topology: Multi-pass membrane protein
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A0A0P5PLB7
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MEMFFNICYNYYFSSRIRLRTYDKKKKLVGWYVARCGSMSKREGYINELKEYIQVDSFGPCGNMSCPETNGSPGEALQPCLDMLADNYKFVLAFERFICDDFVTKRFFDILSRETVPIVFGGADYARIAPPHSFIDALSFNPRQLADRLLELDKSDRQYYRHFWWKDFYQVHSGYQELSTRPFCDLCEKLNSNLPRKVYRDIDAWWYNSTKCSGPEDHGIVIRNKGNEDLHSIQIPWSLDD
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Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 241
Sequence Mass (Da): 28421
Location Topology: Single-pass type II membrane protein
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D0QQ77
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YKETWNIGVVLLLLVMATAFVGYVLPWGQMSFWGATVITNLLSAIPYVGNTLVQWIWGGFSVDNATLTRFFAFHFLLPFIIAAVTMLHLLFLHETGSNNPLGLNSDVDKISFHPYFSYKDLLGFVVVLIALTSLTLFSPNLLGDPDNFTPANPLVTPPH
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Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
Subcellular Location: Membrane
Sequence Length: 159
Sequence Mass (Da): 17631
Location Topology: Multi-pass membrane protein
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Q574A2
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LHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLFTGLTLNQQLCKIQFFSMFIGVNLTFFPQHFLGLSGMPRRYSDYPDAFMIWNIVSSIGSIMSLLSVIFMLYILWEAFVSNRKNIHPLNLLSSIEWLQNMPPAEHSYSELPMLTTL
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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: 148
Sequence Mass (Da): 17149
Location Topology: Multi-pass membrane protein
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A0A5M3YTL6
|
MVGCCNELNTGYAADGYARASNNRVAVAIVPYIVGGLSALNAIAGAYSEHLRVIVISGCPDAQMPVFSLDVLEDTLLTCLRESRPVHIEVANDLAHISCLAPGQRPAPPNVEDTSHNAARLSCSQSAILPLAEKLGYAVFVHPDARIFPESHSQFAGCLRPTVVNFEAEKVFLEADIWVVLGGRWSDLHMLGSIDLGNEAHRMIDLQHNSARLPNGLQGSIDLNMPVSELIKSEIASYDRTVRELAGLRHPCGTSSEPLAVTITPNSPESPVTLASVVDGIQQLLGEKDTLVVDTGETWFTSQDIYLPFRRMPLPNTARTVSNQSHCPNHNPCEEQEAANPDAGVISMRIHALDDMEYGLERAAKETSKLVLFECCIRPDDINPALRRLGVQFSGKEQANGCESGEACGTVESSFGQNGQSRAPEGNMHSTLARPDTPILRTALGATLTDPPPMGFFDHLQKGGAFSLQPKKPQIRKVVQSRPAPPPSRSVSQTPASSSRRSPAEKVKKARDSISRSASREPDHTSTKRRLGTPSQSRKRQTPELRLSSDDDDSDTDTSFEVRKRARTEDSAEPDLARRVRSLKAFTEEGVKPLPMVHAADITSVQKPGSFKPAFGEEGRPTEILLQYPSASPKERYNLVVPRDKDDFRPIDDIFQVIDIVSQHYVPEEEADIFNNESTGIKRKLRRALAHSSETDFRQVVADYNDTIERLRRDGTIAKKLDSTHRLTLPLVERILTQIYSRTVSPRVESLRQYENGTDNVYGELLPRFISTIFKETKLKSNMVFVDLGSGVGNVVLQAALEIGCESWGCEMMQNACELAELQQTEFKARCRLWGIAPGKTHLVRGDFLKEQSIIDVLKRADVILINNQAFTPQLNTELVNHFLDMKEGCQIVSLKSFVPAGHKIQSRNLNSPINLLKVKQRNYWSNSVSWTDVGGTYFIATKDSSRLKAFAESLG
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Function: Histone methyltransferase that specifically trimethylates histone H3 to form H3K79me3. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histone.
Catalytic Activity: L-lysyl(79)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(79)-[histone H3] + 3 S-adenosyl-L-homocysteine
EC: 2.1.1.360
Subcellular Location: Nucleus
Sequence Length: 956
Sequence Mass (Da): 105498
|
W5VNA1
|
FIFGAWAAMVGTSLSLLIRVELSQAGNLMGDDQLYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSFLLLIGSSLVESGAGTGWTVYPPLSSNLSHSGASVDLTIFSLHLAGVSSILGALNFITTVINMRTYGMVMERVPLFVWSVKITAILLLLSLPVLAGAITMLLSDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIINHYSGKKESFGSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATLHGSQFNYDPAVLWALGFIFLFTIGGLTGIVLSNSSLDIILHDTYYVVA
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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: Membrane
Sequence Length: 356
Sequence Mass (Da): 38798
Location Topology: Multi-pass membrane protein
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A0A6S8FXN3
|
METMSVDVLSLESNPGKMRTSITTRSLNTSLSSVASTGISQLVGDKDQDRFVVKTTEEDKPDYFAVFDGHGQFALAADMSADHLYDLILDIDAEIANADKSPEDEVAASLPLGPLVPTDEAIVQAFHIMHDDIVAKAKETNQMRTGTCALCLFLGEPTQKDIQRLAADKSEATSEPAAESEAEDENRGDADSDSNSIGGNTSGTSSKNHSFAKIAWVGDSKCIMVDHFNNPTELTVDHRVSTNPNEVKRIQEMSEKLDIREGLLESEFWENEVKVHEEKGKKPRPKSYIGQRSYNGQPRGPHVLFSYSNGISLQISRTLGDPLAARSATAEPEIAYCDISDGQHYRFVLASDGVWDVFTPKEIANILKKYPDPQHAGQAISYQAKNKRMGKGLNNDDITTIVIEVNPHMRVQKSKGSFLNLGSILGRNSKRKLA
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Function: Enzyme with a broad specificity.
Subcellular Location: Membrane
Sequence Length: 434
Sequence Mass (Da): 47628
Location Topology: Peripheral membrane protein
|
C1L5H5
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MLSVLNSASENVQGISTGTTLFACEYDGGVVIGADSRTSSGTYVVNRVTDKLTQLTKSIYCCRSGSAADTQTVADMVRYQLDFHRLEMNREPTVLEAAVCCQHFCYNYRDDLVAGIIVAGWDEQSGGQIYSIPLGGMLIRQPIVIGGSGSTYTYGYVDHDFRKGMTREECINFVLKGVALAINRDGSSGGCIRLAIISKDGVERILTKGDEVPVYRFS
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Catalytic Activity: Cleavage of peptide bonds with very broad specificity.
EC: 3.4.25.1
Subcellular Location: Nucleus
Sequence Length: 218
Sequence Mass (Da): 23713
|
A0A0P4XAH4
|
MAAALDYRKHKVLFIFLFCFPVLFIIYSLFLQLDADKVEFGIKMNDNLPNTESSRDKGIPALKTILYWNHFFGIENFTFGFGHQPFIDAQCPTHTCTVTNDRMLFNRSDVVIFSVQNMNLSDLPDIRFAHQRFVFYEMESPANTDPQPLLHERIRFGFFNWTMTYRLDSDIVNRDSYGVIVPRKLTLPSMFPIARRSDPTATERKSIGGNKKKLLAWFVSNCVTPSQREMYVEELSRYVPIDIYGKCGNLTCTDRSDCREMLRTDYKFYVGFENSLCTDYVTEKLTAGFLYDTVPIVMGGVDYTQFAPPHSFIDVKDFDSPKELAKYLLLLNETDSLYDRYFDWKPNFDVHLDTKQGWCHLCKLANDERLPLTTYEDILQWWVDDPESCNLPVGNTPIPRTK
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Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 402
Sequence Mass (Da): 46837
Location Topology: Single-pass type II membrane protein
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A0A0P5AQE3
|
MVSPRAPLSKLTAGLLFVSFLIYLVIINRLEVGQSDRVADPASFSSRMLMNLPSSGSGDSNNLHDTISNSGVITAIDNMVNQIGVAGSDLTETRVKDISNEIAKQIADYVVQRLGKAATISNPCSSCWKHGNATDLPVIYLVTPTYRRPEQIPDLTRLAQTLLNVPAVHWIVVEDNSALSPAIASLLKRYGIPHTHLKAQMPEKYKKSKLKPRGVANRNAALDWVRSNCKSGVVYFADDDNTYDIRLFEEMRFTKKVSMWPVGLVTKVGLSSPVVNDKGVVVDFFDGWMANRKFPVDMAGFAVSVQLILEKSDVYMPYVPGHEEDGFLKKLDVSPADIEPKANWCTQIFVWHTQTKSNTPANRTTATGKRYKGTNIDTLQEWIV
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Pathway: Protein modification; protein glycosylation.
Catalytic Activity: 3-O-(beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-xylosyl)-L-seryl-[protein] + UDP-alpha-D-glucuronate = 3-O-(beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + H(+) + UDP
EC: 2.4.1.135
Subcellular Location: Golgi apparatus membrane
Sequence Length: 384
Sequence Mass (Da): 42573
Location Topology: Single-pass type II membrane protein
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A0A8H3VQ52
|
MTKRQSLSGVLGRTLKRPVAPPPSFGDQPGLLSMANSGPNTNGSQFFNTTVPTRYLQERAAVIVLRHDGAFPSAKR
|
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: 76
Sequence Mass (Da): 8195
|
A0A378UZU5
|
MSTTAKHVVEVTAEERVELVARARKLAAEFEKYGKRADEDNLFPSELVPLYKESGLPKLVIPKKYGGLGADVWTTALVEKELASYGDPAITLSFNMHHVMVGIFRELLDEPARERLFTKIVEDGSMLSGTLSEERAGISGLSDTVCVPDGNGGWLASGAKNWATYIENADIVAFTAVITNEDGSLPETFSEHAEREAVFVIPADTPGLSIRRTWNTMSMRASGTQTLVLDKVPVPAEAYSGTYRNGLFNEIEWACFPFAGVYLGVGERALRLVSESLSKKSLGRTQEGEEKAVRDIGYVQYELGKAWTELQSAEWAVRGTAEALFEGADATWNPIERPARVSIGKVAATEAAINVTDTALRLVGGGGIRKGAPLEKLFRDARAGIYHPVNSNQAYDLIGKTALGLFG
|
Pathway: Sulfur metabolism; dibenzothiophene degradation.
EC: 1.14.14.21
Catalytic Activity: dibenzothiophene + 2 FMNH2 + 2 O2 = dibenzothiophene 5,5-dioxide + 2 FMN + 2 H(+) + 2 H2O
Sequence Length: 407
Sequence Mass (Da): 44179
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A0A094ZQV1
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MDQNPLLLKIQRIVNGMPENEGPLLNGLDSIFPLMSNNYISNRRTLRSNLEKFQLSYYQDLLASFGDVKKRLDSLDTCINSILETCLRMNGTLTSVKSETVCLVEEAQKLRSDSKVAEIKAYLLELLVGSYQISAEDAHILSSKISHIDDTFFSALLHGKEIKNICKELLQLNELTFSCSLMNEATEILDRAYENLYEWAQNECMKHVHETPEISPYLQRALSELQNKPVLLKYSLDEYANARRKASVKSFLDVLSVEIDSNSTVGNHSVGTIYTMHIREKPRDHVRIVSDILACVHQITASEKEYINSLCKNCHDTLIADLKIICLDTITESLCSHLKLNMENMLVSHHDAVTLYKMNNIMRFYQHTFRSLIKSTASLNLCLDEVQKLCKRLILSTLKQFVKQTLEQPDHPNLNLSPNELITDTLQLLIQMVGDQDISLLPNDEVKVERAELIDCLVSPLITYCEKSASLLNLNSLSHIRHLDDHLPTNPPDNPSVSIYLANCFNAIQVSLSGVPFTSSQVEQVALKLDNCLNSLVVAQVSFILERTGLLLINQRLGTVQDPNVPQYTISQFHDMLVDFNNYLSNPDKLCLPDINKLCSQQLRRLVRRRSADQIHSYYQSVHQAIMNVTQTCSESDTTVQLYTPQHVAELILNF
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Function: Required for normal Golgi function.
Subcellular Location: Golgi apparatus membrane
Sequence Length: 655
Sequence Mass (Da): 74371
Location Topology: Peripheral membrane protein
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F0UV36
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MAAIWGNGRPGGGDQFPLEQWFFEMPVCTRWWTTATLATSVLVQCGVVSPFQLFYSFRSVFVKSQYWRLITTFFYFGPLNLDLLFRVFFLQRYSRLIEEAAGTTPANFSWLLLYATSFLLVLSPLVSLPFLGSALSASLVYIWSRRNPEMRLHLLGLLAISAPYLPWVLIAFSLVMHGVIPKDEICGVIVGHIWYFFSDVYPSLHGGHRPLDPPAWWRRLFEGR
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Function: May be involved in the degradation of misfolded endoplasmic reticulum (ER) luminal proteins.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 224
Sequence Mass (Da): 25737
Location Topology: Multi-pass membrane protein
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A0A177DFK6
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MAANDYYGNSHPGQSNDRNDAPLPPVPGNHTQHSVSPVSSPFDDRPYPTHTASSGALGGYPIDTSYSNTSYQPPTQYSSTAHINDPYARQPDPFADQNAIPLQTQPKMDGSSPTRYNGDPEYYGMGVEPKRRKSKKKKGWFSGRVTWVVYLLTAVQVGVFVGELIKNGILTGSPIQTKPNFNIMIGPSPYVLINMGARFTPCMHNIKKVIEADGGPVLQWPCPNTTTLTDNKCTLAELCGMGGGVPNQEGITDFKDRSHEPNQWWRFITPIFLHAGIIHIGFNMLLQWTLGRDMEKEIGPLRFALVYFSAGIFGFVLGGNYAPDGITSVGASGSLFGVLALTMLDLLYNWSTRRSPVKDLLFLLLDMAIAFVIGLLPGLDNFSHIGGFLMGIVLGICIIHSPESLRARTGQSEPPYATVDTQPLAHEPVATESKSKITAFAKQPVGFFKGRKPLWWAWWLVRAGGLVAVFIGFILLLRNFYEWRNTCSWCKHLSCLPITTKGVSWCDMGSLNLTTTETPSKRSLNPASLAHFMGEATVGRIL
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EC: 3.4.21.-
Subcellular Location: Membrane
Sequence Length: 542
Sequence Mass (Da): 59546
Location Topology: Multi-pass membrane protein
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A0A0N8CSR2
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MNCNKRNVSFLGAFIAGASSGGCSTILFQPFDVVKTRLQENATVSTVHRKGMLQIFSHIVQKEGPKTLWSGLVPSLWRCVPGVALYFTSLEVIKSIILPKEKITLDPLQALVAGASARCIAGVVLMPFTVIKTRFESGQYRYRTVTEAFSSIYRLEGGRGLMTGLGATLARDIPFSAVYYAVYTQLKQYHPSGPTMGKSFSCGLAAGIIASVVTHPADVIKTSMQLFPSRYQHRTREAILSIYRRLGVRGFFSGLVPRLVRRTLVSALSWTVYDRVMQSFQMA
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Function: Mitochondrial glycine transporter that imports glycine into the mitochondrial matrix. Plays an important role in providing glycine for the first enzymatic step in heme biosynthesis, the condensation of glycine with succinyl-CoA to produce 5-aminolevulinate (ALA) in the miochondrial matrix.
Catalytic Activity: glycine(in) = glycine(out)
Subcellular Location: Membrane
Sequence Length: 283
Sequence Mass (Da): 31232
Location Topology: Multi-pass membrane protein
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A0A0P5F5Z4
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MDDVVSHSRKPVVCRYFAASGTCFYGNDCQFLHNSIPRSSISPTFPIHLFSSPSRSANSTTASISTELSLSIIESNGLDQSFEKNVNKSTFSNYAFSVKDECMHKAQELSISPDIQTAGESNSSLFEENVGGTTYYYTPEDDIKPNHEDLTIQNHGGQATDKIAHTAVLSRRIQSPNQLVSTSQQPNHLFSVYSGPSSFLLSCTGQQRSSFFMNEDIRADLIQRNSVALLTSDPALFPDLPSDVDHYHELVPLETHTLNQAVKSNTYGLITSTYKASNSKTGMRYCLKRIHGYRVTSAKCMSMVELWRKVQQCHLVTLREAFTTKAFGDHSIVFAYDYYPGAETLLTKYLASTAPHLDPFSSDPSAPRPYTMQKNRMLQQQAGKGVLPESLLWSYIIELCSALRSVHSAGLAVRALDPSKVLVTSRGRLRLCGGGIFDVLTYDSSSSNVSALIPHYQQEDLLALGKLILALACNSLLALQRDNVPTSMDIISKNYSSDLRNLVMYLLSTPQGSRAKNIQEVMPMIGARFFSQLEAATLHADYLEDQLARELDNGRLFRLLGKLGTVVDRPELNLDSTWSETGDRYLLKLFRDYMLHPCTDDGRPWVDLAHIVACLNRLDTASQDKICLTSRDQQNVLVVSYAELHQCLETSFNELQQAALAPSHVLGASSSNEQ
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Function: Regulatory subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in general and miRNA-mediated mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein (PABP). PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by XRN1. PAN3 acts as a positive regulator for PAN activity, recruiting the catalytic subunit PAN2 to mRNA via its interaction with RNA and PABP, and to miRNA targets via its interaction with GW182 family proteins.
Subcellular Location: Cytoplasm
Sequence Length: 674
Domain: Contains a pseudokinase domain. The protein kinase domain is predicted to be catalytically inactive because some of the residues important for catalytic activity are substituted and it lacks the equivalent of the binding site for a peptide substrate. However, it has retained an ATP-binding site and ATP-binding is required for mRNA degradation, stimulating the activity of the PAN2 nuclease in vitro. The nucleotide-binding site is juxtaposed to the RNase active site of PAN2 in the complex and may actually bind nucleosides of a poly(A) RNA rather than ATP, feeding the poly(A)-tail to the active site of the deadenylase and thus increasing the efficiency with which this distributive enzyme degrades oligo(A) RNAs.
Sequence Mass (Da): 74857
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A0A0P5QM13
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MPGGLPLSGCYVLNDVLNFRFLAHRLSFDKEGSVKKALKLIELYAEEGIDKERVLIKLASTWEGIQAAKELEEKHDVHCNLTLLFSFCQAVACAEAGVTLISPFVGRILDWYVSNTSTKSYAPEDDPGVKSVTQIYNYYKKFGYKTVVMGASFRNTGEVIALAGCDLLTISPKLLEELDASTVTVTRKLDAEQAKSCDLERLSLDEKAFRWMLNEDQMATDKLSDGIRKFAVDAVKLETFINERLNA
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Pathway: Carbohydrate degradation; pentose phosphate pathway; D-glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage): step 2/3.
Function: Catalyzes the rate-limiting step of the non-oxidative phase in the pentose phosphate pathway. Catalyzes the reversible conversion of sedheptulose-7-phosphate and D-glyceraldehyde 3-phosphate into erythrose-4-phosphate and beta-D-fructose 6-phosphate.
EC: 2.2.1.2
Catalytic Activity: D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = beta-D-fructose 6-phosphate + D-erythrose 4-phosphate
Sequence Length: 247
Sequence Mass (Da): 27564
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A0A314YK84
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MTAVAILGLCFIFVWSMFSSSSSSVTTRIESFDNIGAPPGSRHTRVNIPAAQSSIKGEDEKKFNGSATLSAHEHKSEKKEQKEVANVKKEKGGEGALIVSLDQASEDKLEDDGGESEERGKKRYKIKVMSKLAASICWNILAHKTDEVSDVGVKIYQKPDSNDIYELRRKKYPPLCKENDNPDAACTGQSGQRNGPRGLKGIPTG
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EC: 2.1.1.-
Subcellular Location: Membrane
Sequence Length: 205
Sequence Mass (Da): 22357
Location Topology: Single-pass type II membrane protein
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A0A7C4SPT4
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MYVVEVVITNKRIARDPEGETIYKDLISKHGYDKVRGVISGKYLEIMVDSESPDDALNYVRDLCRKLRLYNPSVHDVRVRLNAQGCSD
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Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 1/2.
Function: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
Catalytic Activity: ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate
EC: 6.3.5.3
Subcellular Location: Cytoplasm
Sequence Length: 88
Sequence Mass (Da): 10101
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A0A8J1U1V7
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SQLFHYSQFHYRAFSLVDASVLCFQRRRKRSSGTREYIPQYRSGPYALLITLYNDSREPGSRGFMTKRQLQTEAQPLADKSFTIPDPGVRYTAWSSMGTLIQKGYVIKESNPAKYSITDTGSELADKILRNAPDDVLRMQQPAADGAPP
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Function: Interacts with EME1 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, D-loops, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of stalled or collapsed replication fork intermediates. May be required in meiosis for the repair of meiosis-specific double strand breaks subsequent to single-end invasion (SEI).
EC: 3.1.22.-
Subcellular Location: Nucleus
Sequence Length: 149
Sequence Mass (Da): 16856
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A0A8J1XJI2
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MDDHTLPVTKNKMKNMSKHDKKLLKKQHRSIGTLLKHSATQPSTTPTKFLYVGNAGLGNGIQREQVFNLFSKYGQISDISTPVGKPYAFVSYTLVESAKDAMENLNGAVIACEESQAPNCSSGVNIYIAYVEPGSDVNSKNLKSELPEGLIILEEFVSEEEEQSLLAAIDWNDRTPDSAIGSLKHRKVKHYGYEFLYGINNVDLNCPLKDGIPSQCEQVLDRLIQGKYITSYPDQLTVNQYAPGQGIPPHIDTHSAFEDGLVSISLGCQVVMEFRHPSGNISPVLLPRRSAMVMTKESRYVWSHGITPRKFDIVPCSSNDPANSGLTLSKRETRTSLTFRKCLVGPCQCNYQAQCDSPRDTVNSLLDVKNEEADVLEEEHVHKVYEEIAGHFSATRHTPWPKVKSFVEDIAPGSILADIGCGNGKYLGINNSIGQFGCDRSSNLAGICLERGHQAFVCDALKVAMRDNSVDAAISIAVIHHFSTQARRVKAIEELARILQPKGRALVSVWAVEQKLHKKKSNYLKEIKQTNIQCEDSVNRQIDLKCGNQSQDKQMDDSQNDTDQVVKGQDDHNQGVKGQYDPNQGVQCQDGLTRGIMQQKNCINGENKDVSISTATGEKPYANVQSKSERTEKGESLSRIELKTHVNRTEFKSQDMFVPWHLKNKTREKKDNPVCSNEKVYHRYYHVFKQGELEELCRSVPSIAVKESYYDQGNWCVIFEKE
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Catalytic Activity: 5-(carboxymethyl)uridine(34) in tRNA + S-adenosyl-L-methionine = 5-(2-methoxy-2-oxoethyl)uridine(34) in tRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.229
Subcellular Location: Cytoplasm
Sequence Length: 722
Sequence Mass (Da): 80795
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T0BHB9
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MDKIFVLGAGAMAESFIKGVTQGDVADAKSIYVINRHRPDRLAELSETYGVTPAASMEAAKEAGVIILAVKPYDMRLALVELSPYLHGQLVISFAAGIPIAFMENVTQGRAQIIRTMPNVPVAVLEGAIAMATGASVNRESVDVAKRLLGKIGIVVELEEHLMDAATAFSGSGPGFVSYFLEAMEDAAVQLGFSAELARQLLIQTVVGTAKVLEEWRLSPAELRRLVTSPNGTTHAGLTVLGNLGMREAIAQALVQAEGRSREMGEQYTAVE
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Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-proline from L-glutamate 5-semialdehyde: step 1/1.
Function: Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline.
Catalytic Activity: L-proline + NAD(+) = 1-pyrroline-5-carboxylate + 2 H(+) + NADH
EC: 1.5.1.2
Subcellular Location: Cytoplasm
Sequence Length: 272
Sequence Mass (Da): 28953
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A0A1A7Q0S2
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MSETLSVNQIPILVDTPVGRVLYQIARKLALLGGFIFLILIAISLYSLVGRKLGFGGVVGDIELVQAGSAVAGSLFLPFCTIMYEHLKVDFFTMKLPKAIQNKMDALADLALFAVAILLVYRMIFQSMALYDFAEVTALMSIPVWVPNMLMIPGFILMALCSLYYCVVHATKKEV
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Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 175
Sequence Mass (Da): 19273
Location Topology: Multi-pass membrane protein
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A0A286ZNE1
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MENVTTVDEFLLLELTSNQELQPIIFMTLLVVYIIDLFGNGSILVVVTSEPRLYSPMYFFLGNLSCLDICYSSVTLPMLMANLFSTHKAISFLGCISQLHFFHFLGGTEALLLAVMGFDRFVAICYPLRYTVIMNLRVCILLAAVAWITSFFYALMHSVMTARLNFCHSLKLSYFFCDVKPLLELACGDIWLNRWLIFIVTGSLSMAACFLTLLSYFYIITFLLLKHRSCHMLHKALSTCASHFMVVSLFYGTVGLTYIPPASATSVSQARYVAVIHTTVTSVLNPLIYTLRNKEVKLALRRVFGRKWKLSV
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Function: Putative odorant or sperm cell receptor.
Subcellular Location: Cell membrane
Sequence Length: 312
Sequence Mass (Da): 35357
Location Topology: Multi-pass membrane protein
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A0A6I4Z2V9
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MPSSPPSPPPASTPTAVPRRSPSRSGSPCSTPSKWQRPMPEELVALAPAKVNLTLEVGGARTDGYHELASVLQTLALADEVTLRPASTPSMQVAGPFAAGTPEDAGNLAWRAVDALAGVLGREPEPFHIRIVKHIPPAGGLGGGASDAATVLRLLARRWPDAGEEALATAAAAVGSDEPFLLSGGTALVEGRGERVTPLPDLPEHGVVLFIPPDTLLNKTATLFAALDRDGQVDEPAVSRSLAGRLPVRVTGADLYNSFERVAFDCFPGLAELWERLEARTGEAVRLAGAGPTLFWIGPAESVDAVVGVAEGLGCTVIPTVTAGSLWRR
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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: 329
Sequence Mass (Da): 34152
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A0A6J2YTQ9
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MDPVRNKNRVSLKIKCPNPLFEKWLTEWRDKAVANDSKMQYTFNNALHCLRRYPLPLNSGRDCKILKGFGGKICKMLDDKLLKYSNEENYKTKNINMSNAVIDQPFKEYIPQFRSEGEKKNTKNISPQMSKSIDQSFREYIPQQGTGGYAILLAIYKESLKSDYPGFLRKADIILHGQQFVNSSFTKANPGSHYTAWSSMKTLISKKLILKISHPPKYSLSEEGTLLAKRLYEKGYFKCSKPKYLDDNLKEIEVDNAVQDNTSEVIQLSKLCDSRNPLKKDASKYKINKKNTNSYSGMQEFVLTSERFNIILYVDNNETSGKINDEAIIFLKKYNIKYEIKNLKVGDFLWVCRDYETENELVLPFIIERKRMDDFASSIKDKRYHEQKFRLKRSGIENLIYLVESYGKNQHLGLPLQTLYQAASYTALQEHFFIKFTGSLNESIEYLAYFTRTLIQIYKRKTLKSCGKDSLIDVDINQDVLYLMPFKQFNENAVKNKNMKVSEYFIKSLIQIKGMSVERALAITEKYSSPALLRKAYKSMTTMEGEKLLSSIKYDRGGKTIGIALSKTVYQIFNLRNY
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Function: Interacts with EME1 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, D-loops, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of stalled or collapsed replication fork intermediates. May be required in meiosis for the repair of meiosis-specific double strand breaks subsequent to single-end invasion (SEI).
EC: 3.1.22.-
Subcellular Location: Nucleus
Sequence Length: 578
Sequence Mass (Da): 67126
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A0A947T594
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MIRIFAILGVIALIVQQWFIWAYAPLAQSGVVQKIFYLHMPLAWWGLISFFVVFCASLGYLFKRTVVLDTLAAAAAELGVLFCGLALVSGSIWARAEWGHWWVWDPKLTTTLIMWYVYAGYLVLRSSPVAAERKGLVSAVLGVVAFLDVPLVFFATKLWGGVHPADTARKASGMTAKMWHTVFAGLVAMGIIWGIYLTIRWRQRRLAEWLDACMAGA
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Function: Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes.
Subcellular Location: Membrane
Sequence Length: 217
Sequence Mass (Da): 24215
Location Topology: Multi-pass membrane protein
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A0A8B8N6V6
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MASLSASISCRSSPLVSPQALLGEPEERRSVLSHLPRSPACRVGVLPSLRRRDLSKTIHASVTDVSVDIAMKEVQLPKGETWSVHKFGGTCVGNSQRIKNVANIVMKDDSERKLVVVSAMSKVTDMMYDLIDKAQSRDDTYVFALDNVLEKHRSTALDLLEGNDLATFLSQLDGDINNLKAMLRAIYIAGHATESFTDFVVGHGELWSAQLLSFVIKKNGVHCKWMDTREVLIVCPTNSDQVDPDFPESEQRLEKWYSQNPSKTIIATGFIASTPYNIPTTLKRDGSDFSAAIMGALLRARQVTIWTDVDGVYSADPRKVGEAVILKTLSYQEAWEMSYFGANVLHPRTIIPVMRYDIPIVIRNIFNLSATGTKICRPSVSEDDDSHKLESYVKGFATIDNLALVNVEGTGMAGVPGTASAIFGAVKDVGANVIMISQASSEHSVCFAVPEKEVEAVAEALQSRFRQALHAGRLSKVFPSFVIRVHLVC
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Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.
EC: 2.7.2.4
Catalytic Activity: ATP + L-aspartate = 4-phospho-L-aspartate + ADP
Sequence Length: 489
Sequence Mass (Da): 53661
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A0A0A1DTW2
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MKVLVTGGAGYLGSITAKALEQAGHTPVILDSLLSGPRAYVGDRIFYEGDVADRALLRRVVAEHPDLDATIHMAARIVVPESVALPYEYYRDNVTKSLEMFDELTALGKPRILFSSTASLYALTPQFEVTEDDPVDPTSPYARTKRMMEMVLEDLAKATDLRAIILRYFNPIGADPDLETGYHLRDATHVVPLMAQTALGIRPTFTLTGTDHPTRDGTGIRDYIHVWDLARAHVRAVEEFDKVLDTVAAPYTYINLGAGDGVTVRELLAAVERVVGKPVPVVEAPARPGDAAGAFANADKAAELLGWRTELSLDEAIASALAWGEKRKDVLGYA
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Pathway: Carbohydrate metabolism; galactose metabolism.
EC: 5.1.3.2
Catalytic Activity: UDP-alpha-D-glucose = UDP-alpha-D-galactose
Sequence Length: 334
Sequence Mass (Da): 36343
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A0A1U7F3W9
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MRLKTWGVYECANIAGVVYTLLLIFGIYFLILFYTCPATYQPDQCAQANCFGIVIILELLVNFLLFIIYSRRNDPQRWLQGVAVLTTVKGAGKYCLECNRIAPLRSHHCKLCNMCILRKDHHCFVTGACVGIANQRFFIVFVLWASIGAAVGSFYNLMYLLRYMDFNIYPFGWLKLLAPVAVLRWIISYEIFTNTAICVLFSICMAISVVALIFFGSQMFYTLNGYTMYDYHTLSRKIELHGDGETYSERLRMIFGHYWAVNFIVPLLCFPNQLTADVARNLFSSYSKDM
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Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 290
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 33376
Location Topology: Multi-pass membrane protein
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A0A8G1G9E8
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RMNNASFWLLIPSLMILIFSMFVSEGSGTGWTLYPPLSSFSGHSGFSVDMTIFSLHIAGVSSIMASMNFISTIINMKLFKVEFISLFSWSLLLTSILLLLSLPVLAGAITMLLFDRNLNTSFFDPVGGGDPVLYQHL
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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: 137
Sequence Mass (Da): 15077
Location Topology: Multi-pass membrane protein
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A0A0N4VS76
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MLTRCLPLVQGQTVMYASCAALSTSKPAGKRMKTFEIYRWNPEKKGSKPEMQKYEVDLDDCGSMVLDALLKIKSEQDPTFTFRRSCREGICGSCAMNIAGENNLACTLKIDTDLSKTTKIYPLPHMYVIKDLVPDLSLFFEQYRSIQPWLQKNEKLTLGEKQMFQSANERARIDGLYECILCACCSSSCPSYWWNADKYLGPAVLMQAYRWIVDSRDDYARDRLARIHDAYSAFKCHTIMNCTKTCPKHLNPARAIGEIKSLLTGMKSKPAPEPAKMLARTFLTTRSHALMYASCAALSTSKPGEARMKTFEIYRYDPERKSKPQMKRYTIDLDTCGHMILDALIKIKDEHDSGLTFRRSCREGICGSCGMSIGGENTLACICRIDSDTSKVTKIYPLPHMYVIRDLVVDMNLFYEQYTSISPWIHKKKDLTLGQKQFFQTIKERAKVDGLYECILCLCCSTSCPSYWWNADRYLGPAVLMQAYRWIIDSRDDYAYERLHRMHDVYSMYKCHTIMNCTKTCPKKLNPAKAIGELKALLTGYKMKPAPEPTPANFYK
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Cofactor: Binds 1 [2Fe-2S] cluster.
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; fumarate from succinate (eukaryal route): step 1/1.
Function: Iron-sulfur protein (IP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
EC: 1.3.5.1
Subcellular Location: Mitochondrion inner membrane
Catalytic Activity: a quinone + succinate = a quinol + fumarate
Sequence Length: 556
Sequence Mass (Da): 63628
Location Topology: Peripheral membrane protein
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A0A095H8J3
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MNRRNFVTAALASAASTAIPAWAASNGIKAVGFDGLALFDPRPIFAMVEQFLPGRGAAFVATWRARQFDYTWLRTMMGSYVDFVQISADALQFTEEAEKASLAPEQRQQLLAGFLNLKVWPDVVPALKQLKAHGIGLAPLTDFSLPMLEAGVRNNPELRGVFDHLLSTDLVKAYKPDPRSYQMGIDAFGLPREQIAFVAFAGWDAAGAKTFGFPTLWANRLKAPTEQLGVMPNQIGADFKPLPAFVGL
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Function: Catalyzes the hydrolytic dehalogenation of small (S)-2-haloalkanoic acids to yield the corresponding (R)-2-hydroxyalkanoic acids.
EC: 3.8.1.2
Catalytic Activity: an (S)-2-haloacid + H2O = a (2R)-2-hydroxycarboxylate + a halide anion + H(+)
Sequence Length: 248
Sequence Mass (Da): 27074
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A0A7V8VRF0
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MRLTNFPTGPESVPPALPAPSLPPLHSFDQSGSRAAGDLALRDIVAALRRRYRLVLAVAVFTTAAAAFLALNEAPTFTASAVIQVSETRRVLATGIELPTATDDRLTSPFLSQIALLRSRTLAGTVVDSAGLRLVPDFEGFRPSFLREARVSADAVSDTLRLRFDPDGVTGLFNGDASRARYGVPLELPGVILVISERPETQTSLWQVIPREAAIDDLLGKLYVKPRTQTNVVEIAYSARRPSVAQRVVNRVATLYQSMSAHSAQDQSRRRREFLEARIAQTDSDLMRAQSALTEFRRQVRVYGASNKLQSEQHDLAQLDARIDELAAQRQMYGSLLGALQAGQTDRRQDGLRTLMASPGIRDNLAVAQLHGRLTKLQATYDSLSTGPWRRAETDPDVVRLRSLIAGVDSQLVSTVQGELVWIETTLQTLGGTRARSVRSLDSLSGLEPEEMRLAQQIDALRNTGDKLRDDYQNARMAEAVEVGPVEIIDLADLPYAPDARLRMLKLFLGAVLGLGLGGALAVLFETRDTSIRNTEGLERVLQMPGLATIPRQAVSSPSSSGLAREAYRVLRTNLLFSRTGQLPGSLVITSATSGEGKSTTAANLAITCAESGMRVLLIDCDLRRAKQHHVFGVPRSPGVAQLLLGTAKAEEALRPSPVPGLTLLTAGSEEADVIEVMRSARMLSMIRTLREQFDLLIIDSPPVLAGADASILSALADGVLLVLRAGCTNHREALAAVQQLNAVGAHMLGAVLNDAPVESYPYLSAYDAYHTQAPEPV
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Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Subcellular Location: Cell inner membrane
Sequence Length: 778
Sequence Mass (Da): 84122
Location Topology: Multi-pass membrane protein
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A0A098GGX0
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MSVLELIRPDLQSMQSYKPGGDTLDCRLHANELPWCPVSFAQVPLNHYPDIRQQQQLQQLLANYYQININQLVLTRGSDDGIDMLMRLFLRAGQDSFMQCPPTFPMYEFYGRLQQADALNCPLEANNDFSFSIEKLISLWQPNCRLIMLCRPNNPTGNLLELTSIETLCNYFKNKAVVVVDEAYIEFAQTTSATSLIPSFDNLIVLRTLSKAYGLAGLRLGSIIAQPQLIKAIENTMPPYTLSSAVLDLAQRALIDKSWFTNKIKDILNERQRLITQLQQLTLIDKIYPSRANFILIASSYAAQLAAWMAELDIAVRHFAAGPLQNMLRVTVGEQAQNQRLLNALRRFQQEKC
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Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Length: 353
Sequence Mass (Da): 40107
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A0A948NFA6
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MSIISKILEAKQAEVDEMEEIANIPSCKRRNFVESLLSQKPSFIAEIKPKSPSEGEILAPEAIPEIVKTYDQFASAISVLCDKQFFGGGYDLLSEVAAQTDKPLLAKEFIISEKQIARAVTSGASAILLIAAIVEEDVLTRFIHEAIKLDLSVLLELHTMDDIEKAASAMKGLSAEENLRVVLGINNRDLDTLNISLDTTTKLVPKIKEKIGDNNLLISESGISSPEDVRALSQFVDGFLVGTSILKSSDPGVFFSSLKTACDQK
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Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
EC: 4.1.1.48
Catalytic Activity: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
Sequence Length: 265
Sequence Mass (Da): 28798
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A0A2V5U7C6
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MSIVTKTGDKGETSLMYGRRVSKADPRVDAYGCIDELTAALGLARSFSTDKFLSDEISAAQKDLVVVMGELATTPGDRERYVNDGFHVTTAGMVDRITAVILELEKDKSLYPKHWVIPGGTTLSAALDFARTTCRRAERHIATFGAGEKNFNPEILRYLNRLSDLCWILARYAEKQSRTSS
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Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 2/7.
EC: 2.5.1.17
Catalytic Activity: 2 ATP + 2 cob(II)alamin + reduced [electron-transfer flavoprotein] = 2 adenosylcob(III)alamin + 3 H(+) + oxidized [electron-transfer flavoprotein] + 2 triphosphate
Sequence Length: 181
Sequence Mass (Da): 20041
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A0A6L8BBE1
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MTTAFNKVGLFWGRKNKQGSVSLAQEIAVLLGSRGLDVFVPGHRKLPETFGTCQRVPARKLAAHVDLIIAIGGDGTMLDASRGAALHGVPLLGVNRGRLGFLNDISPENLSTAIETLLQGDYVAESRQMLEARIFGGSTDRGPLLALNDVVLKTVDTGHMEDFITTVDGDYVNTHGGDGLIVATATGSTAYALSCGGPIIQPDVDALVIVPIAPHTLSDRPLVVKSSSTIRVTADLRPGSGGAQVTCDGDTLGTVGTDEVVEIRAATETVQLLHPRGQNFYQQLRSKLYWGHTNRPPRRKIDID
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Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
EC: 2.7.1.23
Subcellular Location: Cytoplasm
Sequence Length: 304
Sequence Mass (Da): 32368
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A0A4X1USY1
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MGLYYATGRGTDIRTAQHIFAVLYLATLLLVFLIYHQTCKVPPFVFFFMCCASYRVHSIFVLRLFNDPVAMALLFLSINLLLAQRWGWGCCCFRSTPLPSGPSLTFCVSITFSPDFCSRGPKGVVPQCGSVRAALGESRIYKKYPPPQAPNTHIFLPSSIPSRQHLLLGLVIAYSKYSTYICSLRLSVETRYRLPPSSLLPGCAECELPWSFLAGEGRRCYGDRGVVHFGAGYMALELTSTLPLPYPLQPGGVCEDERATLCPWVTVPSPHTIRPPWGPPQAGHLCCPSVINMRLRVSLGSSADITPSSGGAGATLPAGEPHRLPVPLV
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Pathway: Protein modification; protein glycosylation.
Function: Adds the first Dol-P-Man derived mannose in an alpha-1,3 linkage to Man(5)GlcNAc(2)-PP-Dol.
Catalytic Activity: a dolichyl beta-D-mannosyl phosphate + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol = a dolichyl phosphate + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + H(+)
EC: 2.4.1.258
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 329
Sequence Mass (Da): 35950
Location Topology: Multi-pass membrane protein
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A0A7C8PPJ2
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MSATPIRLWSLTVPATGEIVALEELGIPLNVSITMAAIDPTEEVKGDGPKLSTLKLLHQNMSEPDVEDFDDDESIDSDLASGEDDSEEDSEEEEEEEKPKGKGKGKGKVADKKDDKKADKKADKKAEEDDEGDEDDDDLLLEGSDDEDDDYEEVVVCTLDSTKTYQQPLQLTVGDGEPVFFKVTGSYTVYLTGNYVTEPRQLPPSYGGDDSEDEDDLYSDDEDEFDMDAEDELQQVLAQLKSGAYDDVDADSDEESDDLDDLEDPRITEIDDDEEAPELVKSKKPEEALTNKEKKAAAKAAQLKAKAAETAAKALSAKKRSADEMDIDVPPSSETLSSGSAAPAAATEAPQSSLSKKQQKKLKANSGEPVSVSTPTEKKKVQFASQLEQGPTPNGNKSPATPVEKKKAEKTKDEKPTAQSSKSRTVDGVKIEDHKLGSGPEAKKGQKVSMRYIGKLTDGKVFDSNKKGKPFTFNLGKGDVIKGWDIGVAGMKVGGERKLVIPANLAYGNKALPGIPKNSTLVFEVKLLEIK
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Function: PPIase that acts as a histone chaperone. Histone proline isomerase that increases the rate of cis-trans isomerization at prolines on the histone H3 N-terminal tail. Proline isomerization influences H3 methylation thereby regulating gene expression.
EC: 5.2.1.8
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Length: 531
Sequence Mass (Da): 57430
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T0CSV5
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MLIIGIAGGTGSGKTSVARAILEQLGAQSVALISQDAYYQDHSDLPFERRQQLNYDHPDSFDNDLLREHVTTLRQGGSIEMPIYDFKTHNRSAQTIHVPARPVIILEGIHVLVDPELRALLDIKVFVDTDPDVRVLRRIRRDIEERGRSIESVYDQYLSTVKPMHDAFIEPSKRFADLIIPEGGQNQIAIALLTTRVSQFLSENN
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Pathway: Pyrimidine metabolism; CTP biosynthesis via salvage pathway; CTP from cytidine: step 1/3.
Catalytic Activity: ATP + cytidine = ADP + CMP + H(+)
EC: 2.7.1.48
Subcellular Location: Cytoplasm
Sequence Length: 205
Sequence Mass (Da): 23129
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A0A011T834
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MSQTAPENRGSAVAIRTVVSLVVVALGVWALFHVNPADAYLWIKSLHVIAVIAWMAGMLYLPRLFVYHCAAKPGSETSETFKVMEKRLLRFIINPAMIVTWIAGLWMAWEIFGFQGGWLHAKLLLVVLMSGLHGYLAKSTRLFAEDRNMRSAKHWRIINEVPTILMILIVILVIVKPF
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Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1.
Function: Catalyzes the oxidation of protoporphyrinogen IX to protoporphyrin IX.
EC: 1.3.99.-
Subcellular Location: Cell membrane
Catalytic Activity: 3 A + protoporphyrinogen IX = 3 AH2 + protoporphyrin IX
Sequence Length: 178
Sequence Mass (Da): 20112
Location Topology: Multi-pass membrane protein
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A0A1J0CQ36
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LSQPGGLLGDDKIYNVIVTAHAFVMIFFMVMPIMIGGFWNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSAVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGISSILGAINFITTILNMKPPAVSQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLN
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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: Membrane
Sequence Length: 176
Sequence Mass (Da): 18820
Location Topology: Multi-pass membrane protein
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A0A2R6WFN5
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MFPPNDPREAGGAGAQSERPMMMPTMNRERPYPLGMSRVESDRRRQRSLSKAADFSTTHVQDDDLTKEREEDRDPRRQSWLTRNESGPKERKDNQVEEERASSADEHRPNDAFMIRTSEPVRAPPFSSAEGMGLIVLPSEPDSSRPRSLEQQQLNRPSQEVPSATTMTSTPPDSPLVLFDSSTGPTSDILLSRDPFPADDFSAASSSDTFTQSSPEALSPQWSVKDGRAADADDDDDSSSSASDASAASTLRARYRRRSSLAVGPQDESDLLREWRRKKREELEDKPRKSEERRRQTLEIAKKEMNAFYATRSAELQARKKINREKEIEDKAEHNIGKDSKMPLNLWEVVVSLLPPAPTAERLKSSGNRTPSTTAATPQNILTPSTFFSQHLSAIPPATPPKQGSVNAKHGKDVNKKDSSSTNAGEEVEVVPPVKTTDISRMRQILMKLKSKPPNIFNKASDFL
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Function: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.
Subcellular Location: Cytoplasmic vesicle membrane
Sequence Length: 464
Sequence Mass (Da): 51710
Location Topology: Peripheral membrane protein
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A0A0R3X1A8
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MDPFDLVSEDVPSISFERNQLEILANPCAFYNAVRDGVKTARRRIVLATLYLGTGELEQRLVEAIATNKNNPQVTLLADATRSMRTIRATAEFVDTQQRRMNGRTFMTTQSSPLFLLRRIAQLPSSQVALYRNHRLHGWMHWVVPERLNELLGLQHMKVYVFDDDIIISGANLSEEYFKTRQDRAWLFRGVPALADFYSNLIDIIVSLSYRVTAKGELKAISKETNLELAEGKTYCSLFRSRIKAFLTEARAKYAATNAPTVYGTAVFPLVQMGAYGIHQEILLVKRLLHFLPACDLAFTTGYFCPTHELEVAMAAIAQLSEHQGSQVNILCAAPQASSFFNSKGLSGVVPAAYREMLISFLQRTSQLPNIHVQEYFRPGWTFHAKGLWVNTHGIDATTLASIGSSNYGYRSRDLDLESQIVVVTRDMELRRRIEAERRWLWDARYLRPVTLEGLLLPTEPRFKWFARWTLPFLRRIM
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Pathway: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
Function: Functions in the biosynthesis of the anionic phospholipids phosphatidylglycerol and cardiolipin.
Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + sn-glycerol 3-phosphate = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + CMP + H(+)
EC: 2.7.8.5
Subcellular Location: Mitochondrion
Sequence Length: 478
Sequence Mass (Da): 54592
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A0A966X6X5
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MTSGSARRPDRSGAVPRGAEPGFARGMEMRERIPAHLRDIEATLGEATTGTVLRATSGYFDVMPHDHDVAPAPMYRCRVRDRMRKNFVFSESHAHAQRVDDVQRREVVEPVVAGDRVRFRPSHVSGVQVPAGVIDEVLPRTRALTRQAVTDGKIPVGQTLVANLDQIVVVASAAHPLPRWGFVDRLLASCAASGFEARVCLNKVDFGIDADMVTELGWYARAGYGVHLTSATTMEGIDELRDAVAGRTTAFTGPSGVGKSTLLNAIEPGLALKVGEISRSTNKGKHTTRFAQLFPLENGGFLADTPGLRQLALWDVSDSDIDQLFPEFAAFIGKCRYGNCSHVTDDGCAIRAAVELGDLSQRRYFSYVKLFTDG
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Cofactor: Binds 1 zinc ion per subunit.
Function: One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase that catalyzes slow GTP hydrolysis, GTPase activity is stimulated by the 30S ribosomal subunit.
EC: 3.6.1.-
Subcellular Location: Cytoplasm
Sequence Length: 374
Sequence Mass (Da): 40655
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T0BXN6
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MNIVVVGSMNMDVVNRVSHHPLPGETIKGKGTSYIPGGKGANQAVAAARAGASVQMVGAVGTDGFGKELIASIARDGIDTSKILEKEGTSGLAFITVNDEGENNIILSEGANGKVTPDDVRTALGNANFDALLVQNEILLESSYEAIRVAHEKSAKVFYNPAPAHAVPKDILQLVDILVVNETEASVVLGKPLSTHTDYADAAKQLVTLGAKAVILTLGSSGSLYADNALTVHVPAFRVQAVDTTAAGDTFIGAFASVFSGENPMESLRFASAASAIAVTRSGAQTSIPEHGEIVEFLQSSVETLPHFERWESSHVDHD
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Cofactor: Requires a divalent cation, most likely magnesium in vivo, as an electrophilic catalyst to aid phosphoryl group transfer. It is the chelate of the metal and the nucleotide that is the actual substrate.
Pathway: Carbohydrate metabolism; D-ribose degradation; D-ribose 5-phosphate from beta-D-ribopyranose: step 2/2.
Function: Catalyzes the phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium. The resulting D-ribose-5-phosphate can then be used either for sythesis of nucleotides, histidine, and tryptophan, or as a component of the pentose phosphate pathway.
EC: 2.7.1.15
Subcellular Location: Cytoplasm
Catalytic Activity: ATP + D-ribose = ADP + D-ribose 5-phosphate + H(+)
Sequence Length: 319
Sequence Mass (Da): 33330
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A0A095FAY9
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MARAPKITLRSKAEIAQSRVAGKLAAEVLQMIGEHVKPGVTTDELDTLCREYIVNVQKATPANIGYHGFPKTICASVNHVVCHGIPSAHVLEDGDIINIDVAVIKDGWFGDTSRMYYVGEPAPAARHLVDTTYEAMRAGILAVRPGATLGDVGHAIQSVAHAAGYSVVREYCGHGIGTVYHDEPQVLHYGRPGIGLKLVPGMIFTIEPMLNAGKAETKQLSDGWTVVTRDRSLSAQWEHMVVVTEHGFEVLTPWPEGTGSYASIGAAQGSESASAA
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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: 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). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed.
EC: 3.4.11.18
Catalytic Activity: Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
Sequence Length: 276
Sequence Mass (Da): 29463
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V9KQM8
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MAISRGVWCCQRVLAWVPVLIITLVVLWSYYAYVFELCVFTISNPAEKGAYLVMFHICFVLFLWTYWKAIFTEPLQPSRKFQLPRTDREQYEREERPEIQKQILLDVARQLPVYTRTSAGAIRYCDRCQVIKPDRCHHCSICDMCVLKMDHHCPWVNNCIGFSNYKFFLLFLGYSIVYCLFVAATVMQYFIKFWTGGLPDGRAKFHVLFLLFVAVMFFLSLLFLLSYHCWLVSLNRSTLEAFSAPVFHYGPDKNGFNLGRGKNLKQVFGQEKTQWFLPTFTSQGDGHFFPMRSMNESRNPLLANEEHSDESESDGENLGQSVSSSVTVDMEN
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Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 332
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 38587
Location Topology: Multi-pass membrane protein
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A0A7C8P4Y3
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MLSRALIRAPLRAGNPAARQILLRRNYASQAGSTFTKEREAVKAHAAQSSELWRKLSLYVAIPALILSSINAYNLWNEHWEHESHLPPQEERPQYPYLNIRVKRFPWGDGDKTLFWNDNVNYKKADE
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Pathway: Energy metabolism; oxidative phosphorylation.
Subcellular Location: Membrane
Sequence Length: 127
Sequence Mass (Da): 14773
Location Topology: Single-pass membrane protein
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A0A6B1I8Y3
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MERPRGVGGGSRTIRAFFASLRPVSAGSFSVGARPRRVRRPSRSASLFGKPARKNRRGPSRLGDRSSSRGSRAQCQSAIGADRPVAWLVPRGNSTDALTRSQLGEGATLVNAHRPRLHFAQHFLVARGVIEAIAGLVRPAAGEVVVEIGPGRGALTEVLLATVDRLVAVEIDRDLVALLRARQDARRLRLIEGDILQVDLGKVLRDAGGCRLLIVGNLPYNITAPLIFHLLAHADCISRAIVMVQREVARRLVASPGSKDYSLLSVLVAMRAEVEMRLQVERDCFRPVPAVDSSVVEFRFAPKPRYAVQDADCFDRLVRRAFGQRRKMLRNSLLGLNPEGGRPWLETLGQQAGIELTRRPEELSLAEFIRLSDAYWHLGKDRP
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Function: Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
Catalytic Activity: adenosine(1518)/adenosine(1519) in 16S rRNA + 4 S-adenosyl-L-methionine = 4 H(+) + N(6)-dimethyladenosine(1518)/N(6)-dimethyladenosine(1519) in 16S rRNA + 4 S-adenosyl-L-homocysteine
EC: 2.1.1.182
Subcellular Location: Cytoplasm
Sequence Length: 383
Sequence Mass (Da): 42195
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A0A250XW87
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MAALVEPLGLERDVSRAVELLERLQRSGELPPQKLQALQRVLQSRFCSAIREVYEQLYDTLDISGSAEIRAHATAKATVAAFTASEGHAHPRVVELPKTDEGLGFNIMGGKEQNSPIYISRVIPGGVADRHGGLKRGDQLLSVNGVSVEGEQHEKAVELLKAAQGSVKLVVRYTPRVLEEMEARFEKMRSARRRQQHQSYTSLESRG
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Function: Plays a role in establishing and maintaining the asymmetric distribution of channels and receptors at the plasma membrane of polarized cells.
Subcellular Location: Basolateral cell membrane
Sequence Length: 207
Sequence Mass (Da): 22896
Location Topology: Peripheral membrane protein
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T0CAN0
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MQVREIVRRFLQQHVDAQNTLILGVSGGLDSMAMLHVMQALSGERPPLFRSLLVVHVHHGLRELADRDADFVRSYCQTQGIACKEVRVTVDAQSKEGIEAAARTARYAALTEVARAYPHPVIALAHHQGDQVETVLLRWLRGAGLHGLSGMRAVSQRAGVLLIRPLLVMSKEALAAYAHQHGVPHVEDETNADDRFTRNFLRRHVVPQLARLQPEIGAVTARLTETLQDDDDYLRAEAQKLRESVVDEPTAGLFRIRRKALIAAHVSLQRRLIQILLNCFALTGWSSRHIEAVRHLAETDGGESSVQLPHGVEAWRSYENLYIGHAKPRTGQDEASMVVWNPAQMHRLTVDGSTVRWRFFAVRMRRRDVLRHHFTGLWRIYVPVGVQLEIRLGVSTAVRVRPLGLNGSKKLQDIYTDKKIPRTFRSQWPIVAVAGQVVWLPGLVRTEVETVEGTDDGDVFVIVAHMNRAAREEIGTFLRETRRMISE
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Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
EC: 6.3.4.19
Subcellular Location: Cytoplasm
Sequence Length: 487
Domain: The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Sequence Mass (Da): 54919
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A0A1N6M2W8
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MDHRDLGLKHSIFQHIGEYSIEALFRVSKDYGKKYGVIGVEKGELIEREVSRLQLETDERPVIGDWVICQELQGDDVITELLPRETQLARTRSSGTQQAIAANISHIFITTSMNAEFNLNRLERYLVLAKASGVQPTVVLTKRDLVDDPSEYVNQIAQLDPSLLALPVSTQTGEGLDELLSLIQKTDTCVLIGSSGVGKSSLINFLLGEEVLETLDISDEGARGSHTTSNRFLFMLPTGGLIIDSPGLRQVGIGASTKNVEETFSDVEALADDCRYRNCTHEKEEGCAIQAALADGSLSPRRYKSYLKLMTESRYADNPEAFQRERHRQWRQVTKNRKEKEKVLGRYKEF
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Cofactor: Binds 1 zinc ion per subunit.
Function: One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase that catalyzes slow GTP hydrolysis, GTPase activity is stimulated by the 30S ribosomal subunit.
EC: 3.6.1.-
Subcellular Location: Cytoplasm
Sequence Length: 350
Sequence Mass (Da): 39223
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A0A2V7RJT9
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MLQSQRVALTATAAAATDKLGDILVREGLITLEQLKKALQEQKSSGMRLGYTLVKLGFVEETEVTKCLARQYRMPAVDLTRFEVDPKILKLLPPDIATKHTVLPLKREGRTLTVAIADPNNVAAIEDIKFITRCDVFPVIAGEYTLRNAIDRYYQQSDAQLQTLLKSVEAAEEDLEVVEEQQDEDVKAQDLADDAPVVKLINGLLTDAVKRGASDIHIEPFEHEMRVRYRVDGVLQEVMKPPIKMRAALTSRVKIMAQLNIAERRVPQDGRIKLKFGSKVIDFRVSTLPVLFGEKIVLRILDKGNLTLDLAKFGFEPKSEADLLKAILNPYGMVLVTGPTGSGKTTTLYSALSRINTIEVNILTAEDPVEYNLMGINQVLVRNEVGMTFAAALKAFLRQDPNIIMVGEIRDLETGSIAIKAALTGHLVLSTLHTNDAPSTVTRMVDMGIEPFNVASAVNLIVAQRLVRRICSSCKQQHEYSDEELHAFGIHRSDGPFFKGQGCDTCNGTGYKGRQGLYEVMSMSSALRRLVLKGASTEELRDEGVKEGMLTLRMDGMVKIKKGVTTLEEVVKETAA
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Catalytic Activity: ATP + H2O + cellular proteinSide 1 = ADP + phosphate + cellular proteinSide 2.
EC: 7.4.2.8
Subcellular Location: Cytoplasm
Sequence Length: 576
Sequence Mass (Da): 63650
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A0A8D1R1D6
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MGENAEIEYSITEGEGLDMFDVITDQETQEGIITVKKILDFEKKKVYTLKVEASNPHVEPRFLYLGPFKDSATVRIMVEDVDEPPVFSKLAYILQIREDAQINTTIGSVTAQDPDAARNPVKYSVDRHTDMDRIFNIDSGNGSIFTSKLLDRETLLWHNITVIATEIMTVVLFAALRRQRKKEPLIISKEDIRDNIVSYNDEGGGEEDTQAFDIGTLRNPEAIEDSKLRRDIVPEALFLPRRTPAARDNTDVRDFINQRLKENDTDPTAPPYDSLATYAYEGTGSVAESLSSLESATTDGDQDYDYLSDWGPRFKKLADMYGGVDSDKDS
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Function: Cadherins are calcium-dependent cell adhesion proteins.
Subcellular Location: Cell membrane
Sequence Length: 330
Sequence Mass (Da): 37153
Location Topology: Single-pass type I membrane protein
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A0A833Q7L5
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MDYDYDLFVIGAGSGGVRLARISASLGARVGIAEVEQIGGTCVLRGCIPKKLLVYASHFPDDVEDAAGYGWRFGEGEFSWPTLIAAKDREINRLSAIYIKLLNDAGVSMHEGRATIVDAHTVEVGGKRYSTRHIGVATGSWPTLPEIPGIEHAITSREALDLPELPRRVAVVGGGYIAVEFAGIFNGLRSKVDLYYRGEEILRHFDDDLRRVLHEEISKHGVAIHTQAQVRAITRNADGSLTLDVDGTPQGPYDAVLYATGRHPNTAGLGLENAGVELEKGGAVRVDAYSATNVPSIHAIGDVTSRPQLTPVATRDGALLAANLFGGQRVEADHRAIPSAVFSQPELATVGLSEAEARAEYGALDIYKTSFRALKHTLTGRDEKIFMKLVVVRDTQRVVGAHMIGRDAAETIQGIAIAVRMGATKAQFDATIGIHPSAAEEFVTLRTRSPDPA
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Cofactor: Binds 1 FAD per subunit.
Function: Maintains high levels of reduced glutathione.
EC: 1.8.1.7
Catalytic Activity: 2 glutathione + NADP(+) = glutathione disulfide + H(+) + NADPH
Sequence Length: 453
Sequence Mass (Da): 48647
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A0A4X1WAJ6
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MHAALAGPLLAALLATARARPQPPDGGQCRPPGSQRDLNSFLWTIRRDPPAYLFGTIHVPYTRVWDFIPDNSKAAFQASARVYFELDLTDPYTISALASCQLLPHGENLQDVLPRELYWRLKRHLDYVKLMMPSWMTPAQRGKGLYADYLFNAIAGNWERKRPVWVMLMVNSLTETDVRSRGVPVLDLYLAQQAEKMKKSTGAVERVEEQCHPLNGLNFSQVLFALNQTLLQHESVRAGSLQAPYTTEDLIKHYNCGDLNAVIFNHDTSQLPNFINTTLPPHEQVTAQEIDSYFRQELIYKRNERMGKRVMTLLQENEDKSCFFAFGAGHFLGNNTVIDVLRQAGLEVEHTPAGQTIHSPVAQSSASPPARTSASPTAATPAAAVPPAPSPTPTAAPEEEDPALSPHLLLPDSLSQLEEFGRQKKWHKRQNKHQRPRQFNDLWVRIEDSTTASPPPLPFQTTQSSGTAKPPVQLSDLLQQQEEPGRASNSAPSSQPALGLLPTVAASIAAPFLLHTLGPS
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Cofactor: Divalent metal cations. Mn(2+) or Co(2+).
Function: Metalloprotease that acts as a negative regulator of the Wnt signaling pathway by mediating the cleavage of the N-terminal residues of a subset of Wnt proteins. Following cleavage, Wnt proteins become oxidized and form large disulfide-bond oligomers, leading to their inactivation.
EC: 3.4.-.-
Subcellular Location: Cell membrane
Sequence Length: 520
Sequence Mass (Da): 57625
Location Topology: Single-pass type I membrane protein
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I1U702
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THTRTLLTIRGLQTFIPLMTTWWLIASLSNLGLPPSINLFGELMIISSMFYWAKTTITLTGLTTLITATYTLYIFLTTQRNKTPKHLITTPSHTREHLLMALHSMPLGLLITHPNLLF
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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.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.2
Subcellular Location: Membrane
Sequence Length: 118
Sequence Mass (Da): 13406
Location Topology: Multi-pass membrane protein
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A0A2Z6SAF3
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MFKRKTSCIYQGRIIPPNIWRDVLSKQQNTQNFTSAAENLESENSVNEQNQQNHTPPPTPPNPPNSIPADILQASLPFVNEYGWTIDALSQGAKKLGYPYISHGLFPRGGAELIDYFLEDSRKKMTHEILDKMDGLKVHQKIRFACVTRLNLTKPYIRKWPEALAIMAQPNNVPMSIEHLAKLVDDMWHLAGDKSADMNWYSKRAILAAIYTSTELYMTQDTSPDFTGTFQFLNRRLQDSATFGSLINEINTFVDFAAKSTFGILSSKGIGRF
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Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: Lipid-binding protein involved in the biosynthesis of coenzyme Q, also named ubiquinone, an essential lipid-soluble electron transporter for aerobic cellular respiration.
Subcellular Location: Mitochondrion
Sequence Length: 273
Sequence Mass (Da): 30922
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A0A7C4KXA3
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MVDKLIISLTVDEGKVVRVSGPASIEVLSGEVLVAGAVFQSSSKLVISRYRSYGVKALKRSELKVILGDGGSLDEPQQGEEVIDLWVRLCEELVNLRTDLRVIIIGPPEAGKTSLAAFIANQLLQRGREVCIVDADIGQEDIAIPCTIGVAKPKDKFIWLRELQPLMMKFVGCNSPQYCLAQFITAFQEVINDVCRPGVDLIVNTDGWVSSYSALELKQLMIRMLRPTHVLVLDDELFNYFRNSFKGYGFEVLLIPKPRFVRERSREDRRYLRHHSYLKLFSNVRRVELDINKLVLINSLVLTGKELSIDELSNYVKIPDNLRNGVIYASVLTNTVNIVLRKGLRLSNEEVVCSGGLELNIVNEGDEKGLLVGVLDRNLRTVSVGVVERVDYLNKRIYILTPWGDEVLGLIIGRVRLNEKYEEVGRVVKCIL
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Function: Polynucleotide kinase that can phosphorylate the 5'-hydroxyl groups of both single-stranded RNA (ssRNA) and single-stranded DNA (ssDNA). Exhibits a strong preference for ssRNA.
EC: 2.7.1.78
Catalytic Activity: a 5'-end dephospho-2'-deoxyribonucleoside-DNA + ATP = a 5'-end 5'-monophospho-2'-deoxyribonucleoside-DNA + ADP + H(+)
Sequence Length: 432
Sequence Mass (Da): 48597
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A0A6G1M8Z9
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MPRSRDMHMDDEDDDNAFTDTRKVTQEKEDVDAKFPNRPRNEKPSPPFSILYRELFNPLMQNLKNPTKTRGKRSTQKAPQEKRREIITRFIARWRRDVGNDIWPAFRLIMPDKDRERSVYGLKEKALGTVLIKVLRISRDSDDAYNLLHWKQPRIGGDSKATGAGDFPSRCETAISKRALRTDPGDLTIDDVNELLNRLAEDSKNHTPVIQEFYNRMNAEELTWLIKIILKQMKVGATEKTFLDCWHQDADELYNVSSSLKLVCWDLWDPEFRLDSTDKGVKLGQTFQPQLAQFQLRSFEDVVKKMQPTEDDKVFWIEEKLDGERMQLHLHDDGTFKFYSRKAKEYTDHYGSSVDDENGTLTRYLKKAFKPGVRNIILDGEMVTWDPIEDAMVAFGTLKSAVIAQRTDDPSAHRPFFRVFDILYLNDTSLIKYTLRDRRNALISAVEPVHRRLEVHTYTEGTTVEDIKVKLREVVAEASEGLVIKNPRSMYCLGDRNDDWLKVKPDYVKDLGENFDLLVIGGYYGQGSRGGRLSSFMCGLRAPNGKYYSFTKVGGGFSAQDYNWIRHQTEGKWNTWNARKPPTEYIELAAGQAERPDEWIKPEDSIIISVKGAAVTPSDQFKTGLTLRFPRFTKLREDRSWDSALSLNEFFRRKRELDEQQQKENEMHIEQRRATKRVRKQFKIAGADQIVEPVAVSNDHLFEGMNFWIMTESSKPRKSKAEIEGIVKACGGNIFQSDGGAPNVKCIADKSVVKVLTLKKKNVEVIRPQWVFDCQELGCILPLEADRHMLFIPPDSKDKFEETIDPYGDSYYRDTTAEDLSKLLRDCVKLENDETITEEAVSELKDELSQVDPPIGWMFQHIVAYLDTPQNAQKNHISATAEDILKGNGQSRSQLDKIGLNLMMCQNLLEFGDGKIVDDFENEDITHIIVDYQDLTRVRAIRSLLSARDTIPRVTLTDWIEESWRDETLLGVENFPVEV
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Function: Involved in ds DNA break repair. Has a role in non-homologous integration (NHI) pathways where it is required in the final step of non-homologous end-joining.
Catalytic Activity: ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.
EC: 6.5.1.1
Subcellular Location: Nucleus
Sequence Length: 979
Sequence Mass (Da): 112838
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A0A0R3TKV5
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MNSTGRKQSDIDNDICRNPEMREVVGDADLRKTLHKSGEKVFQVYWGTATTGKPHVAYFVPICKIADMLHAGAKVTILFADLHAYLDNIKSPWSILCHRANYYETVIKAMLESVGVSLDKLFFVRGSEYELTRSYSEDVYRICADTSIRDARKAGAEVVKQVANPLVSGLLYPLLQALDEEYLHVDAQFGGIDQRKIFMMCERILPRLGYRKRIHLMNPMVPGLTGGKMSASEAASKIDLLESSADLRMKLNSASCPPGQTAADGNGVLAFIKFVVFPLIRLKKADSGVTINAKTFSTYEELEAAYIAGDSNVTDGALKDCIFEHLDPPMEVVRNRFKNPKLVNLLADAYPTDEAACAAKHATESANASLFMKNDQLTELKGTLDSLQQTMRITKEGPGLLAAATVFGLDKEKIVNSLSGRVVRVLWSVKPTGLPHLGLYLPIRDLALLSKHLGFIIIVVIDDIGAFLEGKCPWNQRESRFKLYETVITGLIKSACGDMKYFRIVRGSHFKCEGSYMLDLYRLVSLVPENDAAGCSGAISSAQLKALGSDDTEDEGTGANLSALLLPCMKLLDAYHLKADIRVGSPSSIEKQELFAQKFLPRFDKKFKMPFYAVNTMLPALISSADVTVMPCPSMSPFVPSLRDPQMAHSVAAQAQAKVLADQCIPLVEPAVPGTNVSTLPNNSTFVMPALKRRLKQTFCQPGNDKLNPILDILKMVIIPEFKRDAVDHIVLPRPPKHGGPIHVKLEECELDEDSKCRLDDIFASEDLHPGDLKTALEEFIEKHLRSRLTKHLPDAQTLNALIDDAFPVPSKKGKNKPNQSSKPKESIKEDRRPKGSSDKAAAFDPMMLEFCVGEIVAVDSHPNSTDYKVCRVSFGGKKNCTSVISLPKDDLINKKAIFMTNLKPTVIEGVTSEVKVVCVDEKHLFDIPEHPVGTKLQFKLIGKGGAPKGKQVASPVTIIDYAGHPGWQAFFADIYRDSGNLCWRNNWRLMVA
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Catalytic Activity: ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L-tyrosyl-tRNA(Tyr)
EC: 6.1.1.1
Subcellular Location: Nucleus
Sequence Length: 993
Sequence Mass (Da): 109570
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A0A5G2QJG2
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MDIWNHTSLSDFILLGLFSYSPYEFFLFSLVLLASATALTGNIFFLLLIQADRRLHTPMYFFLSQLSIMDLTMMGTVVPKMAANFLLGSKFISWGGCATQVFLVVMVGGAECFLLAVMAYDRYVAVCHPLMYPVLMNWKACRLMALASWMGGVADSMIDVGVVFSFPYCSSLQVDHFFCEVPALLRLSCADTLLFEDLIYACCVVMLLLPLGVIVASYARILMAVMRMPSTEGKQKALTTCSTHLAVVGLYYGGAIFSYMQRASARTPAGDRATSIFYTVLTPMLNPLIYSLRNKDVMRALKKVLSR
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Function: Putative odorant or sperm cell receptor.
Subcellular Location: Cell membrane
Sequence Length: 307
Sequence Mass (Da): 34125
Location Topology: Multi-pass membrane protein
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