ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
B1A0U4 | MALSGLGSGPEGNPNNHQGKAIPTLNPSHGQGPSFLFSWVSFLVPFWSWYPFSPLPLKGIPGENSSSPNGLKNFHGIGLNGTERGMGHFHPISGNRLGLRLTLVAGWFLEPFPTFLAVLIRTQGDSTPSRSFVAFFVGTLGLGQEGITGSFNRKIAGPATIDPQDWAMEEGVLTNFLWPPFTTFFRTTKGFPVQWHGEGSFVVPGIFSLPQPLPWWLLLPDTPTGAGKPPESRQHQPSHSMNGAIVDIPGGLTQTPSSPDRSSSTNSIADEEKKLDYKPTSPTSDTEKGESLPLTASQSEIIASPTFSEMIRVIFSGPTL... | Function: Major facilitator-type transporter; part of the gene cluster that mediates the biosynthesis of elsinochromes, pigments consisting of at least four interconvertible tautomers (A, B, C and D) that have a core phenolic quinone to which various side chains are attached and which play an important role in fungal p... |
Q8SQW6 | MASHEIQKVWADGCFDMFHYGHANALRQSKALGDYLIAGVHSSLSINQEKGLPVMEDEERYEVVEGCRYVDEVVRDAPFVTQTSMIKEYGVSIVAHGNDIVLDSSGQDSYCQVRRMGIFREVERTFGISTTEIVGRMMLKNRGSWLDGENGESSKDSGYHDRLLSLFMSSMGREKRGKVVFMDGNFDLFHAGHVASLRIARGMGDYLIVGIHDDETTKEYTRSYPVLSTKERMLTLMACRYVDEIVVSPYLVGSEFIKRHGIDVVAPSFDSKDLSRYDGIKDVVEHSYAENRFNYLSAEHIVNRIISNYQDYANRQKKRT... | Catalytic Activity: CTP + H(+) + phosphoethanolamine = CDP-ethanolamine + diphosphate
Sequence Mass (Da): 36594
Sequence Length: 322
Pathway: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from ethanolamine: step 2/3.
EC: 2.7.7.14
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Q9UTI6 | MASSSNIKHRLWLDGCMDFFHYGHSNAILQAKQLGETLVIGIHSDEEITLNKGPPVMTLEERCLSANTCKWVDEVVPSAPYVFDLEWMRRYGCQYVVHGDDISTDANGDDCYRFAKAADQYLEVKRTEGVSTTELLDRLLSSVPLEIYSTPVSVLSSQIDLLRRFATDSDGLTPFTDVFIYNTEKPETLISGTTLLRLNPEKNIIYIDGDWDLFTEKHISALELCTRMFPGIPIMAGIFADEKCFEKPMLNLLERILNLLQCKYISSILVGPPPASLFASSKYIKLCFDEQISKVYYPIFSTDVSIPALDISLSNTPNNS... | Catalytic Activity: CTP + H(+) + phosphoethanolamine = CDP-ethanolamine + diphosphate
Sequence Mass (Da): 41557
Sequence Length: 365
Pathway: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from ethanolamine: step 2/3.
EC: 2.7.7.14
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P33412 | MTVNLDPDKVWIDGCFDFTHHGHAGAILQARRTVSKENGKLFCGVHTDEDIQHNKGTPVMNSSERYEHTRSNRWCSEVVEAAPYVTDPNWMDKYQCQYVVHGDDITIDANGEDCYKLVKEMGRFKVVKRTYGVSTTEIIHRILTKKSLPPTHPDYYPTTQELSFYSVAQDAVSKHCYVFQRDLDNVLVNGGYKFDAEDCVYVDGDFDLFHMGDIDQLRKLKMDLHPDKKLIVGITTSDYSSTIMTMKERVLSVLSCKYVDAVIIDADATSMSQYNCEKYHIGTAVLTAAGKFSEYLTKELIVKRVESQREVYIARNQKKG... | Function: Ethanolamine-phosphate cytidylyltransferase which catalyzes the second step of phosphatidylethanolamine biosynthesis. Involved in the maintenance of plasma membrane and required for proper sporulation.
Catalytic Activity: CTP + H(+) + phosphoethanolamine = CDP-ethanolamine + diphosphate
Sequence Mass (Da): 36... |
Q9H8V3 | MAENSVLTSTTGRTSLADSSIFDSKVTEISKENLLIGSTSYVEEEMPQIETRVILVQEAGKQEELIKALKTIKIMEVPVIKIKESCPGKSDEKLIKSVINMDIKVGFVKMESVEEFEGLDSPEFENVFVVTDFQDSVFNDLYKADCRVIGPPVVLNCSQKGEPLPFSCRPLYCTSMMNLVLCFTGFRKKEELVRLVTLVHHMGGVIRKDFNSKVTHLVANCTQGEKFRVAVSLGTPIMKPEWIYKAWERRNEQDFYAAVDDFRNEFKVPPFQDCILSFLGFSDEEKTNMEEMTEMQGGKYLPLGDERCTHLVVEENIVKD... | Function: Guanine nucleotide exchange factor (GEF) that catalyzes the exchange of GDP for GTP. Promotes guanine nucleotide exchange on the Rho family members of small GTPases, like RHOA, RHOC, RAC1 and CDC42. Required for signal transduction pathways involved in the regulation of cytokinesis. Component of the centralsp... |
Q07139 | MADDSVLPSPSEITSLADSSVFDSKVAEMSKENLCLASTSNVDEEMPQVEARVIMVQDAGKQEELLKALKTIKIMEVPVIKIKESCPGKSEEKLIKSIINMEMKVPCVKMDSMEEFESLDSPEFENIFVVTDFQNSVFNDLYKADCRIVGPPVILNCAQRGEPLPFSCRPLYCTSMLNLVLCFTGFRKKEELVKLVTLVHHMGGVIRKECNSKVTHLVANCTQGEKFRVAVSLGTPIMKPEWIYKAWERRNEQCFCAAVDDFRNEFKVPPFQDCILSFLGFSDEEKHSMEEMTEMQGGSYLPVGDERCTHLIVEENTVKD... | Function: Guanine nucleotide exchange factor (GEF) that catalyzes the exchange of GDP for GTP. Promotes guanine nucleotide exchange on the Rho family members of small GTPases, like RHOA, RHOC, RAC1 and CDC42. Required for signal transduction pathways involved in the regulation of cytokinesis. Component of the centralsp... |
Q7W980 | MRKDETSNTSPDISVAQPASALRYHLRPPRRNDGAAIHQLVSECPPLDLNSLYAYLLLCEHHAHTCVVAESPGGRIDGFVSAYLLPTRPDVLFVWQVAVHSRARGHRLGRAMLGHILERQECRHVRHLETTVGPDNQASRRTFAGLAGERGAHVSEQPFFDRQAFGGADHDDEMLLRIGPFTHPPH | Function: Catalyzes the acetylation of L-2,4-diaminobutyrate (DABA) to gamma-N-acetyl-alpha,gamma-diaminobutyric acid (ADABA) with acetyl coenzyme A.
Catalytic Activity: acetyl-CoA + L-2,4-diaminobutanoate = (2S)-4-acetamido-2-aminobutanoate + CoA + H(+)
Sequence Mass (Da): 20729
Sequence Length: 186
Pathway: Amine and... |
O52249 | MNATTEPFTPSADLAKPSVADAVVGHEASPLFIRKPSPDDGWGIYELVKSCPPLDVNSAYAYLLLATQFRDSCAVATNEEGEIVGFVSGYVKSNAPDTYFLWQVAVGEKARGTGLARRLVEAVMTRPEMAEVHHLETTITPDNQASWGLFRRLADRWQAPLNSREYFSTDQLGGEHDPENLVRIGPFQTDQI | Function: Catalyzes the acetylation of L-2,4-diaminobutyrate (DABA) to gamma-N-acetyl-alpha,gamma-diaminobutyric acid (ADABA) with acetyl coenzyme A. Does not acetylate amino acids like GABA, L-ornithine, L-lysine and L-aspartate.
Catalytic Activity: acetyl-CoA + L-2,4-diaminobutanoate = (2S)-4-acetamido-2-aminobutanoa... |
P68104 | MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDSTEPPYSQKRYEEIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANMPWFKGWKVTRKDGNASGTTLLEALDCILPPTRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDV... | Function: Translation elongation factor that catalyzes the GTP-dependent binding of aminoacyl-tRNA (aa-tRNA) to the A-site of ribosomes during the elongation phase of protein synthesis . Base pairing between the mRNA codon and the aa-tRNA anticodon promotes GTP hydrolysis, releasing the aa-tRNA from EEF1A1 and allowing... |
P86934 | MGKEKVHMNLVVVGHVDAGKSTATGHLIYKCGGIDKRTIEKFEKEAADIGKASFKYAWVLDKLKAERERGITIDIALWKFESPKSVFTIIDAPGHRDFIKNMITGTSQADAAILIIASAQGEFEAGISKDGQTREHALLAFTLGVKQMVVCCNKMDDKTVNYGQERYDEIVKEVSAYIKKVGYNVEKVRFVPISGWQGDNMIEKSEKMPWYKGPTLLEALDMLEPPVRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVMKPGDVVTFAPANVTTEVKSIEMHHEQLAEATPGDNVGFNVKNVSVKDIRRGNVCGNTKND... | Function: This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
PTM: Phosphatidylethanolamine (PE) is a direct precursor of the ethanolamine-phosphoglycerol (EPG) moiety.
Sequence Mass (Da): 49106
Sequence Length: 449
Subcellular Location: Cytoplasm
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Q05639 | MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFETTKYYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDSTEPAYSEKRYDEIVKEVSAYIKKIGYNPATVPFVPISGWHGDNMLEPSPNMPWFKGWKVERKEGNASGVSLLEALDTILPPTRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGILRPGMVVTFAPVNITTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDI... | Function: This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
PTM: Trimethylated at Lys-165 by EEF1AKMT3 . Mono-, di-, and trimethylated at Lys-36 by EEF1AKMT4; trimethylated form is predominant. Methylation by EEF1AKMT4 contributes to the fine-tunin... |
P60608 | MNSPCDRLQQFIQVLLEESWSFPSFANTLHWPENLLSYIDELVWQGSLQNFHQHEVRFDKPPLRLPLTGFSSLTENWSSRQAVSSRLVATAASPPAGCQAPIAFLGLKFSSLGPARKNPALCFLYDQSNSKCNTSWVKENVGCPWHWCNIHEALIRTEKGSDPMFYVNTSTGGRDGFNGFNLQISDPWDPRWASGVDGGLYEHKTFMYPVAKIRIARTLKTTVTGLSDLASSIQSAEKELTSQLQPAADQAKSSRFSWLTLISEGAQLLQSTGVQNLSHCFLCAALRRPPLVAVPLPTPFNYTINSSTPIPPVPKGQVPL... | Function: Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. Endogenous envelope proteins may have kept, lost or modified their original function during evolution. This endogenous envelope protein has lost its original fusogenic properties.
PTM: The CXXC motif is highl... |
A7RR04 | MGIITLLANRRGLHAILSNAQRIVGCRFVSSSIIPDASRLRNIGISAHIDSGKTTLTERLLFYTGRISHMHEVKGKDNVGATMDSMELERQRGITIQSAATYVNWKDHNINIIDTPGHVDFTVEVERALRVLDGAVLVLCAVGGVQSQTLTVNRQMKRYNVPCIAFINKLDRMGANHNRVLSQLRAKLNHNAALLQLPVGLEGNNTGVVDIIRWKAYYFDGDNGEIVREDVIPEDMVDECRKRRQELIEVVADVDPELGDLFLEEVKPSESQIIAAIRRATIERTFTPVFVGSALKNKGVQPLLDGVLDYLPNPTEVKNY... | Function: Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA m... |
Q07803 | MRLLRITAGLGRGPLPRVPAILGWQGKQANWKTYRWCSSGSIPNEKIRNIGISAHIDSGKTTLTERVLYYTGRIATMHEVKGKDGVGAVMDSMELERQRGITIQSAATYTMWRDVNINIIDTPGHVDFTIEVERALRVLDGAVLVLCAVGGVQCQTMTVSRQMKRYNVPFLTFINKLDRMGSNPARALQQMRSKLNHNAAFVQIPIGLEGDFKGIIDLIEERAIYFDGDFGQIVRYDEIPADLRAAAADHRQELIECVANSDEQLGELFLEEKIPSVSDLKLAIRRATLSRSFTPVFLGSALKNKGVQPLLDAVLEFLPN... | Function: Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA m... |
Q9USZ1 | MLKLSFRSLTSRLPRLSTLVVRGYASVANTGIEASNTSENNLNIQEQLNDNDKKRLKQIRNIGISAHIDSGKTTFTERVLYYTGRIKDIHEVRGKDNVGAKMDFMELEREKGITIQSAATHCTWERTVDQIEANEKQKTDFEKSYNINIIDTPGHIDFTIEVERALRVLDGAVLVLCAVSGVQSQTITVDRQMRRYNVPRISFVNKMDRMGADPWKVIQQINTKLKIPAAAVQIPIGQEDKLEGVVDLIQMRAIYNRGSKGEKIEISQQVPENLIELAKEKRSALIEKLADLDEEIADIYVMEEDPTPEQLMGAIRRTTL... | Function: Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA m... |
A7EVV9 | MSMHRVARAVASSEACAGALRGSVSRTRFLCLNAPVQRFGARNALLGAGLGAKRHFFQSPIIRSGVAQAVLEKAAADPSALTQEAIVDNLNAAERDRLRRVRNIGIAAHIDSGKTTATERVLFYTGRINAIHEVRGKDAVGAKMDSMELEREKGITIQSAATFCDWMKVENGKEEKYHINLIDTPGHIDFTIEVERALRVLDGAVMILCAVSGVQSQTITVDRQMRRYNVPRISFINKMDRMGANPFKAVEQINQKLRIPAAALQVPIGSEDSFNGVVDLIRMKAIYNDGPKGEIIRETDEIPEELKQLCKEKRALLIET... | Function: Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA m... |
B8MJJ5 | MVRPAQVRALSGLARSATFVRLLPSQSQNALRCASLPVSRLGALPLRATTQITSAPLRQWHQIRNSSATATASLAEQAAADPEGLSQAEIISNIDAEEWKRISKVRNIGIAAHIDSGKTTATERVLFYTGRINAIHEVRGRDSVGAKMDSMDLEREKGITIQSAATFCDWVKKENGKEEKYHFNLIDTPGHIDFTIEVERALRVLDGAVMILCAVSGVQSQTITVDRQMKRYNVPRISFVNKMDRMGANPFKAIDQINNKLKLPAAAVQVPIGAEDEFQGVVDLIRMKAIYNEGPRGETIVEKDEIPEHIKPLAEERRRI... | Function: Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA m... |
Q4P257 | MVAIPRVAAARSLARQLARQSLRTTSFASAPVRIAIASTPLARSPSSFRSLSSSTRRSAAAAAAAAAAKATPAHDDSHTPMAVLTEADLGRLVRQRNVGISAHIDSGKTTLTERVLFYTGRIKDIHEVRGRDAVGAKMDHMELEREKGITIQSAATYCSWKATPPTEKASVSGDAANVESKELMEKKQDFHINIIDTPGHVDFTIEVERALRVLDGAVLVLCAVSGVQSQTITVDRQMRRYSVPRISFINKMDRAGANPWRVIGQIRNKLKMPAAAVQIPIGAEDDFNGVIDLIRWKAVYNEGHKGIDIRETDEIPAEYL... | Function: Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA m... |
P38732 | MITQTELDNCLQWAQNNGAFIDPKISFRITEDAGVSAFVNEKFSPKPDQALIRVPETLLITSQQALSEFSQAANERSLLNSVTQLYLSKLKFGTDAVHLKSFYKPYLDVLPLHLPQPYFWSTDEVMNLHGTDVYLTMRDTLNKLVKEWRMLFQALSIEHSSQDKQFLSLFQENKDSAVVPLEQFCAHINGCKLEDSEWNSFVAYLWSYCIFNSRAFPRVILGRAGTDRTNLNEGFLYPIVDLLNHKNDVPVRWEMNEQNELCFMSQTTTFSAQDELFNNYGNISNEKCLLNYGFWDSSNKFDFSRLTLKLPSTLVSGLPV... | Function: S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that monomethylates elongation factor 1-alpha (TEF1/TEF2) at 'Lys-30'.
Sequence Mass (Da): 67452
Sequence Length: 585
Subcellular Location: Cytoplasm
EC: 2.1.1.-
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P38347 | MFDPLDLYTPDDIQVEALQFNLAEREPKDPCSPQRDEILTAVDEEESDDDDTIIDNLDLPSVKYAPPEVILCILILLKPDRQVNFNQETGKNKSVLEVCKSHGLEPDLLKRLLTWYTEEWPNKRLNSLEKICNKIPMLRFTVSKELLLGYYTSVLKKYNNSCGLNEEIIQELLKELSSRISENCGRTAQPSIVRYFELRNLSTSIPLHEPSLTADNLGWKTWGSSLILSQLVVDHLDYLHTTNVNMLANSDIKQIKVLELGAGTGLVGLSWALKWKELYGTENIEIFVTDLPEIVTNLKKNVSLNNLGDFVQAEILDWTN... | Function: S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that mono- and dimethylates elongation factor 2 (EFT1/EFT2) at 'Lys-613' and methylates elongation factor 3A (YEF3).
Sequence Mass (Da): 47977
Sequence Length: 419
Subcellular Location: Cytoplasm
EC: 2.1.1.-
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P0CU27 | MVASRNPQTARFCWQYLQLEQSLDFPDGELLRDEAVQETIYQQLFAPNAPTPLPPARYRLRVLKELTSRIESAIEDWETHGISDNLMDAMAELVAQPLPSEAEAAQERCYVTYYLSLLEGGLEKPHITLLESRSLISASGTTGLRTWEAALHLGQFLSVNSGLVKDKRVLELGTGTGYLAVLCAKYLGTSHVIASDGSEEVVEKLSDNLFVNGLQDSDKVQPMELKWGHALLGTEEEHWNGGRKIDVVLGADITYDVSVIPALIATLEELVDLYPGISIIIAATERNRETYETFLAACGRRGFSVTPESFPVPSRAEQKG... | Function: S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that methylates elongation factor 2.
Sequence Mass (Da): 37265
Sequence Length: 336
Subcellular Location: Cytoplasm
EC: 2.1.1.-
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O14118 | MHGAPEFLTKVKQQYLQQVDLYRFQWVSKPTDWPILFNDYAQVFLSEIVTPSAYTRAFLKSYFRFLDSIDSGHNERNEALLYTYIESLSSTYIPPVQYSLGEYDILIRESRHVLLREGTTGARTWEAGMALAEYIYQHPVQSGMRVLELGAGTGLVSILCAKMGSIVLATDGDTKVCDGVRENARLNNCDINVKKLLWGVDPPEFSDIVFASDVTYDCDLRCLATTLTQIITINPNCKIILSASLRRQETFFNFLKLIQNLYARQLEVWDSPKILYYDSPPIVFYEVSK | Function: S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that methylates elongation factor 2.
Sequence Mass (Da): 33051
Sequence Length: 289
Subcellular Location: Cytoplasm
EC: 2.1.1.-
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P47163 | MNEDLFYDRLHQRCPGKYLLEELETSKSNDVLHASRFVCEMELVQKTNAYYCKTIVKMLLDHEWIFAKAFTIVNDGEDEIEIYDYLYEKYIKLLSTGKPDPMMKDVVRYRFDEDVKIKIEETPNLISAASTTGFRTWEAALYMGDFLIHKPLQELAPVQGQDDGKKKLNVLEVGAGTGIVSLVILQKYHEFVNKMYVTDGDSNLVETQLKRNFELNNEVRENEPDIKLQRLWWGSDRVPEDIDLVVGADVTYDPTILPDLCECLAECLALDRCKLCLLSATIRSESTVQLFSQECNKLGLKCTIVTSTEYDANNEIRAMK... | Function: S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that mono-, di- and trimethylates elongation factor 2 (EFT1/EFT2) at 'Lys-509'.
Sequence Mass (Da): 39024
Sequence Length: 339
Subcellular Location: Cytoplasm
EC: 2.1.1.-
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Q9P7Z3 | MSGLPESKLGTKQYWDNVYEREVSNFTEFNDEGEVWFGEEAEERIVQWLEDHISTSFREVSEAAPFRVLDLGTGNGHLLFRLLEEEDTLLPSPCQLVGVDYSEAAIVLAKNIARHRQFSDKVKFQQLDIIKDSKFCSKDWDLILDKGTFDAISLSGELLDGRPLNSVYVDRVRGMLSPNGIFLITSCNWTIQELEERFTKNGFIVHSTVPVPVFEFQGSTGSSTSVIAFQIDPSFNRK | Function: S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that mono- and dimethylates elongation factor 1-alpha at 'Lys-316'. May play a role in intracellular transport.
Sequence Mass (Da): 27011
Sequence Length: 238
Subcellular Location: Cytoplasm
EC: 2.1.1.-
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P40516 | MKRSEKKSMSSALKNGIMERTQPEKVVQMQGTADLSTSKLGTKKYWDELYALELENFRRNPQDTGDCWFSDSDAEQKMIDFLVDNIGAYRISENASVVDLGTGNGHMLFELHQTEFQGKLVGIDYSEESVKLASNIAEATGVDNFISFQQADIFSGDWKPGKYDIVLDKGTLDAISLSGMKINGKLDVVDVYAGVVERILKKDGIFLITSCNFTQDELVKIIETDNLKMWKTIKYPVFQFGGVQGATICSVAFVKQN | Function: S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that mono- and dimethylates elongation factor 1-alpha (TEF1 and TEF2) at 'Lys-316'. May play a role in intracellular transport.
Sequence Mass (Da): 28690
Sequence Length: 257
Subcellular Location: Cytoplasm
EC: 2.1.1.-
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Q5WRN3 | MSDTDDIPQLSADTLAALSMFQAEQQEKIEQLQSGIIEKIDEDWQLSQFWYDDETSRKLVAEGVAAALEGSEARPARIGCVSSPTLVKFFHETEEYKTGQIQLTLFEFDDRFGLKFPTEFVHYDYKHPTDLPAELLAKFDVIIADPPFLAAECLIKTAHSIRLLGKSDVKVLLCTGAIMEDYASRLMAMHRTSFEPRHANNLANDFSCFANYQTLTFC | Function: S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that methylates elongation factor 1-alpha.
Sequence Mass (Da): 24660
Sequence Length: 218
Subcellular Location: Cytoplasm
EC: 2.1.1.-
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Q86A24 | MSDSSDDEITLSKESLSALQDFYKSREVEQQDKFEISEDWQLSQFWYEEETSKFVANVIEQETIGGNVVVCLSTPSIYKVLHKNNNLLLNNNLFEYDKRFDVYGEKFHFYDYNNPEDGISEQLKGNVDYICLDPPFLSEECIEKVAKTIALLRKPTTRLLLLTGRIQWNNIQKYLPEMMICEFEPKHPRLQNDFFCCSNYHSKLLGLENKK | Function: S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that methylates elongation factor 1-alpha.
Sequence Mass (Da): 24823
Sequence Length: 211
Subcellular Location: Cytoplasm
EC: 2.1.1.-
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Q9VMH7 | MDDDISLPADTLAILNEFLLERSKREAEEENQIANKTGKDAQFEEDWQLSQFWYSTETKHALRDVVRKLLAERTEDSGDFSIALLSCPSLYKDIREIHDTVHIFEFDKRFEAYGTDFVHYDLNCVGSNPDYLKEHHQQYDLIVADPPFLSQECIAKTCEIITRLQRNQKESKVILCSGEVVEPWLTARLPVLKCSFRPEHERNLGNKFVSYANFNLDEYIENK | Function: S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that methylates elongation factor 1-alpha.
Sequence Mass (Da): 26043
Sequence Length: 223
Subcellular Location: Cytoplasm
EC: 2.1.1.-
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P53200 | MSDSDSDSDYELTLSANALAALEEFKREEQQHQEAFQKLYDETDEDFQKKKKEEGMKLFKEDWQLSQFWYSDDTAAILADAILEGADENTVIAIVSAPSVYAAIQKKPTNEIPTEHIYLFEFDKRFELLAGRDHFFFYDYNKPLDFSDEIKGKVDRLLIDPPFLNEDCQTKSSITAKCLLAPNDNSKTKKGVFKHRLISCTGERMSEVISKVYSDTRITTFLPEHSNGLSNEFRCYANFECSSWKFAS | Function: S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that trimethylates elongation factor 1-alpha (TEF1 and TEF2) at 'Lys-79' . Required for replication of Brome mosaic virus (BMV) .
Sequence Mass (Da): 28582
Sequence Length: 248
Subcellular Location: Cytoplasm
EC: 2.1.1.-
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P53970 | MESIFGGFGDLVVPRPKEHLGQTDLSFGGKLLPALKICEDGGESGCGGKVWIAGELLCEYILEKSVDHLLSKTVNGTKQFKKVLELGSGTGLVGLCVGLLEKNTFHDGTKVYVTDIDKLIPLLKRNIELDEVQYEVLARELWWGEPLSADFSPQEGAMQANNVDLVLAADCVYLEEAFPLLEKTLLDLTHCINPPVILMAYKKRRKADKHFFNKIKRNFDVLEITDFSKFEHYLKERTHLFQLIRK | Function: S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that methylates elongation factor 1-alpha (TEF1 and TEF2) at 'Lys-390'.
Sequence Mass (Da): 27738
Sequence Length: 246
Subcellular Location: Cytoplasm
EC: 2.1.1.-
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P49778 | MISVNDFRTGLTIEVDGGIWRVVDFQHVKPGKGAAFVRSKLRNLRTGAIQEKTFRAGEKVAKAQIETKTMQYLYANGDQHVFMDTSSYEQLELSATQIEEELKYLLENMSVHIMMYQDETLGIELPNTVELKVVETEPGIKGDTASGGTKPAKTETGLVVNVPFFVNEGDTLVVNTSDGSYVSRA | Function: Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase (... |
Q8A1F7 | MINAQDIKNGTCIRMDGKLYFCIEFLHVKPGKGNTFMRTKLKDVVSGYVLERRFNIGEKLEDVRVERRPYQFLYKEGEDYIFMNQETFDQHPIAHDLINGVDFLLEGAVLDVVSDASTETVLYADMPIKVQMKVTYTEPGMKGDTATNTLKPATVESGATVRVPLFISEGETIEIDTRDGSYVGRVKA | Function: Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
... |
A1UR93 | MKINGNEIRPGNVIEHQGSLWVAVKCNAVKPGKGGAFNQVELKNVIDGTKLNERFRAAETVEKVRLEQKDFTFLYQQGEALVFMDTESYEQLELQRDFVGDRAAFLQDGMTVTVELHEEKPLGISLPDQVTVTIAEADPAIKGQTVTSSYKPAILENGIRILVPPFVQAGERIIVDTNELTYIRRVSEKG | Function: Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
... |
B2KCP2 | MISTTDFKEGLIFENENGEIVEIVDYQHHRKSQARAVVRVKLRKLGSGSYVETSYRPEDKFKEVSVEKRPFMYLYSEGDMAHFMNNESYDQVAVPLDKLENQRKYLIENMECTGLYINDQLFDIVLPIKVVLTIKSTVPGVKGDTVSNLTKEAELETGVTIKVPLFINEGDKVIMDTRYCTYVERA | Function: Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
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B1GZJ0 | MISTSDFKNGTNILVDGEPYQIAWFQNHKPGKGGAVMRVKLRHLKKGGIIERTFKSGEKFKALTITRQKKRFLYKESNNFNFMDMDTYEQITVHPELLGKMVNFLKENLEVEAIYLENELIGIDLPVIIEMTIAEAEHGIKGDSVSNTTKTAKLETGADIHVPLFIKEGDRIKVDTRTGEYVERA | Function: Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
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Q2NAZ6 | MKISGVDIRPGNIIEYEGGIWKVAKIQHTQPGKGGAYMQVEMKNLQDGRKTNVRFRSADTVEKVRLDTQDYQFLYEDGDQLVFMDQDTYEQINLDSDLLGDARPFLQDGMTVQLELWEEKPISVQLPQQVEADIVEADAVVKGQTASSSYKPAVLDNGVRIMVPPHIESGTRIVVDVYEQTYVGKAG | Function: Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
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Q885R6 | MKTGKELKPGTVIRLENDPWLVQKAEFTKSGRNSAIMKTKLKNLLTGYKTEIVYSADDKLDDVILDRKEATLSFISGDTYTFMDTTDYTMYELNAEDIESVLPFVEEGMTDVCEAVFFDERLVSVELPTTIVRQVDYTEGSARGDTSGKVMKPAKLKNGTELSVADFIEIGDMIEIDTREGGSYKGRAK | Function: Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
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Q8D2R7 | MIIYYSANQSKSGLKILLKNEPCLILENQFVKPGKGQPFNRIKIKKLISGKIFTKIFKSNEKLIYADVLDVKVKSLYKDKKYWNFIKKENFEQFKISKKNLGEKYKWIIEQLECIVTFWDENPINITLPRFVDIKVCNANFDIKGDTIKSGNKYIILTTGAIIKAPIFIRSEEIVRVDTNLGEYVSRIK | Function: Involved in peptide bond synthesis. Alleviates ribosome stalling that occurs when 3 or more consecutive Pro residues or the sequence PPG is present in a protein, possibly by augmenting the peptidyl transferase activity of the ribosome. Modification of Lys-35 is required for alleviation.
PTM: May be beta-lysyl... |
Q73FP5 | MAERANDIRPGQVLEHNGGLFLVVGIMHTQPGKGGAYIQAEMKNIKTGAKHYERFRSDATIRRAILDEEEYVYLFTEGNIVNLMHPSNYEQITINLDLLGEKKIYLQDNMKIKVVAYQDKIISAHVPDYVTLAVKETESVIKGQTATASYKPAILENGMRVNVPQFIKEEDKIVVYTPGDSYYERVKE | Function: Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
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Q0C7P6 | MQLTQLLALALSLATSEAAYKGFNYGDKKPDGSSKYQADFASEFETAQNLVGAPGFTSARLYTMIQAGTANDPISAIPAAIAQNTSLLLGLWASGNNMNNELTALKAAISQYGEDLSKLVVGISVGSEDLYRNSVLGQKVNAGVGVDPHVLASYIEEVRSTISGTPLSGAPLGHVDTWNDWVNGSNAAVIDAVDWVGFDGYPYFQNTMANSIDDAKALFNEAVAKTKSAAGNKEVWITETGWPVSGKTENLAVASIPNAKRFWDEVGCPLFDNTNTWWYTLQDAFGASVPNPSFGIVGSTLTTQPLFDLSCSKSNTTSSS... | Function: Glucanases play a role in cell expansion during growth, in cell-cell fusion during mating, and in spore release during sporulation. This enzyme may be involved in beta-glucan degradation and also function biosynthetically as a transglycosylase (By similarity).
PTM: The GPI-anchor is attached to the protein in... |
Q5AUT0 | MFTKTQILALALSIASAEAVSKGFNYGANKPDGTLKVQADFEAEFRTAKNLETTSGFNSARLYTMIQGTGSTPISAIPAAIAEETTLLLGLWASGGNMDNEIAALKAAINQYGDEFAKLVVGISVGSEDLYRNSEIGVQANAGIGIEPEELVSYIQRVREAIAGTALSGAPIGHVDTWNAWTNGSNAAVAEAVDWLGFDGYPFFQNTMQNSIDDAKALFDESVQKTKAVAGNKEVWITETGWPVSGDSQNLAIASVENAKQFWDEVGCPLFDNVNTWWYILQDASGSSVPNPSFGIVGNTLSTTPLFDLSCSASSKKNSS... | Function: Glucanases play a role in cell expansion during growth, in cell-cell fusion during mating, and in spore release during sporulation. This enzyme may be involved in beta-glucan degradation and also function biosynthetically as a transglycosylase.
PTM: The GPI-anchor is attached to the protein in the endoplasmic... |
A1DJ47 | MQFTQLVALALALATSEAAHQGFNYGNTKSDGSAKSQSDFQAEFSTAKNLVGTSGFTSARLYTMIQGGTANTPISAIPAAVAEETSLLLGLWASGGNFANEIAALKTAIADYGDDLAKLVVGISVGSEDLYRNSVDGVKAKAGLGTNPDEIVSYINQVRSTIAGTKLSGAPIGHVDTWTAWVNGSNSAVIDACDWLGFDGYPYFQNTMANSISDAKALFDESVAKTEAVAKGKEVWITETGWPVSGNTENLAVANLANAKTYWDEVGCPLFGKTNTWWYILQDANPVTPNPSFGIVGSTLSTTPLFDLSCSASSSAAASS... | Function: Glucanases play a role in cell expansion during growth, in cell-cell fusion during mating, and in spore release during sporulation. This enzyme may be involved in beta-glucan degradation and also function biosynthetically as a transglycosylase (By similarity).
PTM: The GPI-anchor is attached to the protein in... |
Q5BCX8 | MKFSSVLALAASAKLVASHATVFAVWINDEDQGLGNTADGYIRTPPNNSPVTDVTSTDLTCNVNGDQAAAKTLEVAAGDKITFEWHHNSRDSSDDIIADSHKGPVLVYMAPTEAGSAGKNWVKIYEDGYNDGTWAVDTLIANKGKHSVTVPDVPAGNYLFRPEIIALHEGNREGGAQLYMECVQFKVTSDGTTQLPEGVSLPGAYTATDEGILFDIYSSFDSYPIPGPAVWDGASSGSGSSGSGSSSSAAATSSAEKTATSTTAAATTTAVATSTSSATQVQPTSVATFTTSVRPTTSAAPTTSAPTSSAAPTGGTGTGS... | Function: Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds, like in carboxymethylcellulose (CMC), hydroxyethylcellulose (HEC) and beta-glucan. Involved in the degradation of complex natural cellulosic substrates.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cel... |
Q9GZT9 | MANDSGGPGGPSPSERDRQYCELCGKMENLLRCSRCRSSFYCCKEHQRQDWKKHKLVCQGSEGALGHGVGPHQHSGPAPPAAVPPPRAGAREPRKAAARRDNASGDAAKGKVKAKPPADPAAAASPCRAAAGGQGSAVAAEAEPGKEEPPARSSLFQEKANLYPPSNTPGDALSPGGGLRPNGQTKPLPALKLALEYIVPCMNKHGICVVDDFLGKETGQQIGDEVRALHDTGKFTDGQLVSQKSDSSKDIRGDKITWIEGKEPGCETIGLLMSSMDDLIRHCNGKLGSYKINGRTKAMVACYPGNGTGYVRHVDNPNGD... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-... |
Q96KS0 | MDSPCQPQPLSQALPQLPGSSSEPLEPEPGRARMGVESYLPCPLLPSYHCPGVPSEASAGSGTPRATATSTTASPLRDGFGGQDGGELRPLQSEGAAALVTKGCQRLAAQGARPEAPKRKWAEDGGDAPSPSKRPWARQENQEAEREGGMSCSCSSGSGEASAGLMEEALPSAPERLALDYIVPCMRYYGICVKDSFLGAALGGRVLAEVEALKRGGRLRDGQLVSQRAIPPRSIRGDQIAWVEGHEPGCRSIGALMAHVDAVIRHCAGRLGSYVINGRTKAMVACYPGNGLGYVRHVDNPHGDGRCITCIYYLNQNWDV... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Prolyl hydroxylase that mediates hydroxylation of proline residues in target proteins, such as ATF4, IKBKB, CEP192 and HIF1A . Target proteins are preferentially recognized via a LXXLAP motif . Cellular oxygen sensor that catalyzes, under normoxic conditions, the post... |
Q91YE2 | MDSPCQPQALNQALPQLPGSVSESLESSRARMGVESYLPCPLLPAYHRPGASGEASAGNGTPRTTATATTTTASPLREGFGGQDGGELWPLQSEGAAALVTKECQRLAAQGARPEAPKRKWAKDGGDAPSPSKRPWARQENQEAKGESGMGCDSGASNSSSSSSNTTSSSGEASARLREEVQPSAPERLALDYIVPCMRYYGICVKDNFLGAVLGGRVLAEVEALKWGGRLRDGQLVSQRAIPPRSIRGDQIAWVEGHEPGCRSIGALMAHVDAVIRHCAGRLGNYVINGRTKAMVACYPGNGLGYVRHVDNPHGDGRCI... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Prolyl hydroxylase that mediates hydroxylation of proline residues in target proteins, such as ATF4, IKBKB, CEP192 and HIF1A . Target proteins are preferentially recognized via a LXXLAP motif (By similarity). Cellular oxygen sensor that catalyzes, under normoxic condi... |
Q7QBW3 | MSDTISCTPETATFEAPQLQFNEDGWGPCELPDAFKDIPYQPFSKSDRLGKISDWTGTAQTDKKFSNKYASQFGGGSQYAYFHEEDETTFHLVDSARIQKPPHQRGRFRGNMRNNRSGRGRGARGGVQVGGMTTLSKSANKMRDQRRGTTRKWGMRGPPPKIRDASVTVRPDWVTIEEMDFPRLAKLSLPSVKEGEDIMTCGTLEYYDKTYDRVNVKNERPLQSVDRIFHTVTTTDDPIIRQLSKTHGNVYATDAILATIMCCTRSNYSWDIVIDKIGGKLFMDKRDNTEFDLLTVNETASEPPQEDGNSLNSPRNLAIE... | Function: mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifica... |
P56820 | MVTEAFEFVAVPFNSDGWGPPDASDVSSSASPTSVAAANLLPNVPFASFSRSDKLGRVADWTRNLSNPSARPNTGSKSDPSAVFDFSAFAIDEGFGLASSGGNPDEDAAFRLVDGKPPPRPKFGPKWRFNPHHNRNQLPQRRDEEVEAKKRDAEKERARRDRLYNNNRNNIHHQRREAAAFKSSVDIQPEWNMLEQIPFSTFSKLSYTVQEPEDLLLCGGLEYYNRLFDRITPKNERRLERFKNRNFFKVTTSDDPVIRRLAKEDKATVFATDAILAALMCAPRSVYSWDIVIQRVGNKLFFDKRDGSQLDLLSVHETSQ... | Function: mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifica... |
Q3T122 | MAKFMTPVIQDNPSGWGPCAVPEQFRDMPYQPFSKGDRLGKVADWTGATYQDKRYTNKYSSQFGGGSQYAYFHEEDETSFQLVDTARTQKTAYQRNRMRFAQRNLRRDKDRRNMLQFNLQTLPKSAKQKERERIRLQKKFQKQFGVRQKWDQKSQKPRDSSVEVRSDWEVKEEMDFPQLMKMRYLEVSEPQDIECCGALEYYDKAFDRITTRSEKPLRSIKRIFHTVTTTDDPVIRKLAKTQGNVFATDAILATLMSCTRSVYSWDIVVQRVGSKLFFDKRDNSDFDLLTVSETANEPPQDEGNSFNSPRNLAMEATYIN... | Function: mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, a complex required for several steps in the initiation of protein synthesis of a specialized repertoire of mRNAs. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, e... |
P30642 | MALPKFELLSLADNTVGWGPLASSSSADEPVPFQQFNKADRIGRVADWIGVDRFYRRGNERYNERVYGSAANAGSQFDYIHGMDEHNFQLVDTSKPMARNPQRNFRVRQMHLRKMMQKENEKREMVNQSTNLRMKRSIAKEQQRAFKMWQRRGGNARQGQRGQGGRFGGDRPKERLPSVQVRPEWVVLEEMNLSAFSKLALPNIPGGDDIGDHQYGSLQYYDKTIDRVSVKNSIPLQRCAGVFYNVTTTEDPVIQELAQGGAGNVFGTDIILATLMTAPRSVYSWDIVAYRVGDKLFFDKRNTRDILNPVETLTVSETSA... | Function: mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifica... |
Q9C5Z2 | MATMARSFLQAISKDEAVAPPLRVVQIEGLAVLKIIKHCKEFSPTLVTGQLLGLDVGSVLEVTNCFPFPVRDDDEEIEADGANYQLEMMRCLREVNVDNNTVGWYQSTVLGSYQTVELIETFMNYQENIKRCVCIIYDPSKADLGVLALKALKLSDSFMELYRGGNFTGEKLREKNFSWMDIFEEIPIKVSNSALVSAFMTELETDTPVSQGDYDRLHSSTTPFLENNMEFLIKCMDDLSMEQQKFQYYYRNLSRQQAQQQAWLQKRRTENMARKSAGEEPLPEEDPSNPIFKAIPEPSRLESFLITNQVSNFCGQINGV... | Function: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and i... |
P26378 | MEWNGLKMIISTMEPQVSNGPTSNTSNGPSSNNRNCPSPMQTGATTDDSKTNLIVNYLPQNMTQEEFRSLFGSIGEIESCKLVRDKITGQSLGYGFVNYIDPKDAEKAINTLNGLRLQTKTIKVSYARPSSASIRDANLYVSGLPKTMTQKELEQLFSQYGRIITSRILVDQVTGVSRGVGFIRFDKRIEAEEAIKGLNGQKPSGATEPITVKFANNPSQKSSQALLSQLYQSPNRRYPGPLHHQAQRFRLDNLLNMAYGVKRLMSGPVPPSACPPRFSPITIDGMTSLVGMNIPGHTGTGWCIFVYNLSPDSDESVLWQ... | Function: RNA-binding protein that is involved in the post-transcriptional regulation of mRNAs . Plays a role in the regulation of mRNA stability, alternative splicing and translation . Binds to AU-rich element (ARE) sequences in the 3' untranslated region (UTR) of target mRNAs, including GAP43, VEGF, FOS, CDKN1A and A... |
O94533 | MFQYEALHVGCNRIPTAATWSSNLGLIYGAERLIAVADPFKEINYLMAGHSGRINCVCELATNSEYRSPFILSGASDKTLRLWQLEEEYFTCIKTIELEATVNCLCVNENLVVCGCSNSSCIVYSWNAEQRNLTEISRFTCSEIIPLEFAIVKLDHGIILTVCGSSKKIMVYGSDSAISSFKLKAVLRGHLDWVRTLSFKKTSGSTATLASGSQDRYIRLWNISLWGSEDEKVSEEFFESVLSNKPVRFTLGKIDLKIVFDALLMGHEDWVMSVDWHPTKEMILSSSADSSMIVWEPDTNTGIWVVTGRMGEMASSHGST... | Function: Component of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) . The elongator complex catalyzes formation of carboxymethyluridine in the wobble base... |
Q5EBD9 | MSAPIVQLAHAAFSVNRCPSCVSWSRTGILACATCHSIALYDPQKNVVISTLNGHTGRVNCVHWVQKNDCSAETELVSGGSDKKVIIWAIEKNKCEQPVAAEGHTEVVNAVHAVYTQRSENELLIVSAASDCTVRLWLRRNVKTECLQTLSFGKGFVLDVCISFLPGSLVPVLACGADDSRIHLYVLQNEQFEKTQVLHGHEDWIRGVEWAVTGQNLFLASCAQDCLIRIWKIFRKTAKENSKTEDENSIKLKENIFKVKEKDTETSYAVTLETVLTGHENSIYAVHWQPSFSRDGSIVQPMSLLSASMDKTMILWEPDE... | Function: Component of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine). The elongator complex catalyzes the formation of carboxymethyluridine in the wobble b... |
P42935 | MVECITPEAIFIGANKQTQVSDIHKVKKIVAFGAGKTIALWDPIEPNNKGVYATLKGHEAEVTCVRFVPDSDFMVSASEDHHVKIWKFTDYSHLQCIQTIQHYSKTIVALSALPSLISVGCADGTISIWRQNIQNDEFGLAHEFTIKKGFFYPLCLSLSKVEEKKYLLAIGGTNVNVFIASFILSDSGIEKCRVVAELEGHEDWVKSLAFRHQETPGDYLLCSGSQDRYIRLWRIRINDLIDDSEEDSKKLTLLSNKQYKFQIDDELRVGINFEALIMGHDDWISSLQWHESRLQLLAATADTSLMVWEPDETSGIWVCS... | Function: Component of the elongator complex, a multiprotein complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) . The elongator complex catalyzes formation of carboxymethylur... |
Q23651 | MDQKGSQRALLAQTINEIVKLLIEAHNQKKDVNLNRLKCIVAQKNGLSFQPKLVDIIAGVPSDYKDSLLPKLKAKPVRTASGIAVVAVMSKPHRCPHINFTGNICVYCPGGPDSDFEYSTQSYTGYEPTSMRAIRARYNPYLQTRGRLNQLMQLGHSVDKVEFIVMGGTFMSLPEDYRDFFIRNLHDALSGHTSASVEEAVAYSERSKMKCIGITIETRPDYCLPRHLNDMLLYGCTRLEIGVQSTYEDVARDTNRGHTVKSVCETFHMAKDTGYKVVIHMMPDLPNVGLERDKEQFLELFESPAFRPDGLKLYPTLVIR... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalytic tRNA acetyltransferase subunit of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methox... |
A0A1C7D1B7 | MKKLSRTISGVTPVAVMTKPLPCPGKCIYCPTFAATPQSYTPESPAVLRAKSCEYQAYKQVALRLRIIQDMGHPTDKVELIIMGGTFLSADITYQYGFIKDCYDALNGVVAGSLEEAKTINETAQHRCVGLCIETRPDICGKAEIQRMIDFGTTRVELGVQMLDDDIYKLVERGHRVSDVAEATCLLREYGLKVHYHWMPGLPGSSPEKDLALSRMVFEDPRFCPDGLKLYPTMVVEGTILEQWWKEGRYTPYPNGTMTGLIADIKALVPPYVRISRVLRDIPAVFISAGLKDSLRDGVRQILESRHQKCRCIRCREYGH... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: tRNA uridine(34) acetyltransferase, which mediates formation of carboxymethyluridine in the wobble base at position 34 in tRNAs . The proposed mechanism is the following: (i) recruits S... |
Q1ZXC6 | MSLMNDPRPVSKKAGAKPVYGKNTPQFTKTVGEIVNALINAYKEGKKVNLLKIKTELAAKNSLSDQPKSVDIISAIPESYKNTLLPLLKAKPVRTASGIAVVAVMCKPHRCPHLAMTGNICVYCPGGPDSDFEYSTQSYTGYEPTSMRAIRARYNPFLQTRHRIDQLKRLGHNVEKVEFIIMGGTFMSLPSDYRDYFIRNLHDALSGHTSNNVAEAVKYSEQSNVKCVGITIETRPDHCLKLHLSNMLTYGCTRLEIGVQSVFEDIARDTNRGHTVRAVLESFQLAKDSGFKVVAHMMPDLPNMGMERDIYGFMEFFENP... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalytic tRNA acetyltransferase subunit of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methox... |
Q9H9T3 | MRQKRKGDLSPAELMMLTIGDVIKQLIEAHEQGKDIDLNKVKTKTAAKYGLSAQPRLVDIIAAVPPQYRKVLMPKLKAKPIRTASGIAVVAVMCKPHRCPHISFTGNICVYCPGGPDSDFEYSTQSYTGYEPTSMRAIRARYDPFLQTRHRIEQLKQLGHSVDKVEFIVMGGTFMALPEEYRDYFIRNLHDALSGHTSNNIYEAVKYSERSLTKCIGITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVARDTNRGHTVKAVCESFHLAKDSGFKVVAHMMPDLPNVGLERDIEQFTEFFENPAFRPDGLKLYPT... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalytic tRNA acetyltransferase subunit of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methox... |
D5VRB9 | MKEKLMRCIIERILKEYKEGKTLDKKRIEQIKSECLRIYRIGIGHPSNSEILKYATEEEKKILIPILRKKPVRTISGVAVVAVMTSPAKCPHGKCIFCPGGLDSVFGDVPQSYTGREPATMRGLMFNFDPYLQTRARIEQLEKVGHPTDKIELIIMGGTFPAREIEYQDWFIKRCLDAMNERESKSLEEAQKINETAKHRCVALCIETRPDYCSEKEINQMLKLGATRVELGVQSIYNEILKLCKRGHSVEDTIKATQLLKDSGLKVSYHLMPGMPGSSIEMDKKMFKEIFTNPDFMPDMVKIYPCLVIEGTELYEMWKR... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: tRNA uridine(34) acetyltransferase, which mediates formation of carboxymethyluridine in the wobble base at position 34 in tRNAs . The proposed mechanism is the following: (i) recruits S... |
O14023 | MSTSSLAFLKAKACAEIVAELIASENQNKVINLNALKMRISKKHQLSESPRLTDIIAAIPPDAYLKESLMRKLRAKPVRTASGIAVVAVMCKPHRCPHIAMTGNVCVYCPGGPDSDFEYSTQSYTGYEPTSMRAIRARYDPYEQARGRVEQLRSLGHTVDKVEYIIMGGTFMSLPESYRHTFIANLHNALSGATTEDLDEAVKFSEQSETKCVGITIETRPDYCLDQHLDEMLRYGCTRLEIGVQSVYEDVARDTNRGHTVKAVCETFQLAKDTGYKVVTHMMPDLPNVGMERDIFQFQEYFENPAFRTDGLKLYPTLVI... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalytic tRNA acetyltransferase subunit of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methox... |
Q6GLC5 | MAGVALKREGPQFISEAAVRGNAAVLDYCRTSVSALSGATAGILGLTALYGFIFYFLASFLLSLLLVLKSGRKWNKYFKSRKPLFTGGLIGGLFTYVLFWTFLYGMVHVY | Function: Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins. Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing featu... |
Q12431 | MSSNEEVFTQINATANVVDNKKRLLFVQDSSALVLGLVAGFLQIESVHGFIWFLILYNLINVIYIVWICQLQPGKFYQSPLHDIFFESFFREITGFVMAWTFGYALIG | Function: Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins . Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing feat... |
Q9NPA0 | MAAALWGFFPVLLLLLLSGDVQSSEVPGAAAEGSGGSGVGIGDRFKIEGRAVVPGVKPQDWISAARVLVDGEEHVGFLKTDGSFVVHDIPSGSYVVEVVSPAYRFDPVRVDITSKGKMRARYVNYIKTSEVVRLPYPLQMKSSGPPSYFIKRESWGWTDFLMNPMVMMMVLPLLIFVLLPKVVNTSDPDMRREMEQSMNMLNSNHELPDVSEFMTRLFSSKSSGKSSSGSSKTGKSGAGKRR | Function: Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins . Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing feat... |
Q0IHY5 | MPAVALGVSVGWRSLSLWLLALLQLCSADLDVLSPGSGSDKFKVEGRAVVPGVRPQDWVNTARVLVDGEEHVGFLRTDGSFVVHDVPSGSYVVEVISPAHRFEPVRVDITSKGKMRARYVNHIKTSEVVRLPYPLQMKSSGPPSYFIKRETWGWTDFLMNPMVMMMVLPLLIFVLLPKVVNTSDPEMRREMEQSMNMLNTNPELPDVSEFMTRLFTSKSSSKSSGSGKAGKSVGKRR | Function: Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins. Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing featu... |
Q9W1Y1 | MCDYKVSERAYAKLIFHAAKYPHQAVNGLLLAEKTSKGSQVEIVDAIPLFHQCLYVTPMAEVALMLIDAHAEREGLVIAGYYAAPENFYDNQVDKTPAAKIADKIQENFKNACFVVVDNKLMTLQHDRAAIQVFNCPGDSGARWSKAKFTLSQASDTLEGVSLLLKRGAMRDLVDFDNHLDNPDKNWTNDFLNQPLNDLQKLY | Function: Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized multi-pass membrane proteins like rhodopsins.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 22781
Sequence Length: 203
S... |
O43402 | MPGVKLTTQAYCKMVLHGAKYPHCAVNGLLVAEKQKPRKEHLPLGGPGAHHTLFVDCIPLFHGTLALAPMLEVALTLIDSWCKDHSYVIAGYYQANERVKDASPNQVAEKVASRIAEGFSDTALIMVDNTKFTMDCVAPTIHVYEHHENRWRCRDPHHDYCEDWPEAQRISASLLDSRSYETLVDFDNHLDDIRNDWTNPEINKAVLHLC | Function: Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins . Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing feat... |
O70378 | MPGVKLTTQAYCKMVLHGAKYPHCAVNGLLVAERQRPRKEHPPGAGSHTLFVDCIPLFHGTLALTPMLEVALTLIDSWCKDNSYVIAGYYQANERVKDASPNQVAEKVASRIAEGFGDAALIMVDNAKFTMDCAAPTIHVYEQHENRWRCRDPHHDYCEDWPEAQRISASLLDSRSYETLVDFDNHLDDIRSDWTNPEINKAVLHLC | Function: Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins. Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing featu... |
Q9Y3B6 | MGEVEISALAYVKMCLHAARYPHAAVNGLFLAPAPRSGECLCLTDCVPLFHSHLALSVMLEVALNQVDVWGAQAGLVVAGYYHANAAVNDQSPGPLALKIAGRIAEFFPDAVLIMLDNQKLVPQPRVPPVIVLENQGLRWVPKDKNLVMWRDWEESRQMVGALLEDRAHQHLVDFDCHLDDIRQDWTNQRLNTQITQWVGPTNGNGNA | Function: Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins . Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing feat... |
Q9WZP2 | MEFLKRSFAPLTEKQWQEIDNRAREIFKTQLYGRKFVDVEGPYGWEYAAHPLGEVEVLSDENEVVKWGLRKSLPLIELRATFTLDLWELDNLERGKPNVDLSSLEETVRKVAEFEDEVIFRGCEKSGVKGLLSFEERKIECGSTPKDLLEAIVRALSIFSKDGIEGPYTLVINTDRWINFLKEEAGHYPLEKRVEECLRGGKIITTPRIEDALVVSERGGDFKLILGQDLSIGYEDREKDAVRLFITETFTFQVVNPEALILLKF | Cofactor: A flavin ligand is bound near the 3-fold axis channel; FMN is consistent with the observed density, absorbance data and mass spectrometry.
Function: Shell component of a type 1 encapsulin nanocompartment. Assembles into proteinaceous shells 23-24 nm in diameter with 2-2.5 nm thick walls. Cargo protein Flp (fe... |
Q4W945 | MDQYSNLFAFEDYLGAQARSIPDLPEVDVLSPRVVRVLGGNPGQMQLQGTNTYILGTGAERLLIDSGQGRARWEQLMASLAAEHKFRISTVLLTHWHLDHTGGVPHLFRIFPELRGANAIYKYHPDPSQQAIVDGQVFSVEGATVRAVFTPGHSTDHMCFLLQEEEAIFTGDTVLGHGTTGVEDLEEYMQSLRKIQSLGCRIGYPGHGAVIENMQQKVQQEIDRKQRRERQVLLALQNIQREKRTVGDANGAATQAELIEAIFGRLPADVADRFFAPYMKDILMKMARDKQVGFRFKGGQKHWFANVSQENPVCR | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Atrochrysone carboxyl ACP thioesterase; part of the gene cluster that mediates the biosynthesis of endocrocin, a simple anthraquinone interesting for many biotechnological applications . The pathway begins with the synthesis of atrochrysone thioester by the polyketid... |
A4DA85 | MASVQGLIKIVAITGGVWLSGKITAHSLVSVPALLQTRSADGLSPCTILRVWRRIYEQGHRHSPQIAACTSTAFAYLAWCASDRTPRLLYGTAACSVMGIVPYTLLFMGPTNSRLLERSAAEEEKVPGATRGEDMVNVPSEMTTEELLSHWRFLAGIRGLLPLAGGILGLFAALYSNEGAR | Function: Anthrone oxygenase; part of the gene cluster that mediates the biosynthesis of endocrocin, a simple anthraquinone interesting for many biotechnological applications . The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) encA . The atrochrysone carboxyl ACP thioester... |
Q4W946 | MTKPQPPPILDFSVFYGHDSQAKAQLVQRVRECCLNNGFFQITGHKVSPELQRRTFDCAKRFFDLPLIEKKKIERSPDAFNRGYEAFQSHMSQPGSAPDRKEGLFLGPDLAEDHPYCVQKKLNCGPNRWPQGLDDLEEFKLVSMEYYAALFQLAKDVVAVLALTMDYEETFFDPLTEGAIATLRYLHYPPQPVGDAEAGLGTGAHRDYSCITLLLQDGTGGLQVLDEPTGQWLDVKPVPGAYIVNLANVFARMTNGHYKSALHRVVNKSGMERYSIPFFFTGNPDYVCECLSRFRKEGEPVRHPPATVHEVVAEAVRGTV... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: 2-oxoglutarate-Fe(II) type oxidoreductase; part of the gene cluster that mediates the biosynthesis of endocrocin, a simple anthraquinone interesting for many biotechnological applications . The pathway begins with the synthesis of atrochrysone thioester by the polyket... |
Q8U1L4 | MLSINPTLINRDKPYTKEELMEILRLAIIAELDAINLYEQMARYSEDENVRKILLDVAREEKAHVGEFMALLLNLDPEQVTELKGGFEEVKELTGIEAHINDNKKEESNVEYFEKLRSALLDGVNKGRSLLKHLPVTRIEGQSFRVDIIKFEDGVRVVKQEYKPIPLLKKKFYVGIRELNDGTYDVSIATKAGELLVKDEESLVIREILSTEGIKKMKLSSWDNPEEALNDLMNALQEASNASAGPFGLIINPKRYAKLLKIYEKSGKMLVEVLKEIFRGGIIVTLNIDENKVIIFANTPAVLDVVVGQDVTLQELGPEG... | Function: Fusion of the shell and cargo protein of a type 1 encapsulin nanocompartment . The nanocompartment is probably involved in iron storage (Probable). Expression in E.coli generates spherical particles (PfSPs) about 30 nm in diameter . The purified N-terminus has ferroxidase activity .
Catalytic Activity: 4 Fe(2... |
P46841 | MTSAQNESQALGDLAAGQLANATKTVPQLSTITPRWLLHLLNWVPVEAGVYRVNRVVNPERVAVKAEAGAGTEAPLPETFVDYETSPREYTLRTISTLLDIHTRVSDLYSSPHDQITQQLRLTIETIKERQECELVNSPEFGLLAQVTPEQTIRTFAGAPTPDDLDALITKVWKMPSFFLTHPQGIAAFGREATYRGVPPVVVSLFGAQFITWRGIPLIPSDKVPVQDGETKFILVRTGEERQGVVGLFQPGLVGEQAPGLSVRFTGINQAAIATYLVTLYTSLAVLTDDALAVLDNVAVDQFHEYK | Function: Shell component of a type 2A encapsulin nanocompartment. Forms encapsulin nanocompartments about 24 nm in diameter from 60 monomers. Probably encapsulates at least cysteine desulfurase (CyD, AC O32975) and allows passage of cysteine into its interior, probably involved in sulfur metabolism (By similarity). Ex... |
I3NID5 | MTSAQNESQALGDLAARQLANATKTVPQLSTITPRWLLHLLNWVPVEAGIYRVNRVVNPEQVAIKAEAGAGSEEPLPQTYVDYETSPREYTLRSISTLVDIHTRVSDLYSSPHDQIAQQLRLTIETIKERQELELINSPEYGLLAQATPEQTIQTLAGAPTPDDLDALITKVWKTPSFFLTHPLGIAAFGREATYRGVPPPVVSLFGAQFITWRGIPLIPSDKVPVEDGKTKFILVRTGEERQGVVGLFQPGLVGEQAPGLSVRFTGINQSAIATYLVTLYTSLAVLTDDALAVLDDVAVDQFHEYK | Function: Shell component of a type 2A encapsulin nanocompartment. Forms encapsulin nanocompartments about 24 nm in diameter from 60 monomers, probably involved in sulfur metabolism (By similarity). Probably encapsulates cysteine desulfurase (Probable).
Sequence Mass (Da): 33671
Sequence Length: 307
Domain: Has 4 domai... |
Q55032 | MTDNAPQLALRDVAARQLANATKTVPQLRTITPRWLVRLLHWTPVEAGIYRVNQVKDASQITVACSERDESELPETFVDYIDNPREYLLSAVNTVVDVHTRISDLYSNPHDQIREQLRLTIEIMKERQESELINSREYGLLNNVAPGQLVHTRNGAPTPDDLDELLIRVWKEPAFFLAHPQAIAAFGRECTRRGVPPATVSLFGSSFITWRGVPLIPSDKVPLENGKTKILLLRVGESRQGVVGLYQPNLPGEQGMGLSVRFMGINRKALASYLVSLYCSLAVLTDDALAVLDNVDVTQYHTYRYN | Function: Shell component of a type 2A encapsulin nanocompartment. Expression in E.coli generates nanocompartments with an average diameter of 25 nm. They can be disassembled by treatment with 6M guanidine hydrochloride and reassembled with cargo. The nanocompartment is probably involved in sulfur metabolism . Probably... |
B8GKX5 | MVKIGVHVSIAGSIARAVERAMAIDCDTFQIFSRNPRGWTFKPLAEEDAALFQGALGTSGIGPAVVHMPYLPNLASPKEEIWRKSVEALTEELHRCSMLDVPYLVTHLGHHMGEGIGAGEGRVQQAIDAAFSQSDPGSSRVMLLLENTAGEKNSVGSRFEEIGRIRESCSDPDRIGVCMDTCHAFAAGYDLRNEVGLSRTLEAFEDGIGIEHLHVIHLNDAKADIGSHLDRHTHIGLGMIGEEGCSGILTHPTLASLPFICETPEDAVRDNAANIRAVRRLAVPRA | Cofactor: Binds 3 Zn(2+) ions.
Function: Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products.
Sequence ... |
Q5UPY4 | MQSNINICTLSIFIIESMTTRIGRHINISKGFVSAPEYAKNIGCSVFQIFLGAPQQILSKARQKDELIEFGKQLIKHDLIMVVHGSYTINLCHPPGSKKFETSIKSLVKDLNATNLIGDRCLGVIIHMGKNISENKLTVDQAIDNYVTGIKTALSQTPDNTTIVLETGASQGSEVASHIDGLAQIYWCLNDAERERVYFCIDTCHIWATGYDISSPTGVKKFFKEFDKKIGVEKISCIHFNDSKTGLESKVDRHADLCYGEIGSNGLKAIAKFAKEYKIHLIMETPLDAINPETNQEISYNEEYNKVKSWLK | Cofactor: Binds 3 Zn(2+) ions.
Function: Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic sites (AP sites) to produce new 5'-ends that are base-free deoxyribose 5-phosphate residues (By similarity).
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphooligonuc... |
Q2RJF1 | MRLGAHLSIAKGLPRTAAMATSIGANTFQYFTRNPRGGAARQIPGKEIQAWREARRRADLYPIAGHLPYTVNLGAAAERQQEFTRMVLHDDTLRVAAIDGEYLISHPGHYEGERQAGLDRIIQLIEEAYLSITPPGPMLLLETMAGQGKEVGTIDDLCYILEGLGWPDRVGVCLDSAHLFAAGWDLRTPAGCQQLVQELAAKIGLDRVKAMHLNDSAAPLGSHRDRHAGIGKGELGREGIAAVVNDPFLGELPLFLETPVANYEEYGEEIALIQKLKSV | Cofactor: Binds 3 Zn(2+) ions.
Function: Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products.
Sequence ... |
P63536 | MLIGSHVSPTDPLAAAEAEGADVVQIFLGNPQSWKAPKPRDDAAALKAATLPIYVHAPYLINLASANNRVRIPSRKILQETCAAAADIGAAAVIVHGGHVADDNDIDKGFQRWRKALDRLETEVPVYLENTAGGDHAMARRFDTIARLWDVIGDTGIGFCLDTCHTWAAGEALTDAVDRIKAITGRIDLVHCNDSRDEAGSGRDRHANLGSGQIDPDLLVAAVKAAGAPVICETADQGRKDDIAFLRERTGS | Cofactor: Binds 3 Zn(2+) ions.
Function: Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products.
Sequence ... |
Q7NBA9 | MKSNKIKYLGCFVGATKPDFMLGMVKTVVDYGATSFMFYSGPPQSFRRTPTAQFKLDLAKAYLAKHNLGDLGDNYVVHAPYLINLANGDSTKRERSFNFFLDELKRTNELGAKYFVLHPGSALNVKDKTQALDHLATELNRAISMTKDTIICLETMADKGQQICSKFEELRYVIDQISDKSRIGVCFDTCHVHDAGYDLAKTQELIDHFDQVIGLKYLYVIHLNDSKNPMGARKDRHANIGYGKIGFENLLNFIYHKEICNKIIILETPWIDDPIRGEVPLYKEEIEMIRNKKFVEGLVNEES | Cofactor: Binds 3 Zn(2+) ions.
Function: Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products.
Sequence ... |
P47477 | MPKLLGSFISFKAPNYFVQSAQDAIAIDATALMVFLGPPHSAYRVPFNKMQFSLGYELLKTKNINSNGLVVHAPYIINCASKDPLKQQNAISVLTNEIQLCNLAGAHYLVLHPGSAVAQTTNEALDNLVKVLNQVINKTKTTVICLETMAGKGNEIGRDLTELKYVIDRIVDKDRIGVCLDTCHFHDSGIDFSDLTGVFNTITTKLGFEFLKVIHLNESKNNCGSKKDRHANINAGMIGFENLMKFISHPQIKDLPIILETPSTSLNYPTIYREEISQIRSWFKTYQPDAN | Cofactor: Binds 3 Zn(2+) ions.
Function: Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products.
Sequence ... |
B8ZSC5 | MLIGSHVSSTDPLAAAEVEGADVVQIFLGNPQSWKAPTLRSDADVLKATALPVYVHAPYLINVASANSRVRIPSRKILQQTCDAAADIGAAAVVVHGGYVADDNDLEDGFQRWRKALDQLQTDVPVYLENTAGGDHAMARRFDTIARLWDVIGETGIGFCLDTCHAWAAGEGLIHVVDRIKAITGRIDLVHCNDSKDEAGSGRDRHANLGSGQIDAELLVAAVKVAGAPVICETAEEGRKDDIAFLREKTSG | Cofactor: Binds 3 Zn(2+) ions.
Function: Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products.
Sequence ... |
Q6MUC7 | MDKILLGCHVSMNKQNNYLVGSVNEAISYKANTFMIFTGPPQSTLRTNTNHLYINQMHELMNSYKIDAKDLVVHAPYIINIANSVDQNKWKFTVDFLIQEIKRCEEIKIPTLVLHPGSYTTGNYKDSLNQIIKALNIVSNYQVNVKIALETMSGKGTEVCSRLEDFKYILDNVKNKDKVGVCLDTCHLHDAGYDLSKWTEFKEQMKQNFSLDKVLCIHLNDSKNMISSHKDRHANIGYGYVGFDTLVNVVFDKDFSNISKILETPYIDKTPPYKIEIEDLLNKTFTNRL | Cofactor: Binds 3 Zn(2+) ions.
Function: Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products.
Sequence ... |
Q98PU8 | MIKLGSHVSFKSPNYLYDSIKESIKNGANCAMIFLGAPQNTKRVDFEKYQYEKYLKDFSNLIKPEDIVVHAPYIINPASLEKADFAISFLSSEIKRMDKAKFKYLVLHPGFYGKNNVKDSLDQLARSIQKIFEITKDSNVEIMLETMSGKGSEVGKSYEEILYVIDKVKSPRLGACLDTCHVWDAGYNINDYQVFKDELIKTGILKHIKVIHLNDSKNELGSHKDRHANIDKGLIGLKNLKRIVHDPIFENIPIILETPWTEKGPIYDQEIAMLLEK | Cofactor: Binds 3 Zn(2+) ions.
Function: Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products.
Sequence ... |
Q9YBF1 | MGDRCAPIKASGVLIGDSVLVTDVEQARSLYSCGYYGQPLDVEKPRGADFEGPLRLSLIESLYLAEKGVLEVAKPDGSSVGVEDLRTAVRGNPRFSMLYNIYRDLRERGFVVRSGLKFGSDFAVYRLGPGIDHAPFIVHAYSPEDNIDPVEIVRAGRLSHSVRKKFVFAVTRGGDVSYLMIDWFRP | Function: Endonuclease that removes tRNA introns. Cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and 5'-OH termini. Recognizes a pseudosymmetric substrate in which 2 bulged loops of 3 bases are separated by a s... |
O29362 | MIGGDFAVVKAKKSLERRGFGVKRGDKIYLHPLEVVYLQIKGIESFGELEDVLSWAESRMEDFSTYYFVYEDLRDRGNKVKIQGEFLLTKKPYLPISERKTIRMEEIAEKARNFDELRLAVVDEESEITYFRVYEPDMMGEQKEELPEIAGILSDEYVITKQTEIFSRYFYGSEKGDLVTLSLIESLYLLDLGKLNLLNADREELVKRAREVERNFDRRYEVYRNLKERGFVVKTGFKFGSEFRVYRKVESVDDLPHSEYLVDIADSREIRLIDLARAVRLAQNVRKRMVFAYGKNYLCFERVKV | Function: Endonuclease that removes tRNA introns. Cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and 5'-OH termini. Recognizes a pseudosymmetric substrate in which 2 bulged loops of 3 bases are separated by a s... |
O07118 | MQGRLEDGVVHLPGDARQRFHDSRGYGRPTGGDDLEVAPVEAAHLLSRDDIDGVDGMGLRELLARTGTTLDFVVYKDLRDRGFYLSPAREGWPGVADAADADFLVYPRGKGPWDGEVEHRVRVVGERESIPVSSLGEVVLAIVDEDGDLTYFDTEGDDPEGTAAEDLPADLDAELLSDRALVWDGVDRLYQRGFFGQRLYGRNADSGPLQLSLLEAAYLARADALAIDEADVVSRGRDVEGDRFDRRLAVYAALREAKTVPKSGFKFGSDFRVYTEFESVDDLSHSEFLVRVVAPDHTFVPRDLSLDVRLAGGVRKRMVF... | Cofactor: Divalent cations; Ca(2+) better than Mg(2+).
Function: Endonuclease that removes tRNA introns. Cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and 5'-OH termini. Recognizes a pseudosymmetric substrate ... |
Q8TGX1 | MKTQLEGDRVLAGKEAVAELYKTGYFGRPREDGLELSLVEAAYLQFRGKIEIELEGRKLDFRALFEQASLRQPNFELKYIVYKDLKERGYYVQPSAADFRVYPRGSHPGKSAAKIFVHVLSERQPLPVKLLQDSVISAENVHKQFILAVVDEESDLTFYEIKTASPQGEMPEPYPEVKTDATFLEDRVIAWDAEASGALYAGGFYGKMLDPERLQLSLVESLYLFSRGIIVVRDRKDRIFSFDEFVEKASEIESSFLRKYGAYKALRDSGHVVKTGFKFGTHFRVYRKVESIEKIPHSEYLVNVIPSDYEFRLPVMSGAV... | Function: Endonuclease that removes tRNA introns. Cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and 5'-OH termini. Recognizes a pseudosymmetric substrate in which 2 bulged loops of 3 bases are separated by a s... |
Q58819 | MVRDKMGKKITGLLDGDRVIVFDKNGISKLSARHYGNVEGNFLSLSLVEALYLINLGWLEVKYKDNKPLSFEELYEYARNVEERLCLKYLVYKDLRTRGYIVKTGLKYGADFRLYERGANIDKEHSVYLVKVFPEDSSFLLSELTGFVRVAHSVRKKLLIAIVDADGDIVYYNMTYVKP | Function: Endonuclease that removes tRNA introns. Cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and 5'-OH termini. Recognizes a pseudosymmetric substrate in which 2 bulged loops of 3 bases are separated by a s... |
Q8TGZ7 | MLCAGNGGKELPRAKVFEGGSLVSKDYEDLKRRYFGTEHGNVLFLDPFETVYLTEKGEIDPETPEGEPMSVEELLSFFERRRPGFRAGYVVYRDLTERGYVVKSGFKYGGRFRVYEEDPDREHSKYVVRVVEPDTELSTRDVLRATRLAHSVRKDFVLAVVEDVEEPRIEYVMWRWKRL | Function: Endonuclease that removes tRNA introns. Cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and 5'-OH termini. Recognizes a pseudosymmetric substrate in which 2 bulged loops of 3 bases are separated by a s... |
O07165 | MRVEGQLGDEVVTIKATSIARRLHGKSHYGKMYEDRLQLSLIEAAYLMERGKLKLMKDDDEVSPEEFISLLGERGLYSKYLVYRDLRNRGYIVKTGFKYGAEFRLYERGGAPGRTHSAYLVRVISENDTIHALDFSSYVRVAHGVNKKLLMAFLDDEEDITYYLVDWIRP | Function: Endonuclease that removes tRNA introns. Cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and 5'-OH termini. Recognizes a pseudosymmetric substrate in which 2 bulged loops of 3 bases are separated by a s... |
Q7Q9C0 | MAAVVALGANVLSAKSIICDIEGTTTSISFVKDTLFPYALKHVEGYLKNNWNEEATKTVVTALREQAEEDKKAEVEGVVPIPTGDSEDIIPEIVKNVEWQMSLDRKTGSLKTLQGLVWAKGYKDGSIKGHVYDDVQKAFEQWTENGRKIYIYSSGSVDAQKLLFEHSEQGDLLKYLSGHYDTKIGAKREKESYTSILKNIESSPEEALFLTDVYAEAKAAKEAGLNVVLLDRPGNSELSEEERKDFPVIATFSDLSFAAETKEENGGATNGKRKIEETNDDVAEEDKAQVYPNKK | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy... |
Q753F5 | MEEDYGVFILDVEGTVCPIAFVREQLFPYFLDKVEELINNADETERDLLADMQSRHGGAAAASLLRQLVAEDVKDPALKALQGRVWERGYASGEITAPVYADAVRFIQRNAGRVYIYSSGSVQAQRLLFGHVSNPSGDGVLDLTGHLAGFFDIPAAGRKTEAKSYERILAAIGLERQPGAAIFVSDSVAELDAASASGLSVRLAVRPGNERVSGARYTTLTDFEGL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy... |
Q0VD27 | MVVLSVPAEVTVILLDIEGTTTPIAFVKDILFPYVKENVEEYLQAHWEEEECQQDVRLLRKQAEEDSHLDGAVPIPAASGNGADDPQWMIQAVVDNVYWQMSLDRKTTALKQLQGHMWRAAFKAGHMKAEFFEDVVPAVRKWREAGMKVYVYSSGSVEAQKLLFGHSTEGDILELVDGHFDTKIGHKVESESYQKIASSIGCSTNNILFLTDVSREASAAEEAGVHVAVVVRPGNAGLTDDEKTHFSLITSFSELYLPSST | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy... |
C3XR70 | MSDSRLRRRQGTAGTDNKRRADGPHDISGLLDGVSVVLLDIEGTTTPITFVKDELFPYVCSHVRQHLEEHWKEEECQEDIAALRKQAKEDKEMDGVVLIPECTTKDDDEEARKKVLSAVVDNVLLNMDADRKVTALKQLQGHMWRAAYQTGKIKGEYVKLTFADVVPAIRGWLETGRQVYIYSSGSVEAQKLLFGFSTEGDLLELFSGHFDTTTGLKVETESYRRIAKTVGCDPANILFLTDVVREAKPSREAGMKTCLTVRPGNAPLTEEDWANYPVIKSFSELACDVSPTKMRSRGKAAT | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy... |
A8Y461 | MTNTTTIQFNALLLDIEGTITSISFVKDELFPYAFENVGKYLEEHYDKPATQIIIEDLRRLAEQQLETDADVVKIRERKQECIEDVTKNVRHWIKRDKKLTPMKALQGLIWEEAYQRGYVKGHVYPDVLPILKIIESRQIPIYIYSSGSVHAQKLLFANSVEGDMTKILYGYFDTNIGLKGETSSYTKISEQIGVPEKDILFLTDVEAEAAAASKAGLQTRLVIRPGNATLTQEAKNAYGTIHTLEEIL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy... |
Q21012 | MTTTTIQFNALLLDIEGTITSISFVKDELFPYAFENVGNYLEEHYDNPATQIIVEDLRHIADQQAENDVAVVRIREPRKECIEDVTKNVRHWIKRDKKLTPMKALQGLIWEEAYQRGDVKGHVYPDVLPVLKIVENRKIPIYIYSSGSVHAQKLLFANSIEGDMTKILYGYFDTNIGLKGESNSYTKISERIKIPPSEILFLTDVEAEAAAAKKAGLQTKLVVRPGNAGLTQEAINAYGTIESLEEIL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy... |
Q5AM80 | MTTTAKTDDIPIDTVILDIEGTVCPITFVKDTLFPYFIEKLPSILDKFQYPLSNTSASSDDQVLNILKQLPDNITKSSESIYKHFKNLVDQDIKDPILKSLQGLIWKQGYEKNELQAPIYQDSIEFIESFPTKSSTNNKIYIYSSGSIKAQILLFGHVKSTTTTITNEVIDLNPKLNGYFDITTAGFKNQSNSYKKILQEINKSSTPKSVLFLSDNINEVNAAIEAGMKSYIVIRPGNPPIDDDDDGNDDKINHKIIYSLDELDL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy... |
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