ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
O13737 | MTYLSRSYSFYAAYHSNPVNIKIHQVCIPLLLLTALVLLHNFVITLINSKLQINVAHLVGLAYQIFYVTLDPLDGLLYSPVLYLFSYILPSKLFTIFSRSLVNRSAAVVHVICWILQFIGHGVFEKRKPALLDNLIQSLFIAPLFAFLETGPFVGYYPSVVSKIRANIKLKDVGENYPNLSEFLFPPSMVEDAVSGVVEDASQLSYCIRPLRLSDIDDGIVF | Function: Dioxygenase that catalyzes the alpha-oxidation of 2-hydroxy fatty acids in an iron-dependent manner (By similarity). Involved in metabolism of phytosphingosine and is required for proper endoplasmic reticulum stress response (By similarity).
Catalytic Activity: (R)-2-hydroxyhexadecanoate + O2 = CO2 + H2O + pe... |
A0A1S4BDC4 | MATTKQKVTAPSPSPSSSTASCCPSTSILRREATAAIAVVGDGLQNWTNIPSVDEKQKKTASSALASLPTTEPLSTNTSTKGIQIMTRAQTCHPLDPLSAAEISVAVATVRAAGETPEVRDGMRFIEVVLVEPDKSVVALADAYFFPPFQSSLMPRTKGGSQIPTKLPPRRARLIVYNKKTNETSIWIVELNEVHAAARGGHHRGKVIASNVVPDVQPPIDAQEYAECEAVVKSYPPFRDAMRRRGIDDLDLVMVDPWCVGYHSEADAPSRRLAKPLVFCRTESDCPMENGYARPVEGIYVLVDVQNMQIIEFEDRKLVP... | Cofactor: Binds 1 copper ion per subunit (By similarity). Can also use zinc ion as cofactor (By similarity).
Function: Involved in the biosynthesis of pyridine alkaloid natural products, leading mainly to the production of anabasine, anatabine, nicotine and nornicotine, effective deterrents against herbivores with anti... |
P25338 | MGEGLLDLRSQLGFYKFYHHNPKNVLIHSIFVPTILFSGSCMLHRVKIYQSISLTAVLSVLFSIFYCLLYLPTGLLAGVLLLLLNLALIDHRVDLTFKQELGLFTIGWIFQFVGHGVFEKRRPALIDNLVQSLVLAPYFIMFEFLFKLGFMPRLKATLEHDLEIKQRNLRMQRQ | Function: Dioxygenase that catalyzes the alpha-oxidation of 2-hydroxy fatty acids in an iron-dependent manner . Involved in metabolism of phytosphingosine and is required for proper endoplasmic reticulum stress response .
Catalytic Activity: (R)-2-hydroxyhexadecanoate + O2 = CO2 + H2O + pentadecanoate
Location Topology... |
O00566 | MAPQVWRRRTLERCLTEVGKATGRPECFLTIQEGLASKFTSLTKVLYDFNKILENGRIHGSPLQKLVIENFDDEQIWQQLELQNEPILQYFQNAVSETINDEDISLLPESEEQEREEDGSEIEADDKEDLEDLEEEEVSDMGNDDPEMGERAENSSKSDLRKSPVFSDEDSDLDFDISKLEQQSKVQNKGQGKPREKSIVDDKFFKLSEMEAYLENIEKEEERKDDNDEEEEDIDFFEDIDSDEDEGGLFGSKKLKSGKSSRNLKYKDFFDPVESDEDITNVHDDELDSNKEDDEIAEEEAEELSISETDEDDDLQENED... | Function: Component of the 60-80S U3 small nucleolar ribonucleoprotein (U3 snoRNP). Required for the early cleavages during pre-18S ribosomal RNA processing . Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus... |
Q9WV34 | MPVAATNSESAMQQVLDNLGSLPNATGAAELDLIFLRGIMESPIVRSLAKAHERLEETKLEAVRDNNLELVQEILRDLAELAEQSSTAAELARILQEPHFQSLLETHDSVASKTYETPPPSPGLDPTFSNQPVPPDAVRMVGIRKTAGEHLGVTFRVEGGELVIARILHGGMVAQQGLLHVGDIIKEVNGQPVGSDPRALQELLRSASGSVILKILPSYQEPHLPRQVFVKCHFDYDPARDSLSPCKEAGLRFNAGDLLQIVNQDDANWWQACHVEGGSAGLIPSQLLEEKRKAFVKRDLELTPTSGTLCGSLSGKKKKR... | Function: Postsynaptic MAGUK scaffold protein that links CADM1 cell adhesion molecules to core components of the postsynaptic density (By similarity). In CA1 pyramidal neurons, required for synaptic KCNN2-containing channel function and long-term potentiation expression . Seems to negatively regulate SRC function in ep... |
Q89XM4 | MPAASDRETDVVLIGAGIMSATLGAFLKELEPSLTIQMLETLDDCAQESSDSWNNAGTGHAANCEMNYTPQRPDGSIDISKALQVNVEFDLSRQFWSYLIGRGAIADPRSFIHPVPHMSFVHGTENVEFLRKRFKAMSAHHCYEGMEHTEDPRKIAEWAPLVMDGRSGDEPVAATRIITGTDVDYGALTHLLVGHLVSQPGCAVHYNSCVTGLVREQGGRWRIEVRDTASGETRSVRAKFVFIGAGGGALPLLEKSGLPEARGYGGFPVSGIWLRCDDPEINKRHHAKVYGKAAVGSPPMSVPHLDTRVIGGKHSLLFGP... | Catalytic Activity: (S)-malate + a quinone = a quinol + oxaloacetate
Sequence Mass (Da): 55455
Sequence Length: 512
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; oxaloacetate from (S)-malate (quinone route): step 1/1.
EC: 1.1.5.4
|
P56954 | MSQQEFDVLVIGAGISGAALFYELARYTNIKNIALIEKYNTAATLNSKGTSNSQTIHCGDIETNYTLEKARKVKRTADMIVKYGLMQNAQNNFMFSHQKMALAVGDIECDYMKKRYEEFKELYPYIKFFDKAKIKQIEPKVVLGEDCNQDRPENICAMGVESGEVFTTVDFGKMSINLIEQAQKQNKNTFVAFNQEIIHIEKKDDIFILKTSNHQEYHAKSVVVNAGAHSLYLAHKMNLGMDKSCWPVAGSFYLTKQKLLNGKVYMVQNPKLPFAALHGDPDLLADMNTRFGPTALVIPKLERYHGLKSVPEFFEALKLD... | Cofactor: The FAD is tightly bound.
Function: Catalyzes oxidation of malate to oxaloacetate in the citric acid cycle. Donates electrons to quinones of the electron transfer chain (By similarity).
Catalytic Activity: (S)-malate + a quinone = a quinol + oxaloacetate
Sequence Mass (Da): 50586
Sequence Length: 448
Pathway:... |
C3PH30 | MSSDKKTAQVVDEVEVALIGAGIMSATLGAMLRELEPSWTQMVFERLDGPALESSSPWNNAGTGHSALCELNYTPEKNGRIDISKALNINEKFQVSRQFWSHQLNNGILTDPKAFINPVPHVSFAQGSIQVDYLKRRFDALKDNHMFPNMQFSDDDATFQEKLPLMSQGRDFNSQKVAISWTDAGTDVNFGALAKQFFTAAKAAGTEIRYGHEVVDIKREGSKWRVVAKNLHTGDYQAVHAKFVFVGAGGYALDLLRKAGVREVSGFAGFPVSGLWLRSKNPELVKQHHAKVYGKAAVGAPPMSVPHLDTRVIDGEEGLL... | Catalytic Activity: (S)-malate + a quinone = a quinol + oxaloacetate
Sequence Mass (Da): 55235
Sequence Length: 500
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; oxaloacetate from (S)-malate (quinone route): step 1/1.
EC: 1.1.5.4
|
Q8FP91 | MIVVFRHESTIGHVFLTGGDYHSGAGGFSRAPSTAVTYVAPWLRTSQFPGGDRGLSGGGQRGRLWAYGPGYVEGIYVPPYQQAYTTELRTTCTCTPSRSRPGQVFTTCRSAIHPCAGPRVDSCVQHAGCVRQTTRGDKRKLNMSDSPKNAQKVTDEADVVLVGAGIMSATLGAMLRQLEPSWSQVIFERLDGAAQESSSPWNNAGTGHSALCELNYTPEKNGKIDISKAVNINEKFQVSRQFWAHQVEEGILPDPKEFINAVPHVSFGHGADQVAYIKNRYNALKDHPLFPGMQYADDEETFTEKLPLMAQGRDFSDPVA... | Catalytic Activity: (S)-malate + a quinone = a quinol + oxaloacetate
Sequence Mass (Da): 70126
Sequence Length: 642
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; oxaloacetate from (S)-malate (quinone route): step 1/1.
EC: 1.1.5.4
|
O69282 | MSDSPKNAPRITDEADVVLIGAGIMSSTLGAMLRQLEPSWTQIVFERLDGPAQESSSPWNNAGTGHSALCELNYTPEVKGKVEIAKAVGINEKFQVSRQFWSHLVEEGVLSDPKEFINPVPHVSFGQGADQVAYIKARYEALKDHPLFQGMTYADDEATFTEKLPLMAKGRDFSDPVAISWIDEGTDINYGAQTKQYLDAAEVEGTEIRYGHEVKSIKADGAKWIVTVKNVHTGDTKTIKANFVFVGAGGYALDLLRSAGIPQVKGFAGFPVSGLWLRCTNEELIEQHAAKVYGKASVGAPPMSVPHLDTRVIEGEKGLL... | Cofactor: The FAD is tightly bound.
Catalytic Activity: (S)-malate + a quinone = a quinol + oxaloacetate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 54832
Sequence Length: 500
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; oxaloacetate from (S)-malate (quinone route): step 1/1.
Subce... |
A7MNG1 | MSKITLSRKHAPAFSLIALLVSSAAYAENTTEKTDVLLIGGGIMSASLGTVLQEIQPDWKQLMVEKLDGVALESSNGWNNAGTGHSANMELNYTPEREDGSIDVTKALEINEAFMISRQFWSSQVKRGVLNDPHSFINSTPHMSFVWGDKNVEYLTKRYQALQQTTLFQGMQFSTDQQQIKKWAPLIIEGRDPKQKVAATWTPVGTDVNYGEITRQLVGSLKKTSNFKLETSSEVTDFKRNADNSWHVTITDVKSGKEHAVDAKYVFIGAGGGALKLLQKTGIPEADNYAGFPVGGSFLVSENPEIARQHGEKVYGQASV... | Catalytic Activity: (S)-malate + a quinone = a quinol + oxaloacetate
Sequence Mass (Da): 60653
Sequence Length: 552
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; oxaloacetate from (S)-malate (quinone route): step 1/1.
EC: 1.1.5.4
|
Q03521 | MLEQVILFTILMGFLISVLLSPILIPFLRRLKFGQSIREEGPKSHQKKSGTPTMGGVMIILSIIVTTIVMTQKFSEISPEMVLLLFVTLGYGLLGFLDDYIKVVMKRNLGLTSKQKLIGQIIIAVVFYAVYHYYNFATDIRIPGTDLSFDLGWAYFILVLFMLVGGSNAVNLTDGLDGLLSGTAAIAFGAFAILAWNQSQYDVAIFSVAVVGAVLGFLVFNAHPAKVFMGDTGSLALGGAIVTIAILTKLEILLVIIGGVFVIETLSVILQVISFKTTGKRIFKMSPLHHHYELVGWSEWRVVVTFWAAGLLLAVLGIYI... | Function: Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known ... |
Q8A255 | MLYYLFEWLHKLNFPGAGMFGYTSFRALMAVILALLISSIWGDKFINLLKKKQITETQRDAKTDPFGVNKVGVPSMGGVIIIVAILIPCLLLGKLDNIYMILMLITTVWLGSLGFADDYIKIFKKDKEGLHGKFKIIGQVGLGLIVGLTLYLSPDVVIRENIEVHTPGQEMEVIHGTNDLKSTQTTIPFFKSNNLDYADLVGFMGEHAQTAGWFLFVIITIFVVTAVSNGANLNDGMDGMAAGNSAIIGATLGILAYVSSHIEFASYLNIMYIPGSEELVIYICAFIGALIGFLWYNAYPAQVFMGDTGSLTIGGIIAVF... | Function: Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known ... |
Q9RTD0 | MMVVAALLSWFLLGLFIHYSKKFGWGQPIRQDGPQTHLAKEGTPTAGGVAFVLALLLVFVGLLAFGGIGQANLSREVMILLAALGMGVVGGIDDFLKIRSRKFGGKKELLAREKFPLQVLVALLFAGFAAPLASHQLLPGFMSIGGYPIFDMLFIAFVMVGSVNAFNFTDGLDGLLAGVGMIVLLPLVAVSPIAALMVAVLLGFLWFNAHPARVFMGDMGSHAIGAVAAGAYALYSDVWLLPIAAIIPVAAVLSVVIQVASVRLRKRKVFKMSPIQHHFELSGWPETHVTLRFWVVTGIATALTWWLMGGRP | Function: Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known ... |
C0Q8P0 | MLFHYLYPLHTEISFFNLFRYITFRTIYGGLTAFLICFLLGPWVINRLSRMQIGQFIQNDGPETHFEKEGTPTMGGILILFSLGVSTLLWADLTNHYILITLLSMLLFGAIGFIDDYLMQVKKRNMGFTARGKFLVQIMAGLVISYLVYLCPDFDTSLSIPFLKNFTPDLGIWYIPFATLVIVGTSNAVNLTDGLDGLAIGPIIIAGVTYMIFAYVASHITIASYLQVKHIASCGEITIVCGILAGAGLGFLWFNAHPAQVFMGDTGSIPLGAILGTIAVITKQEILLLVVGGLFVIEALSVIIQVGYFKLSKGKRVFRM... | Function: Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known ... |
Q24TE3 | MWERIFLAAALALTITLILGPLMIPVLRVMKFGQTIREEGPKRHLAKAGTPTMGGIIFLVGIVVSALVMAEKPTSLEMVMVISAMLGYGLIGFIDDFIKVVLHRSLGLRAYQKLIGQIALALLLTWGANRYLGRGTDLVIPFTSIHLELGLFYYPFVSFIIVGITNAVNLTDGLDGLAAGTTLFSMLSYVSIATLAASQGGGVAILAYESDLAVFAAAAVGGCFGFLRFNKNPARVFMGDTGSLALGGALVGLAVLTKTELILLIIGGVYVVEAISVILQVFSYQTTGKRIFRMSPLHHHFELGGWNEWRVVMVFWLASL... | Function: Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known ... |
A8ZXW6 | MLYHLLYPLHTHISFFNVFQYITFRTIYASLTAFLICFLLGPFTIRTLARMQIGQYIRELGPQSHQGKAGTPTMGGLLIVFSVLVACLLWADLTNRYIWVTLAALAGFTTIGFIDDYLMQIKKRNKGLSARAKFLAQTVLAAGICLLIFAASDTNTVLLVPFFKRVAPDLGLFYIVLGVFVIVGTSNAVNLTDGLDGLVTGPLVISFVAYMVFAYVAGNAIISNYLQVIHVPGSGEVTVFCGAMAGGLMGFLWFNAYPAQIFMGDVGSLSLGGALGTVAIITKQEILLTLVGGLFVVETLSVIFQVGFFKATKGRRIFRM... | Function: Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known ... |
A4J2A8 | MDYTVVWLAAGISFLVTLVLGPVTIPLLQRLKFGQTIRAEGPAAHMAKTGTPTMGGIMFLIGIAVAGAVLLVSNIPGRAEGLVVLAVTLGYGLIGFLDDFIKVVLKRNLGLKAREKILGQLVFATVLAVVAVFKLGRGTDYIIPFSSGISFDLGWWPFFFLTLFVLLGTSNGVNLTDGLDGLASGATVFTATAFAILALVTGKIGLAIVLAAVVGGCLGFLFYNRHPAKVFMGDTGSLALGGALGAGAVVTRNELLLVVIGGLYVLETLSVIIQVISFKTTGRRVFRMSPLHHHFELSGWSERKVVRNFWLLSFLFSLVG... | Function: Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known ... |
Q728U5 | MLYNLLYPLSSDITVFNVFRYITFRSAWALATALLVSIVVGPRFIAWLQRLKCRQFIHEDVTCHMSKAGTPTMGGLLIGFAVTFSVLLWADLRNPYIWLTLLVFTGFGFIGFLDDYTKLRRRNNKGLTASAKFLWQVGVAVAAMYLLVQLPAYSTKLAFPFFKGLTPDLGWLYIPFAVAVMVGSSNGVNLTDGLDGLAIGPTIVAGIVFSIFIYVAGHSQIAGYLQVPYVPGVGEVAVFCGALVGAGLGFLWFNAYPAQVFMGDVGSLSLGGTLGFLAVLCKQELLLLVVGGLFVVETLSVILQVGYFKFSGGKRIFRMA... | Function: Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known ... |
B8E328 | MNIILFTSLVAFFVFLLILKYWINFQKSKGIGKYIRKEGPSSHFQKSGTPVMGGIIFLIVSIPFLFFKETFFPSLSTILFGLLGLLDDFKLMVNKDYGIRPLRKIFLSFIITLLLYIFSFHDYKIYWGSKLIISSRIFYVILFFVVFIAVPNAINLTDGLDGLAGGTSLITLFFFLIYNFQFNNELTLEISLMITALIAFLWFNSHPAEIFMGDVGAFALGGFIASLSIINKVELLLVFLGGIFLIESLSVFIQVFFYKWKKRRVFLMSPLHHHFELKGWKETKVVWRFYIIHLIMMIGGIILWNLT | Function: Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known ... |
B2J5G4 | MDAKLSPEQGLNISGIALASLLAVGLGTTAFFLDSMANRLPWQSMSLTLPLLLCAMGSGVVGFWVIPLLQALKTGQIIREDGPQAHLKKAGTPTMGGIFFIPVGVIIACILSNFATDVLAVSALTTSYGFIGWLDDWQILRRKSNKGISPRTKLALQVGFAAVFCLWLMFNQPSNITNIALPWVSFTLPLGFLFWPLAGFVLVAESNATNLTDGIDGLAAGTVAIALLALGALIAPTAPGLMVFCAALSGGCLGFLAHNRNPARVFMGDTGSLALGGALAAVALLTNTLVALFILSGIFFVETLSVMAQVSYYKATKGPD... | Function: Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known ... |
Q04ES8 | MIFQIFSALLIGFLIAFAAIPFLIGYLTSRGEVGVERSGKHGFGVDTSGKNGTPSMGGVTFILSSLFATLIVMFLFRLDSLNIIFFIVSFLSFGLIGLIDDALKVFYHRDEGFRFIPKLIAQIISAALITIILVAVHIPDKLTFPFFRALPLYFLVQFIFYLVWFVGWSNAANFVDGIDGLLAGIALLIFAGYGIIGIKENQNLMVIFDFSVVGSLLAYFIFNRPKAKIFMGDCGSMALGAGMAINAIFLQHPWSLLWFGLILALDTTSVMIQVLVYHFFHVRVFPVAPLQHSFQRAGWSEWKIDSLFWTIQLIITMIGV... | Function: Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known ... |
B1ZU32 | MLSHLADLQDYFGPLRLLRYITVRTLLAAVTSLTIGFVIAPWLIAKFRELKLGHGYIDDRTGALGATYFDKKNTPTMGGLIIFLSVFTSAALWAAPNIWVFVSLFVYAALTIPGWRDDYLKVVHKNRNGISSWEKIGWQSLATVVALGLLLWHPASAQKIREFWVPFVKYPLIPHMHWAVLLVLIYLWIVGFSNAINLTDGLDGLAIGCTIPVALVFGIMAYVADHVFLSQYLLTSHVPGTGELAVICGALIGGCMAFLWYNCHPAEVFMGDTGSLALGGLIGVMAFMIHQPLTLVIVGGVFVAEMLSVVVQVGVFKITK... | Function: Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known ... |
B3CVD3 | MLYNLLVSHINSCYIFSIFYNVIVRSGIAILLSFSISFSLIPILIKYFKYWKNLAQPIRNLGHKSHIAKAGTPTMGGIAIIFSIIISTLMLADYKNIYVLTTIFGMLSLAILGLIDDYQKVTKKNTKGINATCKLISQIMVSIICCMIVNYNLNSEIANHLIIPFFKKLTIDLSIFYIPFALFIIIGSSNAVNLTDGLDGLVTVPIIIVSFCLGLMCYLADNAQYININHLQILHVQQASELTVLCSAIIGASLGFLWYNIQPAKIFMGDVGSLSLGGAIGIISVISKNEIRLGIIGGLFVIEALSAIIQIYSIRYLGGK... | Function: Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known ... |
Q6MBS3 | MILFAIDYLERVWTLKVPSVFSYYSTRMILAAITSLLLSIFLGPYFIRKLYELKIGQSIRKEDCPLLGQLHEKKQNTPTMGGILILSSMLVSLVLWMDLTHIFTLILFVTTVFLGLIGGRDDYLKLKYKNTKGMSARGKLFFQFVLSAAIASYFLLSSVNEMFEKWTWFQPPVIKEQIVVKNSETLQEMPSQTKSISLKEYASRLYIPFFKEPVVTFGGISLILMAFFIFFVITGSSNAANLTDGLDGLLAGCLVTAAGSLCLIAFVSNHVDIARYLNILYIEGSGEIAIYLCALIGASLGFLWYNGYPAQVFMGDTGSL... | Function: Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known ... |
Q67Q50 | MEQTTLLRLAGAGLTALAGALALGPVVIPLMRRLRAGQTIRAEMSARHQAKAGTPTMGGVIFIIPAILATLIFAPRSGDALPRLIIALVLTVGHGLVGFADDYIKVVLKRSLGLRARDKLLAQVGLAAVLGYGAVEVLGLGTAVTLPVLNLTLELGRPLYYLLVLIMVWGTASAVNFADGLDGLLGGLSVITFSFYGLVVALALGQTDMAVLGTALVGGVLGFLHYNRHPARIFMGDVGSFALGGALAALAVLTKTEFLLVIVGAVYVIEVISVILQVLSFRLTGRRIFKMAPLHHHFELLGWSEGQVLRLFWGAGLLFT... | Function: Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known ... |
Q9YFY8 | MPKVLHVADVHLGARPYGLEERRDDIFRSFEFVVETALKDRPDAVLIAGDLFDKPKLPLRDVKQAVELVRALTDAGIPVLAAHGEHDTPSVRDETLLSLMEASLDGFKAPLYRSGMRPGDFVVDLGSLKVAVVPFFKVPLEERRRLTLRFLREFDQISRTSSGTLVLLAHMSLDAEMQFDAVASPSDLPSGAKYAALGHLHAPRIRLDAPTPYAYPGVLDPLKVEEINTPGSPLYVDLSGDAPIIEKVKVPRRPQYRIEVDIGDGGSIYNAVNRGLRRVLANVRASREDWLKPLIHVIIKSDKPISKARVIAEARKAAGG... | Cofactor: Binds 2 manganese ions per subunit.
Function: Part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair. The complex may facilitate opening of the processed DNA ends to aid in the recruitment of HerA and NurA. Mre11 binds to DSB ends and has both double-stra... |
Q9XGM2 | MSREDFSDTLRVLVATDCHLGYMEKDEIRRHDSFKAFEEICSIAEEKQVDFLLLGGDLFHENKPSRTTLVKAIEILRRHCLNDKPVQFQVVSDQTVNFQNAFGQVNYEDPHFNVGLPVFSIHGNHDDPAGVDNLSAIDILSACNLVNYFGKMVLGGSGVGQITLYPILMKKGSTTVALYGLGNIRDERLNRMFQTPHAVQWMRPEVQEGCDVSDWFNILVLHQNRVKSNPKNAISEHFLPRFLDFIVWGHEHECLIDPQEVSGMGFHITQPGSSVATSLIDGESKPKHVLLLEIKGNQYRPTKIPLTSVRPFEYTEIVLK... | Cofactor: Binds 2 manganese ions per subunit.
Function: Involved in DNA double-strand break repair (DSBR). Possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity. Also involved in meiotic DSB processing (By similarity).
Sequence Mass (Da): 80291
Sequence Length: 720
Subcellu... |
O29231 | MKFAHIADVHLGYEQYNQPWRAEDFAKAFKVIAEKAVESNADFVVIAGDLFHRSLPSPRTIKEAVETLWMFRKENIPVFAVEGNHDKTSRDISAYHLLESLGLLNVLGLRRNPVRGENVESLRIQNVYLVKGVVDDVEILGDRHRSKWQLEKVLPLLKPQSDKSVLVLHQAVKEVVDIDLDMAYELTINDLPEASYYAFGHIHLPKIYEFDGKAIAYPGSVERYDLREASKIVRYRDELVLKDGIRKGFILVKNFRPEFVEIETRELYDVEIEDESVEGLEKKFLEVLGRADKEGIMVAKLKSSDAVDVRRLSEVAAKRV... | Cofactor: Binds 2 manganese ions per subunit.
Function: Part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair. The complex may facilitate opening of the processed DNA ends to aid in the recruitment of HerA and NurA. Mre11 binds to DSB ends and has both double-stra... |
Q9IAM7 | MSAVSLQDDEDTFKILIATDIHLGYLEKDAVRGNDTFVTFNEILEHAQKNEVDFILLGGDLFHENKPSRKTIHTCLESLRKYCMGDRPVSFEVLSDQAVNFQLSKFPWVNYQDENLNIFMPIFSIHGNHDDPTGVDALCALDILSCAGLLNHFGRSTSVEKIDISPILLRKGRTKIALYGLGAIPDERLYRMFVNKQVTMLRPKEDEDSWFNMFVIHQNRSKHGATNYIPEQFLDDFINLAVWGHEHECKITPAQNEQQHFYVTQPGSSVVTSLSPGEAVKKHIGLLRVKGKKMKMQRIALETVRTFYMEDVVLADHPEL... | Function: Component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis. The complex possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by MRE11. RAD50 ma... |
Q9HRW4 | MARVIHTGDTHLGYQQYHAPQRRQDFLDAFDAVITDAIDEGVDAVVHAGDLYHDRQPGLRDILDTIALLRPLQDADIPFLAVVGNHEGTRDAQWLDLFETLGLAERLDDSPRVVADTAFYGLDYVPQSKRDDHDYTVADHDADHAALVSHGLFTPFPYANWDLDAVLADATVEFDAVLLGDNHTPDTAQLGDTWVTYCGSTERASASERDPRGYNIVSFSSDATTDVAISRKSLNTREFVFVDADLGPTDGTAFIQERLRERALDDAVVVVTITGDGDTVTPAEIERFGDDRGALLTRVNDRREFDTGDDAPDVDVSFAD... | Cofactor: Binds 2 manganese ions per subunit.
Function: Part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair. Mre11 binds to DSB ends and has both double-stranded 3'-5' exonuclease activity and single-stranded endonuclease activity.
Sequence Mass (Da): 42685
Sequ... |
D4GUK0 | MTRVIHTGDTHLGYQQYHSPERRQDFLDAFERVVADALDGDVDAVVHAGDLYHDRRPELPDLLGTLAALRRLDDAGIPFLAIVGNHESTRGGQWLDLFERLGLATRLGRDPHVVGGVAFYGLDHVPRSRRDELDYQFDPVDADRAVLVAHGLFTPFAHADWETETVLAESNVDFDAVLLGDNHVPDTAELDGTWVTYCGSTERASASERDPRGYNLVEFTPDAVDIRRRTLETRPFAFVEVDLAGDEGIERVRQRVREFDLEDAVVIVELRGEGETVTPAAVESFAVEEGALVARVNDKRDIDDDGDLATDVTFADPDDA... | Cofactor: Binds 2 manganese ions per subunit.
Function: Part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair. Mre11 binds to DSB ends and has both double-stranded 3'-5' exonuclease activity and single-stranded endonuclease activity (By similarity). In polyploid o... |
P49959 | MSTADALDDENTFKILVATDIHLGFMEKDAVRGNDTFVTLDEILRLAQENEVDFILLGGDLFHENKPSRKTLHTCLELLRKYCMGDRPVQFEILSDQSVNFGFSKFPWVNYQDGNLNISIPVFSIHGNHDDPTGADALCALDILSCAGFVNHFGRSMSVEKIDISPVLLQKGSTKIALYGLGSIPDERLYRMFVNKKVTMLRPKEDENSWFNLFVIHQNRSKHGSTNFIPEQFLDDFIDLVIWGHEHECKIAPTKNEQQLFYISQPGSSVVTSLSPGEAVKKHVGLLRIKGRKMNMHKIPLHTVRQFFMEDIVLANHPDI... | Function: Component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis . The complex possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by MRE11 . RAD50 ... |
Q8TRL2 | MDREIRILHTADTHLGYRQYHSEVRRQDFFKAFETVIQDAVDMQVDAVVHAGDLFDSRNPTLEDLLETMNILSRLKAVDIPFFGIVGNHESKQNTQWLDLFEEMGLAERLGKTPKLVGNTTIYGIDSVPKSKIPLYDYSGFELPDSLPENCKKLLVMHQIVQPFPYADWDCAEVLENLPFKVDAILLGDYHKYEKIKVGEEETWATYSGSTERNSASENEPRSYNIITLSGEGLEISRRTIPTRNFLFITAKIDGEEKPYEQIFSAINEHLEEIPESVVFLDISGNSDSVLSFSEIEEYLLSKGALVSKVKDARIKETLP... | Cofactor: Binds 2 manganese ions per subunit.
Function: Part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair. The complex may facilitate opening of the processed DNA ends to aid in the recruitment of HerA and NurA. Mre11 binds to DSB ends and has both double-stra... |
Q58719 | MMFVHIADNHLGYRQYNLDDREKDIYDSFKLCIKKILEIKPDVVLHSGDLFNDLRPPVKALRIAMQAFKKLHENNIKVYIVAGNHEMPRRLGEESPLALLKDYVKILDGKDVINVNGEEIFICGTYYHKKSKREEMLDKLKNFESEAKNYKKKILMLHQGINPYIPLDYELEHFDLPKFSYYALGHIHKRILERFNDGILAYSGSTEIIYRNEYEDYKKEGKGFYLVDFSGNDLDISDIEKIDIECREFVEVNIKDKKSFNEAVNKIERCKNKPVVFGKIKREFKPWFDTLKDKILINKAIIVDDEFIDMPDNVDIESLN... | Cofactor: Binds 2 manganese ions per subunit.
Function: Part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair. The complex may facilitate opening of the processed DNA ends to aid in the recruitment of HerA and NurA. Mre11 binds to DSB ends and has both double-stra... |
Q8TXI3 | MRMAHVADVHLGHALMNLRSREEAVMETFERLMEEVRECSVDVLVIAGDLFEHARPKTEALYLAVEKLSELKEDGVEIVATAGNHEIRRRKGAVSPISVLERMGLVRHLYYSERRPERHRYTATFDGVRVTFHGLQYLPKNSFVERAKVIRAKYRPDPEADVNVAIFHQALPGTIPDESEIVEPAYFPEGHDYYAMGHVHVPSREEKIHGSPAPYPGSPEPLTFLEVKDERGAHKRRGFFLVEFDRGGLVEYEFVEVEWSRELSVVEVSGERWEEELRRRVRRGQIVKVVAKDTGASPEEVEKVAIEAGADRCVVELRER... | Cofactor: Binds 2 manganese ions per subunit.
Function: Part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair. The complex may facilitate opening of the processed DNA ends to aid in the recruitment of HerA and NurA. Mre11 binds to DSB ends and has both double-stra... |
Q8PUY5 | MDREIRILHTADTHLGYRQYHSEVRRQDFFKAFETVIKDAVDMQVDAVVHAGDLFDSRNPTLEDLLETMNVLSRLKVANIPFFGIVGNHESKQSTQWLDLFEEMGLAGRLGKAPKMVGDVAIYGIDSVPKSKIPLFDYSGFEIPESLPENCRKLLVMHQIMQPSPFPDWDCAEVIENLPFKADAVLLGDYHEYEKIKVGESWVTYSGSTERNSASEKEPRSYSIITLSGEGLEISRRTIPTRNFLFITAKVDGEEKPFEQIFSTVNEHLEEIPESVVFLDVSGDSSSVLSFSEIEEYLLSKGALVVKVKDARVKEGIPEE... | Cofactor: Binds 2 manganese ions per subunit.
Function: Part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair. The complex may facilitate opening of the processed DNA ends to aid in the recruitment of HerA and NurA. Mre11 binds to DSB ends and has both double-stra... |
P62131 | MQFVHMADNHLGYRQYNLDERENDIYESFLECIDKIIEIRPDFVIHSGDLFESPQPPVNAIRCAMEGLLKLKEKNIPIYLIHGNHDIPKSQQKGKPFGLLKKILGNSLLTFGKNKSHVFNNEVFIGGIEYVSQNKIPKTYEDLEKINSDSKNYKKKILLFHQSVNPFIPQSFEMQVTDFPDDFNYIAGGHIHQRALKPINDGNSVFSYAGSTDIMSVSEVKDYKKNGKGFYLGDLSGDFDINSIQKIDVECRNFLIDKKIKNENDYKKTVEELQNLQSEKKKPILYCDIVENLFNSFNDEIANLTLYKRISRIDENLEES... | Cofactor: Binds 2 manganese ions per subunit.
Function: Part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair. The complex may facilitate opening of the processed DNA ends to aid in the recruitment of HerA and NurA. Mre11 binds to DSB ends and has both double-stra... |
O26641 | MGSVISAEIFRRYQQYKATGELRRKPVIGIVIEEAPRVLGKEVIERQGNNIYSTIAREGRKFNIGLIAITQLVSLIPRTVLANMNTKIILGNEMAQERAEIIGSASQDLSADNRTIASLDKGEAIVSSIFTKFAVPVKIPLFEEFIESAGLESEDTDDDMIEFYRVGLSMYRFAHLSDCHLGAQKHPDLRELEFEAFRMALDDALQKDVDFMIIAGDLFHSNIPNMETVKRATLELRRVREAGVPIYVNYGSHDYSPSSTSMIDILESAGVIDKVVRPIPGKKLGLEFTVDEKTGAKITGLSGRSRTLEAEYFMKLDREA... | Cofactor: Binds 2 manganese ions per subunit.
Function: Part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair. The complex may facilitate opening of the processed DNA ends to aid in the recruitment of HerA and NurA. Mre11 binds to DSB ends and has both double-stra... |
P62132 | MIAFISDLHLGNIYANKKETEEHSYNALAKIEEKLLEYQPDLVLVGGDIFDKNKVSGKEIGVFIDFINKMNKNNIGVVSISGNHDGKYWLKESFDHAIPYILYKSGINPENGYEYYSFAGIYLKNSRDWKTLSMIEDKYDISIVGFSFYTKDRLPELYEYLSIIDREKSDYILLMHQSLKSLLPQDPAAIDLTIENYKYALFGHMHMKYYKDKIIVTPPPYSISLKEANTEKGFWLIDKKPVFVPIEDSRPFIKMAIDLDNPIEIKPNKNAILILDVYYRESQIDKLNLLKKTLSENFLYVKINPILKETSKIIVKKSEN... | Cofactor: Binds 2 manganese ions per subunit.
Function: Part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair. The complex may facilitate opening of the processed DNA ends to aid in the recruitment of HerA and NurA. Mre11 binds to DSB ends and has both double-stra... |
Q76NT0 | MISIFKILSSPKPATTTTNIINPINIINGIRYFSSNQEDYPLFKKPVFNGKVLRGGRKVFKNDLIYSKKESHYNNNNNSNNNSNNNNNNNNSNNRNNNNFSNNRNNNNNRNNNNNNSNRNNNNSNDNNFRNNNNNNRRTEYYKNDFDSSKYISNKPEIRIFDLHEQAVYGINPVWVALSSGNRTFNALYVCGTLLPKLKELGIDIKNIENSKREYISDFDHNYGRETNQIEDENQDEQYSNQHDEQEQNEYEEEQEEEKVQEEEEDNNNNNNIKKTTFNRYNDRKNLVALKEIVKNSFKLKIPVRSVNKGTLDSFSKGRP... | Function: S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of a 2'-O-methylguanosine in the mitochondrial large subunit ribosomal RNA (mtLSU rRNA), a universally conserved modification in the peptidyl transferase domain of the mtLSU rRNA.
Catalytic Activity: a uridine in rRNA... |
Q6IN84 | MALLSTVRGATWGRLVTRHFSHAARHGERPGGEELSRLLLDDLVPTSRLELLFGMTPCLLALQAARRSVARLLLQAGKAGLQGKRAELLRMAEARDIPVLRPRRQKLDTMCRYQVHQGVCMEVSPLRPRPWREAGEASPGDDPQQLWLVLDGIQDPRNFGAVLRSAHFLGVDKVITSRRNSCPLTPVVSKSSAGAMEVMDVFSTDDLTGFLQTKAQQGWLVAGTVGCPSTEDPQSSEIPIMSCLEFLWERPTLLVLGNEGSGLSQEVQASCQLLLTILPRRQLPPGLESLNVSVAAGILLHSICSQRKGFPTEGERRQLL... | Function: S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of 2'-O-methylguanosine at position 1145 (Gm1145) in the 16S mitochondrial large subunit ribosomal RNA (mtLSU rRNA), a universally conserved modification in the peptidyl transferase domain of the mtLSU rRNA.
Catalytic... |
Q02997 | MNNQPCSIVWRRFLTSKVKPAVRIPNENLKANKPTNFTKNFPLNERTKAWERAGEDKESWFKRKYAHVHAKQKSQPQVDLYGKKEAHYSRLKQDILSSKRQQEEHKSKYSRKSVTLGLRPNPLMEYIYGTNSVIAALN | Function: S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of the 2'-O-methylguanosine corresponding to position 2270 in S.cerevisiae 21S mitochondrial large ribosomal RNA, a universally conserved modification in the peptidyl transferase domain of the 21S rRNA.
Catalytic Acti... |
O94631 | MIRSRVNLAREVPKKAKAHLSKERRLIKEDSEFVFGTHSVKNALATRKRECRALYVQNADIHSEFEEFLNKLQYKIPIKSVNKEHLNQITACRPHNGVVLEASSLNVPTISDLLFPAGEEYNNKNGQDSPHNDLNEGKSSSSDNYPPLYVYVDGITDPQNMGAVIRSAYILGAKGILLSKKHNTFLSPVVSKASAGALEVFNISHVKNPMVFLRNSVLKGWKVIGTKPALPDNKDQIYTPHKIKTELMNEPKILVLGSEKGLRTNILTQCSHYVSIPGGDKYVDSLNVSVAAGILLYSLVN | Function: S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of the 2'-O-methylguanosine corresponding to position 2270 in S.cerevisiae 21S mitochondrial large subunit ribosomal RNA (mtLSU rRNA), a universally conserved modification in the peptidyl transferase domain of the mtL... |
P25270 | MTSLTNAVFKRYLAVTPSAHQALKTRIKKKSSSFDKFFPQQSNSRKKQWETLNEDKASWFKRKYAHVHAREQDRAADPYGKKKAHVEKLKEIKNQAKLNQKSHKSKFQNKDIALKLMNDNPIFEYVYGTNSVYAALLNPSRNCHSRLLYHGTIPSKFLQIVDELKVTTELVDKHRLNLLTNYGVHNNIALETKPLQPVEIAYLGDMDTSSAALSIHELGFNNENIPHELPYGTKTDAKKFPLGLYLDEITDPHNIGAIIRSAYFLGVDFIVMSRRNCSPLTPVVSKTSSGALELLPIFYVDKPLEFFTKSQEMGGWTFIT... | Function: S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of 2'-O-methylguanosine at position 2270 (Gm2270) in the 21S mitochondrial large subunit ribosomal RNA (mtLSU rRNA), a universally conserved modification in the peptidyl transferase domain of the mtLSU rRNA. This modi... |
O62251 | MFSTKKSQGNLHKYIQRQSTDEFAVKAREHNYRARSAFKLIEINEKFKFLKPESTVIDIGCAPGSWLQVVVQKCPNGYASGVDLQNVLPIRGADILSLSDITDPAVKLKIREKLAHRQVDVVLSDMAPNPTGDNATDHLRLIELCRSVFRLFSVENEIELVKNGVYLCKIWDGSARAEFVRELSDRFSTVKTVKPTACRDNSAELYLFCRNFKK | Function: S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of 2'-O-methyluridine at position 808 (Um808) in the mitochondrial large subunit ribosomal RNA (mtLSU rRNA), a universally conserved modification in the peptidyl transferase domain of the mtLSU rRNA.
Catalytic Activit... |
Q86AH1 | MLANRANRLVLKRLVHLNTSNIIKPICSYRSLASSSKSKTQFTKKPPISEFSIDEILEHFILKKKTIEGKENKDKNTIKVEKVNTKIDRFSSEVIIKEKNKKNNNIEDEDEFGIEEMIAKNNNNNNNPNNNNNNNNTKKVPTFNRFSTEVIVKSNNNNINEFENEEITKNNLNKKAPKFNRSSSGVVINTTSNDNNNDKNNNEFENEEIMLNSGKTNKKASKMDRYSSEVIIKEKNNEEILVNNNNNNNNNTTTTTNNNNNNKASKMERYSSEVIIKEKKDNNNDIEKDDIEKDEIIVNIMNGFEDKDESAVEFLKRHRI... | Function: S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of a 2'-O-methyluridine in the mitochondrial large subunit ribosomal RNA (mtLSU rRNA), a universally conserved modification in the peptidyl transferase domain of the mtLSU rRNA.
Catalytic Activity: a uridine in rRNA +... |
Q9VDT6 | MRLVFTGNCVFKRLLHTEIGGKYAKQQPRNLKGRSKSSQEWLTRQLADPYVEKARMMNYRCRSAFKLLEIDDKYGILRPGDTVLECGAAPGSWTQVAVERTNANGKQERAPQGAVFSIDLLHFHAVPGATIFGGMDFTSSLAQKRLREALQDRKVNCVLSDMAPNATGVRMLDQESITNLCYEVLRFALAMSAPQAHLVVKVWDNGDVPKLERDMLRFYEKVKRVKPRASRGDSAEHFLVARNFKGATDS | Function: S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of 2'-O-methyluridine at position 1579 (Um1579) in the mitochondrial large subunit ribosomal RNA (mtLSU rRNA), a universally conserved modification in the peptidyl transferase domain of the mtLSU rRNA.
Catalytic Activ... |
Q9UI43 | MAGYLKLVCVSFQRQGFHTVGSRCKNRTGAEHLWLTRHLRDPFVKAAKVESYRCRSAFKLLEVNERHQILRPGLRVLDCGAAPGAWSQVAVQKVNAAGTDPSSPVGFVLGVDLLHIFPLEGATFLCPADVTDPRTSQRILEVLPGRRADVILSDMAPNATGFRDLDHDRLISLCLTLLSVTPDILQPGGTFLCKTWAGSQSRRLQRRLTEEFQNVRIIKPEASRKESSEVYFLATQYHGRKGTVKQ | Function: S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of 2'-O-methyluridine at position 1369 (Um1369) in the 16S mitochondrial large subunit ribosomal RNA (mtLSU rRNA), a universally conserved modification in the peptidyl transferase domain of the mtLSU rRNA.
Catalytic A... |
Q9CPY0 | MAGHLKLVGVPLKVRRLHTAVCHYRGRTGAEHLWLTRHLKDPFVKAAKVESYRCRSAFKLLEMNEKHQILRPGLRVLDCGAAPGAWSQVAVQRVNATGADSSSPVGFVLGVDLLHIFPLAGATFLCPADVTDPRTFQKILELLPSRRADVILSDMAPNATGIRDLDHDKLISLCLTLVDMAVDILHPGGTLLCKTWAGSKSHLLQKRLTQEFQSTRVVKPEASRKESSEVYLLATQYRGGKGTRRP | Function: S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of 2'-O-methyluridine at position 1369 (Um1369) in the 16S mitochondrial large subunit ribosomal RNA (mtLSU rRNA), a universally conserved modification in the peptidyl transferase domain of the mtLSU rRNA.
Catalytic A... |
P78860 | MFGSKTLFSWAAKRSKDFYRKKSKIDNFRSRAAYKLIELNSKYRFINKEDVVIDVGFAPGSWSQVAKKLVGNKGKVIGIDIQHIAPPEGVLPIYGDIRDPNTLTKLFEALRLLHEPNTNDSIDCRVVDAVISDMLHKATGIRIRDHALSMELCASALHVALTFLKSNGSFICKFYMGDEDADLQNLLKSHFRFVQVMKPKASLKESREAYFVCLERKP | Function: S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of the 2'-O-methyluridine corresponding to position 2791 in S.cerevisiae 21S mitochondrial large subunit ribosomal RNA (mtLSU rRNA), a universally conserved modification in the peptidyl transferase domain of the mtLSU... |
P53123 | MILVYNRIRSIISSSLGRIHVRYNSNSQNRWLNRQLKDPYTKEAKVQNLRSRAAFKLMQIDDKYRLFSKNRTDQRILDLGYAPGAWSQVARQRSSPNSMILGVDILPCEPPHGVNSIQANILAKRTHDLIRLFFSKHFQLNRHDDLHKDHGYFQNMLEEELTHVKDTELYREIFTSDDIYETPNTNSTLIEREKFPVDVIISDMYEPWPQTTGFWNNITNQAYFRMANTSGVSIRDHYQSIDLCDAALVTAIDLLRPLGSFVCKLYTGEEENLFKKRMQAVFTNVHKFKPDASRDESKETYYIGLKKKRNVDKLDVFSNS | Function: S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of 2'-O-methyluridine at position 2791 (Um2791) in the 21S mitochondrial large subunit ribosomal RNA (mtLSU rRNA), a universally conserved modification in the peptidyl transferase domain of the mtLSU rRNA.
Catalytic A... |
Q566V3 | MAALMYNVSRGLVMLGERSLFQRERYQILVNSRRFLRGLRRRPVAVLYPDGERETLIKSKRATDITSQGFTQKGKARKDVTERAAYKNCSGFVSERAEESSQINKLKLAGLRFEKAPAGDNRLARVSSVARSRAFRDKEGKVLLEGRRLICDALSAGASPQMIFFSLLERLQELPLDKLQQAKLIKVKYEDIKLWSDLVTPQGLIAIFSKPDASRLTFPKDARLQSVPLFLICDNVRDAGNLGTILRCAAAAGGDRVLLSKGCVDAWEPKVLRSAMGAHFRLPVFPNLDWDDISKHLPKNVIVHVADNYSTSTKQLVSGQ... | Function: S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of 2'-O-methylguanosine at position 1485 (Gm1485) in the mitochondrial large subunit ribosomal RNA (mtLSU rRNA), a conserved modification in the peptidyl transferase domain of the mtLSU rRNA.
Catalytic Activity: a uri... |
Q0UG00 | MPPPPKRKWPNRPRGGGGANGSASGTPTTPRSTVAQQPKRPKVEDAAPAAEGVDVKQMYSTSAGNASAKPFSELSSVLDKSLLDGLDKMGFEFMSPVQQKVLTELPSLSSDCVVQAKTGTGKTVAFLLPAIQNLLAGNMPPRGKVAILVVCPTRELALQIAKECNGVTACLPRKMECHTAFGGTSRASNLKAFLNGNPTILVATPGRLDDILGEEHVRERFTHLKTVVLDEADQMLDAGFAPAVKKILRRIPPKSDGWQGMCFSATLPKEVLDIAKIVLFPGFTHLTTVDPNEVPTHERVPQYFLSVPNVGQTFAALSAL... | Function: ATP-dependent RNA helicase required for mitochondrial splicing of group I and II introns. Also required for efficient mitochondrial translation (By similarity).
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 59705
Sequence Length: 550
Domain: The Q motif is unique to and characteri... |
A5DEZ5 | MSWVRSVAIRTALCRQVRSRYQSYGSTRLFSSSLRSWEEPEVVTKTPKADIDHEAVKAHQESSPLKSIEVPFTSLEASRKFDKSIFRGLYNSKMKNMTVVQQRAIMPMMDTKTGVVVRAKTGTGKTLAFALPCIQAALENPQQTQKGRIQALVVAPTRDLALQIEAEFKKVLQHQTRNVHRKTDTFVLIGGRKNDLHPKAKAAIVIATPGRLEAILRDPRMLPMFSDLKYRVYDEADRLLDQGFAPTLEVIEERLRDAKAEALEPDNHFKTALFSATVDDAVTNFAHETIGKEYEYINCVDKDAEESHENIHQGIVRTQS... | Function: ATP-dependent RNA helicase required for mitochondrial splicing of group I and II introns. Also required for efficient mitochondrial translation (By similarity).
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 81388
Sequence Length: 714
Domain: The Q motif is unique to and characteri... |
O13622 | MNISLKGAIFSTVGRFNLPKVQGFIRWNSTMKSQQPTLFSEVASLSSTFKNSLSRAGFEKMTPVQQRVLNEVFPNEENAVVQAKTGTGKTLAFLLVAFKDVLKGKPRLNSSKIHSVILSPTRELALQIFEEARKLTYGTGIRVSYAIGGNSKMREENAIRRGNANLLIATPGRLEDHLQNPRILESLSTDSFILDEADRLMDMGFAESILNIHEAVTTTKTRKLCFSATMPPKVSNVFRGILGTDFKLINCLDPNEPPTHERVPQFVIETKLDKVFSSSLSLLQQLTSSNPSSRIIVFLPTISMVDFVGGVLENHLKIPC... | Function: ATP-dependent RNA helicase required for mitochondrial splicing of group I and II introns. Also required for efficient mitochondrial translation (By similarity).
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 59449
Sequence Length: 535
Domain: The Q motif is unique to and characteri... |
P15424 | MLTSILIKGRTPVLASRNLLAALSNCNHITWAVSRRLYNDGNRDQRNFGRNQRNNNSNRYRNSRFNSRPRTRSREDDDEVHFDKTTFSKLIHVPKEDNSKEVTLDSLLEEGVLDKEIHKAITRMEFPGLTPVQQKTIKPILSSEDHDVIARAKTGTGKTFAFLIPIFQHLINTKFDSQYMVKAVIVAPTRDLALQIEAEVKKIHDMNYGLKKYACVSLVGGTDFRAAMNKMNKLRPNIVIATPGRLIDVLEKYSNKFFRFVDYKVLDEADRLLEIGFRDDLETISGILNEKNSKSADNIKTLLFSATLDDKVQKLANNIM... | Function: ATP-dependent RNA helicase required for mitochondrial splicing of group I and II introns. Specifically involved in the ATP-dependent splicing of the bl1 intron of COB. Also required for efficient mitochondrial translation.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 76269
Sequen... |
P10333 | MNQILLCSPILLLLFTVASCDSEQQLDSAMHLKSDSTKSASLKNVAPKNDETQAKIAKDDVALKDAKKGDYIMDIDISDLPLDDYPINRSKSLKSSSIDLNNIPFNKGLDDFPAKEKNQGSNQSALKALQQRLLTEQNNSLLLRNHSIYLMKEIEARKTDIIKVRQLNLDLELELNTVNRRLLELNGQLQNTRKSTKPCKKRSSKDSAPPAANQFQEANVRNTYRNKYLTLLKELSQKINNEIAKVATDVPTETNPSQGNLPTL | Function: Male seminal protein which enhances ovulation in female Drosophila by stimulating the release of oocytes by the ovary following mating . Acts by increasing octopamine (OA) neuronal signaling in the female genital tract leading to the postmating relaxation of the oviduct muscles . This activation of the OA sig... |
Q9HUG8 | MSDSPQNPGPSSLKIYFRLLGYVKPYIGMFLLSIVGFLIFASTQPMLAGILKYFVDGLSNPDAALFPNVQWPWLRDLHLVYAVPLLIILIAAWQGLGSFLGNFFLAKVSLGLVHDLRVALFNKLLVLPNRYFDTHSSGHLISRITFNVTMVTGAATDAIKVVIREGLTVVFLFLYLLWMNWKLTLVMLAILPVIAVMVTTASRKFRKQSKKIQVAMGDVTHVASETIQGYRVVRSFGGEAYEEKRFLDASQSNTDKQLRMTKTGAVYTPMLQLVIYVAMAILMFLVLWLRGDASAGDLVAYITAAGLLPKPIRQLSEVSS... | Function: Involved in lipopolysaccharide (LPS) biosynthesis. Translocates lipid A-core from the inner to the outer leaflet of the inner membrane. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation.
Catalytic Activity: ATP + H2O + lipid A-c... |
Q88D92 | MAETPRPAEHTSSLKIYFRLLSYVKPYVGIFLLSIVGFVIFASTQPMLAGILKYFVDGLSNPEAVLFPNVPYLRDLQLLQAVPLLIILIAAWQGLGSFLGNYFLAKVSLSLVHDLRVALFNKLLVLPNRYFDNHNSGHLISRITFNVTMVTGAATDAIKVVIREGLTVVFLFAYLLWMNWHLTLVMVAILPVIAVMVSIASKKFRKQSKKIQVAMGDVTHVASETIQGYRVVRSFGGEAYEQQRFGQASQSNTDKQLRMTKTGSLYTPMLQLVIYSAMAALMFLVLFLRGDSTAGDLVAYITAAGLLPKPIRQLSEVSST... | Function: Involved in lipopolysaccharide (LPS) biosynthesis. Translocates lipid A-core from the inner to the outer leaflet of the inner membrane. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation.
Catalytic Activity: ATP + H2O + lipid A-c... |
Q3IGX5 | MDQSTTQIYKRLISYVGAYRTVAIVAIIGMIGYSGMDALFIQLMKPFIDEGLNERNADVLKYAPFVVIALVIGRGVFNFMSSYCLSYVGSQVVRSLRQELFEHILHLPVSFHDKNSTGDLISKITFDTEQVQQAITKALLIVVREGAFVVFLLAVMFYTSWQLSLIFLVIIPLVAVIVTVVSKRFRHISKSIQSAMGQVTRSSEQMLSGHKVIHGFGGQNQEIDQFSKVNNHNRQQRIKMDATKALSVSIIQVLAASAMAVILWVVSMPSMIDTISSGDFVVLISSMMMLLRPLKQLANVNSDMQRGVSAAQSVFLILDE... | Function: Involved in lipopolysaccharide (LPS) biosynthesis. Translocates lipid A-core from the inner to the outer leaflet of the inner membrane. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation.
Catalytic Activity: ATP + H2O + lipid A-c... |
Q1QBW0 | MSQAYQPDSTKTSAKTPVAPTVATLNPPKRKTLMRLLAYLKPYWWAILLTIIGFAINAATEIWIAKLLQYITDAINQNDQSKQDLFPFIIVMLFFVRGVGSFLGNYYTALVSRNLVYELRVEVFNKLLRLPSSFYLANPAGTISSKLIFDVEQVTAASTDSMKTLLRDGLTVVALMGFLLYSNWRLTLILFVVLPPILWLIRVASKRYLKLSKGIQETMGDVSHITNEVINGYQVVKNYGGQVYESKRFDVTSKKNLRQGMKVVVTNSINTPAVQLLMAMAMAVVVWLALRPAVIDDISAGQFISYIAAAGLLSKPVRSL... | Function: Involved in lipopolysaccharide (LPS) biosynthesis. Translocates lipid A-core from the inner to the outer leaflet of the inner membrane. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation.
Catalytic Activity: ATP + H2O + lipid A-c... |
Q21NS8 | MSTPAKPTSVESYKRLLSYAFKYKAYFIISFIGFGVFAAMEAQLINILEYFVDRLEGRPSAPVLGLSADVTSSLWFVPISVVVLSIIRGIGAYFGNFYMSLVGLNVITNLRRQIFSQMIYLPQSFYDTKNSGELISLLVYNIEQVTGSVTNAVKTLFRDGMSVAWFLAMMLIINWKLTLAFICVAPVLGGLMYIASKYFRKVSHKIQSAVGRVSHVATESIQGIKLVKSYGGEKYELDRFNDATNQNLHYGTKFERVSAFQTPVLHIVLALALAVTFYLIMILWDSDSSKAVVYATYAAAIAKPFRQLTKINSIIQKGLA... | Function: Involved in lipopolysaccharide (LPS) biosynthesis. Translocates lipid A-core from the inner to the outer leaflet of the inner membrane. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation.
Catalytic Activity: ATP + H2O + lipid A-c... |
Q8EDF0 | MTASPKNEMWTVFKRLMGYLKPMKGMFLLSVVGLIVYGLVDAAFISFIGPFIDKGFSSSAPAISNGIALPTSQGFHADNQVLLMAPIVVILMFSLRGFANFVSTYGISYMSARLIMDMRQQVFEHYLSLPVSYMDKENTGNLISKVTFDTEQIARASGSALISIVRDSVTIIGMLGLMFYNSWKLSLCILVIGPIMGVVITIVSRRFRKVSKQIQTAMGDVSAATEQMIKGHKNVLAFGGQETETARFAKINDRNRHQNMKLAVAQAVSQPLIMVIGSFALAFVLYAASLDSMKADLTAGTFATILGAMMAMLQPIKNLT... | Function: Involved in lipopolysaccharide (LPS) biosynthesis. Translocates lipid A-core from the inner to the outer leaflet of the inner membrane. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation.
Catalytic Activity: ATP + H2O + lipid A-c... |
B3EA78 | MLQEFKTFIMKGNVLDLAVGVIIGAAFGKIVNSAVNDLIMPVVGLALGKVDFSNLFISLKGGEYATVAAAKAAGAPTLNYGIFLNTTLDFLIMALVIFMIIKAANKVRKTEEPAPAPVPRECPFCKSAVHDEASRCPHCTSQLNATA | Function: Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 15570
Sequence Length: 147
Subcellular Location: Cell inner membrane
|
Q8PHE9 | MGMVSEFKQFAMRGNVIDLAVGVVIGAAFGKIVTALVEKIIMPPIGWAIGNVDFSRLAWVLKPAGVDATGKEIPAVAIGYGDFINTVVQFLIIAFAIFLVVKLINRVTHRKPDAPKGPSEEVLLLREIRDALKNDTLKPPGAL | Function: Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 15392
Sequence Length: 143
Subcellular Location: Cell inner membrane
|
B2HQV2 | MRPMRAGAGAAGESCKDDGVRPDDVSRLTADAVVRRVALLAVHTSPLAQPGTGDAGGMNVYVLQSALHLAKRGIEVEIFTRATASADPPVVRVAPGVLVRNVVAGPFEGLDKYDLPTQLCAFAAGVLRAEAAHEPGHYDIVHSHYWLSGQVGWLARDRWAVPLVHTAHTLAAVKNAALANGDAPEPPLRTVGEQQVVDEADRLIVNTDDEAKQLISIHRADPARIDVVHPGVDLEVFRPGDRQQARTALGLRPEEKVVAFVGRIQPLKAPDIVLRAVAKLPGVRIIVAGGPSGSGLASPDGLAQLADELGIAERVTFLPP... | Function: Catalyzes the transfer of a N-acetyl-glucosamine moiety to 1D-myo-inositol 3-phosphate to produce 1D-myo-inositol 2-acetamido-2-deoxy-glucopyranoside 3-phosphate in the mycothiol biosynthesis pathway.
Catalytic Activity: 1D-myo-inositol 3-phosphate + UDP-N-acetyl-alpha-D-glucosamine = 1D-myo-inositol 2-acetam... |
A0QQZ8 | MRLATDLETPRRVAVLSVHTSPLAQPGTGDAGGMNVYVLQTALQLARRGVEVEVFTRATSSADAPVVPVAPGVLVRNVVAGPFEGLDKNDLPTQLCAFTAGVLRAEATHEPGYYDVVHSHYWLSGQVGWLARDRWAVPLVHTAHTLAAVKNAALAAGDAPEPPLRAVGEQQVVDEADRLIVNTEVEAQQLVSLHNADRSRIDVVHPGVDLDVFTPGSRDAARAVFGLPTDQKIVAFVGRIQPLKAPDILLRAAAKLPGVRVLIAGGPSGSGLAQPDTLVRLADELGISDRVTFLPPQSREQLVNVYRAADLVAVPSYSES... | Function: Catalyzes the transfer of a N-acetyl-glucosamine moiety to 1D-myo-inositol 3-phosphate to produce 1D-myo-inositol 2-acetamido-2-deoxy-glucopyranoside 3-phosphate in the mycothiol biosynthesis pathway.
Catalytic Activity: 1D-myo-inositol 3-phosphate + UDP-N-acetyl-alpha-D-glucosamine = 1D-myo-inositol 2-acetam... |
A1SP12 | MRADRPGHRSRGINPGPGMFTLVGPDERDDPEVAVDPIRRVAMISLHTSPLDQPGTGDAGGMNVYVIELSKRLAAQGIAVDIFTRATTSAVEPLVEAYDGVQVRHIHAGPFEGLTKAELPGQLCVFAREVLRAEAAQPVGHYDVVHSHYWLSGQVGALARDRWGVPLVHSMHTMAKVKNDALAEGDTPEPAARIIGEEQVVEAADMLVANTDIEAKQLVNMYDADPSRVEVVHPGVDLGVFRPQDRSTARARLGLPEDAAVLLFAGRIQPLKAPDVLLRAVAELLAQTPELRSRLVVPIVGGPSGSGLEHPESLAQLASE... | Function: Catalyzes the transfer of a N-acetyl-glucosamine moiety to 1D-myo-inositol 3-phosphate to produce 1D-myo-inositol 2-acetamido-2-deoxy-glucopyranoside 3-phosphate in the mycothiol biosynthesis pathway.
Catalytic Activity: 1D-myo-inositol 3-phosphate + UDP-N-acetyl-alpha-D-glucosamine = 1D-myo-inositol 2-acetam... |
Q73YS9 | MRSWSSPQVPQLPGRGPELRLYDTSDRQVRPVAAGAGPGSAATMYVCGITPYDATHLGHAATYLAFDLIYRQWLDLGHDVHYVQNVTDVDDPLLERAARDGVDWRALAEREVSLFREDMAALRILAPRDYVGATEAIADVVELVEKMLASGAAYVVDGEFPDIYYRADATLQFGYESGYDRETMLRLFAERGGDPQRPGKTDALDALLWRAARPGEPSWPSPFGNGRPGWHVECAAIALSRIGSGLDIQGGGSDLIFPHHEFTAAHAECVRGERRFARHYVHAGMIGWDGHKMSKSRGNLVLVSQLRGRGVEPAAIRLGL... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the ATP-dependent condensation of GlcN-Ins and L-cysteine to form L-Cys-GlcN-Ins.
Catalytic Activity: 1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside + ATP + L-cysteine = 1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-glucopyranoside + AMP + diph... |
A0QZY0 | MQSWSAPAIPVVPGRGPALRLFDSADRQVRPVTPGPTATMYVCGITPYDATHLGHAATYLTFDLVHRLWLDAGHTVQYVQNVTDVDDPLFERAERDGIDWRTLGDRETQLFREDMAALRVLPPHDYVAATDAIAEVVEMVEKLLASGAAYIVEDAEYPDVYFRADATAQFGYESGYDRDTMLTLFAERGGDPDRPGKSDQLDALLWRAERPGEPSWPSPFGRGRPGWHVECSAIALTRIGTGLDIQGGGSDLIFPHHEYSAAHAESVTGERRFARHYVHTGMIGWDGHKMSKSRGNLVLVSQLRAQGVDPSAIRLGLFSG... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the ATP-dependent condensation of GlcN-Ins and L-cysteine to form L-Cys-GlcN-Ins.
Catalytic Activity: 1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside + ATP + L-cysteine = 1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-glucopyranoside + AMP + diph... |
L7X3S1 | MRTESIKTNRPMDLLLQYLQPISVALVVIALVWNYGRRNPTKKLAPEASGGRPIMGHLHLFNDGELTHRKLGAMADTYGPVFNIRFGSHKTLVVSDWEIVKECFTTNDKLFSNRPGTLGIKLMFYDADSVGYAPYGAYWRDLRKISTLKLLSNHRIDTIKHLRSSEVESCFESLYSQWGNGEKSGEFAPVRMDSWLGDLTFNVVARIVAGKKNFSANGDVGAQRYKAAMDEAMRLMRFFAFSDVIPSLSWLDNLRGLVREMKKCASEIDSIMATWVEEHRVKRNSGGNSQLEHDFIDVCLDIMEHSSLPGDDPDLVVKST... | Function: Involved in the biosynthesis of the isoquinoline alkaloid sanguinarine . Catalyzes the conversion of N-methylated protoberberine alkaloids N-methylstylopine and N-methylcanadine into protopine and allocryptopine, respectively . Can also use (S)-cis-N-methyltetrahydrothalifendine and (S)-cis-N-methyltetrahydro... |
Q61474 | METDAPQPGLASPDSPHDPCKMFIGGLSWQTTQEGLREYFGQFGEVKECLVMRDPLTKRSRGFGFVTFMDQAGVDKVLAQSRHELDSKTIDPKVAFPRRAQPKMVTRTKKIFVGGLSVNTTVEDVKHYFEQFGKVDDAMLMFDKTTNRHRGFGFVTFESEDIVEKVCEIHFHEINNKMVECKKAQPKEVMSPTGSARGRSRVMPYGMDAFMLGIGMLGYPGFQATTYASRSYTGLAPGYTYQFPEFRVERSPLPSAPVLPELTAIPLTAYGPMAAAAAAAAVVRGTGSHPWTMAPPPGSTPSRTGGFLGTTSPGPMAELY... | Function: RNA binding protein that regulates the expression of target mRNAs at the translation level. Regulates expression of the NOTCH1 antagonist NUMB. Binds RNA containing the sequence 5'-GUUAGUUAGUUAGUU-3' and other sequences containing the pattern 5'-[GA]U(1-3)AGU-3'. May play a role in the proliferation and maint... |
O22467 | MGKDEEEMRGEIEERLINEEYKIWKKNTPFLYDLVITHALEWPSLTVEWLPDREEPSGKDYSVQKMILGTHTSESEPNYLMLAQVQLPLDDTESEARQYDDDRSEFGGFGCATGKVQIIQQINHDGEVNRARYMPQNPFIIATKTVNAEVYVFDYSKHPSKPPLDGACNPDLKLRGHSSEGYGLSWSKFKQGHLLSGSDDAQICLWDINATPKNKSLDAQQIFKAHEGVVEDVAWHLRHEYLFGSVGDDQYLLIWDLRSPSASKPVQSVVAHSMEVNCLAFNPFNEWVVATGSTDKTVKLFDLRKLSTALHTFDSHKEEV... | Function: Core histone-binding subunit that may target chromatin assembly factors, chromatin remodeling factors and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA. Component of several complexes which regulate chromatin metabolism. These include the chromatin assembly ... |
Q9A9I6 | MLSLHKTLEMPSADTALPGRAAPIPTAQTHFVNGHALKGPYPEGLETAIVAMGCFWGVERVFWKVPGVYVTAAGYAAGITPNPTYEEVCTGRTGHTEVVLVVFDPKVVTYEALLKTFWENHDPTQGMRQGNDIGTQYRSGLYVTSDAQAAAAAESKAAYQQALSARGLGTITTEIAPAGPFYFAEDYHQQYLAKNPNGYCGIGGTGVVCPIGLGVEG | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine (By similarity).
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol +... |
Q9CFC8 | MSTERAIFAGGCFWCMVEPFEERPGILAVTSGYTGGHIEYPTYDQVLSKASGHTEAVEILFDNELISYDELLDIYWSLIDPTDADGQIYDRGANYRPVIFVESEEQRIAAQKSKIALEKSGIWDKPIVVPIEEAKTFWPAEEYHQQYYKKDPKRYQAMHKARERYLALQRFKGKFKFLRKNTR | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine (By similarity).
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol +... |
Q8YXZ4 | MELKIGSTEAPMEKATFGAGCFWGVEAAFRKVKGVVSTSVGYMGGHFPNPCYLDVLSRITGHAEVVQIEYDPQLVSYEDLLAVFWDIHDPTTLNRQGPDKGEQYRSVIFFHNEQQAEAAQQSKAKVQVSGRFELDIVTEIKHKSEYYLATEEHQQYFEKQAKR | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine (By similarity).
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol +... |
Q98JV5 | MATSTERAVLAGGCFWGMQDLIRRYPGVISTRVGYSGGDVANATYRNHGTHAEAIEINFDPAVISYRTLLERFFQIHDPTTRNRQGNDVGMSYRSAIYYTSDEQKRVAEDTIADVDASGLWPGKVVTEVAPAGAFWEAEPEHQDYLEKYPNGYTCHFVRPGWKLPVREKAVS | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine (By similarity).
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol +... |
Q92SY7 | MFLIDMFNKKTILPDAATALPGREEEIPTATTHFVSGRPLQGPYPEGMKKVLFGMGCFWGAERLLWEIPGVYVTAAGYSGGLTPNPTYQETTTGLTGHTEVVLVVYDPAKVSLQRLLKTFFEEHDPTQGMRQGNDVGTTYRSAIYVYDEEQLAEANAARNAFQKALRVYNHDREITTEIAKAGPFYFAEDYHQQYLAKNPDGYCGLRGTGVSCPIGA | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine (By similarity).
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol +... |
Q7UJK0 | MPFDSEIVEVKTRPGEEVATLAGGCFWCTEAVFERMEGVNDVVSGYIGGKIKNPNYKQVCGKMTGHAEAVQIYYDPSKTNFEELLKVFFKTHDPTTLNRQGADGGPQYRSSIFVHNDEQREIAKKTMEKLGEEYRDPIVTLIEPATKFYVAEEYHQDYYRRNPNAGYCQAVVAAKVRKFNRNFGDKIKGSGK | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(S)... |
P0A084 | MNINTAYFAGGCFWCMTKPFDTFDGIEKVTSGYMGGHIENPTYEQVKSGTSGHLETVEIQYDVALFSYNKLLEIFFSVIDPLDTGGQYQDRGPQYQTAIFYTNDHQKELAETYIEQLKNTINADKAIATKILPASQFYKAEDYHQDFYKKNPERYAEEQKIRQEYKNKQ | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine (By similarity).
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol +... |
P72622 | MGFFDLFGKKTAMVAPNEALPGRSATMPVPDKHFVNGNPLKAPFPQGMETALFGLGCFWGAERKFWQIPGVYSTAVGYAAGYTPNPTYQEVCTGMTGHNEVVLVAFDPQQVSYDQLLKVFWESHNPTQGMRQGNDVGTQYRSGIYTYSEAQQQAALASKQAYQQALQQAGYGEITTEILPAPDFYYAEDYHQQYLAKNPNGYCGLGGTNVACPIGTEVSLGA | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine (By similarity).
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol +... |
Q9A9E9 | MRRLIVLFAAALAVLGATAPALAAPKTETAVFAGGCFWCMEHDMQGVPGVLKVESGYTGGHLKNPTYRDVTSETSGHYEAVRVTYDPAKLDYGFLLYRYWRLVDPTDDGGQFCDRGPSYRPAVFVTPAQRPIAEKSRTEAAKRLKTGTMKTQILPAQTFYLAEEYHRDYAKRNKLNYFAYRTGCGRDARLKQVWGG | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine (By similarity).
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol +... |
Q9CE42 | MATERAIFAGGCFWCMVQPFEEREGILSVISGYTGGNVENPTYEQVKKHLTGHTEAVEIIFDNSKITYQSLVELYWTLTDPTDAFGQFEDRGDNYRPVIFVENEEQEKIAKESKAQLQASGNFDSPIVTSIETVQKFWPAEDYHQGFYKKNPEDYAQSSKIRHDFLEKQWKK | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine (By similarity).
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol +... |
Q98DV6 | MDEKAAPGSETAIFAGGCFWGVQGVFQHVKGVSKAVSGYTGGAKDDAVYETVGTGRTGHAESVEITYDPSKVTYGQLLQVYFSVAHNPTQLNFQGPDSGTQYRSTIFAENDTQKQIAQSYIDQLDKAKLYPAPIVTTIETGKTFYPAENYHQDFLTLNPTYPYIVYNDLPKVANLKQLFPALYSEKPVLVLSASN | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine (By similarity).
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol +... |
Q92LI5 | MLRLLFGFLVTCFLLLPARAAEPQYAIFAGGCFWCVESDFDAVPGVLETISGYAGGKSANPTYEDYAKGGHREVVRVKFDPDRVSYAELVGVLFRTTDPTDGDGQFCDRGFAYTTAIHALNERQAMDAKAEKIKAEAELGRPIVTPVEGAAKFWPAEDYHQDFGKRNPIRYWYYRNGCGRNRTVEKLWGDRAYAGVSH | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine (By similarity).
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol +... |
Q8FLU6 | MAFFFRPEPKMVTPEEALKGGRHPVLESPQPHTVLGTPITGPWKEGQKRVWIGLGCFWGVEQMYWKMDGVESTSVGYAGGYTPNPTYREVCSGRTGHTEIVEVVYDPEKITLAELVARGLEAHDPTQGYRQGNDVGTQYRSAFYVETGEEAETVRQIVSTYGETLKSHGFGEITTEVDVITPADYYLAEDYHQQYLHKNPDGYCPHHSTGIPCGVEA | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(S)... |
Q9RTB6 | MGWHPLGEHGAPHNSSMTQQTNSQGTQPGAAQEQAIFAGGCFWCTEAVMQDLRGVQKVESGYIGGTVPNPDYRSVCGGQTGHAEAVRVTFDPNQISYRDLLGLFFATHDPTSLNRQGADVGTQYRSALFPLTQEQEQTAREMIEQLGTEDVFGRPIVTSIEPASTFYVAEDYHQNYYKNNPGQGYCMAVISPKVAKLRQYYGDKLR | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine (By similarity).
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol +... |
Q551H3 | MTKATFAAGCFWSVELLFQRVAGVTKTRVGYTNGTVENPTYRQVCSGKTGCAEAVELEYDPEKVTYNQLLGLFWSKHDPTTLNRQGNDVGTQYRSGIYYHNEEQKNEAIASKEKEQLKYKDPISTEILPAGVFYPAETEHQQYLGNY | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine (By similarity).
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol +... |
P08761 | MSLTITSSVTHPELKDLSTVRNEQKELNISPVHDVNVTKATATFGMGCFWGAESLYGATRGVLRTTVGYAGGSSDLPTYRKMGDHTEVLEIDYDPTVISFKELLDLFWNNHEYGLTTPIKRQYASLILYHDEEQKQVAHASKLEEQERRAPEIITTEIASKENFYPAEAYHQKYRLQGHKDLASSLNLSPKLLQTSYVATKLNGYLAGVGGIEQFKAEAETMGLTPTQRQYCYYHVEQNEGQGLYC | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reduction of methionine sulfoxide in proteins to methionine . Does not catalyze the reverse reaction involving the oxidation of methionine residues .
PTM: Conjugated to URM1, a ubiquitin-like prote... |
P54153 | MEGNNSSSKSTTNPALDPDLDSPDQPGLEFAQFAAGCFWGVELAFQRVGGVVKTEVGYSQGNVHDPNYKLICSGTTEHAEAIRIQFDPNVCPYSNLLSLFWSRHDPTTLNRQGNDVGKQYRSGIYYYNDAQAQLARESLEAKQKEFMDKKIVTEILPAKRFYRAEEYHQQYLEKGGGRGCKQSAAKGCNDPIRCYG | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine (By similarity).
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol +... |
Q9EWF7 | MAAQTQRAVLAGGCFWGMEELIRRLPGVTATRVGYTGGDVPNATYRNHGTHAEAIEILFDPEATDYRALLEFFFQIHDPSTKNRQGNDIGLSYRSAIYYVDDEQKRIAEDTIADVDASGLWPGKVVTEVEPVGPFWEAEPEHQDYLQRYPDGYTCHFPRPGWRLPARSGSEG | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(S)... |
Q9A149 | MERAIFAGGCFWCMVQPFEEQAGILSVRSGYTGGHLPNPSYEQVCAKTTGHTEAVEIIFDPKQIAYKDLVELYWTQTDPTDAFGQFEDRGDNYRPVIYYTTERQKEIAEQSKANLQASGRFDQPIVTTIEPAEPFYLAEDYHQGFYKKNPKRYAQSSAIRHQFLEENWS | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(S)... |
Q885Q1 | MDKLQKTLEEWKEMLDPAQYSVCRLKGTERPFSGKYNDTKTAGVYHCICCNEALFDSTTKFDSGCGWPSFYAPLEGSAVVEVRDVSHGMIRTEVVCARCDAHLGHVFPDGPPPTGLRYCINSVCLELVPRE | Cofactor: Binds 1 zinc ion per subunit. The zinc ion is important for the structural integrity of the protein.
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(R)-S-oxide-[protein]
Sequence Mass (Da): 14623
Sequence Length: 131
EC: 1.8.4.12
|
Q4ZQC6 | MDKLQKTLEEWKQMLDPEQYNVCRLKGTERPFSGKYDKVKTDGIYHCICCDEPLFDSTTKFDSGCGWPSFYAPLENSAVIEVRDMSHGMIRTEVVCAKCDAHLGHVFPDGPPPTGLRYCINSVCLDLVPRS | Cofactor: Binds 1 zinc ion per subunit. The zinc ion is important for the structural integrity of the protein.
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(R)-S-oxide-[protein]
Sequence Mass (Da): 14823
Sequence Length: 131
EC: 1.8.4.12
|
Q8XYL1 | MTIEKTDAEWRDQLSDIEYRVTREAATERPFTGRYWDHWARGIYHCVCCGTPLFESSTKFDAGCGWPSYFAPINGEVIAEKTDHSHGMVRIEVQCKQCGAHLGHVFEDGPAPTGLRYCINSAALKFGD | Cofactor: Binds 1 zinc ion per subunit. The zinc ion is important for the structural integrity of the protein.
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(R)-S-oxide-[protein]
Sequence Mass (Da): 14418
Sequence Length: 128
EC: 1.8.4.12
|
Q88DZ3 | MRYPWFRLAIFIVGCLFPVWWLYEAAMNLLGPDPGKIMMDRLGLGALTFLLVTLSMTPLQKLTGWSGWIVVRRQLGLWVFAYIVLHILCYLFFILGLDWGQLAVELRKRPYIIVGALGFLGLLVLAVTSNRYSQRRLGARWKKLHRLVYAVLGLGLLHFLWIVRSDLREWAIYAFIGAVLMVLRIPAVARALPKVAR | Cofactor: Binds 1 FMN per subunit.
Function: Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by t... |
Q8XV51 | MLPSMLPPKSLRAVRIAVWLLALVPFLRLVVLGATDRYGANPLEFVTRSTGTWTLVLLCCTLAVTPLRRLTGMNWLIRIRRMLGLYTFFYGTLHFLIWLLVDRGLDPASMVKDIAKRPFITVGFAAFVLMIPLAATSTNAMVRRLGGRRWQWLHRLVYVTGVLGILHYWWHKAGKHDFAEVSIYAAVMAVLLGLRVWWVWRGARQGAIAGGAVPLRD | Cofactor: Binds 1 FMN per subunit.
Function: Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by t... |
Q92QE8 | MRSLPALPKRLHGPSIWALYILGFLPAVWGFYLGATGRLPGNAVKEFEHLLGIWALRFLIATLAITPIRDLFGVNWLRYRRALGLLAFYYVMMHFLTYMVLDQTLLLPAIVADIARRPFITIGMAALVLLIPLAVTSNIWSIRRLGQRWNKLHRLVYVIAAAGALHFAMSVKVVGPEQMLYLFLVAVLVAWRAVRKRFLRWRRQGTAPMRSQARAG | Cofactor: Binds 1 FMN per subunit.
Function: Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by t... |
Q2RWU7 | MTGGSVLKDRDRLGRIAVFVACLLPLVWYGARFVGGDLGANPIEAFTRKLGEWGLIFLLASLAATPARLLWGWTFPLRRRRMVGLFAFFYVCLHLLSYIGLDQFFDWGAIWADIVKRTYITVGMAALLLLVPLAVTSTRGMVRRLGGKRWIALHRLVYPAAVLGVLHYMLMVKADLSEPLIFAGILGLLLAVRLVPAVRRRRSGRAPS | Cofactor: Binds 1 FMN per subunit.
Function: Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by t... |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.