ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q21059 | MVSYWPVLIVLCLLPICHAKSYFADFVNGKGPFKQADALKFMDKMTILNKLQADILGIPQPDEFSALDFEDKIESKPDEIPYLFEGDMVLTDEQMDLIIKNVRDQYWARKSSTNEFLYAIRGKRSMTSFLSERWSFPVPYYIDTSSGVNTNAVLAGVAKWEQETCARFTRLNSYSSSSRQNALRFISGNGCYSNIGKVSRFPQDVSIGWGCTSLGTVCHEIGHALGFYHEQARYDRDDYVSILTQNIQDMYLSQFTKQSASSMVDYGVGYDYGSVMHYDQAAFSSTGGNTIATRDPNFQATIGQRVAPSFADVKRINFAY... | Cofactor: Binds 1 zinc ion per subunit.
Function: Metalloprotease (By similarity). Required for normal hatching and migration of neuroblasts. May act by degrading eggshell proteins at hatching .
Sequence Mass (Da): 66259
Sequence Length: 605
Subcellular Location: Secreted
EC: 3.4.24.-
|
A8Q2D1 | MALLKPFLSRTFSSFFATITGGRNLIDSIEELITTNYWLIFVMIIVCTCSAPSNGAFFLNDPYGYPFVSLQDDSIESVSATTITTTTIISTIITTTTATQRIFQEKAKTFGQSAEEIQKVKYYLEKIQKFEAKQHPEEIRQQHTTKNSEAIKDDLQIAVEVAKFEKRQKDSITLNPEENGQYYEGDIVLDAQQAHEIYESMIQHGRRTKRKFIRSELRRWDSHKPIIYSFDGSHTIREQRVIELALEHWHNITCLNFERRDDEIQENRIVFTDVDGCASNVGRHPLGEPQFVSLAPECIRLGVIAHEVAHALGFWHEQSR... | Cofactor: Binds 1 zinc ion per subunit.
Function: Metalloprotease which cleaves the carboxyl terminus of procollagens to mature collagens. Probably involved in cuticular collagen maturation.
Sequence Mass (Da): 68968
Sequence Length: 599
Subcellular Location: Secreted
EC: 3.4.24.-
|
P98060 | MHKIFIIFGLLSLCAAHSLRDLSNKDEEDPPSSAPGVRKRRMMSEEDQKTVDYYMDKLNKLADEKHPEEIERHKNPELVAWDRKRDSVLNPEEQGKFFQGDIVLYPEQAKALYEQALTEGKTRVKRKFIGSNLRRWDASRPIIYAFDGSHTQREQRIIELALEHWHNITCLNFQRNDQANSGNRIVFTDVDGCASNVGRHPLGEEQLVSLAPECIRLGVIAHEVAHALGFWHEQSRPDRDQYVTVRWENIDKDSKGQFLKEDPDDVDNAGVPYDYGSIMHYRSKAFSKFDDLYTISTYVTDYQKTIGQRDQLSFNDIRLM... | Cofactor: Binds 1 zinc ion per subunit.
Function: Metalloprotease which cleaves the carboxyl terminus of procollagens, such as sqt-3, to mature collagens (By similarity). Involved in cuticular collagen maturation .
Sequence Mass (Da): 67257
Sequence Length: 592
Subcellular Location: Secreted
EC: 3.4.24.-
|
D5FM38 | MKEIAHSQAYGNRVFSRDSAVDSKKDVSISAEQPKTISKLTPYLFEGDIFLSTKQAMNILDSLASKNKTNKKGQQRMAHDAPLYLFRGANEKGKRFAAEYDAKWFQFPIKYRFDESLDILHISQILKALEIWQSNTCIKFENDQEASGDYIEFFEGDGCYSMVGRFGGRQGISIGKGCERTGTIIHEVGHTLGLWHEQSRPDAEEYITVVKEYIIPSYISEFLTRSEHEITTFNVPYDLGSVMHYGSTAFSIDQRSKTLLTKDPFYQMTIGQRDSLSFYNIKLINEAYCKGDCKEKNECKNGGYLNPSNCQSCLCPSGFG... | Cofactor: Binds 1 zinc ion per subunit.
Function: Metalloprotease. Involved in molting, a process during larval stages in which a new cuticle is formed and the old cuticle is shed.
Sequence Mass (Da): 65102
Sequence Length: 581
Subcellular Location: Secreted
EC: 3.4.24.-
|
Q18206 | MRLCHSIILFNSLISISICSKADDPALLVASEFKEHFNVEEKQLETVEELLIKMKKLAHSRSFKGREFGHDAVEDSKKEVAISTQQGTINKKVSPFLFEGDIFLSRRQAVDILKALSKDKTKRLRRSFVSDKTATWKTMPIKYRFHESIDFYTISQIIAAIRFWEDSTCITFENVSDSPDGDYIEFFSGQGCYSMIGRNGGRQGISIGESCVKMGVIEHEIGHALGLWHEQSRPDALGYVTIERDFILPSYISDFLQRDDEIDTLGIPYDLGSVMHYGSTAFSVDQKSKTVVTRDSLYQQTIGQREKLSFYDVATINTAY... | Cofactor: Binds 1 zinc ion per subunit.
Function: Metalloprotease (By similarity). Involved in molting, a process during larval stages in which a new cuticle is formed and the old cuticle is shed .
Sequence Mass (Da): 69462
Sequence Length: 617
Subcellular Location: Secreted
EC: 3.4.24.-
|
Q93243 | MKSQACLKVCLALIGLVSIVSTAYIANDVVSDYAEVKELLAAFYRKHAKKYGHDYDPAAIQAIAENMDKSVKNDKTEATVNRKLWNEVFENDIILTLPQAESLLSESNSPRSRRQAHPDPRNFWPNLTISYEFYGGEETWRQLIRSAIRHVEQNVCFKFKENGGDRDGLRYYRGNGCWSNVGRVGGRQLVSIGYGCDSLGIVSHETLHALGLWHEQSRDDRDNFISIVADKITRGTEGNFAKRTAANSDNLGQPYDLGSVMHYGAKSFAYDWSSDTIKTRDWRYQNTIGQRDGLSFKDAKMINTRYCSNVCQRSLPCLNE... | Cofactor: Binds 1 zinc ion per subunit.
Function: Metalloprotease (By similarity). Plays an essential role in molting, a process during larval stages in which a new cuticle is formed and the old cuticle is shed . Required during ecdysis, the opening of the cuticle to allow the worm to escape .
Sequence Mass (Da): 85180... |
Q20942 | MPSPSYNRHIIIASCFCCLLIFSSAARVPKASKKHLARVKQLLNDEAERHNTLIQSDSVTVFDDIQRNPNTGVHHDELAVNNADEYFQGDVDLSEQQVKIIEDQFTQGKREKRKIGRNPLYKKWDTRGPISFDYAESIPFQTRQKIRSAMLLWQQHTCLRFEEGGPNVDRLEFFDGGGCSSFVGRVGGTQGISISTPGCDVVGIISHEIGHALGIFHEQARPDQERHIAINYNNIPLSRWNNFQAVGENHAETYNLPYDTGSVMHYGPYGFASDPYTPTIRTLERVQQSTIGQRAGPSFLDYQAINMAYGCTESCADLPC... | Cofactor: Binds 1 zinc ion per subunit.
Function: Metalloprotease (By similarity). As part of the innate immune response to molting and injury to the adult epidermis, positively regulates the activity of the transcription factor sta-2 to promote the expression of epidermal antimicrobial peptides such as nlp-29 . Throug... |
Q20176 | MRFSANIAIIVNIIFLFIVVEFVLPTFIRSGDVRFRRYYRNNGRVSRAATAKKERIWPEGIIPFVIASNFSGEHQHLFLRAMRHWENFTCVSFVPRQPHHKHYITFTVDKCGCCSYVGRRGEGPQAISIGKNCDKFGIVVHELGHVVGFWHEHTRPDRDMYVDIFYKSIQTGQDYNFEKSKPEEVDSLGEPYDFSSIMHYARDTFSRGAFYDTILPKPNSGFRLEIGQRVQLSEGDIRQTKKLYKCAECGGTLMQESGNLAIQHAGVCTWHIISPQGHTIFLNITGSTLSPPSSLCGKEEDNVITVRDGVSISSPVLDRI... | Cofactor: Binds 1 zinc ion per subunit.
Function: Metalloprotease.
Sequence Mass (Da): 104083
Sequence Length: 928
Subcellular Location: Secreted
EC: 3.4.24.-
|
O80483 | MGCQDEQLVQTICDLYEKISKLESLKPSEDVNILFKQLVSTCIPPNPNIDVTKMCDRVQEIRLNLIKICGLAEGHLENHFSSILTSYQDNPLHHLNIFPYYNNYLKLGKLEFDLLEQNLNGFVPKSVAFIGSGPLPLTSIVLASFHLKDTIFHNFDIDPSANSLASLLVSSDPDISQRMFFHTVDIMDVTESLKSFDVVFLAALVGMNKEEKVKVIEHLQKHMAPGAVLMLRSAHGPRAFLYPIVEPCDLQGFEVLSIYHPTDDVINSVVISKKHPVVSIGNVGGPNSCLLKPCNCSKTHAKMNKNMMIEEFGAREEQLS | Function: Synthesizes nicotianamine, a polyamine which serves as a sensor for the physiological iron status within the plant, and/or might be involved in the transport of iron.
Catalytic Activity: 3 S-adenosyl-L-methionine = 3 H(+) + nicotianamine + 3 S-methyl-5'-thioadenosine
Sequence Mass (Da): 35751
Sequence Length:... |
Q502I6 | MLNVPSQAFPAAGSQQRVAPAGQSRNKVVLKPGHSLLDWIRLTKSGQDLTGLRGRLIEVTEDELKKHNTKKDCWTCIRGMVYNLSAYMDFHPGGEEELMRAAGIDSTDLFDEVHRWVNYESMLKECLVGRMAVKPSPALQAHTEKTESTHLNGLSAPPSLRPEPLSAPLPAKDHRPRYDWFQTDGTVNIVVYTKRKIPSAGCAVVDLQDDNLRVEMLLGRMSYLLYWRLSSRVQDHVDVQTAHSVGKVQLCLRKSVKEKWTQLGQSLEHHDTFIQCKDRGLFYRECVLLSKTDVTHNTQLLRLQLPRGSRMQVPVGRHVY... | Function: NADH-cytochrome b5 reductase involved in endoplasmic reticulum stress response pathway.
Catalytic Activity: 2 Fe(III)-[cytochrome b5] + NADH = 2 Fe(II)-[cytochrome b5] + H(+) + NAD(+)
Sequence Mass (Da): 59452
Sequence Length: 527
Subcellular Location: Endoplasmic reticulum
EC: 1.6.2.2
|
Q7L1T6 | MLNVPSQSFPAPRSQQRVASGGRSKVPLKQGRSLMDWIRLTKSGKDLTGLKGRLIEVTEEELKKHNKKDDCWICIRGFVYNVSPYMEYHPGGEDELMRAAGSDGTELFDQVHRWVNYESMLKECLVGRMAIKPAVLKDYREEEKKVLNGMLPKSQVTDTLAKEGPSYPSYDWFQTDSLVTIAIYTKQKDINLDSIIVDHQNDSFRAETIIKDCLYLIHIGLSHEVQEDFSVRVVESVGKIEIVLQKKENTSWDFLGHPLKNHNSLIPRKDTGLYYRKCQLISKEDVTHDTRLFCLMLPPSTHLQVPIGQHVYLKLPITGT... | Function: NADH-cytochrome b5 reductase involved in endoplasmic reticulum stress response pathway. Plays a critical role in protecting pancreatic beta-cells against oxidant stress, possibly by protecting the cell from excess buildup of reactive oxygen species (ROS). Reduces a variety of substrates in vitro, such as cyto... |
Q6IPT4 | MMAEREEDDDTEEAWMQLRPTEPLPSQCCGSGCSPCVFDLYHRDLARWEAAQASKDRSLLRGPESQSCPSKLNPETFVAFCIIAMDRLTKDTYRVRFALPGNSQLGLRPGQHLILRGIVDDLEIQRAYTPISPANAEGYFEVLIKCYQMGLMSRYVESWRVGDTAFWRGPFGDFFYKPNQYGELLLLAAGTGLAPMVPILQSITDNENDETFVTLVGCFKTFESIYLKTFLQEQARFWNVRTFFVLSQESSSEQLPWSYQEKTHFGHLGQDLIKELVSCCRRKPFALVCGSAEFTKDIARCLLCAGLTEDSYFLF | Function: NADH-cytochrome b5 reductases are involved in desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction.
Catalytic Activity: 2 Fe(III)-[cytochrome b5] + NADH = 2 Fe(II)-[cytochrome b5] + H(+) + NAD(+)
Sequence Mass (Da): 35892
Sequence ... |
B1AS42 | MAETEEEEDSEAWLRLKPVEPLPSQCCGSGCSPCVFDLYYRDLERWETARARNDRSLLSGKQPPESQSCSAKLSPETFLAFHISTMEKVTKDTYLVRFTLPGNSRLGLRPGQHLILRGVVDGLEIQRAYTPISPVTAEGYFDVLIKCYRTGLMSQYVESWRTGDTAFWRGPFGSFLYEPKKYGELLMLAAGTGLAPMVPILQSITDDEDDETFVTLVGCFKTFEGIYLKTFFQEQARFWNVQTFFVLSQEVSPEQLPWSYRDKTHFGRLGQELVAELVACCRRKPFTLVCGSPAFNEDMARCLLSAGLTEDSYFLF | Function: NADH-cytochrome b5 reductases are involved in desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction.
Catalytic Activity: 2 Fe(III)-[cytochrome b5] + NADH = 2 Fe(II)-[cytochrome b5] + H(+) + NAD(+)
Sequence Mass (Da): 35884
Sequence ... |
Q9DDD5 | PKNSEEQKITEMVYNIFRILLYHAIKYEWGGWRVWVDTLSIAHSKVTYEAHKEYLAKMYEEYQRQEEENIKKGKKGNVSTISGLSSQTTGAKGGMEIREIEDLSQSQSPESETDYPVSTDTRDLLMATKVSDDVLGSAERPGGGVHVEVHDLLVDIKAERVEATEVKLDDMDLSPETLVTGENGALVEVESLLDNVYSAAVEKLQNSVHGSVGIIKKNEEKDGGPLITLADEKDEPSTNSTSFLFDKIPSQEEKLLPDLSISHISIPNVQDTQMHLGVNDDLGLLAHMTGGVDITSTSSIIEDKEFKIHTNSVGMSSIFE... | Function: Binds to type II regulatory subunits of protein kinase A and anchors/targets them to the membrane. May anchor the kinase to cytoskeletal and/or organelle-associated proteins (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 87803
Sequence Length: 793
Subcellular Location: Cyt... |
A4UHQ3 | MDADRIVFKVHNQLVSVKPEVIVDQYEYKYPAIKDRKKPSITLGKAPDLNRAYKSILSGINAARLDPDDVCSYLAAAMALFEGICPDDWESYGILIARKGDKITPANLVNIQRTDVEGNWALAGGLDVIKDPTTAEHASLVGLLLCLYRLSKVSGQNTGNYKTNVADRMEQIFETAPFVKIVEHHTLMTTHKMCANWSTIPNFRFLAGTYDMFFSRIEHLYSAIRVGTVVTAYEDCSGLVSFTGFIRQINLTAKEAILYFFHKNFEEEIKRMFEPGQETAVPHSYFIHFRSLGLSGKSPYSSNAVGHVFNLIHFVGSYMG... | Function: Encapsidates the genome, protecting it from nucleases. If expressed without protein P it binds non-specifically RNA and therefore can bind it's own mRNA. Interaction with protein P abolishes any non-specific RNA binding, and prevents phosphorylation. The soluble N-P complex encapsidates specifically the genom... |
P18272 | MDSRPQKIWMAPSLTESDMDYHKILTAGLSVQQGIVRQRVIPVYQVNNLEEICQLIIQAFEAGVDFQESADSFLLMLCLHHAYQGDYKLFLESGAVKYLEGHGFRFEVKKRDGVKRLEELLPAVSSGKNIKRTLAAMPEEETTEANAGQFLSFASLFLPKLVVGEKACLEKVQRQIQVHAEQGLIQYPTAWQSVGHMMVIFRLMRTNFLIKFLLIHQGMHMVAGHDANDAVISNSVAQARFSGLLIVKTVLDHILQKTERGVRLHPLARTAKVKNEVNSFKAALSSLAKHGEYAPFARLLNLSGVNNLEHGLFPQLSAIA... | Function: Oligomerizes into helical capsid to encapsidate the viral genome, protecting it from nucleases and the cellular innate immune response . VP35 binds to and stabilizes monomeric NP, keeping it soluble . Upon virus replication, NP is recruited to bind cooperatively viral genomic RNA and VP35 is released . The en... |
P69596 | MASGKAAGKTDAPAPVIKLGGPKPPKVGSSGNASWFQAIKAKKLNTPPPKFEGSGVPDNENIKPSQQHGYWRRQARFKPGKGGRKPVPDAWYFYYTGTGPAADLNWGDTQDGIVWVAAKGADTKSRSNQGTRDPDKFDQYPLRFSDGGPDGNFRWDFIPLNRGRSGRSTAASSAAASRAPSREGSRGRRSDSGDDLIARAAKIIQDQQKKGSRITKAKADEMAHRRYCKRTIPPNYRVDQVFGPRTKGKEGNFGDDKMNEEGIKDGRVTAMLNLVPSSHACLFGSRVTPKLQLDGLHLRFEFTTVVPCDDPQFDNYVKIC... | Function: Packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP) and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M. Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as vi... |
Q2UFN3 | MSAFASENLTSALLVVGTAIFAVLVGAKFLGGSGKPRKVLNPTEFQNFVLKEKNEISHNVAIYRFALPRPTDILGLPIGQHISLAATIEGQPKEVVRSYTPISSDNEAGYFDLLVKAYPQGNISKYLTTLKIGDNMKVRGPKGAMVYTPNMCRHIGMIAGGTGITPMLQIIKAIIRNRPRNGGNDTTQVDLIFANVNPEDILLKEELEQLVKEDDGFRVYYVLNNPPEGWTGGVGFVTPDMIKERLPAPAQDIKIMLCGPPPMISAMKKATESLGYTKARPVSKLEDQVFCF | Function: NADH-dependent reductase for dph3 and cytochrome b5. Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2. Dph1 and dph2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine resid... |
Q0CY37 | MSTFLQDNGDLSAVLVKFAPFAVAVIAILAAWKFTGSSKPRKVLNPSEFQNFVLKEKTDISHNVAIYRFALPRPTDILGLPIGQHISLAATIEGQPKEVVRSYTPISSDNEAGYFDLLVKAYPQGNISKYLTTLKIGDTLKVRGPKGAMVYTPNMCRHIGMIAGGTGITPMLQIIKAIIRNRPRNGGNDTTKIDLIFANVNEEDILLRDELEKLAKEDDGFRIFYVLNNPPPGWNGGFGFVTAEMIKEHLPAPAKDVKILLCGPPPMVSAMKKATESLGYTKARPVSKLEDQVFCF | Function: NADH-dependent reductase for dph3 and cytochrome b5. Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2. Dph1 and dph2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine resid... |
Q59P03 | MSETTTVPPIETVSEPNPFIVFATVATIISAFIGYYFLQQSKKHTPVLKPDEFQKFPLIEKIRVSHNSAIYRFGLPKSTDRLGLPIGQHISIGATIDGKEVVRSYTPISTDDQLGHFDLLIKTYENGNISRHVAGKNVGEHIEIRGPKGFFTYTPNMVKSFGMIAGGTGIAPMYQIITAILKNPEDKTKIHLVYANVTESDILLKEELDNFAARHPDRLKIHYVLNEAPANWQGSVGFVTPEIIDTHLPKASNDTNLLLCGPPPMVSAMKKAAVELGFQKAKPVSKLGDQVFVF | Function: NADH-dependent reductase for DPH3 and cytochrome b5. Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2. DPH1 and DPH2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine resid... |
Q6FLT3 | MDGIKILATFSVLVLFYKLFTYSKKGGVSQKEAVKALLKTEFREFELVEKEQLTHNTAKYKFKLADESHVLGLPIGQHITVKTIIGGKPVSRSYTPTSLDEECVGFFELLVKSYPEGNISKHIGDMKIGEKINISGPRGFYEYVPNVHKHLAMVAGGTGITPMFQIMKAIARDPSDKTRVTLLYGNVLEEDILLKQELDDLVKQRPDQFKITYLLDKPERDDWEGGVGYVTLDLMKESFPSAEEDVQLLVCGPPGMVSSVKRNAVALGFPRAKPVSKMEDRVFVF | Function: NADH-dependent reductase for DPH3 and cytochrome b5. Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2. DPH1 and DPH2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine resid... |
Q54NC1 | MQISDFILVIIGSVALAAGVKYVFTLTSGSNKDKKGGEAEKGKQVEKALDPQEYRKFQLKEKFIVNHNTRIFRFALPNEDDILGLPIGQHISLRAVVGGKEVYRPYTPISSDEERGYFDLLIKVYEKGAMSGYVDNMFIGDSIEVKGPKGKFNYQPNMRKSIGMLAGGTGITPMLQVIKAILKNPSDKTEISLVFGNITEEDILLKKELDELAEKHPQFKVYYVLNNPPKGWTQGVGFVSKEIIESRLPSPSDQTMVIMCGPPMMNKAMTGHLETIGFNESNIFTF | Function: Electron donor reductase for cytochrome b5. The cytochrome b5/NADH cytochrome b5 reductase electron transfer system supports the catalytic activity of several sterol biosynthetic enzymes (By similarity).
Catalytic Activity: 2 Fe(III)-[cytochrome b5] + NADH = 2 Fe(II)-[cytochrome b5] + H(+) + NAD(+)
Location T... |
Q5AZB4 | MSALSLENITGVYAPSALLVVGTFILKKEWVPFAVALAAGFVAWKLSVGGSSKPRKVLNPNEFQNFVLKEKNDISHNVTIYRFALPRPTDILGLPIGQHISLAATIEGQPKEVVRSYTPISSDNEAGYFDLLVKAYPQGNISKYLTTLKVGDTMKVRGPKGAMVYTPNMCRHIGMIAGGTGITPMLQIIKAIIRNRPRNGGNDTTQVDLIFANVNPDDILLKDELEKLAAEDDGFRIYYVLNNPPEGWTGGVGFVTPDMIKERLPAPASDIKILLCGPPPMVSAMKKATESLGYTKARPVSKLEDQVFCF | Function: NADH-dependent reductase for dph3 and cytochrome b5. Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2. Dph1 and dph2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine resid... |
B0CQN7 | MSGRVEVENIPGQVANLLKNVTAGDLLNVASSPAFLVAAAAIVIAAAFYSKVFNSTRPKPLDPSIWKEFPLQKKNQVSPNTAIYTFKLPHAEDVLGLPIGQHISVSADINGKNIVRSYTPISRQNARGRFELIIKTYEKGNISRHVASLKIGDTLRVKGPKGNFKYTPGLTAHLGMIAGGTGLAPMIQIVRAILQNPPDRTNITLIYANVNEEDILLRAELDALAMGYESRFNLFYVLNNPPSGWTGGVGFVTKEHIKDLLPNPNESNSKILICGPPPMVTAMKKNLEEIKYPVPNTISKLDDKVFVF | Function: NADH-dependent reductase for DPH3 and cytochrome b5. Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2. DPH1 and DPH2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine resid... |
A4R935 | MAPPLSSKVYVDGVYIPAALIVIGTAIVKRDWVVYSVALALALGTWKFFQLKPKKVLDPTKFQEFELKEKTIISHNVAIYRIQLPSPSSILGLPIGQHISIGADIPQPDGSSKEVVRSYTPISGDEQPGYVDLLIKSYPTGNISKYMAGLSVGQSIRVRGPKGAFVYQPNMVRHFGMIAGGTGITPMLQVVRAIVRGRAAGDTTQVDLIFANVTKEDILLKEDLDALAAEDKGFRVHYVLDRPPEGWTGGVGFVTQDMITKWLPKPADDVKILLCGPPPMVSGLKKATEALGFKKARPVSKLEDQVFAF | Function: NADH-dependent reductase for DPH3 and cytochrome b5. Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2. DPH1 and DPH2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine resid... |
Q9UR35 | MTLSNPAIAAASGVILAGAYLIDPSALPFVAAGVAATWARVLFKKTAVKTPPMDPKEYRKFKLVDKVHCSPNTAMYKFALPHEDDLLNLPIGQHISIMANINGKDISRSYTPTSSSDDVGHFVLCIKSYPQGNISKMFSELSIGDSINARGPKGQFSYTPNMCRAIGMIAGGTGLTPMLQIIRAIVKNPEDKTQVNFIFANVTEEDIILKAELDLLSQKHPQFKVYYVLNNAPEGWTGGVGFVNADMIKEHMPAPAADIKVLLCGPPPMVSAMSKITQDLGYDKVNAVSKLPDQVFKF | Function: NADH-dependent reductase for DPH3 and cytochrome b5. Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2. DPH1 and DPH2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine resid... |
A1DHW1 | MSALSSENINGVYIPSALLIFGTFIVKKEFVPYAVALTAILAGLKLFTGGSKPRKVLNPTEFQEFVLKEKTDISHNVCIYRFALPRPADILGLPIGQHISLAATIEGQPKEVVRSYTPISSDNEAGYFDLLVKAYPQGNISKYLTTLKIGDTMKVRGPKGAMVYTPNMCRHIGMIAGGTGITPMLQIIKAVIRNRPRNGGNDTTKLDLIFANVNPDDILLKEELDKLAAEDPDFNIYYVLNNPPQGWTGGVGFVTPEMIKEHLPAPASDVKILLCGPPPMISAMKKATESLGYTKARPVSKLEDQVFCF | Function: NADH-dependent reductase for dph3 and cytochrome b5. Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2. Dph1 and dph2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine resid... |
A5DQ25 | MSQNEPNPLVIFSTLAAIILAAVAVYVVKLNKKNGPVLKPDVFQKFPLIEKTRLSHNTCIYRFGLPKSTDRLGLPIGQHISIGATINGKEVVRSYTPISRDDELGYFDLLIKTYEQGNISRHVDSKSVGDHIEVRGPKGFFTYTPNMVEHLGMIAGGTGIAPMYQVLTAILTNPDDKTKISLVYANVTEEDILLRAELDLFAKEHPDRFKVHYVLNNAPENWNGSVGFVTPEIMEKHLPNKDQDGYLLLCGPPPMISAMKKNAVTLGYPKARPVSKLGDKVFVF | Function: NADH-dependent reductase for DPH3 and cytochrome b5. Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2. DPH1 and DPH2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine resid... |
O46383 | DPGSQGVGAEAENTGERTGGEAEAPAEGENGERSGGDAALGGESEGKAENESEGDIPAERRGDDEDEGEIQAEGGEVKGDEDEGEIQAGEGGEVEGDEDEGEIQAGEGGEVEGDEDEGEIQAGEGGEVEGDEDEGEIQAGEGGEVKDDEGEIQAGEAGEVEGEDGEVEGGEDEGEIQAGEGGEGETGEQELNAEIQGEAKDDEEGVDGEGGGDGGDSEDEEEEDEEEDEEEEEEEEEEEEEENEQPLSLEWPETRRKQAIYLFLLPIVFPLWLTVPDVRRLEAKKFFVITFLGSILWIAM | Function: Calcium, potassium:sodium antiporter that transports 1 Ca(2+) and 1 K(+) in exchange for 4 Na(+). Critical component of the visual transduction cascade, controlling the calcium concentration of outer segments during light and darkness. Light causes a rapid lowering of cytosolic free calcium in the outer segme... |
Q9IAL8 | MHLPRRRRLQRNRIFFFLAVVSLLSVYQLQFSPSAIPALLTAHQHEDPVKVTSREPFRNKTSKTGNVTAAPKIRHCVYIDPEPTVPITASEDTTQRENVNESYPDEKPVYESKGEYPQDLFSVEERRQGWVVLHIFGMMYVFVALAIVCDEYFVPALGVITEKLQISEDVAGATFMAAGGSAPELFTSLIGVFISHSNVGIGTIVGSAVFNILFVIGTCALFSREILHLTWWPLFRDISFYIVDLLMLILFFLDSVIDWWESLLLLTAYATYVFTMKHNVSLEQWVKEELSKKLNAVQAASAEHMRKKSSVAVAEDGTKP... | Function: Calcium, potassium:sodium antiporter that transports 1 Ca(2+) and 1 K(+) in exchange for 4 Na(+) . Critical component of the visual transduction cascade, controlling the calcium concentration of outer segments during light and darkness. Light causes a rapid lowering of cytosolic free calcium in the outer segm... |
Q9IAL7 | MALCKKTVGSVLEEWCLNEPLFGCKRHQNVRKKLRLIRIIGLLVSVVAISTFSLSISAFFKMETHSTVLASSLESQKLVHGHQRTLLDFMEQNEGSTPDSPTSMKHEAEHDNATEEHSKGEYPEDLFSLEERRKGAVILHVIGMIYMFIALAIVCDEFFVPSLTVITEKLSISDDVAGATFMAAGGSAPELFTSLIGVFISHSNVGIGTIVGSAVFNILFVIGMCALFSREILNLTWWPLFRDVSFYIVDLILLIIFFLDNLIMWWESLTLLTAYFCYVTFMKFNVQVEEWVKKVLNRNKVEKATTGDAEGKSPTAGDKD... | Function: Calcium, potassium:sodium antiporter that transports 1 Ca(2+) and 1 K(+) in exchange for 4 Na(+) . Required for learming and memory by regulating neuronal Ca(2+), which is essential for the development of synaptic plasticity (By similarity).
Catalytic Activity: Ca(2+)(out) + K(+)(out) + 4 Na(+)(in) = Ca(2+)(i... |
Q9UI40 | MDLQQSTTITSLEKWCLDESLSGCRRHYSVKKKLKLIRVLGLFMGLVAISTVSFSISAFSETDTQSTGEASVVSGPRVAQGYHQRTLLDLNDKILDYTPQPPLSKEGESENSTDHAQGDYPKDIFSLEERRKGAIILHVIGMIYMFIALAIVCDEFFVPSLTVITEKLGISDDVAGATFMAAGGSAPELFTSLIGVFIAHSNVGIGTIVGSAVFNILFVIGMCALFSREILNLTWWPLFRDVSFYIVDLIMLIIFFLDNVIMWWESLLLLTAYFCYVVFMKFNVQVEKWVKQMINRNKVVKVTAPEAQAKPSAARDKDEP... | Function: Calcium, potassium:sodium antiporter that transports 1 Ca(2+) and 1 K(+) in exchange for 4 Na(+) . Required for learming and memory by regulating neuronal Ca(2+), which is essential for the development of synaptic plasticity (By similarity).
Catalytic Activity: Ca(2+)(out) + K(+)(out) + 4 Na(+)(in) = Ca(2+)(i... |
O54701 | MDLHQSATVRLLQEWCSHESPSGCRRHYNTRKKLKLIRVIGLVMGLVAVSTVPFSISAFTETYSQNNRGEASDVTGPRAAPGHRQRTLLDLNDKIRDYTPQPPASQEDRSENGTDHAQGDYPKDVFSLEERRKGAIILHVIGMIYMFIALAIVCDEFFVPSLTVITEKLGISDDVAGATFMAAGGSAPELFTSLIGVFIAHSNVGIGTIVGSAVFNILFVIGMCALFSREILNLTWWPLFRDVSFYIVDLIMLIIFFLDNVIMWWESLLLLTAYFAYVVFMKFNVQVERWVKQMINRNKVVKVTVSEAQAKASTAGDKEE... | Function: Calcium, potassium:sodium antiporter that transports 1 Ca(2+) and 1 K(+) in exchange for 4 Na(+) . Required for learming and memory by regulating neuronal Ca(2+), which is essential for the development of synaptic plasticity (By similarity).
Catalytic Activity: Ca(2+)(out) + K(+)(out) + 4 Na(+)(in) = Ca(2+)(i... |
Q9HC58 | MRPSGDEDRARRRRRRRRRRDLLLSQLCFLASVALLLWSLSSLREQKELDLMDLVGEDRKWMMARKLMQVNDTLTSEDAGLRNSKNCTEPALHEFPNDIFTNEDRRQGAVVLHVLCAIYMFYALAIVCDDFFVPSLEKICERLHLSEDVAGATFMAAGSSAPELFTSVIGVFITKGDVGVGTIVGSAVFNILCIIGVCGLFAGQVVALSSWCLLRDSIYYTLSVIALIVFIYDEKVSWWESLVLVLMYLIYIVIMKYNACIHQCFERRTKGAGNMVNGLANNAEIDDSSNCDATVVLLKKANFHRKASVIMVDELLSAYP... | Function: Calcium, potassium:sodium antiporter that transports 1 Ca(2+) and 1 K(+) in exchange for 4 Na(+).
Catalytic Activity: Ca(2+)(out) + K(+)(out) + 4 Na(+)(in) = Ca(2+)(in) + K(+)(in) + 4 Na(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71992
Sequence Length: 644
Subcellular Location:... |
Q8C567 | MLPTLTALLCLGLCLSQRINTEKETLPKPIIWAKPSIMVTNGNSVNIWCQGAQSASEYQLYFEGSFFALERPKPSRSMNKVRFFISQMTSHTAGIYTCFYQSGELWSKSSNPLKLVVTGLYDTPNLWVYPRPEVTLGENVTFFCQLKTATSKFFLLKERGSNHIQNKYGNIQAEFPMGPVTRAHRGTYRCFGSYNDYAWSFPSEPVTLLITGGVENSSLAPTDPTSSLDYWEFDLSTNESGLQKDSAFWDHTTQNLIRIGLACIILITLVWLLTEDWLSKRKDHEEANRLTNWECRRRWRMQHYFEEEQRNAISMMELKA... | Function: Cytotoxicity-activating receptor that may contribute to the increased efficiency of activated natural killer (NK) cells to mediate tumor cell lysis.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 37266
Sequence Length: 325
Subcellular Location: Cell membrane
|
Q9Z0H5 | MLPTLTALLCLGLCLSQRINTEKQTLPKPIIWAKPSIMVTKGNSVNIWCQGAQSASEYQLYFEGSFFALERPKSSRSMNKVKFFISQMTSHTAGIYTCFYQSGELWSESSNPLKLVVTGLYDTPTLWVHPGPEVTLGENVTFSCHLKTATSKFFLLKERESNHIQHKYGNIQAEFPMGPVTRAHRGTYRCFGSYNDYAWSFPSEPVTLLITGEVENTSLAPTDPVSSLDYWEFDLSTKESGLQKDSAFWDHTAQNLIRIGLACIIVMALVWLLAEDWLSRRKDHEKLNRLTSWECRGRRRMHRYHEEEQRDAISMRELKA... | Function: Cytotoxicity-activating receptor that may contribute to the increased efficiency of activated natural killer (NK) cells to mediate tumor cell lysis.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 37178
Sequence Length: 325
Subcellular Location: Cell membrane
|
O95944 | MAWRALHPLLLLLLLFPGSQAQSKAQVLQSVAGQTLTVRCQYPPTGSLYEKKGWCKEASALVCIRLVTSSKPRTMAWTSRFTIWDDPDAGFFTVTMTDLREEDSGHYWCRIYRPSDNSVSKSVRFYLVVSPASASTQTSWTPRDLVSSQTQTQSCVPPTAGARQAPESPSTIPVPSQPQNSTLRPGPAAPIALVPVFCGLLVAKSLVLSALLVWWGDIWWKTMMELRSLDTQKATCHLQQVTDLPWTSVSSPVEREILYHTVARTKISDDDDEHTL | Function: Cytotoxicity-activating receptor that may contribute to the increased efficiency of activated natural killer (NK) cells to mediate tumor cell lysis.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 30677
Sequence Length: 276
Subcellular Location: Cell membrane
|
O14931 | MAWMLLLILIMVHPGSCALWVSQPPEIRTLEGSSAFLPCSFNASQGRLAIGSVTWFRDEVVPGKEVRNGTPEFRGRLAPLASSRFLHDHQAELHIRDVRGHDASIYVCRVEVLGLGVGTGNGTRLVVEKEHPQLGAGTVLLLRAGFYAVSFLSVAVGSTVYYQGKCLTWKGPRRQLPAVVPAPLPPPCGSSAHLLPPVPGG | Function: Cell membrane receptor of natural killer/NK cells that is activated by binding of extracellular ligands including BAG6 and NCR3LG1. Stimulates NK cells cytotoxicity toward neighboring cells producing these ligands. It controls, for instance, NK cells cytotoxicity against tumor cells. Engagement of NCR3 by BAG... |
Q05777 | MKACSILFTTLITLAAAQKDSGSLDGQNSEDSSQKESSNSQEITPTTTKEAQESASTVVSTGKSLVQTSNVVSNTYAVAPSTTVVTTDAQGKTTTQYLWWVAESNSAVSTTSTASVQPTGETSSGITNSASSSTTSTSTDGPVTIVTTTNSLGETYTSTVWWLPSSATTDNTASSSKSSSGSSSKPESSTKVVSTIKSTYTTTSGSTVETLTTTYKSTVNGKVASVMSNSTNGAFAGTHIAYGAGAFAVGALLL | Function: Cell wall biogenesis protein that participates in the organization of the beta-glucan assembly . Involved in the mechanism responsible for cell tolerance to polyhexamethylene biguanide (PHMB), an antifungal agent .
Location Topology: Lipid-anchor
Sequence Mass (Da): 25762
Sequence Length: 254
Subcellular Loca... |
O16242 | MCSSEECLIDKSWTSEEKCEYIKCNQDSCEGGGYLTWSHYVKCQYNIGVRVILIILGILYLIILFVIMSSIADDFFCPAISGIVSHLRMSESIAGVTFLAFGNGAPDVFSSISSVLTTPKPKADLALGDLFGTSIFVTTVVLAIIIFTKSFKVAIIPTLRDLIFYMTTLAFIVFCFLKFDKIEVWMPATFLGIYGVYVVTVIILGIYRTHRKKRNLKKKNKELEDFLSRPSSAASTTPIFGAMKLKEETISVSALFHFMIGYSQFIKNLTRANLKRTTNNNNNDNKNEKRGIVNLGFSEPYSIPSERKISTIFKQNTFET... | Function: Mitochondrial sodium/calcium antiporter that mediates sodium-dependent calcium efflux from mitochondrion, thereby acting as a key regulator of mitochondrion calcium homeostasis (Probable). Required for patterning of neural circuits: functions in the same pathway as RAC-dependent effectors of the unc-6/netrin ... |
Q8GWA1 | MLWIKNLARISQTTSSSVGNVFRNPESYTLSSRFCTALQKQQVTDTVQAKEDVVNALEPQRYDGLAPTKEGEKPRVLVLGSGWAGCRVLKGIDTSIYDVVCVSPRNHMVFTPLLASTCVGTLEFRSVAEPISRIQPAISREPGSYYFLANCSKLDADNHEVHCETVTEGSSTLKPWKFKIAYDKLVLACGAEASTFGINGVLENAIFLREVHHAQEIRRKLLLNLMLSEVPGIGEDEKKRLLHCVVVGGGPTGVEFSGELSDFIMKDVRQRYSHVKDDIRVTLIEARDILSSFDDRLRHYAIKQLNKSGVKLVRGIVKEV... | Cofactor: Binds 1 FAD per subunit.
Function: Alternative NADH-ubiquinone oxidoreductase which catalyzes the oxidation of mitochondrial NADH does not translocate protons across the inner mitochondrial membrane.
Catalytic Activity: a quinone + H(+) + NADH = a quinol + NAD(+)
Location Topology: Peripheral membrane protein... |
Q9ST63 | MPWFKNLIKISKTITNQSSSYKSITPLASPLLTQFLQFTKQYSTNDHVVGLEATKSDQKPRIVVLGSGWAGCRLMKDIDTNIYDVVCVSPRNHMVFTPLLASTCVGTLEFRSVAEPIGRIQPAVSTQPASYFFLANCNAIDFDNHMIECETVTEGVETLEAWKFNVSYDKLVIASGAHALTFGIKGVNEHATFLREVHHAQEIRRKLLLNLMLSDVPGVSEEEKRRLLHCVVVGGGPTGVEFSGELSDFILKDVHQRYAHVKDYIHVTLIEANEILSSFDDRLRVYATNQLTKSGVRLVRGLVQHVQPDNIILSDGTNVP... | Cofactor: Binds 1 FAD per subunit.
Function: Alternative NADH-ubiquinone oxidoreductase which catalyzes the oxidation of mitochondrial NADH does not translocate protons across the inner mitochondrial membrane.
Catalytic Activity: a quinone + H(+) + NADH = a quinol + NAD(+)
Location Topology: Peripheral membrane protein... |
O80874 | MFMIKNLTRISPNTSSIITRFRNSGSSSLSYTLASRFCTAQETQIQSPAKIPNDVDRSQYSGLPPTREGEKPRVVVLGSGWAGCRLMKGIDTNLYDVVCVSPRNHMVFTPLLASTCVGTLEFRSVAEPISRIQPAISREPGSFFFLANCSRLDADAHEVHCETLTDGLNTLKPWKFKIAYDKLVIASGAEASTFGIHGVMENAIFLREVHHAQEIRRKLLLNLMLSDTPGISKEEKRRLLHCVVVGGGPTGVEFSGELSDFIMKDVRQRYAHVKDDIHVTLIEARDILSSFDDRLRRYAIKQLNKSGVRFVRGIVKDVQS... | Cofactor: Binds 1 FAD per subunit.
Function: Alternative NADH-ubiquinone oxidoreductase which catalyzes the oxidation of mitochondrial NADH does not translocate protons across the inner mitochondrial membrane.
Catalytic Activity: a quinone + H(+) + NADH = a quinol + NAD(+)
Location Topology: Peripheral membrane protein... |
Q8GXR9 | MAVLSSVSSLIPFSYGATRLTSKASLASRTSGFNLSSRWNSTRNSPMLYLSRAVTNNSGTTEISDNETAPRTYSWPDNKRPRVCILGGGFGGLYTALRLESLVWPEDKKPQVVLVDQSERFVFKPMLYELLSGEVDVWEIAPRFSDLLTNTGIQFLRDRVKTLLPCDHLGVNGSEISVTGGTVLLESGFKIEYDWLVLALGAESKLDVVPGAMELAFPFYTLEDAIRVNEKLSKLERKNFKDGSAIKVAVVGCGYAGVELAATISERLQDRGIVQSINVSKNILTSAPDGNREAAMKVLTSRKVQLLLGYLVQSIKRASN... | Cofactor: Binds 1 FAD per subunit.
Function: Bifunctional oxidoreductase ables to act both on prenyl naphthoquinones and on prenyl benzoquinones . May serve a respiratory function . Involved in an electron flow toward the plastoglobule plastoquinone pool . Required for plastochromanol-8 accumulation and for phylloquino... |
Q8I4N3 | MMGDSHSSFTTTTDEHLYNQFSPGRRKNDFPAASSSSSSPNLRRSPNRTVSSPRVQQKPITIFDQIVDWFQAEISVRKRLAGAACGYLSTIFFIVTVSILKLTIWAPFSSVQDSLAWWIYPNAWASIIFVGIASVAMSLFSIIKFCKVDQLPRLAATDTFALAGVALEFVTRLTFVYTAFCVADFSFSREFAFVAISLAIAISSALVVFRSDYQLNFSHIQVNSVKTLIDFGTSLPYANISEICGIDAAISYTAAVALILVVGPMVSGFSAWWLLLNIPFHVVLFGLCFTQQFYSKISMKIVNQIVMKPISFPFPPPYTV... | Function: Component of the nuclear pore complex (NPC), which plays a key role in de novo assembly and insertion of NPC in the nuclear envelope (By similarity). Plays a role in postmitotic nuclear pore complex assembly potentially by promoting localization of nuclear pore complex proteins to the nuclear rim .
Location T... |
G0S235 | MAAAVRRSPYKDFLQPALQRRFATATLVVLATAYFEALLLARWSSWLWSWFPLGPTGFRAALFFLCGIFVIILRISQYHPGIRTSDSPIATLVRYAPRWTTFETLFTYALSAWIFSLVYLGTVPDDAGFERITYFTYDRARLNEKPIFLTTHLVLLGIYQGVRHLYSDIDRLSLGTAQPSNGDSSKATGEDGHVSTQMRRFRDQLPKIVVHSLHQSVMGLLLSASLYPLLLRDLLWRVNMTMLRPLYSLPRTNVPPANLPYSPSTLLRCLAASVMVMFAWTAANTAFSLLLVKSPLKNGKPLTADAKDPNGSLLNGLKNK... | Function: Functions as a component of the nuclear pore complex (NPC) and the spindle pole body (SPB), probably by playing a key role in de novo assembly and insertion of both structures in the nuclear envelope. NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural com... |
Q9VCG4 | MSASSSSNACKLLLLGRCLRAVLLSVAIQFLLLTVFLLFVNFQLLHPLAWVTGTLRLVASWYTWFASIPLVASVVLYGVILCQQHLSERRYCPTRYRWLLHYGPRKVLFLFAHLLVGLLTAWLYTGYLHTDYQHLKYKCYGQDCISAYNVYLLGIGMTAGCYYFVSVHMRKEISIEFPIVEQSRAEKMRELLYASLAKSLLSSLLPTISYTAVFCLFGPMVCHRLSHILSVDMDERLDGFFGVVTNVRLLFYGYLLTAQILSNMHLMRCFYGILLSEDLPLVVTKPRAAFAHEQDITLVAGLGVFNVYVVQCLAAHHFYK... | Function: Component of the nuclear pore complex (NPC), which plays a key role in de novo assembly and insertion of NPC in the nuclear envelope.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 65387
Sequence Length: 578
Subcellular Location: Nucleus
|
Q9BTX1 | MATAVSRPCAGRSRDILWRVLGWRIVASIVWSVLFLPICTTVFIIFSRIDLFHPIQWLSDSFSDLYSSYVIFYFLLLSVVIIIISIFNVEFYAVVPSIPCSRLALIGKIIHPQQLMHSFIHAAMGMVMAWCAAVITQGQYSFLVVPCTGTNSFGSPAAQTCLNEYHLFFLLTGAFMGYSYSLLYFVNNMNYLPFPIIQQYKFLRFRRSLLLLVKHSCVESLFLVRNFCILYYFLGYIPKAWISTAMNLHIDEQVHRPLDTVSGLLNLSLLYHVWLCGVFLLTTWYVSWILFKIYATEAHVFPVQPPFAEGSDECLPKVLN... | Function: Component of the nuclear pore complex (NPC), which plays a key role in de novo assembly and insertion of NPC in the nuclear envelope. Required for NPC and nuclear envelope assembly, possibly by forming a link between the nuclear envelope membrane and soluble nucleoporins, thereby anchoring the NPC in the memb... |
Q8VCB1 | MATAASGPCAGGSPRDILWRVLGWRIVTSIVWSVVLLPVCITAFIVLSSINLFHPIQWLSDSCNDFYSSQVIFHLLLLAVVIIIISIFNVEFYTVVPSISGSRLALIARILHPQQLTHSFIHAAMGMAVAWCAAIMTKGQYSSLVVPCTGTESLDSPAAQTCLNEYHLFFLLSGAFMGYSYSLLYFINNMNYLPFPIIQQYKFLRFRRSLLLLVKHSCVESLFMVRNFCIVYYFFGHIPKAWISTALDLHTDEQAHRPLDTIGGLLNVSLLYHVWLCGVFLLVTWYSSWILFKIYATEAHVFPVQPPFAEASDECLPKVL... | Function: Component of the nuclear pore complex (NPC), which plays a key role in de novo assembly and insertion of NPC in the nuclear envelope. Required for NPC and nuclear envelope assembly, possibly by forming a link between the nuclear envelope membrane and soluble nucleoporins, thereby anchoring the NPC in the memb... |
O13961 | MVMLRTSFPSGSRTKAVRYHTLLRPILQQRFLRACFALLCLCCITSYWFSSGPFISLSFWFLSLVRGFVCFFFMFPYFVMLKSRMSTQKVTKQSLGAQLFYDFSPKSFFLVYLTFAVSVSCLCLFYIKGHASSIRLQWIASPNAYELPSLNERFVYMTYFSHILILALTVEHLYLQRDSPSRPVINVSFFNYIFQNLGWLIRFSFRKSIICCLFTPFSYAILRSYIWRFAALLTSCCRRIAYTKTPPKWPLSLRLLLHSFWMAFIVCLTFQIALLIFRVFLYSGPMIRGKLLSARSNDPNGTLVDGMKTKKKPLTECIAT... | Function: Component of the nuclear pore complex (NPC) and the spindle pole body (SPB), which plays a key role in de novo assembly and insertion of both structures in the nuclear envelope. Involved in the formation of the bipolar mitotic spindle. Anchors the spindle pole body in the nuclear envelope.
Location Topology: ... |
P32500 | MIQTPRELLNPRYTYHTIFSDVCKTRFNHLVTRLFFICSIIQTVVISLLALPHSPLWELALAFIPNILALNLVSLLIIVTRKNYMHVKNFGFANSLTFILGQLLSVKFLVYQGVYSMGSILLSFVLGVVFGRGGSGWKPYYKLFIWLVVPTIYNLQHHVTDADKLSFNCENFFQAPQDYVLERVKRIMEKSVILSVISMFVLPIFTTVFFSRQKSGLFDSFTNGVLAVTNLLIISCIIFITFEFINIAFDAHMSIGCLHKGKLISNLSSTPMETLLSGLSADKPFTRLTAYQELAYRATSLDPSLRAPIYHSKFRSSSGN... | Function: Functions as a component of the nuclear pore complex (NPC) and the spindle pole body (SPB), probably by playing a key role in de novo assembly and insertion of both structures in the nuclear envelope. In SPB duplication NDC1 is required for the insertion of the cytoplasmic side of the SPB in the nuclear envel... |
P27724 | MTKIETRTEPMVLNMGPHHPSMHGVLRLIVTLDGEDVVDCEPVIGYLHRGMEKIAESRTNIMYVPYVSRWDYAAGMFNEAITVNAPEKLADIEVPKRAQYIRVIMLELNRIANHLLWLGPFMADVGAQTPFFYIFREREMIYDLWEAASGMRLINNNYFRVGGVAVDLPYGWNDKCEDFCDYFLPKVDEYEKLITNNPIFRRRVEGVGTVTREEAINWGLSGPMLRGSGVKWDLRKVDHYECYDELDWEVQYETAGDCFARYLVRIREMRESVKIIRQALKAMPGGPYENLEAKRLQEGKKSEWNDFQYQYIAKKVAPTF... | Function: NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, a... |
A4GGF0 | MFLMVTEFINYSEQIIRAARYIGQGLMITLSHANRLPVTIQYPYEKIISSERFRGRIHFEFDKCIACEVCVRVCPIDLPIVDWKLETDIRKKRLLNYSIDFGICIFCGNCIEYCPTNCLSMTEEYELSTYDRHELNYNLIALGRLPVSVIDDYTIRTIQIK | Cofactor: Binds 2 [4Fe-4S] clusters per subunit.
Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ... |
P19050 | MSPNPANPTDLERVATAKILNPASRSQVTQDLSENVILTTVDDLYNWAKLSSLWPLLYGTACCFIEFAALIGSRFDFDRFGLVPRSSPRQADLIITAGTITMKMAPALVRLYEEMPEPKYVIAMGACTITGGMFSSDSTTAVRGVDKLIPVDVYIPGCPPRPEAIFDAIIKLRKKVANESIQERAITQQTHRYYSTSHQMKVVAPILDGKYLQQGTRSAPPRELQEAMGMPVPPALTTSQQKEQLNRG | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox... |
P17062 | MSTSTHALTLQNPIQAPQVTKELSENVILTCLDDIYNWARLSTLYPMMFGTACCFMEFMAAFGPRFDLERFGSIPRATPRQADLMITAGTITMKYAPALVQLYEQIPEPKYVIAMGACTITAGMFSADSPTAVRGVDKLIPVDVYIPGCPPRPEAVIDGIIKLRKKVAGESRQDYTEDLQTHRFHAVRHRMKPVSPILTGQYLRHHEDLTPHHDPLLIK | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox... |
Q85FL6 | MVLTSDHLDKKNIRKIEYKGEDSFSNSMSKLPLQGGMSDSIFMASISDFSNWSRLSSLWPLLYGTSCCFIEFASLIGSRFDFDRYGLVPRSSPRQADLIVTAGTITMKMAPSLIRLYEQMPEPKYVIAMGACTITGGMFSTDSYSTVRGVDKLIPVDIYLPGCPPKPEAIMDAVTKLRKKIARNRFVNRASRPIRTKYFSISHQLNLVPGTCAGKYNWDRENCGTKLAPANFSENCQKFANEHDELKSAI | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone... |
Q8DLN5 | MLLKSTTRHVHIYAGHVVDGEVHPDTETLTLNVDPDNELEWNEAALAKVEAKFRELVANAAGEDLTEYNLRRIGSDLEHFIRSLLMQGEIGYNLNSRVRNYSLGIPRVNHS | Function: NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, a... |
B7H073 | MAIERTLSIVKPDAVSKNHIGEIFARFEKAGLKIVATKMKHLSQADAEGFYAEHKERGFFGDLVAFMTSGPVVVSVLEGENAVLAHREILGATNPKEAAPGTIRADFAVSIDENAAHGSDSVASAEREIAYFFADNEICPRTR | Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
Catalytic Activity: ATP + dZDP = ADP + dZTP
Sequence Mass (Da): 15462
Sequence Length: 143
Pathwa... |
A3MZ69 | MIQQTLCLIKPDATQRNLIGKILSHLEEAGLTIKALKKVQLNQEQAEGFYAEHQGKEFFAPLVEFMISAPIVAVVLEGENAIAHYRELMGATNPEQRKAGTIRALYAISGRENSVHGSDSEQSAKREIAYFFTPNEIL | Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-t... |
A6VMK7 | MALERTLSIIKPDAVERNLVGKILSRFEENGFQIVAMKMLRLNQAQAEGFYAEHQGKPFFDGLVEYMTSAPVVVSVLEKDNAVKDYRTLIGATDPQQAAEGTIRKDFAESRRRNSVHGSDSEESAVREIAYFFVESEICPR | Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-t... |
Q9PIG7 | MEKTLSIIKPDAVKKGVIGKILDRFESNGLRIAAMKKVQLSKEQAENFYAVHKERPFFKDLVEFMISGPVVVSILEGEGAVLKNRDLMGATNPKEAKAGTIRADFAESIDANAVHGSDSLENAKIEIEFFFKPNEIC | Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-t... |
P56075 | MKQRTLSIIKPDALKKKVVGKIIDRFESNGLEVVAMKRLHLSVKDAENFYAIHRERPFFKDLIEFMVSGPVVVMVLEGKDAVAKNRDLMGATDPKLAQKGTIRADFAESIDANAVHGSDSLENAHNEIAFFFAARDL | Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-t... |
A1SMD1 | MSLRTLVLLKPDAVRRGLVGAILSRYEAKGLTIVAMEQRTIDAAVADQHYAEHVAKEFYPPLRDFVTGGPLVALVLEGDNSVDVVRLLNGATDGSKAAPGTIRGDFSLSNRENLVHGSDSPESAEREIGIWFPGL | Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-t... |
B2IX22 | MERTFLAIKPDGVQRGLVGEIIRRFETKGFTLVGLKFLKVSKELAEQHYGVHRERPFFGSLVEFITSSPVVAMVWEGDGVVASARKIIGATNPLTSEPGTIRGDFGINIGRNLIHGSDAPETAQQEIALWFKDEELVNWQPHITPWLHE | Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-t... |
A6LCB6 | MEKTLVILKPCTVQRGLIGEIVTRFEKKGLRLAGMKMVWLTDEILSEHYAHLKEKPFFQRIKDAMSVCPVIVCCWEGVDAIHVVRTLAGTTNGRNAAPGTIRGDYSMSVQENIVHASDSPETAEIELKRFFKDDEIFDYELKNLLSLYANDEF | Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-t... |
Q9CM17 | MAVERTLSLIKPDAVKRHLIGAILSRFEQAGFRVVAAKMLHLTQAQAEGFYAEHQDKAFFPELVAYMISAPVLALVLEKENAVKDYRTLIGATNPAVAAEGTIRRDFAIDGRHNSVHGSDSLDSAKREIAYFFVESEIF | Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-t... |
Q0I6J3 | MAAERSFIAIKPDGVQRGLVGEILGRFERKGFKLVGLKQLTPSRELAEQHYGVHKERPFFGGLVDFITSGPVVAMVWEGDGVITSARKMIGATKPLEAEPGTIRGDLAINIGRNVIHGSDAPETAEFEIGLWFNPSELSDWTPSDQTWRVEG | Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
Catalytic Activity: ATP + dZDP = ADP + dZTP
Sequence Mass (Da): 16661
Sequence Length: 152
Pathwa... |
A6LJZ9 | MERTFVYLKPNAVRRGLVGEIIKRFEQRGIKIVALKLFWMTREQAERLYEMHKGKNFYNELIEFVTGGPVVAMVVEAPRVIEMVRHIIGNTDPLKAGTGTIRGEFALTVTKNLIHASDSKENFEREYKIFFSENEIVDYYLDVQDDI | Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-t... |
B0KAQ8 | METTLAIVKPDGVKRGLIGEILKRYENKGLRLKAAKVITPTIELLEKHYEEHKGKPYYKPLIQYMSSGPVFAMVLEGENAVKIVRLLNGATKVEEALPGTIRGDFAISTTFNIIHGSDSIESAKREIALWFPELA | Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-t... |
Q5SLV5 | MERTFVMIKPDGVRRGLVGEILARFERKGFRIAALKLMQISQELAERHYAEHREKPFFPGLVRFITSGPVVAMVLEGPGVVAEVRKMMGATHPKDALPGTIRGDFATTIDENVIHGSATLEDAQREIALFFRPEELL | Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-t... |
Q8DM56 | MERTFLAIKPDGVQRGLVGTIIQRFEQKGYTLVGLKLMRVSRELAEQHYGEHKDKPFFPGLVNFITSGPVVAMVWEGRGVIANARKLIGATNPLNAEPGTLRGDFAVDVGRNVIHGSDSPENAEREINLWFQTQELVPWEPALTSWVYEM | Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-t... |
Q97BK5 | MDRTLVLLKPDAVKRRLVGKIIERFEEKGLKIVAMKFMQMTKDQAKTHYSVHQNKPFFNDLVNYITSGPIVAMILEGAHAIEIVRLMSGATDGSKAQPGTIRGDYSMGIEKNIIHASDSLEAYNHEMPIFFSDNEIIEWAYGDEVIY | Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-t... |
Q54F42 | MSSNMQAMKQMRPALVSLTQQQARRRCFKLYRNCIRSIPHLIQHYNLSYNMSEMRNRFRSNFVEFEEVTEKNQLDRLAFIGETELFDAMSLLKTRSHVVNYFDTQPVNAKTISESEKLLNNFFE | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed to be not involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (... |
P56556 | MAGSGVRQATSTASTFVKPIFSRDMNEAKRRVRELYRAWYREVPNTVHQFQLDITVKMGRDKVREMFMKNAHVTDPRVVDLLVIKGKIELEETIKVWKQRTHVMRFFHETEAPRPKDFLSKFYVGHDP | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed to be not involved in catalysis. Required for proper complex I assembly . Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for ... |
Q9CQZ5 | MAAAATGLRQAAAAAASTSVKPIFSRDLNEAKRRVRELYRAWYREVPNTVHLMQLDITVKQGRDKVREMFMKNAHVTDPRVVDLLVIKGKMELQETIKVWKQRTHVMRFFHETETPRPKDFLSKFYMGHDP | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed to be not involved in catalysis. Required for proper complex I assembly. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for t... |
P42114 | MPITPTKYAITTRQSANWSDAKRRVFALYRRWLRSTPEMQSMYSLPLPISVIRTRIRQEFERNRFVNKLPVVDVLLTKGHADYQETMNFWRQTTHMMSYFNEESFRGAKRLPSSFIDGFLQGRN | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed to be not involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. ... |
Q05752 | MASATRFIQWLRNWASGRDLQAKLQLRYQEISKRTQPPPKLPVGPSHKLSNNYYCTRDGRREAMPPSIVMSSQKVLVAGKPAESSAVAASEKKAVSPAPPIKRWELSQDEPYL | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
... |
O95182 | MASATRLIQRLRNWASGHDLQGKLQLRYQEISKRTQPPPKLPVGPSHKLSNNYYCTRDGRRESVPPSIIMSSQKALVSGKPAESSAVAATEKKAVTPAPPIKRWELSSDQPYL | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
... |
Q9Z1P6 | MASATRVIQKLRNWASGQDLQAKLQLRYQEIAKRTQPPPKLPVGPSHKLSNNYYCTRDGRREVVPPSIIMSSQKALVSGKAAESSAMAATEKKAVTPAPPMKRWELSKDQPYL | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
... |
Q0MQA6 | MASATRLIQRLRNWASGQDLQAKLQLRYQEISKRTQPPPKLPVGPSHKLSNNYYCTRDGRRESVPPSIIMSSQKALVSGKPAESSAVAATEKKAVTPAPPIKRWELSSDQPYL | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
... |
P42029 | MPGIVELPSLEDLKVQEVKVSSSVLKAAAHHYGAQCDKPNKEFMLCRWEEKDPRRCLEEGKLVNQCALEFFRQIKRHCAEPFTEYWTCIDYSGLQLFRRCRKQQAQFDECVLDKLGWVRPDLGDLSKVTKVKTDRPLPENPYHSRARPEPNPEVEGDLKPARHGSRLFFWTM | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
... |
Q54P46 | MESFTRAELVAQRDGVWAVCGEVFEAYEKCRMEKGSDPELCLRESTAVVGCSQKVMREIVKNCQKELNESVKCIEENNMRTIPCEEENKAFNECFDKLVAPKFL | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (... |
P51970 | MPGIVELPTLEELKVDEVKISSAVLKAAAHHYGAQCDKPNKEFMLCRWEEKDPRRCLEEGKLVNKCALDFFRQIKRHCAEPFTEYWTCIDYTGQQLFRHCRKQQAKFDECVLDKLGWVRPDLGELSKVTKVKTDRPLPENPYHSRPRPDPSPEIEGDLQPATHGSRFYFWTK | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis . Complex I functions in the transfer of electrons from NADH to the respiratory chain . The immediate electron acceptor for the enzyme is believed to be ubiquinone... |
Q9DCJ5 | MPGIVELPTLEELKVEEVKVSSAVLKAAAHHYGAQCDKTNKEFMLCRWEEKDPRRCLKEGKLVNGCALNFFRQIKSHCAEPFTEYWTCLDYSNMQLFRHCRQQQAKFDQCVLDKLGWVRPDLGQLSKVTKVKTDRPLPENPYHSRARPEPNPVIEGDLKPAKHGTRFFFWTV | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
... |
P21976 | MASRIPQFNQQVLYDTTPLPDSIPKVKELGASSAPLMSAAYFIGARCRDYNDDFMQCKNENPGKGEFECLKEGRRVTRCARSVIADINKSCLEEFRKHWTCLEDNNQQLWQCRPAEWKLNKCVFENLGLKKEIPDQPPNVTPVHLRKQMIYAHWPIPRSAEPFVPPTQTGDNNKAPAAASSSS | Cofactor: Binds 1 iron-sulfur cluster.
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for th... |
Q02373 | MPDSWDKDVYPEPPRRTPAPSPQTSLPNPITYLTKAFDLLVDRPVTLVREFIERQHAKNKYYYYHREFRRVPDITECQEKDVLCMFEAEMQWRRDYKVDQEIVNIIQERLKACQQREGESHRQNCAKELEQFTQVVKAYQDRYHDLGAHYSARKCLAKQKQRMLAERKAAKEAAAA | Function: Accessory subunit that is involved in the functional assembly of the mitochondrial respiratory chain complex I. Complex I has an NADH dehydrogenase activity with ubiquinone as an immediate electron acceptor and mediates the transfer of electrons from NADH to the respiratory chain.
Location Topology: Periphera... |
O96000 | MPDSWDKDVYPEPPRRTPVQPNPIVYMMKAFDLIVDRPVTLVREFIERQHAKNRYYYYHRQYRRVPDITECKEEDIMCMYEAEMQWKRDYKVDQEIINIMQDRLKACQQREGQNYQQNCIKEVEQFTQVAKAYQDRYQDLGAYSSARKCLAKQRQRMLQERKAAKEAAAATS | Function: Accessory subunit that is involved in the functional assembly of the mitochondrial respiratory chain complex I. Complex I has an NADH dehydrogenase activity with ubiquinone as an immediate electron acceptor and mediates the transfer of electrons from NADH to the respiratory chain.
PTM: The formation of intram... |
P80267 | GRKKGVQFDEGAPDDFDPNNPYKKDVAFL | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (... |
Q9NX14 | MAAGLFGLSARRLLAAAATRGLPAARVRWESSFSRTVVAPSAVAGKRPPEPTTPWQEDPEPEDENLYEKNPDSHGYDKDPVLDVWNMRLVFFFGVSIILVLGSTFVAYLPDYRMKEWSRREAERLVKYREANGLPIMESNCFDPSKIQLPEDE | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
... |
Q02376 | MAPSALLRPFWKLLAPARFPSVSSSRSKFYIQEPPHGSPNWLKVGLTLGTSVFLWIYLIKQHNEDVLEYKRRNGLE | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
... |
O43677 | MAPSALLRPLSRLLAPARLPSGPSVRSKFYVREPPNAKPDWLKVGFTLGTTVFLWIYLIKQHNEDILEYKRRNGLE | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
... |
Q9CQY9 | MAPSVVLRSFSRLLAPARLPSCSSTRSKFYVREPVNAKPNWLAVGLSVGASVFMWIYLIQTHNEDVLEYKRRNGLE | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
... |
P30826 | MFFFDFLFFFFVCFYMCFVCCVTICLPIELTIVSLLVRGNHFLRFYWCGLERCIACRLCDLICPSLALDVRVGWSFGGHRFADWFTLSYRRCIYCGFCMHVCPTDAITHSLFVMCFCCLAMYLLAPKFLLFGCCFMLFDFYLCFV | Cofactor: Binds 2 [4Fe-4S] clusters per subunit.
Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immed... |
Q9FNN5 | MAPVRGILGLQRAVSIWKESNRLTPALRSFSTQAASTSTTPQPPPPPPPPEKTHFGGLKDEDRIFTNLYGLHDPFLKGAMKRGDWHRTKDLVLKGTDWIVNEMKKSGLRGRGGAGFPSGLKWSFMPKVSDGRPSYLVVNADESEPGTCKDREIMRHDPHKLLEGCLIAGVGMRASAAYIYIRGEYVNERLNLEKARREAYAAGLLGKNACGSGYDFEVYIHFGAGAYICGEETALLESLEGKQGKPRLKPPFPANAGLYGCPTTVTNVETVAVSPTILRRGPEWFSSFGRKNNAGTKLFCISGHVNKPCTVEEEMSIPLK... | Cofactor: Binds 1 FMN.
Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for... |
Q92406 | MISRAAAPSSSIASLSSRSLRAQAPAARSFATVQDNAPPVKHYGGLKDQDRIFTNLYGHHGADLKSAMKYGDWHRTKDIVLKGHDWLISELKASGLRGRGGAGFPSGLKYSFMNFKDWDKDPRPRYLVVNADEGEPGTCKDREIMRKDPQKLIEGCLVVGRAMNANAAYMYIRGEFYQEATVLQRAINEAYEAGLIGKNACGTGYDFDVYIHRGMGAYVCGEETSLIESIEGKAGKPRLKPPFPAAVGLFGCPSTVTNVETVAVTPTIMRRGASWFSSFGRERNAGTKLFCISGHVNNPCTVEEEMSISLRDVIDRHCGG... | Cofactor: Binds 1 FMN.
Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for... |
Q54I90 | MMNLGNRVKSVIKLTSTTGLTGKDFQATKVATFSTAQVQQAQENVRSYGGLKDKDRIFTNLYGEHDVYLKGAIARGDWYKTKNIIDKGKDWILKEMMASGLRGRGGAGFPSGLKWSFMPKTTSKDRPQYLVINADEGEPGTCKDREIMRHDPHKLIEGCLLAGFAMRACAAYIYIRGEFHYEAKVLEQAIDEAYKAGLIGENACGTGYKFDVYVHRGAGAYICGEETALIESIEGKQGKPRLKPPFPAMAGLYGCPTTVTNVETVAVAPTILRRGGAWFASFGRPKNAGTKLFCISGHVNNPCTVEEEMSIPLRELIDKH... | Cofactor: Binds 1 FMN.
Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for... |
P49821 | MLATRRLLGWSLPARVSVRFSGDTTAPKKTSFGSLKDEDRIFTNLYGRHDWRLKGSLSRGDWYKTKEILLKGPDWILGEIKTSGLRGRGGAGFPTGLKWSFMNKPSDGRPKYLVVNADEGEPGTCKDREILRHDPHKLLEGCLVGGRAMGARAAYIYIRGEFYNEASNLQVAIREAYEAGLIGKNACGSGYDFDVFVVRGAGAYICGEETALIESIEGKQGKPRLKPPFPADVGVFGCPTTVANVETVAVSPTICRRGGTWFAGFGRERNSGTKLFNISGHVNHPCTVEEEMSVPLKELIEKHAGGVTGGWDNLLAVIPG... | Cofactor: Binds 1 FMN.
Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(ou... |
P24917 | MLSRTAAPTKASARTLSRAAAEQCRTFATVQDGSANPVRHYGGLKDQDRIFQNLYGRYPPDLKHAKKMGDWHKTKEILLKGHDWIIGEVKASGLRGRGGAGFPSGLKWSFMNFKDWDKDDKPRYLVVNADEGEPGTCKDREIMRKDPHKLVEGCLVAGRAMNATAAYIYIRGEFIQEAAILQNAINEAYADGLIGKNACGSGYDFDVYLHRGAGAYVCGEETSLIESLEGKPGKPRLKPPFPAAVGLFGCPSTVANVETVAVAPTICRRGGNWFAGFGRERNQGTKLFCISGHVNNPCTVEEEMSIPMRELIDKHCGGVR... | Cofactor: Binds 1 FMN.
Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for... |
O94500 | MLSRGHCCKLKHSFNGLRNVALKRLVGSKAGYRMFPNLIEKRIRRIDDALADGEYENLSEILKYDPLNIIELVQESELRGRGRYGFPTGEKMLSLYKATSSERGRKEKPVVIVNAAENDIGSFKDRLLLRHEPHKIIEGAIIAARAVEASACYLFIRKDYYEETVMMQKCIIQAYAKKLLGKNLLGTSIGLELLIHPGAGSYITGEESALIQSLQGEFPVPDIPINNTITSGLFGLPTLVLNVETVSNLPAIIKKGPKFFISMGRPNNRGTKLFSISGEVNEPNVIEACMSIPLKDLIENYAGGVRGGWNKLVGIFPGGP... | Cofactor: Binds 1 FMN.
Sequence Mass (Da): 50095
Sequence Length: 452
Subcellular Location: Mitochondrion
EC: 1.6.-.-
|
O22769 | MLARLAAKRLLEIRQVFRQPTSQVTRSLSTALNYHLDSPDNKPDLPWEFSEANQSKVKEILSYYPSNYKQSAVIPLLDLAQQQNGGWLPVSAMNAVAKVIEVAPIRVYEVATFYSMFNRAKVGKYHLLVCGTTPCMIRGSRDIESALLDHLGVKRGEVTKDGLFSVGEMECMGCCVNAPMITVADYSNGSEGYTYNYFEDVTPEKVVEIVEKLRKGEKPPHGTQNPKRIKCGPEGGNKTLLGEPKPPQFRDLDAC | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron... |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.