ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
| texts
stringlengths 108
11.1k
|
|---|---|---|
Q21059 | MVSYWPVLIVLCLLPICHAKSYFADFVNGKGPFKQADALKFMDKMTILNKLQADILGIPQPDEFSALDFEDKIESKPDEIPYLFEGDMVLTDEQMDLIIKNVRDQYWARKSSTNEFLYAIRGKRSMTSFLSERWSFPVPYYIDTSSGVNTNAVLAGVAKWEQETCARFTRLNSYSSSSRQNALRFISGNGCYSNIGKVSRFPQDVSIGWGCTSLGTVCHEIGHALGFYHEQARYDRDDYVSILTQNIQDMYLSQFTKQSASSMVDYGVGYDYGSVMHYDQAAFSSTGGNTIATRDPNFQATIGQRVAPSFADVKRINFAYCNSTCSNYLDCQNGGYINPNDCNNCKCPPGFGGQLCDVAGTNSNGCGAGDITATSSIQTISASGALTCNYVIKAPVGAKVYFQMTAATFSRYSPCTTNYLEINYGRDFSRVGARFCASYPTISLSETNTLVVIYKGVNGARFSLNYRYDPVTFSTSAPTTTSTTTTTAPITVPTVSPTTTTTRQTTTTARTSTTTTTTQAPPTTTTSTSQCASWSACSAQCGGCGTQSRRCGTYVETVYCNTNPCTGGYCCRPFFYVTSFGTGYCRRPGADTPAAPQRYVEQRKG | 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 | MALLKPFLSRTFSSFFATITGGRNLIDSIEELITTNYWLIFVMIIVCTCSAPSNGAFFLNDPYGYPFVSLQDDSIESVSATTITTTTIISTIITTTTATQRIFQEKAKTFGQSAEEIQKVKYYLEKIQKFEAKQHPEEIRQQHTTKNSEAIKDDLQIAVEVAKFEKRQKDSITLNPEENGQYYEGDIVLDAQQAHEIYESMIQHGRRTKRKFIRSELRRWDSHKPIIYSFDGSHTIREQRVIELALEHWHNITCLNFERRDDEIQENRIVFTDVDGCASNVGRHPLGEPQFVSLAPECIRLGVIAHEVAHALGFWHEQSRPDRDNYVTVRWENIDRDSKGQFLKELPTDVDNGDVPYDYGSIMHYRSKAFGRYEDLFTLNTNIMDYQKTIGQRDQLSFNDIRLMNVIYCSDSCAQKLPCQRGGYTDPRRCGRCRCPDGFTGKLCERIMPGFGADCGGRIELTSSWKRITSPNYPRDFKEGQECSWLLVAPPGQRVQLRFYGEFEMYCKVRHSLCMDYIEIRNSTDFANTGMRYCCYGTPKSSIMSATEDMLVLFRSFYRGGKGFQAQVRALPTTVFNIRTVRSMDEFNANLNKHAVADS | 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 | MHKIFIIFGLLSLCAAHSLRDLSNKDEEDPPSSAPGVRKRRMMSEEDQKTVDYYMDKLNKLADEKHPEEIERHKNPELVAWDRKRDSVLNPEEQGKFFQGDIVLYPEQAKALYEQALTEGKTRVKRKFIGSNLRRWDASRPIIYAFDGSHTQREQRIIELALEHWHNITCLNFQRNDQANSGNRIVFTDVDGCASNVGRHPLGEEQLVSLAPECIRLGVIAHEVAHALGFWHEQSRPDRDQYVTVRWENIDKDSKGQFLKEDPDDVDNAGVPYDYGSIMHYRSKAFSKFDDLYTISTYVTDYQKTIGQRDQLSFNDIRLMNKIYCSAVCPSKLPCQRGGYTDPRRCDRCRCPDGFTGQYCEQVMPGYGATCGGKISLTRSTTRISSPGYPREFKEGQECSWLLVAPPGHIVEFQFIGEFEMYCKIRHSLCMDYVEVRNSTDFANTGMRYCCYGTPPTRIRSATTDMVVLFRSFYRGGKGFEARARAVPEAGNWNSWSPWTACSATCGACGSRMRTRTCPPGNACSGEPVETQICNTQACTGMCAQKREEEGQCGGFLSLLRGVRCRQEKTVMAPCENACCPGFTLQRGRCVR | 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 | MKEIAHSQAYGNRVFSRDSAVDSKKDVSISAEQPKTISKLTPYLFEGDIFLSTKQAMNILDSLASKNKTNKKGQQRMAHDAPLYLFRGANEKGKRFAAEYDAKWFQFPIKYRFDESLDILHISQILKALEIWQSNTCIKFENDQEASGDYIEFFEGDGCYSMVGRFGGRQGISIGKGCERTGTIIHEVGHTLGLWHEQSRPDAEEYITVVKEYIIPSYISEFLTRSEHEITTFNVPYDLGSVMHYGSTAFSIDQRSKTLLTKDPFYQMTIGQRDSLSFYNIKLINEAYCKGDCKEKNECKNGGYLNPSNCQSCLCPSGFGGSKCEMHASSESNSKCGGTLKAIIDWQYIESPGYPDGYPTNVICNWLIETDKEERIEISFEDNFGIFCSSTCVDYIELKIGNDLANTGYRICCYDKPNDSLVSAKYQAVIIFRATTGEDTGFKLKFRKTMKPAQTTPSLPKTTTTAPHTTIVGNDIWSEWGEWSQCSRSCGACGIKSRLRICKTAQCSGKVQQFLTCNLQACPVDIRCTKVKFKNRLCADGNTCGKPGELLSSCSRPSCCPPFENVDGKCQTDQPLLIPLE | 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 | MRLCHSIILFNSLISISICSKADDPALLVASEFKEHFNVEEKQLETVEELLIKMKKLAHSRSFKGREFGHDAVEDSKKEVAISTQQGTINKKVSPFLFEGDIFLSRRQAVDILKALSKDKTKRLRRSFVSDKTATWKTMPIKYRFHESIDFYTISQIIAAIRFWEDSTCITFENVSDSPDGDYIEFFSGQGCYSMIGRNGGRQGISIGESCVKMGVIEHEIGHALGLWHEQSRPDALGYVTIERDFILPSYISDFLQRDDEIDTLGIPYDLGSVMHYGSTAFSVDQKSKTVVTRDSLYQQTIGQREKLSFYDVATINTAYCKDECKSEKTKCENGGYMRPSKCSECLCPDGLGGEKCEKNEDSKNAECGGIIKLTEEWKEIESPNYPDPGYEADQKCSWLLKAEKGKRVEIEFIEDFSFLCTSTCVDFVELKISDDLRNTGFRFCCYDKPEISFVSQTDTAIIIFRSQLSTDIGFKIQAKSTDAEPRTTIAPTIITTTLAPITVDAPNVWADWGEWSMCSRTCGGCGIRSRVRSCRSKKCEGRRQEFGTCNLKACPVDKHCAKLLSNNRLCNGKVCTKNDIAISSCDAPQCCPPFINVDGVCQSDQENQHDELWLSI | 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 | MKSQACLKVCLALIGLVSIVSTAYIANDVVSDYAEVKELLAAFYRKHAKKYGHDYDPAAIQAIAENMDKSVKNDKTEATVNRKLWNEVFENDIILTLPQAESLLSESNSPRSRRQAHPDPRNFWPNLTISYEFYGGEETWRQLIRSAIRHVEQNVCFKFKENGGDRDGLRYYRGNGCWSNVGRVGGRQLVSIGYGCDSLGIVSHETLHALGLWHEQSRDDRDNFISIVADKITRGTEGNFAKRTAANSDNLGQPYDLGSVMHYGAKSFAYDWSSDTIKTRDWRYQNTIGQRDGLSFKDAKMINTRYCSNVCQRSLPCLNEGYTDPNNCGRCRCPSGYGGTYCETVEYTSCGGSLTASSSYKKIESGIVQPDANCVWRIRNPGGNVEVMFDQVNFQCADPCQSYVEVKYLSQKTSTGARLCCSLPSVIRSEGDDVIIILRGTPNTAVGWRGFTLKYRAIGGTPITPATVRPTYATTTRPYWTRTASGWIHIKNPPLYKPDGQIYTSDEQSAETKYSSEELYDPSTFLSPSSSSASPALLLPSDASPQRPSAQEHDLSQLSQNALTRPTPTTTVAPDTASWSAWGEWSACSQPCGGCGTKTRVRACYGGNQVCPGSNLDRESCNAHACAKPKKGMICNGRLLLPCDLLAKLNFGSNNYLNPKLKQSGFARSSTLPLPRISQRKPVFVNELEVHPPTERFLSSSTRRVKRQTANRFCEKRFIYQCPTALLTIQMEYKPDTQGTNDAYFQQYPECCSGYTPRRGVCYKN | 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
Sequence Length: 765
Subcellular Location: Secreted
EC: 3.4.24.-
|
Q20942 | MPSPSYNRHIIIASCFCCLLIFSSAARVPKASKKHLARVKQLLNDEAERHNTLIQSDSVTVFDDIQRNPNTGVHHDELAVNNADEYFQGDVDLSEQQVKIIEDQFTQGKREKRKIGRNPLYKKWDTRGPISFDYAESIPFQTRQKIRSAMLLWQQHTCLRFEEGGPNVDRLEFFDGGGCSSFVGRVGGTQGISISTPGCDVVGIISHEIGHALGIFHEQARPDQERHIAINYNNIPLSRWNNFQAVGENHAETYNLPYDTGSVMHYGPYGFASDPYTPTIRTLERVQQSTIGQRAGPSFLDYQAINMAYGCTESCADLPCLRNGYTHPNNCSMCACPEGLSGRYCEQVYPSNAQCGGVIFATKEVKYITSPNYPDKFPIDTECNWIIAAPIEGRVFMEFEGDFDFLCEDTCDKAYVEVKYHSDKRLTGARYCCSLLPKNRFISFKNEMIIIMRGYRSSGAGFKAKFWSNLGEPEGVSTPLPPTTAPLPEISETTQKPEPTTVQSTTTYTTAIPRRTAKKQFFTRKPITIPLTPLTSSSTTTESTTVSSTTQSTTWLPTEPSFATGETEITTASPTITLFPSLSTILPPINSLAGVLPSTQAPDIINSVLECGCGAWSEWQGECSQQCGGCGHRLRKRECKKEACRKEEKRPCNFSACPDGTNFLINNAEFHILWRGCCVGLFRSGDQCSALETESNPFFKIINSLLNIQDAKNNDTLIAKRMMRGEH | 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 . Through regulating the expression of epidermal antimicrobial peptides such as nlp-29, modulates sleep duration and locomotion quiescence during the sleep-like state called lethargus which occurs during molting between larval and adult stages . This may occur through the sleep-active RIS neuron .
Sequence Mass (Da): 81023
Sequence Length: 727
Domain: The TSP type-1 domain may be involved in modulating sleep behaviors.
Subcellular Location: Secreted
EC: 3.4.24.-
|
Q20176 | MRFSANIAIIVNIIFLFIVVEFVLPTFIRSGDVRFRRYYRNNGRVSRAATAKKERIWPEGIIPFVIASNFSGEHQHLFLRAMRHWENFTCVSFVPRQPHHKHYITFTVDKCGCCSYVGRRGEGPQAISIGKNCDKFGIVVHELGHVVGFWHEHTRPDRDMYVDIFYKSIQTGQDYNFEKSKPEEVDSLGEPYDFSSIMHYARDTFSRGAFYDTILPKPNSGFRLEIGQRVQLSEGDIRQTKKLYKCAECGGTLMQESGNLAIQHAGVCTWHIISPQGHTIFLNITGSTLSPPSSLCGKEEDNVITVRDGVSISSPVLDRICGGDSLFRTIASSGNRMLIQVRSSTPAASLPFATYYAICGGPIYANEGVIHSPKYPESYPPNSDCQWTIHVDENSQVAIEFVYFHLEQHKECIYDRLILTEGISKNSKKDGKEMSETFCGLIEKKTIVSKTNQISLRFFSDNSVQKTGFELRFTKELNECATDKNICHHYCVNTVGGFKCACRVGYSLSSNGFSCDSTCGGYLKASNGSISSPNFPEMYPNSKTCIWEIEAPDGYHIFLNFTKFNVEGMKTECAYDYVKIGDSEKLCGEYHEALLFTTPRNRVRIEFSSDSSVERDGFFANFIADFDECQNDNAGCEHTCQNRLGSYVCTCNPGYILAEDKHNCKEGSCFFEVNAPAGDINSPNYPNDYPKGQNCSWHFVTTPGHRLMLTFSSFQVEEHAQCKYDAVSVYDGGDGSAQLAGVFCGLAPPPLLLSSSNELYLTFSSDASVSRRGFQAHYTSLCGGRLTAESTPGHIYSHATFSDSKYGKNQDCSWIVRAKSPGRGVRIQFSTFNIESEEGCQYDYIEIYDGPEATLERLVGRFCGDTSPEVITSTGPELLLIMHTDNAEEEKGFVAEYREAPRSSSTKRTFVSKTRHSPLEEPIHDRNE | 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: 320
EC: 2.5.1.43
|
Q502I6 | MLNVPSQAFPAAGSQQRVAPAGQSRNKVVLKPGHSLLDWIRLTKSGQDLTGLRGRLIEVTEDELKKHNTKKDCWTCIRGMVYNLSAYMDFHPGGEEELMRAAGIDSTDLFDEVHRWVNYESMLKECLVGRMAVKPSPALQAHTEKTESTHLNGLSAPPSLRPEPLSAPLPAKDHRPRYDWFQTDGTVNIVVYTKRKIPSAGCAVVDLQDDNLRVEMLLGRMSYLLYWRLSSRVQDHVDVQTAHSVGKVQLCLRKSVKEKWTQLGQSLEHHDTFIQCKDRGLFYRECVLLSKTDVTHNTQLLRLQLPRGSRMQVPVGRHVYLKTSVQGTDVVKPYTAVDQMLIPPSQSSAEVGSDIHLMIKVYPDGVLTPHIANLPIGASLSVGGPEGSFTLRVLRDVTHLYMLAAGTGFTPMARLIRLALQDFTVIRKMKLMFFNRQERDILWQSQLDELCTKEERFEVQHVLSEPADSWTGRRGRIDACMLQNFLERPENSKCLVCVCGPAGFTESAVQLVRQLDFSEEELHVFQA | 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 | MLNVPSQSFPAPRSQQRVASGGRSKVPLKQGRSLMDWIRLTKSGKDLTGLKGRLIEVTEEELKKHNKKDDCWICIRGFVYNVSPYMEYHPGGEDELMRAAGSDGTELFDQVHRWVNYESMLKECLVGRMAIKPAVLKDYREEEKKVLNGMLPKSQVTDTLAKEGPSYPSYDWFQTDSLVTIAIYTKQKDINLDSIIVDHQNDSFRAETIIKDCLYLIHIGLSHEVQEDFSVRVVESVGKIEIVLQKKENTSWDFLGHPLKNHNSLIPRKDTGLYYRKCQLISKEDVTHDTRLFCLMLPPSTHLQVPIGQHVYLKLPITGTEIVKPYTPVSGSLLSEFKEPVLPNNKYIYFLIKIYPTGLFTPELDRLQIGDFVSVSSPEGNFKISKFQELEDLFLLAAGTGFTPMVKILNYALTDIPSLRKVKLMFFNKTEDDIIWRSQLEKLAFKDKRLDVEFVLSAPISEWNGKQGHISPALLSEFLKRNLDKSKVLVCICGPVPFTEQGVRLLHDLNFSKNEIHSFTA | 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 cytochrome c, feericyanide and methemoglobin.
Catalytic Activity: 2 Fe(III)-[cytochrome b5] + NADH = 2 Fe(II)-[cytochrome b5] + H(+) + NAD(+)
Sequence Mass (Da): 59474
Sequence Length: 521
Subcellular Location: Endoplasmic reticulum
EC: 1.6.2.2
|
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 Length: 315
EC: 1.6.2.2
|
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 Length: 316
EC: 1.6.2.2
|
Q9DDD5 | PKNSEEQKITEMVYNIFRILLYHAIKYEWGGWRVWVDTLSIAHSKVTYEAHKEYLAKMYEEYQRQEEENIKKGKKGNVSTISGLSSQTTGAKGGMEIREIEDLSQSQSPESETDYPVSTDTRDLLMATKVSDDVLGSAERPGGGVHVEVHDLLVDIKAERVEATEVKLDDMDLSPETLVTGENGALVEVESLLDNVYSAAVEKLQNSVHGSVGIIKKNEEKDGGPLITLADEKDEPSTNSTSFLFDKIPSQEEKLLPDLSISHISIPNVQDTQMHLGVNDDLGLLAHMTGGVDITSTSSIIEDKEFKIHTNSVGMSSIFERELASLFKGLEYAEMTATTPETEFFCSKTVPNVDAGSIISVTERFVDGKEAGKEIRKIQTTTTTQAVQGRSVTQQDRDLRVDLGFRGMPMTEEQRRQFSPGPRTNMFRIPEFKWSPMHQRLLTDLLFALETDVHVWRSHSTKSVMDFVNSNENIIFVHNTIHLISQMVDNIIIACGGILPLLSAATSPTGSKTELENIEVTQGMSAETAVTFLSRLMAMVDVLVFASSLNFSEIEAEKNMSSGGLMRQCLRLVCCVAVRNCLECRQRQRERVNKTSLISSKAQDALQGVTASAATKTPLENVPGNLSPIKDPDRLLQDVDINRLRAVVFRDVDDSKQAQFLALAVVYFISVLMVSKYRDILEPQRETARSGSQAGRNIRQEINSPTSTETPAVFPENIKDKETPTPVEDIQLESSIPHTDSGIGEEQMPNILNGTDLETSTGPDAMSELLSTLSSEVKKSQESLTESPSEILK | 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: Cytoplasm
|
A4UHQ3 | MDADRIVFKVHNQLVSVKPEVIVDQYEYKYPAIKDRKKPSITLGKAPDLNRAYKSILSGINAARLDPDDVCSYLAAAMALFEGICPDDWESYGILIARKGDKITPANLVNIQRTDVEGNWALAGGLDVIKDPTTAEHASLVGLLLCLYRLSKVSGQNTGNYKTNVADRMEQIFETAPFVKIVEHHTLMTTHKMCANWSTIPNFRFLAGTYDMFFSRIEHLYSAIRVGTVVTAYEDCSGLVSFTGFIRQINLTAKEAILYFFHKNFEEEIKRMFEPGQETAVPHSYFIHFRSLGLSGKSPYSSNAVGHVFNLIHFVGSYMGQVRSLNATVIATCAPHEMSVLGGYLGEEFFGKGTFERRFFRDERELAEHEAIESTKTDVALADDGTVNSDDEELYSGGTRTPEAVYTRIMVNGGKLKKSHIKRYVSVSSNHQARPNSFAEFLNKTYSSDPR | 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 genomic RNA, with protein N protecting the genome like a pearl necklace. The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for viral transcription and replication. Protein N binds protein P in the NC through a different interaction, and can be phosphorylated. Subsequent viral replication is dependent on intracellular concentration of newly synthesized protein N. During replication, encapsidation by protein N is coupled to RNA synthesis and all replicative products are resistant to nucleases (By similarity).
PTM: Phosphorylated by host.
Sequence Mass (Da): 50531
Sequence Length: 451
Subcellular Location: Virion
|
P18272 | MDSRPQKIWMAPSLTESDMDYHKILTAGLSVQQGIVRQRVIPVYQVNNLEEICQLIIQAFEAGVDFQESADSFLLMLCLHHAYQGDYKLFLESGAVKYLEGHGFRFEVKKRDGVKRLEELLPAVSSGKNIKRTLAAMPEEETTEANAGQFLSFASLFLPKLVVGEKACLEKVQRQIQVHAEQGLIQYPTAWQSVGHMMVIFRLMRTNFLIKFLLIHQGMHMVAGHDANDAVISNSVAQARFSGLLIVKTVLDHILQKTERGVRLHPLARTAKVKNEVNSFKAALSSLAKHGEYAPFARLLNLSGVNNLEHGLFPQLSAIALGVATAHGSTLAGVNVGEQYQQLREAATEAEKQLQQYAESRELDHLGLDDQEKKILMNFHQKKNEISFQQTNAMVTLRKERLAKLTEAITAASLPKTSGHYDDDDDIPFPGPINDDDNPGHQDDDPTDSQDTTIPDVVVDPDDGSYGEYQSYSENGMNAPDDLVLFDLDEDDEDTKPVPNRSTKGGQQKNSQKGQHIEGRQTQSRPIQNVPGPHRTIHHASAPLTDNDRRNEPSGSTSPRMLTPINEEADPLDDADDETSSLPPLESDDEEQDRDGTSNRTPTVAPPAPVYRDHSEKKELPQDEQQDQDHTQEARNQDSDNTQSEHSFEEMYRHILRSQGPFDAVLYYHMMKDEPVVFSTSDGKEYTYPDSLEEEYPPWLTEKEAMNEENRFVTLDGQQFYWPVMNHKNKFMAILQHHQ | 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 encapsidated genomic RNA is termed the nucleocapsid and serves as template for transcription and replication. The nucleocapsid is helical with a pitch of 10.81 NP per turn and a diameter of about 22nm . Each NP binds to six nucleotides of viral genomic RNA, three being exposed to the solvant and three hidden into the nucleocapsid . Recruits also host PPP2R5C phosphatase to dephosphorylate VP30 and thereby promote viral transcription . Upon virion assembly and budding, NP binds to VP24 and possibly host STAU1 .
PTM: Phosphorylated by host.
Sequence Mass (Da): 83287
Sequence Length: 739
Domain: Comprizes a N-terminal arm involved in oligomerization, a NP core region involved in RNA binding, a disordered region follwoed by a C-terminal tail involved in protein-protein interactions . During oligomerization, NP N-terminal arm binds to a neighbor NP thereby displacing VP35 bound to monomeric NP .
Subcellular Location: Virion
|
P69596 | MASGKAAGKTDAPAPVIKLGGPKPPKVGSSGNASWFQAIKAKKLNTPPPKFEGSGVPDNENIKPSQQHGYWRRQARFKPGKGGRKPVPDAWYFYYTGTGPAADLNWGDTQDGIVWVAAKGADTKSRSNQGTRDPDKFDQYPLRFSDGGPDGNFRWDFIPLNRGRSGRSTAASSAAASRAPSREGSRGRRSDSGDDLIARAAKIIQDQQKKGSRITKAKADEMAHRRYCKRTIPPNYRVDQVFGPRTKGKEGNFGDDKMNEEGIKDGRVTAMLNLVPSSHACLFGSRVTPKLQLDGLHLRFEFTTVVPCDDPQFDNYVKICDQCVDGVGTRPKDDEPKPKSRSSSRPATRGNSPAPRQQRPKKEKKLKKQDDEADKALTSDEERNNAQLEFYDEPKVINWGDAALGENEL | 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 viral replication.
PTM: ADP-ribosylated. The ADP-ribosylation is retained in the virion during infection.
Sequence Mass (Da): 45032
Sequence Length: 409
Subcellular Location: Virion
|
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 residue, the reaction is assisted by a reduction system comprising dph3 and a NADH-dependent reductase, predominantly cbr1. By reducing dph3, also involved in the formation of the tRNA wobble base modification mcm5s 2U (5-methoxycarbonylmethyl-2-thiouridine), mediated by the elongator complex. The cytochrome b5/NADH cytochrome b5 reductase electron transfer system supports the catalytic activity of several sterol biosynthetic enzymes.
Catalytic Activity: 2 Fe(III)-[cytochrome b5] + NADH = 2 Fe(II)-[cytochrome b5] + H(+) + NAD(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 31925
Sequence Length: 292
Pathway: Protein modification; peptidyl-diphthamide biosynthesis.
Subcellular Location: Mitochondrion outer membrane
EC: 1.6.2.2
|
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 residue, the reaction is assisted by a reduction system comprising dph3 and a NADH-dependent reductase, predominantly cbr1. By reducing dph3, also involved in the formation of the tRNA wobble base modification mcm5s 2U (5-methoxycarbonylmethyl-2-thiouridine), mediated by the elongator complex. The cytochrome b5/NADH cytochrome b5 reductase electron transfer system supports the catalytic activity of several sterol biosynthetic enzymes.
Catalytic Activity: 2 Fe(III)-[cytochrome b5] + NADH = 2 Fe(II)-[cytochrome b5] + H(+) + NAD(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 32523
Sequence Length: 296
Pathway: Protein modification; peptidyl-diphthamide biosynthesis.
Subcellular Location: Mitochondrion outer membrane
EC: 1.6.2.2
|
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 residue, the reaction is assisted by a reduction system comprising DPH3 and a NADH-dependent reductase, predominantly CBR1. By reducing DPH3, also involved in the formation of the tRNA wobble base modification mcm5s 2U (5-methoxycarbonylmethyl-2-thiouridine), mediated by the elongator complex. The cytochrome b5/NADH cytochrome b5 reductase electron transfer system supports the catalytic activity of several sterol biosynthetic enzymes.
Catalytic Activity: 2 Fe(III)-[cytochrome b5] + NADH = 2 Fe(II)-[cytochrome b5] + H(+) + NAD(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 32472
Sequence Length: 294
Pathway: Protein modification; peptidyl-diphthamide biosynthesis.
Subcellular Location: Mitochondrion outer membrane
EC: 1.6.2.2
|
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 residue, the reaction is assisted by a reduction system comprising DPH3 and a NADH-dependent reductase, predominantly CBR1. By reducing DPH3, also involved in the formation of the tRNA wobble base modification mcm5s 2U (5-methoxycarbonylmethyl-2-thiouridine), mediated by the elongator complex. The cytochrome b5/NADH cytochrome b5 reductase electron transfer system supports the catalytic activity of several sterol biosynthetic enzymes.
Catalytic Activity: 2 Fe(III)-[cytochrome b5] + NADH = 2 Fe(II)-[cytochrome b5] + H(+) + NAD(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 31937
Sequence Length: 285
Pathway: Protein modification; peptidyl-diphthamide biosynthesis.
Subcellular Location: Mitochondrion outer membrane
EC: 1.6.2.2
|
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 Topology: Single-pass membrane protein
Sequence Mass (Da): 31879
Sequence Length: 286
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.6.2.2
|
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 residue, the reaction is assisted by a reduction system comprising dph3 and a NADH-dependent reductase, predominantly cbr1. By reducing dph3, also involved in the formation of the tRNA wobble base modification mcm5s 2U (5-methoxycarbonylmethyl-2-thiouridine), mediated by the elongator complex. The cytochrome b5/NADH cytochrome b5 reductase electron transfer system supports the catalytic activity of several sterol biosynthetic enzymes.
Catalytic Activity: 2 Fe(III)-[cytochrome b5] + NADH = 2 Fe(II)-[cytochrome b5] + H(+) + NAD(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 33823
Sequence Length: 310
Pathway: Protein modification; peptidyl-diphthamide biosynthesis.
Subcellular Location: Mitochondrion outer membrane
EC: 1.6.2.2
|
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 residue, the reaction is assisted by a reduction system comprising DPH3 and a NADH-dependent reductase, predominantly MCR1.1. By reducing DPH3, also involved in the formation of the tRNA wobble base modification mcm5s 2U (5-methoxycarbonylmethyl-2-thiouridine), mediated by the elongator complex. The cytochrome b5/NADH cytochrome b5 reductase electron transfer system supports the catalytic activity of several sterol biosynthetic enzymes.
Catalytic Activity: 2 Fe(III)-[cytochrome b5] + NADH = 2 Fe(II)-[cytochrome b5] + H(+) + NAD(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 33656
Sequence Length: 308
Pathway: Protein modification; peptidyl-diphthamide biosynthesis.
Subcellular Location: Mitochondrion outer membrane
EC: 1.6.2.2
|
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 residue, the reaction is assisted by a reduction system comprising DPH3 and a NADH-dependent reductase, predominantly CBR1. By reducing DPH3, also involved in the formation of the tRNA wobble base modification mcm5s 2U (5-methoxycarbonylmethyl-2-thiouridine), mediated by the elongator complex. The cytochrome b5/NADH cytochrome b5 reductase electron transfer system supports the catalytic activity of several sterol biosynthetic enzymes.
Catalytic Activity: 2 Fe(III)-[cytochrome b5] + NADH = 2 Fe(II)-[cytochrome b5] + H(+) + NAD(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 33630
Sequence Length: 309
Pathway: Protein modification; peptidyl-diphthamide biosynthesis.
Subcellular Location: Mitochondrion outer membrane
EC: 1.6.2.2
|
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 residue, the reaction is assisted by a reduction system comprising DPH3 and a NADH-dependent reductase, predominantly CBR1. By reducing DPH3, also involved in the formation of the tRNA wobble base modification mcm5s 2U (5-methoxycarbonylmethyl-2-thiouridine), mediated by the elongator complex. The cytochrome b5/NADH cytochrome b5 reductase electron transfer system supports the catalytic activity of several sterol biosynthetic enzymes.
Catalytic Activity: 2 Fe(III)-[cytochrome b5] + NADH = 2 Fe(II)-[cytochrome b5] + H(+) + NAD(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 32331
Sequence Length: 298
Pathway: Protein modification; peptidyl-diphthamide biosynthesis.
Subcellular Location: Mitochondrion outer membrane
EC: 1.6.2.2
|
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 residue, the reaction is assisted by a reduction system comprising dph3 and a NADH-dependent reductase, predominantly cbr1. By reducing dph3, also involved in the formation of the tRNA wobble base modification mcm5s 2U (5-methoxycarbonylmethyl-2-thiouridine), mediated by the elongator complex. The cytochrome b5/NADH cytochrome b5 reductase electron transfer system supports the catalytic activity of several sterol biosynthetic enzymes.
Catalytic Activity: 2 Fe(III)-[cytochrome b5] + NADH = 2 Fe(II)-[cytochrome b5] + H(+) + NAD(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 33756
Sequence Length: 309
Pathway: Protein modification; peptidyl-diphthamide biosynthesis.
Subcellular Location: Mitochondrion outer membrane
EC: 1.6.2.2
|
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 residue, the reaction is assisted by a reduction system comprising DPH3 and a NADH-dependent reductase, predominantly CBR1. By reducing DPH3, also involved in the formation of the tRNA wobble base modification mcm5s 2U (5-methoxycarbonylmethyl-2-thiouridine), mediated by the elongator complex. The cytochrome b5/NADH cytochrome b5 reductase electron transfer system supports the catalytic activity of several sterol biosynthetic enzymes.
Catalytic Activity: 2 Fe(III)-[cytochrome b5] + NADH = 2 Fe(II)-[cytochrome b5] + H(+) + NAD(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 31520
Sequence Length: 284
Pathway: Protein modification; peptidyl-diphthamide biosynthesis.
Subcellular Location: Mitochondrion outer membrane
EC: 1.6.2.2
|
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 segment of both retinal rod and cone photoreceptors and the light-induced lowering of calcium is caused by extrusion via this protein which plays a key role in the process of light adaptation.
PTM: The uncleaved signal sequence is required for efficient membrane targeting and proper membrane integration and topology.
Location Topology: Multi-pass membrane protein
Catalytic Activity: Ca(2+)(out) + K(+)(out) + 4 Na(+)(in) = Ca(2+)(in) + K(+)(in) + 4 Na(+)(out)
Sequence Mass (Da): 31671
Sequence Length: 300
Subcellular Location: Cell membrane
|
Q9IAL8 | MHLPRRRRLQRNRIFFFLAVVSLLSVYQLQFSPSAIPALLTAHQHEDPVKVTSREPFRNKTSKTGNVTAAPKIRHCVYIDPEPTVPITASEDTTQRENVNESYPDEKPVYESKGEYPQDLFSVEERRQGWVVLHIFGMMYVFVALAIVCDEYFVPALGVITEKLQISEDVAGATFMAAGGSAPELFTSLIGVFISHSNVGIGTIVGSAVFNILFVIGTCALFSREILHLTWWPLFRDISFYIVDLLMLILFFLDSVIDWWESLLLLTAYATYVFTMKHNVSLEQWVKEELSKKLNAVQAASAEHMRKKSSVAVAEDGTKPADGKKLQPTTALQRGTSSASLHNSQMRSTIFQLMIHTLDPLAGAKFKDRVDILSNIAKVKADSLTGQGTKPEAEEEKQASQNTVQVTPASDSEPSKDKQKEDTPQDGQPPSDSDNSEDSSSDSEDDSDDDSTDDEENDEPLSLEWPETRKKQAIYLFLFPIVFPLWSTIPDVRNPDSKKFFVITFFGSIIWIAAFSYLMVWWAHQVGETIGISEEIMGLTILAAGTSIPDLITSVIVARKGLGDMAVSSSVGSNIFDITVGLPVPWFLYSVFNGFSPVAVSSNGLFCAIVLLFLMLLFVIISIALCKWKMNKILGVTMFALYFVFLIISVMLEDRIISCPVSV | 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 segment of both retinal rod and cone photoreceptors and the light-induced lowering of calcium is caused by extrusion via this protein which plays a key role in the process of light adaptation (By similarity).
PTM: The uncleaved signal sequence is required for efficient membrane targeting and proper membrane integration and topology.
Location Topology: Multi-pass membrane protein
Catalytic Activity: Ca(2+)(out) + K(+)(out) + 4 Na(+)(in) = Ca(2+)(in) + K(+)(in) + 4 Na(+)(out)
Sequence Mass (Da): 73772
Sequence Length: 663
Subcellular Location: Cell membrane
|
Q9IAL7 | MALCKKTVGSVLEEWCLNEPLFGCKRHQNVRKKLRLIRIIGLLVSVVAISTFSLSISAFFKMETHSTVLASSLESQKLVHGHQRTLLDFMEQNEGSTPDSPTSMKHEAEHDNATEEHSKGEYPEDLFSLEERRKGAVILHVIGMIYMFIALAIVCDEFFVPSLTVITEKLSISDDVAGATFMAAGGSAPELFTSLIGVFISHSNVGIGTIVGSAVFNILFVIGMCALFSREILNLTWWPLFRDVSFYIVDLILLIIFFLDNLIMWWESLTLLTAYFCYVTFMKFNVQVEEWVKKVLNRNKVEKATTGDAEGKSPTAGDKDDQTLTTKPRLQRGGSSASLHNSLMRNSIFQLMIHTLDPLAEELGSYGNLKYYDTMTEEGKFKERASILHKIAKKKCQVEDSERQNGAANHEKGAKVEVAVTPPSDSGPVQNGIAHNVDEENEEDEDQPLSLAWPDTPRKQLTYLLVLPIVFPLWVSLPDVRNPRSRKFFPITFFGSISWIAFFSYLMVWWAHQVGETIGISEEIMGLTILAAGTSIPDLITSVIVARKGLGDMAVSSSVGSNIFDITVGLPLPWLLYAVINNFSPVTVSSNGLFCAIVLLFIMLLFVILSIAFCKWRMNKFLGFLMFGLYFVFLIVSVLLEDKVIQCPVSI | 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+)(in) + K(+)(in) + 4 Na(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 72696
Sequence Length: 651
Subcellular Location: Cell membrane
|
Q9UI40 | MDLQQSTTITSLEKWCLDESLSGCRRHYSVKKKLKLIRVLGLFMGLVAISTVSFSISAFSETDTQSTGEASVVSGPRVAQGYHQRTLLDLNDKILDYTPQPPLSKEGESENSTDHAQGDYPKDIFSLEERRKGAIILHVIGMIYMFIALAIVCDEFFVPSLTVITEKLGISDDVAGATFMAAGGSAPELFTSLIGVFIAHSNVGIGTIVGSAVFNILFVIGMCALFSREILNLTWWPLFRDVSFYIVDLIMLIIFFLDNVIMWWESLLLLTAYFCYVVFMKFNVQVEKWVKQMINRNKVVKVTAPEAQAKPSAARDKDEPTLPAKPRLQRGGSSASLHNSLMRNSIFQLMIHTLDPLAEELGSYGKLKYYDTMTEEGRFREKASILHKIAKKKCHVDENERQNGAANHVEKIELPNSTSTDVEMTPSSDASEPVQNGNLSHNIEGAEAQTADEEEDQPLSLAWPSETRKQVTFLIVFPIVFPLWITLPDVRKPSSRKFFPITFFGSITWIAVFSYLMVWWAHQVGETIGISEEIMGLTILAAGTSIPDLITSVIVARKGLGDMAVSSSVGSNIFDITVGLPLPWLLYTVIHRFQPVAVSSNGLFCAIVLLFIMLLFVILSIALCKWRMNKILGFIMFGLYFVFLVVSVLLEDRILTCPVSI | 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+)(in) + K(+)(in) + 4 Na(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 73664
Sequence Length: 661
Subcellular Location: Cell membrane
|
O54701 | MDLHQSATVRLLQEWCSHESPSGCRRHYNTRKKLKLIRVIGLVMGLVAVSTVPFSISAFTETYSQNNRGEASDVTGPRAAPGHRQRTLLDLNDKIRDYTPQPPASQEDRSENGTDHAQGDYPKDVFSLEERRKGAIILHVIGMIYMFIALAIVCDEFFVPSLTVITEKLGISDDVAGATFMAAGGSAPELFTSLIGVFIAHSNVGIGTIVGSAVFNILFVIGMCALFSREILNLTWWPLFRDVSFYIVDLIMLIIFFLDNVIMWWESLLLLTAYFAYVVFMKFNVQVERWVKQMINRNKVVKVTVSEAQAKASTAGDKEEPTLPNKPRLQRGGSSASLHNSLMRNSIFQLMIHTLDPLAEELGSYGKLKYYDTMTEEGRFREKASILHKIAKKKCQVDENERQNGAANHVDYAAEKIELPNSTSTEVEMTPSSEASEPVQNGNLSHSIEAADAPQATETAEEDDDQPLSLSWPSNTRKQITFLIVLPIVFPLWITLPDVRKPASKKFFPITFFGSITWIAVFSYLMVWWAHQVGETIGISEEIMGLTILAAGTSIPDLITSVIVARKGLGDMAVSSSVGSNIFDITVGLPLPWLLYTIIHRFKPVTVSSNGLFCAIVLLFIMLIFVILSIALCKWRMNKILGFIMFGLYFAFLVVSVLLEDKVLECPVSI | 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+)(in) + K(+)(in) + 4 Na(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 74657
Sequence Length: 670
Subcellular Location: Cell membrane
|
Q9HC58 | MRPSGDEDRARRRRRRRRRRDLLLSQLCFLASVALLLWSLSSLREQKELDLMDLVGEDRKWMMARKLMQVNDTLTSEDAGLRNSKNCTEPALHEFPNDIFTNEDRRQGAVVLHVLCAIYMFYALAIVCDDFFVPSLEKICERLHLSEDVAGATFMAAGSSAPELFTSVIGVFITKGDVGVGTIVGSAVFNILCIIGVCGLFAGQVVALSSWCLLRDSIYYTLSVIALIVFIYDEKVSWWESLVLVLMYLIYIVIMKYNACIHQCFERRTKGAGNMVNGLANNAEIDDSSNCDATVVLLKKANFHRKASVIMVDELLSAYPHQLSFSEAGLRIMITSHFPPKTRLSMASRMLINERQRLINSRAYTNGESEVAIKIPIKHTVENGTGPSSAPDRGVNGTRRDDVVAEAGNETENENEDNENDEEEEEDEDDDEGPYTPFDTPSGKLETVKWAFTWPLSFVLYFTVPNCNKPRWEKWFMVTFASSTLWIAAFSYMMVWMVTIIGYTLGIPDVIMGITFLAAGTSVPDCMASLIVARQGMGDMAVSNSIGSNVFDILIGLGLPWALQTLAVDYGSYIRLNSRGLIYSVGLLLASVFVTVFGVHLNKWQLDKKLGCGCLLLYGVFLCFSIMTEFNVFTFVNLPMCGDH | 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: Cell membrane
|
Q8C567 | MLPTLTALLCLGLCLSQRINTEKETLPKPIIWAKPSIMVTNGNSVNIWCQGAQSASEYQLYFEGSFFALERPKPSRSMNKVRFFISQMTSHTAGIYTCFYQSGELWSKSSNPLKLVVTGLYDTPNLWVYPRPEVTLGENVTFFCQLKTATSKFFLLKERGSNHIQNKYGNIQAEFPMGPVTRAHRGTYRCFGSYNDYAWSFPSEPVTLLITGGVENSSLAPTDPTSSLDYWEFDLSTNESGLQKDSAFWDHTTQNLIRIGLACIILITLVWLLTEDWLSKRKDHEEANRLTNWECRRRWRMQHYFEEEQRNAISMMELKATPGAL | 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 | MLPTLTALLCLGLCLSQRINTEKQTLPKPIIWAKPSIMVTKGNSVNIWCQGAQSASEYQLYFEGSFFALERPKSSRSMNKVKFFISQMTSHTAGIYTCFYQSGELWSESSNPLKLVVTGLYDTPTLWVHPGPEVTLGENVTFSCHLKTATSKFFLLKERESNHIQHKYGNIQAEFPMGPVTRAHRGTYRCFGSYNDYAWSFPSEPVTLLITGEVENTSLAPTDPVSSLDYWEFDLSTKESGLQKDSAFWDHTAQNLIRIGLACIIVMALVWLLAEDWLSRRKDHEKLNRLTSWECRGRRRMHRYHEEEQRDAISMRELKATPGDM | 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 BAG6 also promotes myeloid dendritic cells (DC) maturation, both through killing DCs that did not acquire a mature phenotype, and inducing the release by NK cells of TNFA and IFNG which promote DC maturation.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 21593
Sequence Length: 201
Subcellular Location: Cell membrane
|
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 Location: Cell membrane
|
O16242 | MCSSEECLIDKSWTSEEKCEYIKCNQDSCEGGGYLTWSHYVKCQYNIGVRVILIILGILYLIILFVIMSSIADDFFCPAISGIVSHLRMSESIAGVTFLAFGNGAPDVFSSISSVLTTPKPKADLALGDLFGTSIFVTTVVLAIIIFTKSFKVAIIPTLRDLIFYMTTLAFIVFCFLKFDKIEVWMPATFLGIYGVYVVTVIILGIYRTHRKKRNLKKKNKELEDFLSRPSSAASTTPIFGAMKLKEETISVSALFHFMIGYSQFIKNLTRANLKRTTNNNNNDNKNEKRGIVNLGFSEPYSIPSERKISTIFKQNTFETDLESLESLADLDGSDDEGREEKFGYAHHTVFTSHDQISLVASEIEEIEITTWRSWDWVWDLFNHLKSWPSRDEFSEMNIFIKIVTVIKVVPVFFFKLTVPSNEMSWCKPLFILHCFASIQFALFSIQIITLKPFDGSPGLWLYGLGFSAILAMVAMYFLPLSKEQKYYKEIYSYLGFLMSIAWIYATSNEIVSVVTMIGVVTGLSMELLGLTIMAWSNCIGDIVADIAVVKQGYPKMAMAAAIGGPLFNLLIGFGLPFTIAAAQGKEMELLINPVYRLLMLFLGISLVTTFVALFIQRFTVRRPHAVLLIFIFVVFLIFICLAEFHVLEWN | 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 signaling pathway to set left/ right patterning of the VD/DD GABAergic circuit .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 73508
Sequence Length: 651
Subcellular Location: Mitochondrion inner membrane
|
Q8GWA1 | MLWIKNLARISQTTSSSVGNVFRNPESYTLSSRFCTALQKQQVTDTVQAKEDVVNALEPQRYDGLAPTKEGEKPRVLVLGSGWAGCRVLKGIDTSIYDVVCVSPRNHMVFTPLLASTCVGTLEFRSVAEPISRIQPAISREPGSYYFLANCSKLDADNHEVHCETVTEGSSTLKPWKFKIAYDKLVLACGAEASTFGINGVLENAIFLREVHHAQEIRRKLLLNLMLSEVPGIGEDEKKRLLHCVVVGGGPTGVEFSGELSDFIMKDVRQRYSHVKDDIRVTLIEARDILSSFDDRLRHYAIKQLNKSGVKLVRGIVKEVKPQKLILDDGTEVPYGPLVWSTGVGPSSFVRSLDFPKDPGGRIGIDEWMRVPSVQDVFAIGDCSGYLESTGKSTLPALAQVAEREGKYLANLFNVMGKAGGGRANSAKEMELGEPFVYKHLGSMATIGRYKALVDLRESKEGKGISMAGFLSWFIWRSAYLTRVVSWRNRFYVAINWLTTFVFGRDISRI | 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
Sequence Mass (Da): 56628
Sequence Length: 510
Subcellular Location: Mitochondrion inner membrane
EC: 1.6.5.9
|
Q9ST63 | MPWFKNLIKISKTITNQSSSYKSITPLASPLLTQFLQFTKQYSTNDHVVGLEATKSDQKPRIVVLGSGWAGCRLMKDIDTNIYDVVCVSPRNHMVFTPLLASTCVGTLEFRSVAEPIGRIQPAVSTQPASYFFLANCNAIDFDNHMIECETVTEGVETLEAWKFNVSYDKLVIASGAHALTFGIKGVNEHATFLREVHHAQEIRRKLLLNLMLSDVPGVSEEEKRRLLHCVVVGGGPTGVEFSGELSDFILKDVHQRYAHVKDYIHVTLIEANEILSSFDDRLRVYATNQLTKSGVRLVRGLVQHVQPDNIILSDGTNVPYGLLVWSTGVGPSPFVNSLDIPKAKGRIGIDEWLRVPSVQDVYSIGDCSGFLESTGRQVLPALAQVAERQGKYLASLLNKVGKQGGGHANCAQNINLGDPFVYKHLGSMATIGRYKALVDLRESKEAKGVSLAGFTSFFVWRSAYLTRVVSWRNKIYVLINWLTTLVFGRDISRI | 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
Sequence Mass (Da): 54902
Sequence Length: 495
Subcellular Location: Mitochondrion inner membrane
EC: 1.6.5.9
|
O80874 | MFMIKNLTRISPNTSSIITRFRNSGSSSLSYTLASRFCTAQETQIQSPAKIPNDVDRSQYSGLPPTREGEKPRVVVLGSGWAGCRLMKGIDTNLYDVVCVSPRNHMVFTPLLASTCVGTLEFRSVAEPISRIQPAISREPGSFFFLANCSRLDADAHEVHCETLTDGLNTLKPWKFKIAYDKLVIASGAEASTFGIHGVMENAIFLREVHHAQEIRRKLLLNLMLSDTPGISKEEKRRLLHCVVVGGGPTGVEFSGELSDFIMKDVRQRYAHVKDDIHVTLIEARDILSSFDDRLRRYAIKQLNKSGVRFVRGIVKDVQSQKLILDDGTEVPYGLLVWSTGVGPSPFVRSLGLPKDPTGRIGIDEWMRVPSVQDVFAIGDCSGYLETTGKPTLPALAQVAEREGKYLANLLNAIGKGNGGRANSAKEIELGVPFVYKHLGSMATIGRYKALVDLRESKDAKGISMTGFVSWFIWRSAYLTRVISWRNRFYVAINWFTTFVFGRDISRI | 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
Sequence Mass (Da): 56503
Sequence Length: 508
Subcellular Location: Mitochondrion inner membrane
EC: 1.6.5.9
|
Q8GXR9 | MAVLSSVSSLIPFSYGATRLTSKASLASRTSGFNLSSRWNSTRNSPMLYLSRAVTNNSGTTEISDNETAPRTYSWPDNKRPRVCILGGGFGGLYTALRLESLVWPEDKKPQVVLVDQSERFVFKPMLYELLSGEVDVWEIAPRFSDLLTNTGIQFLRDRVKTLLPCDHLGVNGSEISVTGGTVLLESGFKIEYDWLVLALGAESKLDVVPGAMELAFPFYTLEDAIRVNEKLSKLERKNFKDGSAIKVAVVGCGYAGVELAATISERLQDRGIVQSINVSKNILTSAPDGNREAAMKVLTSRKVQLLLGYLVQSIKRASNLEEDEGYFLELQPAERGLESQIIEADIVLWTVGAKPLLTKLEPSGPNVLPLNARGQAETDETLRVKGHPRIFALGDSSSLRDSNGKILPTTAQVAFQEADFTGWNIWAAINNRPLLPFRFQNLGEMMTLGRYDAAISPSFIEGLTLEGPIGHAARKLAYLIRLPTDEHRFKVGISWFAKSAVDSIALLQSNLTKVLSGS | 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 phylloquinone (vitamin K1) production . Probably not directly involved in cyclic or chlororespiratory electron flows under standard growth conditions, but participates in the redox metabolism of plastoquinone-9 and the tocophrol recycling-intermediate alpha-tocopherol quinone . Catalyzes the penultimate step in the biosynthesis of vitamin K1 .
Catalytic Activity: a quinone + H(+) + NADH = a quinol + NAD(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 56916
Sequence Length: 519
Subcellular Location: Mitochondrion
EC: 1.6.5.9
|
Q8I4N3 | MMGDSHSSFTTTTDEHLYNQFSPGRRKNDFPAASSSSSSPNLRRSPNRTVSSPRVQQKPITIFDQIVDWFQAEISVRKRLAGAACGYLSTIFFIVTVSILKLTIWAPFSSVQDSLAWWIYPNAWASIIFVGIASVAMSLFSIIKFCKVDQLPRLAATDTFALAGVALEFVTRLTFVYTAFCVADFSFSREFAFVAISLAIAISSALVVFRSDYQLNFSHIQVNSVKTLIDFGTSLPYANISEICGIDAAISYTAAVALILVVGPMVSGFSAWWLLLNIPFHVVLFGLCFTQQFYSKISMKIVNQIVMKPISFPFPPPYTVHSPTPEQTRTLPNVIETDDSLLKFFALHDLRTIAWNDEKRRVDVFSLSQPGKHPRNWKAVSLPCVRMLDELCSRMTVSAARLVGYSWDDHDIENEDVPRDALLMPRKMREMAYRGTGQSRQQKSMAPIRSHNTQTVGLLSKISNFLGFGVTEKLVISRFDAHMNAYAAEALYMLVVDSMGEDRFGVVQKDLKDLITLLCKLIAAIDTYERAKASVADKSDVTFLRIVDASLKSSLQRVVTTFGSHLSSLNLPEEHSRTIRMICLTDEL | 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 Topology: Multi-pass membrane protein
Sequence Mass (Da): 65763
Sequence Length: 588
Subcellular Location: Nucleus
|
G0S235 | MAAAVRRSPYKDFLQPALQRRFATATLVVLATAYFEALLLARWSSWLWSWFPLGPTGFRAALFFLCGIFVIILRISQYHPGIRTSDSPIATLVRYAPRWTTFETLFTYALSAWIFSLVYLGTVPDDAGFERITYFTYDRARLNEKPIFLTTHLVLLGIYQGVRHLYSDIDRLSLGTAQPSNGDSSKATGEDGHVSTQMRRFRDQLPKIVVHSLHQSVMGLLLSASLYPLLLRDLLWRVNMTMLRPLYSLPRTNVPPANLPYSPSTLLRCLAASVMVMFAWTAANTAFSLLLVKSPLKNGKPLTADAKDPNGSLLNGLKNKKLSIKCFAMWELAYIARDFPDRRKAIFEDMDRKDGPMWSQVYKICLDTLHTLSSNIDAYTAPPAPATTPQQAETALGDKPRTSAPPKEDHIFAPLPSNKSAFRTSVSSAFQNAALAGPGGPPASLSPVAKRTLHAARSRLLEAAAPNAEIEVTPSSFFRELALKYVLSSPLAGYPFRQTRRRRLASAVLGSPYGEPSLYVNAASAVSGLAVSSLREDRYGHVQRDVASLIRELTSLGEKLNAFVNEGGMGKHWTDVVELEGEDKCEEVEEVVNAVKHALKRVIVAFEPYARDLRLTRGEVKKAREVAGLEQEVEVREVMPEMVQIR | 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 components and of docking or interaction partners for transiently associated nuclear transport factors.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71820
Sequence Length: 646
Subcellular Location: Nucleus
|
Q9VCG4 | MSASSSSNACKLLLLGRCLRAVLLSVAIQFLLLTVFLLFVNFQLLHPLAWVTGTLRLVASWYTWFASIPLVASVVLYGVILCQQHLSERRYCPTRYRWLLHYGPRKVLFLFAHLLVGLLTAWLYTGYLHTDYQHLKYKCYGQDCISAYNVYLLGIGMTAGCYYFVSVHMRKEISIEFPIVEQSRAEKMRELLYASLAKSLLSSLLPTISYTAVFCLFGPMVCHRLSHILSVDMDERLDGFFGVVTNVRLLFYGYLLTAQILSNMHLMRCFYGILLSEDLPLVVTKPRAAFAHEQDITLVAGLGVFNVYVVQCLAAHHFYKLALRKNSPQRAEIFQLTEPGNRPASWRSLCDQCLSILGSFTEELTESMQKISILKCAQSLPMPKITESLTTSLMAEKVLLRQYNQKHGIRPIVSPSREVAVESPADGIRHFPNWCERVSTQLEQSLQRLLQRVPGIVYLFNEPEGAKTTFLLANSLPVVYMTQALAQVCAASLKEDPYGVVQNDLPAIIKAINKLRNELDKLSSVIGNIRISSSSFNVLRCAVRRSLYAICLSFCDYLDDLLPPGEELRQLQDLVCQE | 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 | MATAVSRPCAGRSRDILWRVLGWRIVASIVWSVLFLPICTTVFIIFSRIDLFHPIQWLSDSFSDLYSSYVIFYFLLLSVVIIIISIFNVEFYAVVPSIPCSRLALIGKIIHPQQLMHSFIHAAMGMVMAWCAAVITQGQYSFLVVPCTGTNSFGSPAAQTCLNEYHLFFLLTGAFMGYSYSLLYFVNNMNYLPFPIIQQYKFLRFRRSLLLLVKHSCVESLFLVRNFCILYYFLGYIPKAWISTAMNLHIDEQVHRPLDTVSGLLNLSLLYHVWLCGVFLLTTWYVSWILFKIYATEAHVFPVQPPFAEGSDECLPKVLNSNPPPIIKYLALQDLMLLSQYSPSRRQEVFSLSQPGGHPHNWTAISRECLNLLNGMTQKLILYQEAAATNGRVSSSYPVEPKKLNSPEETAFQTPKSSQMPRPSVPPLVKTSLFSSKLSTPDVVSPFGTPFGSSVMNRMAGIFDVNTCYGSPQSPQLIRRGPRLWTSASDQQMTEFSNPSPSTSISAEGKTMRQPSVIYSWIQNKREQIKNFLSKRVLIMYFFSKHPEASIQAVFSDAQMHIWALEGLSHLVAASFTEDRFGVVQTTLPAILNTLLTLQEAVDKYFKLPHASSKPPRISGSLVDTSYKTLRFAFRASLKTAIYRITTTFGEHLNAVQASAEHQKRLQQFLEFKE | 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 membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 76305
Sequence Length: 674
Subcellular Location: Nucleus
|
Q8VCB1 | MATAASGPCAGGSPRDILWRVLGWRIVTSIVWSVVLLPVCITAFIVLSSINLFHPIQWLSDSCNDFYSSQVIFHLLLLAVVIIIISIFNVEFYTVVPSISGSRLALIARILHPQQLTHSFIHAAMGMAVAWCAAIMTKGQYSSLVVPCTGTESLDSPAAQTCLNEYHLFFLLSGAFMGYSYSLLYFINNMNYLPFPIIQQYKFLRFRRSLLLLVKHSCVESLFMVRNFCIVYYFFGHIPKAWISTALDLHTDEQAHRPLDTIGGLLNVSLLYHVWLCGVFLLVTWYSSWILFKIYATEAHVFPVQPPFAEASDECLPKVLNSNPPRIVKYLALQDLMLLSQYSPSRRQEVFSLSQPGGHPHNWTAISRECLNLLNDMTQKLVLYQEAAATNGRMYSSYSVEPKKLSSAEETAFQTPKPSQTPSVPPLVKTSLFSPKLSTPNVSSPFGTPFGSSVVNRMAGILDVNPFSGSPQSPQLIRRGPRLWTHTSDQQVSAISNPSPCASVTAEGKTVRQPSVIYSWIQNKREQIKNFLSKRVLIMYFFSKHPEASIQAVFSDAQMHIWALEGLSHLVAASFTEDRFGVVQTTLPAILHTLLTLQEAVDKYFKLPHASSKPPRASGSLVDTSYKTLRFAFRASLKTAIYRITTTFGEHLNAVQASAEHQKRLQQFLEFKE | 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 membrane (By similarity).
PTM: Phosphorylated.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 75409
Sequence Length: 673
Subcellular Location: Nucleus
|
O13961 | MVMLRTSFPSGSRTKAVRYHTLLRPILQQRFLRACFALLCLCCITSYWFSSGPFISLSFWFLSLVRGFVCFFFMFPYFVMLKSRMSTQKVTKQSLGAQLFYDFSPKSFFLVYLTFAVSVSCLCLFYIKGHASSIRLQWIASPNAYELPSLNERFVYMTYFSHILILALTVEHLYLQRDSPSRPVINVSFFNYIFQNLGWLIRFSFRKSIICCLFTPFSYAILRSYIWRFAALLTSCCRRIAYTKTPPKWPLSLRLLLHSFWMAFIVCLTFQIALLIFRVFLYSGPMIRGKLLSARSNDPNGTLVDGMKTKKKPLTECIATEELWFIAKRDPQRIKSIFQDIDRSVSIWQELYSITESRCKELATSLKILQSTGDFSAATSKKSGLTKKTNIPYSPNSNHEEINSIPLRNKNIFVPPSQGHSPLLEKIKKQGSLPSTTPVNEGGISDIIPKSLYDQVIRFISTFYKAPVFGIFRKTLRRQNEALLPNPWLFCVTVNSLTQLVLKSLKYDTYGVVARDISSILAVYCDTFDVLVSYKRSLVKNHSNSTNLDDDFKNLNSAANALHCGIIDITEKFQDFFTQLNLSPRIERRCWVLFREYKSNS | 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: Multi-pass membrane protein
Sequence Mass (Da): 69355
Sequence Length: 601
Subcellular Location: Nucleus
|
P32500 | MIQTPRELLNPRYTYHTIFSDVCKTRFNHLVTRLFFICSIIQTVVISLLALPHSPLWELALAFIPNILALNLVSLLIIVTRKNYMHVKNFGFANSLTFILGQLLSVKFLVYQGVYSMGSILLSFVLGVVFGRGGSGWKPYYKLFIWLVVPTIYNLQHHVTDADKLSFNCENFFQAPQDYVLERVKRIMEKSVILSVISMFVLPIFTTVFFSRQKSGLFDSFTNGVLAVTNLLIISCIIFITFEFINIAFDAHMSIGCLHKGKLISNLSSTPMETLLSGLSADKPFTRLTAYQELAYRATSLDPSLRAPIYHSKFRSSSGNTWSLILNECLKTIQINNEKVVQYLRSVQDLGGSATARHKKKVENLDYMYENGKLTSANERLFGNRPSMMAPLRDNGLLDESPNRLRVRTDDSVLLNRGNKKRHRSSYYDNDLDETTQTFNGSIFTHETTFMTAMRLMLKKLKNSIMSFIFPSYAERQSSDESDNYRLLPNGSNKAQISIIDIWSISKKRQAEKLVPLPICHANSVVALTGLLIRSKTEDPKGGIIASVGDILKTLERSICALGEFADWDPESMAYTAFQTQRTAQDRVQQDSEDEDSMKDTTDMISVLYQLSTSAFMEIVLEYNVALNDVYLDADVAKLANWFLEVYASGNPNAT | 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 envelope, thus allowing for the assembly of the nucleoplasmic SPB side. NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 74134
Sequence Length: 655
Subcellular Location: Nucleus
|
P27724 | MTKIETRTEPMVLNMGPHHPSMHGVLRLIVTLDGEDVVDCEPVIGYLHRGMEKIAESRTNIMYVPYVSRWDYAAGMFNEAITVNAPEKLADIEVPKRAQYIRVIMLELNRIANHLLWLGPFMADVGAQTPFFYIFREREMIYDLWEAASGMRLINNNYFRVGGVAVDLPYGWNDKCEDFCDYFLPKVDEYEKLITNNPIFRRRVEGVGTVTREEAINWGLSGPMLRGSGVKWDLRKVDHYECYDELDWEVQYETAGDCFARYLVRIREMRESVKIIRQALKAMPGGPYENLEAKRLQEGKKSEWNDFQYQYIAKKVAPTFKIPAGEHYVRLESGKGELGIFIQGNDDVFPWRWKIRSADFNNLQILPHILKGVKVADIMAILGSIDIIMGSVDR | 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, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
PTM: The initiator methionine has been seen to be kept and removed.
Location Topology: Peripheral membrane protein
Catalytic Activity: a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n H(+)(out) + NAD(+)
Sequence Mass (Da): 45534
Sequence Length: 394
Subcellular Location: Cellular thylakoid membrane
EC: 7.1.1.-
|
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 plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Catalytic Activity: a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n H(+)(out) + NAD(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 18909
Sequence Length: 161
Subcellular Location: Plastid
EC: 7.1.1.-
|
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 reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
Catalytic Activity: a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n H(+)(out) + NAD(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 27346
Sequence Length: 248
Subcellular Location: Cellular thylakoid membrane
EC: 7.1.1.-
|
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 reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
Catalytic Activity: a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n H(+)(out) + NAD(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 24541
Sequence Length: 219
Subcellular Location: Cellular thylakoid membrane
EC: 7.1.1.-
|
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. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Catalytic Activity: a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n H(+)(out) + NAD(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 27983
Sequence Length: 250
Subcellular Location: Plastid
EC: 7.1.1.-
|
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, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration (By similarity).
Catalytic Activity: a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n H(+)(out) + NAD(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 12567
Sequence Length: 111
Subcellular Location: Cellular thylakoid membrane
EC: 7.1.1.-
|
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
Pathway: Purine metabolism.
Subcellular Location: Cytoplasm
EC: 2.7.4.6
|
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'-triphosphate + ADP
Sequence Mass (Da): 15343
Sequence Length: 138
Subcellular Location: Cytoplasm
EC: 2.7.4.6
|
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'-triphosphate + ADP
Sequence Mass (Da): 15874
Sequence Length: 141
Subcellular Location: Cytoplasm
EC: 2.7.4.6
|
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'-triphosphate + ADP
Sequence Mass (Da): 15142
Sequence Length: 137
Subcellular Location: Cytoplasm
EC: 2.7.4.6
|
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'-triphosphate + ADP
Sequence Mass (Da): 15286
Sequence Length: 137
Subcellular Location: Cytoplasm
EC: 2.7.4.6
|
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'-triphosphate + ADP
Sequence Mass (Da): 14527
Sequence Length: 135
Subcellular Location: Cytoplasm
EC: 2.7.4.6
|
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'-triphosphate + ADP
Sequence Mass (Da): 16679
Sequence Length: 149
Subcellular Location: Cytoplasm
EC: 2.7.4.6
|
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'-triphosphate + ADP
Sequence Mass (Da): 17396
Sequence Length: 153
Subcellular Location: Cytoplasm
EC: 2.7.4.6
|
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'-triphosphate + ADP
Sequence Mass (Da): 15408
Sequence Length: 139
Subcellular Location: Cytoplasm
EC: 2.7.4.6
|
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
Pathway: Purine metabolism.
Subcellular Location: Cytoplasm
EC: 2.7.4.6
|
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'-triphosphate + ADP
Sequence Mass (Da): 17103
Sequence Length: 147
Subcellular Location: Cytoplasm
EC: 2.7.4.6
|
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'-triphosphate + ADP
Sequence Mass (Da): 15024
Sequence Length: 135
Subcellular Location: Cytoplasm
EC: 2.7.4.6
|
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'-triphosphate + ADP
Sequence Mass (Da): 15344
Sequence Length: 137
Subcellular Location: Cytoplasm
EC: 2.7.4.6
|
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'-triphosphate + ADP
Sequence Mass (Da): 16820
Sequence Length: 150
Subcellular Location: Cytoplasm
EC: 2.7.4.6
|
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'-triphosphate + ADP
Sequence Mass (Da): 16664
Sequence Length: 147
Subcellular Location: Cytoplasm
EC: 2.7.4.6
|
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 (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 14793
Sequence Length: 124
Subcellular Location: Mitochondrion inner membrane
|
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 the enzyme is believed to be ubiquinone.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 15137
Sequence Length: 128
Subcellular Location: Mitochondrion inner membrane
|
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 the enzyme is believed to be ubiquinone.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 15283
Sequence Length: 131
Subcellular Location: Mitochondrion inner membrane
|
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. The precise function of this subunit is unknown but believed to be important.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 14812
Sequence Length: 124
Subcellular Location: Mitochondrion inner membrane
|
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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 12677
Sequence Length: 113
Subcellular Location: Mitochondrion inner membrane
|
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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 12551
Sequence Length: 113
Subcellular Location: Mitochondrion inner membrane
|
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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 12576
Sequence Length: 113
Subcellular Location: Mitochondrion inner membrane
|
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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 12556
Sequence Length: 113
Subcellular Location: Mitochondrion inner membrane
|
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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 20091
Sequence Length: 172
Domain: Contains four C-X9-C motifs that are predicted to form a helix-coil-helix structure, permitting the formation of intramolecular disulfide bonds.
Subcellular Location: Mitochondrion inner membrane
|
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 (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 11919
Sequence Length: 104
Subcellular Location: Mitochondrion inner membrane
|
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 .
PTM: May contain intrachain disulfide bonds, as evidenced by its electrophoretic mobility under reducing vs non-reducing conditions.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 20105
Sequence Length: 172
Domain: Contains four C-X9-C motifs that are predicted to form a helix-coil-helix structure, permitting the formation of intramolecular disulfide bonds.
Subcellular Location: Mitochondrion inner membrane
|
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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 19992
Sequence Length: 172
Domain: Contains four C-X9-C motifs that are predicted to form a helix-coil-helix structure, permitting the formation of intramolecular disulfide bonds.
Subcellular Location: Mitochondrion inner membrane
|
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 the enzyme is believed to be ubiquinone.
Sequence Mass (Da): 20753
Sequence Length: 183
Subcellular Location: Mitochondrion inner membrane
|
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: Peripheral membrane protein
Sequence Mass (Da): 20965
Sequence Length: 176
Subcellular Location: Mitochondrion inner membrane
|
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 intramolecular disulfide bonds is assisted by CHCHD4 and ensures folding, import into the mitochondrion and is required for the function in mitochondrial respiratory chain complex I assembly.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 20777
Sequence Length: 172
Subcellular Location: Mitochondrion inner membrane
|
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 (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 3269
Sequence Length: 29
Subcellular Location: Mitochondrion inner membrane
|
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.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 17317
Sequence Length: 153
Subcellular Location: Mitochondrion inner membrane
|
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.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 8784
Sequence Length: 76
Subcellular Location: Mitochondrion inner membrane
|
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.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 8734
Sequence Length: 76
Subcellular Location: Mitochondrion inner membrane
|
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.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 8625
Sequence Length: 76
Subcellular Location: Mitochondrion inner membrane
|
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 immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). May donate electrons to ubiquinone.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Sequence Mass (Da): 17129
Sequence Length: 145
Subcellular Location: Mitochondrion
EC: 7.1.1.2
|
Q9FNN5 | MAPVRGILGLQRAVSIWKESNRLTPALRSFSTQAASTSTTPQPPPPPPPPEKTHFGGLKDEDRIFTNLYGLHDPFLKGAMKRGDWHRTKDLVLKGTDWIVNEMKKSGLRGRGGAGFPSGLKWSFMPKVSDGRPSYLVVNADESEPGTCKDREIMRHDPHKLLEGCLIAGVGMRASAAYIYIRGEYVNERLNLEKARREAYAAGLLGKNACGSGYDFEVYIHFGAGAYICGEETALLESLEGKQGKPRLKPPFPANAGLYGCPTTVTNVETVAVSPTILRRGPEWFSSFGRKNNAGTKLFCISGHVNKPCTVEEEMSIPLKELIERHCGGVRGGWDNLLAIIPGGSSVPLIPKNICEDVLMDFDALKAVQSGLGTAAVIVMDKSTDVVDAIARLSYFYKHESCGQCTPCREGTGWLWMIMERMKVGNAKLEEIDMLQEVTKQIEGHTICALGDAAAWPVQGLIRHFRPELERRIRERAERELLQAAA | 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 the enzyme is believed to be ubiquinone (By similarity).
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 53449
Sequence Length: 486
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.2
|
Q92406 | MISRAAAPSSSIASLSSRSLRAQAPAARSFATVQDNAPPVKHYGGLKDQDRIFTNLYGHHGADLKSAMKYGDWHRTKDIVLKGHDWLISELKASGLRGRGGAGFPSGLKYSFMNFKDWDKDPRPRYLVVNADEGEPGTCKDREIMRKDPQKLIEGCLVVGRAMNANAAYMYIRGEFYQEATVLQRAINEAYEAGLIGKNACGTGYDFDVYIHRGMGAYVCGEETSLIESIEGKAGKPRLKPPFPAAVGLFGCPSTVTNVETVAVTPTIMRRGASWFSSFGRERNAGTKLFCISGHVNNPCTVEEEMSISLRDVIDRHCGGVRGGWDNLLAVIPGGSSTPVLPKTICDDQLMDFDALKDSQSGLGTAAVIVMDKSTDIVRAISRLSTFYKHESCGQCTPCREGSKWTMHMMQRMEKGQAREREIDMLQELTKQVEGHTICALGEAFAWPIQGLIRHFRPELEARIREYSKEVGGNGPYAGGWHPEARAEGKLISPGM | 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 the enzyme is believed to be ubiquinone (By similarity).
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 54452
Sequence Length: 496
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.2
|
Q54I90 | MMNLGNRVKSVIKLTSTTGLTGKDFQATKVATFSTAQVQQAQENVRSYGGLKDKDRIFTNLYGEHDVYLKGAIARGDWYKTKNIIDKGKDWILKEMMASGLRGRGGAGFPSGLKWSFMPKTTSKDRPQYLVINADEGEPGTCKDREIMRHDPHKLIEGCLLAGFAMRACAAYIYIRGEFHYEAKVLEQAIDEAYKAGLIGENACGTGYKFDVYVHRGAGAYICGEETALIESIEGKQGKPRLKPPFPAMAGLYGCPTTVTNVETVAVAPTILRRGGAWFASFGRPKNAGTKLFCISGHVNNPCTVEEEMSIPLRELIDKHCGGVIGGWDNLKGVIPGGSSVPVLPKNICDNVLMDFDDLRQHRSGLGTAAVIVMNKETDMIAAIARLSKFYKHESCGQCTPCREGVGWLYDITDRLVTGNAKPDEIDSLEEISRQIEGHTICALGDAAAWPVQGLIRHFRPEIEDRIKQFQLNKKQSPF | 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 the enzyme is believed to be ubiquinone (By similarity).
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 52691
Sequence Length: 479
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.2
|
P49821 | MLATRRLLGWSLPARVSVRFSGDTTAPKKTSFGSLKDEDRIFTNLYGRHDWRLKGSLSRGDWYKTKEILLKGPDWILGEIKTSGLRGRGGAGFPTGLKWSFMNKPSDGRPKYLVVNADEGEPGTCKDREILRHDPHKLLEGCLVGGRAMGARAAYIYIRGEFYNEASNLQVAIREAYEAGLIGKNACGSGYDFDVFVVRGAGAYICGEETALIESIEGKQGKPRLKPPFPADVGVFGCPTTVANVETVAVSPTICRRGGTWFAGFGRERNSGTKLFNISGHVNHPCTVEEEMSVPLKELIEKHAGGVTGGWDNLLAVIPGGSSTPLIPKSVCETVLMDFDALVQAQTGLGTAAVIVMDRSTDIVKAIARLIEFYKHESCGQCTPCREGVDWMNKVMARFVRGDARPAEIDSLWEISKQIEGHTICALGDGAAWPVQGLIRHFRPELEERMQRFAQQHQARQAAS | 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(+)(out) + NAD(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 50817
Sequence Length: 464
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.2
|
P24917 | MLSRTAAPTKASARTLSRAAAEQCRTFATVQDGSANPVRHYGGLKDQDRIFQNLYGRYPPDLKHAKKMGDWHKTKEILLKGHDWIIGEVKASGLRGRGGAGFPSGLKWSFMNFKDWDKDDKPRYLVVNADEGEPGTCKDREIMRKDPHKLVEGCLVAGRAMNATAAYIYIRGEFIQEAAILQNAINEAYADGLIGKNACGSGYDFDVYLHRGAGAYVCGEETSLIESLEGKPGKPRLKPPFPAAVGLFGCPSTVANVETVAVAPTICRRGGNWFAGFGRERNQGTKLFCISGHVNNPCTVEEEMSIPMRELIDKHCGGVRGGWDNLLAVIPGGSSTPILPKHICDTQLMDFDALKDSQSGLGTAALIVMDKSTDVVRAISRLSHFYRHESCGQCTPCREGSKWTEQIMKRFEKGQGREREIDMLQELTKQVEGHTICALGEAFAWPIQGLIRHFRPELEARIRKFAQENGGEALAGGWQRNARQQGKLVSPGM | 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 the enzyme is believed to be ubiquinone.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 54241
Sequence Length: 493
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.2
|
O94500 | MLSRGHCCKLKHSFNGLRNVALKRLVGSKAGYRMFPNLIEKRIRRIDDALADGEYENLSEILKYDPLNIIELVQESELRGRGRYGFPTGEKMLSLYKATSSERGRKEKPVVIVNAAENDIGSFKDRLLLRHEPHKIIEGAIIAARAVEASACYLFIRKDYYEETVMMQKCIIQAYAKKLLGKNLLGTSIGLELLIHPGAGSYITGEESALIQSLQGEFPVPDIPINNTITSGLFGLPTLVLNVETVSNLPAIIKKGPKFFISMGRPNNRGTKLFSISGEVNEPNVIEACMSIPLKDLIENYAGGVRGGWNKLVGIFPGGPCSGILNKNQCEQVTMDFDSLKALDSSLGTGSVIVLNDHDQIFESLLNFAKFYSTNTCHTCPVCRDGVEDVIETLKGLKDGHAHLSQLKDMFSKFNMPSSSKVFCGFGDSMRHQIHSIQRNFPDQITFRTKVT | 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 acceptor for the enzyme is believed to be ubiquinone (By similarity).
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Sequence Mass (Da): 28389
Sequence Length: 255
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.2
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.