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Full Name
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sequence
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2.75k
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5.51k
AlphaFoldDB
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Q12SP7
MURI_SHEDO
Glutamate racemase
Shewanella
MSGPILVFDSGIGGLSVLAEIRKRLPAENYCYLFDNARLPYGDLSESELIRGCVELICQQVQQVEAKIVVVACNTASTLVLPVLRQRLTIPVVGVVPAIKPAALLSKRKHIGVLATPGTVSRDYTHGLISQFAEDCQVDLFGSSELVMLAEQKAAKLPVNNQQLAKILAPIKASKLDVLVLGCTHFPMIKEELSQYLGESVLLLDSGEAIANRVASLLEPAALSEALHSGTTLHGGANSGTKGIGVIHAAYTQAITAGLNITLQEYGISDSSLIVTK
Provides the (R)-glutamate required for cell wall biosynthesis.
Q12SP7
Q72PA2
SUCC_LEPIC
Succinyl-CoA synthetase subunit beta
Leptospira
MKIHEYQAKEILRRHKANVPFGVVIDKKENASKAHDEVTSKTGGSVVVVKAQIHAGGRGKGGGVKVTKTKEDAIAAVDKILGMQLITPQTGPEGKKVLKVYLEQGIDIAKEYYLSILLDRSIRKTIIMASTEGGMEIEEVAETHPEKILKIAIDPGIGLQVNQARQLAFELGLPAESHKSFQSLLAAIYEAYIKEDASLLEINPLILTKQNEIIAGDCKIDLDENALYRHADNAAFRDITEEDPLEVQASEFNLNYVKLDGNIGCMVNGAGLAMATMDIVKLAGAEPANFLDVGGGANKTTVTNGFKIILGDPNVKGIFVNIFGGIVRCDMVAEGIIEAAKAVDLKVPLVVRLQGTNSELGREVLNKSGLKITGVDDLREAASTIAKLIG
Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
Q72PA2
Q8TII9
VATD_METAC
V-ATPase subunit D
Methanosarcina
MAQQDVKPTRSELINLKKKIKLSESGHKLLKMKRDGLILEFFKILNEARNVRTELDAAYEKSTEKINLASAVNGMVAVKSTAFTAKEYPEIQLSGHNIMGVVVPKISSTGVRKPLYERGYGIIGTNSYIDETADAYEELVEKIIAAAELETTMKRLLDEIEKTKRRVNALEFKVIPELIATMKYIRFMLEEMERENTFRLKRVKARMKN
Produces ATP from ADP in the presence of a proton gradient across the membrane.
Q8TII9
A6WP56
SYM_SHEB8
Methionyl-tRNA synthetase
Shewanella
MATSQRKILVTSALPYANGPIHLGHMLEYIQTDIWSRYQKLRGHECHYICADDAHGTPIMLKAQQLGIAPEDMIAQVNKEHQQDFADFNVAFDNYHSTHSEENRLMASDIYLKLRDNGYIKSKSISQLFDPEKSMFLPDRFVKGTCPKCKSPDQYGDNCDSCGATYSPTELINPKSAVSGATPVMKDTEHFFFDLPAFEGMLKEWTRSGALQVEMANKLDEWFEQGLQQWDITRDAPYFGFEIPDAPGKYFYVWLDAPIGYMGSFKNLCAKRPELSFDEFWGKDSTAEVYHFIGKDIVYFHSLFWPAMLHGSGYRQPNSVYAHGYVTVNGAKMSKSKGTFIKARTYLDHLDPEYLRYYYAAKLSSRIDDLDLNLEDFAQRVNSDLVGKLVNLASRTAGFITKRFNGKLAKINDTTLTEAFLAKQDVIADFYESREYGKAMREIMALADIANGFVADAAPWQMVKHDDQQEAAHQVCSNALNLFRILVTYLKPVLPRLAQDVEAFFQLPLTWDALSQDLAGHEIAPFKAMMQRVELDKVNAMVADSKDNLQVTADAPKTAAPEKTAEASSVSSEPLVDDPISETINFDDFAKIDLRIARIIKAEHVADADKLLKLQLDIGGETRQVFAGIKSAYSPEDLEGKLTVMVANLAPRKMRFGMSEGMVLAAGPGGSDLWILEPHEGAQPGMRVK
Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
A6WP56
Q2JII9
GLMU_SYNJB
Glucosamine-1-phosphate N-acetyltransferase
unclassified Synechococcus
MAERELSVAILAAGKGTRMRSQLPKVLHKLGSLSLIERLLRTVLTLKPHRCLVVVGYEQEQVRQALREYPVEFVEQAQQLGTGHAVQQLLPVLGGFQGDLLVINGDVPLLRAETLQALVERHRQVNPEVTLLSAQVADPYGYGRVFCDAQQRVLELVEERDCTPAQRQNRRINSGVYCFHWPALAQVLPHLNRNNAQQEYYLTDAVKRVGKAIALDVADPQEIVGVNDRRQLAQAYQILQDRLKEAWMEAGVTFVDPDSSSLEETVELAPDVVIEPQTHLRGVCRIGPGTRLGPGSWIESSEIGSGCHILYSVVSHSRIGNHVWIGPYAHVRPHSQIGDHCRIGNFVETKNAQIGSHSNAAHLAYLGDAKLGSQVNIGAGTIIANYDGQQKHFTEIGDRSKTGANSVLVAPLQVGSDVTIAAGSTIPARYPLPDDCLVIARSRPVVKPGWRLGIRSSRPQEPQPMPPGSLKIYPLRLFPGQDLKQELERLARQQPLQAGFVLSAVGSLSQATLRLADQTGDHLLSERLEILALSGSLCPDGVHLHLTVADARGQTWGGHLRPGCLIYTTAEIVLADSPEYRFSRQPDPATGYLELHIQPVAGDPCWPSPPPQPQQNQQTKPEADNSRPKSLQ
Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.
Q2JII9
A1UFB6
APT_MYCSK
Adenine phosphoribosyltransferase
unclassified Mycobacterium
MTDISKVIASLMREVPDFPEPGIQFKDLTPLLADAEGLMAVTDALAATAEGADLVAGIDARGFLLGAAVALRLGTGVLAVRKGGKLPPPVHSQTYNLEYGSATLEIPADGLDIAGRSVVIIDDVLATGGTVAATHRLLTSGGATVLHAAVVLELTALGGREVVQPLSVSSLYTV
Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
A1UFB6
B0U1N1
ACCA_XYLFM
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha
Xylella
MNPNYLDFEQPIADLEAKIQELRTASAGPSVNVDTEVRALENKLRLRTAQIFRNLSAWQISQLARHPRRPYTLDYISVVCDEFQELAGDRTLADDKAIVGGLARIGHRPVMLIGHQKGRDNKERLMRNFGMPKPEGYRKALRLMKLAERFGLPLLTFIDTMGAWPGIDAEERNQSEAIATNLIEMAELKIPVICTVIGEGGSGGALAIGIGDRTLMLEYSTYSVITPEGCASILWKDAAKASDAAEQLNLTARRLKEFGLIDKVIREPIGGAHRNPQQMANRLKAVLLNELEALDKVPLVTLLNQRHKRLRTYGAYENH
Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA.
B0U1N1
A0JM41
MYP0_XENTR
Myelin protein zero
Silurana
MESSGLRAPCSLLVLLSALVLPPTLAIEVYTDREVYGTVGSRVTLSCSFWSSEWISDDVSVTWHYQPDHSREMYSIFHYAKGQPSIDAGVFKDRIEWVGSPKWKDASIVLHNLELIDNGTFTCDVKNPPDVVGKSSYVHLQVQEKGAARAGLVLGIIIAVALALVIVVTILILLIRYCWLRRQVRVQRELSALERGKLHKAKDSSKRSSRQTPILYAMLDQTRGKASEKKGKGGIGDSRKDRK
Creation of an extracellular membrane face which guides the wrapping process and ultimately compacts adjacent lamellae.
A0JM41
O84711
CLPX_CHLTR
ATP-dependent Clp protease ATP-binding subunit ClpX
Chlamydia
MTKKNLAVCSFCGRSEKDVEKLIAGPSVYICDYCIKLCSGILDKTPAPATQEIATSSTSSPTSLRVLTPKEIKRHIDSYVIGQERAKKTISVAVYNHYKRIRALMQDKQVSYGKSNVLLLGPTGSGKTLIAKTLAKILDVPFTIADATTLTEAGYVGEDVENIVLRLLQAADYDVARAERGIIYIDEIDKIGRTTANVSITRDVSGEGVQQALLKIIEGTVANIPPKGGRKHPNQEYIRVNTENILFIVGGAFVNLDKIIAKRLGRTTIGFSEETDLAVTNRDHLLAKVETEDLIAFGMIPEFIGRFNCVVNCEELTLDELVEILTEPANAIVKQYTELFEEENVKLIFEKEALYAIAQKAKQAKTGARALGMILENLLRDLMFEIPSDPTVEAIRIEEDTITQNKPPVIIQKSPEAIA
ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.
O84711
Q8PTQ6
NIKR3_METMA
Putative nickel-responsive regulator 3
Methanosarcina
MGKKLMRIGISLPGELLDKFDKTLMKRGYSSRSEGIRDAIRTYNQHYEWMKQIRGSRSATISIVYDCSKKGVTSTLAEIQHEYVDMISSSVHFHMEEDLCFEVIILRGEGEQIVDLAQRILSIKGVKHLRLTTVPEEKNE
Transcriptional regulator.
Q8PTQ6
P25553
ALDA_ECOLI
Glycolaldehyde dehydrogenase
Escherichia
MSVPVQHPMYIDGQFVTWRGDAWIDVVNPATEAVISRIPDGQAEDARKAIDAAERAQPEWEALPAIERASWLRKISAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPRGVFNLVLGRGETVGQELAGNPKVAMVSMTGSVSAGEKIMATAAKNITKVCLELGGKAPAIVMDDADLELAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQAVQFGNPAERNDIAMGPLINAAALERVEQKVARAVEEGARVAFGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPVLPVVAFDTLEDAISMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHGLHEYLQTQVVYLQS
Catalyzes the irreversible oxidation of L-lactaldehyde to L-lactate . Also shows high activity with glycolaldehyde and L-glyceraldehyde . Has weaker activity with various aldehydes such as methylglyoxal, propionaldehyde or benzaldehyde . Involved in the degradation of lactaldehyde produced during metabolism of L-fucose and L-rhamnose . It may be involved in several other metabolic pathways .
P25553
B0UYF2
S7A14_DANRE
Solute carrier family 7 member 14
Danio
MSGLFAKLDPRRVQWGANWFAFRSRVLRTKPVESMLETSGGTGAHGTKLARVLSTVDLVSLGVGSCVGTGMYVVSGLVAKEMAGPGVIVSFIIAAVASILSGVCYAEFGVRVPKTTGSAYTYSYVTVGEFVAFFIGWNLILEYLIGTAAGASALSSMFDSLANHSISGFMINHIGTLNGLGKGEQSYPDILALVIGILVTVIVALGVKNSVGFNNVLNVINLVVWVFIMIAGLFFVSGSNWDEGRFLPYGWSGVMQGAATCFYAFIGFDIIATTGEEAKSPNTSIPYAITASLVTCLTAYVSVSVILTLMVPYTEIDSDAPLMEMFSLHGFQTAKYIVAIGSIAGLTVSLLGSLFPMPRVIYAMAGDGLLFRFLAHVSTYTETPAVACVVSGFLSALLALLVSLRDLIEMMSIGTLLAYTLVSVCVLLLRYQPEGDIHGFVNFLSEQNSKRKEGVLAECEKEACSPVSEGDDYGGVPTNTCGAKNLPSLGDNEMLIGKPDKSTYTASHPNYGTVDMSSGIESDETDSAYLLKLKKLLGPRYYTMRIRLGLPGKMDRPTVATGRIVTRCVVLLFILIFCFCSLIIFGSGQIADGQWWAVLLLVVLLLVLTLLVFIIIQQPENPKRLPYMAPCVPFVPASAMLVNVYLMLKLSTITWIRFGVWCFVGVLIYFGYGMWNSTLEITAREEEAHASTYQRYDMGVDDNFAVDDDLYPSGDQGPFQNWGKGGQQKQPQQEQSEPQSDGLDRLDNHRTSSSSSHSRAKSKASKPSPGFEALVVDDDLDDPLE
May be involved in arginine transport.
B0UYF2
A7N128
HEM6_VIBC1
Oxygen-dependent coproporphyrinogen-III oxidase
Vibrio
MSAIDKHAVKQFLMSLQDSICQQLEQEDGKAVFVEDAWQREKGERLGGGGRTRVLRDGHIFEQGGVNFSHVEGNEMPASATAHRPELAGRRFEAMGVSLVIHPKNPYVPTSHANVRFFIAEKDGEDPIWWFGGGFDLTPFYPFDEDCQSWHDTAKQLCAPFGDEVYPEHKAWCDKYFFLPHRNETRGVGGLFFDDLNQWEFDKCFDYIKAVGEGYCQAYLPIVSRRKDIEFGEREREFQLYRRGRYVEFNLVYDRGTLFGLQSGGRTESILMSMPPLARWEYSYEPQTGSPEAELYERYLTPREW
Involved in the heme biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-IX.
A7N128
O26911
COFH_METTH
FO synthase subunit 2
Methanothermobacter
MNIKTRTKKILQKAMDEPITKEEALYLMGVTGRDLQALMIAADMVREAEAGDRITYIENWNINFTNICSGQCGFCAFKRDAADGDSYYLETERILEIAAEAIEKGARELCIQGGLYPGLDTYFYEDLIRAIKSEFPDVHLHSFSPMEVYYGAQNAELTVEEALKILKRAGLGSMPGTAAEILDDDVRAVICPTKLSTGEWVEVIETAHRVGIPTTCTMMYGHIDGPEHRVEHMDILRRIQEKTGGFTEFVPLPFMHPHAPIYREGLAMPGATGADDLKVYAISRLMFRGLIENIQASWVKLGFKFAQVALLSGANDIGGTLGEENISKSAGASHGVRTEPEEIIRVVRDIGRIPARRDTLYREIEDV
Catalyzes the radical-mediated synthesis of 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil from 5-amino-6-(D-ribitylamino)uracil and L-tyrosine.
O26911
A9B6A7
TATA_HERA2
Sec-independent protein translocase protein TatA
Herpetosiphon
MAGLGVTELLIILAIVIVLFGASRIGDLGGAMGRGIREFRRGVRDEDATAPTDASKNESK
Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
A9B6A7
Q0SIG0
PSA_RHOJR
Proteasome core protein PrcA
Rhodococcus
MTMPYYASAEQIMRDRSELARKGIARGRSVVVLTFRDGVLFVAENPSTALHKVSELYDRLGFAAVGKYNEFENLRRAGIVHADMRGYSYDRRDVTGRSLANAYAQTLGTIFTEQPKPYEVEICVAEVGRVGSPKAPQLYRITYDGSIVDEQHFVVMGGTTEPIATAMRESYRADLDLEAAVGIAVNALRQGGAGEGEKRNVDVASLEVAVLDQSRPRRAFRRITGPALEQLIPAEPAPASEPAPESKPDTETKPADPQD
Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation.
Q0SIG0
B0SYU4
HUTU_CAUSK
Imidazolonepropionate hydrolase
unclassified Caulobacter
MTRLDNTRVIRPATGTELTAKSWLTEAPLRMLMNNLHPDVAERPEELVVYGGIGRAARDWESYDKIVETLRRLEDDETLLVQSGKPVGVFKTHPDAPRVLIANSNLVPRWATWEHFNELDRKGLAMYGQMTAGSWIYIGAQGIVQGTYETFVEMGRQHHGGDLAGKWLLTAGLGGMGGAQPLAAVMAGASCLAIECQPSRIEMRLRTGYLDKATERLDEALAWIAEANAAKAPVSVGLLGNAAELLPAMFAAGVRPDLLTDQTSAHDPINGYLPAGWTLDQWATAKEREPETVNRAARASMAVHVQAMLDFQAAGVPTVDYGNNIRQMALEEGVKNAFDFPGFVPAYIRPLFCRGIGPFRWAALSGDPEDIAKTDAKVKELIPDNPHLHHWLDMAAEKIKFQGLPARICWVGLGDRHRLGLAFNAMVASGELKAPVVIGRDHLDSGSVASPNRETEAMMDGSDAVSDWPLLNALLNTASGATWVSLHHGGGVGMGFSQHAGMVIVADGTEAAAKRLARVLWNDPASGVMRHADAGYEIAKACAREHGLDLPGIL
Catalyzes the conversion of urocanate to 4-imidazolone-5-propionate.
B0SYU4
B3DRY2
APT_BIFLD
Adenine phosphoribosyltransferase
Bifidobacterium
MAQSDITIDALSKVGQQDAEYLVSLVRSVPGFPKEGIIFRDFMPVLADPKGLKILLKALEEALPVSPSEFDSIAGLESRGFLFGPAMAAHLGKGFIAVRKAGKLPPETIGESYDLEYGTASVEIETDAVQAGKRVLIVDDLIATGGTAKAATDLIEKAGGTVVGFSFVMRLDGLDGLDKLDGKPSSSLIAMPA
Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
B3DRY2
B9M5V2
FPG_GEODF
DNA-(apurinic or apyrimidinic site) lyase MutM
Geotalea
MPELPEVETIRRAVGPQVRGKRIIHTNVRATKLRHPLPPELDRLLVGQLIVAMDRRGKYLLLRCKGGTIIFHLGMTGMLYLVKASSPHGKHDHLDLVLDGSYILRFTDPRRFGTIIWTDNDPLQHPLLVAHGPEPLEAEFSASYLYLKRHRRKIPIKQLIMDSRVVAGIGNIYANESLFRAGIAPQTSASDLSPDKDLLLVDAIKGVLTDAVEAGTSNIESALTGERPQGYFPYEFSIYGKKGRPCPKCGSAIRMMRLGGRSTFFCPLCQK
Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.
B9M5V2
B7KL75
GLMM_GLOC7
Phosphoglucosamine mutase
Gloeothece citriformis
MVTSLYRNGNGRLNSYTQDTANLGVVNQLCPLPKTPLFGTDGIRGKVGELLNASLALDLGFCAAQVLKATMPTPGPIIIGQDSRNSSDMLTTAITAGLTSAGVEVWQIGLCPTPCVAYLARNTEAMGGIMISASHNPPEDNGIKFFDHQGLKLSKGLAQQVEDLLRNTLESNSQRESSLSWGKYYHRRELIEQYLQQLSLSIPTDVNLEGMRIVLDLAWGAAVEIAPQVFKSLGAEVICLHDQPDGDRINVNCGSTHLNLLQQAVKEFGADLGVAFDGDADRVLAVDSEGRVVDGDYILYFWGQTLKAQDKLPNNLIIATVMANLGFEKAWQNLGGQLIRTAVGDQHVQAQMWETGAMLGGEQSGHIICHHHGVSGDGIQTALHLAALVRQSGRSLGALVEQSFQPYPQILRNVRVEDRERRCNWKDCNPLQIAIAEAQAAMGDRGRVLVRASGTEPLIRVMVESECAQSANYWTEHLIGVVQKYLA
Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate.
B7KL75
A9M8R8
DAPF_BRUC2
PLP-independent amino acid racemase
Brucella
MATKAAFARMNGLGNQIIVADMRGRADSITSAAAIRLASDSETAFDQIMAIHDPRTPGTDYYIAIINCDGTQAQACGNGTRCVVQALAAETGRHAFTFETRAGILTATEHDDGLISVDMGTPRFDWQDIPLAQAVADTRKIELQVGPADAPVLHSPSIASMGNPHAVFWVDKDVWSYELDKFGPLLENHPIFPERANISIAHVTSSDTIDLRTWERGAGLTRACGSAACAAAVSAARTGRTGRKVTVNVPGGPLLIEWRDDDHVMMTGPAEWEFSGTFDPATGEWSRDTQGLQGSGNADRGTA
Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan.
A9M8R8
Q1JDG6
METN_STRPB
Methionine import ATP-binding protein MetN
Streptococcus
MNEAIIQLDHIDITFRQKKRVIEAVKDVTVHINQGDIYGIVGYSGAGKSTLVRVINLLQAPTNGKITVDGDVTFDQGKVQLSANALRQKRRDIGMIFQHFNLMAQKTAKENVAFALRHSSLSKTEKEHKVIELLELVGLSERADNYPAQLSGGQKQRVAIARALANDPKILISDEATSALDPKTTKQILALLQELNRKLGLTIVMITHEMQIVKDICNRVAVMQNGVLIEEGSVLDIFSNPKEALTQEFITTATGIDEALEKINQQDIVKHLPANALLAQLKYAGTSTDEPLLNSIYRQFEVTANILYGNIEILDHIPVGDMIVVLEGQAENILAAEKALHEAGVDVSILKRGA
Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system.
Q1JDG6
Q9RGS4
YIDC_STACT
Membrane protein YidC
Staphylococcus
MKKKALLPLLLGIMVFLAGCDYSKPENRTGFFYNTFVKNMDNIIHWLGASFNNDYGLAIIVLVLAIRIIVLPFMLSNYKNSHMMREKMIIAKPDMDAVKEKVQRARTQEDKMAANQEMMEVYKKYDMNPMQSMLGCLPMLIQMPIIMGLFFVLKYPSPGGITEHSHFLWFNLAKPDIWITVIAGVLYFLQAYVSTFSMPPEQKQMSYMMMIISPIMIIWVSLSSAAALGLYWSVSAAFLIVQTYIANAYYSKKAKEEVAPMIAAYEKEHGGSGNSKGAKVVSKKNKKKK
Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins.
Q9RGS4
Q9SLP9
CAS1_LUFAE
Cycloartenol synthase
Luffa
MWQLKIGADTVPADPSNAGGWLSSLNNHVGRQVWHFHPELGTPEDLQQIQHARQRFSDHRFEKKHSADLLMRMQFAKNNSSFVNLPQIKVKDKEDVTEEAVSRTLRRAINFYSTIQGDDGHWPGDYGGPMFLIPGLVITLSITGALNAVLSTEHQREICRYLYNHQNKDGGWGLHIEGPSTMFGSVLNYVSLRLLGEEAEDGQGAVDKARKWILDHGGASAITSWGKMWLSVLGVYEWAGNNPLPPELWLLPYLLPFHPGRMWCHCRMVYLPMCYLYGKRFVGPITPIIRSLRKELYLVPYHEVDWNKARNECAKEDLYYPHPLVQDIVWASLHHVYEPLFMRWPAKRLREKALQCVMQHIHYEDENTRYICIGPVNKVLNMLCCWVEDPHSEAFKLHIPRIFDYLWIAEDGMKMQGYNGSQLWDTAFAVQAIMSTKLAEEYGTTLRKAHKYIKDSQVLEDCPGDLQSWYRHISKGAWPFSTADHGWPISDCTAEGLKAVLLLSKLPSEIVGKSIDEEQIYDAVNVILSLQNTDGGFATYELTRSYPWLELMNPAETFGDIVIDYTYVECTSAAIQALVAFKKLYPGHRRDEIDNCVAKAADFIESIQATDGSWYGSWGVCFTYGGWFGIRGLVAAGRRYDNCSSLRKACDFLLSKELASGGWGESYLSGQNKVYTNIKDDRPHIVNTGWAMLSLIDAGQSERDPTPLHRAARILINSQMDDGDFPQEEIMGIFNKNCMISYAAYRNIFPIWALGEYRCRVLQAP
Oxidosqualene cyclase involved in the biosynthesis of cycloartenol.
Q9SLP9
A4G064
HMD_METM5
N(5),N(10)-methenyltetrahydromethanopterin hydrogenase
Methanococcus
MKVAILGAGCYRTHAASGITNFSRAAQVAKEVGIPEITMTHSTITMGAELLHLIPEITEVVVSDPCFAEEPGIVVLDQFDYKTVMEAHLAGDAEKVMPEIREAVKAKAKETPKPPKGCIHFVHPETIGLKVTASDVEAVKNADIVITWLPKGGSQPAIIEKFVGAIKKGAIVTHACTIPTPKFAKIFKDMGRDDLNIIAYHPGAVPEMKGQAFLSEGLADAEKVEEFYCMAKTARGEAFKMPANLISPVCDMGSAVTAPVYAGILAYRDAVTQILGAPADFAQMMADEAITQLLELMRSEGIKNMEDKLNPKALTGTADSMCFGPLADILPTSLKVLEKHTNENKCECSCSIKP
Catalyzes the reversible reduction of methenyl-H(4)MPT(+) to methylene-H(4)MPT.
A4G064
A3DIZ5
RPOC_ACET2
Transcriptase subunit beta'
Acetivibrio
MFELNNFDSIRIGLASPEKIREWSRGEVKKPETINYRTLKPERDGLFCERIFGPQKDWECHCGKYKRIRYKGIVCDRCGVEVTRSKVRRERMGHIELAAPVSHIWYFKGIPSRMGLLLDMSPRALEKILYFAAYVVIDPGQTPLSKKQILSEKEYRDSLEKFGPKFRAGMGAEAVRELLQEINLDELSAELREEIKQSTGQKRVRAIKRLEVVEAFRQSQNKPEWMILDVIPVIPPELRPMVQLDGGRFATSDLNDLYRRVINRNNRLKRLLDLGAPDIIVRNEKRMLQEAVDALIDNGRRGRPVTGPGNRPLKSLSDMLKGKQGRFRQNLLGKRVDYSGRSVIVVGPELKIYQCGLPKEMALELFKPFVMKKLVNDGLAHNIKSAKRMVERVRNEVWDVLEEVIKEHPVLLNRAPTLHRLGIQAFEPVLVEGRALKLHPLVCTAYNADFDGDQMAVHVPLSAEAQAEARFLMLSANNLLKPQDGKPVAVPTQDMVLGSYYLTILKEGAKGEGRVFTSMDEAVMAYDNGEIELHSKIKVRMKRVVDGVEKSKIIETTLGRLIFNEAIPQDLGFVDRSDPDKIFDLEVDFLVGKNELKKIIDKSIKVHGTTKTAILLDKIKELGFKYSTKGAITISISDMVIPEVKAKYIKETEEKIEKITKQYKRGLISDEERYNSVIAAWTEASENITRALINNLDRFNPVYMMSQSGARGNINQIKQLAGMRGLMADTSGKTIEFPIKANFREGLTVMEFFISTHGARKGLADTALRTADSGYLTRRLVDVSQDVIVRETDCGTRKGIEVTDIKDGNEVIEELSERIIGRYPVGNIVHPETGEIIVEAGRMITDQDAEKIVKAGIKKVRIRSVLTCHSEYGVCAKCYGANLATGEECNVGEAVGIIAAQSIGEPGTQLTMRTFHTGGVAGEDITQGLPRVEELFEARKPKGLAIISEIKGTVKISETKKKREIVVTSEDGETRSYLIPYGSRIKVSDGDQVEAGDELTEGSVNPHDILKIKGVEAVQTYLVHEVQKVYRMQGVDINDKHIEVIVRQMLRKVKVEDPGDTSLLPGGLVDVFDFEEENAKAIAEGKKPAVAKRALLGITKAALATDSFLSAASFQETTRVLTEAAIKGKVDPLVGLKENVIIGKLIPAGTGMSRYKDITISTVTE
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
A3DIZ5
Q0WQD2
GAUT3_ARATH
Probable galacturonosyltransferase 3
Arabidopsis
MTTFSTCAAFLSLVVVLHAVHVGGAILESQAPHRELKAYRPLQDNNLQEVYASSAAAVHYDPDLKDVNIVATYSDHYGNIRLGRVKMGDLSPSWVLENPAYQVSRKTKGSQLVIPRDSFQNDTGMEDNASHSTTNQTDESENQFPNVDFASPAKLKRQILRQERRGQRTLELIRQEKETDEQMQEAAIQKSMSFENSVIGKYSIWRRDYESPNADAILKLMRDQIIMAKAYANIAKSKNVTNLYVFLMQQCGENKRVIGKATSDADLPSSALDQAKAMGHALSLAKDELYDCHELAKKFRAILQSTERKVDGLKKKGTFLIQLAAKTFPKPLHCLSLQLAADYFILGFNEEDAVKEDVSQKKLEDPSLYHYAIFSDNVLATSVVVNSTVLNAKEPQRHVFHIVTDKLNFGAMKMWFRINAPADATIQVENINDFKWLNSSYCSVLRQLESARLKEYYFKANHPSSISAGADNLKYRNPKYLSMLNHLRFYLPEVYPKLEKILFLDDDIVVQKDLAPLWEIDMQGKVNGAVETCKESFHRFDKYLNFSNPKISENFDAGACGWAFGMNMFDLKEWRKRNITGIYHYWQDLNEDRTLWKLGSLPPGLITFYNLTYAMDRSWHVLGLGYDPALNQTAIENAAVVHYNGNYKPWLGLAFAKYKPYWSKYVEYDNPYLRRCDINE
May be involved in pectin and/or xylans biosynthesis in cell walls.
Q0WQD2
P40312
CYB5_YEAST
Cytochrome b5
Saccharomyces
MPKVYSYQEVAEHNGPENFWIIIDDKVYDVSQFKDEHPGGDEIIMDLGGQDATESFVDIGHSDEALRLLKGLYIGDVDKTSERVSVEKVSTSENQSKGSGTLVVILAILMLGVAYYLLNE
Membrane bound hemoprotein which function as an electron carrier for several membrane bound oxygenases. It plays a role in fatty-acid desaturation and is also involved in several steps of the sterol biosynthesis pathway, particularly in the 4-demethylation of the 4,4'-dimethyl zymosterol.
P40312
Q39024
MPK4_ARATH
Mitogen-activated protein kinase 4
Arabidopsis
MSAESCFGSSGDQSSSKGVATHGGSYVQYNVYGNLFEVSRKYVPPLRPIGRGAYGIVCAATNSETGEEVAIKKIGNAFDNIIDAKRTLREIKLLKHMDHENVIAVKDIIKPPQRENFNDVYIVYELMDTDLHQIIRSNQPLTDDHCRFFLYQLLRGLKYVHSANVLHRDLKPSNLLLNANCDLKLGDFGLARTKSETDFMTEYVVTRWYRAPELLLNCSEYTAAIDIWSVGCILGETMTREPLFPGKDYVHQLRLITELIGSPDDSSLGFLRSDNARRYVRQLPQYPRQNFAARFPNMSAGAVDLLEKMLVFDPSRRITVDEALCHPYLAPLHDINEEPVCVRPFNFDFEQPTLTEENIKELIYRETVKFNPQDSV
The ANPs-MKK6-MPK4 module is involved in the regulation of plant cytokinesis during meiosis and mitosis. Essential to promote the progression of cytokinesis and for cellularization (formation of the cell plate) during male-specific meiosis. Involved in cortical microtubules organization and stabilization by regulating the phosphorylation state of microtubule-associated proteins such as MAP65-1. Involved in root hair development process. Negative regulator of systemic acquired resistance (SAR) and salicylic acid- (SA) mediated defense response. Required for jasmonic acid- (JA) mediated defense gene expression. May regulate activity of transcription factor controlling pathogenesis-related (PR) gene expression. Seems to act independently of the SAR regulatory protein NPR1 (Nonexpresser of PR1). Phosphorylates MKS1 and transcription factors WRKY25 and WRKY33. The MEKK1, MKK1/MKK2 and MPK4 function in a signaling pathway that modulates the expression of genes responding to biotic and abiotic stresses and also plays an important role in pathogen defense by negatively regulating innate immunity . Phosphorylates MEKK2 upon treatment with flg22 . Involved in stomatal movement regulation by repressing HT1 and HT1-mediated GHR1 phosphorylation .
Q39024
Q824N9
RL5_CHLCV
50S ribosomal protein L5
Chlamydia
MSRLKKLYTEEIRKSLQEKFGYGNTMQIPVLRKIVISMGLAEAAKDKNLFQAHLEELSMISGQKPLVTKARNSIAGFKLREGQGIGAKVTLRGQRMYDFMDRFCNIVSPRIRDFRGFSMKGDGRGCYSLGLDDQQIFPEIDLDRVKRTQGMNITWVTTAQTDVECTTLLELMGLRFKKAQ
This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.
Q824N9
Q5WDS1
TYSY_ALKCK
Thymidylate synthase
Alkalihalobacillus
MEQYLQLCEHVLQNGSPKSDRTGTGTISVFGYQMRFDLEKGFPIVTTKKLHMRSIIHELLWFLKGDTNIRYLQENGVRIWNEWADENGDLGPVYGKQWRSWEGANGKTVDQITEVVEQIKTNPNSRRLIVNAWNVAEIEEMALAPCHCLFQFYVNDGKLSCQLYQRSADIFLGVPFNISSYALLTMMMAQVCGLKPGEFIHTFGDAHLYNNHIEQTKLQLTRKPKQLPTMHINPEVTDLFAFTYDDFELKHYDPYPHIKAEVSV
Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis.
Q5WDS1
Q4FVB6
PAND_PSYA2
Aspartate 1-decarboxylase alpha chain
Psychrobacter
MLLNMLKCKLHRARVTHAELHYEGSCGIDGDLLDLAGLRENESIDIYNVTNGKRFRTYAIRAEAGSGIISLNGAAAHMADLGDIVIICAYAHFDEVEASTYQPRLVYCNEDNTVKDTANIIPVQVA
Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
Q4FVB6
A0Q845
HEM1_FRATN
Glutamyl-tRNA reductase
Francisella
MALISLAIDYKKSPIEVRSEFALSGLDVSMLYRSILAIDNVVHAVILSTCNRTEVYLEISDLRVVDDILVWWQGYVRNPNYKIKDYFKLRQGTEVIMHLMKLACGLESMVLGEPQILGQVKDSYTLSKKNHAIGKELDRVFQKVFATAKRVRSETRIGYCPVSVAFSAITLAKRQLDNICSKNVLIIGAGQTGELLFRHVTALAPKQIMLANRTIEKAQKITSAFRNASAHYLSELPQLIKKADIIIAAVNVSEYIVTCKDVGDKPRVFIDISIPQALDPKLGELEQNVYYCVDDINAVIEDNKDKRKYESSKAQKIIVKSLEEYLEKEKAIISNSAIKELFQKADGLVDLSLEKSLAKIRNGKDAEEIIKRFAYEIKKKVLHYPVVGMKEASKQGRSDCLVCMKRMFGLNVEK
Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
A0Q845
A1BF85
COAD_CHLPD
Pantetheine-phosphate adenylyltransferase
Chlorobium
MKRKAIYPGTFDPFTNGHLDVLDRALNIFDEVEVVIGENSQKKTLFTVNERLEMIREIVIEFPGVTVAVLHDGLLANYARQVEARAIVRGVRQVKDFEYEFQMSLLNRHLYPEVTTVFLMPNVKYTYVASSIIREVAMLGGDVSKFVHPCVLAMLHKKLQENKKSNS
Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
A1BF85
Q13U01
SECA_PARXL
Protein translocase subunit SecA
Paraburkholderia
MTTGFLQKIFGSRNQRLVKQYQKTVAAINALEPQIEQLTDDQLRGKTGEFRQRVASGESLDKLLPEAFAVCREASKRVLKMRHFDVQLIGGMVLHYGKIGEMRTGEGKTLVATLPVYLNALSGRGVHVVTVNDYLAQRDAEWMARLYNFLGLSVGINLSQMDHAAKQEAYAADITYGTNNEFGFDYLRDNMVYETDARVQRALNFAVVDEVDSILIDEARTPLIISGQAEDHTELYVRMNALPPLLERQIGEEKADGTGVEKPGDYTLDEKGRQVFLTESGHEKAERLLSEWGLIGEGESLYAPQNITLMHHVYAALRAHTLFFKDQHYVVQNGEVVIVDEFTGRLMSGRRWSDGLHQAVEAKEHVKIQSENQTLASITFQNYFRMYAKLSGMTGTADTEAYEFNEIYGLETVVIPTNRPPKRIDKQDQIYKTAKERYDAVIRDIRDCYERGQPVLVGTTSIENSELLSHLLKQAGLPHEVLNAKQHAREAEIVAEAGRPKRITIATNMAGRGTDIVLGGNAEKQASFLELDETLPEDEKRRRIQKLHDEWQALHDQVKAAGGLHIIGTERHESRRIDNQLRGRAGRQGDPGSSRFYLSLEDPLLRIFAGDRVRAIMERLKMPEGEAIEAGIVSRSIESAQRKVEARNFDIRKQLLEYDDVSNDQRKVIYQQRNELLEANDITETIGAMRQSVIADIVHQFVPAGSIEEQWDVPELEEVLRNEWQLDLAIQEMINESNSISADEILEAVEAAADEAYEAKVELVGRESFSAFERSIMLQTLDRSWREHLAALDHLRQGIHLRGYAQKNPKQEYKREAFELFAAMLDAVKLEVTRVVMNVQIQSPEQLEQAAEQLEEQGSHLENVEFRHAEFAEAAAAAPVAAEAATAAMIGDAMSHGSSQAAAANMSADNVPKVGRNDPCPCGSGKKYKQCHGKIV
Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
Q13U01
Q3ZYP4
SYE_DEHMC
Glutamyl-tRNA synthetase
Dehalococcoides
MTNEVRVRYAPSPTGYPHLGNIRTAMFNWLFARHNGGKFIVRIEDTDRERYVEGAVESILESLNWLGLDWDEGPDKGGDYGPYYQSERLPLYRKAAEKLVAEGKAYYCHCSSEKLDKMREDQIARKEPPGYDRCCRDMGLGQKEGAVIRFKIPLDGQTAFTDLIRGEVTFDNAKQDDFVILKSDGFPTYHLASVVDDHAMQISHVLRAEEWLPSTPKHLMLYKALGYTPPLYAHLPMILGPDRSKLSKRHGATSTIEYKQAGYLPETMVNFLSLLGWAYDDKTELFSREQLIEYFCLEKVSKTAAIFNYEKLDWMNGMYIRTLSAQDLACRAMPFLEKDVRIAASGHLNLDYTVKVMPLIQERAKKLNELAELCWFIYSDDISYDPALLIDKKLTKETSLSALKAANARLEALPNFDAASMEEHIRPLAAELELKPGQLFGMLRTASTGQQVAPPLFQTMEVLGRQRCLWRIAMAIARLSEMPFQRS
Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
Q3ZYP4
P67023
SYE_STRP1
Glutamyl-tRNA synthetase
Streptococcus
MSKPIRVRYAPSPTGLLHIGNARTALFNYLYARRHGGTFIIRIEDTDRKRHVEDGERSQLENLKWLGMDWDESPETHENYRQSERLALYQQYIDQLLAEGKAYKSYVTEEELAAERERQEAAGETPRYINEFIGMSADEKAKYIAEREAAGIVPTVRLAVNESGIYKWTDMVKGDIEFEGGNIGGDWVIQKKDGYPTYNFAVVVDDHDMQISHVIRGDDHIANTPKQLMVYEALGWEAPEFGHMTLIINSETGKKLSKRDTNTLQFIEDYRKKGYMPEAVFNFIALLGWNPGGEEEIFSREQLIALFDENRLSKSPAAFDQKKMDWMSNEYLKHADFETVYALCKPFLEEAGRLTEKAEKLVELYKPQLKSADEIIPLTDLFFSDFPELTEAEKEVMAGETVSTVLQAFKAKLEAMSDEDFKPENIFPQIKAVQKETGIKGKNLFMPIRIAVSGEMHGPELPNTIYLLGRDKSIEHIKNML
Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
P67023
Q48F57
GLND_PSE14
[Protein-PII]-UMP uridylyl-removing enzyme
Pseudomonas
MPQVDPDLFDRGQFQAELALKASPIAAFKKAIRRAKDVLDDRFKSGRDIRRLIEDRAWFVDNILQKAWDQFEWSEDADIALLAVGGYGRGELHPYSDIDLLILLDSDDHEVFREPIERFLTLLWDIGLEVGQSVRSVNECAQEGRADLTVITNLMESRTIAGPEHLRQRMLEVTSTEHMWPSKEFFLAKHAEQKKRHHKYNDTEYNLEPNVKGSPGGLRDIQTILWVARRQYGTLNLHALAGEGFLLGSENALLASSQEFLWKVRYALHMLAGRSEDRLLFDYQVRIAGLLGYEDSDAKLAIERFMQKYYRVVMSIAELSDLIIQHFEEVILSDDSGTAQPINSRFQLHDGYIEATNPNVFKRTPFAMIEIFVLMAQHPEIKGVRADTIRLLREHRHLINDDFRNDIRNTSLFIELFKCETGIHRNLRRMNRYGILGLYLPEFGHIVGQMQHDLFHIYTVDAHTLNLIKHLRKLQYTEVSEKFPLASKIMARLPKPELIYLAGLYHDIGKGRGGDHSELGAIDAQAFGTRHHLPDWDTRLIVWLVSNHLVMSTTAQRKDLSDPQVIHDFAQFVGDEVHLDYLYVLTVADINATNPTLWNSWRASLLRQLYTETKRALRRGLENPVDREEQIRRTQTAALDILVRNGTDPDDVEQLWSALGDDYFLRHTAGDVAWHSDAILQQPADGGPLVLIKETTQREFEGGTQIFIYAPDQHDFFAVTVAAMDQLNLNIHDARIITSSSKFTLDTYIVLDNEGGSIGDNPERVQEIRNGLTEALRNPDDYPTIIKRRVPRQLKHFAFAPQVTIHNDAQRPVTVLELLAPDRPGLLARIGKIFLEFDLSLQNAKIATLGERVEDVFFITDANNHPLSDPQLCSQLQDAIVKQLSVNSEPGHDLRISI
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Q48F57
A3MSF2
HIS3_PYRCJ
Phosphoribosyl-AMP cyclohydrolase
Pyrobaculum
MDAVPLATPEEAWRIAKSLNYRHIGGTVVAVVQDVETGEVLMVGHMDPVAVVLTLTTGLAHYYSTSRKRIWLKGETSGHYQIVKEFRTDCDGDAVVLKVVQIGAACHTGARSCFSSPASFKIRLNRDA
Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.
A3MSF2
Q8VHL5
CRGN_MOUSE
Gamma-N-crystallin
Mus
MAQRSGKITLYEGKHFTGRKLEVFGDCDNFQDQGFMNRVNSIRVESGAWVCFDHPDFRGQQFILEHGDYPEFFRWNGHNDHMGSCRPVGMHGEHFRIDIFEGCNFTGQCLEFVEDCPFLQSRGWAKSCVNAIKVYGDGAWVLYEEPNYRGRMYVLERGDYRCFSDWGAHSARVQSLRRVLNFF
Crystallins are the dominant structural components of the vertebrate eye lens (Probable). Also plays an important role for integrity and function of auditory nuclei .
Q8VHL5
A7IEC3
BIOB_XANP2
Biotin synthase
Xanthobacter
MTTSTGTTTGTGTARAAEGSLLRSDWTEAEARALYDLPFPELMFRAQSVHRRHFDPTTVETATLLSIKTGGCAEDCGYCSQSAHHETGLKATKLMGVEEVLSQAQKAKDGGATRFCMGAAWRSPKDRDLDAVCAMISGVKAMGLEACVTLGMLTPDQVTRLGAAGLDYYNHNIDTSPAFYPEIVTTRTMDDRLDTLASVRAGGIRLCTGGIVGMGESVDDRIAMLLVLATLDPHPESVPINMWNEIEGTPVMGKADKPDPIAFVRLIALARLLMPQSIVRLSAGRDAMSDEMQALCFLAGANSIFTGDVLLTTANPERDKDAALFARLGIRAAAPAATEMRSAAE
Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
A7IEC3
P26905
DPPD_BACSU
Dipeptide transport ATP-binding protein DppD
Bacillus
MEKVLSVQNLHVSFTTYGGTVQAVRGVSFDLYKGETFAIVGESGCGKSVTSQSIMGLLPPYSAKVTDGRILFKNKDLCRLSDKEMRGIRGADISMIFQDPMTALNPTLTVGDQLGEALLRHKKMSKKAARKEVLSMLSLVGIPDPGERLKQYPHQFSGGMRQRIVIAMALICEPDILIADEPTTALDVTIQAQILELFKEIQRKTDVSVILITHDLGVVAQVADRVAVMYAGKMAEIGTRKDIFYQPQHPYTKGLLGSVPRLDLNGAELTPIDGTPPDLFSPPPGCPFAARCPNRMVVCDRVYPGQTIRSDSHTVNCWLQDQRAEHAVLSGDAKD
Probably part of the ABC transporter DppBCDE involved in dipeptide transport (Probable). Responsible for energy coupling to the transport system (Probable).
P26905
O35775
SYCN_RAT
Proximal small intestine-specific protein 9
Rattus
MSPLCLLLLALALVAVPGARGACPVPADLKKSDGTRTCARLYENSDPYYDNCCQGPELSVDPGTDLPYLPSDWSNSASSLVVAQRCELTVWSLPGKRGKTRKFSTGSYPRLEEYRKGIFGTWAKSISGLYCKCY
Functions in exocytosis in pancreatic acinar cells regulating the fusion of zymogen granules with each other. May have a pore-forming activity on membranes and regulate exocytosis in other exocrine tissues.
O35775
O29346
SYG_ARCFU
Glycyl-tRNA synthetase
Archaeoglobus
MHMSEIMEMLIRRGFLWQSFEIYGGMAGFIDYAPLGNNLRRKIENIWRKYFVINERAAEIDTPTIGIEEVFIASGHATSFTDVAIECENCGRVYRADHYVKEKLGIEVDETVEAVKEVMEVYDLKCECGGRFKDPAPMNLMFSTTIGPGKGKKGYLRPETAQGMFVDFKRLANFFREKLPFGVAQIGRAYRNEISPRQGVIRLREFNQAELEFFVHPGEKKHPHFSLYAKDVVKLVDKFDSQHEITLEEAVEKGIIANQILAYFIGKTRRFLLEIGIKDEKLRFRQHKDVERAHYATDCWDAEVLTSYGWIEVVGIADRTNYDLKRHSKFSGEDLSVFVPYEEPVKVKRRKIVPILSKLGPEFRQKAKKVAEALEALNVEADLDEVEVEVDGEKVKVTKEFFEIQEVEEEVTGEKVIPHVIEPSFGLDRITYSVLEHAFDKDVVDGEERRVLRLKRWVSPIEVAVLPLLSREPFESKGMEIVQMLREEGIFTDYDDSGSIGRRYRRFDEIGTPFCVTVDHQTFEDETVTIRDRDTTAQVRVKLGELPSILKELLRSEKDITEFGEVFRQV
Catalyzes the attachment of glycine to tRNA(Gly).
O29346
Q9KNK2
HSLO_VIBCH
Heat shock protein 33 homolog
Vibrio
MANNMLHRYLFKDLSVRGELVQLDDTYQQMISSQEYPAAVQHLIGELLVATSLLTATLKFEGSITLQLQGNGPVSLVVINGDNNQQVRGVARWKGDIADDASLHDMLGKGHLVITIEPKQGERYQGVVGLEGDTLAQVLEGYFERSEQLKTRLWIRVGKHDGKACAAGMLLQIVPDGKGSAEDFEHLEQLTNTIKDEELFALPAEELLYRLYNQETVQLFTPQQISFRCGCSRERSAAAIVTVAREEINDILAQDGAVALHCDYCGTTYSFDSAQVAELYAPSSANGSTLH
Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.
Q9KNK2
P28418
RBL_GEUQU
Ribulose bisphosphate carboxylase large chain
Geum
VGFKAGVKEYKLTYYTPDYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVPGEESQFIAYVAYPLDLFEEGSVTNLFTSIVGNVFGFKALRALRLEDLRIPPAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEALFKAQAETGEIKGHYLNATAGTCEEMMKRAIFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRMSGGDHIHAGTVVGKLEGEREITLGFVDLLRDDFIEKDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLAREGNEVIREAAKWSPELAAACEVWKEIKFEF
RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.
P28418
Q3KLB0
ENO_CHLTA
2-phosphoglycerate dehydratase
Chlamydia
MFDVVISDIEAREILDSRGYPTLCVKVITNTGTFGEACVPSGASTGIKEALELRDKDPKRYQGKGVLQAISNVEKVLMPALQGFSVFDQITADAIMIDADGTPNKEKLGANAILGVSLALAKAAANTLQRPLYRYLGGSFSHVLPCPMMNLINGGMHATNGLQFQEFMIRPISAPSLTEAVRMGAEVFNALKKILQNRQLATGVGDEGGFAPNLASNAEALDLLLTAIETAGFTPREDISLALDCAASSFYNTQDKTYDGKSYADQVGILAELCEHYPIDSIEDGLAEEDFEGWKLLSETLGDRVQLVGDDLFVTNSALIAEGIAQGLANAVLIKPNQIGTLTETAEAIRLATIQGYATILSHRSGETEDTTIADLAVAFNTGQIKTGSLSRSERIAKYNRLMAIEEEMGPEALFQDSNPFSKA
Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
Q3KLB0
B2HWM9
OBG_ACIBC
GTP-binding protein Obg
Acinetobacter calcoaceticus/baumannii complex
MRFVDEAVITVEAGDGGNGVASFRREKFVPFGGPDGGDGGRGGSIYIQADDDTSTLVDYRYTRKFRAERGKNGAGANCTGRGGEDVVLKVPVGTTIVDTDSGDIIGDLVEDGQRVMVASGGEGGLGNTHFKSSTNRAPRKCTTGTKGEFREIRLELKVLADVGLLGMPNAGKSTFIRAVSAAKPKVADYPFTTMVPNLGVVDADRHRSFVMADIPGLIEGAAEGAGLGIRFLKHLARTRILLHIIDVQPIDGSDPAHNAKAIMNELAKFSPTLAKLPIVLVLNKLDQIAEESREEWCQHILDELQWTGPVFKTSGLLEEGTKEVVYYLMDQIEQQREREVEDPEYAAEVRAFREQLEAETREQTIAAKEAYRAMRKAQRLESMMDDDDDFDDDEDDGDVESIYVRD
An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control.
B2HWM9
Q02QY1
RNFD_PSEAB
Rnf electron transport complex subunit D
Pseudomonas
MALPRPTSPHARGSNRTPAIMRLVLGACVPGLLTLTWLYGPGTLLNLAWASLVALACEAAMLALRKRPPGVFLKDGSALVTALLLAVALPPYAPWWLTLVATFFALVFGKHLYGGLGQNPFNPAMLGYVVALVSFPLEMTRWPSPDSALGLPDSLREFLGLATRPDAWAHATALDVLKTDRSLTVDELFAGNPAFGHLGSAGSEWVNLAFLLGGLFLLWRRLFTWHAPLGMLAGLFAMSLLFWNGSGSDSHGSPLFHLFSGATMLGAFFIVTDPVSGATSNRGRLVFGLGVGVLTYVIRAWGGYPDGVAFAVLLMNLAAPTIDYYTRPRTYGHRKAERGFKAGD
Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
Q02QY1
Q38YR8
CH10_LATSS
Chaperonin-10
Latilactobacillus
MLKPLEDRVVIAVKDEAEQTVGGIVIASNAKQKPQTGKVVAVGAGAMTSDGQRIPLDVKENDEVIYDKYAGSEVEYEGQQYLVLHAKDIIAIIE
Together with the chaperonin GroEL, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. GroES binds to the apical surface of the GroEL ring, thereby capping the opening of the GroEL channel.
Q38YR8
Q8CPM1
COXX_STAES
Heme O synthase
Staphylococcus
MNKDQTLSHTTGRVSFKELQQIIKMGLVQGNLIPAFAGAWLAIVMTNHSFLSSIPQILLMLVGSTLIMGGACALNNYYDQDIDRIMPSKQGRPTVNDRISDRNLLMLSFGMMLIGEACLFLLNIPSGVLGLIGIVGYVSYYSIWSKRHTTWNTVVGSFPGAVPPLIGWVAIDGSLSLAAVALFLVVFCWQPIHFYALAIKRSDEYALANIPMLPSVKGFKRTRVSMFIWLVLLLPLPFLLSNLGVTFVVIATLLNLGWLALGFTTFRKESNQTKWATQMFVYSLNYLVVFFALVVVVSLIKMI
Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
Q8CPM1
Q9UWW8
VATB_SACS2
V-ATPase subunit B
Saccharolobus
MLSVREFSNISMIKGPLVYVQGVTDASYNELVEIEMPNGERRRGLVIDSQMGIAIVQVFEGTTGVSPTGTKIRMLGRGLEVKISEEMLGRIFNPLGDSLDNGPPVIKGEKRDINGSPLNPAAREYPEEFIQTGISAIDGLNALLRGQKLPIFSGSGLPANMLAAQIAKQATVRGEESNFAVVFAAIGARYDDALFFRKFFEETGAINRVAMIVSLANEPPVMKTLTPKTALTLAEYLAFEQDMHVLAILIDMTNYCEALREISAAREEVPGRGGYPGYMYTDLATIYERAGKVIGKKGSITQMPILTMPNDDITHPIPDLTGYITEGQIVLDRALYNKGIYPPINVLMSLSRLAKDGIGEGKTRDDHKDVSNQLFASYARAVDTRGLAAIIGEDSLSEVDRKYLLFGELFERKFVSQGFNENRSIETTLDIGWEILSVLPESELTNIKTQYIQKYHPNYRGKK
Produces ATP from ADP in the presence of a proton gradient across the membrane. The archaeal beta chain is a regulatory subunit.
Q9UWW8
C1DFV8
DEF_AZOVD
Polypeptide deformylase
Azotobacter
MAILTILEFPDPRLRTIAKPIETVDDGIRRLIDDMFETMYAAPGIGLAATQVNVHKRLVVMDLSEDKNEPRVFINPEFEALTEELEPYQEGCLSVPGFYENVDRPQKVRIRALDRDGQPFELVAEGLLAVCIQHECDHLNGKLFVDYLSTLKRDRIRKKLEKQHRQHG
Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
C1DFV8
A6W5U4
RS3_KINRD
30S ribosomal protein S3
Kineococcus
MGQKVNPFGFRLGITTDHRSRWFADSTKTGQRYADYVKEDVAIRRLMSKGMERAGISKVEIERTRDRVRVDIHTARPGIVIGRRGAEADRIRTELEKLTGKQVQLNILEVKNPEVDAQLVAQGVAEQLASRVSFRRAMRKGMQTTMRSGAKGIRVQCAGRLGGAEMSRSEFYREGRVPLHTLRANIDYGFYEARTTFGRIGVKVWIYHGDITSRELAQSQAAAPRAPRRNERGDRPDRGARRTRPAQDTTAPVAEAVATGSAPTGTAATEPVIGKGSNGTEA
Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation.
A6W5U4
Q9ZDT4
PSD_RICPR
Phosphatidylserine decarboxylase beta chain
typhus group
MKQYNDLFKIIHREGYIFIASFALVSFLLASFNEKLGCIGFIATIWCIYFFRNPDRFVPISDDLVISPADGIIQEIKEASPPPELGLGDLEMIRVSIFLNIFNIHVNRIPANGKILALHYNPGKFFNASLDKASLYNERQSVLMETDQGQKIVFVQIAGLIARRIVCDLEEDNEVKMGERYGIIRFGSRVDVYLPLKTALLVSKGQTAIGGETIIADFGRKKTEEFKFERK
Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
Q9ZDT4
Q9XLE1
CYB_REDFU
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
Redunca
MTNIRKTHPLMKIVNNAFIDLPAPSNISSWWNFGSLLGICLMLQILTGLFLAMHYTSDTATAFSSVTHICRDVNYGWIIRYMHANGASMFFICLFMHVGRGLYYGSYMFLETWNIGVILLFATMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTNLVEWIWGGFSVDKATLTRFFAFHFILPFIIMALAMVHLLFLHETGSNNPTGISSDVDKIPFHPYYTIKDILGALLLILALMLLVLFTPDLLGDPDNYTPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALVLSILILVLMPLLHTSKQRSMMFRPISQCLFWILVADLLTLTWIGGQPVEHPYIIIGQLASIMYFLLILILMPTASTIENNLLKW
Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
Q9XLE1
B6HRA4
SDHF2_PENRW
Succinate dehydrogenase assembly factor 2, mitochondrial
Penicillium chrysogenum species complex
MSAPRILHRVARPVPSSISTITRLNRQFGTTALRLKDGSDEASPEVKAHRANQANKAPNQFVPNTTSTMTKDFVNVGQKPAPPEMLNSANPNYRPSDPYPGRIEHFTGGRQDNGAQKPELGVGEMEGITFKVEPLKRVGEELATKRARLLYQSRKRGILESDLLLSTFADVYLGKMNYDQLVEYDSFLDENDWDIYYWATQDSPEEISPSTPKEDTITETWKESGAKSGEWAQTIGAFRAAYRPVPSRWQNSEVLALLREHVRDKSATGFEKAKNKKTGGGGGLGRMPDVQVFNSGHIVHRRHVLRMLYI
Plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Required for flavinylation (covalent attachment of FAD) of the flavoprotein subunit of the SDH catalytic dimer.
B6HRA4
P58793
PURA_FUSNN
IMP--aspartate ligase
Fusobacterium
MAGYVVVGTQWGDEGKGKIIDVLSEKADYVVRFQGGNNAGHTVVVDGEKFILQLLPSGVLQAGTCVIGPGVVIDPKVFLDEIDRIEKRGAKTDHVIISDRAHVIMPYHIEMDKIRESVEDRIKIGTTKKGIGPCYADKISRDGIRMSDLLDLKQFEEKLRYNLKEKNEIFTKIYGLEPLDFDTIFEEYKGYAEKIKHRIVDTIPMVNKALDENKLVLFEGAQAMMLDINYGTYPYVTSSSPTLGGVTTGAGISPRKIDKGIGVMKAYTTRVGEGPFVTEIKGEFGDKIRGIGGEYGAVTGRPRRCGWLDLVVGRYATEINGLTDIVMTKIDVLSGLGKLKICTAYEIDGVIHEYVPADTKSLDRAIPIYEELDGWDEDITQIKKYEDLPVNCRKYLERVQEILGCPISVVSVGPDRSQNIHIREI
Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
P58793
B9DNH1
YQGF_STACT
Putative pre-16S rRNA nuclease
Staphylococcus
MLTHKIIGLDVGSKTVGVAVSDLMGWTAQGLDTLRINEEENELGITKLAEIIKKEDADTVVIGLPKNMNNSIGFRGEASLKYKEELLKILPDINVVMWDERLSTMAAERSLLEADVSRSKRKKVIDKMAAVFILQGYLDSLQ
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
B9DNH1
Q2V3I3
EPFL4_ARATH
CHALLAH-LIKE2
Arabidopsis
MGTFRRRRRFLLAALVTFALLHLFSASSIVSADGRWIGQRTGSDLPGGFIRSNKRFGGPGSSPPTCRSKCGKCQPCKPVHVPIQPGLSMPLEYYPEAWRCKCGNKLFMP
Acts primarily as positive regulator of inflorescence growth. Endodermal expression is sufficient for proper inflorescence architecture . Redundantly involved with EPFL6 in procambial development regulation. Controls stomatal patterning. Mediates stomatal development inhibition. TMM (AC Q9SSD1) functions to dampen or block CLL2 signaling. Acts as growth-regulatory ligand for ERECTA family receptors.
Q2V3I3
A1SA65
PURA_SHEAM
IMP--aspartate ligase
Shewanella
MGKNVVVLGTQWGDEGKGKIVDLLTEQAKYVVRYQGGHNAGHTLVIDGVKTVLHLIPSGILRDNVKCIIGNGVVLAPDALMKEISMLKERGVPVEDRLLISEACPLILPFHCAVDIAREKARGNKAIGTTGRGIGPAYEDKVSRRGLRVGDLFNAELFAEKLKEVMKYHNFMLTEYYGAEAVDYQTTLDDALAMADYLKSMCVDVTEMLDQARKAGENILFEGAQGTLLDIDHGTYPFVTSSNTTAGGVATGSGFGPCHLDYVLGIMKAYTTRVGAGPFPTELECEIGDHLGTKGHEFGATTGRKRRPGWLDAVAMKRAIQINSLTGICLTKLDVLDGLEEVKICVGYQQPDGTVTTVTPLAAEGYELVTPVYETLPGWSENTFGVTSMDQLPQAAVNYIKRIEEILETPIDIISTGPDRNETFIRVSPFN
Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
A1SA65
Q2W548
COXX2_MAGSA
Heme O synthase 2
Magnetospirillum
MTANLKVLASVFKLRIGVFCALAAIAGALATPGAVPDFAPVMAVALAVLLSAAAAGAFNHYWERDIDPMMNRTRNRPFATGQFAAGPLWPLGLLALTVAAVALAAFAANAWAALHVFLGAFVYGIVYTVWLKRRTAWNIVIGGLSGSFAVLAGAAVAVPTLSPESLILALVLFLWTPPHFWSLATALKDDYAAAGIPMLPVVCSETETNRIILANTIALVASSLLPAFFGAGPLYLGAAILGGGWFLYKSVALVRRPGRKAAMGNFFASLIQLVLLLTAVMVEPLLAG
Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
Q2W548
Q6CMK7
SLD1_KLULA
Delta 8-(E)-sphingolipid desaturase
Kluyveromyces
MSRVLSRRDIADRIAKGQTIVIYEDSVLNLDKWIKFHPGGDKSIYHMIGRDATDEMNAYHDDQTITKFKIWKIGRIDYPWENMLPPIQGGRFSKIDERDDIGDYDINLTSKWRSVDESNQYTKIPKNDRLASEAEVKIYPKIPQGVVPSLDLKEAYEKKIVVDPAIVSENYDNERVYEDLTNFPSLDVKNQEWIASEYRKLHGEITAAGLYQCNYVRYLKEFLRIGTLFGISFYLLSLKWFAISAICLGFAWQQLVFIAHDAGHISITHNYQVDNIIGMTVASWIGGLSLGWWKRNHNVHHLVTNDPVHDPDIQHLPFFAVSTRLFHNVYSTYYDKFLWFDKFAQKVVPIQHYLYYPILCFGRFNLYRLSWMHVLLGQGPRRGKAAWFRYYELAGLSFFNYWFFYLIIYKQMPTNAERFKYVMISHIATMIVHVQITLSHFAMSTSDLGVTESFPMRQLRTSMDVDCPRWLDFFHGGLQFQVIHHLFPRLPRHNLRDAQSLVIKFCDKVGIKYSIYGFAAGNDVVISHLQQIAQQAHTMLECAKTMKKEATDTEFHTNKHVLAANVNEKRKQE
Delta(8)-fatty-acid desaturase which introduces a double bond at the 8-position in the long-chain base (LCB) of ceramides. Required for the formation of the di-unsaturated sphingoid base (E,E)-sphinga-4,8-dienine during glucosylceramide (GluCer) biosynthesis.
Q6CMK7
B3H6D0
HIP45_ARATH
Heavy metal-associated isoprenylated plant protein 45
Arabidopsis
MFDWIHGNSRLPIALSIVELLVDMDCKGCEKKVRRAISKLDGVDTVEIDVDRQKVTVTGYVDREEVLKMVKRTGRTAEYWPFPYNGYYGDYYTYPSQHLEQSDQKIYQTISYSGKYDFYDVDDFQNTNNSTINGYYPSSSQKVQPNIDENALHLFSDDNAHACTIM
Heavy-metal-binding protein.
B3H6D0
A5D9W7
MCA1_PICGU
Metacaspase-1
Meyerozyma
MFPGSGRQTYQQQGYPPPQGAPQYNYGPPQGPPQGYYNGPPQGYNGPPQGPPPQNYNYGHYGPPQGQGQGYGQGGPAPQMYNNNRQSGAMNDVSTAPQRFGNTDMTYQLSNCSGRKKALLVGINYFGSSNELRGCVNDIKNMSNFLNRRFGYSYDDMVILTDDQNQRNKIPTKENIIRAMQWLVKDARPNDSLVFHYSGHGGITKDLDGDEDEGYDEVIYPVDFQQAGHIVDDDMHAIMVRPLPPGCKLTALFDSCHSGTALDLPFVYSTKGVVKEPNLWKDAGTDAFGAFMQYERGNIGGAISSIGGLLKKVTNSSSSNRQQVINIKASPADVISISGCKDDQTSADASINNNATGAMSWAFIKTMTDMPEQSYLSLLNNMRTLLKEKYSQKPQLSSSHPQDMNIRFIM
Involved in cell death (apoptosis).
A5D9W7
Q3Z2G2
MNTP_SHISS
Probable manganese efflux pump MntP
Shigella
MNITATVLLAFGMSMDAFAASVGKGATLHKPKFSEALRTGLIFGAVETLTPLIGWGMGMLASRFVLEWNHWIAFVLLIFLGGRMIIEGFRGADDEDEEPRRRHGFWLLVTTAIATSLDAMAVGVGLAFLQVNIIATALAIGCATLIMSTLGMMVGRFIGSIIGKKAEILGGLVLIGIGVQILWTHFHG
Probably functions as a manganese efflux pump.
Q3Z2G2
Q2LWT5
DUT_SYNAS
dUTP pyrophosphatase
Syntrophus
MTGIRISVQTLPHFEGLSLPRYMSEHAAGMDICAAVADEVVILPGERALIPTGIAIALPEGFEAQIRPRSGLALKHGVTLVNAPGTIDADYRGEIGVLLINHGNDPFVVARGSRVAQMVIAPVCRVAWSESGSLETTTRGDGGFGHTDES
This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.
Q2LWT5
O48109
CYB_PYTRG
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
Python
MPHHYILTLFGLLPVATNISTWWNFGSMLLTCLMLQVLTGFFLAVHYTANINLAFSSIIHITRDVPYGWLMQNLHAIGASMFFICIYIHIARGLYYGSHLNKETWMSGITLLITLIATAFFGYVLPGGQMSFRAATGITNLLTAVPYLGATMTTWLWGGFAINDPTLTRFFALHFILPFAIISLSSLHIILLHEEGSSNPLGTNPDIDKIPFHPYHSYKDLLLLTLMLLTLMITVSFFPDIFNDPDNFSKANPLVTPQHIKPEWYFLFAYGILRSIPNKLGGALALVMSIMILLTAPLTHTAHLRPMTFRPLSQLMFWTLISTFITITWAATKPVEPPYIIISQTTATLYFTFFISTPILGWIENKMMNSC
Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
O48109
Q6X4A2
CIPKV_ORYSJ
OsCIPK31
Oryza sativa
MYRAKRAALSPKVKRRVGKYELGRTIGEGTFAKVRFAKNTENDEPVAIKILDKEKVQKHRLVEQIRREICTMKLVKHPNVVRLFEVMGSKARIFIVLEYVTGGELFEIIATNGRLKEEEARKYFQQLINAVDYCHSRGVYHRDLKLENLLLDASGNLKVSDFGLSALTEQVKADGLLHTTCGTPNYVAPEVIEDRGYDGAAADIWSCGVILYVLLAGFLPFEDDNIIALYKKISEAQFTCPSWFSTGAKKLITRILDPNPTTRITISQILEDPWFKKGYKPPVFDEKYETSFDDVDAAFGDSEDRHVKEETEDQPTSMNAFELISLNQALNLDNLFEAKKEYKRETRFTSQCPPKEIITKIEEAAKPLGFDIQKKNYKMRMENLKAGRKGNLNVATEVFQVAPSLHVVELKKAKGDTLEFQKFYRTLSTQLKDVVWKCDGEVEGNGAAA
Involved in cold stress tolerance. CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner.
Q6X4A2
Q0SXQ7
UBIA_SHIF8
4-HB polyprenyltransferase
Shigella
MEWSLTQNKLLAFHRLMRTDKPIGALLLLWPTLWALWVATPGVPQLWILAVFVAGVWLMRAAGCVVNDYADRKFDGHVKRTANRPLPSGAVTEKEARALFVVLVLISFLLVLTLNTMTILLSIAALALAWVYPFMKRYTHLPQVVLGAAFGWSIPMAFAAVSESVPLSCWLMFLANILWAVAYDTQYAMVDRDDDVKIGIKSTAILFGQYDKLIIGILQIGVLALMAIIGELNGLGWGYYWSIVVAGALFVYQQKLIANREREACFKAFMNNNYVGLVLFLGLAMSYWHF
Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 3-octaprenyl-4-hydroxybenzoate.
Q0SXQ7
Q6MC72
AMPA_PARUW
Leucyl aminopeptidase
Candidatus Protochlamydia
MEFALTLHIEKRKKADVLVLPFWKGTSQPEAAIALHPLKLSLDSVFNTGDFKGKEGETLFLYVEGLVEMRVALLGLGEKNKVSTEALRKSYGCLAKACLGKKLKTLNILMPEFNKTEEDAFIKAITEGLLLPNYVYDRLKSKQEEDDEVTLLQKINFISSNKHVLALAEEVAAICDGVYYTRDLINGNADEITPQYLAKCAQGLSQEYPQIKTTVFDKKRLEKEQMGLLLAVNRGSNLDPTLIIMEYKGNPKSKDHTVIIGKGVTYDTGGLNIKPTGGIETMKCDMSGGAACFGTMLAACHLDLKVNLTAIIPATENSVDAASFKPGDVYRSYLGKTVEMTNSDAEGRLILADALAYASQNLKPSRLIDIATLTGAIEISLGSEASGLMSTDDQLAKSLIQAGENTHERLWRMPLYEGYQEKLKSDIADLKSWNGRSGSSCVAAMFLKNFVGKDIPWAHLDIAGTAYVTEPKKYMPKYASGVGVRLLVEFLKQLSMVKN
Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
Q6MC72
B1JT65
RIMO_BURCC
Ribosome maturation factor RimO
Burkholderia cepacia complex
MSQSPKVGFVSLGCPKALVDSEQIITQLRAEGYEISGSYDGADLVVVNTCGFIDEAVQESLDAIGEALTENGKVIVTGCLGAKSSASGSNLIEEVHPKVLAVTGPHAVGEVMQAVHSHLPKPHDPFVDLVPAAGIKLTPRHYAYLKISEGCNHRCTFCIIPSMRGDLVSRPVAEVMLEAENLFKSGVKELLVISQDTSAYGVDVKYRTGFWNGKPIKTRMTDLVAALGELAAQYGAWVRLHYVYPYPSVDEVIPLMAEGPFKGHVLPYLDVPFQHAHPEVLKRMKRPANAEKVLERVQKWREICPDLTIRSTFIAGFPGETEEQFETLLDFIREAELDRVGCFAYSPVEGATANDLDGALPDEVREERRARFMEVAEEVSANRMQRKIGKTLKVLIDEVSAEGGIGRTAADAPEIDGVVYVEPAAKASKRYKVGDFVSVKITGADGHDLWGEV
Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12.
B1JT65
Q8RGE1
ATPG_FUSNN
F-ATPase gamma subunit
Fusobacterium
MPGMKEIKSRIKSVQSTRQITNAMEIVSTTKFKRYSKLVTESRPYEESMRKILGNIASGVKNEGHPLFDGRKEVKSIAIIVITSDRGLCGSFNSSTLKELEKLVEKNKNKNITIIPFGRKAIDFITKRNYEFSESFSKISPDEMNKIAGEISEEVVEKYNNHIYDEVYVIYNKFISALRYDLTCERIIPITRPEVELNSEYIFEPSTEYILSALLPRFINLQIYQAILNNTASEHSARKNSMSSATDNADEMIKTLNIKYNRNRQSAITQEITEIVGGASAL
Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
Q8RGE1
Q9Y3Y2
CHTOP_HUMAN
Small arginine- and glycine-rich protein
Homo
MAAQSAPKVVLKSTTKMSLNERFTNMLKNKQPTPVNIRASMQQQQQLASARNRRLAQQMENRPSVQAALKLKQSLKQRLGKSNIQARLGRPIGALARGAIGGRGLPIIQRGLPRGGLRGGRATRTLLRGGMSLRGQNLLRGGRAVAPRMGLRRGGVRGRGGPGRGGLGRGAMGRGGIGGRGRGMIGRGRGGFGGRGRGRGRGRGALARPVLTKEQLDNQLDAYMSKTKGHLDAELDAYMAQTDPETND
Required for effective mRNA nuclear export and is a component of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NFX1 pathway. The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production. Stimulates DDX39B ATPase and helicase activities. In cooperation with ALYREF/THOC4 enhances NXF1 RNA binding activity .
Q9Y3Y2
Q471H6
HUTG_CUPPJ
Formiminoglutamate hydrolase
Cupriavidus
MRMAVTQNPWQGRVDSGEVGDTTRLFRIVNTLESSEAKTLGGSPVLLGFGCDAGVLRNQGRAGAAHGPDAIRQALANVPAHGLPALYDAGNIACEHGDLESAQLALAGSVHNILSRGGFPLVLGGGHEVAWGTWQGLRAHLDARNDDGRLLIINIDAHFDLRTSRPASSGTPFDQIANACAERGQPFDYVCLGVSRLSNTPALFSRAHALGVSYVEDVDMQERHLASRLAELAARIDATDHVYLTIDLDALPATVMPGVSAPAAYGVPLPVVEEIALLARRSGKLRAADLAEYNPQYDRDNLGARVAARLAWRLLG
Catalyzes the conversion of N-formimidoyl-L-glutamate to L-glutamate and formamide.
Q471H6
B8J823
SYT_ANAD2
Threonyl-tRNA synthetase
Anaeromyxobacter
MSDLVKVTLPDGSQKEAPRGTPVIDFVKGQIGPGLAKAAYFARLDGEPVDLSRAIERDARLEIVTTRNPEALEVARHDAAHVMASVVQKLYPGTQVTIGPAIEDGFYYDFARETPFTPEDLERIEKATNEAIKADLPFVRSEISMEAALALFEGMGERYKVEIVKDIAAKGAKTLTLYKHGDWVDFCLGPHGPSTGRIGVVKLLNVAGAYWRGDAKNAMLQRIYGTAFFDKKELDAHLAKLEEVKKRDHRRLGPQLGLFTFHEFAPGAPFWLPAGTVLYNVLEDAMRRLVLKNGYQEVKTPLLFNKRLWETSGHWGKYRENMFLVVDSESDPALPLEDRCSFSLKPMNCPSHHLIYRMDKRSYRELPVRYFTTDALHRNEASGSLGGLTRVRQFEQDDAHIYLREEQVTDEVLRIFELMKVVYGAFGLGFEATFSTRPEQRIGDDALWDRAEALLRKSLDATGLKWTLNAGDGAFYGPKIDMLVTDSLGRKWQTCTIQLDYAAPERFDLTFVGEDNKEHRPVVIHRAIYGSFERFVAILVEHYAGAFPAWLAPVQARVVTVSDRFEAWAREAGEALQARGWRVEVDASSDKLGAKIRNAQLAKIPFTLVVGEKEVEAKGVSPRRHGGEDLKTMPLETFAELMAREATAPF
Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr).
B8J823
A6SX19
EFP_JANMA
Elongation factor P
Janthinobacterium
MKPAKEIRVGNIIMVDSKPMIVLRSDVNGSSRTGFTYKWKMKNLLTNTPMENVFRGDDKFDVVVLDKKPVTYSYFADPLYVFMDEEYNQYEIEEENLGDALHYLKDGMECEAVFYDGKAISVELPITIARQVVYSEPAVKGNTSGNVLKEAKIENAVEAHRHTVQVPLFVSQDDVIEIDTRTNEYKRVVRN
Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
A6SX19
A9M0D4
RUVC_NEIM0
Holliday junction resolvase RuvC
Neisseria
MAASVRILGIDPGSRVTGFGVIDVRGRDHFYVASGCIKTPADAPLADRIAVIVRHIGEVVAVYKPQQAAVEQVFVNVNPASTLMLGQARGAALAALVSHKLPVSEYTALQVKQAVVGKGKAAKEQVQHMVVQMLGLSGTPQADAADGLAVALTHALRNHGLASRLNPSGMQVKRGRFQ
Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group.
A9M0D4
Q9QZL9
DKKL1_MOUSE
Protein soggy-1
Mus
MCRLRVLLLLLPLAFVSSSALPIHDVDSQQNTSGFLGLQRLLQSFSRLFLKNDLLRDLDNFFSSPMDFRDLPRNFHQEENQEHRMGNHTLSSHLQIDKVTDNQTGEVLISEKVEASIEPERNPEGDWKVPKVEAKEPPVPVQKVTDSLHPEPRQVAFWIMKMPRRRTQPDVQDGGRWLIEKRHRMQAIRDGLRGGAREDSLEDGVHIPQHAKLPVRKTHFLYILRPSQQL
Involved in fertilization by facilitating sperm penetration of the zona pellucida . May promote spermatocyte apoptosis, thereby limiting sperm production. In adults, may reduce testosterone synthesis in Leydig cells . Is not essential either for development or fertility .
Q9QZL9
Q7WI95
IXTPA_BORBR
Nucleoside-triphosphate pyrophosphatase
Bordetella
MSAEILNPNLRRVVLASNNAGKLREFSALFAPLGIELVPQSELGVSEAEEPHATFVENALAKARHASRHTGLPALADDSGLCVVALGGAPGVHSARYAQQPGGARSDAANNALLVRELAAAGDRRAWYVALLALVRTENDPCPLIGEGLWHGEIVDAPAGEHGFGYDPHFYLPQQGCTAAQLAPEHKNRISHRAQALAQLLDKLRATGPVDRP
Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
Q7WI95
Q1QDK7
SYP_PSYCK
Prolyl-tRNA synthetase
Psychrobacter
MKASQFLFATLKETPSDADIASSQLMVRAGLIRKIASGLYIWLPMGLRVLQKVERIVREEMQNIGAQEVLMPMTQPAELWQLTGRFNDYGPELLRFKDRHDRDFVLGPTHEEVITNLAQGELRSYKQLPITFFQIQNKFRDEIRPRFGVMRAREFTMKDAYSFHVDQASLAKTYDEMYDAYTRIFTRLGLDFRAVQADTGSIGGFASHEFHVLADSGEDDIAFSDSSEYAANVELAESVSMAERQPATMARENIDTVNMPTCEAVAEHLNVPLATTVKTLIVQGHTPEGEPQLIAVVLRGDHTLNTIKAEKIEEANVPLMMATEEELKAAGLHKGYIGVELNMPVFVDRAAAALSDFVSGANEINKHTTGMNWERDAHITRIVDIRNVHEGDPSPDGKGTLQIKRGIEVGHIFQLGDKYSQAMNCTVSGEDGKPVTLMMGCYGIGVSRIIAAAIEQNNDENGIMWPSTPDISDSLAPFEVAIVPMKSKEDTVMETATALYEELKALGINVLLDDRNERPGVKFADLELIGIPHRIVVSDRNLAEDKYEYVNRRDSEKQLLSRDEVIAKVSGK
Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS.
Q1QDK7
P62590
INT2_ECOLX
E2 protein
Escherichia
MKTATAPLPPLRSVKVLDQLRERIRYLHYSLRTEQAYVHWVRAFIRFHGVRHPATLGSSEVEAFLSWLANERKVSVSTHRQALAALLFFYGKVLCTDLPWLQEIGRPRPSRRLPVVLTPDEVVRILGFLEGEHRLFAQLLYGTGMRISEGLQLRVKDLDFDHGTIIVREGKGSKDRALMLPESLAPSLREQLSRARAWWLKDQAEGRSGVALPDALERKYPRAGHSWPWFWVFAQHTHSTDPRSGVVRRHHMYDQTFQRAFKRAVEQAGITKPATPHTLRHSFATALLRSGYDIRTVQDLLGHSDVSTTMIYTHVLKVGGAGVRSPLDALPPLTSER
Putative integrase believed to be involved in the insertion of antibiotic resistance genes into plasmids and transposons.
P62590
E3PQQ8
CCAP_CONVL
ConoCAP-c
Dauciconus
MVSLGHVLFVILLPVLLPVAADDPDDQMLSQISLPSSSRSEYDDNDVSKRVFCNGFTGCGGRHRDRSRRQERYGKRLIPVLAKRPFCNSFGCYNGKRSLSGAGPALSTPVDPSRNNKARTMARMLDAAASARHEQQQQLLQQREQRGLESRDPAASGDLSKRLFCNGYGGCRGGKRTLYSPWLERMNEVADDRSARNALCTRLGWRE
Synthetic conoCAP-c decreases the heart frequency of 12% in Drosophila larvae.
E3PQQ8
Q8LPS1
LACS6_ARATH
Long chain acyl-CoA synthetase 6, peroxisomal
Arabidopsis
MDSSSSSSSAAARRRINAIHSHLVTSSRSSPLLRSNPTAGEFCLDNGYSVVLPEKLNTGSWNVYRSAKSPFKLVSRFPDHPDIATLHDNFEHAVHDFRDYKYLGTRVRVDGTVGDYKWMTYGEAGTARTALGSGLVHHGIPMGSSVGIYFINRPEWLIVDHACSSYSYVSVPLYDTLGPDAVKFIVNHATVQAIFCVAETLNSLLSCLSEMPSVRLVVVVGGLIESLPSLPSSSGVKVVSYSVLLNQGRSNPQRFFPPKPDDVATICYTSGTTGTPKGVVLTHANLIANVAGSSFSVKFFSSDVYISYLPLAHIYERANQILTVYFGVAVGFYQGDNMKLLDDLAALRPTVFSSVPRLYNRIYAGIINAVKTSGGLKERLFNAAYNAKKQALLNGKSASPIWDRLVFNKIKDRLGGRVRFMTSGASPLSPEVMEFLKVCFGGRVTEGYGMTETSCVISGMDEGDNLTGHVGSPNPACEVKLVDVPEMNYTSADQPHPRGEICVRGPIIFTGYYKDEIQTKEVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYAKCKFVGQCFIYGDSFNSSLVAVVSVDPDVLKSWAASEGIKGGDLRELCNNPRVKAAVLSDMDTVGREAQLRGFEFAKAVTLVLEPFTLENGLLTPTFKIKRPQAKEYFAEAITNMYKELGASDPSANRGL
Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation (Probable). Preferentially uses palmitate, palmitoleate, oleate, linoleate and eicosenoate as substrates . Can use myristate and linolenate as substrates . May play a regulatory role both in fatty acid import into glyoxysomes and in fatty acid beta-oxidation . Functions redundantly with LACS7 in lipid mobilization for beta-oxidation during seed germination, which is essential for postgerminative growth and seedling establishment .
Q8LPS1
Q6MPX9
MACB_BDEBA
Macrolide export ATP-binding/permease protein MacB
Bdellovibrio
MIDIKGIRKSYQMGDTKVDVLKGISLKIERGDFVAIMGPSGSGKSTLMHILGLLDVPSEGSYNLNGREVADLSEDELAIVRREEIGFIFQQFNLLPRMEAWQNVSLPLIYSEDGFSYDKAQALLDKVGLAERIHHKSNELSGGQQQRIAIARSLINNPRIIFADEPTGNLDSKSEKEIIQILHKLNDQGITVIVVTHEEEIGQQAKRLIRLRDGVIQSDERLQALPAAPTTAQEKRQEKTAKWPVREMIEHLHQGFQTLAANKVRSGLSMLGILIGVAAVVGMLALGTGARQSIEKQLSSLGSNLLVLRAGNVRVGGVMQESGVRIRISLDDVSTIKNQISGIKDVSPSSSGRGQITYLNKNWNTQVMGVAPAYEQMRASTPIFGRFFSEEENQRRTLVAVIGTTVARELFGEKSPIGEMIKINKVNFRVIGVLPEKGAAGPQDQDDRILVPVVTAMYRLFGRNYVDSVDIEVRDAADIPEVQDSLQELMNKRHRVPVSSQGDAFNVFNMADIQQALNSTSQTLSMLLASIAAISLVVGGIGIMNIMLVSVTERTKEIGLRKAIGARRRDILLQFLAESIVVSVCGGLLGIALGVGFSLLISKVLGWSTVVSAGSVILSFGFSALIGIVFGSYPASKASKLHPIEALRYE
Non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. Confers resistance against macrolides.
Q6MPX9
Q8WUH2
TGFA1_HUMAN
Transforming growth factor-beta receptor-associated protein 1
Homo
MMSIKAFTLVSAVERELLMGDKERVNIECVECCGRDLYVGTNDCFVYHFLLEERPVPAGPATFTATKQLQRHLGFKKPVNELRAASALNRLLVLCDNSISLVNMLNLEPVPSGARIKGAATFALNENPVSGDPFCVEVCIISVKRRTIQMFLVYEDRVQIVKEVSTAEQPLAVAVDGHFLCLALTTQYIIHNYSTGVSQDLFPYCSEERPPIVKRIGRQEFLLAGPGGLGMFATVAGISQRAPVHWSENVIGAAVSFPYVIALDDEFITVHSMLDQQQKQTLPFKEGHILQDFEGRVIVATSKGVYILVPLPLEKQIQDLLASRRVEEALVLAKGARRNIPKEKFQVMYRRILQQAGFIQFAQLQFLEAKELFRSGQLDVRELISLYPFLLPTSSSFTRSHPPLHEYADLNQLTQGDQEKMAKCKRFLMSYLNEVRSTEVANGYKEDIDTALLKLYAEADHDSLLDLLVTENFCLLTDSAAWLEKHKKYFALGLLYHYNNQDAAAVQLWVNIVNGDVQDSTRSDLYEYIVDFLTYCLDEELVWAYADWVLQKSEEVGVQVFTKRPLDEQQKNSFNPDDIINCLKKYPKALVKYLEHLVIDKRLQKEEYHTHLAVLYLEEVLLQRASASGKGAEATETQAKLRRLLQKSDLYRVHFLLERLQGAGLPMESAILHGKLGEHEKALHILVHELQDFAAAEDYCLWCSEGRDPPHRQQLFHTLLAIYLHAGPTAHELAVAAVDLLNRHATEFDAAQVLQMLPDTWSVQLLCPFLMGAMRDSIHARRTMQVALGLARSENLIYTYDKMKLKGSSIQLSDKKLCQICQNPFCEPVFVRYPNGGLVHTHCAASRHTNPSSSSPGTRT
Plays a role in vesicle-mediated protein trafficking of the endocytic membrane transport pathway. Believed to act as a component of the putative CORVET endosomal tethering complexes which is proposed to be involved in the Rab5-to-Rab7 endosome conversion probably implicating MON1A/B, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion. The CORVET complex is proposed to function as a Rab5 effector to mediate early endosome fusion probably in specific endosome subpopulations . Functions predominantly in APPL1-containing endosomes and in degradative but not recycling trafficking of endocytosed cargo .
Q8WUH2
A8ESU8
RL22_ALIB4
50S ribosomal protein L22
Aliarcobacter
MAKAILKFIRVSPIKARLIAREVQGMNAEYAIASLQFTPNKAAGIISKVIASAVANAGLDPVDAVITSARVDKGPVLKRFTPRARGSASPKHKPTAHIMIEVAAATKGDK
The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome.
A8ESU8
Q2S919
RL16_HAHCH
50S ribosomal protein L16
Hahella
MLQPKRTKFRKVHKGRNTGLAQRGNKVSFGEFGLKATGRGRITARQIEAARRTMTRRIKRGGKIWIRIFPDKPITKKPLEVRMGKGKGPVEYWVAEIEPGRMLYEMEGVSEELAREAFTLAAAKLPVATTFVTRTVM
Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs.
Q2S919
Q4AAV4
OBG_MESHJ
GTP-binding protein Obg
Mesomycoplasma
MRFVDYVSIEVVAGKGGDGIISFRREAHVDKGGPDGGDGGWGGSIYFVGDSGMNTLLPFYQTKKIFGYNGENGRPKRQTGANGKDIFIKVPLGTQVFLKKSLICDIILEKKYLIAKGGRGGLGNFHFRNSKNKAPRISENGELGQNFYLDLQLKVMADIGLVGKPNAGKSTLLSLISNSKPKIANYEFTTLAPQLGVVKIYENSFVTADLPGLIQGASSGKGMGIIFLKHIERCRAIVHVIDFGSDNKNPIKDFIEIKSELEKFNKKLLDLNQIVIANKCDLPNFQFNLANFKRKFPKIKIIKSSLISAKQNEINIIKEKMFGLLGEKQKKLEIQEINTSKIEFNLKAPFLIKSRNNGFFEITGELIQKIIQKIPLNSQENILRFNAKVKKIGLWDELIKKGIKPGDLVRIYEFEFHWN
An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control.
Q4AAV4
P49765
VEGFB_HUMAN
VEGF-related factor
Homo
MSPLLRRLLLAALLQLAPAQAPVSQPDAPGHQRKVVSWIDVYTRATCQPREVVVPLTVELMGTVAKQLVPSCVTVQRCGGCCPDDGLECVPTGQHQVRMQILMIRYPSSQLGEMSLEEHSQCECRPKKKDSAVKPDRAATPHHRPQPRSVPGWDSAPGAPSPADITHPTPAPGPSAHAAPSTTSALTPGPAAAAADAAASSVAKGGA
Growth factor for endothelial cells. VEGF-B167 binds heparin and neuropilin-1 whereas the binding to neuropilin-1 of VEGF-B186 is regulated by proteolysis.
P49765
A7FLI9
DPO4_YERP3
DNA polymerase IV
Yersinia
MRKIIHVDMDCFFAAVEMRDDPRLRDIPLAIGGSKERRGVISTANYPARRYGVRSAMPTAMAFKLCPQLTLLPGRMAAYKEASQHIREIFARYTPLIEPLSLDEAYLDVSDSLACGGSATLIAQEIRQSIASELNLTASAGIAPIKFLAKIASELNKPNGQYVITPNQIQPFLQDLPLSKIPGVGAVTAKRLQALGLVTCGEIQKYPLAELLKHFGKFGRVLWERSHGIDEREISPDRLRKSVGVEKTLAEDIYDWESCEALIEELYLELETRLRKVKPDLHIARQGVKLKFHDFQQTTQEHTWPVLNKADLLQIAHAAWNERRAERGVRLVGLHVTLLDPQLERQLLLDWG
Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.
A7FLI9
Q9AP06
KATG_BURCE
Peroxidase/catalase
Burkholderia cepacia complex
MSNEGQCPFNHANGGGTTNRDWWPNELRLDLLSQHSSKTDPLDPGFNYAEAFNSLDLDALRKDLAALMTDSQDWWPADFGHYGPLFVRMAWHSAGTYRMGDGRGGAGRGQQRFAPLNSWPDNVSLDKARRLLWPIKQKYGQKISWADLLILTGDVALTTMGFKTFGYAGGREDTWEPDRDVYWGSETTWLGGDLRYDKGGACESQHGGNAGRNLENPLAAVQMDLIYNPEGGPDGNPDPVAAAYDIREVFGRMAMNDEETVALIAGGHAFGKTHGAGPADNVGLEPEAAGLEQQGLGWKNSFGTGKGADTITSGLEVTWSDTPTQWGMGFFKNLFGYEWELTKSPAGAHQWVAKNAEPTIPHAHDPSKKLLPTMLTTDLSLRFDPVYEKISRHFMDNPDVFADAFARAWFKLTHRDMGPRARYLGPDVPTEELIWQDPIPAVDHVLTTRNVAPLKETILASGLSVAELVSTAWASASTFRGSDKRGGANGARIRLAPQKDWAVNEPARLAKVLKVLERIQGEFNSTQPGGKKISLADLIVLAGGAGIEQAAKRAGHDVVVPFAPGRMDASQEQTDAHSFAVLEPVADGFRNFVKGKFAVPAEALLIDKAQLLTLTAPQMTALVGGLRVLNVQTGDEKHGVFTDQPETLTVDFFRNLLDMATEWKPIAGEDTYEGRDRRTGELKWTGTRVDLVFGSNAVLRALSEVYASADGEAKFIRDFVAAWVKVMNLDRFDLACKKRWYIDASGLPGEPALSARIQWR
Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Required for maintaining the normal activity of the TCA cycle.
Q9AP06
Q07V79
RBFA_RHOP5
Ribosome-binding factor A
Rhodopseudomonas
MPRHHQKNSGREASQRQLRVGESVRHAIAEILAQGGVHDPVLEGHLVTVPEVRMSPDLKLATIYVMPLGGRDTELVLKALDHNKKFLRGEVSRRVNLKFAPELRFRADDRFDEAERIEKLLRTPAVQRDLQHDSDESE
One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Associates with free 30S ribosomal subunits (but not with 30S subunits that are part of 70S ribosomes or polysomes). Required for efficient processing of 16S rRNA. May interact with the 5'-terminal helix region of 16S rRNA.
Q07V79
Q03614
NTDO_CAEEL
Sodium-dependent dopamine transporter
Caenorhabditis
MQLVPTDDPDEKIGRTSNGMQNATLPIDGPVNTEPKDPAREQWSGKLDFLLSVVGFAVDLGNIWRFPYLCFKNGGGVFLIPYSIMVLLTGVPLFYMELCLGQYYRKGAITTWGRICPLFKGIGYCVILTAFYVDFFYNVILAWGLHYLYTSFSFNLPWASCNNSYNSPACYEPHWSEDGTAMCRSANQSVSAEKISAAEEYFYKGFLGLHEANAPNSHVIRSVTDLGNVRWDIALSLFVVYLICYFSMWKGIHTSGKVVWFTALFPYVVLGILFIRGVTLPGWQNGIEYYLRPNFEMLKRPSVWQDAATQVFFSLGPGFGVLMAYSSYNDFHNNVYVDALFTSFINCATSFLSGFVIFSVLGYMSCKSGKPIEAVAQEGPGLVFVVYPEALSTMPYAPFWSVLFFLMLMTLGLDSSFGGSEAIITGLSDEFPILKKNREVFVGCLFAFYMVIGIAMCTEGGILIMEWLIIYGTTWGLLIAVFCEAMVIAYIYGLRQFVHDVKEMMGFRPGNYWKFCWSCAAPFILLSMITSNFINYQALTYQDYTYPTAANVIGIIFALSGASFIPLVGIYKFVNARGNTISEKWQRVTMPYRKRPNQTEYIPIPTTQPHSDIML
Dopamine transporter . Terminates the action of dopamine by its high affinity sodium-dependent reuptake into presynaptic terminals.
Q03614
Q9WUH7
SEM4G_MOUSE
Semaphorin-4G
Mus
MWGRLWPLLFSFLTVTAVPGPSLRRPSRELDATPRLTISYEELSQIRHFKGQTQNYSTLLLEEASERLLVGARGALFSLSARDIRDRTHKEIHWEASPEMQSKCHQKGKNNQTECFNHVRFLQRLNATHFYACGTHAFQPLCAAIDAETFILPTSFEEGKEKCPYDPARGFTGLIIDGGLYTATRYEFRSIPDIRRSRHPHSLRTEEAPMHWLNDAEFVFSVLVRESKTSAVGDDDKIYFFFMEREEGSSSFTQSRSSHRVARVARVCKGDLGGKKILQKKWTSFLKARLICHIPQYETLRGVCSLNADTSSHTHFYAVFTLTTQWKTLEASAICRYDLAEIQAVFTGPFMEYQDGARRWGRYEGGVPEPRPGSCITDSLRSRGYNSSQDLPSLVLDFVKLHPLMARPVVPTRGRPLLLKRNVRYTHLTGTHVSTPAGPTYDLLFLGTADGWIHKAVVLGSGMHIIEEIQVFREPQSVDNLVISPMQHSLYVGAASGVLQFPLSSCSRYQSCYDCILARDPYCGWDSSIHACMVATTVANRTELIQDIERGNRGCEGSRDAGPPPPLKTRSVLRGDDVLLPCDQPSNLARALWLLNGSKSLSDGQDGYRVGVDGLLVTDTQLEHSGNYGCYAEENGLRMLLASYSLTVRPATPAPAPQAPATPGAQLAHDMRMFYVVAIAILGGLCLILASSLLYVACLKGGRRGRRRKYSLGRAGRAGGSAVQLQTVSGQCPGEEDEGDDGEGTGGLESGCLQIIPGEGAPAPPPPPPPPPPAELTNGLVALPSRLRRMNGNSYVLLRQSNNGVPAGPCSFAEELSRILEKRKHTQLVEQLDESSV
Cell surface receptor for PLXNB2. May play a role in axon guidance.
Q9WUH7
P69929
TX9A_ANTMC
Peptide toxins Am-1
Antheopsis
MKRIFIVALLFATCLVNAKPSINDADIKREPEPNVAVPPCGDCYQQVGNTCVRVPSLCPSRKREPEPNVAVPPCGDCYQQVGNTCVRVPSLCPSRKREPEPNVAVPPCGDCYQQVGNTCVRVPSLCPSRKREPEPNVAVPPCGDCYQQVGNTCVRVPSLCPSRKREPEPNVAVPPCGDCYQQVGNTCVRVPSLCPSRKREPEPNVAVPPCGDCYQQVGNTCVRVPSLCPSRKR
May inhibit voltage-gated sodium channels (Nav).
P69929
B0C0B6
RECO_ACAM1
Recombination protein O
Acaryochloris
MSRTYKATGINLKSMPFGEADRLLTILTREQGLVRAVAPGCRKPKSKLGGRSALFVVNDLMLVQGRSLDKIAQAETLESYPGLSQNLAKLTTSQYLAELTLYQALSGQPQTELWDLFCQQLTQLQNATLAQVPCCLIHGTLKLLAGAGIAPQVHACCVTHQPLDPPTSNPTWRVGFSAGAGGTVTLTGPPRPRTAIQQAAEQAIAYPLGADYRVQGKLSAQELALLQDLNPAEIQPASPLPLPLIATYPLVIWQGVESALRHYAEAYFDRPIRSAALIDTCFTPLPDLTSVPS
Involved in DNA repair and RecF pathway recombination.
B0C0B6
B1YLP7
EFP_EXIS2
Elongation factor P
Exiguobacterium
MVSVNDLKTGLTIKTSDGMIWQVLEFQHVKPGKGAAFVRTKMRNIRNGNIQEMTFRGGERVERAHIERNKMQYLYPMGETYVFMDTESYEQLELTTAQVEAALPFLLENMEVQIAIYNGEVLGIELPNTIVMTIVEAEPGVKGDTASNVKKNATVETGHIIHVPLFIEAGEKVTVDTRTGDFTGRYNG
Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
B1YLP7
Q73X85
MURI_MYCPA
Glutamate racemase
Mycobacterium avium complex (MAC)
MSSALAPVGIFDSGVGGLTVARAIIDQLPDEHIIYVGDTGHGPYGPLSIPEVRAHALAIGDDLVGRGVKALVIACNTASAACLRDARERYEVPVVEVILPAVRRAVATTRNGRIGVIGTQATINSHAYQDAFAAARDTEITAVACPRFVDFVERGVTSGRQVLGLAEGYLEPLQRAQVDTLVLGCTHYPLLSGLIQLAMGDNVTLVSSAEETAKEVLRVLAERDLLHPHPDDPRAAGPSRVFEATGDPEAFTRLAARFLGPAVSGVRPVHHVRID
Provides the (R)-glutamate required for cell wall biosynthesis.
Q73X85
Q0HKG4
G1091_SHESM
Glycosyl hydrolase family 109 protein 1
Shewanella
MHNIHRRHFLKAAGAVTAGLVTANIALNANASSVAPKPRVGKSVIGLIAPKMELVRVGFIGVGERGFSHVEQFCHLEGVELKAICDTHQAVIDRAVEHIVNQNRPKPAVYTGNDLSYRELLNRDDIDIVIISTPWEWHAPMAIDTMESGKHAFVEVPLALTVEECWQLVDTAERTQKNCMMMENVNYGREELMVLNMVRQGVFGELLHGEAAYIHELRWQMKEIDHKTGSWRTYWHTKRNGNLYPTHGLGPISQYMNINRGDRFDYLTSMSSPALGRTLYAKREFPADHERNQLKYINGDMSTSLIKTVKGRTIMVQHDTTTPRPYSRHNLIQGTNGVFAGFPNRIAVEHGGFGKSYHEWDMDMQKWYDKYDHPLWQRIGKEAEINGGHGGMDFVMLWRMVYCLRNGEALDQDVYDGAAWSVVNILSEQSLNNRSNSVNFPDFTRGAWKHATPLGIVGA
Glycosidase.
Q0HKG4