accession
stringlengths 6
10
| name
stringlengths 6
11
| Full Name
stringlengths 1
147
⌀ | taxon
stringlengths 3
46
⌀ | sequence
stringlengths 16
2.75k
| function
stringlengths 6
5.51k
| AlphaFoldDB
stringlengths 6
10
|
|---|---|---|---|---|---|---|
Q2L058
|
RL21_BORA1
|
50S ribosomal protein L21
|
Bordetella
|
MYAVVKTGGKQYRVAAGEKLKVEQIPADIGQEITLDQVLSVGEGDQLKVGTPLVAGAVVKATVLAHGRHDKVKIFKMRRRKHYQKRQGHRQNYTEIRIEAITA
|
This protein binds to 23S rRNA in the presence of protein L20.
|
Q2L058
|
P72656
|
RNE_SYNY3
|
Ribonuclease E/G
|
unclassified Synechocystis
|
MPKQIVIAEKHQVAAVFWKDQIQELVVSTGSQQVGDIYLGLVDNILPSIDAAFINIGDTEKNGFIHVSDLGPVRLRRTAGSISELLSPQQRVLVQVMKEPTGNKGPRLTGNISMPGRYMVLMPYGRGVNLSRRINREEERSRLRALAVLIKPPGMGLLVRTEAEDVPEDAIIEDLENLQKQWELVQQQAMTRSAPMLLDRDDDFIKRVLRDMYSSEVNRIVVDTPAGMKRIKQQLMNWDQGRLPEGVLIDCHRESLSILEYFRVNATIREALKPRVDLPSGGYIIIEPTEALTVIDVNSGSFTHSANSRETVLWTNYEAATEIARQLKLRNIGGVIIIDFIDMDSHKDQLQLLEHFNRCLETDKARPQIAQLTELGLVELTRKRQGQNLYELFGQPCPECGGLGHLVELPGEKGFVSLSPTAVNSSIPPRLVEKPILSPPVAKVNDLPKKEEAKISSPLDLLFHPNYQEQGDRDSNRRRRRRRGSEFSEKENIKSVGISRSKGPSPSPTKEKVTGTAPPRRERPSRRVEKTLVPVDVAMTTLEQDIYARMGISPLIKTEYADQDPRSFMVSVVTAGAALEGNTNGSGSLVNAVITTVDNGDNGDNVPSDGLTIVSEVTAPTPVIEQPREETVEPEQVVLPQLDDETPAAPVAEESAPIETKKRPGRRRRRSSAE
|
CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Endogenous RNase E is required for correct processing of pre-crRNA for the CRISPR3 subtype III-B system in this genome (genes sll7080 to sll7095). This CRISPR3 system does not include a cas6 gene, which is the usual RNase involved in crRNA maturation.
|
P72656
|
Q9Z615
|
FENR_BUCAP
|
Flavodoxin--NADP reductase
|
Buchnera
|
MNPWINANVLKVHKWTQNLFSLILNAEIAPFQAGQFTKLALNEENINFSNNVKKKKIQRAYSFVNAPSNKNLEIYIVRILNGKLSNLLYNLKSGDNLFIKEKSFGFFTLDEIPNCKTLWMFATGTGIGPYCSILQEYKNINRFKNIILIHAVRYQNELTYLPLMKQLYKSYNGKLKIETIVSREKNHNSLYGRIPLLLQNQILEKKIGLKINRNDSHVMLCGNPAMVKDTYLFLQKDRCMQKNLRRKHGHITMENYW
|
Transports electrons between flavodoxin or ferredoxin and NADPH.
|
Q9Z615
|
B0UHX5
|
RPOC_METS4
|
Transcriptase subunit beta'
|
Methylobacterium
|
MNQEVMNLFNQQAQPQSFDQIKISISSPEKILSWSYGEIKKPETINYRTFKPERDGLFCARIFGPIKDYECLCGKYKRMKYKGVICEKCGVEVTLARVRRDRMGHIELAAPVAHIWFLKSLPSRIGLLLDMALKDLERILYFESYVVIEPGLTPLKERQLLSEEEYLRAQEEYGEDSFTAMIGAEAIRRILQDLNLEKIAADLRQEIATTTSDLKPKKLLKRLKIIEAFQLSGNKPEWMILTVVPVIPPDLRPLVPLDGGRFATSDLNDLYRRVINRNNRLKRLIELRAPDIIIRNEKRMLQEAVDALFDNGRRGRVITGANKRPLKSLADMLKGKQGRFRQNLLGKRVDYSGRSVIVVGPELKLHQCGLPKKMALELFKPFIYARLDAKGFSATVKQAKKLVEKEKPEVWDILDEVIREHPVMLNRAPTLHRLGIQAFEPKLIEGKAIQLHPLVCAAFNADFDGDQMAVHVPLSLEAQLEARVLMMSTNNILHPANGAPIIVPSQDIVLGLYYLSIVADGAPGEYKSNNPLNPMQGVYGDFGELEHALASRAVTLHSKVKWRWKGLGPDGEEVTRTYDTTPGRVILSSVLPRHPKVPFDVVNKLMTKKEISAMIDTVYRHCGQKESVIFCDRIMGLGFSHAFKAGISFGKDDMVVPENKWTIVDETRALVKDYEQQYQDGLITQGEKYNKVVDAWAKCSDRLASEMMNRISSVQKDEKGADKQVNSIYMMSHSGARGSPAQMKQLAAMRGLMAKPSGEIIESPIISNFKEGLDVLEYFNSTHGARKGLADTALKTANSGYLTRRLVDVAQDAVIREVDCGTDAGIRMRAIIDAGQVVATLATRILGRATAEDLVAQDGSIIVPKGQMIEERHLDAINKAGIQEVKIRSVLVCATKNGVCATCYGRDLARGTPVNQGEAVGVIAAQSIGEPGTQLTMRTFHIGGAAQIADSSFIESSFEGTVRIRNRGLARNSDGDLIAIGRNVAVVIVGPDGTERAVHRLQYGARVRVDEGDSIKRGQRIAEWDPYTRPILTEVDGIVAYEDLIDGQSITETTDESTGIAKRVVIDWRGSARTADLRPALAIHDQNGKVLKLPRGSDARALLPVEAIIGVDPGARVKAGDILARVSTESAKTRDITGGLPRVAELFEARRPKDAAIIAEKSGTISFGRDYKNKRRLSLTPHDGSEPVEYLIPKGKHIHLQDGDVVEVGDFIVDGNPAPHDILAIKGVEELAAYLVNEIQEVYRLQGVSINDKHIEVIVRQMLQKVEITDSGDSEILTGDQIDRTELQEINEQLVSEGKKPVQGVPVLLGITKASLQTRSFISAASFQETTRVLTEAAVNGKVDTLEGLKENVIVGSLIPAGTGAMIADIKSIARRRDELIMAQKTAESGAALQELPAAE
|
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
|
B0UHX5
|
Q1QSR9
|
TRMB_CHRSD
|
tRNA(m7G46)-methyltransferase
|
Chromohalobacter
|
MSDSSSSSENAPATPESPGRPPRGIKSYVLRAGRMTAAQSRGLEEVWPRLGLSVAEGRQSLEALFGRRAPCVVEVGFGMGQSLVEQAAANPETDFIGIEVHAPGVGKLLDEADKRGLTNLRVYRDDALEVLDKCLPESSLTGLQLFFPDPWPKKKHHKRRIVQPAFVELVRTRLAPHGYLHMATDWEAYAEHMVEVMEEAPGYRNTAPPESAPYVPRPEFRPLTKFESRGERLGHGVWDLIYARVE
|
Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
|
Q1QSR9
|
Q1QTJ9
|
HEM6_CHRSD
|
Oxygen-dependent coproporphyrinogen-III oxidase
|
Chromohalobacter
|
MAHPHLDKVKEYLLDLQDRLCDGLAAEEGDTAFREDSWTREAGGGGRSRVIENGEVFEKGGVNFSHVFGERLPASASAARPELAGRSFHAVGVSWVLHPRNPHVPTAHGNVRFFIAEKEGAEPVWWFGGGFDLTPFYPVFEDVVHWHRVAQETCAPFGDDVYPRFKRWCDEYFTLHHRDETRGVGGLFFDDLNEWEFERCFAFQRAVGDAFLEAYVPIVRRRQATEYGERERDFQAFRRGRYVEFNLVWDRGTLFGLQSGGRTESILMSMPPLAQWQYCWTPEPGSPEARLADEFLTPREWLEEAEA
|
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.
|
Q1QTJ9
|
Q48FA7
|
RIMO_PSE14
|
Ribosome maturation factor RimO
|
Pseudomonas
|
MSTVTTPSAPKVGFVSLGCPKALVDSERILTQLRMEGYEVVATYEDADVVVVNTCGFIDTAKAESLEVIGEAIKENGKVIVTGCMGVDANVIRDVHPSVLSVTGPQQYEQVVNAVHDVVPPRKDHNPLIDLVPPQGVKLTPRHYAYLKISEGCNHSCSFCIIPSMRGKLVSRPVGDVLDEAKRLVKSGVKELLVISQDTSAYGVDVKYRTGFWDGQPVKTRMTELCQALGSMGVWVRLHYVYPYPHVDELIPLMAAGKILPYLDIPFQHASPKILKLMKRPAFEDKTLARIKNWREQCPDLIIRSTFIVGFPGETEEDFQYLLDWLTEAQLDRVGCFQYSPVEGAPANLLDAAIVPDDVKQDRWDRFMAHQQAISAARLQMKIGKEIEVLIDEVDDRGAVGRCFFDAPEIDGNVFIGLEEGSTVQPGDKIMCRVTDADEYDLWAEML
|
Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12.
|
Q48FA7
|
Q8ZTE6
|
NTPTH_PYRAE
|
Nucleoside triphosphate phosphohydrolase
|
Pyrobaculum
|
MTWRERAELRIGISGMPGVGKTTLVLKIAELARSRVKVCGFVTVEVREGGTRIGFDVVDLANGRRMALARVGRGEPSVGKYVVNLEACNVISEALRRECDLKIIDEIGAMEFKCKNFGEDLQTALHTSPRVIATVHRNYIDIAKKLGLEIIWLTRENWGLVFRQLLIQLGLTQ
|
Has nucleotide phosphatase activity towards ATP, GTP, CTP, TTP and UTP. May hydrolyze nucleoside diphosphates with lower efficiency.
|
Q8ZTE6
|
A4GGA7
|
RPOC2_PHAVU
|
Plastid-encoded RNA polymerase subunit beta''
|
Phaseolus
|
MAERTNLMFHNKVIGGTAIKRLISRLIDHFGMAYTSHILDQVKTLGFRQATATSISLGIDDLLTIPSKGWLVRDAEHQNLILEKQHHYGNVHAVEKLRQSIEIWYATSEYFRQEMNPNFRMTDPFNPVHIMSFSGARGNASQVHQLVGMRGLMSDPQGQMIDLPIQSNLREGLSLTEYIISCYGARKGVVDTAVRTSDAGYLTRRLVEVVQHIVIRRTDCGTIRGISVNTQNEMMPESTWTQTLIGRVLADDIYRGSRCIAVRNQDIGIGLFNQFKTFQTQPISIRTPFTCRNTSWICRLCYGQSPTQGHLVELGEAVGIIAGQSIGEPGTQLTLRTFHTGGVFTGGTAEQVRAPYNGKIKFNEDLVHPTRTRHGHPAFLCYIDLYVSIENGDIIHNVTIPPKSFLLVQNNQYVKSEQVIAEILAGTYTFNFKEKVRKHVYSDLEGEMHWSTNVYHASEFKYSNVHILPKTSHLWILSGKSDRSGSVSFSTRKDQDQLNIHSLSTGERDICNHLASNNKIRHKLFHFNPSEKKERRISDYSIINQIICIDHCHFTHPAIFHDTTDLLAKRRRNRFIIPFQFQSIQERDKALMLASSISIEIPINGLFRRNSIFAYFDDPQYRTQSSGITKYRTIDINYILKKEDFVIEYPGVKEFKTKYQMKVDQFFFIPEEVYILPEFSSIMVRNNSIVEVDTPITVNIRSQVSGLVRLEKKKKKIQLKIFSGNIYFPGEMDKISRHSAMLIPPRTVKKNSKGSKKKMKNWIYAQWITITKKKYFVLVRPVILYEIADRIKLIKFFSQDMLQERDNLELQVINYILSGNGKSIRGISNTSIQLVRTCLVLNWDQDKKVSSIEKGHASFVELSINGLVRYFLKIALVKSHISYIRKRNDPSGSRFILDNESDWTNINPFFSMNSREKVQQSLSQNHGTIHMLLNRNDKCRSLIILSSSNCFQIRSFHDGKYYKEEMNPIQRDPLIPIKNSLGPLGIALQVANLDFYLLITHNQISINKNGQLDKLKETFQVFKYYLIDENERIYKPDISSNILLNPFYLNWHFFHHNSCEKKTFPIISLGQFICENVCIVQMKNAPHLKSGQILTVQMDSVGIRSANPYLATPGTTVHGHYGEILSEGDILVTFIYQKSRSGDITQGLPKVEQVLEVRSIDSISINLEKRVGTWNGRITRILGIPWGFFISAELTIAQSRISLVNQIQKVYRSQGVHIHNRHIEIIVRQITSKVLVSEDGMSNVFLPGELIGLLRAERAGRSLEESICYRVLLLGITKTSLNTQSFISEASFQETARVLSKAALRGRIDWLKGLKENVVLGGMMPVGTGFKRIIYRSKQRQYNKITSETKKRIDMIYQSNLGFKNS
|
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
|
A4GGA7
|
E0ZS47
|
UREG_ORYSI
|
Urease accessory protein G
|
Oryza sativa
|
MASHDHDHHHHHHHSHDDGDHHHSHHQDGSHGGGGGSWVGEDGRVWHSHDGLAPHSHEPIYSPGDFSKRAPPLISRRFAERAFTVGIGGPVGTGKTALMLALCRSLREKYSLAAVTNDIFTKEDGEFLIKHGALPEERIRAVETGGCPHAAIREDISINLGPLEELSNLYKADLLLCESGGDNLAANFSRELADYIIYIIDVSGGDKIPRKGGPGITQADLLIINKTDLAPAVGADLAVMERDALRMREGGPFVFAQVKHGVGVEEIVNHILQAWEIATGNKRR
|
Required for the maturation and activation of urease via the functional incorporation of the urease nickel metallocenter.
|
E0ZS47
|
Q3M5D2
|
RS20_TRIV2
|
30S ribosomal protein S20
|
Trichormus
|
MCANNKSALKRAQIAERNRVRNKTYKSSVKTLMKNYLSAVQAYAANPTPESKQEAQTRLAAAYSRIDKAVKRGILHPNNGARKKSRLASKLKPIEQTA
|
Binds directly to 16S ribosomal RNA.
|
Q3M5D2
|
Q09013
|
DMPK_HUMAN
|
Myotonic dystrophy protein kinase
|
Homo
|
MSAEVRLRRLQQLVLDPGFLGLEPLLDLLLGVHQELGASELAQDKYVADFLQWAEPIVVRLKEVRLQRDDFEILKVIGRGAFSEVAVVKMKQTGQVYAMKIMNKWDMLKRGEVSCFREERDVLVNGDRRWITQLHFAFQDENYLYLVMEYYVGGDLLTLLSKFGERIPAEMARFYLAEIVMAIDSVHRLGYVHRDIKPDNILLDRCGHIRLADFGSCLKLRADGTVRSLVAVGTPDYLSPEILQAVGGGPGTGSYGPECDWWALGVFAYEMFYGQTPFYADSTAETYGKIVHYKEHLSLPLVDEGVPEEARDFIQRLLCPPETRLGRGGAGDFRTHPFFFGLDWDGLRDSVPPFTPDFEGATDTCNFDLVEDGLTAMVSGGGETLSDIREGAPLGVHLPFVGYSYSCMALRDSEVPGPTPMELEAEQLLEPHVQAPSLEPSVSPQDETAEVAVPAAVPAAEAEAEVTLRELQEALEEEVLTRQSLSREMEAIRTDNQNFASQLREAEARNRDLEAHVRQLQERMELLQAEGATAVTGVPSPRATDPPSHLDGPPAVAVGQCPLVGPGPMHRRHLLLPARVPRPGLSEALSLLLFAVVLSRAAALGCIGLVAHAGQLTAVWRRPGAARAP
|
Non-receptor serine/threonine protein kinase which is necessary for the maintenance of skeletal muscle structure and function. May play a role in myocyte differentiation and survival by regulating the integrity of the nuclear envelope and the expression of muscle-specific genes. May also phosphorylate PPP1R12A and inhibit the myosin phosphatase activity to regulate myosin phosphorylation. Also critical to the modulation of cardiac contractility and to the maintenance of proper cardiac conduction activity probably through the regulation of cellular calcium homeostasis. Phosphorylates PLN, a regulator of calcium pumps and may regulate sarcoplasmic reticulum calcium uptake in myocytes. May also phosphorylate FXYD1/PLM which is able to induce chloride currents. May also play a role in synaptic plasticity.
|
Q09013
|
Q7NK24
|
CYSH_GLOVI
|
PAdoPS reductase
|
Gloeobacter
|
MNLLQDQPAMGIDQTTLEHLARQWEDLAPEAILAEAVRCFGDKLVLASAFGPESIILLDMLVKVWPRPQAFFLETGFHFPETLALKDRVLARFPQLQLEVVGPLMSVAQQNAIYGERLHDRNPDHCCAIRKVEPLNRALAPYKAWIAGMRREQSPTRGQIGVVQWDSRRGMVKFNPLATWTHKQVWAYIVERDLPYNPLHDEGFPSIGCSPLNCTAPVADGADPRSGRWRGKAKTECGLHA
|
Catalyzes the formation of sulfite from phosphoadenosine 5'-phosphosulfate (PAPS) using thioredoxin as an electron donor.
|
Q7NK24
|
A9KNK1
|
UPPP_LACP7
|
Undecaprenyl pyrophosphate phosphatase
|
Lachnospiraceae
|
MDFIELLKVIFLGIVEGITEWLPISSTGHLLLVDEFLKVNLSKDFMSMFNVVIQLGAILAVVVLFFKKLWPFSKEEKNFIKKDTFTLWFKIVVACIPGIVMIPFDSKIEDLFFNPQTIATTLILYGILFIIIENRNAGKQPKVAKLSDITYQMAFMIGLFQILAMIPGTSRSGATIIGAMLFGASRYVAAEFTFFLAIPTMFGASLLKLLKFGFTFTGAEIVALITGMLTAFIVSIIVIKFLMGYIKKNNFKVFGWYRIVLGAIVAGYFLLAR
|
Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
|
A9KNK1
|
P25066
|
P43_XENBO
|
Thesaurin-B
|
Xenopus
|
MQNVGPTEPSKSQVFRCPAAGCKAVYRKEGKLRDHMAGHSEQKLWKCGKKDCGKMFARKRQIQKHMKRHLTLKKHSCPTAGCKMTFSTKKSLSRHKLYKHGDAVPLKCSVPGCKRSFRKKRALRIHVSEHSNEPLSVCDVPGCGWKSTSAAKLAAHHRRHGGYRCSYEDCQTVSPTWTALQTHLKKHPLELQCAACKKPFKKASALRRHKATHAKNPLQLPCPRQDCDKIFSTVFNLTHHLRKVHLCLQTHRCPHSNCTRSFAMRESLVRHLVVHDPERKKLKLKFGRRPSKFLGRGTRCPTPVVEEDLSHLFSRKLLFHYKTRLETNLSGLFNERQLREPAEPEVNLSGLFQLPQGRPKAEKAA
|
p43 is a 5S RNA binding protein which is a major constituent of oocytes and comprises part of a 42S ribonucleoprotein storage particle.
|
P25066
|
Q3MAP6
|
Y2322_TRIV2
|
Nucleoid-associated protein Ava_2322
|
Trichormus
|
MTGKGQGFGFGLGKMKELAEAFKKAQQVQEGAKRLQEELEQMEILGEAGGGLVKVIVSGNQEPKRVEISPDALAQGADLLSDLVTAAMKDAYIKSTATMRERMEDLTSGLELPGF
|
Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection.
|
Q3MAP6
|
Q9H6K4
|
OPA3_HUMAN
|
Optic atrophy 3 protein
|
Homo
|
MVVGAFPMAKLLYLGIRQVSKPLANRIKEAARRSEFFKTYICLPPAQLYHWVEMRTKMRIMGFRGTVIKPLNEEAAAELGAELLGEATIFIVGGGCLVLEYWRHQAQQRHKEEEQRAAWNALRDEVGHLALALEALQAQVQAAPPQGALEELRTELQEVRAQLCNPGRSASHAVPASKK
|
May play some role in mitochondrial processes.
|
Q9H6K4
|
O57776
|
FTSZ1_PYRHO
|
Cell division protein FtsZ 1
|
Pyrococcus
|
MLKLVENVVERVSSEETKVQEVQVPQSSIDEELKKIVEQIKARIHVVGVGGAGCNTVNRMMEVGVTGAKIIAVNTDAQDLLKVKAHQKILIGKEITRGLGAGNDPKIGEEAAKESEREIREALEGADMVFVTCGLGGGTGTGAAPVIAEMARKMGALTVSVVTLPFTMEGIRRAKNAEYGLKRLAKASDTVIVIPNDKLLEVAPKLPIQMAFKVADEILVQAVKGITELITKPGLVNLDFNDVRAVMKDGGVAMIGIGESDSEKRALEAAEQALNSPLLDVDISGAKGALISISGADVKLEEAQQIIEYVTRNVDPKAQVIWGIQLEPELEKTIRVMVIVTGITSRYVTFQEETPAPSEEETTPVKIDIPEL
|
Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity.
|
O57776
|
Q576B4
|
NU5M_BOSIN
|
NADH dehydrogenase subunit 5
|
Bos
|
MNMFSSLSLVTLLLLTMPIMMMSLNTYKPSNYPLYVKTAISYAFITSMIPTMMFIHSGQELIISNWHWLTIQTLKLSLSFKMDYFSMMFTPVALFVTWSIMEFSMWYMHSDPNINKFFKYLLLFLITMLILVTANNLFQLFIGWEGVGIMSFLLIGWWYGRADANTAALQAVLYNRIGDIGFILAMAWFLTNLNTWDLQQIFMLNPSDSNMPLIGLALAATGKSAQFGLHPWLPSAMEGPTPVSALLHSSTMVVAGIFLLIRFYPLTENNKFIQSITLCLGAITTLFTAMCALTQNDIKKIIAFSTSSQLGLMMVTIGINQPYLAFLHICTHAFFKAMLFMCSGSIIHSLNDEQDIRKMGGLFKAMPFTTTALIVGSLALTGMPFLTGFYSKDLIIEAANTSYTNAWALLMTLIATSFTAIYSTRIIFFALLGQPRFPTLVSINENNPLLINSIKRLLIGSLFAGYIISNNIPPTTIPQMTMPYYLKTTALIVTILGFILALEISNMTKNLKYHYPSNAFKFSTLLGYFPTIMHRLAPYMNLSMSQKSASSLLDLIWLEAILPKTISLAQMKASTLVTNQKGLIKLYFLSFLITILISMMLFNFHE
|
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. Essential for the catalytic activity and assembly of complex I.
|
Q576B4
|
A3Q192
|
PSA_MYCSJ
|
Proteasome core protein PrcA
|
unclassified Mycobacterium
|
MSFPYFISPEQAMRERSELARKGIARGRSVVALAYADGVLFVAENPSRSLQKVSELYDRVGFAAVGRFNEFNNLRSGGIRFADTQGYAYSRRDVTGRQLANVYAQTLGTIFTEQAKPYEVELCVAEVAHFGESKAPELYRITYDGSIADEPHFVVMGGATEPIIAKLNDSYTENAELADAVRIAVDALESGGNGAERRTLGPSTLEVAILDANRPRRAFRRITGSALEALLPQRDAEASADAGAADKPAE
|
Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation.
|
A3Q192
|
Q87TS0
|
YIDD_PSESM
|
Putative membrane protein insertion efficiency factor
|
Pseudomonas
|
MRKLALVPIQFYRYAISPLMASHCRFYPSCSCYAYEAIDNHGLLRGGWLSIRRLGRCHPWNPGGYDPVPAVPTSRSSSMAE
|
Could be involved in insertion of integral membrane proteins into the membrane.
|
Q87TS0
|
P23572
|
CDK1_DROME
|
p34 protein kinase
|
Sophophora
|
MEDFEKIEKIGEGTYGVVYKGRNRLTGQIVAMKKIRLESDDEGVPSTAIREISLLKELKHENIVCLEDVLMEENRIYLIFEFLSMDLKKYMDSLPVDKHMESELVRSYLYQITSAILFCHRRRVLHRDLKPQNLLIDKSGLIKVADFGLGRSFGIPVRIYTHEIVTLWYRAPEVLLGSPRYSCPVDIWSIGCIFAEMATRKPLFQGDSEIDQLFRMFRILKTPTEDIWPGVTSLPDYKNTFPCWSTNQLTNQLKNLDANGIDLIQKMLIYDPVHRISAKDILEHPYFNGFQSGLVRN
|
Plays a key role in the control of the eukaryotic cell cycle . It is required in higher cells for entry into S-phase and mitosis . In embryos, promotes the release of Rif1 from chromatin during mid-blastula transition . p34 is a component of the kinase complex that phosphorylates the repetitive C-terminus of RNA polymerase II .
|
P23572
|
Q7LYX6
|
MALG_THELN
|
Trehalose/maltose transport system permease protein MalG
|
Thermococcus
|
MREEVLKRILLIIGAILMAIICLFPFIWMIVVSFAEDPTFLGSPLVEYKSTLENYVRVLSDPTLHFPAYLKNSIIIASLVTLTTVSISSLAAYAVSRIEFKGRLLIPIFVLGLSMFPQISLVGYLFKFIEKLGWVNTYQALYFPYVAWTLPLSLWILLSYFSQLPKDLDEAAMIDGASRIKTLTTIILPLSAPALFSTALLVFIAAFNEFMFALLFTTDHRARTVPVGIALFQGVHGEIPWGSVMAASVISTIPLVIMALLFQKYIVSGLTAGALKGE
|
Part of the ABC transporter complex MalEFGK involved in trehalose/maltose import. Responsible for the translocation of the substrate across the membrane.
|
Q7LYX6
|
Q39085
|
DIM_ARATH
|
Protein ENHANCED VERY-LOW-FLUENCE RESPONSE 1
|
Arabidopsis
|
MSDLQTPLVRPKRKKTWVDYFVKFRWIIVIFIVLPFSATFYFLIYLGDMWSESKSFEKRQKEHDENVKKVIKRLKGRDASKDGLVCTARKPWIAVGMRNVDYKRARHFEVDLGEFRNILEINKEKMTARVEPLVNMGQISRATVPMNLSLAVVAELDDLTVGGLINGYGIEGSSHIYGLFADTVEAYEIVLAGGELVRATRDNEYSDLYYAIPWSQGTLGLLVAAEIRLIKVKEYMRLTYIPVKGDLQALAQGYIDSFAPKDGDKSKIPDFVEGMVYNPTEGVMMVGTYASKEEAKKKGNKINNVGWWFKPWFYQHAQTALKKGQFVEYIPTREYYHRHTRCLYWEGKLILPFGDQFWFRYLLGWLMPPKVSLLKATQGEAIRNYYHDMHVIQDMLVPLYKVGDALEWVHREMEVYPIWLCPHKLFKQPIKGQIYPEPGFEYENRQGDTEDAQMYTDVGVYYAPGCVLRGEEFDGSEAVRRMEKWLIENHGFQPQYAVSELDEKSFWRMFNGELYEECRKKYRAIGTFMSVYYKSKKGRKTEKEVREAEQAHLETAYAEAD
|
Plays a critical role in the general process of plant cell elongation. Involved in the synthesis of campesterol, an early precursor of brassinolide. Required for the conversion of 24-methylenecholesterol to campesterol and for the conversion of isofucosterol to sitosterol. Necessary for both the isomerization and reduction of 24-methylenecholesterol. Regulates indirectly phytochrome-mediated light responses through the modulation of brassinosteroid biosynthesis.
|
Q39085
|
A0T0L2
|
PSAC_PHATC
|
PsaC
|
Phaeodactylum
|
MSHTVKIYDTCIGCTQCVRACPTDVLEMVPWDGCKAGQIASSPRVEDCVGCKRCETACPTDFLSVRVYLGAETTRSLGLAY
|
Apoprotein for the two 4Fe-4S centers FA and FB of photosystem I (PSI); essential for photochemical activity. FB is the terminal electron acceptor of PSI, donating electrons to ferredoxin. The C-terminus interacts with PsaA/B/D and helps assemble the protein into the PSI complex. Required for binding of PsaD and PsaE to PSI. PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn.
|
A0T0L2
|
Q1JS90
|
RN2VB_ODOVE
|
2VEb
|
Odorrana
|
MFTLKKSFLLLFFLGTITLSLCEEERGADDDDGEEEVKRGIMDTVKGVAKTVAASLLDKLKCKITGC
|
Antimicrobial peptide.
|
Q1JS90
|
Q980F0
|
MOAA_SACS2
|
Molybdenum cofactor biosynthesis protein A
|
Saccharolobus
|
MIDRFGRPLEDLRITLTHACNFECFFCHMEGEEGDNYLLSKEDILLVAKVARKFGINSVKLTGGEPTLRRDLVEIVRGLKQLGYEDVSMTTNGFLLKDLAHKLKLAGLDRINISLHAVSRDTFKKITGVDAFDRVIEGIKSAIDVGLVPVKLNFVVNRRNREEAFKFIELSQNLGVNEIHLIELHPVGLGKLAFKEHDDLREIEEYIEKISIKKLIRKKHFRPRYVLPSGLIVEVVKPYANPIFCAGCNRIRLSVDGKLKTCLYREDNVIDVLDILKGEYSEDVKEELLGRAFMIAIAIREPNFKYKI
|
Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate.
|
Q980F0
|
Q5QYI0
|
RPOZ_IDILO
|
Transcriptase subunit omega
|
Idiomarina
|
MARVTVEDAVDRVGNRFDLILLASRRARQLANGKEPLVETKNEKPTVIALREIEQGLIDNERLDIEDQAAQKQQDAEELRAVDALRGIE
|
Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
|
Q5QYI0
|
Q10357
|
CCS1_SCHPO
|
Superoxide dismutase 1 copper chaperone
|
Schizosaccharomyces
|
MFEVEYLIKDCDDVNKNTLEQEFQDLNIEDWKWDAATGQLIVKGSVSPSKVLRRLENATSKPILIRGASNKESGVSILYEANEDITQIPKVYGLCRFIPTEEKIFLDLIATQLLPNREYTGLVTISGDISRGLKSAGDSLVTLFNANSNEQGKIVLDKEVSGSLPNWIGHCFVLKCVDDSDSATMGIISRSAGLGQNTKQICACTGKSLWTEHAELKSVNEGSSCCSKKDSSPSEKPSCCSQEKKSCCSSKKPSCCSQEKKGCCSTEKTSCCSQEKKSCCTSEKPSCCSNGKSTVCA
|
Copper chaperone for superoxide dismutase 1 (sod1). Binds copper ions and delivers them specifically to sod1. Also has a role in cell protection against copper ion toxicity during conditions of copper excess. The C-terminal region is thought to act specifically in this sequestration role.
|
Q10357
|
Q30S45
|
EFP_SULDN
|
Elongation factor P
|
Sulfurimonas
|
MATIGMGDIKKNIRLIIGEVPCKVIEFQHVKPGKGAAFVRMKAKSFLNGRVFEKTVHAGDKFEVPEITFKTMQYLYDDGEQYQFMDNDSYEQIGLSYEQCDDASKWFKDGIQVDMIFYKGNAISVSAPEVMELLITDTPPNFKGDTSSGSKKPATLETGAVVQVPYHVLEGDTIRVNTVDCEYLEKVK
|
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.
|
Q30S45
|
Q8RGC8
|
FBPC_FUSNN
|
Fe(3+) ions import ATP-binding protein FbpC
|
Fusobacterium
|
MSVNIKIENAQKRYGDNIIIENLSLDIKQGEFFTLLGPSGCGKTTLLRMIAGFNSIEKGNFYFNEKRINDLDPAKRNIGMVFQNYAIFPHLTVEQNVEFGLKNRKVSKEEMKIEIDKFLKLMQIDEYKDRMPERLSGGQQQRVALARALVIKPDVLLMDEPLSNLDAKLRVEMRTAIKEIQNSIGITTVYVTHDQEEAMAVSDRIAVMKDGEIQHLGQPKDIYQRPANLFVATFIGKTNVLKGNLNGSILKVAGKYEVSLNNIKDKNIKGNVVISIRPEEFVIDENQTKDGMRAFIDSSVFLGLNTHYFAHLESGEKIEIVQESKIDSIIPKGAEVYLKVKQDKINVFTEDGSRNILEGVNNDAIGVAYVK
|
Part of the ABC transporter complex FbpABC involved in Fe(3+) ions import. Responsible for energy coupling to the transport system.
|
Q8RGC8
|
A5FS53
|
ISPE_DEHMB
|
4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase
|
Dehalococcoides
|
MLTLLAPAKVNLSLEVLYRRKDGYHELRSIIQSLSLCDRLSFSPSKTVHISSDSQDWQADLSLVSKAVELFSERCGQNTGVNLKIAKRIPLVSGLGGDSSCAAAVLKGLNKLWGCGYPCWRLMEIGAELGSDVPFFIMGGTAMMEGRGETVTPLPTLTQMWAVLLVPALDMPADKTAALYRNLRPDSFTSGEISDKLLESICQGKLSLSLCFNAFEKVAFELFPELVKYRWQFLEAGAYQISLAGAGPTLFTLLKDKNTAEKIYHNLCQKGHQAYLVSTLGPLD
|
Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
|
A5FS53
|
Q1GCN5
|
HSLV_RUEST
|
ATP-dependent protease subunit HslV
|
unclassified Ruegeria
|
MAEDQFPGWHGTTIIGVRKGDEVVVAGDGQVSLGQTVIKGSARKVRRLSPGGYDVVAGFAGSTADAFTLLERLEAKLEATPGQLQRASVELAKDWRTDKYLQKLEAMLIVTDGKDLYVITGAGDVLEPEHDVAAIGSGGNFALAAARGMMDSDRDAETVARDAMAIASDICVYTNGNLTVERIGK
|
Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
|
Q1GCN5
|
Q9ZDY3
|
ODO1_RICPR
|
Alpha-ketoglutarate dehydrogenase
|
typhus group
|
MEEYFNKTGYLFSGNAVFVEELYRQYLANPNSVDQTWQEFFADIKDNNVVLNKSTAKVISTNVTNKELLNNNLSSETLNNLKAKEMISAYRRNAHYLANLDPLGLEIRKTKNDLKLNIEAFGLDSSQLGENINIMDEFIGTWNCKLSELVTKLDKVYTSSIGVEFDQIENVEEKNWLYTKLETDITFTSEEKKSILNDLVEVECFEQFLHIKFPGAKRFSIEGGDASIVAMNKAIDLSMHQGVEEIVIGMAHRGRLNTLTKVVGKPYKEVIASFINGNIFPDGLNVSGDVKYHLGYSADRVRANQKIHLSLADNPSHLEAINSIVAGKVRAKQDIFVDTKRSKIKAILVHGDAAFCGQGVVAESLSMSPLTAYNVGGILHFVINNQLGFTANAADTRASRYSTEFAKIISAPILHVNGDDIEAVLKATDIAVEYRQKFSKDVVVEIICYRKYGHNEGDEPMYTQSKMYNIIKSKPTPGSIYANELVKNGIIDNNYYAKLKEKFKIRLDQEYEQAKSYKQETHFFEGYWKGISRIRGKDAITGVNKKILQDLGTKLCEIPKDFAINPKLIRLFEVRKTTLTTDQPIDWATAEQLAFAHLLCSGINIRLTGQDSARGTFSHRHSILHNQIDDTTYIPLNNLSKTQAKYEVANSNLSEYAALGFEYGYSLANPKNLVLWEAQFGDFANGAQIIFDQFISSSATKWLRMSGLVVLLPHAFEGQGPEHSSARLERFLQLAAEENMYITYPTTPASIFHLLRRQILESTRKPLIVMSPKSLLRHKYAVSKLDELGENTTFIPILDEVTKIDTNNVTKVILCSGKVYYDLFAMRTNNSNIVIIRLEQLYPFEKKLVASLLKKYNKAQAFIWCQEEPKNMGAWHYIATHLNDALKEAEINNEFKYVGREESASPAVGSLQVHNKQQEKLLMEALGDDIIKEKLY
|
E1 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the decarboxylation of 2-oxoglutarate, the first step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2).
|
Q9ZDY3
|
P53869
|
MRX7_YEAST
|
Mitochondrial organization of gene expression protein 7
|
Saccharomyces
|
MPPRSIEEWFYYKLLSSPGFHRFVRKVYRKVNGIKEDPFTDQSTAFQYLYKPTPRQKFKALRLLFWDEMRSTFGFRRRLGDRFKKD
|
Component of MIOREX complexes, large expressome-like assemblies of ribosomes with factors involved in all the steps of post-transcriptional gene expression.
|
P53869
|
Q0TLZ4
|
MNME_CLOP1
|
tRNA modification GTPase MnmE
|
Clostridium
|
MKEFDTIAAIATALGEGGIAIIRVSGNKALEIVNKIFRGINGKDLLDIKPYTMRYGHMIDENNEIIDEVIVSFMKGPRSFTAEDTVEINCHGGIVATNKVLQNVIKAGARLAEPGEFTKRAFLNGRIDLSQAEAVMDIITAKTELSMKSAMTQSQGRLSTEINNLRKEALDILALIEYAVDFTEDDEEPDETIPVKVKEDVITLRGKVNNLIDTADEGKLIRDGLSMVIVGKPNVGKSSLLNALLNEKRAIVTDIAGTTRDVIEEYINLDGIPVRLVDTAGIRETEDVVEKIGVEKSKEKINEADLVILMLDTSRELDEEDKEIIDYIKDRKYIVLLNKVDLDRKLSSEIVDNLENKIELSAKTGFGIDDLKSKIKDLFFNGSIDAESVMVTNTRHKEALYRASENLDGALNGLNNNEFLDLVSIYVTSALRALGEITGAELEEDLVNKIFAEFCCGK
|
Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
|
Q0TLZ4
|
A0KU20
|
TORD_SHESA
|
Chaperone protein TorD
|
Shewanella
|
MSNVDINHARALVYQLLSSLFAREIDEQRLKQLTSEQAQQFWTQLGYAPEFSASVASIQKVLNGLTSDEALLELAADYCGLFLVGTKHSASPYASLYLNREEEPLLFGQQHQQMSEFLHQSKLQVQSHFPEPADHLAVILAYMGHLACHSEDAAQLSFLNACIDSWLAKFVAKVVECDSKHSNGFYSALATLTLAWVQQDKQQLEQAMH
|
Involved in the biogenesis of TorA. Acts on TorA before the insertion of the molybdenum cofactor and, as a result, probably favors a conformation of the apoenzyme that is competent for acquiring the cofactor.
|
A0KU20
|
Q9F6B2
|
SLYA_EDWTA
|
Edwardsiella hemolysin activator
|
Edwardsiella
|
MESTLGSDLSRLVRVWRALIDQRLKPLELTQTHWVTLYNIHRLPPDQSQIQLAKAIGIEQPSLVRTLDQLEDKGLITRHICANDRRAKRIKLTDDAEPVIKEVTGVISLTRSEILDGISTDEIALLTNLVERLEQNIIHLQNK
|
Transcription regulator that can specifically activate or repress expression of target genes.
|
Q9F6B2
|
A4SG06
|
GCSPA_CHLPM
|
Glycine dehydrogenase (aminomethyl-transferring) subunit 1
|
Chlorobium
|
MPFIINTDSDRAEMLAAAGAASFNDLIADIPEEIRLKKSLDLAPALDEMAVRRQLESLAARNRSTAGYVSFLGGGAYDQFIPSAIRAIVSRSEFYTAYTPYQAEVSQGTLQAIYEYQSLICRLYGMDVANASMYDGATALAEAALMAMNVTGKERIVVAGQLHPWNSSVLSTYLGAAGHSPVVQNSVEEGVGSIASLRGMVDGTVAAVIVQQPNFYGCLEDVEAIGAIAREAGALFIVSADPHSLGVLEAPGAYGADIAVGEGQPLGSAQSFGGPYLGIFTVREKFVRKIPGRLVGMTKDRDGRDGFILTLQTREQHIRREKATSNICTNQALNALQAAVYLSLLGRQGMQEVAGQSLERAHYLAARIVEIPGYSLRFSAPFFREFVLNTPVHPAVIVERMLEEGIFAGIDLSVFGDEGLLVSVTEKRTKEEMDRFALLLSSF
|
The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
|
A4SG06
|
Q5PN95
|
SOTB_SALPA
|
Probable sugar efflux transporter
|
Salmonella
|
MTINPVSRKVAWLRVVTLAIAAFIFNTTEFVPVGLLSDIAESFHMQTAQVGIMLTIYAWVVAVMSLPFMLLTSQMERRKLLICLFVLFIASHVLSFLAWNFTVLVISRIGIAFAHAIFWSITASLAIRLAPAGKRAQALSLIATGTALAMVLGLPIGRVVGQYFGWRTTFFAIGMGALITLLCLIKLLPKLPSEHSGSLKSLPLLFRCPALMSLYVLTVVVVTAHYTAYSYIEPFVQNVAGLSANFATVLLLLLGGAGIIGSLVFGKLGNRHASSLVSIAIALLVVCLLLLLPAADSEAHLAILSIFWGIAIMVIGLGMQVKVLALAPDATDVAMALFSGIFNIGIGAGALVGNQVSLHWSMSAIGYIGAIPACAALVWAVLIFRKWPVTLEEQPH
|
Involved in the efflux of sugars. The physiological role may be the reduction of the intracellular concentration of toxic sugars or sugar metabolites.
|
Q5PN95
|
C6BYG6
|
MURG_MARSD
|
Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase
|
Maridesulfovibrio
|
MKRIVLTTGGTGGHVFPALAVAHEIKNRFPQCEILFIGGKGPEREMVERAGISFKGLPAKGVLGGGIKKVFSSLWIVSAMIMALKEIASFKPDAVIGFGGYAGFCPVLAAWLLGVPTAIHEQNSVPGVTNRILGKVVKRVFASFEDRNGSFPAAKTVVVGNPVRKEIIDSGNCADTKTVLVFGGSQGAAAINDAVIDGLAKLKEAGISLRHQTGKADFEKVRKGYEQNGMDTGKVSPFIHNMGEAYAEASLVVCRAGASTVFEVAAAGKPAIFIPFPHATHDHQTGNARSLADLGAAELIPQAELGGNRLADEIIKLIADQDRLKGMGSKALSFARTDAASAIAEGVGDIIRMKTVRGAA
|
Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
|
C6BYG6
|
B1ZNE4
|
RS19_OPITP
|
30S ribosomal protein S19
|
Opitutus
|
MSRSIKKGFFVDYHLLEKIEKANKAGAKKPIQTWSRRSTITPDFVGHTFSVHNGKAFIAVYVTENMVGHKLGEFALTRIFKAHGGMTRKEI
|
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
|
B1ZNE4
|
Q7Z417
|
NUFP2_HUMAN
|
Nuclear FMR1-interacting protein 2
|
Homo
|
MEEKPGQPQPQHHHSHHHPHHHPQQQQQQPHHHHHYYFYNHSHNHHHHHHHQQPHQYLQHGAEGSPKAQPKPLKHEQKHTLQQHQETPKKKTGYGELNGNAGEREISLKNLSSDEATNPISRVLNGNQQVVDTSLKQTVKANTFGKAGIKTKNFIQKNSMDKKNGKSYENKSGENQSVDKSDTIPIPNGVVTNNSGYITNGYMGKGADNDGSGSESGYTTPKKRKARRNSAKGCENLNIVQDKIMQQETSVPTLKQGLETFKPDYSEQKGNRVDGSKPIWKYETGPGGTSRGKPAVGDMLRKSSDSKPGVSSKKFDDRPKGKHASAVASKEDSWTLFKPPPVFPVDNSSAKIVPKISYASKVKENLNKTIQNSSVSPTSSSSSSSSTGETQTQSSSRLSQVPMSALKSVTSANFSNGPVLAGTDGNVYPPGGQPLLTTAANTLTPISSGTDSVLQDMSLTSAAVEQIKTSLFIYPSNMQTMLLSTAQVDLPSQTDQQNLGDIFQNQWGLSFINEPSAGPETVTGKSSEHKVMEVTFQGEYPATLVSQGAEIIPSGTEHPVFPKAYELEKRTSPQVLGSILKSGTTSESGALSLEPSHIGDLQKADTSSQGALVFLSKDYEIESQNPLASPTNTLLGSAKEQRYQRGLERNDSWGSFDLRAAIVYHTKEMESIWNLQKQDPKRIITYNEAMDSPDQ
|
Binds RNA.
|
Q7Z417
|
A2BPT4
|
CH601_PROMS
|
Chaperonin-60 1
|
Prochlorococcus
|
MAKQLNFSNESREALEKGVNFVANAVKVTIGPKAKNVVIEKKFGSPDIVRDGSTVAKEIEIENPIANLGAKLIEQVASKTKESAGDGTTTATILTQKMVQEGLKNIASGANPMELKKGMEAGLAFVLEKLSSKSISLSGSDIQKVATVSAGGDEEIGSIISKAMDIVTSDGVITVEESQSLETELDITEGMSFDRGYSSPYFVTDQERQVCELENPKILITDQKISTLVDLVPILEEIQKAGSPFLILAEDIEGEALTTLVLNKNSGVLNVASVRAPLFGERRKAALEDIAILTGAKLISEDKSMTLDKVSINDLGKAKKITITKDKTTIVAFEDTKDLVEARVEKLKREVNITESEYDQDKINERIAKLAGGVALIKVGAATETEMKYKKLRIEDSLNATKAAIEEGVVSGGGQTLIEISDDLLNLSETSSDDLRTGINIVKEALLEPTKQIAKNAGFNGDVVVAEIQRLNKGFNANSGQYEDLKDSGILDPTKVIRLALQDSVSIAAMLLTTEVAMADIPEPEAAAPGGPGGDPMGGMGGMGMPGMGGMGMPGMGGMGMPGMGGMGMPGMGGMGMPGMM
|
Together with its co-chaperonin GroES, 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.
|
A2BPT4
|
A7MGV2
|
NDK_CROS8
|
Nucleoside-2-P kinase
|
Cronobacter
|
MAIERTFSIIKPNAVAKNVIGSIFARFESAGFKIIGTKMLHLTVEQARGFYAEHEGKPFFDGLVEFMTSGPIVVSVLESENAVQRHRDLLGATNPANALAGTLRADYADSFTENGTHGSDSVESANREIAYFFGEGEICPRTR
|
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.
|
A7MGV2
|
P92671
|
CYB_OSPRO
|
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
|
Osphranter
|
MTNLRKSHPLIKIVNHSFIDLPAPSNISAWWNFGSLLGACLIIQILTGLFLAMHYTSDTLTAFSSVAHICRDVNYGWLIRNLHANGASMFFMCLFLHVGRGIYYGSYLYKETWNIGVILLLTVMATAFVGYVLPWGQMSFWGATVITNLLSAIPYVGTTLVEWIWGGFSVDKATLTRFFAFHFILPFIITALVLVHLLFLHETGSNNPSGINPDSDKIPFHPYYTIKDALGLMLMLFILLMLALFSPDMLGDPDNFSPANPLSTPPHIKPEWYFLFAYAILRSIPNKLGGVLALLASILILLIIPLLHTSKQRSLMFRPISQTLFWILTANLITLTWIGGQPVEQPFIIIGQLASISYFLLIIILMPLAGLFENYMLEPKW
|
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.
|
P92671
|
Q9UTP3
|
FTA6_SCHPO
|
Sim4-mal2-associated protein 6
|
Schizosaccharomyces
|
MEDKYILLSAVETFKSRLEELLMQSAKVQKQTMLRKELASSMNDMASTVQEALNKKKSS
|
Component of the kinetochore, a multiprotein complex that assembles on centromeric DNA and attaches chromosomes to spindle microtubules, mediating chromosome segregation and sister chromatid segregation during meiosis and mitosis. Component of the inner kinetochore constitutive centromere-associated network (CCAN), which serves as a structural platform for outer kinetochore assembly.
|
Q9UTP3
|
Q9PGI7
|
NUOI_XYLFA
|
NDH-1 subunit I
|
Xylella
|
MMNRVMHYFKSLLLLELLAGLWLTLKYTFRPKYTVLYPMEKFPQSPRFRGLHALRRYPNGEERCIACKLCEAVCPALAITIDSAKREDGTRRTTRYDIDLFKCIFCGFCEESCPVDSIVETHILEYHFEKRGENIVTKPQLLAIGDRFEAEIAERRAADAAFR
|
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
|
Q9PGI7
|
Q49YB7
|
NRDR_STAS1
|
Transcriptional repressor NrdR
|
Staphylococcus
|
MKCPKCNSTHSRVVDSRHADEVNAIRRRRECEECETRFTTFEHIEKRPLIVVKKDGTREQFLREKILNGLVRSCEKRPVRYEQLEDITNNVEWKLRDEGRAEISSREIGEHVMNLLMHVDQVSYVRFASVYKEFKDVDQLLQSMQGILAENKRSDS
|
Negatively regulates transcription of bacterial ribonucleotide reductase nrd genes and operons by binding to NrdR-boxes.
|
Q49YB7
|
A5FRX9
|
RS19_DEHMB
|
30S ribosomal protein S19
|
Dehalococcoides
|
MSRSVKKGPALCPKLMKKVEVASATNQKSIIKTWARWSTITPLMVGLNVGVHDGRRHVPIYITENMVGHKLGEFTTTRNFRGHAKAEKVSQVK
|
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
|
A5FRX9
|
O88508
|
DNM3A_MOUSE
|
DNA methyltransferase MmuIIIA
|
Mus
|
MPSSGPGDTSSSSLEREDDRKEGEEQEENRGKEERQEPSATARKVGRPGRKRKHPPVESSDTPKDPAVTTKSQPMAQDSGPSDLLPNGDLEKRSEPQPEEGSPAAGQKGGAPAEGEGTETPPEASRAVENGCCVTKEGRGASAGEGKEQKQTNIESMKMEGSRGRLRGGLGWESSLRQRPMPRLTFQAGDPYYISKRKRDEWLARWKREAEKKAKVIAVMNAVEENQASGESQKVEEASPPAVQQPTDPASPTVATTPEPVGGDAGDKNATKAADDEPEYEDGRGFGIGELVWGKLRGFSWWPGRIVSWWMTGRSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFCSAFHQATYNKQPMYRKAIYEVLQVASSRAGKLFPACHDSDESDSGKAVEVQNKQMIEWALGGFQPSGPKGLEPPEEEKNPYKEVYTDMWVEPEAAAYAPPPPAKKPRKSTTEKPKVKEIIDERTRERLVYEVRQKCRNIEDICISCGSLNVTLEHPLFIGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLLVGPGAAQAAIKEDPWNCYMCGHKGTYGLLRRREDWPSRLQMFFANNHDQEFDPPKVYPPVPAEKRKPIRVLSLFDGIATGLLVLKDLGIQVDRYIASEVCEDSITVGMVRHQGKIMYVGDVRSVTQKHIQEWGPFDLVIGGSPCNDLSIVNPARKGLYEGTGRLFFEFYRLLHDARPKEGDDRPFFWLFENVVAMGVSDKRDISRFLESNPVMIDAKEVSAAHRARYFWGNLPGMNRPLASTVNDKLELQECLEHGRIAKFSKVRTITTRSNSIKQGKDQHFPVFMNEKEDILWCTEMERVFGFPVHYTDVSNMSRLARQRLLGRSWSVPVIRHLFAPLKEYFACV
|
Required for genome-wide de novo methylation and is essential for the establishment of DNA methylation patterns during development . DNA methylation is coordinated with methylation of histones . It modifies DNA in a non-processive manner and also methylates non-CpG sites . May preferentially methylate DNA linker between 2 nucleosomal cores and is inhibited by histone H1 . Plays a role in paternal and maternal imprinting . Required for methylation of most imprinted loci in germ cells . Acts as a transcriptional corepressor for ZBTB18 . Recruited to trimethylated 'Lys-36' of histone H3 (H3K36me3) sites . Can actively repress transcription through the recruitment of HDAC activity . Also has weak auto-methylation activity on Cys-706 in absence of DNA .
|
O88508
|
C0ZY16
|
EFTS_RHOE4
|
Elongation factor Ts
|
Rhodococcus erythropolis group
|
MANYTAADVKRLRELTGSGMMACKNALADADGDFDKAVEQLRIKGAKDVGKRAERTTAEGLVVAKDGVMIEINCETDFVAKNDEFIKLADEIVTVAAAGKPADLDALKALELDGKTIDTVIAEQSAKIGEKLELSRVASFDGPVAVYLHKRSSDLPPAVGVLIEYTGEGDAAAEAARGAAMQVAALKAKYVTRDEVPAEIVASERHIAEETARAEGKPEQALPKIIEGRVNGFFKDVVLTEQSSVTDSKKTVKAILDEAGVTIKRFVRFEVGASA
|
Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.
|
C0ZY16
|
A3N2P2
|
LIPB_ACTP2
|
Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase
|
Actinobacillus
|
MNQLIVRQLGVQPYEEIWHQMQDFTDNRNENTADEIWLVQHPSVFTQGSAGKPEHLLNPTNIPVVQTDRGGQITYHGEGQQVMYVLIDIKRLKAQGKDVSVRDLVTALEQCVVKTLADYGIEGYPKPDAPGVYINGKKICSLGLRIRQGRSFHGLAFNVNMDLTPFRNINPCGYAGLEMTQLKDYIAESEAQCDLVSPKLVAHFYNILGYNAQQIINK
|
Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
|
A3N2P2
|
I1S163
|
FSL4_GIBZE
|
Fusarielin biosynthesis cluster protein 4
|
Fusarium
|
MSVIGLWLVTVTATLSLFVWQLIFLLSIPKSIVVCLIAESLFFVAWFFYWTVIYPRYLTPFRHLPTPASRSILTGNQNGLFTENSWDVARRVSQTVPNSGLIRYYVALSNERILVTNTRALSDVLTNHSHDFGKSNLAKFALKRLTGNGLGFLEGNEHKVHRKNLMPAFTRKHVKELTPIFWDKAMEMVKGMEAEVRCGKDTSTQGTGIVEIHDWATRATLDIIGTAGFGYDFGTLHNPSNEIGQQYKKMFLEPSTAFNWLELLGNYIDFRFLMTLPVKKNRDLTAGSNFMREIAKKVIRERRHELFQRMTSQAGNMKNTKKDIITTALASDCFTDDQLVDHVMAFLVAGHESTATAFEWAMYELGHRPEMQKRVRDEVRTYLPSPSAGGVKNITFESVPYLQAICNEVLRLYPFLPFATRVAEKDTWVADQFVPKGTIVAYAAHISNRDSELWSGPALDAFDPERWMEPGKESSGGANSNYAMLTFSAGPKSCIGEAWTRAELPCLVGAMVGSFEIELVEGKQADGTVYPTVDFKMGKVLKSRDGVFVRLRRLEDW
|
Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of fusarielins F, G and H, decaketide compounds with 5 methylations and a decaline core that act as mycoestrogens as they stimulate growth of MCF-7 breast cancer cells . The initial compound in the pathway is produced by the reducing polyketide synthase FSL1. FSL1 lacks an active enoyl reductase (ER) domain and biosynthesis of fusarielins relies on the trans-acting enoyl reductase FSL5, before it is released through hydrolysis catalyzed by the thioesterase FSL2 . Fusarielins F, G, and H have a C11=C12 cis double bond and is fully reduced between C10 and C11 and between C12 and C13. FSL3 can be involved in the formation of the C11=C12 cis double bond by moving a hypothetical C10=C11 or C12=C13 trans double bond to form prefusarielin . Prefusarielin is oxygenated at C15 and C16 by FSL4, resulting in fusarielin F, which subsequently is epoxidized into fusarielin G by the same enzyme . The final step in the pathway is a reduction of the carboxylic acid moiety to yield fusarielin H via a still undetermined mechanism .
|
I1S163
|
B5ZSI4
|
AROB_RHILW
|
3-dehydroquinate synthase
|
Rhizobium
|
MNAIPSASSVQTVHVPLGERAYDILIGPGLIARAGAEIASRLKGRKAAVVTDENVAPLYLQALVASLDEAGIASAAVVLPAGEKTKSFEHLMTACDKVLEARVERNDCVIALGGGVIGDLSGFAAGIVRRGVRFVQVPTSLLAQVDSSVGGKTGINSRHGKNLIGVFHQPDLVLADTDVLNTLSEREFRAGYAEVAKYGLIDKPDFFAWLEANWKAVFTGGAARIEAIAASCQAKADVVVADERENGPRALLNLGHTFGHALETATAYDSSRLVHGEGVSIGMVLAHEFSARMNLASPDDARRVERHLQEVGLPTRMSDIPGALPPAETLMDAIAQDKKVKSGKLTFILTRGIGQSFVADDVPASEVISFLREKHP
|
Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
|
B5ZSI4
|
A4JGH4
|
UPP_BURVG
|
UPRTase
|
Burkholderia cepacia complex
|
MKQDSRFPNLFILDHPLIQHKLTHMRDKDTSTRTFRELLREITLLMGYEITRNLPITTRRVATPLVEVDAPVIAGKKLAIVPVLRAGIGMSDGLLDLVPSARVGHIGVYRADDHRPVEYLVRLPDLEDRVFILCDPMVATGYSAVHAVDVLKRRNVPAANIVFVALVAAPEGVQVFQDAHPDVKLYVASLDSHLNEHAYIVPGLGDAGDRLFGTKN
|
Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
|
A4JGH4
|
Q87BT4
|
TYSY_XYLFT
|
Thymidylate synthase
|
Xylella
|
MKQYLELLNDVLVHGIKKPDRTGTGTRSVFGWQMRFDLSQGFPLVTTKKLHLRSIIHELLWFLRGETNIAYLKKHQVHIWDEWADATGELGPVYGKQWRRWAGADGHEIDQIRWLVEEIKRNPDSRRLVISAWNVADLPQMALVPCHALFQFYVANGKLSCQLYQRSADIFLGVPFNIASYALLTHMLAQVTGLVVGDFVHTLGDAHLYANHVEQASVQLGRVPRPQPVLRLNQAVTDLFDFTYDDIVIEGYDPYPAIKAPVAV
|
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.
|
Q87BT4
|
P48038
|
ACRO_RABIT
|
Acrosin heavy chain
|
Oryctolagus
|
MLPTAVLLVLVVSVVAKDNATCDGPCGLRFRQNPQGGFRVVGGQAAQQGAWPWMVSLQIFTPRNNRRYHACGGVLLNAHWVLTAAHCFNNKQKVYEWRMVFGAQEIEYGTDKPVRPPLQERYVEKVVTHDQYNYMTEGNDIALLKITPPVPCGPFIGPGCLPNSKAGPPKAAQTCYVAGWGYVKENAPRPSPTLMEARVDLINLELCNSTQWYNGRITASNLCAGYPSGKIDTCQGDSGGPLMCRENQGEPFVVQGITSWGVGCARAKRPGIYTATWPFLDWIASRIGSNALRMIQPATPTPPTTRSPGVHQPPSAHPPWYFQHASGPPHPHPHPHPHPHPRPPQPPAAQAPPPPPPPPPPPPPPPPPPPPPPPPPPPASTKPPQALSFAKRLQQLVEVLKGGSTFSGAKRVDTAAAAAEATEIPEVTLAS
|
Acrosin is the major protease of mammalian spermatozoa. It is a serine protease of trypsin-like cleavage specificity, it is synthesized in a zymogen form, proacrosin and stored in the acrosome.
|
P48038
|
Q6F992
|
RUVA_ACIAD
|
Holliday junction ATP-dependent DNA helicase RuvA
|
Acinetobacter
|
MIGCLIGEVFALEAPTVLLNVNGVGYEIDTPLSTFCQLQKGQHVTLWTHLVVREDAQQLYGFIDAQEKLIFRTLLKVNGVGPKMALGILSTLSIELFIHTIEHDDINTLIKVPGVGRKTAERLMIELRDRFKALSVQATTGSTVTSAQIQFSSNSPIAEAEAALQSLGYKPIEAQKAIAAVKADYTEAADLIRAALKSMMK
|
The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB.
|
Q6F992
|
Q9AVE3
|
SCRA_ARALY
|
S locus cysteine-rich-like protein a
|
Arabidopsis
|
MRCSVLFVVSYVIMSLLISHVQGMEDQKWKKVCNLEGNFPGRCVGNGDEQCKRDLTEDGNNPSKCRCRFRAGRRHCRCIYCEVFGM
|
Involved in self-incompatibility.
|
Q9AVE3
|
Q8UJ43
|
Y095_AGRFC
|
Nucleoid-associated protein Atu0095
|
Agrobacterium tumefaciens complex
|
MRDIMGMMGKVKEMQSKMEKVQQEIAALEIEGRAGGGLVTVILNGKGEMRGLKIDPSLFKEDEVEILEDLIVAAHKDAKEKGEAQAQEKMADLTAGLPLPPGMKLPF
|
Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection.
|
Q8UJ43
|
Q30P06
|
ENO_SULDN
|
2-phosphoglycerate dehydratase
|
Sulfurimonas
|
MFIDNVSAIEVMDSRGNPTVKTTVELSDGTKESAIVPSGASTGKREALELRDGGSRYMGKGVLKAVENVNAQISDALIGLSPFNQAVIDATMKELDGTDNYGNLGANAVLGVSMAVARAAAKSLGIPLYRYLGGANAMVIPTPMLNIINGGSHADNSVDFQEYMIMPVGFEDFATSLQASAEVYHNLKAILKSKKHNTALGDEGGFAPDLSSNEEPIQIIMQAIEKAGYKAGEQMAIALDVAASELVSDGGYRLDSENRTVTSAELVDYYVDLCNKYPIVSIEDGLSEDDWDGWKLLTEKLGDRVQLVGDDLFVTNATILNEGIKKGIANSILIKPNQIGSVSETMQTVRLAQRNGYKCVMSHRSGESEDAFIADFAVALNCGEIKTGSTARGERTAKYNRLLEIENEVVYGEYLGSELFN
|
Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
|
Q30P06
|
Q9LMU0
|
FCL2_ARATH
|
GDP-4-keto-6-deoxy-D-mannose-3,5-epimerase-4-reductase 2
|
Arabidopsis
|
MADNTGSEMKSGSFMLEKSAKIFVAGHRGLVGSAIVRKLQDQGFTNLVLRTHSELDLTSQSDVESFFATEKPVYVILAAAKVGGIHANNTYPADFIGVNLQIQTNVIHSAYTHGVKKLLFLGSSCIYPKFAPQPIPESALLTGPLEPTNEWYAIAKIAGIKMCQAYRLQHQWDAISGMPTNLYGQNDNFHPENSHVLPALMRRFHEAKANNADEVVVWGSGSPLREFLHVDDLADACVFLMDQYSGFEHVNVGSGVEVTIKELAELVKEVVGFKGKLVWDTTKPDGTPRKLMDSSKLASLGWTPKISLKDGLSQTYEWYLENVVQKKQ
|
Catalyzes the two-step NADP-dependent conversion of GDP-4-dehydro-6-deoxy-D-mannose to GDP-fucose, involving an epimerase and a reductase reaction.
|
Q9LMU0
|
B9MIA2
|
MNMA_ACIET
|
tRNA-specific 2-thiouridylase MnmA
|
Diaphorobacter
|
MTKHRVVVGLSGGVDSAVTAHLLKQQGHEVVGIFMKNWEDDDDSEFCSSRQDFLDAASVADVIGIEIEHVNFAAEYKDRVFAEFLREYQAGRTPNPDVLCNAEIKFKAFLDHAMRLGAEKIATGHYARVRQNPATGLFELLKGLDPSKDQSYFLHRLNQAQLSKTLFPVGDLHKTEVRRIAADIGLPNAKKKDSTGICFIGERPFREFLNRYIQHAPGPILDDRGRKLGRHVGLSFYTLGQRQGLGIGGVKEKGAQRGAGDHAPWFVARKELETNTLRVVQGHEHPWLLSHRLDAQDASWIAGHPPAAGACAAKTRYRQQDAACTVLAAQGDAFSLQFPEAQWAVTPGQSAVLYDGEVCLGGGVIAAVNG
|
Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
|
B9MIA2
|
A6VMZ1
|
APT_ACTSZ
|
Adenine phosphoribosyltransferase
|
Actinobacillus
|
MNKQLDLIKSSIKSIPNYPKEGIIFRDITSLTEIPEAFTATVNLIAEAFRHKGITKIIGTESRGFIFGAPVAVALGLPFILVRKPGKLPREVISQSYQLEYGEDKLEIHADAIQKGDNVLVIDDLLATGGTVEACIKLVNRLGGDVKHAAFVINLPDLGGGERLRKQGVEPFTLVDFAGH
|
Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
|
A6VMZ1
|
A6LPC4
|
ADDA_CLOB8
|
ATP-dependent helicase/nuclease AddA
|
Clostridium
|
MGNTKWTDEQLSAIETRNCNLLVAAAAGSGKTAVLVERIIRIITNEENPVDIDKLLVVTFTNAAAAEMRERIADAISKELENNPRSKNLQRQLTLLNRANITTMHSFCLDVIKNNYHRIDLDPSFRIGDQTEGILIKSEVIEELFEDKYEEEDIGFTNLVEIFSSYKNDNNLKNLVLDLYNFTMSGPWPEKWLINSAEAFNIKQLDELDRTNWVRVLAQSVKIELDGYVKMLEKAIEVTSKTDGLEPYMDNLLMELSYIKKAYESTDNGLEAMFNSLSSVQFSRLKSIKKDKVSDELSQNTVKKIRDDVKKGISELLNNAYSVNPQQMLRNIQGSYPYIKKLIELVLEFSARFSKRKRERNILDFNDLEHLCLKILSDYDDENNIIPSSIAMNFKEYFDEVLVDEYQDSNNVQETIINLVSRKNDDNPNVFMVGDVKQSIYRFRQAKPELFIEKYNTYDSSNGVNRKIQLYKNFRSRREIIDGVNYIFKEVMSEVVGELEYTDEEALNLGADFKENKFKDTIVGGPIEVNIIDKSHNETVVEDNEEQEEINNVILEGRIVAKRIKELMSKSEDEQIFKVLDKESGEYRPLKYRDIVILLRATKNWSEPLLDELSAEGIPVYADTGSGYFESIEIRTIISLLKVVDNPMQDIPVISVMRSPIMGFSAEEISDIRLVKKDNYFYENIKYISEEAYNSINESYSDVLIAKCKYFINSVDKWRNKSIYMAIDEFIWYLYMDTAYYGYVGAMPNGVLRQANLKILFQRARQFEKTSFKGLFNFINFINKLIKSSGDMGSAQVLGENEDVVRIMSIHKSKGLEFPVVFLCGLGKNFNLMDLNKSILYHDELGLGPDFIDIGKRFSIGTLAKESIKKKMKFETLSEEMRILYVACTRAKEKLIMTGTVGNLEKSAEKWLGSASLDYNRISPSEVLKGKSYLDWICMSLCQHRDGSVLSESFGTENLILKDDNSRWKVSFWNKGDLIDKTKTEVLEQGEGYELTIINNKPYDNYLYEEVDKILSYKYPFKASTTIKSNISVSDLKRRHAEEDYDTEQLYREKVKVVPKFLQEKKGLTPSEKGTAVHFVMKKIDFNRVSSTEEIKEQLHELFEKEFLLSEELKVINPTKILSFFRSDLGKKILDLNCRGEKIYREIPFYTEISSLEVDKTLDNIYKDEKIRLQGIIDCFFEYKGDIILIDYKTDYIMEGHEDEFKEKYRKQLDYYSDAIFKLTGKKVKYKYLYSFYLEKEIKII
|
The heterodimer acts as both an ATP-dependent DNA helicase and an ATP-dependent, dual-direction single-stranded exonuclease. Recognizes the chi site generating a DNA molecule suitable for the initiation of homologous recombination. The AddA nuclease domain is required for chi fragment generation; this subunit has the helicase and 3' -> 5' nuclease activities.
|
A6LPC4
|
C3MF10
|
YBEY_SINFN
|
Endoribonuclease YbeY
|
Sinorhizobium
|
MTALDIQISVEEGDWPSEDELQGLSTRILDVTVAFLIAEEKQPFPDDPPELSLVFTDDQSIREINAEWRNQDKPTNVLSFPAFPVTPGNMPGPMLGDIIVAYETLEREAAEMEKPFEEHLTHLLVHGFLHLFGYDHIEDDEAERMEGLETRILARLGLSDPYGDQPRIDSLEQ
|
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
|
C3MF10
|
P0A2W0
|
ACP_STRPN
|
Acyl carrier protein
|
Streptococcus
|
MAVFEKVQEIIVEELGKDASEVTLESTFDDLDADSLDLFQVISEIEDAFDIQIEAENDLKTVGDLVAYVEEQAK
|
Carrier of the growing fatty acid chain in fatty acid biosynthesis.
|
P0A2W0
|
Q54RR5
|
ACDSB_DICDI
|
Probable short/branched chain specific acyl-CoA dehydrogenase
|
Dictyostelium
|
MIKKLILDPKNVSIIKNGIRNYSKSKSFIQPITTLSEEETLLKETVANFANEKVRPLVKVMDETSELNKGLLKDLFDMNLMGIDISDSYGGANMNFMGSIIAIEELAKVDPAISVIVDVQNTLVNNCINRYGSIQQREKYLSMLATNTVGSFCLSESGSGSDAFALATRAVRQSDGTFVLNGTKQWITNAKEAGVFIVMANVDPSQGYKGITAFIVESNNPGLRIGKKEDKLGIRASSTCEVILDNCVVKPTDILGELGRGYKIAIEGLNEGRIGIAAQMLGLAQGVFDSTIPYLMERKQFGKPIATFQGMQFTYADLAVDIEAGRLLTYNAARIKEAGLPFVFQASMAKLHCSRVAEKAASACISMLGGVGFTKEFPAEKFFRDSKVGQIYEGTSNIQLQTIAKEIVKNFNK
|
Probable short and branched chain specific acyl-CoA dehydrogenase that catalyzes the removal of one hydrogen from C-2 and C-3 of the fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-CoA.
|
Q54RR5
|
A7FFU1
|
RECO_YERP3
|
Recombination protein O
|
Yersinia
|
MDGWQRAFVLHGRPYSETSLMLDLFTEGEGRMRVLAKGARGRRSNLKGCLQPFTPLLVRWSGRGEVKTLRSAEPVSLALPLSGSMLYSGLYVNELLSRVLEHQTSYSALFFDYLHCLQALAGSDGSPEHALRQFELAMLANLGYGVDFLHCAGSGQPVSDTMTYRYREEKGFIASLVVDHYSFTGRQLLALANREFPDADTLRAAKRFTRIALKPYLGGKPLKSRELFRQFVIKPPADPSP
|
Involved in DNA repair and RecF pathway recombination.
|
A7FFU1
|
B9KP41
|
RBFA_CERSK
|
Ribosome-binding factor A
|
Cereibacter
|
MAHRSHTGTGPSQRQLRVGELIRRTLADVLNRGEIHDPELNRLSITVGEVRCSPDLKVATVHVMPLGGKDVEEAIALLSKHRGELRHHITRQMTLKYAPDLRFRPDETFDRLDETRRLFSDETVMRDIRGGGEADED
|
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.
|
B9KP41
|
A8GXR0
|
FPG_RICB8
|
DNA-(apurinic or apyrimidinic site) lyase MutM
|
belli group
|
MPELPEVETLKNSLESKLIGLVIKKVEFKRDNLRYKLSADLADQIVNTNIINVRRRAKYLIIDFNNNHSLIVHLGMSGRFTLQPNNYEVKKHDHVVFNLSNNEKLIFNDTRRFGMIYSFHTELLEKDFFANLALEPLSDSFELQYLKSKLMNKKVPIKNLLMDNRIVVGVGNIYASESLHLAKIHPDKFGKDLNDDEIKNLIAAVKNVLSKAIIAGGTTLKDFVNGDNKPGYFTQQLMVYARDGQECLSCSSSIIKTKHSGRSTFYCKSCQKA
|
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.
|
A8GXR0
|
Q9LDD5
|
PYRP2_ARATH
|
Haloacid dehalogenase-like hydrolase domain-containing protein
|
Arabidopsis
|
MAEAIGAVSLVGHRPSIVRITVKNELKTQKSQSIVRFPVKVDYSAKGVLSHLMTQSVKKNRMSVFPIRALAMELTKEKKKDDRLPKTWNYLDSGADDKPSLWPPENKADKPSLHNPLLRQERMGCGWLGAIFEWEGVLIEDNPDLDNQSWLTLAQEEGKSPPPAFMLRRVEGMKNEQAISEVLCWSRDPVQVRRMAKRKEEIFKALHGGVYRLRDGSQEFVNVLMNNKIPMALVSTRPRETLENAVGSIGIRKFFSVIVASEDVYRGKPDPEMFIYAAQLLDFIPERCIVFGNSNQTIEAAHDGRMKCVAVASKHPIYELGAAELVVRRLDELSIIDLKKLADTDLTEFEPELEMEKEDERELPSSAVAVDDF
|
Catalyzes the dephosphorylation of 5-amino-6-(5-phospho-D-ribitylamino)uracil, also known as ARPP, but has no activity toward flavin mononucleotide (FMN) .
|
Q9LDD5
|
P25619
|
HSP30_YEAST
|
30 kDa heat shock protein
|
Saccharomyces
|
MNDTLSSFLNRNEALGLNPPHGLDMHITKRGSDWLWAVFAVFGFILLCYVVMFFIAENKGSRLTRYALAPAFLITFFEFFAFFTYASDLGWTGVQAEFNHVKVSKSITGEVPGIRQIFYSKYIAWFLSWPCLLFLIELAASTTGENDDISALDMVHSLLIQIVGTLFWVVSLLVGSLIKSTYKWGYYTIGAVAMLVTQGVICQRQFFNLKTRGFNALMLCTCMVIVWLYFICWGLSDGGNRIQPDGEAIFYGVLDLCVFAIYPCYLLIAVSRDGKLPRLSLTGGFSHHHATDDVEDAAPETKEAVPESPRASGETAIHEPEPEAEQAVEDTA
|
Probably cooperates with other heat shock proteins in the translocation of polypeptides through membranes. It may counteract the altering effect of heat shock on the plasma membrane.
|
P25619
|
Q979Y3
|
PDXS_THEVO
|
Pdx1
|
Thermoplasma
|
MALDLEKLKFGTELIKRGFSSMTKGGVIMDVTTAEQAKIAEKAGAVAVMALERVPADIRAAGGVARMADPKKIREILDAVTIPVMAKVRIGHISEAYTLEKLGVDMLDESEVLTPADPFFHLYKKKLTVPVVSGARNLPEAVRRIFEGAAMVRTKGEAGTGNIIEAVRHIRKVNEEIAIVRRMTQDEIKTAAENIASSYFQLRNEASTDLFGQSGKVLYDDVYYGMSREKIVKGISDILRQIRKLNRLPVVNFAAGGVATPADGALMMELGADGVFVGSGIFKSPDPEKMAKSIVEAVENYKDYDVVARVSEGLQGMPGIDIESIPRDSRLQERGW
|
Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by the PdxT subunit. Can also use ribulose 5-phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively.
|
Q979Y3
|
O14776
|
TCRG1_HUMAN
|
Transcription factor CA150
|
Homo
|
MAERGGDGGESERFNPGELRMAQQQALRFRGPAPPPNAVMRGPPPLMRPPPPFGMMRGPPPPPRPPFGRPPFDPNMPPMPPPGGIPPPMGPPHLQRPPFMPPPMSSMPPPPGMMFPPGMPPVTAPGTPALPPTEEIWVENKTPDGKVYYYNARTRESAWTKPDGVKVIQQSELTPMLAAQAQVQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQVQAQVQAQVQAQAVGASTPTTSSPAPAVSTSTSSSTPSSTTSTTTTATSVAQTVSTPTTQDQTPSSAVSVATPTVSVSTPAPTATPVQTVPQPHPQTLPPAVPHSVPQPTTAIPAFPPVMVPPFRVPLPGMPIPLPGVAMMQIVSCPYVKTVATTKTGVLPGMAPPIVPMIHPQVAIAASPATLAGATAVSEWTEYKTADGKTYYYNNRTLESTWEKPQELKEKEKLEEKIKEPIKEPSEEPLPMETEEEDPKEEPIKEIKEEPKEEEMTEEEKAAQKAKPVATAPIPGTPWCVVWTGDERVFFYNPTTRLSMWDRPDDLIGRADVDKIIQEPPHKKGMEELKKLRHPTPTMLSIQKWQFSMSAIKEEQELMEEINEDEPVKAKKRKRDDNKDIDSEKEAAMEAEIKAARERAIVPLEARMKQFKDMLLERGVSAFSTWEKELHKIVFDPRYLLLNPKERKQVFDQYVKTRAEEERREKKNKIMQAKEDFKKMMEEAKFNPRATFSEFAAKHAKDSRFKAIEKMKDREALFNEFVAAARKKEKEDSKTRGEKIKSDFFELLSNHHLDSQSRWSKVKDKVESDPRYKAVDSSSMREDLFKQYIEKIAKNLDSEKEKELERQARIEASLREREREVQKARSEQTKEIDREREQHKREEAIQNFKALLSDMVRSSDVSWSDTRRTLRKDHRWESGSLLEREEKEKLFNEHIEALTKKKREHFRQLLDETSAITLTSTWKEVKKIIKEDPRCIKFSSSDRKKQREFEEYIRDKYITAKADFRTLLKETKFITYRSKKLIQESDQHLKDVEKILQNDKRYLVLDCVPEERRKLIVAYVDDLDRRGPPPPPTASEPTRRSTK
|
Transcription factor that binds RNA polymerase II and inhibits the elongation of transcripts from target promoters. Regulates transcription elongation in a TATA box-dependent manner. Necessary for TAT-dependent activation of the human immunodeficiency virus type 1 (HIV-1) promoter.
|
O14776
|
Q7MAV4
|
TRMD_PORGI
|
tRNA [GM37] methyltransferase
|
Porphyromonas
|
MRIDIITVLPEMIENTLNCSIIGRAQERGLLELKLHQLRDYSTDKWKRVDDYPFGGEPGMVMQIEPIDRIITELKTQREYDEVIFTSPDGERFDQPMANELSLLSNLIVLCGHYKGIDYRIREHLITREISIGDYVLTGGELAAAVMTDAIARLIPGVLNDAGSALSDTFQDNLLAPPVYTRPAEYKGWRVPDILLSGHEANIAKWRLEQAVERTKRLRPDLIKD
|
Specifically methylates guanosine-37 in various tRNAs.
|
Q7MAV4
|
P71065
|
EPSO_BACSU
|
Putative pyruvyl transferase EpsO
|
Bacillus
|
MDSKHSMISLKQKLSGLLDVIPKQSEIIYADYPLYGNVGDLFIMKGTEAFFKEHGIRVRKRWNPDNFPIGRKLDPNLIIVCQGGGNFGDLYPYYQGFREKIVQTYPNHKIVILPQSIYFQNKDNLKRTAEIFSKHANLHIMTREKASYATAQAYFTTNHIQLLPDMAHQLFPVIPTQQPSNQKLRFIRTDHEANQALQEHAEAESYDWRTVLSASDRRTIAFLQTLNVLNKKAGNPLPIAYIWEKYSDYIVQKAIRFFSRYESVETSRLHGHILSSLLQKENTVIDNSYGKNANYFHTWMEGVPSTRLIQHASKKENLPAHM
|
May be involved in the production of the exopolysaccharide (EPS) component of the extracellular matrix during biofilm formation. EPS is responsible for the adhesion of chains of cells into bundles.
|
P71065
|
Q7U3I9
|
UREG_PARMW
|
Urease accessory protein UreG
|
Parasynechococcus marenigrum
|
MSSKLRLGVAGPVGSGKTALVEALCLRLRDQLQLAVVTNDIYTQEDAQFLTRAGALEPERIRGVETGGCPHTAIREDCSINRAAVADLEGQFPDLDLVMVESGGDNLAASFSPELVDLCIYVIDVAAGDKIPRKGGPGITRSDLLVINKIDLAPLVGADLSVMEADTRRMRGERPWCFTNLQNGDGLVQVVEFVLQQLPNA
|
Facilitates the functional incorporation of the urease nickel metallocenter. This process requires GTP hydrolysis, probably effectuated by UreG.
|
Q7U3I9
|
Q8TFD3
|
DOTC_DOTSE
|
Dothistromin biosynthesis protein C
|
Dothistroma
|
MSEDHTKADNLSEKDPHSPERSDSSSHEDAHAREEEESSDDDGALDGKPASLIAIVMIALSLIGLQLAVFLSALDTTIVTVALPAISAHFNSTAAYTWVGSAYLLANAASTPIWGKLADIFGRKPMLLLANALFMIGSLVCALSINVGMLITARAIQGAAGGGLLTLVDTIIGDLFSLRTRGTYLGMIGGVWAIACALGPIVGGAFTSSVTWRWCFYINLPIDGLAFGIIFFFLKLKTPKTPILEGFAAIDWAGSFFIIGGTLMFLFGLQYGGITFPWDSATVICLLVFGVVCIVLFGLVEWKFARFPIIPLRLFQYRNNCGALLVAFFHSFVFTSAFYYLPLYFQAVKGATPILAGVYILPAVLSTGVSAAATGAFIGNTGNYLIPMYFGMSMMILGYGLLINFDAGSGWAKLIIYQLIAGIGNGPNFQAPLVALQTKIKQSDIATGTATFNFVRNIATAISVVAGQVLYQNQLKKMTSTLQQLGPAASLIAAGDAGANTQAINALPTPQRDLARSAIADALSPMWIMYTAFAAAGLFCILLVSKTELTTTHEVTEVGLEAQKKAEAERKAERQAKDLEKAQKS
|
Efflux pump; part of the gene cluster that mediates the biosynthesis of dothistromin (DOTH), a polyketide toxin very similar in structure to the aflatoxin precursor, versicolorin B . One function of dotC may be to transport early-stage dothistromin biosynthetic intermediates from the cytoplasm into vacuoles, thereby affecting the rate of dothistromin production .
|
Q8TFD3
|
Q3JEC8
|
AMPA_NITOC
|
Leucyl aminopeptidase
|
Nitrosococcus
|
MNFHVTSGTPEKQRTAALVVGIYEDEKLSSYAQRIDKASEGYVSRLIKQGDFTGKKGQALLLFALPGVKAERVLLMGCGQKDKVTAKNLRQSWSGAVKALQACGATEAMICPLEAKPKDEELTQWARLIVETAEQALYRYEHTKSKKESLKKPLAKLTLLLDQRSQQPLAEQGIQQGQAIAKGVNLARDLGNLPGNICTPTYLADEARRLAKEYKSLKAKILEQAEMEKLGLGALLAVSRGSRQPPKLITLEYKGAPGKQKPIVLVGKGLTFDAGGISIKPGERMDEMKYDMCGGAGVLGTMQACAELELPLNVIAVVPSSENLPDGAANKPGDVLTSLSGQTIEVLNTDAEGRLILCDALTYSKRYRPDVVIDVATLTGACVIALGAHASGLLSNDQSLAEHLLAAGQTSDDRAWQLPLWDDYQQQLDSNFADMANIGGRGAGTITAACFLARFTEEFRWAHLDIAGTAWLSGKEKGATGRPVPLLTQYLIQRAQEAKTS
|
Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
|
Q3JEC8
|
A0A0C4DH26
|
KVD41_HUMAN
|
Probable non-functional immunoglobulin kappa variable 6D-41
|
Homo
|
MVSPLQFLRLLLLWVPASRGDVVMTQSPAFLSVTPGEKVTITCQASEGIGNYLYWYQQKPDQAPKLLIKYASQSISGVPSRFSGSGSGTDFTFTISSLEAEDAATYYCQQGNKHP
|
Probable non-functional open reading frame (ORF) of V region of the variable domain of immunoglobulin light chains . Non-functional ORF generally cannot participate in the synthesis of a productive immunoglobulin chain due to altered V-(D)-J or switch recombination and/or splicing site (at mRNA level) and/or conserved amino acid change (protein level) . Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens . The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen .
|
A0A0C4DH26
|
B4PNV2
|
EI3D1_DROYA
|
Eukaryotic translation initiation factor 3 subunit p66
|
Sophophora
|
MSETINTAAQFPSFEKPTVQFNEKGWGPCELPDTFKDVPYQPFSKNDRLGKICDWTNTSNNDKKYQNKYASSFGTGNQYSYYHEEDETTFHLVDTARVQKPPHQRGRFRNMRNSRSGRGRNARGGLNTHGMTTLSGKNVKARDPRHGRGMGKKFGHRGPPPKMRESSVAVRADWASIEEMDFPRLIKLSLPNIKEGVDIVTCGTLEYYDKTYDRINVKNEKPLQKIDRIVHTVTTTDDPVIRRLSKTVGNVFATDAILATIMCSTRSNYSWDIVIEKVGDKIFMDKRDHTEFDLLTVNESSVEPPTDDDSSCNSPRNLAIEATFINHNFSQQVLKTGDQEPKYKFEESNPFISEDEDIQVASVGYRYKKWELGSDIVLVARCEHDGVLQTPSGDSQFMTIKALNEWDSKLANGVEWRQKLDTQRGAVLANELRNNACKLAKWTVQAVLAGSDQLKLGYVSRINPRDHSRHVILGTQQFKPHEFATQINLSMDNAWGILRCIIDLVMKQKDGKYLIMKDPNKPIIRLYDIPDNTFDSDDSDDGEGDDEGFQQVYNYAHNKI
|
mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. In the eIF-3 complex, eif3d specifically recognizes and binds the 7-methylguanosine cap of a subset of mRNAs.
|
B4PNV2
|
C1FJ20
|
GATB2_MICCC
|
Glutamyl-tRNA(Gln) amidotransferase subunit B-2, chloroplastic/mitochondrial
|
Micromonas
|
MLRRALASRSSEAAIISTRVSLPRGSIPPPPTSSSSSSSSSREGRRPRFFSTTTTSAERPVDDDEWETVVGLELHVQIGAKTKLFSGAERLYGAEANANVAPFDAALPGSLPAVNARAVELAARLGFALGADVQSRSSFDRKHYHYPDLPHGYQITQQRSPIALGGSLDVFVRDGVSGTLRVERLQLEMDTGKSSKAKSSTLVDLNRAGSTLVEIVTAPDLRGAEEASAAAETFQKVVRFLGVGDANMEEGSMRVDVNVSHRTRDGAVAGERCEVKNLNSFRSIARAVAHERTRQIALLKRGQRVRRQTRSFDPATGATAVLRDKEALLDYRFAPEPDLPPVVIEPAALRAIKAAVPELPSTAAARLTNTAGLAPKLAQTIASKPSTVAYFDACAEAADAWSTRNGTVTVDKQDVANWVTGVLVGAVKRAGVTHKGGAGGEPLRGLPESAGAARVGELLARVAASTSMDSGALEATCAAVVASMPEQLAAYRGGRTRAMGSFVGEVMKRTKGRADPRRAAEIIKTLVDQ
|
Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in chloroplasts and mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
|
C1FJ20
|
P70596
|
MC4R_RAT
|
Melanocortin receptor 4
|
Rattus
|
MNSTHHHGMYTSLHLWNRSSHGLHGNASESLGKGHSDGGCYEQLFVSPEVFVTLGVISLLENILVIVAIAKNKNLHSPMYFFICSLAVADMLVSVSNGSETIVITLLNSTDTDAQSFTVNIDNVIDSVICSSLLASICSLLSIAVDRYFTIFYALQYHNIMTVRRVGIIISCIWAACTVSGVLFIIYSDSSAVIICLITMFFTMLVLMASLYVHMFLMARLHIKRIAVLPGTGTIRQGANMKGAITLTILIGVFVVCWAPFFLHLLFYISCPQNPYCVCFMSHFNLYLILIMCNAVIDPLIYALRSQELRKTFKEIICFYPLGGICELPGRY
|
Receptor specific to the heptapeptide core common to adrenocorticotropic hormone and alpha-, beta-, and gamma-MSH. Plays a central role in energy homeostasis and somatic growth. This receptor is mediated by G proteins that stimulate adenylate cyclase (cAMP).
|
P70596
|
P0A629
|
PSTC1_MYCBO
|
Phosphate transport system permease protein PstC 1
|
Mycobacterium tuberculosis complex
|
MLARAGEVGRAGPAIRWLGGIGAVIPLLALVLVLVVLVIEAMGAIRLNGLHFFTATEWNPGNTYGETVVTDGVAHPVGAYYGALPLIVGTLATSAIALIIAVPVSVGAALVIVERLPKRLAEAVGIVLELLAGIPSVVVGLWGAMTFGPFIAHHIAPVIAHNAPDVPVLNYLRGDPGNGEGMLVSGLVLAVMVVPIIATTTHDLFRQVPVLPREGAIALGMSNWECVRRVTLPWVSSGIVGAVVLGLGRALGETMAVAMVSGAVLGAMPANIYATMTTIAATIVSQLDSAMTDSTNFAVKTLAEVGLVLMVITLLTNVAARGMVRRVSRTALPVGRGI
|
Part of the binding-protein-dependent transport system for phosphate; probably responsible for the translocation of the substrate across the membrane.
|
P0A629
|
A8AFT6
|
TREA_CITK8
|
Alpha,alpha-trehalose glucohydrolase
|
Citrobacter
|
MITPALRHSGTLSFAIKLTVASTLLTFASLSAHAEEQPASPPQPPDILLGPLFNDVQSVKLFPDQKTFADAVPNSDPLMILADYRMQRNQSGFDLRHFVDVNFTLPKEGEKYVPPEGQSLREHIDGLWPVLTRTTESAGKWDSLLPLPEPYVVPGGRFREVYYWDSYFTMLGLAESDHWDKVADMVANFGYELDSWGHIPNGNRTYYLSRSQPPFFAFMVELLAQHEGDDALKKYLPQLQKEYAYWMEGVENLQPGEQNKRVVKLDDGTVLNRYWDDRDTPRPESWMEDITTAKSNPNRPATEIYRDLRSAAASGWDFSSRWMDDPNQLSTIRTTSIVPVDLNALLYKLEKMLARASKAAGDDANANQYEALASARQKGIETHLWNNQEGWYADYDLKSKKVRNQLTAATLFPLYVNAAAKDRASKVAAATQAHLLQPGGLSTTSVKSGQQWDAPNGWAPLQWVATEGLQNYGQDNVAMDVTWRFLTNVQHTYDREQKLVEKYDVSSTGTGGGGGEYPLQDGFGWTNGVTLKMLDLICPKEKPCDSVPATRPAAPGASQPAPQKQVETTP
|
Provides the cells with the ability to utilize trehalose at high osmolarity by splitting it into glucose molecules that can subsequently be taken up by the phosphotransferase-mediated uptake system.
|
A8AFT6
|
Q54NN1
|
DERL2_DICDI
|
Probable derlin-2 homolog
|
Dictyostelium
|
MAQPFEDWYKNLPIVTKIYMTGCVVTSVSVYLGLVGPLRLYLNFPLVFGKYEFWRLFTNFFFYDEIGMNFFFHMYFLVRHSRLLEESSFRGRSADYLFMWIFGSFLLLIMDAFLFYTKIVTKVLFLAPSIAFMVIYVWSRRNPNMHISFLGLFTFSAPYLPWVILIMGYLFNHDLTTDLLGAVAGHAYYFLEDAYPLISNRRLLKTPGFLKNLMDGQEQPIVDAHQQQEVQQAQQQEVQQPVQNFLNEDDLDQQ
|
May be involved in the degradation process of specific misfolded endoplasmic reticulum (ER) luminal proteins. May also be involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for proteasomal degradation.
|
Q54NN1
|
A8FXC6
|
TGT_SHESH
|
tRNA-guanine transglycosylase
|
Shewanella
|
MKFELDTTQGRARRGRLVFERGTVETPAFMPVGTYGTVKGMTPEEVRATGADILLGNTFHLWLRPGEEIMRKHGDLHDFMNWQRPILTDSGGFQVFSLGDIRKITEEGVHFRSPINGEKIFLDPEKSMQIQNSLGSDVVMIFDECTPYPATEDEARKSMQMSLRWAQRSRDEFDKLENPNSLFGIIQGGVYEDLRDESLKGLVDIGFDGYAVGGLAVGEPKADMHRILEHTCPQIPTDKPRYLMGVGKPEDLVEGVRRGVDMFDCVMPTRNARNGHLFTTEGVIKIRNARHRDDTSPLDDKCDCYTCKNYSRAYLYHLDRCNEILGARLNTIHNLRYYQKLMEGLRGAIETGTLDAFVEEFYTSQGREVPEVPELTD
|
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
|
A8FXC6
|
Q9Y2A7
|
NCKP1_HUMAN
|
p125Nap1
|
Homo
|
MSRSVLQPSQQKLAEKLTILNDRGVGMLTRLYNIKKACGDPKAKPSYLIDKNLESAVKFIVRKFPAVETRNNNQQLAQLQKEKSEILKNLALYYFTFVDVMEFKDHVCELLNTIDVCQVFFDITVNFDLTKNYLDLIITYTTLMILLSRIEERKAIIGLYNYAHEMTHGASDREYPRLGQMIVDYENPLKKMMEEFVPHSKSLSDALISLQMVYPRRNLSADQWRNAQLLSLISAPSTMLNPAQSDTMPCEYLSLDAMEKWIIFGFILCHGILNTDATALNLWKLALQSSSCLSLFRDEVFHIHKAAEDLFVNIRGYNKRINDIRECKEAAVSHAGSMHRERRKFLRSALKELATVLSDQPGLLGPKALFVFMALSFARDEIIWLLRHADNMPKKSADDFIDKHIAELIFYMEELRAHVRKYGPVMQRYYVQYLSGFDAVVLNELVQNLSVCPEDESIIMSSFVNTMTSLSVKQVEDGEVFDFRGMRLDWFRLQAYTSVSKASLGLADHRELGKMMNTIIFHTKMVDSLVEMLVETSDLSIFCFYSRAFEKMFQQCLELPSQSRYSIAFPLLCTHFMSCTHELCPEERHHIGDRSLSLCNMFLDEMAKQARNLITDICTEQCTLSDQLLPKHCAKTISQAVNKKSKKQTGKKGEPEREKPGVESMRKNRLVVTNLDKLHTALSELCFSINYVPNMVVWEHTFTPREYLTSHLEIRFTKSIVGMTMYNQATQEIAKPSELLTSVRAYMTVLQSIENYVQIDITRVFNNVLLQQTQHLDSHGEPTITSLYTNWYLETLLRQVSNGHIAYFPAMKAFVNLPTENELTFNAEEYSDISEMRSLSELLGPYGMKFLSESLMWHISSQVAELKKLVVENVDVLTQMRTSFDKPDQMAALFKRLSSVDSVLKRMTIIGVILSFRSLAQEALRDVLSYHIPFLVSSIEDFKDHIPRETDMKVAMNVYELSSAAGLPCEIDPALVVALSSQKSENISPEEEYKIACLLMVFVAVSLPTLASNVMSQYSPAIEGHCNNIHCLAKAINQIAAALFTIHKGSIEDRLKEFLALASSSLLKIGQETDKTTTRNRESVYLLLDMIVQESPFLTMDLLESCFPYVLLRNAYHAVYKQSVTSSA
|
Part of the WAVE complex that regulates lamellipodia formation. The WAVE complex regulates actin filament reorganization via its interaction with the Arp2/3 complex. Actin remodeling activity is regulated by RAC1. As component of the WAVE1 complex, required for BDNF-NTRK2 endocytic trafficking and signaling from early endosomes.
|
Q9Y2A7
|
A4Y4U6
|
GLGC_SHEPC
|
ADP-glucose synthase
|
Shewanella
|
MSNVRYISNLTRETYALILAGGRGSRLHELTDWRAKPALYFGGKFRIIDFPLSNCINSGVRRVGVVTQYKSHSLIRHVMRGWGHFKKELGESVEILPASQRFSENWYQGTADAVFQNIDIIRHELPKYVMVLSGDHVYRMDYAGILAAHAESGADMTVSCLEVPIAEAAGAFGVIEVDDNMRILGFEEKPQRPKPSPDNPEMCLASMGNYVFNTEFLFEQLKKDSQNATSDRDFGKDIIPSIIEKHNVFAYPFKSPFPNEQAYWRDVGTLDSFWQANMELLSPTPALNLYDAKWPIWTFQEQLPPAKFVFDDDDRRGMALDSIVSSGCIISGATVRRSVLFNEVRVCSYSVVEDSVVLPDVVVLRHCKIKNAIIDRGCIIPEGTVIGYNHDHDRAKGFRVSEKGVTLVTRDMLGLPVGYE
|
Involved in the biosynthesis of ADP-glucose, a building block required for the elongation reactions to produce glycogen. Catalyzes the reaction between ATP and alpha-D-glucose 1-phosphate (G1P) to produce pyrophosphate and ADP-Glc.
|
A4Y4U6
|
Q52071
|
NIFW_ENTAG
|
Nitrogenase-stabilizing/protective protein NifW
|
Pantoea agglomerans group
|
MDWFTRIEGVDELESAQSFFDFFELEVDPVLLRSRHLHIMAQFNQRLTAAVPVHFVDEEESDRADWRLARRLLAESYQHTVAGPLNTQSGLAVYQRNNGSFIGWNDLLEVRP
|
May protect the nitrogenase Fe-Mo protein from oxidative damage.
|
Q52071
|
A1WX30
|
DNAJ_HALHL
|
Chaperone protein DnaJ
|
Halorhodospira
|
MAKRDYYEVLGVNKNASDAEIKKAYRRMAQKFHPDRNPGDEESAERFKEVKEAYEVLSDAQKRAAYDQFGHAGVDPSAGGGPRGYGGGAGPGGPDFSDIFSDVFGDIFGSGGGRGGGRSRAFRGADLRYTLELSLEDAVRGTEEQIQVPTHVECDACKGSGSRAGSKPQTCPTCKGHGDVRVQQGFFSIQQTCPRCGGEGTMVTDPCPKCRGRGRVEDRKTLNVRIPAGVDTGDRIRLSGEGEPGERGGPPGDLYVQVAVREHEFFERDGADLHCQVPVDIVTAALGGEVEVPTLDGRVNLRIPPGTQPNQVFRLRGKGVKPVRGNRQGDLLCRIHVETPVNLTKRQRELLEEFQATLQDTGGKHHPHTSSWLDKVKRFIEEWRI
|
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
|
A1WX30
|
D1ZMX7
|
LCL2_SORMK
|
Long chronological lifespan protein 2
|
Sordaria
|
MRTLTLLLSLLFLASPIAAQFGSFFDQMFGGGGHGGHGHQHQQQHQGHGQQQHPNVPSDPSIYQANYQRAHCDKYLCPDTLACVHYPHHCPCPWPSHEDKVELAEGQRVCVSRGGFKAGEAARKIELARQGLL
|
Probable component of the endoplasmic reticulum-associated degradation (ERAD) pathway.
|
D1ZMX7
|
O14259
|
SFP47_SCHPO
|
Ubp4-interactor sfp47
|
Schizosaccharomyces
|
MNSFSSNEYSTEISTEALNNWQQLVEQRISLELEYAAKLAKLTKSIKAIKQCAPLNDLTKQVCVELMQCNKKHLEASRYFQTHVKEFMKEYVDRENKFSNETISKSSAAALMTSMENFILFTNPVYHNKLQVPSKSDMEIANSLKITQPAEKNSGTANPISAYSLEHAELDERNNQLSEALSMLRLSPFVNNYYPSYQNRKDGKSLMENRGVVLSVDTVTSPISQSPKKLTPTTSPINSTSLSFVDAKKPGSKWPSQYDFPKKTKSTEIPFKTLPSLNINNERELTKHKLPIVKPKLAVFPSNQATASTLQLAPPPVQAIPTLRNPVNLDDKKESLLKYYATHPTITPDGFPIFAYVRALYAYKATLPSEIDLNVDDTLVVLNRQKDGWWKGLVVSPTVGRIGLFPSNYIEELEY
|
Required for the regulation of activity and recruitment of ubp4 to endosomes.
|
O14259
|
A1U2B7
|
IHFA_MARN8
|
Integration host factor subunit alpha
|
Marinobacter
|
MAALTKADMAERLYEELGLNKREAKEMVEAFFDEIRGALSHNEQVKLSGFGNFDLRDKKQRPGRNPKTGEEIPISARRVVTFRPGQKLKQKVEAYAGTQS
|
This protein is one of the two subunits of integration host factor, a specific DNA-binding protein that functions in genetic recombination as well as in transcriptional and translational control.
|
A1U2B7
|
Q39KY0
|
ATPF_BURL3
|
F-type ATPase subunit b
|
Burkholderia cepacia complex
|
MNLNATLFAQMVVFLVLAWFTMKFVWPPLINALDERSKKIADGLAAAEKGKAELDAAHKRVDQELAQARNDGQQRIADAEKRAQAVAEEIKSNAQAEAARIIAQAKAEAEQQIVKAREALRGEVATLAVKGAEQILKREVDQTAHAQLLNQLKAEL
|
Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
|
Q39KY0
|
D8GR66
|
RNFC_CLOLD
|
Rnf electron transport complex subunit C
|
Clostridium
|
MLKSFRGGVHPDDSKKYTANKPIEIAPIPDKVFIPVRQHIGAPTSPVVQKGDEVKKGQLIAKSDAFVSANIYASTSGKVVDIGDYPHPGFGKCQAIVIEKDGKDEWVEGIPTSRNWKELSVKEMLGIIREAGIVGMGGATFPVHVKLAPPPDKKVDVFILNGAECEPYLTADYRSMLENSDKVVAGVQIIMKILNVEKAFVGIEDNKPKAIEAMKKAFEGTKVQVVGLPTKYPQGAEKMLINVLTGREVPSGGLPADVGAVVQNVGTCIAISDAVERGIPLIQRVTTISGGAIKEPKNILVRIGTTFKDAIDFCGGFKEEPVKIISGGPMMGFAQSNLDIPIMKGSSGILGLTKNDVNDGKESSCIRCGRCLKACPMHLNPSMLSILGQKDLYQEAKEEYNLLDCVECGSCVYTCPAKRKIVQYIRYLKSENRAAGEREKAKAAKAKEKKEKEEVLK
|
Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. Couples electron transfer from reduced ferredoxin to NAD(+) with translocation of H(+) out of the cell. Essential for energy conservation during autotrophic growth. Contributes to ATP synthesis during heterotrophic growth.
|
D8GR66
|
P28773
|
CSF2_SHEEP
|
Colony-stimulating factor
|
Ovis
|
MWLQNLLLLGTVVCSFSAPTRQPSPVTRPWQHVDAIKEALSLLNDSTDTAAVMDETVEVVSEMFDSQEPTCLQTRLELYKQGLRGSLTSLTGSLTMMASHYKKHCPPTQETSCETQIITFKSFKENLKDFLFIIPFDCWEPVQK
|
Cytokine that stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.
|
P28773
|
Q9KLQ5
|
FBPC_VIBCH
|
Fe(3+) ions import ATP-binding protein FbpC
|
Vibrio
|
MEKQNFVVLKNICKRFGSNTVIGNLDLEIKKGSLVTLLGPSGCGKTTVLRLVAGLEKPTSGQIFIDGEDVTERSIQQRDICMVFQSYALFPHMSLYENVAYGLKMLKLPSEEVRQRVDEALKIVDLEGMGERYVDQISGGQQQRVALARALVLKPKVLLFDEPLSNLDANLRRSMRETIRELQQRFDITSLYVTHDQAEAFAVSDTVIVMKQGDIMQIGTPQELYKAPKSMFMANFMGEANMFQGHFDGQQIHINGYAIDADLEVTRDKPNGEYQIGVRPEAITLHTQGSESQACQILKSAYMGSMYEVTVKWHDQELLLQLNSAQFNHTLTQHAYVVFNPRGLFLLPYAE
|
Part of the ABC transporter complex FbpABC involved in Fe(3+) ions import. Responsible for energy coupling to the transport system.
|
Q9KLQ5
|
Subsets and Splits
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