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
|
|---|---|---|---|---|---|---|
A5ICS0
|
LOLA_LEGPC
|
Outer-membrane lipoprotein carrier protein
|
Legionella
|
MNKLFLILLLIFSHEVFSQTSAEVLQSKLNAIQTMTANFSQIVKAKNREVSRSSGSMALQRPGRFRWQTKDPLEQLIVADGQKMWIYDVDLEQVTVKNQEKGLGGTAALFLSGYDETLTHDFDVSEKQKGKLTVFDLKSKSAKENFQRIKLIFSQSTLIGLELYDQLGQITDVKLVQIKSNPKLPAKLFQFKPPKGVDVVKQ
|
Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane).
|
A5ICS0
|
B8HEU5
|
ENO_PSECP
|
2-phosphoglycerate dehydratase
|
Pseudarthrobacter
|
MALIDAIHAREILDSRGNPTVEVEVLLSDGQIGRAAVPSGASTGEHEAVELRDGDKGRYLGKGVQKAVDAVIDQIAPALTGFDATDQRSIDQAMLDLDGTPNKGKLGANAILGVSLAVANAAAASADLPLYKYLGGPNAHVLPVPLMNILNGGSHADSDVDIQEFMIAPIGAETFSEGLRWGVEVYHNLKSVLKEQGLSTGLGDEGGFAPNLPSNRAALDLIQEAIKNAGYTPGKDIALALDVASSEFFKDGAYQFEGKALSASEMSAYYAELVADYPLVSIEDPLDENDWEGWKTLTDAIGDKVQLVGDDLFVTNPAILQRGIDTRTANSLLVKVNQIGSLTETLDAVSLAQRAGYTTITSHRSGETEDTTIADISVATNAGQIKTGAPARSERVAKYNQLLRIEEELDDAARYAGRSAFPRFKG
|
Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
|
B8HEU5
|
Q39RS2
|
HCP_GEOMG
|
Prismane protein
|
Geobacter
|
MGMFCNQCEQAAKGVGCDIIGVCGKNPEVAALQDLMLYGLKGLAIYADKARELGVKEEKIDYFVLEGLFTTVTNVDFDPVQIAGKLRTCYDYKERIKALYETAYREKNGSSAPQITAGPAAWVIAGDLEGLVKQGQEHGINTHHADADIRSAIEILIYGLKGMAAYADHAYILGKKDEEVFAFFHKAMAATADPAKGLMDFVGLAMECGKLNIKVMGMLNEGHVAHYGHPVPTKVPTGTRKNKGILVSGHDLRMLEELLKQTDGKGIDVYPHGEMLPAHGYPGLKKYAHLYGNFGGAWQDQAKEFPHFPGAIIFNTNCIQRPADSYKDRLFSWGQVGWPGVKHINGWDFSEVINKALECPELADAPAKEILTGFGHNAVLGVADKVIEGVKAGAIKHFFLIGGCDGAKPGRNYYTELAEKVPQDCVILTLACGKYRFNKLEFGDIGGIPRLLDIGQCNDAYSALQIALALADAFKCGVNDLPLSMILSWYEQKAVVILLSLLHLGIKNIKIGPSLPAFVTPNVLNFLVENFNLGPITTVDADLKAALGQ
|
Catalyzes the reduction of hydroxylamine to form NH(3) and H(2)O.
|
Q39RS2
|
Q9RQ55
|
ILVC_BUCDN
|
Ketol-acid reductoisomerase type II
|
Buchnera
|
MNYFNTLNFRQKINQIKKCRFMEKKEFNKKNEILKNKKIVIVGCGSQGLNQGLNMRDSGLNISYALRKNSILKKNQSWINATKNNFLVGDYESLIPNADLVINLTPDKQHSNVVKELQKLMKKDACLGYSHGFNIVEKLRNIRKDITVIMVAPKCPGTEVREEYKRGFGVGTLIAVHNENDYSNMGLEVAKAWAFSTGGHRAGVLESSFVAEVKSDLMGEQTILCGMLQTASLVCYEKLITTQNHPGYAGKLIQFGWETITESLKHGGITLMMDRLSNSSKIRAFKLSQEIKEFSQNLFQKHMDDIISGDFSSKMIQDWKNKDQNLLNWRYKTKNTSFEQSPDYDKKILEQEYYDHGILMVAILKAGIELSFETMIQSGIMEESAYYESLHELPLIANTIARKKLYEMNMVISDTAEYGNYLFSESAYPILKEFVKNINNTDLGSALPRNSVNNIELYNVNTMIRNHPIEIIGRKLRSYMKNMKTIIVG
|
Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.
|
Q9RQ55
|
Q7U140
|
KDC_MYCBO
|
Alpha-keto-acid decarboxylase
|
Mycobacterium tuberculosis complex
|
MTPQKSDACSDPVYTVGDYLLDRLAELGVSEIFGVPGDYNLQFLDHIVAHPTIRWVGSANELNAGYAADGYGRLRGMSAVVTTFGVGELSVTNAIAGSYAEHVPVVHIVGGPTKDAQGTRRALHHSLGDGDFEHFLRISREITCAQANLMPATAGREIDRVLSEVREQKRPGYILLSSDVARFPTEPPAAPLPRYPGGTSPRALSLFTKAAIELIADHQLTVLADLLVHRLQAVKELEALLAADVVPHATLMWGKSLLDESSPNFLGIYAGAASAERVRAAIEGAPVLVTAGVVFTDMVSGFFSQRIDPARTIDIGQYQSSVADQVFAPLEMSAALQALATILTGRGISSPPVVPPPAEPPPAMPARDEPLTQQMVWDRVCSALTPGNVVLADQGTSFYGMADHRLPQGVTFIGQPLWGSIGYTLPAAVGAAVAHPDRRTVLLIGDGAAQLTVQELGTFSREGLSPVIVVVNNDGYTVERAIHGETAPYNDIVSWNWTELPSALGVTNHLAFRAQTYGQLDDALTVAAARRDRMVLVEVVLPRLEIPRLLGQLVGSMAPQ
|
Decarboxylates branched-chain and aromatic alpha-keto acids to aldehydes.
|
Q7U140
|
Q28UQ8
|
YIDC_JANSC
|
Membrane protein YidC
|
unclassified Jannaschia
|
MDDQNRNLILATGLSFVVILVWFLLFPPPEMVEDPNAIPPAAETGGVETDTGIALTPPVTVADAPAGADTTAPSEVALSEAARIDIDTPAVEGSISLLGGRIDDLSLRNYFTEVDGDQIVRLLSPVGSDDPYYALYGWTPSGDLGYADVPTSDTPWELESGTILTPDSPITLAWDNGSGLIFRRTIEIDDRFMFQVTQSVENTGGAEVNLAPYGIVARHGLPSDLQNFFILHEGVVRKVDGELSELGYSDLPDLDIIAREGVPAEVMEVETNGWIGFTDKYWMTTLIPGENQSFVSVVKYVPSAEIYQTEARLPYMSIAPGETAEVTTQLFAGAKEAEAIRDYENAEPGLIASLFGAEQDASRGEIPRFIDSIDWGWFYFLTKPLFWLLHWLNGAIGNMGLAIISLTLIVKAVLFPLAYRSYVSMAKMKELQPEIEKLKESAGDDRQKLQQGMMELYKKNKVNPAGGCLPILLQIPIFFSLYKVIFVTLELRHAPFFGWLNDLSAPDSSSIINLYGLLPNPAPEPESIMALIFIGILPLLLGISMWLQQKLNPAPTDAMQAQIFAWLPWVFMFMLGSFASGLLVYWIANNTLTFTQQYLIMRSQGFKPDVFGNIRSSFKKKAKEEK
|
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. Aids folding of multispanning membrane proteins.
|
Q28UQ8
|
Q9PBC5
|
HISX_XYLFA
|
Histidinol dehydrogenase
|
Xylella
|
MKIIDWNQLDTAAQAQTLTRPAQTIATQTREAVAALIEQVRRGGDTALRDITARLDGVDLATFEVTAAELAAAATAVAPELQHAMQTAAARIEAFHRAGMTNGYRVETAPGVVCERLVRPIARVGLYVPAGSAPLFSTALMLGVPARLAGCREVVLCTPPSKDGRANPAVLLAARLTGVTRVFTLGGAQAIAAMAYGTASVPTCDKVFGPGNSFVTEAKQQLAQAGVVAIDMPAGPSEVLVIADAAANPAFIAADLLSQAEHGPDSQVLLLSDSDALMTAVQTALALQLQQLSRAEIARQALAQSRLIKVATLETAFDISNRYAPEHLILALRQPRAWLHRVAAAGSVFLGDYTPEALGDYCSGTNHVLPTGGAARAYSGVSVSSFQNMISVQAASRSGIAEIGDCALTLARAEGLDAHANAVALRMGTVP
|
Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.
|
Q9PBC5
|
Q8G1L5
|
UVRC_BRUSU
|
Excinuclease ABC subunit C
|
Brucella
|
MKRLPNNPGVYRMFNSDGDVLYVGKARNLKKRVSNYARGIGHSNRITRMIRETVTMEFVVTRTETEALLLEANLIKRSRPRFNVLMRDDKSFPYILLTGGHRAPGIFKHRGARSRKGDYFGPFASAGAVGRTINALQRAFLLRTCTDSVFETRTRPCLLYQIKRCSAPCTYEISDEDYAGLVAEAKAFLSGKSQSVKDHLAAAMQAASADLDFEHAAVYRDRLAALSHVQSHQGINPQTVEEADVFAIHQEGGMTCIQVFFFRTGQNWGNRAYFPKADSSLGPAEVLGAFLSQFYDDKPCPKLVLLSETVEEQSLITEALSTRAGHKVQVSVPQRGEKKELVQHALTNAREALGRRLAETSSQARLLQGLAETFGLPRAPRRIEVYDNSHIMGTNAVGGMIVAGPEGFVKNQYRKFNIRSTDITPGDDFGMMREVIERRFSRLVKEHGTPAGEVENPDAFPAWPDVILIDGGQGQVGAVRQILGEMGISDLVTAIGIAKGVDREAGRERFFMEGKQPFTLPPRDPVLYFIQRLRDEAHRFAIGTHRARRKKEMVRNPLDEIAGIGPTRKRALLHHFGTAKAVSRAAVEDLMQIDGISEAMARAIHDHFRDK
|
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision.
|
Q8G1L5
|
P85298
|
RHG08_HUMAN
|
Rho-type GTPase-activating protein 8
|
Homo
|
MAGQDPALSTSHPFYDVARHGILQVAGDDRFGRRVVTFSCCRMPPSHELDHQRLLEYLKYTLDQYVENDYTIVYFHYGLNSRNKPSLGWLQSAYKEFDRKDGDLTMWPRLVSNSKLKRSSHLSLPKYWDYRYKKNLKALYVVHPTSFIKVLWNILKPLISHKFGKKVIYFNYLSELHEHLKYDQLVIPPEVLRYDEKLQSLHEGRTPPPTKTPPPRPPLPTQQFGVSLQYLKDKNQGELIPPVLRFTVTYLREKGLRTEGLFRRSASVQTVREIQRLYNQGKPVNFDDYGDIHIPAVILKTFLRELPQPLLTFQAYEQILGITCVESSLRVTGCRQILRSLPEHNYVVLRYLMGFLHAVSRESIFNKMNSSNLACVFGLNLIWPSQGVSSLSALVPLNMFTELLIEYYEKIFSTPEAPGEHGLAPWEQGSRAAPLQEAVPRTQATGLTKPTLPPSPLMAARRRL
|
GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state.
|
P85298
|
Q2GI75
|
DNAJ_EHRCR
|
Chaperone protein DnaJ
|
Ehrlichia
|
MSKSDYYDLLGVSKSATPEEIKKAYRKMALKYHPDKNPGNKEAEEKFKELSEAYDVLIDQDKRAAYDKYGHNAFDSSGRGGFDFNSGFSGDFSDIFNDLFGGGFRGGRGSSRRHDSGAVGSDLRFDIEITLEDSFNGKKVPISYVTYVKCSSCSGSGSEGSAKSVQCSTCHGVGNVRTQQGFFTIERTCHVCNGEGEIIQNKCKKCSGSGRVRDEVNLLVTIPKGIESGNKIRLNGKGEAGYRGARSGDLYVYSNIQKHKFFTRNGSDLYCNVPIKMTLAALGGHIEMPSIDGTWTKVKVPEGSQNGDKLRLKEKGMPIINSSKRGDMYIQITVETPVKLTKKQKELLQKFDDEPNVDCNPQSTGFFQKVKSFWKDIRSN
|
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.
|
Q2GI75
|
Q8KPQ7
|
KGUA_SYNE7
|
GMP kinase
|
Synechococcus
|
MSIGRVVVLTGPSGVGKGTLLKAILSQHPEAFLSISATTRSPRPGEVDGQHYYFLSREEFQTKIAEQEFLEWAEFAGNLYGTPRSPVIEQVNLGRTVILEIELEGARQVRKTLPSARQVMLLPPSVEELERRIRERATEDEAAIARRLLQAQTEIGAAKEFDRCVINDQLDTAITALEAAIFS
|
(Microbial infection) Catalyzes the phosphorylation of dZMP to dZDP, when the bacterium is infected by a phage that produces the substrate for the synthesis of dZTP (2- amino-2'-deoxyadenosine 5'-triphosphate), which is then used by the phage as a DNA polymerase substrate.
|
Q8KPQ7
|
B0R636
|
RADB_HALS3
|
DNA repair and recombination protein RadB
|
Halobacterium
|
MREDDTHLPTGCGALDELLGGGVERGTVTQLYGPPAAGKTNVALTTAVTTAAAGGLAVYVDTEGLSLARFQQLLEARATDPEAASANVIVSDAHDFDEQAQAVRDTADFADRADLIVVDSVTGFYRLARGGDDTTGDALRQVADQITHLLSLARKHDLAVVVTNQVFTDVDNDSDRARPLGGHTLAHWTGTVLRLDRFRGGTRRATLEKHRAKPDGEHAQFQITDGGIDAASADDY
|
Involved in DNA repair and in homologous recombination. May regulate the cleavage reactions of the branch-structured DNA. Has a very weak ATPase activity that is not stimulated by DNA. Binds DNA but does not promote DNA strands exchange.
|
B0R636
|
Q9YGJ9
|
VSPH2_GLOBR
|
Snake venom serine protease Haly-2
|
Gloydius
|
MVLIRVLANLLILQLSYAQKSSELIIGGDECNINEHRSLVLMYYDGHQCDGTLINEEWVLTAAHCDGENMEIQLGVHSKKVPNEDVQTRVPKEKFFCDSNKTYARWNKDIMLIRLDRPVSNSAHIAPLSLPSSPPSVGSVCRIMGWGTFSTTQETYPDVPHCANINIHDFEVCQAAYPGLPATNRILCAGILEGGKDTCKGDSGGPLICNGEIQGIVSWGGHLCGNVLEPGIYTKVFDHLEWIRSIIAGNTDATCPL
|
Snake venom serine protease that may act in the hemostasis system of the prey.
|
Q9YGJ9
|
P38039
|
CYSJ_SALTY
|
Sulfite reductase [NADPH] flavoprotein alpha-component
|
Salmonella
|
MTTPAPLTGLLPLNPEQLARLQAATTDLTPEQLAWVSGYFWGVLNPRSGAVAVTPVPERKMPRVTLISASQTGNARRVAEALRDDLLAANLNVTLVNAGDYKFKQIASEKLLVIVTSTQGEGEPPEEAVALHKFLFSKKAPKLENTAFAVFSLGDTSYEFFCQSGKDFDSKLAELGGERLLDRVDADVEYQAAASEWRARVVDVLKSRAPVAAPSQSVATGAVNDIHTSPYTKDAPLIATLSVNQKITGRNSEKDVRHIEIDLGDSGLRYQPGDALGVWYQNDPALVKELVELLWLKGDEPVTVDGKTLPLAEALEWHFELTVNTANIVENYATLTRSESLLPLVGDKAQLQHYAATTPIVDMVRFSPAQLDAQALIDLLRPLTPRLYSIASAQAEVESEVHITVGVVRYDIEGRARAGGASSFLADRVEEEGEVRVFIEHNDNFRLPANPETPVIMIGPGTGIAPFRSFMQQRAAEGVEGKNWLFFGNPHFTEDFLYQVEWQRYVKEGVLSRIDLAWSRDQKEKIYVQDKLREQGAELWRWINDGAHIYVCGDARRMAADVEKALLEVIAEFGGMDLESADEYLSELRVERRYQRDVY
|
Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component.
|
P38039
|
A4VYR6
|
RS13_STRS2
|
30S ribosomal protein S13
|
Streptococcus
|
MARIAGVDIPNDKRVVISLTYVYGIGLATSKKILAAAGISEDVRVKDLTSDQEDAIRREVDAIKVEGDLRREVNLNIKRLMEIGSYRGIRHRRGLPVRGQNTKNNARTRKGKAVAIAGKKK
|
Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites.
|
A4VYR6
|
Q8T2I8
|
SEPA_DICDI
|
Septase A
|
Dictyostelium
|
MSKKEPEEIKKNVTVGNYNLGVVIGKGGFGTVYQGLDIEDGDFVAIKQINLTKIPKDQLQGIMNEIDLLKNLNHANIVKYIKYVKTKDNLYIVLEYVENGSLSGIIKKFGKFPETLVCVYIRQVLEGLVYLHEQGVVHRDIKGANILTTKEGKIKLADFGVATKFDDTSAAAVVGTPYWMAPEIIELNGATTKSDIWSVGCTVIELLTGSPPYYDLGQMPALFRIVQDDCPPLPEGISPPLKDWLMQCFQKDPNLRISAQKLLKHKWIQASIKKKPVENGAGGVGNGTDSLGAPANIDDIAKNITDYNERINKKPSHQRKPSIHPKSPKGKVFLPPPEEEEDEWGDDFSNTPKSIKLPDKKSPLKLTNNKPSTPLKQQPTNNTPVQQQQQQQQPPPLKLAVPKQPVIENDDDWGDDFNTVSDLSKAVGSLNFNNNKKNETPKPNIKKPTFSEDEDEDDDDDGFGSGGDDEDDDFGDIPTSIKLNPKFGSNIKGNSSGSANTTNSSSTVVQQPKLTVSNNNNNNNKKLPLSPRQPSSGNVKEGINHGSTGSKSGGVIIDQWGEDGEEDNDWGDVATVNFDPKVIRKGTVNKPDLSTRLKNRIALSETALSNSFNNNGNDDEDEDIFADDFDEDDDEDFDLDKNLMKDNYARMSSEILKLMNLLTPEQPEEVISSACTQLITMFKENSEQKTLLIRRHGVIPIMEMLEVSNIQSHVLCSILKVVNQIIDNNMEIQENLCLVGGIPAIMKFSGPEYPASVRLETASFISKMCSTSTLTLQMFIACKGLPILVDFLLSPYAESKRLVWMAVDAIVNVFELQSPTPKNDFCRLFSKCGLLKTLPIVLRDSIADGEAAATYPDRIINLFIMFSAADSVVRKTMSAVEVIRPILDTLSQLMPEQLAKVLKSIKQLSMDHNTLANLQNAGAIRFMVPFLGRRTGAFVAEIHNHVLNTMFHLCRIDPERQYQAAIDGIIPHLQYFITSHSPLNQFALPIICDLAHSKKARSELWKNNGVAFYLSLLEERYWQVNALDSLAVWITDETHKVENIIATNENIKKLIQLFTNAESQSFAGILEPLLKIIQISIPVNILLGTSNFITKIIDKLGHTNPQVRLNLLKIITSLYECHPNAKKMIQEFKLIPIIQKIADTDKSVLVQKMASKLLEAFNANTVI
|
Serine/threonine-protein kinase involved in the spatial and temporal control system organizing cortical activities in mitotic and postmitotic cells.
|
Q8T2I8
|
Q9P6L5
|
SLA2_SCHPO
|
SLA2 protein homolog
|
Schizosaccharomyces
|
MSSFRLQSDHMQSDASLMTSVRKATSIDETAPKRKHVRSCIIFTWDHHTARPFWTAIKVQPLLANEVQTFKALITIHRVLQEGHKSALVDSQSEKGWLKTCERQYDGESSPKGYSDLIRDYVDYLLDKLSFHAQHPEFNGTFEYKEYISLRQVDDPNEGYETVYDMMNLQDHIDEFQKQLFSNFKRSNKNECRIAALVPLVQESYGIYRFLTSMLRALYSTVDAPETLEPLKHRYKSQHHRLRQFYADCSNLRYLTSLISVPRLPHDPPDLEGDDNIPDLPKRPASIAPQPTGASTIAPQPTGTSPSPPVEMNFPDTSDITPAYSEPEPIQDFWSDPTLDQQLAAQQAAQQAAQQQAELAAQQAAAQQAQLAAQQAAEMERQRMAAQQHQQALEAIQMAQAEQQRIAQEQLAQQQFQMQTQGQLAELEQQLLATRGQLEQSNVLLNQYDARVRTLENELSQAGVNLQEQIHQNDDLIESLKNQILTWKNKYEALAKLYTQLRQEHLDLLSKYKQIQLKASSAQEAIDKKEKMEREMKNKNLELADMILERDRARHELETMHRSQRDKQESTERELRLLQEKAASLERNKSSEVSNLLSRYNTEVAHLEDALHSKDRELANLGVELKSTENRYRQLLQEKEEELEIQKAAVDESLLQLSKLQLDRNDIDQAMDTQIDELLKSQLEKLDDIVDSVLATGIQRLDTSLYELDSPMHAGNQYATPEFILSTIENASNNATDFSTAFNNYFADGPNADHSEVINGVNLFSTAIYEVANNAKGLSRTTGDDQGSDRFVGLSRDLVNMAKRFLSSLFSVNTRKMDVNVKTDLVIGENIELQRYLQQLTQYSEKFLNKESENTVGLLNAPGENIEELVDNQLAETAQAIQQAILRLQNIAAKPKDDSLSPSELQVHDSLLSASIAITEAIARLIKAATASQAEIVAQGRGSSSRGAFYKKHNRWTEGLISAAKAVARATTTLIETADGVVNGTSSFEHLIVACNGVSAATAQLVAASRVKANFASKVQDHLEDAAKAVTEACKALVRQVESVALKAKEVQHEDFSSLGVHEYRRKEIEQQVQILKLENDLVAARRRLFDMRKTSYHVAEE
|
Required for cellular morphogenesis and polarization of the cortical cytoskeleton. Required for establishment of new polarized growth zones where it acts in actin organization. Involved plasma membrane internalization and is essential for fluid-phase endocytosis.
|
Q9P6L5
|
E8MJ15
|
LDH1_BIFL2
|
L-lactate dehydrogenase 1
|
Bifidobacterium
|
MVTMNRNKVVIVGTGQVGATAAFGIVTHGLCNELVLIDCSAAKALGEARDLDDGSEFQDRHVKVRAGDYADCKDADIVVITVGRKPPANSNRMAELGFTVGLVGEVVDNVMASGFDGVIVMVSNPVDVMAWYAWKRSGLPRTQVLGTGTALDTSRLKTIIGEETGLDPRNVGGFVMGEHGDSQFTAWSTVSLGGKPFARFLADNQDRFASVSTTEIEEKTRTRGNEIVAAKGGTNFGIASTVAGIVQTILWDERRIVPVSTLLDGEYGEHDVFLGVPTELRANGANEIVELDLSEDERAKLHHSAELVREHCEGLL
|
Catalyzes the conversion of lactate to pyruvate.
|
E8MJ15
|
Q9PE82
|
ATPD_XYLFA
|
F-type ATPase subunit delta
|
Xylella
|
MSQALTLARPYARAAFAIACEKGKCMQWSQALTFSAQVANNPIAAALLCHPQIDHEQAAALLSPEGADPAYVRFLEVIAEAHRLDVLLQVAGLYEKLRAEAEHVIKAKITSAIELAPNELNNIVTALKKRFDCEIEVTTGVDHSLIGGAVIDTGNVVIDGSIKSKLTRLQASLTH
|
This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction.
|
Q9PE82
|
Q6B929
|
PSBA_GRATL
|
Photosystem II Q(B) protein
|
Agarophyton tenuistipitatum
|
MTATLERRESASLWERFCTWITSTENRLYIGWFGVLMIPTLLTATSVFIIAFVAAPPVDIDGIREPVAGSLLYGNNIISGAIIPSSAAIGIHFYPIWEAASLDEWLYNGGPYQLIVLHFLLGVSCYIGREWELSYRLGMRPWISVAFTAPVAAAAAVFLVYPIGQGSFSDGMPLGISGTFNFMLVFQAEHNILMHPFHQLGVAGVFGGSLFSAMHGSLVTSSLIRETTENESANNGYKFGQEEETYNIVAAHGYFGRLIFQYASFNNSRSLHFFLGLWPVVGIWFTAMSVSTMAFNLNGFNFNQSVVDSQGRVINTWADILNRANLGMEVMHERNAHNFPLDLASSNSLPVSLVAPSVNG
|
Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbA) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors.
|
Q6B929
|
Q3A526
|
HLDE_SYNC1
|
D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase
|
Syntrophotalea
|
MDRTNIENFLSRLKDLRALVIGDLMLDEYLWGRTERISPEAPVQVVDVVREDLRLGGAGNVINNLVTLGCQVHVASVLGEGHDGLLLRRRLEEKQVGIEGLQFDAKRTTSRKTRILASGQQMMRFDRESRCPIDATQEAVLAEFVSNSADRFDVILVSDYLKGVLTEDLLQSVIAVGKQKGIPVVIDPKGNDYAKYRGATLLTPNRKETEVASGISIVDEESLRLAARTLMQRIDLETLMVTRSEEGISIFFRNGEEVHLPTQAREVYDVTGAGDTVLSLVGLGLAGGLPVSEAAALANIGAGIVVGKVGTSTVNVEELHEAMAHHALEYDSKIRLRESLRDVLEVERRRGKTVVFTNGCFDLLHVGHVKYLQKARRLGDLLVLGLNSDASIRRLKGPSRPLISEQERAHILAALSCIDYVVVFDEDTPLELIDTLRPDILVKGGDYTPETVVGKDLVESYGGRVELIDLVDGRSTTNIIERILDRYEQG
|
Catalyzes the ADP transfer from ATP to D-glycero-beta-D-manno-heptose 1-phosphate, yielding ADP-D-glycero-beta-D-manno-heptose.
|
Q3A526
|
B9MLX4
|
SPEH_CALBD
|
S-adenosylmethionine decarboxylase alpha chain
|
Caldicellulosiruptor
|
MHALGRHIIAELYGCDKEVLNNRELIEKIMVESALKAGAEVREVAFHKFSPQGVSGVVVISESHLTIHTWPELGYAAVDVFTCGERVDPWQACNYITEMLKASHMTTTEVKRGLFEQPVKVANL
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Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine.
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B9MLX4
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Q74DB5
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ACCA_GEOSL
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Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha
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Geobacter
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MAAQYYMEFEKPVVELEKKVQELAELAGTNAELAGEVTKLEKKVDRMREVIFSNLSRWQTVQVARHIERPFTLDYLNLIFTDFTELHGDRLFGDDHAIVAGLAKLDGEPVVVIGHQKGRDTKEKVYRNFGMPNPEGYRKALRIMELAERFRLPIITFVDTPGAFPGIGAEERGQAEAIARNLREMAALTVPIIVVVTGEGGSGGALAIAVGDRVLMLQYSIYAVISPEGCAAILWSDGTKGEQAAEALKLTAKDLKELEVIDEIVPEPLGGAHRDHEAMARTLHEAIARQLKELKAIPAEQLVEERYQKFRKMSRFIEG
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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.
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Q74DB5
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C5C0H6
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RL6_BEUC1
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50S ribosomal protein L6
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Beutenbergia
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MSRIGKIPVQVPSGVDVDIADRVVTVKGPKGTLTHRVPAPIVVARGDDGALVVTRPDDERTSRSLHGLTRTLLANLVTGVTQGYQKNLEIVGTGYRVTAKGSSLEFALGFSHPVTVSAPEGITFAVESPTKFSVAGIDKQQVGEVAANIRKIRKPEPYKGKGVRYAGEQVRRKVGKAGK
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This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center.
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C5C0H6
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Q96JF0
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SIAT2_HUMAN
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Sialyltransferase 2
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Homo
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MKPHLKQWRQRMLFGIFAWGLLFLLIFIYFTDSNPAEPVPSSLSFLETRRLLPVQGKQRAIMGAAHEPSPPGGLDARQALPRAHPAGSFHAGPGDLQKWAQSQDGFEHKEFFSSQVGRKSQSAFYPEDDDYFFAAGQPGWHSHTQGTLGFPSPGEPGPREGAFPAAQVQRRRVKKRHRRQRRSHVLEEGDDGDRLYSSMSRAFLYRLWKGNVSSKMLNPRLQKAMKDYLTANKHGVRFRGKREAGLSRAQLLCQLRSRARVRTLDGTEAPFSALGWRRLVPAVPLSQLHPRGLRSCAVVMSAGAILNSSLGEEIDSHDAVLRFNSAPTRGYEKDVGNKTTIRIINSQILTNPSHHFIDSSLYKDVILVAWDPAPYSANLNLWYKKPDYNLFTPYIQHRQRNPNQPFYILHPKFIWQLWDIIQENTKEKIQPNPPSSGFIGILIMMSMCREVHVYEYIPSVRQTELCHYHELYYDAACTLGAYHPLLYEKLLVQRLNMGTQGDLHRKGKVVLPGFQAVHCPAPSPVIPHS
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Transfers sialic acid from the donor of substrate CMP-sialic acid to galactose containing acceptor substrates. Has alpha-2,6-sialyltransferase activity toward oligosaccharides that have the Gal-beta-1,4-GlcNAc sequence at the non-reducing end of their carbohydrate groups, but it has weak or no activities toward glycoproteins and glycolipids.
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Q96JF0
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G5ECM9
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CPI2_CAEEL
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Cysele2
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Caenorhabditis
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MKAILVFALIAISIISVNAGMMTGGSVEQDASQKEYSDKAWKAVKGINDQASNNGPYYYAPIKVTKASTQVVAGISTKLEVLVGESNCKKGELQAHEITSSNCQIKDGGSRALYQVTIWEKPWENFEQFTVEKIRDVTADEQF
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Cysteine protease inhibitor which inhibits members of the peptidase C1 family . Does not inhibit asparaginyl endopeptidase . Required for the uptake and/or processing of yolk proteins during the development of oocytes, probably by regulating the catalytic activity of cysteine proteases cpl-1 and cpz-1 . May play a protective role against exogenous cysteine proteases derived from soil bacteria or fungi, or rotting fruits and vegetation .
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G5ECM9
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Q5M6L8
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DNAA_STRT2
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Chromosomal replication initiator protein DnaA
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Streptococcus
|
MTEKEHFFWNKLLELAKEELTQATFDYYVLDTKLIKIQDNVATILLEEVKKLFWEKNMQSFILMTGFEVYNSEIKVEYVFDEALVSETKPTLANNDFSNKREQQTPDLPTLNSDLNSKYTFDNFIQGDENRWSVAASLAVADSPGATYNPLFIYGGPGLGKTHLLNAIGNKVLHDNPQARIKYITAENFINEFVLHIRLDKMDELKLKYRHLDVLLIDDIQSLAKKSTQATQEEFFNTFNVLHDNNKQIVLTSDRNPDQLNEMEERLVTRFKWGLTVNITPPDFETRVAILTNKIMDYDYHFPPETIEYLAGQFDSNVRDLEGALKDISLVANVRQLDTITVEVAAEAIRARKIDGPKLTLIPIEDIQSEVGKFYNVTVKEIKATKRTQNIVLARQVAMYLAREMTDNSLPKIGKEFGGRDHSTVLHAYNKIKNMLAQDDSLRIEIDTIKNKIK
|
Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids.
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Q5M6L8
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Q54SP2
|
FORB_DICDI
|
Formin-B
|
Dictyostelium
|
MFFKGKKKDKEKEKSHGNIGNVISVENKTGSQSNLHVEQNLSNEDLKIQFSQLLYELGVPEAKRVEMELWSNDKKWMLLVQNKDKIKENEEKMKQKGSLYETPQFYLSLLRENASIQKTISDLKVSLASNKLSWIDSFIGLSGFDEILKIFQTFQLKPEKNSIDFLILFDCVNIIKSILNSQSGVKSVMTTSHTFKVLVLCLDQSYPPELRNAVLQLTAALTLLPTVGHSYVLEAIENFKVSNREKVRFQTIIEGAKSVSNTQLHYEYLTSFMNLVNSIVNSPADLQVRIGLRSEFTALKLIELISNSKGVSEDLDTQINLFFECMEEDNDEVGAHYKEVNIRSPSEVSTKIDTLLQSHPALHHHFISIIKGLYTLASTQSDLGGSMWNILDESVGLILKDPSKESQLEKLQNENNNLKLQLSEIKLNNSNNNNNNNNSNNNNNDSNVSTPNINTGSPLLPPQQYQDLEQKLQLTQNEKNESQNKVKQLESEIKGLNSTLTGLQLKVTKLEADLLSVSVTTPPSDTNGTTSPPIEAPSSPSLGAPPPPPPPPPAPPVSGGGPPPPPPPPPPSSGGGPPPPPPPPSSGGPPPPPPPPGGMKKPGAPAVPNLPPKKSSVPSVKMVGLQWKKVNNNVIENSIWMNVKDYNLNDQFKQLEELFQVKKPTATTPTAPVGGASNVAVGGGSGSKSIVSTPTISILDPKRSQAIMIMLSRFKISFPDLSKAITNLDESKLNLEDAKSLLKFVPSSEEIELLKEEDPSCFGKPEQFLWELSKINRISEKLECFIFKQKLSTQIEELTPDINALLKGSMETKNNKSFHQILEIVLSLGNFINGGTPRGDIYGFKLDSLSGLLDCRSPSDSKVTLMTWLIQFLENKHPSLLEFHQEFTAIDEAKRVSIQNLRSEVASLKKGLTLLTNEVEKSEGASKTILSGFVGKSTDAVTLIEKQFNTALESFNSTVQFYGEDVKTSSPEEFFQHVSKFKNEFKRTIESIQKERENVQKLAARKKAAASGPSVPSASGSSINIAPKSGVSPITPTSKSSISISQKPPQSTQPSISVQQQQQQHHGDDDDDIPQNGTFMDQLMSKMKGGEAIRASRRASQYVFTQNGAGGVGAIDALNAALKNKK
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Formins play an important role in the nucleation of actin and the formation of linear actin filaments.
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Q54SP2
|
P38217
|
IMB2_YEAST
|
Transportin
|
Saccharomyces
|
MASTWKPAEDYVLQLATLLQNCMSPNPEIRNNAMEAMENFQLQPEFLNYLCYILIEGESDDVLKQHYSLQDLQNNRATAGMLLKNSMLGGNNLIKSNSHDLGYVKSNIIHGLYNSNNNLVSNVTGIVITTLFSTYYRQHRDDPTGLQMLYQLLELTSNGNEPSIKALSKIMEDSAQFFQLEWSGNTKPMEALLDSFFRFISNPNFSPVIRSESVKCINTVIPLQTQSFIVRLDKFLEIIFQLAQNDENDLVRAQICISFSFLLEFRPDKLVSHLDGIVQFMLHLITTVNEEKVAIEACEFLHAFATSPNIPEHILQPYVKDIVPILLSKMVYNEESIVLLEASNDDDAFLEDKDEDIKPIAPRIVKKKEAGNGEDADDNEDDDDDDDDEDGDVDTQWNLRKCSAATLDVMTNILPHQVMDIAFPFLREHLGSDRWFIREATILALGAMAEGGMKYFNDGLPALIPFLVEQLNDKWAPVRKMTCWTLSRFSPWILQDHTEFLIPVLEPIINTLMDKKKDVQEAAISSVAVFIENADSELVETLFYSQLLTSFDKCLKYYKKKNLIILYDAIGRFAEKCALDETAMQIILPPLIEKWALLSDSDKELWPLLECLSCVASSLGERFMPMAPEVYNRAFRILCHCVELEAKSHQDPTIVVPEKDFIITSLDLIDGLVQGLGAHSQDLLFPQGTKDLTILKIMLECLQDPVHEVRQSCFALLGDIVYFFNSELVIGNLEDFLKLIGTEIMHNDDSDGTPAVINAIWALGLISERIDLNTYIIDMSRIILDLFTTNTQIVDSSVMENLSVTIGKMGLTHPEVFSSGAFANDSNWNKWCLSVNALDDVEEKSSAYMGFLKIINLTSTEVTMSNDTIHKIVTGLSSNVEANVFAQEIYTFLMNHSAQISAINFTPDEISFLQQFTS
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Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for arginine/glycine-rich nuclear localization signals (rg-NLS) and PY-NLS in cargo substrates. Its predominant cargo substrate seems to be mRNA-binding proteins. Required for nuclear transport of NAB2, HRP1/NAB4 and TFG2. Mediates docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to repeat-containing nucleoporins . The complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism . At the nucleoplasmic side of the NPC, GTP-Ran binding leads to release of the cargo. Efficient GTP-Ran-mediated substrate release requires RNA . The importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus .
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P38217
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P81824
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VSP1_BOTJA
|
Snake venom serine protease
|
Bothrops
|
NSLVIVVGGRPCKINVHRSLVLLYNSSSLLCSGTLINQEWVLTAAHCDSKNFKMKLGVHSIKIRNKNERTRHPKEKFICPNRKKDDVLDKDIMLIRLNRPVSNSEHIAPLSLPSSPPSVGSVCYVMGWGKISSTKETYPDVPHCAKINILDHAVCRAAYTWWPATSTTLCAGILQGGKDTCEGDSGGPLICNGLQGIVSGGGNPCGQPRKPALYTKVFDYLPWIESIIAGTTTATCP
|
Snake venom serine protease that induces platelet aggregation through activation of protease-activated platelet receptors (PAR1/F2R and PAR4/F2RL3). On F2R, the cleavage occurs at Arg41-Ser42 (like thrombin cleavage), and Arg46-Asn47. In normal condition of hemostasis, the cleavage of the Arg41-Ser42 bond liberates a new N-terminus that functions as an agonist. However after envenomation, the cleavage of Arg46-Asn47 bond degrades this potential agonist. This may explain why the snake protease is less potent than thrombin in causing platelet aggregation and release reaction. On F2RL3, a thrombin-like activity has also been proven by calcium release from lung fibroblasts transfected with this receptor. Possesses amidolytic activities.
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P81824
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P33782
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FAEH_ECOLX
|
K88 minor fimbrial subunit FaeH
|
Escherichia
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MKITHHYKSLLSAIISVALFYSAAPHADILDGGEIQFNGFVTDDAPKWTWQISSPDQTWAVDTADARTENGQLVFDLSDKGPLPFLEGYLYEVAERGGPGFTPFITFSSNGRPFAVKEGSDTSVQRFRASVPVRDPETGNVSGQLSFTLNQGMAVSTGKQEEGASTPSGMSLVSGQSVTDVQSGSLPQGLKNRLSALLLMNKGFGNGMSAVDNGQVITQGVLADGRVMNLAAAYASAVSDFELRLPAEGTPARWQAGLNVTVTVQ
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K88 minor fimbrial subunit, plays an essential role in the biogenesis of the K88 fimbriae. Fimbriae (also called pili), are polar filaments radiating from the surface of the bacterium to a length of 0.5-1.5 micrometers and numbering 100-300 per cell. They enable bacteria to colonize the epithelium of specific host organs.
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P33782
|
Q97NG0
|
G6PI_STRPN
|
Phosphohexose isomerase
|
Streptococcus
|
MSHIKFDYSKVLDKFVAPHEVEYMQSQVTAADELIRKGTGAGSDFLGWLDLPEKYDREEFDRILKAAEQIKSDSDVLVVIGIGGSYLGAKAAIDFLNHHFANLQTKEERKAPQILYAGNSISSTYLADLVEYVADKDFSVNVISKSGTTTEPAIAFRVFKELLVKKYGQEEANKRIYATTDRQKGAVKVEADANGWGTFVVPDDIGGRFSVLTAVGLLSIAASGADIKALMEGANAARKDYTSDKISENEAYQYAAVRNILYRKGYATEILVNYEPSLQYFSEWWKQLAGESEGKDQKGIYPTSANFSTDLHSLGQFIQEGTRIMFETVVRVDKPRKNVLIPTLEEDLDGLGYLQGKDVDFVNKKATDGVLLAHTDGDVPNMYVTLPEQDAFTLGYTIYFFELAIALSGYLNAINPFDQPGVEAYKRNMFALLGKPGFEELSKELNARL
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Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
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Q97NG0
|
Q7VDB2
|
SYE_PROMA
|
Glutamyl-tRNA synthetase
|
Prochlorococcus
|
MKVRVRLAPSPTGSLHIGTARTALFNWLFAQRNKGSFLIRIEDTDKERSKDEFTSNILEGLQWLGLKWDEAPIIQSKRIHEHKEAIKSLINKGLAYRCFATEEELQTMRDAQINSGEAPRYDNRHRKLTKEQEQKFIKDGRSAVIRFRIEDEESVHWNDMVRGPIHWNSKDLGGDMVISRRAPANEIGDPLYNLVVVLDDAAMEITHVIRGEDHIANTAKQLLLYKALGFKEPSFAHTPLILNKDGRKLSKRDGVTSISDFKTMGYTSQAMTNYMTLLGWSPPEGMGEKFTLKESSSVFDFDRVNNAGAKFDWDKLQWLNSQEIHNWSNEKLLDSLIPLWTKEGWNLSSKDWGLKLVHLIKPSLILINDGIEESRVFFEEPLLKKDAIQQLEIPRAKEALKFICRKLEETPWHGKENEIAIELITSCSKSLDIKKGIIMKSLRAALLGTLQGPDLITSWGLLAMMENDQARIKRCL
|
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).
|
Q7VDB2
|
C8VJW1
|
HXNP_EMENI
|
Nicotinate catabolism cluster protein hxnP
|
Aspergillus subgen. Nidulantes
|
MGATATDIEKVPSAGTPDEPKAGETNVYVDTEAEKSFVRKVDFFVLPMLCLMYFFDCMDRSNLANAKTDGLEEDINLKGNEYSLLILLFYIPFGLFDLPWNLLIKRYSARIMLSLRRYAVTVVWGICALCQCAANNFGGLLAIRIILGVFEAGFFAGSTFYFTLFYTRNEMGFRLAVLQSFAVLASAFSGLISFGLFQINHSAVKGWQWLFIVEGAMTLIIGVIGFWWLPDTAQSAWFLTQRERDAASARLLRDTSAEIETKLELKAAFQTWSDWKFPIWAVITFSYPVAYATAMNFFPIIVARLGYSVVKTNLWTVAPNLVGAVVLLVVAKSSDIFRERSLHIIFSLTVSLVGMLILASIDVSHNKGVSYFACFLLASGAYIPTCLVHAWHNNNNTNENSRAANTGFFVGLGNIAGVLSAATFRTEYAPKYVPTLVATCACNGVCILATAFMGTWMRLENRRKDKEQGARIVAGQVETRMLADGEKSPEWRYFL
|
Major facilitator-type transporter, part of the hnx cluster involved in the purine degradation . The nicotinate hydroxylase hnxS accepts nicotinate as a substrate and catalyzes the first step of nicotinate catabolism . The major facilitator-type transporters hxnP and hxnZ are probably involved in the uptake of nicotinate-derived metabolites, and the oxidoreductases hxnT and hxnY in the further metabolism of 6-OH nicotinic acid .
|
C8VJW1
|
Q98PZ2
|
RL14_MYCPU
|
50S ribosomal protein L14
|
Mycoplasmopsis
|
MLQELSVAKVADNSGAKEVGIIRNLGGSVKKSSNIGDVVICSVKKAIPNGIVKKGQVVKAVIVRTKYGIKRENGQHVSFDDNAVVIIKEDKSPRGTRVFGPVARELREKGYLKIVSLAPEVL
|
Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome.
|
Q98PZ2
|
Q9LI77
|
GATA_ARATH
|
Glutamyl-tRNA(Gln) amidotransferase subunit A, chloroplastic/mitochondrial
|
Arabidopsis
|
MLSTLQPPRSLSLLPLRRFQISKTIVSAASSKTIDTSVISPPQSQILTTRRSLLSGETTAVEIAKSYLSRIRLTEPQLKCFLHVSENVLKDAQEIDQRIAKGEELGPLAGVLIGVKDNICTQGMPSTAASRILEHYRPPFDATAVKKIKELGGIVVGKTNMDEFGMGSTTEASAFQVTANPWDLSRVPGGSSGGSAAAVAARQCMVSLGSDTGGSVRQPASFCGVVGLKPTYGRVSRFGLMAYASSLDVIGCFGSTVADAGMLLHAISGYDRFDSTSSKQDVPEFQSQFLSVDHFESKPLNGVKVGIIRETLEDGVDSGVRSATQEAASHLEALGCILTEVSLPSFSLGLPAYYVIASSESSSNLSRYDGVRYGNQVMAEELNKLYECSRGEGFGGEVKMRILMGTYALSAGYYDAYYKRAQQVRTLIRKDFKAALEQNDILISPAAPSAAYKIGEKKDDPLAMYAGDIMTVNVNLAGLPAMVLPCGLVEGGPSGLPVGLQMIGAAFDEEKLLKVGHIFEQTLKGSSFVPPLLANVA
|
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).
|
Q9LI77
|
Q5HKZ5
|
CYSH_STAEQ
|
Thioredoxin-dependent 5'-adenylylsulfate reductase
|
Staphylococcus
|
MSIERITYDNFQNDPFINELDINDETKGAYEILKWAYQTYENDIVYSCSFGAESMVLIDLISQIKPDAQIVFLDTDLHFQETYDLIDRVKDKYPQLRIKMKKPELTLEEQGEKYNPALWKNDPNQCCYIRKIKPLEDVLSGAVAWISGLRRAQSPTRAHTNFINKDERFKSIKVCPLIYWTEEEVWSYIRDKDLPYNELHDQNYPSIGCIPCTSPVFDSNDSRAGRWSNSSKTECGLHVTDKP
|
Catalyzes the formation of sulfite from adenosine 5'-phosphosulfate (APS) using thioredoxin as an electron donor.
|
Q5HKZ5
|
B3MIF1
|
EIF3C_DROAN
|
Eukaryotic translation initiation factor 3 subunit 8
|
Sophophora
|
MSRFFANGSDSESESSEEEVQATNFNKASAFQFSDDEEEVKRVVRSTKEKRYENLTNIIKTIRNHKKIKDIPNTLSSFEDLTKAYTKALPVISKEENGITPRFYIRCLAELEDFINEVWEDREGRKNLSKNNSKSLGTLRQKVRKYIKDFEDDLSRFREAPDQESEAEDEEAAQDSDGGDAGDDSDAGIKREPAEAAPKVAKTVPAKAAPADDDDSDDSIDWDSDSETETESSDDENQYQNMRERFLKRTTEKEEKDDDKRKDKRKEQKIKIRKRPEDDEDGEWETVVKGHVVEKPKMFEKDAEIDIPLVLAKLVEIMSARGKKRTDRRLQIDLLFELRDISDQHNLGTAVSVKIHFNIISAIFDYNQKISEPMKLEHWALLLEVMQSMLKLLLVNPDIHMSESVAEEHEELATSPFYVRGCPLAAVERLDDEFTKLLKECDPHSNDYVSRLKDEVNVVKTIELVLQYFENDGNNNERCRIYLRKIEHLYYKFDPEVLKKKRGEIPQNTQTSVDVMDRLCKFIYAKDDTDRIRTRAILAHIYHHAMHDNWFQARDLVLMSHLQDNIDAADPATRILYNRMMANLGLCAFRQENIKDAHHCLVDLMVTGKPKELLAQGLLPQRQHERSAEQEKIEKQRQMPFHMHINLELLECVYLVSAMLLEIPYIAAHEFDARRRMISKTFYQQLRSSERQSLVGPPESMREHVVAAAKAMRCGNWQACANFIVNKKMNTKVWDLFYESDRVREMLTKFIKEESLRTYLFTYSNVYTSISIPSLAQMYELPVQKVHSIISKMIINEELMASLDDPTETVVMHRSEPSRLQALAMQFVDKVTNLVDVNEKVFDMKQGNFFQRGNMGNRGDRGYNRNQDGNWGGQLRDIKRIRGQRIQRGRKHQQQQQQQVQTIDEE
|
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.
|
B3MIF1
|
B8DJ66
|
THIM_DESVM
|
4-methyl-5-beta-hydroxyethylthiazole kinase
|
Desulfovibrio
|
MPHTEHIWRNVDAVRRQAPLVHSITNFVVMNVTANALLAAGASPIMAHAREEMAELVNIVSSLVLNIGTLSAPWIDSMFLAGAAAHERGIPVVLDPVGAGASTLRTTTAAQLMERVRPAIVRGNGSEIMALAGAAGATRGVDSTRDAHAAADSARALSRRHHCVTVVSGPVDLVTDGDEEVLITGGHELMPRVTGMGCTATVLVAAHAAVAASPLEGAVSGMAAMSAAGSMAAERAAGPGSFAMHFIDALYALSEADIRARVRVGRP
|
Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ).
|
B8DJ66
|
B1XN08
|
CYSH_SYNP2
|
PAdoPS reductase
|
unclassified Synechococcus
|
MGGMMPDLDLATVNEKLSEANAVEVVQWASQTFPEGLIMSTSFGIQSAVMLHLVTQVIPDIPVVWIDTGYLPEATYRFAEELGDRLNLNLKVYQSPLSPARMEALYGKLWEQDNIEAFNRYDYIRKVEPMQRALKELNAKAWLAGLRKGQTDHRKTLGYVAKQGKQYKIHPILTWTSKDVYEYLMAHDLPYHPYFDKGYVTVGDWHSSRPLMAGDESERDTRFRGLKQECGLHLPSTSEEAQSLDSSGL
|
Catalyzes the formation of sulfite from phosphoadenosine 5'-phosphosulfate (PAPS) using thioredoxin as an electron donor.
|
B1XN08
|
Q0KCT2
|
TPIS_CUPNH
|
Triose-phosphate isomerase
|
Cupriavidus
|
MRQKLVIGNWKMHGSLAANAALLEGIKAGAAKATLAVCAPFPYLAQCQALLNGSQVAWGAQDVSAEARGAFTGEVSASMVGEFGCTYVLVGHSERRTYHGETDQTVAAKALRALEFGIVPVVCVGETLAQREAGETEAVVGRQLQAVLDALTVEQLSRVVLAYEPVWAIGTGKTATSEQAQAVHAFLRGQVAARDAGVAERMAILYGGSVKPDNAAELFSMTDIDGGLIGGASLKSADFLAIGNA
|
Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
|
Q0KCT2
|
Q99315
|
YG31B_YEAST
|
Integrase p58
|
Saccharomyces
|
MSFMDQIPGGGNYPKLPVECLPNFPIQPSLTFRGRNDSHKLKNFISEIMLNMSMISWPNDASRIVYCRRHLLNPAAQWANDFVQEQGILEITFDTFIQGLYQHFYKPPDINKIFNAITQLSEAKLGIERLNQRFRKIWDRMPPDFMTEKAAIMTYTRLLTKETYNIVRMHKPETLKDAMEEAYQTTALTERFFPGFELDADGDTIIGATTHLQEEYDSDYDSEDNLTQNGYVHTVRTRRSYNKPMSNHRNRRNNNPSREECIKNRLCFYCKKEGHRLNECRARKAVLTDLELESKDQQTPFIKTLPIVHYIAIPEMDNTAEKTIKIQNTKVKTLFDSGSPTSFIRRDIVELLKYEIYETPPLRFRGFVATKSAVTSEAVTIDLKINDLHITLAAYILDNMDYQLLIGNPILRRYPKILHTVLNTRESPDSLKPKTYRSETVNNVRTYSAGNRGNPRNIKLSFAPTILEATDPKSAGNRGDSRTKTLSLATTTPAAIDPLTTLDNPGSTQSTFAQFPIPEEASILEEDGKYSNVVSTIQSVEPNATDHSNKDTFCTLPVWLQQKYREIIRNDLPPRPADINNIPVKHDIEIKPGARLPRLQPYHVTEKNEQEINKIVQKLLDNKFIVPSKSPCSSPVVLVPKKDGTFRLCVDYRTLNKATISDPFPLPRIDNLLSRIGNAQIFTTLDLHSGYHQIPMEPKDRYKTAFVTPSGKYEYTVMPFGLVNAPSTFARYMADTFRDLRFVNVYLDDILIFSESPEEHWKHLDTVLERLKNENLIVKKKKCKFASEETEFLGYSIGIQKIAPLQHKCAAIRDFPTPKTVKQAQRFLGMINYYRRFIPNCSKIAQPIQLFICDKSQWTEKQDKAIDKLKDALCNSPVLVPFNNKANYRLTTDASKDGIGAVLEEVDNKNKLVGVVGYFSKSLESAQKNYPAGELELLGIIKALHHFRYMLHGKHFTLRTDHISLLSLQNKNEPARRVQRWLDDLATYDFTLEYLAGPKNVVADAISRAVYTITPETSRPIDTESWKSYYKSDPLCSAVLIHMKELTQHNVTPEDMSAFRSYQKKLELSETFRKNYSLEDEMIYYQDRLVVPIKQQNAVMRLYHDHTLFGGHFGVTVTLAKISPIYYWPKLQHSIIQYIRTCVQCQLIKSHRPRLHGLLQPLPIAEGRWLDISMDFVTGLPPTSNNLNMILVVVDRFSKRAHFIATRKTLDATQLIDLLFRYIFSYHGFPRTITSDRDVRMTADKYQELTKRLGIKSTMSSANHPQTDGQSERTIQTLNRLLRAYASTNIQNWHVYLPQIEFVYNSTPTRTLGKSPFEIDLGYLPNTPAIKSDDEVNARSFTAVELAKHLKALTIQTKEQLEHAQIEMETNNNQRRKPLLLNIGDHVLVHRDAYFKKGAYMKVQQIYVGPFRVVKKINDNAYELDLNSHKKKHRVINVQFLKKFVYRPDAYPKNKPISSTERIKRAHEVTALIGIDTTHKTYLCHMQDVDPTLSVEYSEAEFCQIPERTRRSILANFRQLYETQDNPEREEDVVSQNEICQYDNTSP
|
Integrase (IN) targets the VLP to the nucleus, where a subparticle preintegration complex (PIC) containing at least integrase and the newly synthesized dsDNA copy of the retrotransposon must transit the nuclear membrane. Once in the nucleus, integrase performs the integration of the dsDNA into the host genome.
|
Q99315
|
Q96GS4
|
BORC6_HUMAN
|
Lysosome-dispersing protein
|
Homo
|
MESSRGRPGPETDLLAVAEHQALVFGGGPGRTSSEPPAGLRVSGEEETENVGGANRHPRTSPKTSSCGVVHRPEREALENEPGPQGTLSGAGSRRGAPGAEHEPSLSSRHKNPAPPEGKPSSGRDCRRGGPGGGMDVEQQEEEDNDEEAAAGSRAGRSFSSRLQDSRSLDGLSEACGGAGSSGSAESGAGGGRRATISSPLELEGTVSRHGDLTHFVANNLQLKIRLSGAPPPPPSAPARPCPAPAPTPTPAIPPIDPEVLRDLERLSRELGGRVDRLLRGLGGAVQELTALSVGCIQTYRDAVDSLGEAVDMSIKGMYTLLARCEELERALQPVQGLARQVRDIRRTLEVLEALCK
|
As part of the BORC complex may play a role in lysosomes movement and localization at the cell periphery. Associated with the cytosolic face of lysosomes, the BORC complex may recruit ARL8B and couple lysosomes to microtubule plus-end-directed kinesin motor.
|
Q96GS4
|
A5F4V7
|
RL31_VIBC3
|
50S ribosomal protein L31
|
Vibrio
|
MKAGIHPEYKAVNATCSCGNSFVFNSTLGKDTMHLDVCDKCHPFYSGKQRIVDTGGRVERFNKRFGALSAKK
|
Binds the 23S rRNA.
|
A5F4V7
|
A9BDG0
|
MURG_PROM4
|
Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase
|
Prochlorococcus
|
MSCLLIAASGTGGHLFPALAVAEALPESWKVSWLGVSDRLESSLIPKKYQLSTIGVEGVQSRGIKRIVQIFKLLAATGSVICLIRRNRIQIVLTTGGYIAVPAVLAAKLTGKKVILHESNAIPGKATRLLGRLCDKVALGWPPAKKKLPGCKVTVTGTPVRKSFLMKNKLPSWAPSGPGPLIVVIGGSQGAVGLNDMVRAVLPFLLDQGCRIVHITGKNAQSKIIHTNLVEQPFSDDIPGLLQNADLVISRSGAGALSEFAVCEVPAILVPYPYAADNHQECNAIYASQFGAALIVHQHEPEGKALRNALERLLKKNLSQADTVENLLNLMRKGMAKMAVRDAHIHLMSLLKEAS
|
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).
|
A9BDG0
|
Q6UEG2
|
AFLN_ASPPU
|
Aflatoxin biosynthesis protein N
|
Aspergillus
|
MPEFSLLAGHFGTLKKTIQGMPSDATLHSIMLKISQQFSSGIFYINMWPFSGTWMVVSTPSAASQIQKLNLTKPVILRRPLETVTGGPSMMSMHGETWKKWRALFNPGFNPGYIIGLAPNITDEVATFWLSCAKGQQGEVFPLESLTTRLTVDSICSVVLDTQLHHQIKDHPLATALQRQIDWTTFGTTFNPLKRYLTIRPLVLWYNNKVMDRIIGGEVDRACRTPPDHPSKSVISLALREYLQEQASTNSTRSLAEFKRLVAPQLRVFLFAGRNTTSSTLIYSYYLLAQHPEVLAKIRAEHEDVLGADPAEAQGRIKEDVQLLNKLPYTTAVIKETLRLFPPSASMREGRPDAEIIGEDGQRYPTVGCNVWTLTVALHHNSDYWDQVENFIPERWLVGPEDPLYPVKGAWRAFEFGPRSCIGQTLAMLELRIALAMTIRQFDITPAYDEWDSIHPATTAKEVNGHRAYQAERGAGGAHTADGFPCRVKERC
|
Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of aflatoxins, a group of polyketide-derived furanocoumarins, and part of the most toxic and carcinogenic compounds among the known mycotoxins . The four major aflatoxins produced by A.parasiticus are aflatoxin B1 (AFB1), aflatoxin B2 (AFB2), aflatoxin G1 (AFG1) and aflatoxin G2 (AFG2) . The first step of the pathway is the conversion of acetate to norsolorinic acid (NOR) and requires the fatty acid synthase subunits aflA and aflB, as well as the PKS aflC . AflC combines a hexanoyl starter unit and 7 malonyl-CoA extender units to synthesize the precursor NOR . The hexanoyl starter unit is provided to the acyl-carrier protein (ACP) domain by the fungal fatty acid synthase aflA/aflB . The second step is the conversion of NOR to averantin (AVN) and requires the norsolorinic acid ketoreductase aflD, which catalyzes the dehydration of norsolorinic acid to form (1'S)-averantin . The norsolorinic acid reductases aflE and aflF may also play a role in the conversion of NOR to AVN . The cytochrome P450 monooxygenase aflG then catalyzes the hydroxylation of AVN to 5'hydroxyaverantin (HAVN) . The next step is performed by the 5'-hydroxyaverantin dehydrogenase aflH that transforms HAVN to 5'-oxoaverantin (OAVN) which is further converted to averufin (AVF) by aflK that plays a dual role in the pathway, as a 5'-oxoaverantin cyclase that mediates conversion of 5'-oxoaverantin, as well as a versicolorin B synthase in a later step in the pathway . The averufin oxidase aflI catalyzes the conversion of AVF to versiconal hemiacetal acetate (VHA) . VHA is then the substrate for the versiconal hemiacetal acetate esterase aflJ to yield versiconal (VAL) . Versicolorin B synthase aflK then converts VAL to versicolorin B (VERB) by closing the bisfuran ring of aflatoxin which is required for DNA-binding, thus giving to aflatoxin its activity as a mutagen . Then, the activity of the versicolorin B desaturase aflL leads to versicolorin A (VERA) . A branch point starts from VERB since it can also be converted to dihydrodemethylsterigmatocystin (DMDHST), probably also by aflL, VERA being a precursor for aflatoxins B1 and G1, and DMDHST for aflatoxins B2 and G2 . Next, the versicolorin reductase aflM and the cytochrome P450 monooxygenase aflN are involved in conversion of VERA to demethylsterigmatocystin (DMST) . AflX and aflY seem also involved in this step, through probable aflX-mediated epoxide ring-opening step following versicolorin A oxidation and aflY-mediated Baeyer-Villiger oxidation required for the formation of the xanthone ring . The methyltransferase aflO then leads to the modification of DMST to sterigmatocystin (ST), and of DMDHST to dihydrosterigmatocystin (DHST) . Both ST and DHST are then substrates of the O-methyltransferase aflP to yield O-methylsterigmatocystin (OMST) and dihydro-O-methylsterigmatocystin (DHOMST), respectively . Finally OMST is converted to aflatoxins B1 and G1, and DHOMST to aflatoxins B2 and G2, via the action of several enzymes including O-methylsterigmatocystin oxidoreductase aflQ, the cytochrome P450 monooxygenase aflU, but also the NADH-dependent flavin oxidoreductase nadA which is specifically required for the synthesis of AFG1 .
|
Q6UEG2
|
Q17103
|
MYC_ASTRU
|
c-myc
|
Asterias
|
ARVPDDDMNSLEDSDSMESCFAGEEEFYSSTLTPPTPSEDIWKKFELYPTPPLSPSHNPDDKESDRHPRHHQQDGDGSPSRSYQHLMDDDDLPLVNPQVPLLDLSSAPPIAALIQDCMWSSIIAEERRKLFMKSEKKHAEERATKKASTPSSGVMLPPLVPASEYGTSDCVDPSAVCPYPLSETRLDLFSSGTNTPSDSEEEIDVVTVEKKHHSVHKINTTRPYHKQSTKVRHQLHHRPISVALVGSLRGRPSTATILSIPIKKLKTEGNLEEVKQILQKSNLIRSSSGSSRGSSRGCSRNSSSRRVNQVSHPSSDSEDTEKRACHNVLERQRREDLRTSFLLLRDEVPELGTCDRAAKVVILKKATDYVSSLRDREETLRMDMATEKNRNLQLRRRLEALLAPLTL
|
Transcription factor that binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3'. Activates the transcription of growth-related genes.
|
Q17103
|
Q6D137
|
RS18_PECAS
|
30S ribosomal protein S18
|
Pectobacterium
|
MARYFRRRKFCRFTAEGVVEIDYKDIATLKNYITESGKIVPSRITGTRAKYQRQLARAIKRARYLSLLPYTDRHQ
|
Binds as a heterodimer with protein S6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit.
|
Q6D137
|
O95264
|
5HT3B_HUMAN
|
Serotonin receptor 3B
|
Homo
|
MLSSVMAPLWACILVAAGILATDTHHPQDSALYHLSKQLLQKYHKEVRPVYNWTKATTVYLDLFVHAILDVDAENQILKTSVWYQEVWNDEFLSWNSSMFDEIREISLPLSAIWAPDIIINEFVDIERYPDLPYVYVNSSGTIENYKPIQVVSACSLETYAFPFDVQNCSLTFKSILHTVEDVDLAFLRSPEDIQHDKKAFLNDSEWELLSVSSTYSILQSSAGGFAQIQFNVVMRRHPLVYVVSLLIPSIFLMLVDLGSFYLPPNCRARIVFKTSVLVGYTVFRVNMSNQVPRSVGSTPLIGHFFTICMAFLVLSLAKSIVLVKFLHDEQRGGQEQPFLCLRGDTDADRPRVEPRAQRAVVTESSLYGEHLAQPGTLKEVWSQLQSISNYLQTQDQTDQQEAEWLVLLSRFDRLLFQSYLFMLGIYTITLCSLWALWGGV
|
This is one of the several different receptors for 5-hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. This receptor is a ligand-gated ion channel, which when activated causes fast, depolarizing responses. It is a cation-specific, but otherwise relatively nonselective, ion channel.
|
O95264
|
P21894
|
SYAC_BOMMO
|
Alanyl-tRNA synthetase
|
Bombyx
|
MDTSMTGNEIRKTFIDFFIKKGHKYVHSSSTIPLDDPTLLFANAGMNQFKPIFLGSVDPNSDMAQYIRVVNTQKCIRAGGKHNDLDDVGKDVYHHTFFEMMGNWSFGDYFKKEICAWAWELLTDVFKLSRERLYVTYFEGDPSSGLEPDLECRNIWLNLGVPEAHILPGSMKDNFWEMGETGPCGPCSELHYDRIGDREAAHLVNMDDPDVLEIWNLVFIQFNRETDGSLKLLPTKHIDCGLGLERLVSVIQNKRANYDTDFFMPIFKAIENATGVRPYSGKVGVDDVDGIDMAYRVLADHARTLTIALSDGGCPDNTGRGYVLRRILRRAVRYASEKLNAKPGFFGSLVYTVVELLGDVFPEIKKDPDSIVHVINEEEVQFLKTLLRGRNLLYRTIEKLNNSKTLPGDVAWRLYDTYGFPIDLTQLMCEEKGLNVDMEGYEKSRKESQLVSQGKAAGQEDLIALDVHAISHLQDTGIPATDDSPKYNYLPSSTDKDALYTFAPCTAKIVALRKNKEFVSEISSGQECGVILDRTSFYAEQGGQIFDEGYMVKIDDETVEFTVKNVQVKGGYVLHAGKVEGILKVGDTLSLHIDTERRRLVMNNHTGTHVLNNVLRKVLGNDSDQRGSLVMPDRLRFDFTNKGPMTIKQIKDTENEIKEIIAKNKTVYANYTSLSEAKKINGLRAMFDEHYPDPVRVVSVGVPVEDLIKNPDAPTGFETSVEFCGGSHLHRTSHIGEYVIVSEEGIAKGIRRIVAVTGPEAIKAINKLSVLENEVNNVANFIKEQNESISHKEVSKKIVDLTNEISQAQISYWKKDELRNMLKNLKKQLDDKERAEKAIIITQVTEKAKELCLERKESKYIVSELKAFGNTKALDGALKQVKQFCPNSAAMFFSVDKDADKIYCLAAVPKSDVEKGLLASEWVQSVVDIIGGKGGGKAESAQASGNNPNSLNEAIQIANEYAKSKLN
|
Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain.
|
P21894
|
Q1LWB0
|
TXB1A_DANRE
|
Tax1-binding protein 1 homolog A
|
Danio
|
MSSSCNVGASAGGGGSVVMETSNFAHVIFQNVGKSFLPQAALECHYTLTPFITPHPKDWVGIFKVGWSSARDYYTFLWSPMPENYTEGSTVHRTIIFQGYYVPRSDGEFYQFCYVTHTGEIRGASTPFQFRPATPTGEELLTVEDDGNSDILVRVEEVQQECKELQKALRLLTQERDQLQEKQRQQNQELQKSLIEEKEEAQSRVRQLEQDLLKITQKAVLKETELDCLRDKLQKVISERDSLQTQLKNERDERELYKSHVRSAELENTKLSAELQMLKAVELNREVTIAQYQEELHRLRTERDTHPAETGLKEQLRQAEEQLQATRQQAAMLGSELRDASGGRDRTMTELYRVRQEAEELRAHLAEAQEECRHAQDQLDRMKNQTSQEMGRAGGGVGVASELEAELQKEVEELKLRLNMAAEHYKEKYRECQRLRRQVTKLTQQQETQQGDANRNDASTETTLELHTPDAETPSESYPAEIKTVARDVEKSRDEEGNEQEEEDEEEEECSLSVEAELACMEEKWREQCTINENLKLLLANEEKRFKTQVAEKDREVSALRESLVVVTKEKERLEKQYMREGTTRSRRLEVREPVVLRYPLPYPQDPPPLPLVPQQPAELQFGNPYLEQETRDGADGALSPEQTCRPPPLAPPPWGGPVVCSQPSRSLSPPDGLENPTEERPTGGDGEAPAVCEHQSLESNESHTSFCFDTRPDVHKQCPLCEVIFPPHFEQSSFERHVESHWRVCPVCSEQFPLDCQQQLYEKHVHTHFDGNVLNFDNFD
|
May have anti-apoptotic activity.
|
Q1LWB0
|
E5ASS2
|
FBID_MYCRK
|
3-phospho-D-glycerate guanylyltransferase
|
Mycetohabitans
|
MRCNGMSPVSVAQRNTGIWAVVPLKAPECAKTRLSGVLSHAARQALFFSMASHVIGTLRASPRIASLLVVTPSESTAEMARAAGAEILWGPPDEGMANACSRAMAHIAAAGGERVMFVPGDLPLLDGAAIDMLSRAPVDAIGMAPNRDGHGTNGLICRPGAIPLFFSGPSFSAHQNAARCAGIDVWIVRSREWALDVDLPADLEEFESSIKDAKRRVLCQI
|
Guanylyltransferase that catalyzes the activation of (2R)-3-phosphoglycerate (3PG) as 3-[(R)-glyceryl]-diphospho-5'-guanosine, via the condensation of 3PG with GTP. It is involved in the biosynthesis of a derivative of the hydride carrier cofactor coenzyme F420, 3PG-F420. Can also use (2S)-2-phospholactate (2-PL), with lower turnover, and has weak activity with phosphoenolpyruvate (PEP).
|
E5ASS2
|
Q9NUP1
|
BL1S4_HUMAN
|
Protein cappuccino homolog
|
Homo
|
MEGSFSDGGALPEGLAEEAEPQGAAWSGDSGTVSQSHSSASGPWEDEGAEDGAPGRDLPLLRRAAAGYAACLLPGAGARPEVEALDASLEDLLTRVDEFVGMLDMLRGDSSHVVSEGVPRIHAKAAEMRRIYSRIDRLEAFVRMVGGRVARMEEQVTKAEAELGTFPRAFKKLLHTMNVPSLFSKSAPSRPQQAGYEAPVLFRTEDYFPCCSERPQL
|
Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. Plays a role in intracellular vesicle trafficking.
|
Q9NUP1
|
Q1JG69
|
QUEA_STRPD
|
Queuosine biosynthesis protein QueA
|
Streptococcus
|
MNTNDFDFELPEELIAQTPLEKRDSSKLLIIDHRQKTMVDSHFDHIIDQLNPGDALVMNNTRVLPARLYGEKPDTHGHVELLLLKNTQGDQWEVLAKPAKRLKVGSQVNFGNGHLKATIIDELEHGGRIVEFSYDGIFLEVLESLGEMPLPPYIHEKLEDAERYQTVYAKENGSAAAPTAGLHFTTDLLKKIEAKGVHLVYLTLHVGLGTFRPVSVDNLDEHDMHSEFYSLSEEAAQTLRDVKQAGGRVVAVGTTSIRTLETIGSKFQGDIQADSGWTNIFIKPGYQFKVVDAFSTNFHLPKSTLVMLVSAFAGRDFVLEAYRHAVDEKYRFFSFGDAMFVN
|
Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
|
Q1JG69
|
Q8T116
|
HCYX_SCUCO
|
Hemocyanin subunit X
|
Scutigera
|
MKYCTESLILILAVIGCISAAINFKCPKGTAEEKHQKEIYDLVQRINRPLIPQFKEPNFPTSFLIKGKDPKEFFQAIGHLPKKEVFSLFDERHWDEAMTAYEYLYEAETLDDFIDIAKILYLHLNEDMFYYVFSFAVLYRKDTRNVRLPQVHDVYPDKFLKTDIINKIKQANYQGKQHPVIDATKEFHDLRNPVSYLHYFLEDIGMNSHHYHWHVMNSALRKAYPTEGEKKFYRKGELFYHMHHQMLNRYELERLSNGLPRCPTFENWDDPIAEGYASHLAVDRTGYRYTFRPDNLHVRDLPELTKDNMRVWRDRIFDAATSCSVLRENGSFVKICRTRFYGGLNILGNLIESNLRSINRMFYGNIHCYAHVIAARVTDPDGKYGQGNGVMYDVATSARDPLFYQWHKFLDHFFYEHLTKLPTNHLFHLQNPDVSITNLEIISNGRKNEIHTFWENDIMEISKGHSFTLNSDAKVKIQHLQHEKFEIHLTVQNDKGEDTDLFVRIFLLPLEDEESHELSLEEMVRMAVDIEKRVIPAKPGSNDIVISSRSIGAPANKFFGSFEERYISEDCNFHSHCGWPNYLLVPKGSSQGTPFAFVVMLTLAEDDFTPNMDDTCFCADSWSHCGSLFIQYPENVEMGFPFQPIIECTKEEFFALPNIAKQEVIIKFTGETKDSPLVIQLENDS
|
Hemocyanins are copper-containing oxygen carriers occurring freely dissolved in the hemolymph of many mollusks and arthropods.
|
Q8T116
|
Q92520
|
FAM3C_HUMAN
|
Interleukin-like EMT inducer
|
Homo
|
MRVAGAAKLVVAVAVFLLTFYVISQVFEIKMDASLGNLFARSALDTAARSTKPPRYKCGISKACPEKHFAFKMASGAANVVGPKICLEDNVLMSGVKNNVGRGINVALANGKTGEVLDTKYFDMWGGDVAPFIEFLKAIQDGTIVLMGTYDDGATKLNDEARRLIADLGSTSITNLGFRDNWVFCGGKGIKTKSPFEQHIKNNKDTNKYEGWPEVVEMEGCIPQKQD
|
May be involved in retinal laminar formation. Promotes epithelial to mesenchymal transition.
|
Q92520
|
Q9GV27
|
EIF3H_BOMMO
|
Eukaryotic translation initiation factor 3 subunit H
|
Bombyx
|
MASRAGSARRAPENEATIQYVQCDGLAVMKIVKHCHEESCSNMEVAQGALLGLVVENRLEITNCFPFPKHDDTMDEEEYQLDMMRRLRRVNVDHFHVGWYQSADVGNFLSLSLLESQYHYQTSIEESVVVIYDTKKSARGFLTLKAYRLTPQAIAMYKEGDYTPEALRNLKIGYENLFIEVPIVIRNSPLTNIMISELTEMIPEEEGSKFLDLGTASVLEGQLRSLMERVDELNQEAIKFNRYQQLVVRQQQDKHRWMVKRAQENAARAAKDETPLPEEDVNKLFKPHPVPPRLNPMIVAGQIDTYSQHISQFCSQSLAKLYLTQALQNAKEAKQNN
|
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.
|
Q9GV27
|
Q08747
|
UAF30_YEAST
|
Upstream activation factor 30 KDa subunit
|
Saccharomyces
|
MAELNDYSTMIDILLSDMDLETVTTKKVRMALKEVYAIDVESQGKAINKLIRKHLDLVKERPRFERSLEDLLKENATLAIELTKEITVSKRSSGEEKNDSETKGTHVEKKKGTVSKSPISTRKVTLSKSLASLLGEHELTRTEVVRRLWAYIKAHNLQNPNNKKEILCDEKLELILGKSTNMFEMHKILASHMTEPKKISDCPPLIQEVRRKEKPIVSDSEQSDTKGI
|
Nonessential component of the UAF (upstream activation factor) complex which interacts with the upstream element of the RNA polymerase I promoter and forms a stable preinitiation complex. Together with SPT15/TBP UAF seems to stimulate basal transcription to a fully activated level. UAF30 seems to play a role in silencing transcription by RNA polymerase II.
|
Q08747
|
Q9XIG2
|
PLM_ARATH
|
Protein PHLOEM UNLOADING MODULATOR
|
Arabidopsis
|
MTKGGLGIAAMSYVVIDYMRYVSPVWHSRLMPVLWSVLAIAVVTRVLFYKHWSKELRAAIPFLGSIVFLLCALLFEALCVRSVTAVLGLDWHRETPPLPDTGQWFLLALNESLPGTLVEILRAHIIGLHHFLMLFIMLGFSVVFDSVKAPGLGLGARYIFTMGVGRLLRAITFVSTILPSARPWCASARFNNVPSQPHRWAQKYYVPYANDPAAIRKLLHWDAAYADPGSYIGDYRADWGSMSFLSEFLRPSYSEGSSWFALLKKAGGGCNDLMYSGHMLVAVLTAMAWTEAYGGFSSAMIWLFVAHSAQREIRERHHYTVDCIVAIYVGILLWKMTGFIWSAERKTKQTKLEKIQNSLIHAAKDGDIETVRRLVEEIEVSSRVEKQSKVISNRTMTVFACATVITTLTIVILALTLTSDG
|
Catalyzes the biosynthesis of sphingolipids with very long-chain fatty acid (VLCFA) . Required for the formation of plasmodesmal cytoplasmic sleeve during the transition from type I to type II plasmodesmata to modulate post-sieve elements (SE) unloading and symplastic cell-to-cell molecular trafficking at the phloem pole pericycle (PPP)-endodermis interface in roots .
|
Q9XIG2
|
Q839E5
|
RL15_ENTFA
|
50S ribosomal protein L15
|
Enterococcus
|
MKLHELKPAEGSRQVRNRVGRGTSSGNGKTAGRGQKGQKARSGGGVRLGFEGGQTPLFRRLPKRGFTNINRKDYAVVNLDTLNRFEDGTEVTPVVLKEAGIVKNEKAGIKVLADGELTKKLTVKAAKFSKSAQEAIEAAGGSIEVI
|
Binds to the 23S rRNA.
|
Q839E5
|
A0A075B6X5
|
TVA18_HUMAN
|
T cell receptor alpha variable 18
|
Homo
|
MLSASCSGLVILLIFRRTSGDSVTQTEGPVTLPERAALTLNCTYQSSYSTFLFWYVQYLNKEPELLLKSSENQETDSRGFQASPIKSDSSFHLEKPSVQLSDSAVYYCALR
|
V region of the variable domain of T cell receptor (TR) alpha chain that participates in the antigen recognition . Alpha-beta T cell receptors are antigen specific receptors which are essential to the immune response and are present on the cell surface of T lymphocytes. Recognize peptide-major histocompatibility (MH) (pMH) complexes that are displayed by antigen presenting cells (APC), a prerequisite for efficient T cell adaptive immunity against pathogens . Binding of alpha-beta TR to pMH complex initiates TR-CD3 clustering on the cell surface and intracellular activation of LCK that phosphorylates the ITAM motifs of CD3G, CD3D, CD3E and CD247 enabling the recruitment of ZAP70. In turn ZAP70 phosphorylates LAT, which recruits numerous signaling molecules to form the LAT signalosome. The LAT signalosome propagates signal branching to three major signaling pathways, the calcium, the mitogen-activated protein kinase (MAPK) kinase and the nuclear factor NF-kappa-B (NF-kB) pathways, leading to the mobilization of transcription factors that are critical for gene expression and essential for T cell growth and differentiation . The T cell repertoire is generated in the thymus, by V-(D)-J rearrangement. This repertoire is then shaped by intrathymic selection events to generate a peripheral T cell pool of self-MH restricted, non-autoaggressive T cells. Post-thymic interaction of alpha-beta TR with the pMH complexes shapes TR structural and functional avidity .
|
A0A075B6X5
|
Q0C668
|
RIMM_HYPNA
|
Ribosome maturation factor RimM
|
Hyphomonas
|
MSADTKTQRLIPMGVLKGAHGVRGEVRVKSFTADPDALFTYGPLMDEAGKVLLTPITARPGKDHFIVRPKENLQKEDWDALRGCLLHASRDQLPEADEDEFYFEDLIGMPVYTVGEEPEARVRAVQNFGSGDLLEIEIPGAPATIYVPLTRADVPVIDMAAHRIVIPELSLWANQDEDDAS
|
An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Probably interacts with S19. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
|
Q0C668
|
P39885
|
TCMR_STRGA
|
Tetracenomycin C transcriptional repressor
|
Streptomyces
|
MDSAETDTPSTRSTPNGPGLRQRKLRRTRDQLIREALELFLAQGYEHTTVEQIAEAVEVHPRTFFRHFASKEEVALTPISAIDEAFLAALEVRPAGENPLQAMSGAFRAVLGRVRDGELEGVDGALHMAMMRLVERTPGLLAEYLRRSEEMEGRLARIIAAREGVDLDDDFRPRFIVAVFKAVGRVVSREWYLRADTDLEALSVAFESALDSLRPELFADWRRPGA
|
Represses transcription of the divergently oriented tcmR and tcmA (tetracenomycin C resistance and export) genes by binding to an intergenic operator region. This binding is inhibited by tetracenomycin C.
|
P39885
|
Q82JD2
|
PTA_STRAW
|
Phosphotransacetylase
|
Streptomyces
|
MTRSVYVTGIDRGDGRQVVELGVMELLTRQVDRVGVFRPLVHDGPDRLFELLRARYRLAQDPATVYGMDYHEASALQAEQGTDELMSTLVDRFHLVARDYDVVLVLGTDFADTQFPDELALNARLANEFGAAVIPVVGGRGQTAESVRAETRNAYRAYEGLGCDVLAMVVNRVAREDREELAARLDSLLAVPCYVLPDEPALSAPTVAQITHALGGKVLLGDDSGLARDALDFVFGGAMLPNFLNALTPGCLVVTPGDRADLVVGALAAHSAGTPPIAGVLLTLDERPSDEVLTLAARLAPGTPVVSVAGTSFPTAAELFSLEGKLNAATPRKAETALGLFERYVDTGDLLKRVSAPSSDRLTPMMFEHKLLEQARSDKRRVVLPEGTETRVLHAAEVLLRRGVCDLTLLGPVDQIRKKAADLGIDLGGSQLIDPVTSQLRDSFAEKYAQLRAHKGVSVELAYDVVADVNYFGTLMVQEGLADGMVSGSVHSTAATIRPAFEIIKTKPDTKIVSSVFFMCLADKVLVYGDCAVNPDPNAEQLCDIAVQSAATARQFGVEPRIAMLSYSTGTSGSGADVDKVREATELVRLRRDDLKIEGPIQYDAAVEPSVAATKLPGSDVAGQASVLIFPDLNTGNNTYKAVQRSAGAIAVGPVMQGLRKPVNDLSRGALVQDIVNTVAITAIQAQSPHEKATAQ
|
Involved in acetate metabolism.
|
Q82JD2
|
Q39Z66
|
DAPB_GEOMG
|
4-hydroxy-tetrahydrodipicolinate reductase
|
Geobacter
|
MVKIAVCGAAGRMGQRIIVAAKEAGCTVSGALERPGHELVGQDAGLIAGCGALGVAISDDLNAVVDGCDVLIDFTTPKVSLKNLEACALKKKAIVIGSTGFTPEERALAAELAKDIPAVLAPNMSVGVNVCFKILKDVAKTLGDDFDVEIVELHHNKKKDAPSGTAVRMGEVVAEALGRDYNKVANYHREGICGERTKEEIGMQTVRGGDIVGEHTVYFIGMGERIEISHRAMTRDMFSRGSVRAAQWVVGKAPGLYDMQDVLGLR
|
Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
|
Q39Z66
|
A2BQ26
|
CHLN_PROMS
|
Light-independent protochlorophyllide reductase subunit N
|
Prochlorococcus
|
MSKVEFNKETGPREVFCGLTSIVWLHRRMPDAFFLVVGSRTCAHLIQSAAGVMIFAEPRFGTAILEEKDLAGLADAHEELDRVVNDLIARRPEIKTLFLVGSCPSEVIKLDLATVAEKLNKRFLGQVRFVNYSGSGIETTFTQGEDGALKALIPLMESSNEEKLLLVGTLANNVEDRFKKIFKNLGISNIESFPPRQSTELPKIGKNTKVLLTQPYLSDTVRDLKHRGCEIISAPFPLGIEGSTEWFLAAAKAFKINELKVHEILSPLINRAKLALESHKEILKGKRLFLLPESQLEISLARFLHNECEMDLVEVGTPYLNKDLMKEEINLLPDNTKIVEGQHVEKQLDRVRESNPDLVVCGMGLANPLEAEGISTKWSIEMVFSPIHGIDQAADLAGLFSKPLRRNQILTTKTLVTH
|
Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex.
|
A2BQ26
|
Q09MH8
|
PSAA_CITSI
|
PsaA
|
Citrus
|
MIIRSPEPEVKILVDRDPVKTSFEEWAKPGHFSRTIAKGPETTTWIWNLHADAHDFDSHTSDLEEISRKVFSAHFGQLSIIFLWLSGMYFHGARFSNYEAWLSDPTHIGPSAQVVWPIVGQEILNGDVGGGFRGIQITSGFFQLWRASGITSELQLYCTAIGALIFAALMLFAGWFHYHKAAPKLAWFQDVESMLNHHLAGLLGLGSLSWAGHQVHVSLPINQFLNAGVDPKEIPLPHEFILNRDLLAQLYPSFSEGATPFFTLNWSKYAEFLTFRGGLDPVTGGLWLTDIAHHHLAIAILFLIAGHMYRTNWGIGHGLKDILEAHKGPFTGQGHKGLYEILTTSWHAQLSLNLAMLGSLTIIVAHHMYSMPPYPYLATDYGTQLSLFTHHMWIGGFLIVGAAAHAAIFMVRDYDPTTRYNDLLDRVLRHRDAIISHLNWVCIFLGFHSFGLYIHNDTMSALGRPQDMFSDTAIQLQPVFAQWIQNTHALAPGGTAPGATASTSLTWGGVDLVAVGGKVALLPIPLGTADFLVHHIHAFTIHVTVLILLKGVLFARSSRLIPDKANLGFRFPCDGPGRGGTCQVSAWDHVFLGLFWMYNAISVVIFHFSWKMQSDVWGSISDQGVVTHITGGNFAQSSITINGWLRDFLWAQASQVIQSYGSSLSAYGLFFLGAHFVWAFSLMFLFSGRGYWQELIESIVWAHNKLKVAPATQPRALSIVQGRAVGVTHYLLGGIATTWAFFLARIIAVG
|
PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin-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. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin.
|
Q09MH8
|
Q9M9L7
|
LONM4_ARATH
|
Lon protease homolog 4, chloroplastic/mitochondrial
|
Arabidopsis
|
MLKFLTPTAYASHHVTPATRFRSTPVKNLLFKQLTLLTGWNRSSYELGRRSFSSDLDSDTKSSTTTVSAKPHLDDCLTVIALPLPHKPLIPGFYMPIYVKDPKVLAALQESRRQQAPYAGAFLLKDDASSDSSSSSETENILEKLKGKELINRIHEVGTLAQISSIQGEQVILIGHRQLRITEMVSESEDPLTVKVDHLKDKPYDKDDDVIKATYFQVMSTLRDVLKTTSLWRDHVRTYTQACSLHIWHCLRHIGEFNYPKLADFGAGISGANKHQNQGVLEELDVHKRLELTLELVKKEVEINKIQESIAKAVEEKFSGDRRRIILKEQINAIKKELGGETDSKSALSEKFRGRIDPIKDKIPGHVLKVIEEELKKLQLLETSSSEFDVTCNYLDWLTVLPWGNFSDENFNVLRAEKILDEDHYGLSDVKERILEFIAVGGLRGTSQGKIICLSGPTGVGKTSIGRSIARALDRKFFRFSVGGLSDVAEIKGHRRTYIGAMPGKMVQCLKNVGTENPLVLIDEIDKLGVRGHHGDPASAMLELLDPEQNANFLDHYLDVPIDLSKVLFVCTANVTDTIPGPLLDRMEVITLSGYITDEKMHIARDYLEKTARRDCGIKPEQVDVSDAAFLSLIEHYCREAGVRNLQKQIEKIFRKIALKLVRKAASTEVPRISDDVTTDTEETKSLAKTDLESPETSAEGSTVLTDELATGDPTESTTEQSGEVAETVEKYMIDESNLSDYVGKPVFQEEKIYEQTPVGVVMGLAWTSMGGSTLYIETTFVEEGEGKGGLHITGRLGDVMKESAEIAHTVARRIMLEKEPENKLFANSKLHLHVPAGATPKDGPSAGCTMITSLLSLALKKPVRKDLAMTGEVTLTGRILAIGGVKEKTIAARRSQVKVIIFPEANRRDFDELARNVKEGLEVHFVDEYEQIFELAFGYDH
|
ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial DNA in a site-specific manner.
|
Q9M9L7
|
Q3JDR4
|
RF1_NITOC
|
Peptide chain release factor 1
|
Nitrosococcus
|
MKDSIRSKLETLAERQQELTALLAEPEIASAQKKFRELSQEYAQLEPVIGCFRDFEQAQSVLNESKALLQDQDPELRVLAQEEIAAAEKKLERLDRELHTLLLPSDPNDKRNIFLEIRAGTGGDEAALFASDLLRMYLRYAEQRGWRTEIMGDSPGEHGGHKEIIVRIVGAGAYSRLKFESGGHRVQRVPQTESQGRIHTSACTVAIMPEAEEIDDIDINPADLRVDTFRASGAGGQHVNKTDSAIRITHLASGIVVECQDERSQHKNRARAMSLLRTKLKSEEEAKLVAEETATRRSLIGSGDRSERIRTYNFPQGRVTDHRINLTLYKLDEILQGNLDAIIDPLVAEHQADQLAALSD
|
Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
|
Q3JDR4
|
Q7U3L0
|
SPEE_PARMW
|
Spermidine synthase
|
Parasynechococcus marenigrum
|
MGGWIDEEHRGVRYGLAGDVLVEETSPFQRISVIRSERYGKGLLLDGCWMTAEQQERHYHEALVHPALCSAEAIERVLVIGGGDGGTARECLRYPEVIHLDLVEIDGRVVELSQEHLPGIGGAVWSDSRCQLTVGDGIAWAANAPDQSYDVVLVDGSDPAGPAEGLFNRAFFEHCRRILKPGGVFATQSESPEAFREVHVAMVRLLREVFGHADPLYGWVPMYPSGWWSWTFAAVDGPRYRTVQPARAALVAEGCEIWSPRWQQGALDAVPAFIARELAP
|
Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine.
|
Q7U3L0
|
Q96190
|
COX2_RHIUN
|
Cytochrome c oxidase polypeptide II
|
Rhinoceros
|
MAYPLQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYMMDEINNPSLTIKTMGHQWYWSYEYTDYEDLTFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMTIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLISTRPGLYYGQCSEICGSNHSFMPIVLELVPLKHFEKWSTSML
|
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
|
Q96190
|
Q50265
|
RS19_ASTYP
|
30S ribosomal protein S19
|
Candidatus Phytoplasma asteris
|
MPRSVKKGPIVASHLLAKIEKQKNLKNKKVIQTWSRSSTITPIFVGHKIAVYNGREHIPVYITENMVGHKLGEFSPTRTYRGHNKKDKKIQKK
|
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
|
Q50265
|
Q4UXZ0
|
MSCL_XANC8
|
Large-conductance mechanosensitive channel
|
Xanthomonas
|
MGMVSEFKQFAMRGNVIDLAVGVVIGAAFGKIVTALVEKIIMPPIGWAIGNVDFSRLAWVLKPAGVDATGKEIPAVVIGYGDFINTVVQFVIIAFAIFLVVKLINRLSQRKPDAPKGPSEEVLLLREIRDSLKNDTLKNPTVP
|
Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell.
|
Q4UXZ0
|
Q9RXX6
|
IXTPA_DEIRA
|
Nucleoside-triphosphate pyrophosphatase
|
Deinococcus
|
MQQQTGGRRRQIRRVVVATSNAGKVRELQGALAPLGWQCEGLGAVTLPEETGSTYEENAALKACAAAMATGLPALADDSGIEVLALGGQPGVYSARFGNVNSDVERNVLLLEKMRRHTDRRAKFVSVLVLAYPDGKLEEYRGEVTGQLLEGPRGESGFGYDPLFLPDGSELSMGEMTLEQKQAISHRGQALAALLAAHGA
|
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.
|
Q9RXX6
|
B2HFW2
|
ARC_MYCMM
|
Mycobacterial proteasome ATPase
|
Mycobacterium
|
MADSERSEAFGTPDDTPLSSNDAAELEQLRREAAVLREQLESAVGPQGTARSARDVHQLEARIDSLAARNSKLMETLKEARQQLLALREEVDRLGQPPSGYGVLLSTHDDDTVDVFTSGRKMRLTCSPNIEISLLRKGQTVRLNEALTVVEAGTFESVGEISTLREVLADGHRALVVGHADEERIVWLAEPLVAEDLPDGFPDALNDDTKPRKLRPGDSLLVDTKAGYAFERIPKAEVEDLVLEEVPDVSYEDIGGLTRQIEQIRDAVELPFLHKELYREYALRPPKGVLLYGPPGCGKTLIAKAVANSLAKKMAEVRGDDSREAKSYFLNIKGPELLNKFVGETERHIRLIFQRAREKASEGTPVIVFFDEMDSIFRTRGTGVSSDVETTVVPQLLSEIDGVEGLENVIVIGASNREDMIDPAILRPGRLDVKIKIERPDAEAAQDIYSKYLTETLPVHADDLAEFEGERPACIKAMIEKVVDRMYAEIDDNRFLEVTYANGDKEVMYFKDFNSGAMIQNVVDRAKKNAIKSVLETGQPGLRIQHLLDSIVDEFAENEDLPNTTNPDDWARISGKKGERIVYIRTLVTGKSSSASRAIDTESNLGQYL
|
ATPase which is responsible for recognizing, binding, unfolding and translocation of pupylated proteins into the bacterial 20S proteasome core particle. May be essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase may function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis.
|
B2HFW2
|
A6LU43
|
NUSB_CLOB8
|
Antitermination factor NusB
|
Clostridium
|
MNRKLSREKAMELLFGMTLSKDTMEDAVEAFVENYEGDIKEIDLTYVKQVLIGVNNNKEAIDKVIQENLHNWKIERISKVNLSILRIATYELLYDKEVPRGVAINEALEITRRYSDEKSVSFINGVLDKIKQD
|
Involved in transcription antitermination. Required for transcription of ribosomal RNA (rRNA) genes. Binds specifically to the boxA antiterminator sequence of the ribosomal RNA (rrn) operons.
|
A6LU43
|
Q9PGS5
|
TGT_XYLFA
|
tRNA-guanine transglycosylase
|
Xylella
|
MSRLQFQLQATDGAARRGQLSFPCGTVQTPAFMPVGTYGAVKGVLPGQLCDLGAEIILGNTFHLFLRPGLEVIADHGGLHGFMRWNGPILTDSGGFQVFSLAHRRKISEQGVTFAAPTDGAQVFLGPEESMKIQKVLNSDIVMIFDECTPYPATEDVARDSMELSLRWAQRSRDAHDALDNDAALFGIIQGGVHPDLRGRSLDGLQAIGFDGYGIGGLAVGESESERNVILEYLHPRVPADRPRYLMGVGRPEDLVESVARGVDMFDCVMPTRHARNGQYFTGFGTVKIRNACYARDVDPIEPGCGCPACVGGYTRAYLRHLDRCNEMLASMLGTLHNLWYYETLMANMRAAITAGTFFAFRRSFYLARGLDLPPLPEVAGCAG
|
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).
|
Q9PGS5
|
P17709
|
HXKG_YEAST
|
Glucose kinase 1
|
Saccharomyces
|
MSFDDLHKATERAVIQAVDQICDDFEVTPEKLDELTAYFIEQMEKGLAPPKEGHTLASDKGLPMIPAFVTGSPNGTERGVLLAADLGGTNFRICSVNLHGDHTFSMEQMKSKIPDDLLDDENVTSDDLFGFLARRTLAFMKKYHPDELAKGKDAKPMKLGFTFSYPVDQTSLNSGTLIRWTKGFRIADTVGKDVVQLYQEQLSAQGMPMIKVVALTNDTVGTYLSHCYTSDNTDSMTSGEISEPVIGCIFGTGTNGCYMEEINKITKLPQELRDKLIKEGKTHMIINVEWGSFDNELKHLPTTKYDVVIDQKLSTNPGFHLFEKRVSGMFLGEVLRNILVDLHSQGLLLQQYRSKEQLPRHLTTPFQLSSEVLSHIEIDDSTGLRETELSLLQSLRLPTTPTERVQIQKLVRAISRRSAYLAAVPLAAILIKTNALNKRYHGEVEIGCDGSVVEYYPGFRSMLRHALALSPLGAEGERKVHLKIAKDGSGVGAALCALVA
|
Two isoenzymes, hexokinase-1 and hexokinase-2, can phosphorylate keto- and aldohexoses in yeast, whereas a third isoenzyme, GLK, is specific for aldohexoses. All glucose phosphorylating enzymes are involved in glucose uptake.
|
P17709
|
A1RI59
|
SSTT_SHESW
|
Na(+)/serine-threonine symporter
|
Shewanella
|
MKQESSLLAKLANGSLVLQILLGIAAGVILASFSQDAAKQVAFLGSLFVGALKAIAPILVFILVASSIANQKKNTQTNMRPIVVLYLFGTFAAALTAVVLSSIFPTNLVLVAGIEGTSPPQGIGEVINTLLFKLVDNPVNALMTGNYIGILAWGVGLGLALHHANDSTKQVFADMSHGISQMVRFIIRLAPIGIFGLVAATFAETGFAAIAGYAQLLAVLLSAMAIIALIVNPLIVYVKIKRNPYPLVLRCLRESGVTAFFTRSSAANIPVNMALCEKLNLNKDTYSVSIPLGATINMGGAAITITVLTLAAVHTLGIQVDLPTALLLSVVAAVSACGASGVAGGSLLLIPLACSLFGISNDIAMQVVAVGFIIGVIQDAAETALNSSTDVIFTAAACEAAENKAKLG
|
Involved in the import of serine and threonine into the cell, with the concomitant import of sodium (symport system).
|
A1RI59
|
O34453
|
NOSO_BACSU
|
NOSoxy-like protein
|
Bacillus
|
MEEKEILWNEAKAFIAACYQELGKEEEVKDRLADIKSEIDLTGSYVHTKEELEHGAKMAWRNSNRCIGRLFWNSLNVIDRRDVRTKEEVRDALFHHIETATNNGKIRPTITIFPPEEKGEKQVEIWNHQLIRYAGYESDGERIGDPASCSLTAACEELGWRGERTDFDLLPLIFRMKGDEQPVWYELPRSLVIEVPITHPDIEAFSDLELKWYGVPIISDMKLEVGGIHYNAAPFNGWYMGTEIGARNLADEKRYDKLKKVASVIGIAADYNTDLWKDQALVELNKAVLHSYKKQGVSIVDHHTAASQFKRFEEQEEEAGRKLTGDWTWLIPPISPAATHIFHRSYDNSIVKPNYFYQDKPYE
|
Catalyzes the production of nitric oxide.
|
O34453
|
Q3II28
|
RISB_PSET1
|
6,7-dimethyl-8-ribityllumazine synthase
|
Pseudoalteromonas
|
MKIIEGSKYAPGKKFAIVISRFNDFIGSSLLAGAIDELKRTGGVSDDDITVVYVPGAVELPLAAKRIAAKKQYDAIIALGVVIRGGTPHFDLVAGESNKGLAQVSLEYDIPVAFGVLTTESIEQAIERAGTKMGNKGGEAALGALEMVNVLDKI
|
Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
|
Q3II28
|
P46613
|
PSBF_BETVU
|
PSII reaction center subunit VI
|
Beta
|
MTIDRTYPIFTVRWLAVHGLAIPTVSFLGSISAMQFIQR
|
This b-type cytochrome is tightly associated with the reaction center of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
|
P46613
|
Q0V8T7
|
CTP5C_MOUSE
|
Contactin-associated protein-like 5c
|
Mus
|
MDSVPRLNSVFTLVLSGLWHFGLTATNYNCDDPLTSFLSLRAFSSSSDLTGRSSPAQLNWRMGTGGWSPADSNAQQWLQMDLGNRVEITAVATQGRYGSSDWVTSYRLMFSDTGHNWQQYTQEGSIWRFVGNMNANSVVHHKLLNSVRARFVRFVPLEWNPNGKIGMRVEVYGCSYRSDVADFDGWSSLLYRFNQKTMSTLKDVISLKFKSIQRDGVLFHGEGQRGDHITLELQNGRLALYLNLDDSKAQVSSTAPLATLGSLLDDQHWHSVLLERVGKQANFTVDKNTQHFQTKGETDALDIDYELSFGGIPVPSKPGTFLKKNFHGCIENLYYNGVNIIDLAKRRKHQIYSGNVTFSCSEPQTVPITFVNSRSSYLLLTGTPQIDGLSVSFQFRTWNEDGLLLSTELSEGSGTLLLILEGGTLRLLIKKLARHGTEIFTGSGLNDGMWHSVSISARRNRVTLTLDNDAASLPPDTSWLQIYSGNSYYFGGCPDNLTDSQCLNPIKAFQGCMRLIFIDNQPKDLISVQQGSLGSFSDLHIDLCSIKDRCLPNYCEHGGQCAQTWTNFYCNCSDTGYTGATCHDSIYEQSCEVYRHRGKTAEFFYVDSDGSGPLGPLQVFCNITEDKIWMTVQHNNTGLTWVQGSNPEKPYAMTLNYGGSLEQLEALIDGSEHCEQEVTYYCKRSRLLNTPDGVPFTWWIGRSNEKHPYWGGSLPGVQQCGCGLEESCLDIRHFCNCDADTDEWTNDTGYLSFKDHLPVTQIIITDTNRSKSEAAWRIGPLRCYGDRHFWNAVSFSTEASFLHFPTFRVEFSADIFFFFKTTALSGVFLEILGIKDFLRLEMSSPSEVIFAIDVGNGPIDLLVQSPYPLNDNQWHYIRAERNLKETSLQVDNLPQSMREASEEGHFQFQLNSQLFVGGKSSRQKGFFGCIRSLHLNGQNIDLEERAKVTSGVRPGCPGHCSSYGRNCQNGGKCVEKHIGYSCDCTNSPYEGPFCQKEISALFDSDTSVTYMFQEPYSVTKNTNLSSSAIYTDTAPSKEIIMLSFMTAQAPTLLLYLNFSSQNFLAILLSWNGSLQIHYQLSKEESHVFTINTENLANRRVHQVKMSRDGPELSIQMDQQLFSYTFSLESEFQRARSLVLGKVTETLGLDPEVARANTLGFVGCLSSVQYNHITPLKAALRHASISPVTVQRTLTESSCVSMVDSDANAVTTVYSSTDPFGERDEREPLTNAVPSDLAVIGGIIAVVTFISFSVIGIMTHFFYQHKRSHYASQMKEKEYPENVDSSSRNDIDLQNTTRECKQEDFI
|
May play a role in the correct development and proper functioning of the peripheral and central nervous system and be involved in cell adhesion and intercellular communication.
|
Q0V8T7
|
P49959
|
MRE11_HUMAN
|
Meiotic recombination 11 homolog A
|
Homo
|
MSTADALDDENTFKILVATDIHLGFMEKDAVRGNDTFVTLDEILRLAQENEVDFILLGGDLFHENKPSRKTLHTCLELLRKYCMGDRPVQFEILSDQSVNFGFSKFPWVNYQDGNLNISIPVFSIHGNHDDPTGADALCALDILSCAGFVNHFGRSMSVEKIDISPVLLQKGSTKIALYGLGSIPDERLYRMFVNKKVTMLRPKEDENSWFNLFVIHQNRSKHGSTNFIPEQFLDDFIDLVIWGHEHECKIAPTKNEQQLFYISQPGSSVVTSLSPGEAVKKHVGLLRIKGRKMNMHKIPLHTVRQFFMEDIVLANHPDIFNPDNPKVTQAIQSFCLEKIEEMLENAERERLGNSHQPEKPLVRLRVDYSGGFEPFSVLRFSQKFVDRVANPKDIIHFFRHREQKEKTGEEINFGKLITKPSEGTTLRVEDLVKQYFQTAEKNVQLSLLTERGMGEAVQEFVDKEEKDAIEELVKYQLEKTQRFLKERHIDALEDKIDEEVRRFRETRQKNTNEEDDEVREAMTRARALRSQSEESASAFSADDLMSIDLAEQMANDSDDSISAATNKGRGRGRGRRGGRGQNSASRGGSQRGRADTGLETSTRSRNSKTAVSASRNMSIIDAFKSTRQQPSRNVTTKNYSEVIEVDESDVEEDIFPTTSKTDQRWSSTSSSKIMSQSQVSKGVDFESSEDDDDDPFMNTSSLRRNRR
|
Component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis . The complex possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by MRE11 . RAD50 may be required to bind DNA ends and hold them in close proximity . This could facilitate searches for short or long regions of sequence homology in the recombining DNA templates, and may also stimulate the activity of DNA ligases and/or restrict the nuclease activity of MRE11 to prevent nucleolytic degradation past a given point . The complex may also be required for DNA damage signaling via activation of the ATM kinase . In telomeres the MRN complex may modulate t-loop formation .
|
P49959
|
A4IX64
|
MURG_FRATW
|
Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase
|
Francisella
|
MSLENKNIIITAGGTGGHIYPALAIAELLRQNKANVTWVGTPNSMEASIVPEYFNIQFIKSSGVRRKGIIKKITFPLKLAYNTLKSRSLLKKLKADLVIGFGGYVSGPICLAAAQINIPVIIHEQNAKIGLTNRILAKFATTICLAFEIENLHKQFSSKQLAKTKIVGNPVRKDIVALNDKARIYTDSSTLKILVLGGSQGAKAINEIIPKLIQKSNEQGINIKVWHQTGKLSLEETKDAYKDISQNHIKDIAAFIDDMAIAYNWADLVICRAGALTVSECAIAGLPAIFIPLPSAVDDHQFFNAQNIVNNNAGFCLRQQQMTLENLLAIIKPLNQDRSKLEQMSKMAKKTLIKNSSEQILDCVKKILNNK
|
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).
|
A4IX64
|
O78514
|
PSBH_GUITH
|
Photosystem II reaction center protein H
|
Guillardia
|
MALRTRLGELLRPLNSEYGKVAPGWGTTPAMGFVMLLFFLFLLIILQIYNSSLILENVDVDWASLGN
|
One of the components of the core complex of photosystem II (PSII), required for its stability and/or assembly. PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
|
O78514
|
Q6M183
|
MPTA_METMP
|
GTP cyclohydrolase IV
|
Methanococcus
|
MQCNDVQATEPDIKVSLTRVGVTNLKKLVKLKRKNKRDIVLLPTFEVFVDLPSSQKGIHMSRSPEVIEEVVENILLEKEIYGVEDLSVEIVMKLFEKHEYATRAEVMLYSDYMMEEKSPVTKKDSQEIGKIIARAYGVKDSNGKIDVKKMVGAEVVGITACPCAQNMLKENAVVSLTEKGFSSEDIEKILDSVTIATHNQRGIGTVMIEVPNGYTVGISKIIKIIKDSMSGEVYELLKRSDEAFVVEAAHKNPKFVEDCAREMIKRVVDVFDYLPEDTQVLVRQVNKESIHRHDAFAERNSTIRELRDELKTLTN
|
Converts GTP to 7,8-dihydro-D-neopterin 2',3'-cyclic phosphate, the first intermediate in the biosynthesis of coenzyme methanopterin.
|
Q6M183
|
Q5E8W9
|
THIC_ALIF1
|
Thiamine biosynthesis protein ThiC
|
Aliivibrio
|
MSSSRKQARLDAKTNIESLSVQPYPNSNKVYIEGSRPDIRVPMREISLADSLVGGTKESPIFEPNEPIQVYDTSGVYTDPSYDIDVYKGLPKLRQEWIEERNDTELLDGVSSVYSQERLADETLDELRYGNLPTIRRAKQGQCVTQLHYARQGIITPEMEYIAIRENMGRQKFADEQLNHQHPGHSFGANLPKEITPEFVRREVAEGRAIIPSNINHPEAEPMIIGRNFLIKVNANIGNSSVSSSIEEEVEKLVWSTRWGGDTVMDLSTGRNIHETREWILRNSPVPIGTVPMYQALEKVNGVAENLNWEVMRDTLIEQAEQGVDYFTIHAGLLLRYVPMTAKRVTGIVSRGGSIIAKWCLAHHQESFLYTHFREICEICAKYDVALSLGDGLRPGSVADANDEAQFAELRTLGELTKVAWEYDVQVIIEGPGHVPMHMIKENMDEQLKHCHEAPFYTLGPLTTDIAPGYDHITSGIGAAMIGWYGCAMLCYVTPKEHLGLPNKDDVKTGLITYKLAAHAGDLAKGHPGAQIRDNALSKARFEFRWEDQFNLSLDPITAREYHDETLPQESGKVAHFCSMCGPKFCSMKISQEVREYAKDSEQVALDQAIEIKMIDDPLEGMRQKSEEFKASGSELYHPVVEAE
|
Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction.
|
Q5E8W9
|
Q7VR53
|
PDXH_BLOFL
|
Pyridoxal 5'-phosphate synthase
|
Candidatus Blochmannia
|
MLELSKIHNLRREYISKQFRRSNLTKNPMHLFSKWLYEAYCQIPDPNAMCLSTVDHTGQPFQRLVLLKYFNDKTIVFFTHLNSRKAIHINNNPKISLCFPWNIINRQIIITGSVYKISKKEAQKYFYTRPKNNQISTWASKQSTIISSKKVLKNKFLKLKKKYFQKSVPFPHFWVGYKININSMEFWQGGIYRLHDRFLYKKNKKKWYINRLSP
|
Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
|
Q7VR53
|
Q83AC6
|
LPTD_COXBU
|
LPS-assembly protein LptD
|
Coxiella
|
MKQGKSFIFYCLVLLLCGFQQLSSAVTASIAKAIKTTDRKQRVSETLPTGLSYRRFYQHIAHLLGWVPAPDLVCRGYFKEPLILTEHPHPGPATKEPAIVTAKGPSMVTAQGVSILRKDVVVTQPGRIVEADKAYIYRDSKTGHVTKIILIGHVRLHEADKRIVADKGTLTLYPKTAILMNAAYHIYNGEPYFYKFKYPFDAWGIAKHAVRDASNVITLRHATYSTCKPTAPAWSMSATTLVLNRNTHRGEAYNMLLHIGRVPIFYFPYFNFPIDNYRKTGFLIPYAGHSSSSGWFFALPFYWNMAPNYDLTLTPEFMSERGLNLQSLFRFLSTKSSGTIYLNYLPNDKVFQQFRETTLSKFPPSVLAEHPVFIPYVDKLKKMKNQRAFFSMNETTLFNSEWSSRVILNYVTDPYFFQDLGGQLGGSSLANQLLNQIDLQYNGLHWQFMGMLQAYQTLHLISQWTTPALDQYSRLPDFNIVGYYPDIARHVDFNFNAEAVNFDYRSDFVPDKPRGQRFHMRPGISFPFYFASGYIIPQLWADATAYNITHFQPGQAHTSSRLLPIFDIDSGLYFDRNFHLGHRSFIQTLEPRFFYLYVPYQNQDRFPNFDTVLLPFSFEQLFALNQFTGNDRLQNANQASFALTSRVLDAQNGSPILTANVGFIYYLENQRVCLTPGCTPSNYHYSPIIGELTFYPFPYWSFTGSLAWDPNLGQTNNTSVELAYNNGGKKADIRYLFVHGNEDSIVTPTTLIVPGNAYSQNTNHVISSGAWPLLKKWNAVGYWDYNITERRTDVYSIGVQYNTCCWALSFSIRRTYAGLKVDPNGALQRQYDTAYGFELQLKGLGNLGTAPISTVTVLDAMNNGVSNDVR
|
Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane.
|
Q83AC6
|
Q9S6S1
|
PEPQ_LACDE
|
Proline dipeptidase
|
Lactobacillus
|
MNLDKLQNWLQENGMDVAYVSSPTTINYFTGFITDPEERIFKLFAFKDAEPFLFCPALNYEEAKASAWDGDVVGYLDSEDPWGKIAEEIKQRTKDYQNWAVEKNGLTVAHYQALHAQFPDSDFSKDLSDFIAHIRLFKTESELVKLRKAGEEADFAFQIGFEALRNGVTERAVVSQIEYQLKLQKGVMQTSFDTIVQAGKNAANPHQGPSMNTVQPNELVLFDLGTMHEGYASDSSRTVAYGEPTDKMREIYEVNRTAQQAAIDAAKPGMTASELDGVARKIITDAGYGEYFIHRLGHGIGMEVHEFPSIANGNDVVLEEGMCFSIEPGIYIPGFAGVRIEDCGVLTKEGFKPFTHTSKELKVLPVKE
|
Strict dipeptidase active on Xaa-Pro dipeptides, except Gly-Pro and Pro-Pro.
|
Q9S6S1
|
Q5U2P6
|
PIANP_RAT
|
Paired immunoglobin-like type 2 receptor-associating neural protein
|
Rattus
|
MWPAQLLSQLLPLWPLLLLPLSLPAQGSSHRSPPAPARPPCVRGGPSAPRHVCVWERAPPPSRSPRVPRSRRQVLPGTAPPATPSGFEEGPPSSQYPWAIVWGPTVSREDGGDPNSVNPGFLPLDYGFAAPHGLATPHPNSDSMRDDGDGLILGETPATLRPFLFGGRGEGVDPQLYVTITISIIIVLVATGIIFKFCWDRSQKRRRPSGQQGALRQEESQQPLTDLSPAGVTVLGAFGDSPTPTPDHEEPRGGPRPGMPQPKGAPAFQLNR
|
Acts as a ligand for PILRA in neuronal tissues, where it may be involved in immune regulation.
|
Q5U2P6
|
A6WIP6
|
RIMO_SHEB8
|
Ribosome maturation factor RimO
|
Shewanella
|
MTVETFKPKQTTTLDIPVKTLEAASTNAVTTGNRIGFVSLGCPKNLVDSERILTQLRIDGYEVTNSYDNADLVIVNTCGFIDAAVEESLDAVREALEENGKVIVTGCLGAKENQIREVHPDVLEITGPHSYEAVLKHVHKYVPKPEHNPFTSLIPQTGVKLTPKHYAYLKISEGCDNRCTFCIIPSLRGDLDSRPAGSILDEAKRLVESGVQEILVVSQDTSAYGKDKGGRTDFWNGMPVKQDITSLARQLGKMGAWVRLHYIYPYPWVDDLIPLMAEGLILPYLDIPMQHASPRILKMMKRPGRVDRQLEAIQRWREICPDLVIRSTFIVGFPGETEEDFQILLDFLKEARLDRVGCFKYSEVDGAVANTIAELISEDVKEDRYHRFMEVQAEISAERLARFVGRTLDILIDDVDEEGAIGRSFADAPEIDGMVFINGETELEPGMLVRARITHSDEHDLWAEVVDADTQD
|
Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12.
|
A6WIP6
|
Q7TQN9
|
GP142_MOUSE
|
Probable G-protein coupled receptor 142
|
Mus
|
MHLNSNPNSYICDAYQHADLLWSLSPHVLTKAVQPQVTLLPTVNGSNPRYDGVDGHWPESPERSPCVAGIIPVIYYSVLLSLGLPVALARLAARTRKPSYHYLLALTASDIVTQVIIVFVGFLLQGAVLARQVPQAVVRTANILEFAANHASVWIAVLFTVDRYNALCRPLRHRATSSPGRTHRAIAAVIGVTLLTGIPFYWWLDVWRDADPPSTMDKLLKWAHCLIVYFIPCNVFLVTNSAIILRLRKRGQRGLRPLVSKSTAILLGVTSLFALLWAPRIIVMLYHLYVAPVHRDWRVHLALDIANMLAMLNTEVNFGLYCFISKTFRATVRQVICDVHMACALKSQPKQTVVELMLKSVGTEL
|
Orphan receptor.
|
Q7TQN9
|
O94287
|
YOO2_SCHPO
|
Uncharacterized chloride channel protein C887.02
|
Schizosaccharomyces
|
MKDDQLIDWIHERYEEQKSANRLAGRFRFLGLETKYSIISIISGIFIGLTAALLNALASLLNSFREGYCTVNILFDKQTCCSTLTEDYECQEFFFWRNNHSVFVSCLIYVSVSVGFAFIATTLGYVVAPAARASGIPTIKAILSGYKYPDMNVFFSIKTLCSKSLAVCFSVASGLWVGKEGPFVHIATNIIYLVERIAPSLADSEIFTRQLLAAAMASGIAASFNAPVGGVIFALEQLASSSFPSLFTGSIWYEFLCSASSVVALQLIRSWHTDVGYLSYVSLDRRWSYKDTLPFIFISILCGCLGSVLIYLNMKFASKTKGFSKISNVFFVIFLSLITSLTAYAILGESELLFNPMELFPQVINSCSPSSSTVLCETTFWVTAIVLFTSALLGLLLTSATFGAAIPTGIIVPSLAIGACIGRAVGTLLKSRFPSLAGTSIYGVIGSIAFLSSTTRLVVALVVILFELTGALNIALPLMLATLISKWVSDSIIETSIYDAWIQFRNIPYFPSSNSLKFSIPLNFPVRSPEQLVRLPIRSCSIEELERAMHDSSQSFFVVLKNDTEFFEGFISRNKVSELLNRRPMSSNMQTTDNTGLDPLRSASAPVDSTFDLFDYIHPTTFTLNYDTPPVLMLKLFKDAGITNLALLNHGKLHGVLTKIDIIEYAKKCKTHTGNTYSELPTGVTYETDIFNRADD
|
Voltage-gated chloride channel.
|
O94287
|
Q9PE41
|
CLPP_XYLFA
|
Endopeptidase Clp
|
Xylella
|
MDDVTKALNLVPMVVEQTSRGERAYDIYSRLLKERLIFLVGPIDDYMANLIVAQLLFLEAENPEKDINIYINSPGGVVTAGMAIYDTMQYIKPAVSTICVGQAASMGALLLASGASGKRYALPNSRVMIHQPLGGFQGQATDIDIHAREILALRARLNEILAKHTGQSLETIAHDTERDNFKSAVDAQAYGLVDQVLGQRPEELIQSS
|
Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
|
Q9PE41
|
Q9HWK6
|
LYSC_PSEAE
|
PvdS-regulated endoprotease
|
Pseudomonas
|
MHKRTYLNACLVLALAAGASQALAAPGASEMAGDVAVLQASPASTGHARFANPNAAISAAGIHFAAPPARRVARAAPLAPKPGTPLQVGVGLKTATPEIDLTTLEWIDTPDGRHTARFPISAAGAASLRAAIRLETHSGSLPDDVLLHFAGAGKEIFEASGKDLSVNRPYWSPVIEGDTLTVELVLPANLQPGDLRLSVPQVSYFADSLYKAGYRDGFGASGSCEVDAVCATQSGTRAYDNATAAVAKMVFTSSADGGSYICTGTLLNNGNSPKRQLFWSAAHCIEDQATAATLQTIWFYNTTQCYGDASTINQSVTVLTGGANILHRDAKRDTLLLELKRTPPAGVFYQGWSATPIANGSLGHDIHHPRGDAKKYSQGNVSAVGVTYDGHTALTRVDWPSAVVEGGSSGSGLLTVAGDGSYQLRGGLYGGPSYCGAPTSQRNDYFSDFSGVYSQISRYFAP
|
Lysine-specific endoprotease . Involved in corneal virulence.
|
Q9HWK6
|
A4SJR5
|
IF2_AERS4
|
Translation initiation factor IF-2
|
Aeromonas
|
MAEVSVKQLATDIDTPVDRLLQQFVDAGISKSKADDLVSESEKQTLLAHLKKQHGGDELTAPARMTLQRKTKSTISVQGTGGKNKEVQVEVRKTRTYVKRSALEDEQRQAEAEETARLEAEEKARSEAENKVRLDAEEKARREAEQARREAEEKARIEAQSKARQAPQPAKAASSTAQQEAEKMAKREAEELKRQQEQTALQKAEELAAKKAEEARLMAEQNGPRWAEEEAARAKESSDYHLTTNKHAQAAEDELDRKEETSRRTAAAAVKAPKKAGRREDDRDSRNPRARKGKRGKMAMPNAMKHGFNKPAAVVNRDVVIGETITVAELANKMAVKGVEVIKAMMKMGAMATINQVIDQETAQLVAEEMGHKVVLRRENELEEAVLSDRDETSEAKSRAPVVTIMGHVDHGKTSLLDYIRKAKVAAGEAGGITQHIGAYHVETDSGMITFLDTPGHAAFTSMRARGAKSTDIVVLVVAADDGVMPQTIEAIQHAKAAEVPIVVAVNKIDKPEADPDRVKTELARYNVMSEDWGGDSQFVHVSAKSGEGIDDLLEAILIQSEVLELKAVVDGMASGVVIESFLDKGRGPVATVLVQEGTLRQGDIVLCGLEYGRIRAMRDELGREIKEAGPSLPVEILGLSGVPSAGDEATVVRDEKKAREVALYRQGKFRDVKLARQQKAKLENMFANMTEGEVSEVNVVIKADVQGSVQAICDALVQLSTDEVKVKIVGSGVGGITETDATLAAASSAILVGFNVRADASARKVIESESLDLRYYSVIYDLIDEVKQAMSGKLAPEYRQEIIGLAEVRSVFKSPKFGAVAGCMVTEGVVKRSNRIRVLRDNVVIYEGELESLRRFKDDVNEVRNGYECGIAVKNYNDVREGDQIEVYETIEIQRTL
|
One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex.
|
A4SJR5
|
Q1JDD1
|
SCPA_STRPB
|
Segregation and condensation protein A
|
Streptococcus
|
MDIKLKDFEGPLDLLLHLVSQYKVDIYEVPIVEVIEQYLNYIETLQVMKLEVAGDYMLMASQLMLIKSRRLLPKVVEHIEEEDLEQDLLEKIEEYSRFKAVSQALAKQHDQRAKWYSKPKQELIFEDAILQEDKTVMDLFLAFSNIMAAKRAVLKTNHTVIERDDYKIEDMMASIKQRLEKENVISLSAIFEECQTLNEVISIFLASLELIKLHVVFVEQLSNFGAIILRKEKK
|
Participates in chromosomal partition during cell division. May act via the formation of a condensin-like complex containing Smc and ScpB that pull DNA away from mid-cell into both cell halves.
|
Q1JDD1
|
Q96S96
|
PEBP4_HUMAN
|
Protein cousin-of-RKIP 1
|
Homo
|
MGWTMRLVTAALLLGLMMVVTGDEDENSPCAHEALLDEDTLFCQGLEVFYPELGNIGCKVVPDCNNYRQKITSWMEPIVKFPGAVDGATYILVMVDPDAPSRAEPRQRFWRHWLVTDIKGADLKKGKIQGQELSAYQAPSPPAHSGFHRYQFFVYLQEGKVISLLPKENKTRGSWKMDRFLNRFHLGEPEASTQFMTQNYQDSPTLQAPRERASEPKHKNQAEIAAC
|
Promotes AKT phosphorylation, suggesting a possible role in the PI3K-AKT signaling pathway.
|
Q96S96
|
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