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
|
|---|---|---|---|---|---|---|
B6J7H5
|
MNMA_COXB1
|
tRNA-specific 2-thiouridylase MnmA
|
Coxiella
|
MGIIFYTTQMPNFEQNQVIAVGLSGGVDSSVAALVLKEKGYEVIGLFMQNWETDSKDPFCTAEQDLSDAKAIADHIGIPLYVVNFSKAYWNHVFQHCLDEFAQGRTPNPDVWCNREIKFKSLLDHAKKLGATHLATGHYACIQNENNEYRLLKSNDSHKDQSYFLHLLNQYQLANSVFPIGGYQKSEVRAIAKKRGFINHAKKDSTGICFIGERKFKDFLNEFLLAQPGNIETPEGKIIGKHDGIMFYTVGQRKGLHIGGRPDAGEAPWYVVDKDVKRNVLIVVQGYEHPLLYSQELTCTNLHWIRDTEPSFPLTCKAKTRCRQADQTCVITRLDNDHCHVQFEHPQRAITRGQSVVFYLGNECLGGGIIN
|
Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
|
B6J7H5
|
A2WTA0
|
PLA3_ORYSI
|
Phospholipase A1-II 3
|
Oryza sativa
|
MCCFLLVSVLLATTLTDVASAQRWRQTSGGGKDRWDGLLDPLDADLRRDIIRYGELAQATSDALIGDPASPFAGASRYAPDAFLRKVRASDPDAYRVTRFVYATSSVRLPDAFMPRPAPSAGAAWSGESNWMGYVAVAADGVAANAGRRDIVVAWRGTKRAVEWANDLDITLVPADGVVGPGPGWTQPSVHRGFLSVYTSKSFSSPFNKLSAREQVLAEITRLLRAYKNENCSITITGHSLGAALSTLNAIDIVANGYNVRGSSRVPVPVTAIALASPRVGDDQFKRAFDSTPNLSLLRVRNAPDIVPTILPSAFFKDVGAELLVDTRRSPYLKNPAGPAQWHNLECYLHAVAGTQGAGDGAGFSLVVDRDLALVNKEVDALRDEYQVPAAWWVEKNKGMVQNASGRWVLQDHEEGNLAM
|
Acylhydrolase that catalyzes the hydrolysis of phospholipids at the sn-1 position.
|
A2WTA0
|
Q2IFT9
|
RSMA_ANADE
|
S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase
|
Anaeromyxobacter
|
MTDRYPSPRALLDRYDLRAKKSWGQNFLGEEAVLDDIARLAAPRAGDPVLELGAGLGHLTARLLARGARVVAVERDRDMARVLRGELGDRITLLEADAARLDHAALAARFGAPAAAGEGARLAVVGNLPYHLTSPILFSILDQVAHVSRAVFLLQREVAERLAAPPASRDWGLLSVLLQREAEVSVERIVPPGAFWPPPKVESAVLCALFRPPADAVGDPARFRRLVKAGFGLRRKTLRNALGSAKLAEPARLEAAFAAAGVDPGRRGETLTLAEWAALDRALG
|
Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
|
Q2IFT9
|
B8F6C8
|
AROQ_GLAP5
|
Type II DHQase
|
Glaesserella
|
MKKILLLNGPNLNMLGKREPHIYGSQTLADIENHLQQLAKARGYCLEYFQANGEEPIINRIHQSFQNTDFIIINPGASTHTSVALRDALLSVAIPFVEVHLSNVHAREPFRHHSYLSDVAKGVICGLGAKGYDYALDYAIQFLKSGK
|
Catalyzes a trans-dehydration via an enolate intermediate.
|
B8F6C8
|
Q0AJB4
|
ATPF_NITEC
|
F-type ATPase subunit b
|
Nitrosomonas
|
MNINFTLVSQAIAFSIFIWFTTKFVWPYLLRAIEERQQKIADGLAAGERGKKELELASQRSSEVLKEAKQRAGEIVIQAEKRASDIIEEAKKNARVEGEKILAGAKAEIQHEIFSARESLRQQVAGLAVQGASKILRREVNAKAHADLLASIETELK
|
Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
|
Q0AJB4
|
Q92ME7
|
AROB_RHIME
|
3-dehydroquinate synthase
|
Sinorhizobium
|
MTSHVMPTAERKVRVDLAERSYDILIGPGLIAAAGKEIASRLKGRKMAVITDENVAPRYLEPLMASLGESGIEAVSLILPAGEKTKSFEHLIPVCEAILGARIERNDAVIALGGGVIGDLTGFAAGIVRRGSRFIQIPTSLLAQVDSSVGGKTGINSAHGKNLIGVFHQPDLVLADTAALDTLSPREFRAGYAEVAKYGLIDKPEFFEWLEKNWQAVFAGGPARIEAIAVSCQAKADVVAADERENGRRALLNLGHTFGHALEAATDYDSKRLVHGEGVAIGMVLAHEFSARMNLASPDDARRVEAHLKTVGLPTRLADIPGALPPADRLMEAIAQDKKVKGGKLTFILTRGIGQSFVADDVPSSEVLSFLTEKHPR
|
Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
|
Q92ME7
|
Q73U04
|
Y3564_MYCPA
|
Putative S-adenosyl-L-methionine-dependent methyltransferase MAP_3564
|
Mycobacterium avium complex (MAC)
|
MSSLRTHDDTWDIKSSVGTTAVMVAAARAVETEQPDPLIRDPYAKLLVTNSGAGVLWEAMLDPDIAARVEALDEESAAHLHHMRGYQAVRTHFFDTYFADAVAAGIRQIVILASGLDSRAYRLDWPAGTTVYEIDQPQVLAYKSTTLAENGVTPSADRREVAVDLRQDWPAALRAAGFDPTQRTAWLAEGLLMYLPAEAQDRLFTLIGELSPAGSRVAAETAPNHADERRQQMRERFKKVADEIGFEQTVDVGELMYRDDHRADVTEWLNAHGWRATAEHSTAAMRRLGRWIENVPLADDKDAFSDFVVAERR
|
Exhibits S-adenosyl-L-methionine-dependent methyltransferase activity.
|
Q73U04
|
Q0ID12
|
RL16_SYNS3
|
50S ribosomal protein L16
|
unclassified Synechococcus
|
MLSPKRVKFRKQQRGRMRGVATRGNTIAFGQFALQAQECGWITSRQIEASRRAMTRYVKRGGKIWIRIFPDKPVTMRPAETRMGSGKGNPEFWVAVIKPGRILFEMGGEEITPEIAKEAMRLAQYKLPLKTKFICLDEQEQPAGTKAAASSTVES
|
Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs.
|
Q0ID12
|
Q2NF86
|
VATF_METST
|
V-ATPase subunit F
|
Methanosphaera
|
MKNDIAIMADPDTVTGFMLGGIKSGFPVHNKEEAKTTLKQLVDDEYSIIITTEKIGDELRDDITKYTGSKALPMIIEVPDKSGSHKRETDPMNDLIKRVIGVEMVK
|
Produces ATP from ADP in the presence of a proton gradient across the membrane.
|
Q2NF86
|
Q8GYX8
|
DNJ10_ARATH
|
Chaperone protein dnaJ 10
|
Arabidopsis
|
MVKETEYYDVLGVSPTATESEIKKAYYIKARQVHPDKNPNDPQAAHNFQVLGEAYQVLSDSGQRQAYDACGKSGISTDAIIDPAAIFAMLFGSELFEGYIGQLAMASMASLDIFTEGDQFDTKKIQEKLRIVQKEREDKLAQILKDRLNEYVINKDEFISNAEAEVARLSNAAYGVDMLNTIGYIYVRQAAKELGKKAIYLGVPFIAEWFRNKGHFIKSQLTAATGAYALFQLQEEMKRQLNTEGNYTEEELEEYLQAHKRVMIDSLWKLNVADIEATLCRVCQLVLQDPEAKREELRTRARGLKALGRIFQRAKTASESDPLENSEPQKLNGNGKNHDEDTSTSPKSSEASHSTSGPQEPQSPYVEEFKLGDEQFNYYFPRPAPPPGAGKYSSSGYD
|
Plays a continuous role in plant development probably in the structural organization of compartments.
|
Q8GYX8
|
Q765Z5
|
EDN2_RABIT
|
Preproendothelin-2
|
Oryctolagus
|
MVSVPTAWCSVALALLVALHEGKDQAAATLEQPASSPRARAAHLRLRRCSCSSWLDKECVYFCHLDIIWVNTPGQTAPYGLGNPPRRRRRSLPGRCECSSARDPACATFCHQRSRADAVGVPGSQSSADAFQAGKTWATPGELLRTLRDISAAKTHFAKRQQEATREPRTTHSRHRKR
|
Endothelins are endothelium-derived vasoconstrictor peptides.
|
Q765Z5
|
Q661C7
|
RL6_BORGP
|
50S ribosomal protein L6
|
Borreliella
|
MSRIGRLPIKIPDTVKIDVKGNLVIVEGTRGKLVQDIKDSINVKVENGSVIVNRAFNDKKTKAYHGLYRSLIFNMVKGVTEGFSKSLTINGIGYRVEQQGNSLFLNLGYSTQFEYVVPDGVSVKLDGNTKISVEGIDKFKVGQVAAEIRSLKKPEPYKGKGIKYDNEVIRRKVGKSGVKK
|
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.
|
Q661C7
|
A5UCB7
|
NUSB_HAEIE
|
Antitermination factor NusB
|
Haemophilus
|
MTEQKQVKKPSARRRARECTVQALYSWAVSGNTAEQVELAFVLDQDMDGVDKPYFRKLFRQTIENIETVDFSISPYIDRTFDELDPIETAILRLAVYELRFELDVPYKVVINEAIEVAKVFGADESHKYINGVLDKIAPALGRK
|
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.
|
A5UCB7
|
Q6B903
|
CYB6_GRATL
|
Cytochrome b6
|
Agarophyton tenuistipitatum
|
MGKVYDWFEERLEIQAIADDITSKYVPPHVNIFYCIGGIVFTSFLIQVASGFAMTFYYRPTVAEAFSSVEYIMTDVNFGWLIRSIHRWSASMMVLMLILHMFRVYLTGGFKKPRELTWVTGVILAVLTVSFGVTGYSLPWDQIGYWAVKIVTGVPEAIPVVGGSIVELLRGGVSVGQSTLTRFYSLHTFVLPLLTAVFMLMHFLMIRKQGISGPL
|
Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
|
Q6B903
|
Q73YS2
|
PYRD_MYCPA
|
Dihydroorotate oxidase
|
Mycobacterium avium complex (MAC)
|
MSGAPPAPRGGGHRWYGVARQLFFLVPAERIHTLVFALLRGVTAVGWPRRLLRRLLAPTDPVLASTVFGVRFPGPLGLAAGFDKDGLGLHAWGALGFGYAEIGTVTAGPQPGNPAPRLFRLPADRALLNRMGFNNLGAGALAVRLARRQPDIPIGVNIGKTKATPPDQAVDDYRASARLLGPLASYLVVNVSSPNTPGLRDLQAVGSLRPILSAVLAETSTPVLVKIAPDLSDSDVDDIADLAVELGLAGIVATNTTVSRDGLRTAGVDQLGAGGISGPPVARRAVEVLRRLYGRVGDRLVLISVGGIETADHAWERITAGASLLQGYTGFVYGGGLWAKQIHDGIAQRLRDGGFASLRDAVGSSARESG
|
Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
|
Q73YS2
|
Q90YW1
|
RL8_ICTPU
|
60S ribosomal protein L8
|
Ictalurus
|
MGRVIRAQRKGAGSVFKAHVKHRKGAAKLRHIDFAERHGYIKGIVKDIIHDPGRGTPLAKVVFRDPYRFKKRTELFIAAEGIHTGQFVFCGKKAQLNIGNVLPVGVMPEGTIICCLEEKPGDRGKLARASGNYATVISHNPETKKSRVKLPSGAKKVISSTNRAVVGVVAGGGRIDKPILKAGRAYHKYKVKRNCWPRVRGVAMNPVEHPFGGGNHQHIGKPSTIRRDVPAGRKVGLIAARRTGRLRGTKTVQEKEN
|
Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
|
Q90YW1
|
Q63E02
|
DLTA_BACCZ
|
D-alanine-activating enzyme
|
Bacillus cereus group
|
MKLLEQIEKWAIETPDQTAFVWRDAKITYKQLKEDSDALAHWISSEYPDDRSPIMVYGHMQPEMIINFLGCVKAGHAYIPVDLSIPADRVQRIAENSGAKLLLSAATVTVTDLPVRIVSEDNLKDIFFTHKGNTPNPEHAVKGDENFYIIYTSGSTGNPKGVQITYNCLVSFTQWAVEDFNLQTGQVFLNQAPFSFDLSVMDIYPSLVTGGTLWAIDKDMIARPKDLFASLEQSDIQVWTSTPSFAEMCLMEASFSESMLPNMKTFLFCGEVLPNEVARKLIERFPKATIMNTYGPTEATVAVTGIHVTEEVLDQYKSLPVGYCKSDCRLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFTMIDGERAYKTGDAGYVENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPIKKGEKYDYLLAVVVPGEHSFEKEFKLTSAIKKELNERLPNYMIPRKFMYQSSIPMTPNGKVDRKKLLSEVTA
|
Catalyzes the first step in the D-alanylation of lipoteichoic acid (LTA), the activation of D-alanine and its transfer onto the D-alanyl carrier protein (Dcp) DltC. In an ATP-dependent two-step reaction, forms a high energy D-alanyl-AMP intermediate, followed by transfer of the D-alanyl residue as a thiol ester to the phosphopantheinyl prosthetic group of the Dcp. D-alanylation of LTA plays an important role in modulating the properties of the cell wall in Gram-positive bacteria, influencing the net charge of the cell wall.
|
Q63E02
|
B8CHZ1
|
RHLB_SHEPW
|
ATP-dependent RNA helicase RhlB
|
Shewanella
|
MSETHLSTKKFADFPLHKEVQQALNEVGFEFCTPIQALSLPILLAKKDIAGQAQTGTGKTLAFLVATFNHLLTEAAPTERKINQPRAIIMAPTRELAIQIAKDANLLAKHTGLKVGIVYGGEGYEAQRKVLDKGIDILIGTTGRIIDYVRQGVIDVSAIQAVVLDEADRMFDLGFIKDIRFLFRRMPDAKSRLNMLFSATLSMKVQELAYDHMNEPEKVEIAPNEKTSKNIKEEIFYPSMEEKMPLLLSLLEEDWPEKAIVFSNTKHSCEKVWSWLEGDGHRVGLLTGDVPQKKRLRILEQFTSGDIDVLVATDVAARGLHIADVSHVYNYDLPDDCEDYVHRIGRTGRAGQKGVSVSFACEEYALNLPAIESYIQHSIPVTSYDSEALLDDIPAPKRIHRKPSSHSRNSRDRSGSRPQGGHRGNAPRRHDKTRRHS
|
DEAD-box RNA helicase involved in RNA degradation. Has RNA-dependent ATPase activity and unwinds double-stranded RNA.
|
B8CHZ1
|
B8ZLY7
|
HRCA_STRPJ
|
Heat-inducible transcription repressor HrcA
|
Streptococcus
|
MVTERQQDILNLIIDIFTKTHEPVGSKALQESINSSSATIRNDMAELEKQGLLEKAHTSSGRMPSVAGFQYYVKHSLDFDRLAENEVYEIVKAFDQEFFKLEDILQEAANLLTDLSGCTVVALDVEPSRQRLTAFDIVVLGQHTALAVFTLDESRTVTSQFLIPRNFLQEDLLKLKSIIQERFLGHTVLDIHYKIRTEIPQIIQRYFTTTDNVIDLFEHIFKEMFNENIVMAGKVNLLNFANLAAYQFFDQPQKVALEIREGLREDQMQNVRVADGQESCLADLAVISSKFLIPYRGVGILAIIGPVNLDYQQLINQINVVNRVLTMKLTDFYRYLSSNHYEVH
|
Negative regulator of class I heat shock genes (grpE-dnaK-dnaJ and groELS operons). Prevents heat-shock induction of these operons.
|
B8ZLY7
|
B7K765
|
TSAD_GLOC7
|
tRNA threonylcarbamoyladenosine biosynthesis protein TsaD
|
Gloeothece citriformis
|
MATILSIETSCDETAVAIVKNRNIYSNIVASQIDLHQTYGGVVPEVASRQHLETINPCLEQAFIEANLNWSDIDGIAATVAPGLIGALMVGVSAAKTLSILYQKPFIGVHHLEGHIYASYLSEPDLQPPFLCLLVSGGHTSLIYVKDCGIYEMLGSTRDDAAGEAFDKVARLLQLSYPGGPIIDRMAQTGNPHAFSLPEGRVSLPEGGYHPYDSSFSGLKTAVLRLVQKLEQDHLSLPVHDLAASFQETVARSLTKKTITCALDYNLTTIAVGGGVGANSALRKHLTSAATEHNLKVFFPPLKLCTDNAAMIGCAAADHFNRGHFSPLSIGVQSRLPITEVMKLYQ
|
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
|
B7K765
|
B8DBH8
|
ATPD_LISMH
|
F-type ATPase subunit delta
|
Listeria
|
MSKDLEVAGRYANALFQVAQDKDLVDVFSEELTELKAALNANKDFVKLLENPTFTTEQKKNLASAVFEKINPTLRDFIYLLIDRSREDYLSVIADVYQKRVNDLNGVADADVYSVVPLSEQELTALSRVFAAKMNKTKLNIQNHIDKSLLGGVKVVIGTRIYDDSLKTKLKDMERQIKA
|
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.
|
B8DBH8
|
Q3AV44
|
PNP_SYNS9
|
Polynucleotide phosphorylase
|
unclassified Synechococcus
|
MQGKTQSISFDGREIRLTTGRFAPQAGGSVLVECGDTAVLVTATRSKGRDGIDFLPLICDYEERLYAAGRIPGSYMRREARPPERATLTCRLIDRPMRPLFPSWMRDDLQVVATCLSLDERVPSDVLAVTGASIATLLAGIPFNGPMAAVRVGLLGDDFVLNPSYREIERGDLDLVVAGTADGVVMVEAGANQLPEGDVIEAIDFGYEAIQELIKAQETLLKDLGIKQVKPEAPKEDTTVPAYLEKQCTKAISAVLSKFEQSKEDRDNGLEAVKADAAEAIAALKEDDAVRQAVSSSSKLLGNSFKALTKKLMRQQILKDGKRVDGRGLDEVRQISAMAGVLPRRVHGSGLFQRGLTQVLSTATLGTPSDAQEMDDLHPNTEKLYLHHYNFPPYSVGETRPMRSPGRREIGHGALAERAILPVLPEKDTFPYVVRVVSEVLSSNGSTSMGSVCGSTLALMDAGVPLKAPVSGAAMGLIKEGKDIKILTDIQGIEDFLGDMDFKVAGSEKGITALQMDMKITGLPVKVMAEAVNQARPARLHILEKMLEAIDKPRETLSPHAPRLLSFRIDPELIGTVIGPGGRTIKGITERTNTKIDIEDSGIVTIASHDGAAAEEAQKIIEGLTRKVNEGEMFSGSITRIIPIGAFVEILPGKEGMIHISQLSEARVEKVEDVVKVGDEVTVRVREIDNRGRINLTLRGVPQSGESTEVEPQPTPVAPLS
|
Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
|
Q3AV44
|
A0QSG2
|
RS14Z_MYCS2
|
30S ribosomal protein S14 type Z
|
Mycolicibacterium
|
MAKKALVHKANKKPKFAVRAYTRCNKCGRPHSVYRKFGLCRICLREMAHAGELPGVQKSSW
|
Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site.
|
A0QSG2
|
Q49WZ1
|
KGUA_STAS1
|
GMP kinase
|
Staphylococcus
|
MDNEKGLLIVLSGPSGVGKGTVRKKIFDDPSTSYKYSISMTTRDKRQGEVDGVDYFFKAKSEFEELIKQDQFIEYAEYVGNYYGTPVQYVKDTMDRGYDVFLEIEVEGAKQVRKKFPDALFIFLAPPSLDHLRERLVGRGTESSEKIQSRVHEARKEVEMMNLYDYVVVNDEVELAKQRIQSIVEAEHLKRERIEAKYRKMILEAKK
|
Essential for recycling GMP and indirectly, cGMP.
|
Q49WZ1
|
Q4GWV4
|
DEFCG_CRAGI
|
Mantle defensin
|
Crassostrea
|
MKVFVLLTLAVLLMVSADMAFAGFGCPGNQLKCNNHCKSISCRAGYCDAATLWLRCTCTDCNGKK
|
Antibacterial peptide mostly active against Gram-positive bacteria (M.lysodeikticus, S.aureus, and the marine bacteria, B.stationis, and M.maritypicum) . It acts by selectively inhibiting peptidoglycan biosynthesis through complex formation with the cell wall precursor lipid II (1:1 molar ratio) thus inhibiting cell wall synthesis . It does not disrupt cell membranes . Is noticeably more potent than Cg-Defh1 . It shows no or limited activities against Gram-negative bacteria and filamentous fungi .
|
Q4GWV4
|
Q92S27
|
MURA_RHIME
|
UDP-N-acetylglucosamine enolpyruvyl transferase
|
Sinorhizobium
|
MDRIRIVGGNELHGVIPISGAKNAALPLMIASLLTDDTLTLENVPHLADVEQLIRILGNHGADISVNGRRERQGESYARTVHFTSRNIVSTTAPYELVSKMRASFWVIGPLLAREGKARVSLPGGCAIGTRPVDLFIEGLAALGANIEIDGGYVNATAPAGGLIGARYVFPKVSVGATHVLMMAATLANGTTVLGNAAREPEVVDLAKCLNAMGAKISGQGTSTVTIEGVRSLSGARHRVLPDRIETGTYAMAVAMAGGDVILEDTEASLLDTALEAIRRAGAQISETNSGIRIVRNGAGIKPVDIVTDPFPGFPTDLQAQFMGLMTRSSGVSHITETIFENRFMHVQELARLGAKISLSGQTAKVEGVSRLKGAPVMATDLRASVSLVIAGLAAEGETMVSRVYHLDRGFERLEEKLTRCGAHVERVSD
|
Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine.
|
Q92S27
|
Q60848
|
HELLS_MOUSE
|
Proliferation-associated SNF2-like protein
|
Mus
|
MAEQTEPAVITPAMLEEEEQLEAAGLEKERKMLEEAQKSWDRESTEIRYRRLQHLLEKSNIYSKFLLTKMEQQQLEEQKKKEKLEKKKRSLKLTEGKSLVDGNGEKPVMKKKRGREDESYNISEVMSKEEILSVAKKHKDNEDESSSTTSLCVEDIQKNKDSNSMIKDRLSQTVRQNSKFFFDPVRKCNGQPVPFQQPKHFTGGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPEIPTLLYHGTREDRRKLVKNIHKRQGTLQIHPVVVTSFEIAMRDQNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSLSETAEDIIAKEREQNVLHMLHQILTPFLLRRLKSDVALEVPPKREVVVYAPLCNKQEIFYTAIVNRTIANMFGSCEKETVELSPTGRPKRRSRKSINYSELDQFPSELEKLISQIQPEVNRERTVVEGNIPIESEVNLKLRNIMMLLRKCCNHPYMIEYPIDPVTQEFKIDEELVTNSGKFLILDRMLPELKKRGHKVLVFSQMTSMLDILMDYCHLRNFIFSRLDGSMSYSEREKNIYSFNTDPDVFLFLVSTRAGGLGINLTAADTVIIYDSDWNPQSDLQAQDRCHRIGQTKPVVVYRLVTANTIDQKIVERAAAKRKLEKLIIHKNHFKGGQSGLSQSKNFLDAKELMELLKSRDYEREVKGSREKVISDEDLELLLDRSDLIDQMKASRPIKGKTGIFKILENSEDSSAECLF
|
Plays an essential role in normal development and survival. Involved in regulation of the expansion or survival of lymphoid cells. Required for de novo or maintenance DNA methylation. May control silencing of the imprinted CDKN1C gene through DNA methylation. May play a role in formation and organization of heterochromatin, implying a functional role in the regulation of transcription and mitosis.
|
Q60848
|
B2TIH7
|
RL23_CLOBB
|
50S ribosomal protein L23
|
Clostridium
|
MKLTSHDIIRKPVITEKSMAAMAEKKYTFMVHVNANKSQVKRAVEEVFDVKVKDVNTINGLGKTKRMGVHVGKRSDYKKAIVTLTEESKAIEFFDGLQ
|
One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome.
|
B2TIH7
|
B1I4W9
|
RNPH_DESAP
|
tRNA nucleotidyltransferase
|
Candidatus Desulforudis
|
MIRVDGRAPAQMRPVYITRHYNKYAEGSALIEVGDTRVICTASIDNRVPTFLKGAGKGWVTAEFGMLPRATGVRGIRESVKGHPGGRSLEIQRLIGRSLRAVVDLPALGERTVILDCDVIQADGGTRTAAITGGFVALVDAMQTLVTEGVTPRLPVLDYVAATSVGLFEGEAVLDLCFAEDSAAEVDFNVVMTGTGRFVEVQGTGEGTTFERADVDRLLDLAVVGIRSLVEQQRAVLGSLAEEIGKRRGNQNGAAGTGDQK
|
Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation.
|
B1I4W9
|
Q1BRW0
|
RL5_BURCA
|
50S ribosomal protein L5
|
Burkholderia cepacia complex
|
MARFQEFYKEKVVPGLIEKFGYKSVMEVPRITKITLNMGLGEAIADKKIIENAVGDLTKIAGQKPVVTKARKAIAGFKIRQGYPIGAMVTLRGQAMYEFLDRFVTVALPRVRDFRGVSGRAFDGRGNYNIGVKEQIIFPEIDYDKIDALRGLNISITTTAKTDDEAKALLASFKFPFRN
|
This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.
|
Q1BRW0
|
B8DNL3
|
TIG_DESVM
|
PPIase
|
Desulfovibrio
|
MEYTVEDLSPVKKKVNISVPVEEVEAALSAAIAMYRTNMSLDGFRKGKVPSNLVESRFRKEIYGEATQDLVNVHINEVMTALDANPISRIDFDGGQLERGTPFEYSISFEVLPEFDLPDYDGFAVEQEKAVVDMKEVDEVITRIRTNMAELVPVAEARPGKDGDVVVLDFAAFENGEPVEGISAENFQMNLGDRQALEDFENLVKTLAPGQEGEGPLNFPADFINPDFAGKSLTVKVKVHAVKERRLPEANDELAQKAGGFESMDKMREAVTSSYMQSRTQLVKATAQKTMLDKLLKMVDFPLPESMVDMYVGHLLDDMRSKLERQGKSMESLGKKPEELRAEVRPEAEQVTRTQIFLLRAARKEGVEVNEQEIDGQIQQIAMRSGQDYNALKDYYIKNNLIFSLRDRMLADKAMDAIYEKAAVTEVEPAAK
|
Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
|
B8DNL3
|
Q28642
|
BKRB2_RABIT
|
B2 bradykinin receptor
|
Oryctolagus
|
MLNITSQVLAPALNGSVSQSSGCPNTEWSGWLNVIQAPFLWVLFVLATLENLFVLSVFCLHKSSCTVAEVYLGNLAAADLILACGLPFWAVTIANHFDWLFGEALCRVVNTMIYMNLYSSICFLMLVSIDRYLALVKTMSIGRMRRVRWAKLYSLVIWGCTLLLSSPMLVFRTMKDYRDEGYNVTACIIDYPSRSWEVFTNVLLNLVGFLLPLSVITFCTVQILQVLRNNEMQKFKEIQTERRATVLVLAVLLLFVVCWLPFQVSTFLDTLLKLGVLSSCWDEHVIDVITQVGSFMGYSNSCLNPLVYVIVGKRFRKKSREVYRAACPKAGCVLEPVQAESSMGTLRTSISVERQIHKLPEWTRSSQ
|
Receptor for bradykinin. It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system.
|
Q28642
|
Q2JV83
|
RL23_SYNJA
|
50S ribosomal protein L23
|
unclassified Synechococcus
|
MTESKRILADVLLRPVITEKATALMEQRKYVFEVMPTATKPLIRAAVEEMFGVRVTAVNTLKLPRKQRRVGRSVGYRSRPKRAIVTLAEGDSITLFPDT
|
One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome.
|
Q2JV83
|
P70445
|
4EBP2_MOUSE
|
Phosphorylated heat- and acid-stable protein regulated by insulin 2
|
Mus
|
MSASAGGSHQPSQSRAIPTRTVAISDAAQLPQDYCTTPGGTLFSTTPGGTRIIYDRKFLLDRRNSPMAQTPPCHLPNIPGVTSPGALIEDSKVEVNNLNNLNNHDRKHAVGDEAQFEMDI
|
Repressor of translation initiation involved in synaptic plasticity, learning and memory formation . Regulates EIF4E activity by preventing its assembly into the eIF4F complex: hypophosphorylated form of EIF4EBP2 competes with EIF4G1/EIF4G3 and strongly binds to EIF4E, leading to repress translation. In contrast, hyperphosphorylated form dissociates from EIF4E, allowing interaction between EIF4G1/EIF4G3 and EIF4E, leading to initiation of translation . EIF4EBP2 is enriched in brain and acts as a regulator of synapse activity and neuronal stem cell renewal via its ability to repress translation initiation . Mediates the regulation of protein translation by hormones, growth factors and other stimuli that signal through the MAP kinase and mTORC1 pathways .
|
P70445
|
B4T769
|
MDH_SALNS
|
Malate dehydrogenase
|
Salmonella
|
MKVAVLGAAGGIGQALALLLKNQLPSGSELSLYDIAPVTPGVAVDLSHIPTAVKIKGFSGEDATPALEGADVVLISAGVARKPGMDRSDLFNVNAGIVKNLVQQIAKTCPKACVGIITNPVNTTVAIAAEVLKKAGVYDKNKLFGVTTLDIIRSNTFVAELKGKRPTEVEVPVIGGHSGVTILPLLSQIPGVSFTEQEAAELTKRIQNAGTEVVEAKAGGGSATLSMGQAAARFGLSLVRALQGEKGVVECAYVEGDGQYARFFSQPLLLGKNGVEERKSIGTLSAFEQHSLDAMLDTLKKDIQLGEDFINK
|
Catalyzes the reversible oxidation of malate to oxaloacetate.
|
B4T769
|
P77888
|
PYRF_LACPL
|
OMP decarboxylase
|
Lactiplantibacillus
|
MKRPIIIALDFPTAERALAFLDQFPADLHVTVKIGMELFYAAGPSIVTDVQARGHAVFLDLKLHDIPNTVESAMRVIGRLGVTYTTVHAAGGHVMLSAAKRGLVAGAMAAGVTAPKLLAITQLTSTNQAILNQDQQIMGTVRASVVHYAKLARASDCDGVICSAQEVQAIHTAVGADFLGITPGIRPASAQSDDQQRVMTPAAAAKAGSNGLVIGRPITQAAEPVQAYRDIMTEWSN
|
Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).
|
P77888
|
Q46F67
|
CRCB1_METBF
|
Putative fluoride ion transporter CrcB 1
|
Methanosarcina
|
MGKLFLIGAGGFIGACLRYTVSSQVPRIKNIPAGTLTVNLLGTIVLAFLTFSSEPQSMVYLVNIGILGSFTTFSTFAYETFKLLEEGQNFSFFLNIFLNVALCLVGVSIAYLALSL
|
Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
|
Q46F67
|
Q2SFY4
|
CHEB2_HAHCH
|
Protein-glutamate methylesterase/protein-glutamine glutaminase 2
|
Hahella
|
MNAKIKVLLVDDSAVVRQVLQQVLERDKNIEVIGAAADPIFAQLRMSKQWPDVIVLDVEMPRMDGITFLKKLMAERPTPVVMCSTLTSKGAQTSMKALAAGAVAVVAKPAVGVKEYLESAAGELIMEIKAAAKANMRNMPAATASAQSMALPAKFSADAVIPLRTGGVIAGANKIAALGTSTGGTQALEYVLTRLPRNCPGIVIVQHMPEKFTAAFAERLNSICELEILEAESGHQVAPGRALIAPGGKHMLLRRSGAQYFVEIMSGPPVNRHRPSVDVLFRSVAQAAGRNALGVIMTGMGDDGAKGLLEMRNAGALTIGQDERSCIVYGMPKEAAKIGAVTREISLERIPQCVLDMGASLTASAQRG
|
Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid.
|
Q2SFY4
|
Q89MU0
|
RSMA_BRADU
|
S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase
|
Bradyrhizobium
|
MSAIDDLPPLREVIRQHALSARKSLGQNFLLDLNLTARIARAAAPLDNSTIVEIGPGPGGLTRALLALGARRVVAIEHDERAIPALQDISARYPGRLEIVHGDAMTFDPRPLLNGESAKIVANLPYNIATQLLINWLTTEPWPPWYDMMVLMFQREVGERIVAREDEEAYGRLGVLANWRCETKILFDIAPSAFVPPPKVTSSVVRLVPRAEPLPCDRKMLEQVAAAAFGQRRKMLRQSLKSLGVDPARLAQAAGVDATRRAETIPISGFVAMARELADIRSEG
|
Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
|
Q89MU0
|
B4HNS1
|
TRE12_DROSE
|
Facilitated trehalose transporter Tret1-2 homolog
|
Sophophora
|
MKILMRADTHVSYSVPAEGTKANFTFSQVLAALSVSLCSLVVGFVSAYTSPALVSMTDRTITSFEVTKDAGSWVGGIMPLAALAGGITGGPLIEYLGRRNTILATAVPFIVSSLLIACAVNVIMILCGRFLTGFCVGIASLSLPVYLGETLQPEVRGTLGLLPTALGNIGILVCYVAGSFMNWSILAFLGAALPVPFLILMIIIPETPRWFVNRGQEERARKALKWLRGKEADVEPELKDLMQSQAEADSQATRNTCLELFKRINLKPLSISLGLMFFQQFSGINAVIFYTVQIFKDAGSTIDSNLCTIIVGIVNFFATFMGIILIDRLGRKILLYVSDIAMILTLSILGGFFYCKAHGPDVSHLGWLPLSCFVIYILGFSLGFGPIPWLMMGEILPAKIRGPAASVVTAFNWFCTFVVTKTFQDLTVAMGPHGAFWLFGVVCIVGLFFVIIYVPETRGKSLEEIERKMMGRVPISAVVNIKPFSFNM
|
Fails to transport trehalose.
|
B4HNS1
|
P54017
|
RL2_METJA
|
50S ribosomal protein L2
|
Methanocaldococcus
|
MGKRLISQRRGRGSSVYTCPSHKRRGEAKYRRFDELEKKGKVLGKIVDILHDPGRSAPVAKVEYETGEEGLLVVPEGVKVGDIIECGVSAEIKPGNILPLGAIPEGIPVFNIETVPGDGGKLVRAGGCYAHILTHDGERTYVKLPSGHIKALHSMCRATIGVVAGGGRKEKPFVKAGKKYHAMKAKAVKWPRVRGVAMNAVDHPFGGGRHQHTGKPTTVSRKKVPPGRKVGHISARRTGVRK
|
One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome.
|
P54017
|
Q6A9J5
|
WHIA_CUTAK
|
Probable cell division protein WhiA
|
Cutibacterium
|
MALTLQVKNELATVPVQKLCCRRSEIAATLRFAGGIHLVQHRHLTIEAEVDTGGAARRLRQSIQEVFGFDTDLVVVNGAGLHSNTRYLIRMVRGGADLARLTGLLDRRGRPVRGLPVPIVGGGRCCQAAAWRGAFLARGSLTEPGRSMAMEITAPGEEAAMALVGAARRLDITAKQRESRHVDRVTIRDGDAISAMLTRMGAHESVLAWEDRRLRREVRASANRLANFDDANLRRSARAAVTASARVERALEILGDSVPDHLRAAGRLRLEHRNASLEELGKVHEPPLTKDAIAGRIRRLLALADKTARSNGEPTTLESLPVEMRDDRG
|
Involved in cell division and chromosome segregation.
|
Q6A9J5
|
Q21452
|
LIAS_CAEEL
|
Lipoic acid synthase
|
Caenorhabditis
|
MLARVWVRGLAATKKKPQVLVKDGPSLQDFISSASVAEAVEKYEGKLKLEKGDRRLRLPPWLKKEKILPSENENVSRLKKQLKHLKLATVCQEARCPNLGECWGGSDDSLATATIMLMGDTCTRGCKFCSVKTARAPPPLDPMEPENTSTAVASWGVEYIVLTSVDRDDLPDGGADHLRKTVQLMKLKKPELLIECLLPDFAGDKISVEKMATSGLDVYAHNIETVERLTPWVRDPRAKYRQSLDALRYAKEVSPKLITKTSIMLGLGEAEDEIKQCLADLRASNVDVVTFGQYMQPTKRHLLVKEWVTPEKFDQWAEYSKKLGFLYVASGPLVRSSYKAGEFYLKNVLRNRQN
|
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
|
Q21452
|
Q136E4
|
QUEF_RHOPS
|
PreQ(0) reductase
|
Rhodopseudomonas
|
MSRSPRKTPKSPSLQLGQAVEWPATPDAARLDRVPNPQAGTDYLVRFTAPEFTSLCPVTGQPDFAHLVIDYAPGAWLVESKSLKLYLASFRNHGGFHEDCTVSIGKRIAAEIKPKWLRIGGYWYPRGGIPIDVFWQTGKLPKGMWVPDQGVAPYRGRG
|
Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1).
|
Q136E4
|
O47688
|
COX3_TRASP
|
Cytochrome c oxidase polypeptide III
|
Tragelaphus
|
MTHQTHAYHMVNPSPWPLTGALSALLMTSGLTMWFHFNSMILLMLGLTTNMLTMYQWWRDIIRESTFQGHHTPVVQKGLRYGMILFIISEVLFFTGFFWAFYHSSLAPTPELGGCWPPTGIHPLDPLEVPLLNTSVLLASGVSITWAHHSLMEGHRNHMLQALFITIALGVYFTLLQASEYYEAPFTISDGVYGSTFFVATGFHGLHVIIGTTFLIVCFFRQLKFHFTSSHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS
|
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.
|
O47688
|
B1MBZ5
|
BIOD_MYCA9
|
Dethiobiotin synthase
|
Mycobacteroides abscessus
|
MTILLVTGTSTGVGKTVATAALAAAAVRQGIDVTVCKPVQTGDDHDAGEVARLSGVTRVQTLVRYPEPLAPVASASRAGLELLDHTQMATAIVALDRPGALTLVEGAGGLLVELAADGKTLRDLAMVLDAPVLVVTTADLGTLNHTALTLEALAVQSVPCAGLVVGSFPAEPDLAQRLNRENLANQFGTPVRAVIPEGAARLMPPVFAELSIELFEPQWVAGLVA
|
Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.
|
B1MBZ5
|
A3PLU2
|
RUVB_CERS1
|
Holliday junction ATP-dependent DNA helicase RuvB
|
Cereibacter
|
MTSSDPTLRPERLPEDMDRALRPQSLEEFVGQAEARANLRVFIESARMRGEAMDHTLFHGPPGLGKTTLAQIMARELGVGFRMTSGPVLAKPGDLAAILTNLEPRDVLFIDEIHRLSPVVEEVLYPALEDFALDLVIGEGPAARTVRIDLQPFTLVGATTRLGLLTTPLRDRFGIPTRLQFYTEDELDLIVARGARMMGVDSDPEGTREIARRARGTPRIAGRLLRRVVDFALVEGDGRLTQAIADRALTRLGVDHLGLDLGDRRYIGLIAENYGGGPVGIETIAAALSESRDAVEEVIEPYLLQQGLIQRTPRGRMLAHKAWRHMGIEPPKGPGQSDLFG
|
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.
|
A3PLU2
|
P29590
|
PML_HUMAN
|
Tripartite motif-containing protein 19
|
Homo
|
MEPAPARSPRPQQDPARPQEPTMPPPETPSEGRQPSPSPSPTERAPASEEEFQFLRCQQCQAEAKCPKLLPCLHTLCSGCLEASGMQCPICQAPWPLGADTPALDNVFFESLQRRLSVYRQIVDAQAVCTRCKESADFWCFECEQLLCAKCFEAHQWFLKHEARPLAELRNQSVREFLDGTRKTNNIFCSNPNHRTPTLTSIYCRGCSKPLCCSCALLDSSHSELKCDISAEIQQRQEELDAMTQALQEQDSAFGAVHAQMHAAVGQLGRARAETEELIRERVRQVVAHVRAQERELLEAVDARYQRDYEEMASRLGRLDAVLQRIRTGSALVQRMKCYASDQEVLDMHGFLRQALCRLRQEEPQSLQAAVRTDGFDEFKVRLQDLSSCITQGKDAAVSKKASPEAASTPRDPIDVDLPEEAERVKAQVQALGLAEAQPMAVVQSVPGAHPVPVYAFSIKGPSYGEDVSNTTTAQKRKCSQTQCPRKVIKMESEEGKEARLARSSPEQPRPSTSKAVSPPHLDGPPSPRSPVIGSEVFLPNSNHVASGAGEAEERVVVISSSEDSDAENSSSRELDDSSSESSDLQLEGPSTLRVLDENLADPQAEDRPLVFFDLKIDNETQKISQLAAVNRESKFRVVIQPEAFFSIYSKAVSLEVGLQHFLSFLSSMRRPILACYKLWGPGLPNFFRALEDINRLWEFQEAISGFLAALPLIRERVPGASSFKLKNLAQTYLARNMSERSAMAAVLAMRDLCRLLEVSPGPQLAQHVYPFSSLQCFASLQPLVQAAVLPRAEARLLALHNVSFMELLSAHRRDRQGGLKKYSRYLSLQTTTLPPAQPAFNLQALGTYFEGLLEGPALARAEGVSTPLAGRGLAERASQQS
|
Exhibits antiviral activity against both DNA and RNA viruses. The antiviral activity can involve one or several isoform(s) and can be enhanced by the permanent PML-NB-associated protein DAXX or by the recruitment of p53/TP53 within these structures. Isoform PML-4 restricts varicella zoster virus (VZV) via sequestration of virion capsids in PML-NBs thereby preventing their nuclear egress and inhibiting formation of infectious virus particles. The sumoylated isoform PML-4 restricts rabies virus by inhibiting viral mRNA and protein synthesis. The cytoplasmic isoform PML-14 can restrict herpes simplex virus-1 (HHV-1) replication by sequestering the viral E3 ubiquitin-protein ligase ICP0 in the cytoplasm. Isoform PML-6 shows restriction activity towards human cytomegalovirus (HHV-5) and influenza A virus strains PR8(H1N1) and ST364(H3N2). Sumoylated isoform PML-4 and isoform PML-12 show antiviral activity against encephalomyocarditis virus (EMCV) by promoting nuclear sequestration of viral polymerase (P3D-POL) within PML NBs. Isoform PML-3 exhibits antiviral activity against poliovirus by inducing apoptosis in infected cells through the recruitment and the activation of p53/TP53 in the PML-NBs. Isoform PML-3 represses human foamy virus (HFV) transcription by complexing the HFV transactivator, bel1/tas, preventing its binding to viral DNA. PML may positively regulate infectious hepatitis C viral (HCV) production and isoform PML-2 may enhance adenovirus transcription. Functions as an E3 SUMO-protein ligase that sumoylates (HHV-5) immediate early protein IE1, thereby participating in the antiviral response . Isoforms PML-3 and PML-6 display the highest levels of sumoylation activity .
|
P29590
|
Q9PU85
|
PIM3_COTJA
|
qpim
|
Coturnix
|
MLLSKFGSLAHICSPASMDHLPVKILPPVKVEKEPFDKVYQVGSVLGSGGFGTVYAGSRTADGLPVAVKHVVKERVTEWGTIGGVMVPLEIVLLKKVGSGFRGVIKLLDWYERPDGFLIVMERPELVKDLFDFITEKGALDEDTARGFFRQVLEAVRHCYGCGVVHRDIKDENLLVDLRTGELKLIDFGSGALLKDTVYTDFDGTRVYSPPEWIRYHRYHGRSATVWSLGVLLYDMVCGDIPFEQDEEILRGRLYFRRRISPECQQLIKWCLSLRPSDRPTLEQIFDHQWMHKSEVVKSEDCDIRLRTLDTDVSSTSSSNESL
|
Proto-oncogene with serine/threonine kinase activity that can prevent apoptosis and promote cell survival and protein translation.
|
Q9PU85
|
Q6NET5
|
PCKG_CORDI
|
Phosphoenolpyruvate carboxykinase [GTP]
|
Corynebacterium
|
MSTVSIKGLEGEAPTKNEVLLNWIAENVELFQPDRVVFADGSQEEWDRLTTQLVESGTLIRLNEEKRPNSFLARSNPADVARVESRTFICTPTPEGAGPTNHWADPAEMKAELTERFRGSMKGRTMYVVPFCMGPINDPAPKLGVQLTDSEYVVLSMRIMTRMGAEALAKIGDTGSFVPCLHSVGAPLEPGQEDVAWPCNEEKYITHFPETKEIWSYGSGYGGNAILAKKCYALRIASVMAKEEGWMAEHMLILKLTSPEKKVYYIAAAFPSACGKTNLAMLQPTIDGWSAEVVGDDIAWLRFGEDGRLYAINPENGFFGVAPGTNYSSNPNAMRTMEPGNTLFTNVALTDDGDIWWEDLENMPEHLTDWLGNDWTPESSQPSSHPNSRYCVPLAQCPVAAEEYNDPQGVPISAILFGGRRPDTVPLVSQAHNWDHATMIGALLSSGQTAAAEGTVGALRHDPMAMLPFIGYNAADYLQHWIDMGKKGGDKMPEVFLVNWFRRGDDGRFLWPGFGDNSRVLKWIVDRIEGRVEADETIAGYTARVEDLDLTGLDTPIEDIREALSAPAAQWKSDLADNEEYLTFLGSKGSAVPAEVLEQFEALKARVAAAES
|
Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle.
|
Q6NET5
|
A8FP22
|
RS10_CAMJ8
|
30S ribosomal protein S10
|
Campylobacter
|
MERIRLKLKAYDHRVLDRTVAAIVEAVKRTGADIRGPIPMPTKIKRYTVLKSPHINKDSREQFEIRIHARMLDIVAATPDTVDSLTKLDLAPEVSVEVRAMGK
|
Involved in the binding of tRNA to the ribosomes.
|
A8FP22
|
Q6L1W3
|
ATGT_PICTO
|
Archaeal tRNA-guanine transglycosylase
|
Picrophilus
|
MEILFRENLARIARFKTPHGEIETPTVMPVINPNLNFLDESTLRSYGVQAVITNSYIIKRNQRLNEDALRHGLHSLIKFSGPIMTDSGTFQSHVYGDIEYSNKEIVDFQKAIGSDIITILDVFTEPDESYNSARSKVIETYKRLKEIDFEDKIIAGPVQGSIYPDLRRLSAYLMSDALYLPIGGVVPLLESYRYSDLVKIIFNSKVSSDFSRPVHLFGGGHPMFFAFAVMLGVDLFDSASYIKYAKDNRLLYSEGTRALNDIREFPEWSPIHGKYTPQELLHEESEKRTRMLALHNLKSIFIEINEIKERIYENTLYNYVEEKARSHPALFKAFMSMINYDTSDYSPLSYKSPFFYYDKTSLNHPIIKRIMKFTENYISNSRHTLIISSKYWRPGVKNENVIKNIVECTDFNLLVSWNGIYIPLFLEDSYPVQQLVSSGLNDKKLEEDYLKRLKSINNDIEFYEGEHYDKRLRDYDTEKINTIAMFQFNINERFFDKSNIIKSKSTGHIRNIIEDNNIIATMRNDGYLTLSIKGAYRLLSMKPWPGLRVVVDDESGRFNANGYNVFFKFIKSFDTGIIPGNETLVVSEDDDLYAVGKAAVSGIEMYYYKSGVAVKVHEGVNKKAA
|
Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs.
|
Q6L1W3
|
C1B0C2
|
PSD_RHOOB
|
Phosphatidylserine decarboxylase beta chain
|
Rhodococcus
|
MARKPTPPGTPQPTSVGHIVDLVRGAVPPLHPAGLPFVLAPLGVAVLGRNRKWVRRGALTSAAACAAFFRHPHRVPPNRVGVAVAPADGEVALVDSAVPPSELDMGTEPLPRVSIFLSVLDVHVQRSPVGGEVTKVVHRSGQFLSADLADASEVNERNSMLLHTAEGHDVAVIQIAGLLARRIVCDAKVGDTLPIGDTYGLIRFGSRVDTYFPAGTTLLAERGQRTIGAETVIAQLP
|
Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
|
C1B0C2
|
Q9JSY6
|
UPPP_NEIMA
|
Undecaprenyl pyrophosphate phosphatase
|
Neisseria
|
MDFLIVLKALMMGLVEGFTEFLPISSTGHLIVFGNLIDFHSNHKVFEITIQLGAVLAVVFEYRQRFSNVLHGVGKDRKANRFVLNLAIAFIPAAVMGLLFGKQIKEYLFNPLSVAVMLVLGGFFILWVEKRQSRAEPKIVDVDALRPIDALMIGVAQVFALVPGTSRSGSTIMGGMLWGIERKTATEFSFFLAVPMMVAATAYDVLKHYRFFTLHDVGLILIGFVAAFVSGLVAVKALLRFVSKKNYIPFAYYRIVFGIAIIILWLSGWISWE
|
Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
|
Q9JSY6
|
A6NJ69
|
IGIP_HUMAN
|
IgA-inducing protein homolog
|
Homo
|
MCSYYHMKKRSVSGCNITIFAVMFSHLSAGKSPCGNQANVLCISRLEFVQYQS
|
Enhances IgA secretion from B-cells stimulated via CD40.
|
A6NJ69
|
A1KUK1
|
ISCS_NEIMF
|
Cysteine desulfurase IscS
|
Neisseria
|
MTVKTPVYLDYAATTPVDKRVAEKMIPYLTETFGNPASNSHAFGWEAEEAVEKARADIAALINADPKEIVFTSGATESDNLAIKGAANFYKTKGKHLITVKTEHKAVLDTMRELERQGFEVTYLGVQENGLIDLEELKAAIRDDTILISVMWANNEIGVVQDIPAIGEICRERKIVFHVDAAQACGKVPVDVEAAKIDLLSMSAHKVYGPKGIGALYVRRKPRVRLEAQMHGGGHERGFRSGTLPTHQIVGMGEAFRIAKEELEQDMAHYRKLRDIFLKGIEGIEEVYINGDLEHRAPNNLNVSFNFVEGESLIMAVKELAVSSGSACTSASLEPSYVLRALGRNDELAHSSLRITFGRMTTEEEVQFAAELIKSKIGKLRELSPLWEMFKDGIDLNSIEWAAH
|
Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins.
|
A1KUK1
|
Q9JM55
|
TOB2_MOUSE
|
Transducer of erbB-2 2
|
Mus
|
MQLEIKVALNFIISYLYNKLPRRRADLFGEELERLLRKKYEGHWYPEKPLKGSGFRCVHIGEVVDPVVELAAKRSGLAVEDVRANVPEELSVWIDPFEVSYQIGEKGVVKVLYLGDSEASGTPELDKEIKSSFNPDAQVFVPIGSQDSSLSSSPSPSFGQSPSPTFIPRSAQPITFTTASFAATKFGSTKMKKGGGASGGVSVGGSGAGGQQPPPQQPRMARSPTKNLLKHKSLSLSMHSLNLIPANPAPQSQLSPNAKEFVYNGGGSPSLFFDGVEGPSTSTTAPFGSGGASTCNSSSFDVSQVFGGGANSLFLEKSPFVEGLSYNLNTMQYPNQPFQPVVLAN
|
Anti-proliferative protein inhibits cell cycle progression from the G0/G1 to S phases.
|
Q9JM55
|
Q31WF1
|
IDI_SHIBS
|
Isopentenyl pyrophosphate isomerase
|
Shigella
|
MQTEHVILLNAQGVPTGTLEKYAAHTADTLLHLAFSSWLFNAKGQLLVTRRALSKKAWPGVWTNSVCGHPQLGESNEDAVIRRCRYELGVEITPPESIYPDFRYRATDPNGIVENEVCPVFAARTNSALQINDDEVMDYQWCDLADVLHGIDATPWAFSPWMVMQAANSEARKLLSAFAQHN
|
Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).
|
Q31WF1
|
Q21VE7
|
KUP2_ALBFT
|
Probable potassium transport system protein kup 2
|
Rhodoferax
|
MSRTSNRESLAALTLGAMGVVYGDIGTSPLYTMKEVFSPATGVPLDGVHLIGAVSVIFWGLMMVVTLKYVLLILRADNRGEGGIMALTALAANAAGKTARRRTVLLLMGVFGAALFYGDSVITPAISVLSAVEGLEVVTPAFKSYVLPISVTVLIGLFAVQRFGTSLVGKLFGPVIMLWFAVLSVTGVAEIIQQPAILAALNPLNAFEFLRSQGWHMFVAVGAIVLAFTGVEALYADMGHFGKRPIQLAWLGLVLPALAINYMGQGALLMRDPSALANPFYRLFPQAWLMPAVVLATLATVIASQAVISGAYSMTKQAVLLGLLPRMQVQYTSAKEIGQIYMPEVNWLLLISVLLAVVGFGSSSALASAYGIAVTMTMLITTALTFFVVRDGWGYPLPVALAATAVFLALDTLLVVSCSLKFFQGGWFPLVLGLVIFTVMATWRRGRELLIDNIRHDDPELLPFITALSADVVHRVPRTAVYTVANPDTVPQALMHNLKHNQVLHERNVILTVVFHDVPWIAFDERVQVKPLVPGFWKVQVNYGFKNAPDIPRALELCQSQGLSINLFETSYFLSREIVVPTKGAGMAHWREALFAIMSRNAGSVADFFRLPNNCVIELGTRVQI
|
Transport of potassium into the cell.
|
Q21VE7
|
B8XA41
|
SBS_SOLHA
|
(-)-endo-alpha-bergamotene synthase ((2Z,6Z)-farnesyl diphosphate cyclizing)
|
Solanum subgen. Lycopersicon
|
MIVGYRSTIITLSHPKLGNGKTISSNAIFQRSCRVRCSHSTPSSMNGFEDARDRIRESFGKVELSPSSYDTAWVAMVPSKHSLNEPCFPQCLDWIIENQREDGSWGLNPSHPLLLKDSLSSTLACLLALTKWRVGDEQIKRGLGFIETQSWAIDNKDQISPLGFEIIFPSMIKSAEKLNLNLAINKRDSTIKRALQNEFTRNIEYMSEGVGELCDWKEIIKLHQRQNGSLFDSPATTAAALIYHQHDKKCYEYLNSILQQHKNWVPTMYPTKIHSLLCLVDTLQNLGVHRHFKSEIKKALDEIYRLWQQKNEQIFSNVTHCAMAFRLLRMSYYDVSSDELAEFVDEEHFFAISGKYTSHVEILELHKASQLAIDHEKDDILDKINNWTRTFMEQKLLNNGFIDRMSKKEVELALRKFYTISDLAENRRCIKSYEENNFKILKAAYRSPNIYNKDLFIFSIRNFELCQAQHQEELQQFKRWFEDYRLDQLGIAERYIHDTYLCAVIVVPEPELSDARLLYAKYVLLLTIVDDQFDSFASTDECLNIIELVERWDDYASVGYKSEKVKVFFSTLYKSIEELVTIAEIKQGRSVKNHLLNLWLELVKLMLMERVEWFSGKTIPSIEEYLYVTSITFGARLIPLTTQYFLGIKISEDILESDEIYGLCNCTGRVLRILNDLQDSKKEQKEDSVTIVTLLMKSMSEEEAIMKIKEILEMNRRELLKMVLVQKKGSQLPQICKDIFWRTSNWADFIYLQTDGYRIAEEMKNHIDEVFYKPLNH
|
(2Z,6Z)-farnesyl diphosphate cyclizing enzyme. Produces (+)-alpha-santalene, (+)-endo-beta-bergamotene, (-)-endo-alpha-bergamotene, and at lower amounts, (-)exo-alpha-bergamotene and (+)-epi-beta-santalene. Not able to use geranyl diphosphate, E,E-farnesyl diphosphate or E,E,E-geranylgeranyl diphosphate as substrates, but able to use Neryl diphosphate to make the monoterpene terpineol.
|
B8XA41
|
Q8LK61
|
GAPN_WHEAT
|
Triosephosphate dehydrogenase
|
Triticum
|
MAGTGVFADVLDGEVYKYYADGEWRASASGKTVAIVNPTTRQTQYRVQACTQEEVNKVMDAAKVAQKSWARTPLWKRAELLHKAAAILKEHKTPIAESLVKEIAKPAKDAVSEVVRSGDLVSYTAEEGVRILGEGKLLVSDSFPGNERNKYCLSSKVPLGVVLAIPPFNYPVNLAVSKIGPALIAGNSLVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGGDTGIAISKKAGMVPLQMELGGKDACIVLEDADLDLVAANIVKGGFSYSGQRCTAVKVVLIMEAVADTVVEKVNAKLAKLKVGPPEDDSDITPVVTESSANFIEGLVMDAKEKGATFCQEYRREGNLIWPLLLDHVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAIMISDAMESGTVQINSAPARGPDHFPFQGLKDSGIGSQGITNSINMMTKVKSTVINLPSPSYTMG
|
Important as a means of generating NADPH for biosynthetic reactions.
|
Q8LK61
|
A0LE46
|
RSMG_MAGMM
|
16S rRNA 7-methylguanosine methyltransferase
|
Magnetococcus
|
MENFRYEIESMLQLVGVDMDVISVDPYSDEKLAEFVSELLLWNKKINLIGKSTEKSIWSRHIAESLILLPYVQGSTVLDMGTGAGLPGLPLQIVSGSNIEMHLVEKDQKKVSFLKHVSANLNLKNIRIYNKQFTEKGFDGAPLVNVVTSRALAEINQLVAWADPCLVNGGSLVLIKGPVCKAELEKFEESDLSDKYENGEIVEYKIDSHDVNIVIIKKK
|
Specifically methylates the N7 position of guanine in position 527 of 16S rRNA.
|
A0LE46
|
Q9YGJ6
|
3S1A1_NAJSP
|
Alpha-neurotoxin NTX-1
|
Naja
|
MKTLLLTLLVVTIVCLDLGYTLECHNQQSSETPTTTGCSGGETNCYKKSWRDHRGYRIERGCGCPSVKKGIEINCCTTDRCNN
|
Binds to muscle nicotinic acetylcholine receptor (nAChR) and inhibit acetylcholine from binding to the receptor, thereby impairing neuromuscular transmission.
|
Q9YGJ6
|
C1F1B8
|
MSRA_ACIC5
|
Peptide-methionine (S)-S-oxide reductase
|
Acidobacterium
|
MAKATFGAGCFWGVEASFRQLHGVQDVAAGYEGGKLDNPTYRDVCTDLTGHAEVVEIDFNPDEIRFEQLLEAFFGLHDPTQLNRQGPDWGTQYRSVIFYHSPEQQTVAQAFIDRLTAEKRFPRPIVTQVVPAATFWRAEEYHQRYLEKRGLATCHI
|
Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
|
C1F1B8
|
A6V936
|
DAPE_PSEA7
|
N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase
|
Pseudomonas
|
MTASSPSLSPTLELACELIRRPSVTPVDADCQALMMRRLEAAGFALEPMRIEEVDNFWARRGGDGPVLCFAGHTDVVPTGPVQAWQHQPFDALIDEQGMLCGRGAADMKGSLASMIVAVERFVADHPGHKGAIAFLITSDEEGPAHHGTKAVVERLAARGERLDWCIVGEPSSTSLVGDVVKNGRRGSLGARLTIRGVQGHVAYPHLAKNPIHLAAPALAELAAEHWDDGNAFFPPTSFQISNLNSGTGATNVIPGELSALFNFRFSTESTVEGLQKRVEAILDKHGLDWHVEWALSGLPFLTEPGELLDAVAASIKAVTGRETRPSTSGGTSDGRFIATMGTQVVELGPVNATIHQVNERVLASDLELLTEIYYQTLVRLLA
|
Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls.
|
A6V936
|
Q5AZ85
|
RGLB_EMENI
|
Rhamnogalacturonate lyase B
|
Aspergillus subgen. Nidulantes
|
MRLGVCFSLAAAASVARAALTATENDTSIVLENDRLRATFDKGRGSIIDLYLDGQDFLGPQSGSTGIGPYLDCYCTPSGFYTAGSTNPVTELVQGTDSTGTKYAGIILNDTYTPTGQEFQQYWFLRDGETGFHMFSRLAYYNETTPFLRNLQELRTLFRPNTDLWTHLTSSDLQTAPLPSDEAIAEQIVVQDATWRLNNTPDDAYYQQFSEYFTKYTFSNHWRDNDVHGLYADGSTSDGTTYGAWLVMNTKDTYYGGPLHSDLTVDGIIYNYIVSNHHGEGTPNITNGFDRTFGPQFYLFNGGGSSSLEELRDEARSLASPSWNADFYDSIAKHVIGYVPSSQRGSVKGTIKLPKNAKSPIAVLTVDGHYFQDNSAVPSSHQYWADIDKNGRFSIDRVVAGKYRLTVYADGIFGDFTRDGIVVKARKSTSIKETWKPESAGTEIWRLGTPDKSSGEFRHGAARDPTHPRHPPEYLIYWGAYDWQSDFPGGIDYMIGESDPATDFNTVHWAVFGPTPDNPVAESNTTHDWRIRFDLSAKQLHARKTATLTIQLAGAKAASGNTDVYNASEPYANLPLRSYINEQEEPLTMVIGYDQSSSCIVRSAVSCYQVREKWEFPASWLKEGSNLLRLSLPTNGTNYESAVLPTSVYVQYDALRLELK
|
Pectinolytic enzymes consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Degrades the rhamnogalacturonan I (RG-I) backbone of pectin. Active against linseed rhamnogalacturonan.
|
Q5AZ85
|
A7HL08
|
RIMP_FERNB
|
Ribosome maturation factor RimP
|
Fervidobacterium
|
MSLSQKEIIERVRAIAEPIVTSMGLELFDVKYRIQAGKWVLSIIIDKLDDYVSTRDCELVSYEIEKVLDSHDFIPGRYYLEVSSPGLDRPLKKIEDFRRFVGKLVKVKTKKTYRGYIVDVNMETKEIILRVDNENITIKYDDVKSANLEIEL
|
Required for maturation of 30S ribosomal subunits.
|
A7HL08
|
Q67IC4
|
NU2C_ASPOF
|
NADH-plastoquinone oxidoreductase subunit 2
|
Asparagus
|
MIWHVQNENFILDSTRILMKAFHLLLFHGSFIFPECILIFGLILLLMIDSTSDQKDRPWFYFISSTSLVMSITALLFRWKEEPIISFSGNFQTNNFNEIFQFLILLCSTLCIPLSVEYIECTEMAITEFLLFVLTATLGGMFLCGANDLITIFVAPECFSLCSYLLSGYTKRDVRSNEATTKYLLMGGASSSILVHGFSWLYGSSGGEIELQEIVNGLINTQMYNSPGISIALISTTVGIGFKLSPAPFHQWTPDVYEGSPTPVVAFLSVTSKVAASASATRIFDIPFYFSSNEWHLLLEILAILSMILGNLIAITQTSMKRMLAYSSIGQIGYVIIGIIVGDSNDGYASMITYMLFYISMNLGTFARIVSFGLRTGTDNIRDYAGLYTKDPFLALSSALCLLSLGGLPPLAGFFGKLYLFWCGWQAGLYFLVSIGLLTSVVSIYYYLKIIKLLMTGRNQEITPHVRNYRRSPLRSNNSIEWSMTVCVIASTIPGISMNPILAIAQDTLF
|
NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
|
Q67IC4
|
Q57RG9
|
HUTG_SALCH
|
Formiminoglutamate hydrolase
|
Salmonella
|
MTQWYPASPALWQGRDDSIEAPDARRLFQTVTRSETFFPENWQQKIALMGFACDEGVKRNSGRPGAAGAPDALRKALANMASHQGHERLVDLGNWVAPTPDLEGAQQALRDAVSRCLRAGMRTLVLGGGHETAFGHGAGVLDAFAQESVGIINLDAHLDLRQTDRATSGTPFRQLAQLCDAQSRAFHYACFGVSRAANTQALWREAQWRNVTVVEDLDCHDALAQMTQFIDKVDKIYLTIDLDVLPVWEMPAVSAPAALGVPLIQVLRLIEPVCRSGKLQAADLVEFNPRFDEDGAAARVAARLGWQIAHWWR
|
Catalyzes the conversion of N-formimidoyl-L-glutamate to L-glutamate and formamide.
|
Q57RG9
|
B0TUS0
|
SEQA_SHEHH
|
Negative modulator of initiation of replication
|
Shewanella
|
MKYIEVDEELYRHIASKTEHIGESASDILRRILGLQVESVVQDAPEEISHPSLERVSPKPVKVAKVITKMTSTAVSDFTSLIDADVLAAQKGAVGRFLFILDTVHRASPVQFEQVLQIQGRDRLYFATSKDALLKASKSANPKEIGQSGFWVTTNNNTAKKRTILSEVLLQFGTDEAQVTDIIEKI
|
Negative regulator of replication initiation, which contributes to regulation of DNA replication and ensures that replication initiation occurs exactly once per chromosome per cell cycle. Binds to pairs of hemimethylated GATC sequences in the oriC region, thus preventing assembly of replication proteins and re-initiation at newly replicated origins. Repression is relieved when the region becomes fully methylated.
|
B0TUS0
|
B5XLX5
|
DLTA_STRPZ
|
D-alanine-activating enzyme
|
Streptococcus
|
MIKDMIASIEQFAQTQADFPVYDCLGERRTYGQLKRDSDSIAAFIDSLALLAKSPVLVFGAQTYDMLATFVALTKSGHAYIPVDVHSAPERILAIIEIAKPSLIIAIEEFPLTIEGISLVSLSEIESAKLAEMPYERTHSVKGDDNYYIIFTSGTTGQPKGVQISHDNLLSFTNWMIEDAAFDVPKQPQMLAQPPYSFDLSVMYWAPTLALGGTLFALPKELVADFKQLFTTIAQLPVGIWTSTPSFADMAMLSDDFCQAKMPALTHFYFDGEELTVSTARKLFERFPSAKIINAYGPTEATVALSAIEITREMVDNYTRLPIGYPKPDSPTYIIDEDGKELASGEQGEIIVTGPAVSKGYLNNPEKTAEAFFTFKGQPAYHTGDIGSLTEDNILLYGGRLDFQIKYAGYRIELEDVSQQLNQSPMVASAVAVPRYNKEHKVQNLLAYIVVKDGVKERFDRELELTKAIKASVKDHMMSYMMPSKFLYRDSLPLTPNGKIDIKTLINEVNNR
|
Catalyzes the first step in the D-alanylation of lipoteichoic acid (LTA), the activation of D-alanine and its transfer onto the D-alanyl carrier protein (Dcp) DltC. In an ATP-dependent two-step reaction, forms a high energy D-alanyl-AMP intermediate, followed by transfer of the D-alanyl residue as a thiol ester to the phosphopantheinyl prosthetic group of the Dcp. D-alanylation of LTA plays an important role in modulating the properties of the cell wall in Gram-positive bacteria, influencing the net charge of the cell wall.
|
B5XLX5
|
P48124
|
RK12_CYAPA
|
50S ribosomal protein L12, cyanelle
|
Cyanophora
|
MSSKTDEILEQLKGLTLIEAADLVKAIEEAFGVDASAPVGGGMVMMAPAAGGGADAAEEKSAFDLVLEEVPADKKIAVLKVVRSLTNLGLKEAKDLVEATPKVVKEGASKDELKQLKKNLKQLEQK
|
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation.
|
P48124
|
B6JM18
|
SECA_HELP2
|
Protein translocase subunit SecA
|
Helicobacter
|
MIKAIIGKIIGTRNDRWIKQYKKQVLTINALEPTYEKMSDVELQNAFEELKKRVRSTEKDLQEKTLLEVLPESFAITREASKRILKMRHFDVQLIGGMVLNDGKIAEMKTGEGKTLVATLAVALNALKGESVYVVTVNDYLAHRDSKEMEPLYHFLGYSVGTITASVRDDDERLEIYSKDIVYGTNNEFGFDYLRDNMKYSLEHKVQKSHAFAIVDEVDSILIDEARTPLIISGPVDRRMENYNKADEVAKSMQVEIDFTIDEKNRAILITEEGIKKAENLFGVDNLYKIENAALSHHLDQALKANYLFFIDKDYIVANNEVVIVDEFTGRLSEGRRFSEGLHQALEAKEGVSIKEESQTLADITFQNYFRMFSKLAGMTGTAQTEATEFLEIYNLEVVSIPTNLAIKRKDLNDLIYKSEKEKFDAVILKIKELHDKGQPVLVGTASIEKSETLHALLKKERIPHTVLNAKQHTKEAEIIKDAGLKGAVTIATNMAGRGVDIKLTDEIKELGGLYIIGTERHESRRIDNQLRGRSGRQGDPGTSQFYLSLEDNLLRIFGSDRIKGVMEKLGLKDGEHIESKLVTRAVENAQKKVENLHFESRKHLLEYDDVANEQRKSVYKFRDELLDASYDIGAKIAENREYALNQIFSKLKAFDHQNLSEEELLGLKNVLKEDFNAHVALEDLEKASPIEKFVAEKLKSDYENKMKVLDSEQRSRIERIVYLQILDNAWREHLYTMDNLKTGINLRGYNQKDPLVEYKKESYNLFLEFIEDIKIEAIKTFSKIQFENEQDSSDAERYLDNFSEEREHESVTYRHEETLDEDLNVAMKAFAKTPKRNEPCPCQSGKKYKDCCAKSGPKKGLFAK
|
Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
|
B6JM18
|
A0RQJ3
|
EFTU_CAMFF
|
Elongation factor Tu
|
Campylobacter
|
MAKEKFSRNKPHVNIGTIGHVDHGKTTLTAAISAVLSRRGLAELKDYDNIDNAPEEKERGITIATSHIEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLSRQVGVPYIVVFMNKADMVDDAELLELVEMEIRELLSEYDFPGDDTPIISGSALQALEEAKAGNDGEWSAKIMDLMAAVDSYIPTPVRATDKDFLMPIEDVFSISGRGTVVTGRIEKGIVKVGDTIEIVGIRDTQTTTVTGVEMFRKEMDQGEAGDNVGVLLRGTKKEDVERGMVLCKPKSITPHTKFEGEVYILTKEEGGRHTPFFNNYRPQFYVRTTDVTGSITLPEGTEMVMPGDNLKITVELINPVALEDGTRFAIREGGRTVGSGVVSKIIA
|
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
|
A0RQJ3
|
A5F850
|
FABA_VIBC3
|
Trans-2-decenoyl-[acyl-carrier-protein] isomerase
|
Vibrio
|
MQNKRDSYNREDLLASSQGELFGEGYPQLPAPNMLMMDRITKMSETEGEFGKGLILAELDITPDLWFFDCHFPGDPVMPGCLGLDAMWQLVGFFLGWVGGKGKGRALGVGEVKFTGQILPTAKKVTYEINMKRVVNRKLVMGLADGRVLVDGKEIYVAKDLKVGLFQDTSAF
|
Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E-(2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length.
|
A5F850
|
A7IHF1
|
GCSH_XANP2
|
Glycine cleavage system H protein
|
Xanthobacter
|
MTSVRYTKDHEYVRVEGDVAVVGISDYAQQQLGDVVFVELPEIGKVVTKGGEAAVVESVKAASEVYAPLSGEVVEVNSELEGAPGLVNEAPEGKGWFMKLKLSNPAELDELLNEHAYKDFLDTLA
|
The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein.
|
A7IHF1
|
Q8GXE6
|
AKT6_ARATH
|
Shaker pollen inward rectifier K(+) channel
|
Arabidopsis
|
MEKKKVWFWGVKDDGEGGGGRGGGRTKDAEDDVADHLSRDGTMSQYSLSKGLLPSLGANNRSSRDVILPRFIVSPFDPRYRAWETFLVFLVLYTAWASPFEFGFLQKPRPPLSILDNIVNGFFAVDIVLTFFVAFLDKVTYLLVDDPKRIAWRYASTWLIFDVVSTFPYEIFGSLLHESIQGYGIFSMLRLWRLRRVSNCFARLEKDRKYSYFWVRCSKLLLVTLFVIHCGACFLYSIAAHYPDPSKTFMALTDENWKESPIAVRYNTAMYWSITTFSTTGYGDIHGVNSREMTFILFYMVFNLGLSAYIIGNMTNLVVHVTGRTRKFRDTIQAASGFGQRNNLPVRLQDQMVAHLCLRYRTDSEGLQQQEIIDSLPKAIRSSISHYLFYEVVDKIYLFHGISNDLLFQLVTEMKAEYFPPKEDVILQNEAPTDFYILVTGAVDIIARVNGVEQVVSEAQRGHVFGEVGVLCYRPQLFTVRTKRLSQLLRLNRTVLLNLVQANVGDGAIIMNNLLQHLKDSEDPVMKGVLADTEHMLAQGKMDLPLSLCFAAARGDDLLLHQLLRRGSSPNEMDKDGRTALHIAASKGSHYCVVLLLEHGADPNIRDSEGNVPLWEAIIGRHREIAKLLAENGAKLSLDSVSYFSGLAVEKNCLDALKDIIKYGGDVTLPDGNGTTALHRAVSEGHLEIVKFLLDQGADLDWPDSYGWTPRGLADHQGNEEIKTLFHNHRPVEKKPKPIPGIPQSPVTGKPLMKYSSEPTMHSGELVLDGGQVVVSQKRKLNNFRNSLFGIISAANSADDGGEVPRSPAVPGGGGSMIYPERVTISSPENGETGGKVVLLPNSMEELLKIGENKMGFVPTKVLTREGAEIDDITLIRDGDFLLLSRDP
|
Highly selective inward-rectifying potassium channel that could mediate potassium uptake in the pollen membrane. Plays an important role in pollen tube development. Assuming opened or closed conformations in response to the voltage difference across the membrane, the channel is activated by hyperpolarization. May interact with the cytoskeleton or with regulatory proteins.
|
Q8GXE6
|
Q8CUN1
|
ARGJ_OCEIH
|
Arginine biosynthesis bifunctional protein ArgJ beta chain
|
Oceanobacillus
|
METTTVKEISILKNGHVTSPSGFYAGGVHCGLRRKKLDLGWIYSDTPASAAGVYTQNTFQAAPLLITKHTIEHSKQIQSIIVNSANANSFTGKQGYEDALLMQKLVANQLNIEQHHVAVASTGVIGERLPMDKVRNGIRQLSHTQVDAESFEKAILTTDTSTKHVAVQVEIDGKLVTIGGAAKGSGMIHPNMATMLSFITTDANVNQDSLQQALRKVTDQSYNQITVDGDSSTNDMVLVLANGRAENNELNESHPEWSVFMDAWNIVAIELAKMIARDGEGATKLIEVIVKGASTNQQASQIAKAVISSNLVKTAIYGNDANWGRIIGAIGYSGVPVEASKLSIAIGGIQVVNNGEPIDFDEKDCKQALNQETVNIVIDLQSGMDTATAWGCDLTYDYIRINASYRT
|
Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate.
|
Q8CUN1
|
P23194
|
URIC_DROVI
|
Urate oxidase
|
Drosophila
|
MFATPLRQLSSLKRSGIAGQEQAQLYEITNKGYGKDAVKVMHINRKGPVHSIQELEVGTHLKLYSNKDYMLGNNSDVVATDSQKNTVYLLAKKHGIESPEKFALILAKHFLSTYAHVEEVHVHVEAYPWQRMTQDVSDNIGKGYCENNCNSRSNGNCQLHNHAFIFTPTAHDYCDVILTRQDPKQTVISGIKGLRVLKTTQSSFVNFVDDEFRTLADQYDRIFSTVVECSWEYSDTESVNFLHAWETVKDIVVRNFAGDPSVGIPSPSVQHTLYLSEKQVLDVLPQVSVVSMTMPNKHYFNFDTKPFQQLVPGENNEVFIPTDKPHGTIYAQLSRKSLKSHL
|
Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin.
|
P23194
|
Q14FG1
|
PSBC_POPAL
|
Protein CP-43
|
Populus
|
MKTLYSLRRFYPVETLFNGTLALAGRDQETTGFAWWAGNARLINLSGKLLGAHVAHAGLIVFWAGAMNLFEVAHFVPEKPMYEQGLILLPHLATLGWGVGPGGEVIDTFPYFVSGVLHLISSAVLGFGGIYHALLGPETLEESFPFFGYVWKDRNKMTTILGIHLILLGIGAFLLVFKALYFGGVYDTWAPGGGDVRKITNLTLSPSVIFGYLLKSPFGGEGWIVSVDDLEDIIGGHVWLGSICILGGIWHILTKPFAWARRALVWSGEAYLSYSLGALAVFGFIACCFVWFNNTAYPSEFYGPTGPEASQAQAFTFLVRDQRLGANVGSAQGPTGLGKYLMRSPTGEVIFGGETMRFWDLRAPWLEPLRGPNGLDLSRLKKDIQPWQERRSAEYMTHAPLGSLNSVGGVATEINAVNYVSPRSWLATSHFVLGFFLFVGHLWHAGRARAAAAGFEKGIDRDFEPVLSMTPLN
|
One of the components of the core complex of photosystem II (PSII). It binds chlorophyll and helps catalyze the primary light-induced photochemical processes of PSII. PSII is a light-driven water:plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation.
|
Q14FG1
|
Q1C0H5
|
RSMA_YERPA
|
S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase
|
Yersinia
|
MNNRVHQGHFARKRFGQNFLNDQFVIDSIVSAIHPVPGEAVVEIGPGLGALTEPVAARMDHMTVIELDRDLAARLASHPQLKDKLTIHQQDAMKVNFSELSEQAGQPLRVFGNLPYNISTPLMFHLFSYTDAIRDMHFMLQKEVVNRLVAGPNSKTYGRLTVMAQYYCNVIPVLEVPPTAFTPAPKVDSAVVRLIPHVQMPHPVGDVRMLSRITTQAFNQRRKTVRNSLGDLFTSEQLIELGIDPILRAENISVAQYCKLANWLSAQSTPQK
|
Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
|
Q1C0H5
|
A9GM39
|
COBD_SORC5
|
Cobalamin biosynthesis protein CobD
|
Sorangium
|
MTAAAALLVAVAFDLACGEPPAAVHPVVWMGSAIQALKRAAPAGGRAAELLFGALMALAVPCFFAALGAGVAALLAPHPVLALALSGLLLKPTFALRALRDAAYGVRDALEAGDVTGARGALRSLCSRDPSELDEPALVAASVESVAENASDSFVAPLFYFALFGLPGALFYRAVNTLDAMVGYHGRYEYLGKASARLDDALNFVPARLTALLLLAAGWLRGADARRGLAVLLRDGGLTESPNAGRPMAAMAGLLRVELEKRGHYRLGDPVEPLRRGLIDEACRIVVLATLLFAGLAAALLAAVSFGLGQELFR
|
Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.
|
A9GM39
|
P24882
|
COX2_ASCSU
|
Cytochrome c oxidase polypeptide II
|
Ascaris
|
MNNFFQDFNLLFSSSLFSSYMDWFYNFNCSLLFGVLSFVSTMFVYLLLSSFYFKSKKIEYQFGELLCSVFPTLILVMQMVPSLSLLYYYGLMNLDSSLTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLELGEPRLLEVDNRCVVPCDVNIRFCITSGDVIHSWALPSMSIKLDAMSGILSTLSYSFPVVGVFYGQCSEICGANHSFMPVALEVTLLDNFKSWCVGLLSD
|
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.
|
P24882
|
P93028
|
UBE11_ARATH
|
Protein MODIFIER OF SNC1 5
|
Arabidopsis
|
MLHKRASEANDKNDNTIIGSDLASSKKRRIDFTESSSDKSSSILASGSSRGFHGDSVVQQIDMAFGNSNRQEIDEDLHSRQLAVYGRETMRRLFASNVLISGMHGLGAEIAKNLILAGVKSVTLHDERVVELWDLSSNFVFSEDDVGKNRADASVQKLQDLNNAVVVSSLTKSLNKEDLSGFQVVVFSDISMERAIEFDDYCHSHQPPIAFVKADVRGLFGSVFCDFGPEFAVLDVDGEEPHTGIIASISNENQAFISCVDDERLEFEDGDLVVFSEVEGMTELNDGKPRKIKSTRPYSFTLDEDTTNYGTYVKGGIVTQVKQPKLLNFKPLREALKDPGDFLFSDFSKFDRPPLLHLAFQALDHFKAEAGRFPVAGSEEDAQKLISIATAINTGQGDLKVENVDQKLLRHFSFGAKAVLNPMAAMFGGIVGQEVVKACSGKFHPLFQFFYFDSVESLPSEPVDSSDFAPRNSRYDAQISVFGAKFQKKLEDAKVFTVGSGALGCEFLKNLALMGVSCGSQGKLTVTDDDIIEKSNLSRQFLFRDWNIGQAKSTVAASAAAVINPRFNIEALQNRVGAETENVFDDAFWENLTVVVNALDNVNARLYVDSRCLYFQKPLLESGTLGTKCNTQSVIPHLTENYGASRDPPEKQAPMCTVHSFPHNIDHCLTWARSEFEGLLEKTPAEVNAYLSSPVEYTNSMMSAGDAQARDTLERIVECLEKEKCETFQDCLTWARLRFEDYFVNRVKQLIYTFPEDAATSTGAPFWSAPKRFPRPLQYSSSDPSLLNFITATAILRAETFGIPIPEWTKNPKEAAEAVDRVIVPDFEPRQDAKIVTDEKATTLTTASVDDAAVIDDLIAKIDQCRHNLSPDFRMKPIQFEKDDDTNYHMDVIAGLANMRARNYSIPEVDKLKAKFIAGRIIPAIATSTAMATGLVCLELYKVLDGGHKVEAYRNTFANLALPLFSMAEPLPPKVVKHRDMAWTVWDRWVLKGNPTLREVLQWLEDKGLSAYSISCGSCLLFNSMFTRHKERMDKKVVDLARDVAKVELPPYRNHLDVVVACEDEDDNDVDIPLVSIYFR
|
Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP.
|
P93028
|
B3PI66
|
HSLV_CELJU
|
ATP-dependent protease subunit HslV
|
Cellvibrio
|
MTTILSVRRDGQVVIGGDGQVSLGNTVMKGNARKVRRLYKNQVLAGFAGGTADAFTLFERFEAKLESHNGQLTRAAVELAKDWRTDRSLRRLEALLAVADKEASLIITGNGDVIQPEDDLIAIGSGGMYAQAAARALLENTQLDARNIVEKGLKIAGDICVYTNQNHTIEVLDY
|
Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
|
B3PI66
|
P10999
|
LAML3_XENLA
|
Lamin-B3
|
Xenopus
|
MATSTPSRAREHASAAQSPGSPTRISRMQEKEDLRHLNDRLAAYIERVRSLEADKSLLKIQLEEREEVSSREVTNLRQLYETELADARKLLDQTANERARLQVELGKVREEYRQLQARNSKKENDLSLAQNQLRDLESKLNTKEAELATALSGKRGLEEQLQEQRAQIAGLESSLRDTTKQLHDEMLWRVDLENKMQTIREQLDFQKNIHTQEVKEIKKRHDTRIVEIDSGRRVEFESKLAEALQELRRDHEQQILEYKEHLEKNFSAKLENAQLAAAKNSDYASATREEIMATKLRVDTLSSQLNHYQKQNSALEAKVRDLQDMLDRAHDMHRRQMTEKDREVTEIRQTLQGQLEEYEQLLDVKLALDMEINAYRKMLEGEEQRLKLSPSPSQRSTVSRASTSQTSRLLRGKKRKLDETGRSVTKRSYKVVQQASSTGPVSVEDIDPEGNYVRLLNNTEEDFSLHGWVVKRMHMSLPEIAFKLPCRFILKSSQRVTIWAAGAGAVHSPPTDLVWKSQKTWGTGDNIKITLLDSTGEECAERTLYRVIGEEGETDEDFVEEEELERQFRSQSHQSVDPSCSIM
|
Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin.
|
P10999
|
Q750L0
|
AEP3_ASHGO
|
ATPase expression protein 3
|
Eremothecium
|
MNKIVHKVAEAFRKNGVPRTKWLNPKTIYGLANQKLLGSVEAPHAQGTGLNTVPQVEHYTKACRTKQRDMVRSYLEATGSTHFARLNTPAYNKSSALEFYAKLKALQRYTEGEEVLFQMSSVEVREIISRLVKLTQEGDQIPDEQRRFPTELFMDVAPVPNFNDDPGILEQYIGILTHSAFYYHNTSKIDPIPHILRDLLHPQNEKTASLRTTTMFNDLIYYFGKKSDYASCREYYSQMKLEKKTPNIETYRLLFLNLLKNMQIPKKQLPYKEMIFYLNDMEKFGVPADAKIWAYCYHLLVESVSKKLLLEKMIQHNAPISPDFIVSILRTLDVDCKAILEFAKEYSIPFTPKLLRLCISKLCKEYKFESAWQLLTSLCRSTDVVTTGSVNILLNAAAEKGRLDLAVLTYNSMKVQLGVTPDLRTHRLIFKAMARNGYHENFQDVYHWAVWSMKRSTSGWFVHDAWSRRCESMIKQKCGSVTPPTTENMEKVAAILHRGVWDNRGLFIRCWGEYKELRHVFRLLGSIPPAYKGKTA
|
Required for respiration.
|
Q750L0
|
Q9FJH5
|
HIP3_ARATH
|
Heavy metal-associated isoprenylated plant protein 3
|
Arabidopsis
|
MGEKKNEGDNKKKGGDNKKKNETPSITVVLKVDMHCEGCASRIVKCVRSFQGVETVKSESATGKLTVTGALDPVKLREKLEEKTKKKVDLVSPQPKKEKEKENKNKNDEDKKKSEEKKKPDNNDKKPKETPVTTAVLKLNFHCQGCIGKIQKTVTKTKGVNGLTMDKEKNLLTVKGTMDVKKLVEILSEKLKRAVEIVPPKKEKDKENGNENGEKKKGGGGDGGGKEKTGNKGGGEGVNMMEYMAAQPAYGYGYYPGGPYGYPIQAHAPQIFSDENPNACVVM
|
Heavy-metal-binding protein. Binds high amounts of zinc. May act as an upstream regulator of the salicylate-dependent pathogen response. Involved in abiotic stress responses, and seed and flower development.
|
Q9FJH5
|
A5CW05
|
IF1_VESOH
|
Translation initiation factor IF-1
|
Candidatus Vesicomyosocius
|
MSKSDYIELEGFVKEKLPNTTFMVELENGHCILAHISGKIRKHYIRILPGDKVTVEMTPYDLTKGRITFRHK
|
One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex.
|
A5CW05
|
D0Z9R0
|
TATD_EDWTE
|
DNase TatD
|
Edwardsiella
|
MLDIGVNLTNGQFSGDVPQVVARARQAGLNGMIITGTNLTESAQALHLAQAYPDFCWATAGVHPHDAHRWNENSAADLEPLLRSPAVVAVGECGLDFARNFSTPAQQEAAFEAQLALAAQIGKPVFLHCREAHARFIALLRPWLSRLPGAVLHCFTGTRDELDACLSLGLYIGITGWICDERRGMPLRALLPHIPAERLLLETDAPYLLPRDIQPKPKSRRNEPCFLPHIAEQAARWRQQDANWLKQVTENNARQLFRLA
|
3'-5' exonuclease that prefers single-stranded DNA and RNA. May play a role in the H(2)O(2)-induced DNA damage repair.
|
D0Z9R0
|
B8F4X7
|
DER_GLAP5
|
GTP-binding protein EngA
|
Glaesserella
|
MTPVVALVGRPNVGKSTLFNRLTRTRNALVADFPGLTRDRKYGHANIAGHDFIVIDTGGIDGTEEGVEEKMAEQSLLAIKEADVVLFLVDARAGLLPADVGIAQYLRQRNKTTVVVANKTDGIDADSHIAEFYQLGLGEVEPIAAAQGRGVTQLIEQVLAPLAEKLEAQAVDSDENVADDEQDEWDSDFDFDNEEDTALLDEALEEDQEETDDKNIKIAIVGRPNVGKSTLTNRILGEERVVVYDMPGTTRDSIYIPMERDGQQYTIIDTAGVRKRGKVHLAVEKFSVIKTLQAIQDANVVLLTIDARDGVSDQDLSLLGFILNAGKSLVIVVNKWDGLSQDIKDNVKSELDRRLDFIDFARVHFISALHGSGVGNLFSSIQEAYQCATKKMTTSMLTRILQLAMDDHQPPLVNGRRVKLKYAHPGGYNPPIIVIHGNQIEKLPDSYKRYLSNYFRKSLKIIGSPIRVLFQEGNNPFAGKKNKLTPSQLRKRKRLMKFIKKSKR
|
GTPase that plays an essential role in the late steps of ribosome biogenesis.
|
B8F4X7
|
Q8UA92
|
PANC_AGRFC
|
Pantoate-activating enzyme
|
Agrobacterium tumefaciens complex
|
MRLVKTVAELRDAIAAFRRAGKTIGFVPTMGFLHIGHLTLVARAKAENDATVVSIFVNPLQFGANEDLARYPRDLARDSALLQEAGVDILFAPDVTEMYPRPIQTVVDVPELGSQLEGAVRPGHFAGVTTVVTKLFNLVQPDAAYFGEKDYQQVTLVRRMVEDLAQPVRVIPVATVREADGLACSSRNVYLSPEQRAAAVIVPHALDEAERLYAEGVDDPAAIEAAIEKFIAAEPLASPEVVAVRDPDTLAPVASLQAGPVLVALFVRFGSTRLLDNRVIGREKTAEQEAAQ
|
Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
|
Q8UA92
|
Q9XS41
|
SODM_HORSE
|
Mn-SOD
|
Equus
|
MLCRAACSTSRKLVPALGSLGSRQKHSLPDLQYDYGALEPYINAQIMQLHHSKHHAAYVNNLNVTEEKYQEALAKGDVTAQIALQPALKFNGGGHINHTIFWTNLSPNGGGEPKGKLLDAIKRDFGSFDKFKEKLTAVSAGVQGSGWGWLGFNKDQGRLQIVACPNQDPLQGTTGLIPLLGIDVWEHAYYLQYKNVRPDYLKAIWNVINWENVSERYMACKK
|
Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
|
Q9XS41
|
Q32686
|
RBL_NICPH
|
Ribulose bisphosphate carboxylase large chain
|
Nicandra
|
SVGFKAGVKEYKLTYYTPEYKTKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYRIERVVGEKDQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEALFKAQAETGEIKGHYLNATAGTCEEMIKRAVFARELGVPIVMHDYLTGGFTANTTLAHYCRDNGLLLHIHRAMHAVIDRQKNHGIHFRVLAKALRMSGGDHIHSGTVVGKLEGERDITLGFVDLLRDDFVEQDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVKARNEGRDLAQEGNEVIREACKWSPELAAACEVWKEIVFNFAAVDILDNK
|
RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.
|
Q32686
|
B9E1X0
|
ARGC_CLOK1
|
N-acetyl-glutamate semialdehyde dehydrogenase
|
Clostridium
|
MVQVGVIGGTGYVGAELIRLLSNHNKIKISGISSTSYEGKSINSLYPGFYDLKELVCEKDDEVIKRSDLIFLALPSGVSEPIVEKAVAKDKICIDMGADFRFKNESSYKKWYGKNFITPKLHESSVYGLPELNREYIKKSRVIGNPGCYATSVQIGVLPLISKGLIEEKGIIADCKSGLTGAGKTLSESSHFVNCNESFSAYKVANHRHTPEIEENLNSVSKEGVKLTFIPHLIPINRGILSTIYTTPKDPIDIEKIHQKYCEFYKEEPFVRILPLGKVSKINNVRLSNYCCISIHYDSENNKLIIISCLDNMIKGAAGQAIQNMNIVLGFDEKEGLTALPAVF
|
Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
|
B9E1X0
|
Q32DS4
|
MEND_SHIDS
|
Menaquinone biosynthesis protein MenD
|
Shigella
|
MSVSAFNRRWAAVILEALTRHGVRHICIAPGSRSTPLTLAAAENSAFIHHTHFDERGLGHLALGLAKVSKQPVAVIVTSGTAVANLYPALIEAGLTGEKLILLTADRPPELIDCGVNQAIRQPGMFASHPTHSISLPRPTQDIPARWLVSTIDHALGTLHAGGVHINCPFAEPLYGEMDDTGLSWQQRLGDWWQDDKPWLREAPRLESEKQRDWFFWRQKRGVVVAGRMSAEEGKKAALWAQTLGWPLIGDVLSQTGQPLPCADLWLGNAKATSELQQAQIVVQLGSSLTGKRLQQWQASCEPVEYWIVDDIEGRLDPAHHRGRRLIANIADWLELHPAEKCQPWCVEIPRLAEQAMQAVIARRDAFGEAQLAHRVCDYLPEQGQLFVGNSLVVRLIDALSQLPAGYPVYSNRGASGIDGLLSTAAGVQRASGKPTLAIVGDLSALYDLNALALLRQVSAPLVLIVVNNNGGQIFSLLPTPKSERECFYLMPQNVHFEHAAAMFELKYHRPQNWQELETVLADAWRTPTTTVIEMVVNDTDGAQTLQQLLAQVSHL
|
Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).
|
Q32DS4
|
Q7VLT4
|
FTSB_HAEDU
|
Cell division protein FtsB
|
Haemophilus
|
MRLMIVFFGLLLFFFQYSFWLGKNGWQDYKNAKLEVQRLTAENIKLNARNELIAAEIDDLKNGVDALEERARLDREMVKSDEYFYRIVPRN
|
Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic.
|
Q7VLT4
|
B3E683
|
APT_TRIL1
|
Adenine phosphoribosyltransferase
|
Trichlorobacter
|
MEDLKLTIRDIPDFPKKGIIFKDITTLLQDAKSFTRMIDMIANRYIGQRIDKVVGVEARGFLIGAALAYRLGAGVVLVRKPGKLPSETFSKTYDLEYGTDTLEIHKDAIKPGEKILIADDLLATGGTMAAVVDMVTNMQGEIVECCFMTELTFLDGRKKLPEGKVYSLMQF
|
Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
|
B3E683
|
P05047
|
LECA_SARPE
|
Lectin subunit alpha
|
Boettcherisca
|
MSLTMKNVEGFVIFLVIFTSTAAVPQLQKALDGREYLIETELKYNWHQAWHECARHDQQLVTIESADKNNAIIDLVKRVVGKSHNLWLGGNDEYSSSRDYGRPFFWSPTGQAFSFAYWSENNPDNYKHQEHCVHIWDTKPLYQWNDNDCNVKMGYICEPNHFRETYDQALKQKCEAIKITNSKISTEFDQLHAKQSLEFDSITQNVAKVNEDWKIEIQKLQNATQIAIQQIMENHEKKIRDLSDNLLKQLQDSNEQLKQSTDHMNASFGEKLKGQQAENNEIC
|
Role in the defense system of the organism against microorganisms. This lectin binds galactose.
|
P05047
|
Q3SS86
|
PPK1_NITWN
|
Polyphosphoric acid kinase
|
Nitrobacter
|
MDSIQAIAPEEKKPELELDSAIRASPERFINRELSWLHFNRRVLEESVNPGHPALERVRFLSISANNLDEFFMVRVAGIKAQVREGITERSPDGLTPSEQLVLINETVSDLASDQQAIWRDLRNMLAGVGIVLIDGKDVTKAERSWIADHFLHNIFPLLTPLAIDPAHPFPFIPSLGFTIALQLARTSDGKPMNALIRMPGKIDRFLRIPAASKDDPVRLITIEGATSLFINRLFPGYTVKGQGAFRIIRDSELEIEEEAEDLVRLFETALKRRRRGSVIRLEIEAAMPAELRAFVQRALSAADDEVLLVDGVLAMNELSQLTRLDRPDLEFVPYVPRHPERVRDHGGDVFAAIRQKDLIVHHPYESFDVVVQFLQQAARDPDVVAIKQTLYRTSNNSPIVRALAEAAEAGKSVTALIELKARFDEEANIRWARDLERAGVQVVYGFLELKTHAKLSLVVRREGGSLATYVHTGTGNYHPVTARIYTDLSYFTSDPIIGRDAARVFNYITGYAEPSDIERMAVSPLTLRNRILDHIRGETTFARNGKPAAVWMKMNALVDPDIIDALYEASQAGVSVELIVRGICCLRPGVPGLSENIRVKSVIGRFLEHGRIYCFGMGQTMPGPKAAVYISSADMMPRNLDRRVEVLCPLQNATVHQQVLEQIMVANLKDTEQSWRLLPDGSSTRMKAAKGEEPFNLHNYFMTNPSLSGRGKSLKESSPRRLTRRSERQPPA
|
Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP).
|
Q3SS86
|
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