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
|
|---|---|---|---|---|---|---|
Q4L3F2
|
ISPE_STAHJ
|
4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase
|
Staphylococcus
|
MIYETAPAKINLTLDTLFKRDDGYHEIAMIMTTVDLNDRLSFQKRKDKKIVVDIEHNYVPNDHKNLAYRAAQLMMETYDLNEGVTITIDKDIPVSAGLAGGSADAAATMRGINRLFNLDKSLHELSDLGIQIGTDIPFCIYNRTAVCKGRGEKIRFLKKPPSAWVVLAKPNLGISSADVFKALDLDDAHHVDTEMCEKAIVEGDYKQLCESLSNRLEPVSMSMHPEIKKIKNNMLQCGADGALMSGSGPTVYGLAQKESQAKKIYNAVNGCCNEVYLVRLLG
|
Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
|
Q4L3F2
|
Q0I476
|
PROQ_HAES1
|
RNA chaperone ProQ
|
Histophilus
|
MTEIQKLTNNKEIIAYLAEKFPLCFSLEGEAKPLKIGLFQDLAEALANDEKVSKTQLRQALRQYTSNWRYLHGCRAGAVRVDLNGEPAGILEQEHVEHAAAKLAEAKAKVAERRAVEKANNPKANKKRSVYHSGNKSENKKSAGKKFSKPRQVEQIFVNVDLANLQKGDVVRVKAGDKTTKAEILEVVKEGARVELENGLILTVSADRLFA
|
RNA chaperone with significant RNA binding, RNA strand exchange and RNA duplexing activities.
|
Q0I476
|
B8J832
|
RL20_ANAD2
|
50S ribosomal protein L20
|
Anaeromyxobacter
|
MRVKKGFKARRRRNRVLKLAKGFRGRRKNCYRRANQAVERALNYSTRDRRLKRREFRALWIVRINAAARQNGTTYSKLVAALRKAGIEIDRKILADLALALPGDFAAIVKTAQA
|
Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit.
|
B8J832
|
B7LT80
|
TRHO_ESCF3
|
tRNA hydroxylation protein O
|
Escherichia
|
MPVLHNRISNDALKAKMLAENEPRTTISFYKYFTIADPQTTRDALYKLFTALNVFGRVYLAHEGINAQISVPESHVDKFRQQLYSFDPALNNLRLNIALDDDGKSFWVLRMKVRERIVADGITDPDFDASNVGNYLQAAQVNAMLDDPDALFIDMRNHYEYEVGHFENAMEIPADTFREQLPKAVEMMQEHKDKKIVMYCTGGIRCEKASAWMKHNGFEKVWHIEGGIIEYARKAREQGLPVRFIGKNFVFDERMGERISEDVIAHCHQCGTPCDSHTNCKNDGCHLLFIQCPVCAEKFNGCCSELCCTESALPPEEQRRLRAGRENGNKIFNKSRGRLNTQQGIPELKI
|
Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs.
|
B7LT80
|
B3MSP2
|
EI3G2_DROAN
|
Eukaryotic translation initiation factor 3 subunit 4-2
|
Sophophora
|
MKPFKTSWADEVEADYVDGLPPCSEYIEGDYKYVTEYKFNDDGKKVKVVRTFKIEKQVVSKAVARRRGWVKFGDSRLDKPGPNSQTTMASEEIFMLFMGSKEFEQTHETQMDAGKNIAKCRICNGEHWSVNCPYKGTSMDSKTLMESKANAAAAAALNDPSKPGKYVPPFMKDGAGGAGGKGRERDDSSAVRISNLSESMTETDLEELVKKIGPHTKMYLAREKNTGLCKGFAYVHFKFRQDAAAAIEILNGHGYDHLILCVEWSKPQP
|
RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. This subunit can bind 18S rRNA.
|
B3MSP2
|
B2KBN0
|
DEOC_ELUMP
|
Phosphodeoxyriboaldolase
|
Elusimicrobium
|
MNKTAKLIDHTLLKPGATEFEIKTLCAEALKYGFASVCVNPFWVKLAASELEGSDVKVCTVIGFPLGANTTEAKVFEAKNALENGAQELDMVINIGAVKSGLYELAYHDIKLIRDLGKNFVLKVILETTLLTDAEKIKVCELSACAEADFVKTSTGFAGGGATIEDVKLMKANISSGMQVKASGGVRDLETLTKMVEAGASRIGTSSSIKIIESL
|
Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
|
B2KBN0
|
P59493
|
DEF_BUCBP
|
Polypeptide deformylase
|
Buchnera
|
MSVLKILKYPDDRLRIIAKPISKIDTKIHNIIINMFDTMYYENGIGLAATQVNIPLQIIVIDKIEELNHPLVLINPKITKRSGLTSIQEGCLSIPNYQAEISRSKKITVTALNYFGKRIKLKTSSTLSICIQHEIDHLIGKLLIDYLSNLTNLKLLKKNK
|
Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
|
P59493
|
Q6C922
|
YTH1_YARLI
| null |
Yarrowia
|
MKFETPSRFKFTPYLEREYQFGLDPNRPLCRGFLQFDGCPRGNSCPDKHLAPTFLNKIVCKHWLRGLCKKGLNCEFLHEYNLQKMPECQFYVKNGFCTQSPDCQYLHIDPASKIPVCFNYEKGFCKMGPECSRKHIRRMPCELYMTGFCPKGRVCEFAHPKFVGIYDYMIIKPNPKDKAKDETKQETKEEALQ
|
Component of the cleavage factor I (CF I) involved in pre-mRNA 3'-end processing.
|
Q6C922
|
Q94ID2
|
IPT5_ARATH
|
Cytokinin synthase 5
|
Arabidopsis
|
MKPCMTALRQVIQPLSLNFQGNMVDVPFFRRKDKVVFVMGATGTGKSRLAIDLATRFPAEIVNSDKIQVYKGLDIVTNKVTPEESLGVPHHLLGTVHDTYEDFTAEDFQREAIRAVESIVQRDRVPIIAGGSNSYIEALVNDCVDFRLRYNCCFLWVDVSRPVLHSFVSERVDKMVDMGLVDEVRRIFDPSSSDYSAGIRRAIGVPELDEFLRSEMRNYPAETTERLLETAIEKIKENTCLLACRQLQKIQRLYKQWKWNMHRVDATEVFLRRGEEADEAWDNSVAHPSALAVEKFLSYSDDHHLEGANILLPEISAVPPLPAAVAAISR
|
Involved in cytokinin biosynthesis. Catalyzes the transfer of an isopentenyl group from dimethylallyl diphosphate (DMAPP) to ATP and ADP.
|
Q94ID2
|
Q805B2
|
FGF8B_DANRE
|
Fibroblast growth factor 17a
|
Danio
|
MRLKSSRLGYLFLQFMTLCFYTQMTMQSISMPNFKHHVTEQSRLSDRMSRRLTRTYQLYSRTSGKHVQVLGNKRVNANAEDGDIHAKLVVETDTFGSRVRIRGAKTGYYICMNKKGKLIGRRKGRGKDCIFTEIVLENNYTALQNAKYKGWYMAFTRKGRPRKAMQTRQHQREAHFMKRLPRGHLLTEQKPFDLIPYPLNKRTKHHQRASVN
|
May act as signaling molecule during development of the midbrain-hindbrain boundary (MHB) organizer, and be involved in patterning of the nervous system.
|
Q805B2
|
A7ZHZ2
|
DPO4_ECO24
|
DNA polymerase IV
|
Escherichia
|
MRKIIHVDMDCFFAAVEMRDNPALRDIPIAIGGSRERRGVISTANYPARKFGVRSAMPTGMALKLCPHLTLLPGRFDAYKEASNHIREIFSRYTSRIEPLSLDEAYLDVTDSVHCHGSATLIAQEIRQTIFSELQLTASAGVAPVKFLAKIASDMNKPNGQFVITPAEVPAFLQTLPLAKIPGVGKVSAAKLEAMGLRTCGDVQKCDLVMLLKRFGKFGRILWERSQGIDERDVNSERLRKSVGVERTMAEDIHHWSECEAIIERLYPELERRLAKVKPDLLIARQGVKLKFDDFQQTTQEHVWPRLNKADLIATARKTWDERRGGRGVRLVGLHVTLLDPQMERQLVLGL
|
Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.
|
A7ZHZ2
|
B5FSN3
|
RUVC_SALDC
|
Holliday junction resolvase RuvC
|
Salmonella
|
MSIILGIDPGSRITGYGVIRQVGRQLTYLGSGCIRTKVDDLPSRLKLIYAGVTEIITQFQPDYFAIEQVFMAKNADSALKLGQARGVAIVAAVNQELPVFEYAARQVKQTVVGIGSAEKSQVQHMVRTLLKLPANPQADAADALAIAITHCHVSQNAMQMSESRLNLARGRMR
|
Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group.
|
B5FSN3
|
Q8HVU9
|
NDHI_CHAST
|
NADH-plastoquinone oxidoreductase subunit I
|
Chaenactis
|
MFPMVTEFMNYGQQTVRATRYIGQGFMITLSHANRLPVTVQYPYEKLITSERFRGRIHFEFDKCIACEVCVRVCPIDLPVVDWKLETDIRKKRLLNYSIDFGICIFCGNCVEYCPTNCLSMTEEYELSTYDRHELNYNQIALGRLPMSIIDDYTIRTILNLPEIKT
|
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.
|
Q8HVU9
|
Q5KWC8
|
NRDR_GEOKA
|
Transcriptional repressor NrdR
|
Geobacillus thermoleovorans group
|
MRCPSCHHSGTRVLESRPVEEGRSIRRRRECEQCHYRFTTFERIEEPPLIVVKKEGTREEFSREKILRGLIKACEKRPVALEELEKVTQEIERELRNQGVSEVKSETIGEMVMERLSHIDEVAYVRFASVYRQFKDINVFIEELKELIKKGQR
|
Negatively regulates transcription of bacterial ribonucleotide reductase nrd genes and operons by binding to NrdR-boxes.
|
Q5KWC8
|
P53456
|
ACT2_DIBDE
|
Actin-2
|
Dibothriocephalus
|
MGDEEVQALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTRIMFETFNTPAMYVGIQAVLSLYASGRTTGIVLDSGDGVTHSVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFRCPESLFQPSFLGMESAGIHESTFNAIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITSLAPSTMKIKIVAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPGIVHRKCF
|
Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
|
P53456
|
A6LSQ9
|
RS15_CLOB8
|
30S ribosomal protein S15
|
Clostridium
|
MDKARKLELIKKFGRSEGDTGSPEVQVALLTERIQSLTEHLKVHKKDHHSRRGLLMMVGQRRGLLNYLSDQDIERYRTLIKELGLRR
|
Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome.
|
A6LSQ9
|
Q5LNP1
|
ATPB_RUEPO
|
F-ATPase subunit beta
|
Ruegeria
|
MANAKGKVTQIIGAVVDVQFDDALPEILNALETENNGKRLVLEVAQHLGENTVRTIAMDATEGLVRGAVVTDTGGPISVPVGAATLGRILNVIGEPVDEKGPVNATETRAIHQPAPSFDEQSTSSDILVTGIKVIDLLAPYSKGGKIGLFGGAGVGKTVLIMELINNIAKVHSGYSVFAGVGERTREGNDLYHEMIESNVIKLENLEESQVALVYGQMNEPPGARARVALTGLTLAEQFRDQSGTDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGAMQERITSTKAGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRAISELGIYPAVDPLDSSSRILDPQVVGEEHYQVARDVQGILQRYKSLQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFDVAKVFTGSDGVQVPLEDTISSFKAVVAGEYDHLPEGAFYMVGGIDEVIAKAERMAAEAA
|
Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
|
Q5LNP1
|
Q7ZZN8
|
CRVP2_NAJAT
|
Protein G2b
|
Naja
|
MIAFIVLLSLAAVLQQSSGTVDFASESSNKRENQKQIVDKHNALRRSVRPTARNMLQMEWNSNAAQNAKRWADRCSFAHSPPHLRTVGKIGCGENLFMSSQPYAWSRVIQSWYDENKKFVYGVGANPPGSVIGHYTQIVWYNSHLLGCGAAKCSSSKYLYVCQYCPTGNIIGSIATPYKSGPPCGDCPSACVNGLCTNPCKHHNVFSNCQSLAKQNACQTEWMKSKCAASCFCRTEII
|
Inhibits carbachol-induced muscle contraction and weakly blocks muscle contraction evoked by potassium.
|
Q7ZZN8
|
Q9RWN1
|
PFKA_DEIRA
|
Phosphohexokinase
|
Deinococcus
|
MAYPNPAGIKRVAVLTSGGDAPGMNAAIRAVVRTGAQQGIEVVGVRRGFSGLHRGEVQLLGPRDVANTIQRGGTILLTARSHTWRSPEGRAKGAAVLREWGVDGLVVIGGDGSFHGGYFLQEEHGIPVIGVPGTIDNDLYGTDHTIGYFTAVETALEAVDKLRDTGASHERIFVIEVMGRHAGHIALDVAVAGGAEEVFIPEDKKPIGDVVNIVKDSIAKGKRGSIIIVAEGYDGGAEAVAQAIHAGTGLETRVSILGHIQRGGTPVSSDRILASRLGEAAVYALMDGKKGVMVGRIGGGIAYTPLHETWEKRKDVSRDLYRCAKMLSI
|
Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
|
Q9RWN1
|
A4IJ95
|
PDXT_GEOTN
|
Pyridoxal 5'-phosphate synthase glutaminase subunit
|
Geobacillus
|
MKIGVLGLQGAVQEHVRAIEACGAEAVVVKKTEQLTGLDGLVLPGGESTTMRRLIDRYGLMEPLKQFAADGKPMFGTCAGLILLAKRIVGYDEPHLGLMDITVERNSFGRQRESFEAELSIKGVGDGFVGVFIRAPHIVEVGDEVEVLATYNDRIVAARQGQFLGCSFHPELTDDHRLMRYFLNMVKEAKTVSSI
|
Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
|
A4IJ95
|
Q92EU3
|
DHAL2_LISIN
|
PEP-dependent dihydroxyacetone kinase 2, ADP-binding subunit DhaL
|
Listeria
|
MSELVMDSAFFGHVLQDMGALIEKERDYLTGLDSDIGDGDHGINLSIGFREVNKQLDELLTVSPDIATLLKKSGMILLGKVGGASGPLYGSFFMKCGADVPGKTEVNFDELCGMIINGAAAVQHRGKAELGDKTMMDAFLPGVEVLQNRDTNADPIETFSAFVDAMHAGAQSTIPLIAKKGRALRLGERAIGHLDPGSESSWMLMNVILENLKKAV
|
ADP-binding subunit of the dihydroxyacetone kinase, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone. DhaL-ADP is converted to DhaL-ATP via a phosphoryl group transfer from DhaM and transmits it to dihydroxyacetone binds to DhaK.
|
Q92EU3
|
Q96V54
|
CREB_EMENI
|
Ubiquitin-specific-processing protease creB
|
Aspergillus subgen. Nidulantes
|
MGSFLKSFRKDVGSAAPSVGAPPAKKEPQPLPMTPLEKMLTELGPIRGDGSDKFYGMENFGNTCYCNSILQCLYYSVPFREAVLNYPKRTPIEDLEAALAKALRYQDPNARLEAEALAEKQKAANSPRPGQPPNPQQKPEDKDSPEYKKKLALQTLPLLETTDNSVSYGIPESLFSSLKDMFESIVGSQSRIGIIRPQHFLEVLRRENEMFRTAMHQDAHEFLNLLLNEVVVDVEKAAAKLLESPQPASDVSDSVIPSSSSGSRTPNTTRWVHELFEGLLTSETQCLTCEKASQRDEVFLDLSVDLEQHSSVTSCLRKFSAEEMLCERNKFHCDNCGGLQEAEKRMKIKRLPRILALHLKRFKYTEDLQRLQKLFHRVVYPYHLRLFNTTDDAEDPDRLYELYAVVVHIGGGPYHGHYVSIIKTQDRGWLLFDDEMVEPVDKNYVRNFFGDKPGLACAYVLFYQETTMEAVMKEQEQENTEPPVEVNASTLKQNGFSSSATLAHAHSASQVPTYEDHDRFTGLKRAPTAPQLSTHPEHTTTDSESLPSPAPDPAPLTSLPPIPPIPETPPAPLTSRKSDLQSKKERVKEEKERKAAEKEKEKQRRKEIETRLKDRQRREDDDLKAALEASKVSKEDEDRRNHAENGTSKKNAGGLGRFRSLSQRLSTKESRTSLSRIPPLPNGNHTLSKVPDESEQTHPKSPTPPAPLSRPASQPLNDDLLGSPRADTLAVPTEQEHIKNSKHDRSSHGKWRSFSLRKKSFNILSS
|
Ubiquitin thioesterase component of the regulatory network controlling carbon source utilization through ubiquitination and deubiquitination involving creA, creB, creC, creD and acrB. Deubiquitinates the creA catabolic repressor and the quinate permease qutD. Also plays a role in response to carbon starvation and the control of extracellular proteases activity.
|
Q96V54
|
Q3SRY6
|
RL9_NITWN
|
50S ribosomal protein L9
|
Nitrobacter
|
MEIILLERVAKLGQMGEVVKVKDGFARNFLLRRGKALRATAENRAKYDGMKAELEANNIKAKGEAATVAEKINGRDIVVIRQASETGQLFGSVTVRDIVAALAADGIIVSRPQVWLDAPIKTIGQQKLTVAVHPEVEAEITVTVARSVDEAERIQRGEDISTRREDRDAAAEAIAAAGEFFDPDAQHDDEPAAEDDQNAEEK
|
Binds to the 23S rRNA.
|
Q3SRY6
|
A0KPE4
|
DEOC_AERHH
|
Phosphodeoxyriboaldolase
|
Aeromonas
|
MTDLKLAAQRALNLMDLTTLNDDDTDQKVIDLCRKAKSPAGLTAAVCIYPRFIPIARKTLREIGAADVRIATVTNFPHGNDDIEIAVAETRAAVAYGADEVDVVFPYRAFMAGNEQVGFDLVKACKEACGSQALLKVIIETGELKEEALIRRASEISIDAGADFIKTSTGKVPVNATPEAARIMMEVIKAKNPKVGFKPAGGVKDAAVAGQYLAMAEEILGKDWVSARTFRFGASSLLASLLATLGHGDKPANTSGY
|
Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
|
A0KPE4
|
A6TFL4
|
HLDD_KLEP7
|
ADP-L-glycero-beta-D-manno-heptose-6-epimerase
|
Klebsiella
|
MIIVTGGAGFIGSNIVKALNDKGITDILVVDNLKDGTKFVNLVDLNIADYMDKEDFLIQIMAGEEFGEIEAIFHEGACSSTTEWDGKYMMDNNYQYSKELLHYCLEREIPFLYASSAATYGGRTSDFIESREYEQPLNVYGYSKFLFDEYVRQILPEANSQIVGFRYFNVYGPREGHKGSMASVAFHLNTQLNNGESPKLFEGSDGFKRDFVYVGDVADVNLWFWENGVSGIFNLGTGRAESFQAVADATLAYHKKGSIEYIPFPDKLKGRYQAFTQADLTNLRKAGYDKPFKTVAEGVTEYMAWLNRDA
|
Catalyzes the interconversion between ADP-D-glycero-beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose.
|
A6TFL4
|
Q7VD77
|
PURA_PROMA
|
IMP--aspartate ligase
|
Prochlorococcus
|
MANVVVIGAQWGDEGKGKITDLLSRSADVVVRYQGGVNAGHTIVVDEKVLKLHLIPSGILYPETICLIGSGTVVDPKVMLKEIKMLKDNDIDISGLQLASTAHVTMPYHCVIDAAMEERRGLKKIGTTGRGIGPTYADKSQRNGIRVIDLLDERKLREALEIPLAEKNELLEKIYGKEAIDKEKIIEEYLEFGRLIKPHVVDCTRIIHKASRNKKNILFEGAQGTLLDLDHGTYPFVTSSNPVSGGACIGAGVGPTLIDRVIGVAKAYTTRVGEGPFPTELKGKINDQLCDRGGEYGTTTGRRRRCGWFDGVIGKYAVEVNGLDCLAITKLDVLDELEEIKVCTSYELNGEKIDYFPSSAEDFGKCTPIFKTLPGWKSSTANCRHLEDLPPPAMAYLRFLAELMEVPIAIVSLGASRDQTIVVEDPIHGPKRALLSS
|
Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
|
Q7VD77
|
Q7NBP5
|
SYP_MYCGA
|
Prolyl-tRNA synthetase
|
Mycoplasma
|
MAFKKNLASSKDDNISDWYTEVISKGNLIHYSNIKGFMSFLPNGWKIWQLIKKELTKEFDQRDILELCLPSLISQNDFLLEKKHLEGFAPELFIVTKTSNETEKYILRPTSEIAFCNLWRETLRNYRQLPIKHNQWTSVFRVEKNTRPFLRNSEFFWHEIHSCFETEEQSNDFAVDIWKLYQRFIKDILCIPLVAGEKTEAEKFAGAKTTYTVETIMPDGQALQSATSHNLSQNFSKAFDIRYQTKNNDYQNVFSMSAGVSTRIIGAIIMTHGDDDGLVFPTKVAPYHISLNCIFDDTNQELNAKLKELANKYSQKYRVHLNVNKDSTGEIIKNSQLRGDCCVLLMGPNDLKKNEIVFIDRITKQKQFINLDHLDQKLEELFSTFDQKLYQKAKAVFETKVDFAQTFEEFEQKIASGKFVRVFYCNEDLYEKQIKEKTGASSRCIIKYLDEQTQERCFISNKKAKVEIYFARSY
|
Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro).
|
Q7NBP5
|
B2HCX3
|
RS4_MYCMM
|
30S ribosomal protein S4
|
Mycobacterium
|
MARYTGPVTRKSRRLGTDLVGGDQSFEKRPYPPGQHGRARIKDSEYRQQLQEKQKARFTYGVMEKQFRRYYEEAVRHSGKTGEELLKILESRLDNVVYRAGLARTRRMARQLVSHGHFSVNGVHVNVPSYRVSQYDIIDVRDNSLNTVPFQIARETAGDRPIPSWLQVVGERQRILIHQLPERAQIEVPLTEQLIVEYYSK
|
With S5 and S12 plays an important role in translational accuracy.
|
B2HCX3
|
Q6D2L6
|
FADI_PECAS
|
Fatty acid oxidation complex subunit beta
|
Pectobacterium
|
MSEVLPLITRRGDRIAFVSGLRTPFARQATAYHGVPAIELGKLVTSELLVRTGIDPELIELLVFGQVVQMPEAPNIAREIVLGTGMSVHTDAYSVSRACATSFQAVANVAESIMAGTVEVGIAGGADSSSVLPIGVSKALARTLVDMNKARTLGQKLRLLSGLRPKDLLPVAPAVAEYSTGLRMGDTAEQMAKTYGITREEQDELAHRSHKLAAQAWESGVLRDEVMTAYVPPYEKALSEDNNVRHDSAIEQYSRLRPAFDRRHGTVTAANSTPLTDGAAAVLMMSESKAKSLGLTPLGYLRSYAFSAIGVQRDMLLGPAYASPLALARAGVALADLTLIDMHEAFAAQTLANLKLFASDEFARNQLGRNAALGEVDRAKFNVLGGSIAYGHPFAATGARMITQTLNELRRRGGGLGLTTACAAGGLGAAMVLEVTP
|
Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed.
|
Q6D2L6
|
Q0IDJ4
|
NU3C_SYNS3
|
NDH-1 subunit 3
|
unclassified Synechococcus
|
MVYECQTGVQIEAALMFVLPGYDAFLGFLLIAAAVPVLALVTNKLLAPRSQTGERELTYESGMEPIGGAWIQFNIRYYMFALVFVIFDVETVFLYPWAVAFHRLGLLAFIEALVFITILLVALAYAWRKGALEWS
|
NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
|
Q0IDJ4
|
P12702
|
COX3_PARLI
|
Cytochrome c oxidase polypeptide III
|
Paracentrotus
|
MMAHQHPYYLVEQSPWPLTGAISGLMMNLGLVLWFHTGNIILLFTGLLLLILTLVNWWRDIVREATFQGSHTAIVENGLRYPMILFITSEVCFFFAFFWAFFHSSLAPAVEIGVTWPPSGITPLNPFLVPLLNTAVLLSSGVTITWSHHSILAGNRNEAIQALFLTVVLGIYFTILQAWEYIDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLLVCLIRLSGHHFSTHHHFGFEAAAWYWHFVDVVWLFLYVCIYWWGS
|
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.
|
P12702
|
Q6BHL8
|
IPK1_DEBHA
|
Ins(1,3,4,5,6)P5 2-kinase
|
Debaryomyces
|
MEIYKITTPGEWTYFAKGNANILFKYTGSNDYLRHKLLRVRLLKEDEQYISTCELYDFIELKCKPLFPHQIIDIQLVVLTTDFVNQLNNEGNKLMVKERYGLLLPNILDGDYCKQFLSRNCQLYIGTDTTVQEAGVNRNTVPEKLQGQEQKKLQKQEQFNNDIDSVIFEIKPKWLYDNISSNYCRTCSLNQLRGFQRHFCPLDLLYEETIDQGLDDILSLIPQDLLIEISETNKIPVKQLFRIFLNNPNNVFQKLKEYQRINNKNDLIKNITSIYDVSQNLSLVMTLRDVGLFIKFEKYNKYNNIHNSHNNINNLINIEGYGKFLLTCNIYDLDLKSKLKYKHWLDTEEKLQSIYNSSNPDWRHCVKVHDNTNNLGT
|
Has kinase activity and phosphorylates inositol-1,3,4,5,6-pentakisphosphate (Ins(1,3,4,5,6)P5) to produce 1,2,3,4,5,6-hexakisphosphate (InsP6), also known as phytate.
|
Q6BHL8
|
B7JY20
|
ARGC_RIPO1
|
N-acetyl-glutamate semialdehyde dehydrogenase
|
Rippkaea orientalis
|
MGESERIPVGIIGASGYGGVQLVRLLLEHPQVEIAYLGGKGSAGKPYWDLYPHLSHLVNLTVEPIDLEVVASRCQVVFLGLPNGLACDMAPQLIAKGCKVLDLSADYRFRDLQTYTAWYNKDRSDTETAAKAVYGLPELYRTEIQSASLIGCPGCYPTASLMALSPLLKQGLILPETAIIDAKSGTSGGGRQEKIHLLLAEAEGSLGAYGVAKHRHTPEIEQVCSDLAGHEVKVQFTPHLIPMVRGILSTVYASLRDPGLVRDDILTIYSAFYRSSPFVKILPHGIYPQTKWAWGTNLCYIGIETDPRTDRVIVLSAIDNLMKGQAGQAVQCLNLMMGWEETLGLPQLSFYP
|
Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
|
B7JY20
|
Q2K284
|
METN_RHIEC
|
Methionine import ATP-binding protein MetN
|
Rhizobium
|
MNSVVTRAAIEPRPQAAAEEVVRLIDVKRRFGATPALDGISLNVNRGEILGIIGRSGAGKSTLIRCLNGLERADSGEIRIEGRDITGLQEQELQPLRGRIGMIFQHFNLLSAKTVEDNVALPLKIEGIAKAERLQRAHELLEVVGLADKAQAYPASLSGGQKQRVGIARALAARPALLLSDEATSALDPETTRSILALLRDINRKLGLTILLITHEMEVVRGIADRVAVIDAGRIVEEGQVWSVFANPQTDITRSLLGGIRPQLPDHILSRLSATTGSEVILSVDLAGPEAQGALFAELSAALPHSFRLVHGGIDHIQNQPVARFFIAVPAHEPALAGKVEQFLTARSARVEVLGYDTGHA
|
Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system.
|
Q2K284
|
Q1MFZ8
|
RECA_RHIL3
|
Recombinase A
|
Rhizobium
|
MSQNSLRLVEDKSVDKSKALEAALSQIERSFGKGSIMKLGSNENVVEIETISTGSLGLDIALGVGGLPRGRIIEIYGPESSGKTTLALQTIAEAQKKGGICAFVDAEHALDPVYARKLGVDLQNLLISQPDTGEQALEITDTLVRSGAVDVLVVDSVAALTPRAEIEGEMGDSLPGLQARLMSQALRKLTASISKSNTMVIFINQIRMKIGVMFGSPETTTGGNALKFYASVRLDIRRIGAVKEREEVIGNQTRVKVVKNKMAPPFKQVEFDIMYGEGVSKTGELVDLGVKAGIVEKSGAWFSYNSQRLGQGRENAKTFLRDNPDLAREIELSLRQNAGLIADRFLQNGGPDPDDGDGDATAEM
|
Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage.
|
Q1MFZ8
|
B1P1D3
|
JZT18_CHIGU
|
Jingzhaotoxin-18
|
Chilobrachys
|
MKTTILVVILGLTLLFALSAATELKDEERDCKGFQVKCKKDSECCSSYVCGRQWKWCVYPSPFGR
|
Probable ion channel inhibitor.
|
B1P1D3
|
Q330E5
|
NU2M_MORBE
|
NADH dehydrogenase subunit 2
|
Mormopterus
|
MNPLIMSIILATIILGTTIVMTGSHWLMIWIGFEMNMLAIIPMLMKQHNPRSTEAATKYFFTQATASMLLMLAGIINLMYSGQWTGVKLVNPTASIIMTLALAMKLGLAPFHFWVPEVTQGIPLSSGLILLTWQKLASMTGLYMISPGINLNMLMTMSMLSIAIGGWGGLNQTQLRKIMAYSSIAHMGWMTAILIYNPTMTLLNLVIYILMTTTMFMLFMINSSTTTLSLSHTWNKMPLITTTTLVTLLSMGGLPPLMGFLPKWMIIQEMTKNNNIVLPTIMAITALLNLFFYMRLTYATSLTMFPTTNNMKIKWQFENPKYLSLLTPMIMMSTLTLPLAPMMMILN
|
Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I.
|
Q330E5
|
Q18EY6
|
RS10_HALWD
|
30S ribosomal protein S10
|
Haloquadratum
|
MQQARVRLAGTSPDDLDDICDDVRDIADTTGVNLSGPIPLPTKTLEIPTRKSPDGEGTATWEHWEMRVHKRLIDIDADERALRQLMRIQVPNDVSIEIVLED
|
Involved in the binding of tRNA to the ribosomes.
|
Q18EY6
|
Q34952
|
CYB_LORTA
|
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
|
Loris
|
MTNIRKTHPLTKIINHSFIDLPTPSNISSWWNFGSLLGLCLVIQIMTGLFLAMHYTPDTTTAFSSVTHICRDVNYGWMIRYLHANGASMFFMCLFIHIGRGIYYGSFTFLETWNIGIMLLFTVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTNLVEWIWGGFSVDKATLTRFFAFHFILPFIITALTAIHLLFLHESGSNNPSGMTSDSDKIPFHPYYTLKDILGVIALLITLSTLVLFSPDLLGDPDNYTPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALISSILILALMPFLNMAKQRSMMFRPLSQCLFWTLVANLMVLTWIGGQPVENPFIIIGQLASIMYFSTILIFMPLTNLLENKLLKW
|
Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
|
Q34952
|
A4TDE5
|
RF2_MYCGI
|
Peptide chain release factor 2
|
Mycolicibacterium
|
MDPDRQSDIAALDTTLTTVERVVNVDGLRGRIQQLESDASDPKLWDDQARAQKVTSDLSHAQNELRRVEELRSRLDDLPVLYELAAEEEGAGSSEAFAEADAELAKLREDIAGMEVRTLLSGEYDEREALVNIRSGAGGVDAADWAEMLMRMYIRWAEQHDYPVEVFDTSYAEEAGIKSATFAVHAPYAYGNLSVEQGTHRLVRISPFDNQSRRQTSFADVEVLPVVETTDHIDIPEGDVRVDVYRSSGPGGQSVNTTDSAVRLTHIPTGIVVTCQNEKSQLQNKVSAMRVLQAKLLERKRLEERAEMDALKGDGGSSWGNQMRSYVLHPYQMVKDLRTEYEVGNPAAVLDGDIDGFLEAGIRWRNQKVDDE
|
Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA.
|
A4TDE5
|
P52643
|
LDHD_ECOLI
|
Fermentative lactate dehydrogenase
|
Escherichia
|
MKLAVYSTKQYDKKYLQQVNESFGFELEFFDFLLTEKTAKTANGCEAVCIFVNDDGSRPVLEELKKHGVKYIALRCAGFNNVDLDAAKELGLKVVRVPAYDPEAVAEHAIGMMMTLNRRIHRAYQRTRDANFSLEGLTGFTMYGKTAGVIGTGKIGVAMLRILKGFGMRLLAFDPYPSAAALELGVEYVDLPTLFSESDVISLHCPLTPENYHLLNEAAFEQMKNGVMIVNTSRGALIDSQAAIEALKNQKIGSLGMDVYENERDLFFEDKSNDVIQDDVFRRLSACHNVLFTGHQAFLTAEALTSISQTTLQNLSNLEKGETCPNELV
|
Fermentative lactate dehydrogenase.
|
P52643
|
Q2KE55
|
HSLV_RHIEC
|
ATP-dependent protease subunit HslV
|
Rhizobium
|
MTTIITVRKGGKVVMAGDGQVSLGQTVMKGNARKVRRIGKGDVIAGFAGATADAFTLLERLEKKLEQYPGQLMRAAVELAKDWRTDKYLRNLEAMMLVADKSITLAITGNGDVLEPEHGTTAIGSGGNFAFAAARALMDTDKPAEEIARRALDIAADICVYTNHNIVVELLDVES
|
Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
|
Q2KE55
|
Q9CPA2
|
RBSR_PASMU
|
Ribose operon repressor
|
Pasteurella
|
MATMKDIARIAKVSTSTVSHVINNSRFVSDEIRDKVMHVVKELNYTPSALARSLKVKETKTIGLLVTATNNPFFTEVVSGVEQYCHQHHYNLILSNTEGDTERLRHNLQTLIQKQVDGLLLMCSDARIQIGKDLNVNLPFVVMDWWPTEEKADKIYENSEYGGYLATKQLIEKGHQHIAIITGNLKKSLAQNRLDGYKKALKEANIPLREDCIIESHFDFEGGKRGMEKVLALQPRPTAVFACSDSIAFGAYQTVWHQGLHIPQDISIIGYDNITLAEYMSPPLTTINQPKAELGKLAVETLLQRIKNPTAKHRTLLLEPQLVWRESVRQLYQEKRG
|
Transcriptional repressor for the ribose rbsDACBK operon.
|
Q9CPA2
|
A2WXR5
|
ALFL6_ORYSI
|
PHD finger protein ALFIN-LIKE 6
|
Oryza sativa
|
MEGGGGGGGGGGGGGGGGGGGGAPYATRTAEEVFRDLRGRRAGMIKALTTDVEKFYKLCDPEKENLCLYGYPNETWEVTLPAEEVPPEIPEPALGINFARDGMNEKDWLALVAVHSDSWLLSVAFYFGARFGFDREARRRLFNMINNLPTIFEVVTGAAKKQAKEKTPNSSSKSNKPSSKVQSKAESRSKSKLSAPKDEEGSGDDEGEEEEDDHDNTLCGTCGTNDGKDEFWICCDNCEKWYHGKCVKITPARAEHIKQYKCPDCTNKRTRA
|
Histone-binding component that specifically recognizes H3 tails trimethylated on 'Lys-4' (H3K4me3), which mark transcription start sites of virtually all active genes.
|
A2WXR5
|
Q93705
|
UNC3_CAEEL
|
Uncoordinated protein 3
|
Caenorhabditis
|
MSLTAPLRAGQMNFYDEPYNPVLNLHIQPSVKDENQRSTWPIIDTSNTSTQIARAHFEKHPPNNLRKSNFFHFVIALYDRNSQPIEVERTQFAGFVEKEKEVDGQDTRNGIHYRLSLMFQNGIRSEHDLFVRLIDSSTKQAITYEGQDKNPEMCRVLLTHEVMCSRCCEKKSCGNRNETPSDPVIIDRFFLKFFLKCNQNCLKNAGNPRDMRRFQVVLCSSARIDGPLLAVSDNMFVHNNSKHGRRTKRTDASDDSEYSESAELPSSVPVIKALFPSEGWIQGGTQVVLIGENFFEGLQVAFGTASPNWGESVQLISPHAIRVTTPPKHSAGPVDVTLQYKSKTYSRGTPLRFSYITLAEPGIEYGFQRLQKLLPKYPGDPERLPKDQILKRAAELAEALYNRTSTESLSSYYHTQFDATSDYAARTHTSPRSTLPYGAGPPALSSAVYQTSYPTVNATPAANFLNTQTGFATFGAVNPFAATLQSSSRLS
|
Transcription factor . Involved in motor neuron fate determination and maintenance, acting as an activator of gene expression in a subset of motor neurons . May act in concert with GFI1 homolog pag-3 in motor neuron fate determination . Required to maintain the expression of transcriptional repressors bnc-1 and cfi-1, which play roles in the cell fate of motor neurons . May play a role in the expression of proteins essential for axonal pathfinding and/or neuronal differentiation in both sensory and motor neurons . Cooperates with jmjd-3.1 and wdr-5.1 to ensure robust transdifferentiation of the Y rectal cell to the PDA motor neuron during larval development .
|
Q93705
|
A4Y732
|
AROA_SHEPC
|
5-enolpyruvylshikimate-3-phosphate synthase
|
Shewanella
|
MKQLRLEPVVQVRGEINIPGSKSISNRALLLATLAQGTTTLTNLLDSDDIRHMLASLKQLGVNYRLSQNNTVCELDGIGGVISSASAQELFLGNAGTAMRPLCAALTLGQGEFTLTGEPRMEERPIGDLVDALRQLGANIVYLKNDGFPPLTINATGLNGGDVEIAGDLSSQFLTALLMVAPLAKGSVNIHVKGELVSKPYIDITIALMAQFGVNVINHDYARFEIVAGQRYISPGKVLVEGDASSASYFLAAGAIKGGEVKVTGVGRLSIQGDVKFADVLEKMGADIEWGDDYIIARGSPLTAVDLDMNHIPDAAMTIATAALFAKGTTVIRNIYNWRIKETDRLAAMATELRKVGAEVEEGNDYIKITPPAVINTAEIDTYNDHRMAMCFSMLAFADCGITINDPDCTSKTFPDYFKQFASLQG
|
Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.
|
A4Y732
|
A5VJ33
|
MURG_LIMRD
|
Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase
|
Limosilactobacillus
|
MRLLVSGGGTGGHIYPALALIERLKQVEPDTEVLYVGTTRGLENKIVPDAGIELETMHMQGFKRSLSLENFKTIYLFLNSVHHAKKIISEFKPDVVLGTGGYVSGAVLYAAAKKHIPTVIHEQNSVVGVTNKFLSRYVDQIAIAFEAARSQFPADKVTMAGNPRAQQVAAKKDSDFSWTRYDLKDDVPTLMIFGGSQGAPKINKTVVDAIPEFNKRPYQVIFATGQKRYDDVKKQLAEGNIKPADNVKVVPYIKDMPAKMPRVAALVSRAGATTIAEVTALGVPTILIPSPYVTANHQVKNAQALVKNNAGLMITEDKLDARALLTQADKIMEDEEVRKEMAHAAEKMGRPDAADRLIKILHKAIDEHEK
|
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).
|
A5VJ33
|
Q2W2J8
|
RL16_MAGSA
|
50S ribosomal protein L16
|
Magnetospirillum
|
MLSPKRTKFRKAHKGRIKGVTKGGSALNFGAYGLKALEPERITARQIEAARRALTRHMKRQGRVWIRIFPDLPVSSKPAEVRMGSGKGAPEFWTARVAPGRILFEVDGVAEEIARHGFALAAAKLPIKTKFISRIGDI
|
Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs.
|
Q2W2J8
|
Q21691
|
NRDE3_CAEEL
|
Nuclear RNAi defective-3 protein
|
Caenorhabditis
|
MDLLDKVMGEMGSKPGSTAKKPATSASSTPRTNVWGTAKKPSSQQQPPKPLFTTPGSQQGSLGGRIPKREHTDRTGPDPKRKPLGGLSVPDSFNNFGTFRVQMNAWNLDISKMDERISRIMFRATLVHTDGRRFELSLGVSAFSGDVNRQQRRQAQCLLFRAWFKRNPELFKGMTDPAIAAYDAAETIYVGCSFFDVELTEHVCHLTEADFSPQEWKIVSLISRRSGSTFEIRIKTNPPIYTRGPNALTLENRSELTRIIEAITDQCLHNEKFLLYSSGTFPTKGGDIASPDEVTLIKSGFVKTTKIVDRDGVPDAIMTVDTTKSPFYKDTSLLKFFTAKMDQLTNSGGGPRGHNGGRERRDGGGNSRKYDDRRSPRDGEIDYDERTVSHYQRQFQDERISDGMLNTLKQSLKGLDCQPIHLKDSKANRSIMIDEIHTGTADSVTFEQKLPDGEMKLTSITEYYLQRYNYRLKFPHLPLVTSKRAKCYDFYPMELMSILPGQRIKQSHMTVDIQSYMTGKMSSLPDQHIKQSKLVLTEYLKLGDQPANRQMDAFRVSLKSIQPIVTNAHWLSPPDMKFANNQLYSLNPTRGVRFQTNGKFVMPARVKSVTIINYDKEFNRNVDMFAEGLAKHCSEQGMKFDSRPNSWKKVNLGSSDRRGTKVEIEEAIRNGVTIVFGIIAEKRPDMHDILKYFEEKLGQQTIQISSETADKFMRDHGGKQTIDNVIRKLNPKCGGTNFLIDVPESVGHRVVCNNSAEMRAKLYAKTQFIGFEMSHTGARTRFDIQKVMFDGDPTVVGVAYSLKHSAQLGGFSYFQESRLHKLTNLQEKMQICLNAYEQSSSYLPETVVVYRVGSGEGDYPQIVNEVNEMKLAARKKKHGYNPKFLVICTQRNSHIRVFPEHINERGKSMEQNVKSGTCVDVPGASHGYEEFILCCQTPLIGTVKPTKYTIIVNDCRWSKNEIMNVTYHLAFAHQVSYAPPAIPNVSYAAQNLAKRGHNNYKTHTKLVDMNDYSYRIKEKHEEIISSEEVDDILMRDFIETVSNDLNAMTINGRNFWA
|
Transports small interfering RNAs (siRNAs) from the cytoplasm to the nucleus. Required for RNA interference (RNAi) in nuclei . Required for exogenous RNAi-induced H3K27 methylation .
|
Q21691
|
A0PT89
|
RECA_MYCUA
|
Recombinase A
|
Mycobacterium
|
MAQAPDREKALELAMAQIEKSYGKGSVMRLGDEVRQPISIIPTGSIALDVALGIGGLPRGRVIEIYGPESSGKTTVALHAVANAQAAGGVAAFIDAEHALDPEYAKKLGVDTDSLLVSQPDTGEQALEIVDMLIRSGALDIVVIDSVAALVPRAELEGEMGDSHVGLQARLMSQALRKMTGALNNSGTTAIFINQLRDKIGVMFGSPETTTGGKALKFYASVRMDVRRIETLKDGTNAVGNRTRVKIVKNKVSPPFKQAEFDILYGRGISREGSLIDMGVDQGFIRKSGAWFTYEGEQLGQGKENARNFLLENGGVANEIEKKIKEKLGIGAVVTDDGVLPAPVDF
|
Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage.
|
A0PT89
|
Q88XX0
|
RL18_LACPL
|
50S ribosomal protein L18
|
Lactiplantibacillus
|
MISKPDKNKTRQRRHARVRGKISGTAERPRLNVYRSNKNIYAQVIDDVEGVTLASASTLDSEVKGNNKTEKAASVGEVVAKRAAEKKIVDVVFDRGGYLYHGRVQALAEAARENGLKF
|
This is one 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.
|
Q88XX0
|
P68064
|
HBB2_PANON
|
Hemoglobin beta-2 chain
|
Panthera
|
MGFLSAEEKGLVNGLWSKVNVDEVGGEALGRLLVVYPWTQRFFQSFGDLSSADAIMSNAKVKAHGKKVLNSFSDGLKNIDDLKGAFAKLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGHEFNPQVQAAFQKVVAGVAKALAHRYH
|
Involved in oxygen transport from the lung to the various peripheral tissues.
|
P68064
|
Q9PEN0
|
AOTC_XYLFA
|
N-acetyl-L-ornithine transcarbamylase
|
Xylella
|
MALKHFLNTQDWSCSELNALLTQARAFKHNKLGNGLKGKSIALVFFNASMRTRSSFELGAFQLGGHAIVLQPGKDAWPIEFDTGTVMEAETEEHICEVARVLGHYVDLIGVRAFPKFLDWTYDRQDIVLNGFAKYSPVPVINMETITHPCQELAHIMALQEHFGTTDLRGKKYVLTWTYHPKPLNTAVANSALTIATRLGMDVTLLCPTPDYVLDERYIDWAQQNIADTGSTFQVSHDIDNAYRGADVIYAKSWGALPFFGNWAMEKPIRDQYRHFIVDEAKMALTNNAVFSHCLPLRRNVKATDAVMDGPNCIAIHEAGNRLHVQKAIMAALASQ
|
Catalyzes the transfer of the carbamoyl group from carbamoyl phosphate to the delta-amino group of N(2)-acetyl-L-ornithine to produce N(2)-acetyl-L-citrulline. This is a step in an alternative arginine biosynthesis pathway. The enzyme has no activity with ornithine.
|
Q9PEN0
|
Q12746
|
PGA3_YEAST
|
Processing of GAS1 and ALP protein 3
|
Saccharomyces
|
MSKEDIEGTNILDEPVHGIYIPAALFVVGVAITTYMSGELKILWSLPILFMIIFVRAYSAYKRRRSLYPDRWTSLELEDQTIISKNTALYRFKLKTRLESLDIPAGHHVAVRVPIDGKQEVRYYNPISSKLESGYLDLVVKAYVDGKVSKYFAGLNSGDTVDFKGPIGTLNYEPNSSKHLGIVAGGSGITPVLQILNEIITVPEDLTKVSLLYANETENDILLKDELDEMAEKYPHFQVHYVVHYPSDRWTGDVGYITKDQMNRYLPEYSEDNRLLICGPDGMNNLALQYAKELGWKVNSTRSSGDDQVFVF
|
NADH-dependent cytochrome b5 reductase that reduces coenzyme Q6 at the plasma membrane and mediates lifespan extension by calorie restriction by shifting fermentative to respiratory metabolism, probably through modulating the NAD(+)/NADH ratio.
|
Q12746
|
Q67ES9
|
TR104_RAT
|
Taste receptor type 2 member 21
|
Rattus
|
MLSMLESILLSVATSEAMLGILGNIFIVLVNCTNWVRNKKLSKINFILTGLAISRVFTIWIITLDAYTKVFFLTTLMPSNLHECISYIWVIINHLSVWFATSLSIFYFLKIANFSHYIFLWLKRRADKVFVFLIGYLIITWLASFPLAVTVIKNIKVHHNNTSWLIQLEKRELLINYVFANMGPISLFMVAVFTCFLLTISLWRHRRRMQSTGSKFRDLNTEVHVKAMKVLISFIILFILYFMGVLIETLCLFLTENILLFIFGFTLSSTYPCCHSFILILTSRELKQASMRALQRLKCCET
|
Putative taste receptor which may play a role in the perception of bitterness.
|
Q67ES9
|
D2TDP0
|
SSUD_ERWP6
|
FMNH2-dependent aliphatic sulfonate monooxygenase
|
Erwinia
|
MRLSVFWFLPTHGDGKYLGTNEGARPVDHAYLQQIAQAADRLGFGGVLIPTGRSCEDAWLVAASLIPVTQRLRFLVALRPGVISPTQAARQAATLDRLSNGRALFNLVTGGDAEELAGDGVFLDHGERYAESAEFTRVWRRVLEGETVDYKGKHVHVRGARLMFKPVQQPRPPLWFGGSSEVAQDLAAEQVDVYLTWGEPPAQVKEKIARVQAKAAARGRKVRFGIRLHVIVRETNDEAWQAADRLISHLDDQTIAKAQAALARTDSVGQQRMAALHGGKRDRLEISPNLWAGVGLVRGGAGTALVGDGPTVAARMQEYADLGIETFILSGYPHLEEAYRVGELLFPHLELNIPEVPKPAAVQAHGEHVAHDFAPQKVPQGER
|
Catalyzes the desulfonation of aliphatic sulfonates.
|
D2TDP0
|
Q62052
|
P_MOUSE
|
Pink-eyed dilution protein
|
Mus
|
MRLENKDIRLASAVLEVELHQTSALSVPTCPDPGRLLTVKPATSNYKLGQADPCIPYAGEAAGKSVCVPEHTEFGSFLVKGSSSLKDLSFKEDTPLLWNSSQKKRSQLMPVHHPEFIATEGSWENGLTAWEQKCMLGKEVADLSALASSEKRDLAGSVHLRAQVSKLGCCVRWIKITGLFVFVVLCSILFSLYPDQGKFWQLLAVSPLENYSVNLSGHADSMILQLDLAGALMAGGPSGSGKEEHVVVVVTQTDAAGNRRRRPQQLTYNWTVLLNPRSEHVVVSRTFEIVSREAVSISIQASLQQTRLVPLLLAHQFLGASVEAQVASAVAILAGVYTLIIFEIVHRTLAAMLGALAALAALAVVGDRPSLTHVVEWIDFETLALLFGMMILVAVFSETGFFDYCAVKAYQLSRGRVWAMIFMLCLMAAILSAFLDNVTTMLLFTPVTIRLCEVLNLDPRQVLIAEVIFTNIGGAATAIGDPPNVIIVSNQELRKMGLDFAGFTAHMFLGICLVLLVSFPLLRLLYWNKKLYNKEPSEIVELKHEIHVWRLTAQRISPASREETAVRGLLLEKVLALEHLLAQRLHTFHRQISQEDKNWETNIQELQRKHRISDRSLLVKCLTVLGFVISMFFLNSFVPGIHLDLGWIAILGAIWLLILADIHDFEIILHRVEWATLLFFAALFVLMEALTHLHLVEYVGEQTALLIKMVPEDQRFAAAIVLIVWVSALASSLIDNIPFTATMIPVLLNLSQDPEISLPALPLMYALALGACLGGNGTLIGASTNVVCAGIAEKHGYGFSFMEFFRLGFPVMLMSCTIGMCYLLIAHIVVGWN
|
Could be involved in the transport of tyrosine, the precursor to melanin synthesis, within the melanocyte. Regulates the pH of melanosome and the melanosome maturation. One of the components of the mammalian pigmentary system. Seems to regulate the postranslational processing of tyrosinase, which catalyzes the limiting reaction in melanin synthesis. It can modulate intracellular glutathione metabolism.
|
Q62052
|
F1CJ80
|
KA23J_HOTJU
|
U10-hottentoxin-Hj3a
|
Hottentotta
|
MQKLLIILILFCILKFNVDVEGRTATMCDLPECQERCKRQNKKGKCVIEPEMNIVYHLCKCY
|
May block potassium channels.
|
F1CJ80
|
P0DO11
|
FLZ17_ARATH
|
FCS-Like Zinc finger 17
|
Arabidopsis
|
MTKISVGLQLVTRDSREKLNNIVIKSSLRLNRSNPNISELCFLKTCHLCNKQLHQDKDVYMYRGDLGFCSRECRESQMLIDDRKELEASTKMMLASYRRCNNGAGKSESRNLFDDLRRRRQLFIVP
|
May act as an adapter to facilitate the interaction of SnRK1 complex with effector proteins, conferring tissue- and stimulus-type specific differences in the SnRK1 regulation pathway.
|
P0DO11
|
Q6L367
|
IF1C_SACHY
|
Translation initiation factor IF-1, chloroplastic
|
unclassified Saccharum
|
MTEKKNRREKKNPREAKVTFEGLVTEALPNGMFRVRLENDTIILGYISGKIRSSSIRILMGDRVKIEVSRYDSSKGRIIYRLPHKDSKRTEDSKDTEDLKDTKDSKD
|
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.
|
Q6L367
|
P09824
|
NIFB_RHIME
|
Radical SAM assemblase NifB
|
Sinorhizobium
|
MSTPMILRESRTSTTFSDQLLENAKSVGCSPPSTAPGDIDPGTWDKIKNHPCFSEEAHHYFARMHVAVAPACNIQCNYCNRKYDCANESRPGVASEKLTPDQAVRKVIAVANEVPQLSVLGIAGPGDACYDWKKTRATFERVAREIPDIRLCISTNGLSLPDHVDELAEMNVDHVTITINMVDPRVGVKIYPWIYYGQRRHTGIDAARILHERQMLGLEMLAERGILTKVNSVMIPGVNDEHLIEVNKVVKGRGALLHNVMPLISNRIHGTYYGLTGQRGPEAFELQALQDRLEGTKLMRHCRHCRADAIGLLGDDRGHEFTLAEIPDEITYDASKRQAYRQLVARERGDHLVAKNEANRTVMSVEYGGSLLIAVATKGGGRINEHFGHAKEFHVYTVSQRGIKLAGRRRVEQYCLGGWGEVATLDHIVVALEGIDILLCVKIGDYPRKQLTQAGLRATEAYGHDYIESALGALYAAEFGIEPPVKTATA
|
Involved in the biosynthesis of the iron-molybdenum cofactor (FeMo-co or M-cluster) found in the dinitrogenase enzyme of the nitrogenase complex in nitrogen-fixing microorganisms. NifB catalyzes the crucial step of radical SAM-dependent carbide insertion that occurs concomitant with the insertion of a 9th sulfur and the rearrangement/coupling of two [4Fe-4S] clusters into a [8Fe-9S-C] cluster, the precursor to the M-cluster.
|
P09824
|
P54110
|
RS14Z_METJA
|
30S ribosomal protein S14 type Z
|
Methanocaldococcus
|
MAKKPWKKKYGYGIRPCQRCGHVGPGLIRKYGLNLCRQCFREIAHKLGFKKLD
|
Binds 16S rRNA, required for the assembly of 30S particles.
|
P54110
|
Q73M68
|
RPIA_TREDE
|
Phosphoriboisomerase A
|
Treponema
|
MDTSQLKERVAYHAIDTLFSEGKIFDGMKIGLGTGSTAMPAVHRLAQLLSSGKLKKIYAVPTSFQTSIECEKLGIPIYSLSSQQIGGSLDLAIDGADEIDPDKNLIKGGGAALLKEKIIAYNSKEFVVIADERKKVKSMGKGFALPIEIIPEARLSITKALEAQGIEVFLREGVKKMGPVVTDNGNFIIDVKWPKAADVDPKALEESLNKITGVVENGFFTKNTPRVFIVHQDGNIEDL
|
Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
|
Q73M68
|
P05934
|
CALM_STRPU
|
Calmodulin
|
Strongylocentrotus
|
LTMMARKMKETDSEEEIREAFRVFDKDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVAMMTSK
|
Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases.
|
P05934
|
P0C0I7
|
SPEH_STRP1
|
SPE H
|
Streptococcus
|
MRYNCRYSHIDKKIYSMIICLSFLLYSNVVQANSYNTTNRHNLESLYKHDSNLIEADSIKNSPDIVTSHMLKYSVKDKNLSVFFEKDWISQEFKDKEVDIYALSAQEVCECPGKRYEAFGGITLTNSEKKEIKVPVNVWDKSKQQPPMFITVNKPKVTAQEVDIKVRKLLIKKYDIYNNREQKYSKGTVTLDLNSGKDIVFDLYYFGNGDFNSMLKIYSNNERIDSTQFHVDVSIS
|
Mitogenic for human peripheral blood lymphocytes.
|
P0C0I7
|
Q66JA6
|
CAB45_XENLA
|
Stromal cell-derived factor 4
|
Xenopus
|
MVSKQAFLFSLGSLYLSLLFIFLLMDVYARPANNSALKVETKEKATDNKDENEILPPDHLNGVKMEMDGHLNKEFHQEVFLGKELEEFDEDSEPRRNRRKLAAIFAKVDRNEDKQISASEMQRWIMEKTEEHFQEAVNENKLHFRAVDPDGDGHVSWDEYKIKFLASKGFNEKEVAEKLKNNEDLKIDEETQEVLDNLKDRWFQADNPPPDQLLNEEEFLSFLHPEHSRGMLKFMVKEIIRDLDQDGDKKLTLSEFISLPVGTVENQQAQDIDDDWVRDRKKEYEEVIDANHDGIVTMEELEEYMDPMNEYNALNEAKQMIAVADENQDHLLSLEEILKYSEYFTGSKLMDYARNVHEEF
|
May regulate calcium-dependent activities in the endoplasmic reticulum lumen or post-ER compartment.
|
Q66JA6
|
B2V7F0
|
ILVC_SULSY
|
Ketol-acid reductoisomerase type I
|
unclassified Sulfurihydrogenibium
|
MANIYYDEDASLDYLKDKTVAIIGYGSQGHAHALNLRDSGIKVIIGLLAGSRSIEKAKAEGFEVYSPDEAAKKADVIMILTPDTVQPALYQSAILPNLDEGNALAFAHGFNIHFGQIVPPSYVDVFLVAPKGPGHLVRWMYEEGKGVPGLFAVYQDFTGKAREIAMAYAKGIGATRAGLIETTFKEETETDLFGEQAVLCGGATALIKAGFETLIEAGYQPEVAYFECLHELKLIVDLIYQYGISGMRYSISDTARYGDVTRGKRVYEAVKPLYKKILEEIQEGEFAKEWILENVANRPHFNALVKKDEEHPVEKVGKELRKMMPWLGGRGL
|
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.
|
B2V7F0
|
Q30Y35
|
GATB_OLEA2
|
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B
|
Oleidesulfovibrio
|
MAEYEVVIGLEVHAQLRTSSKLFCACSTEFGSEPNTNVCEICSGMPGVLPVVNRKAVEYAVMMGMAVDCTINNDSVFARKNYFYPDLPYGYQISQFERPLCEHGHLDIPVNGGTKRIGITRIHMENDAGKNIHSAADNASYVDLNRAGTPLIEIVSEPDMRSAEEAVAYLKELRSILLYLGICDGNMEEGSFRCDANVSLRPAGQKEFGTRTELKNVNSFRNVQRAIEVEIARQQDLLEDGEKVVQETRLYDAARNVTASMRGKEEAHDYRYFPDPDLIPLHLEDGWLQEWRKALPELPALRRTRFMEQYGLSVQDAELLTAERELADFYEAAVRHGGVPKKVANLMMGEFMRELNERRISVNEAAMTPEAVAELVRLQEEGVVSSKIVHDIFSDLFTSGSMPEAYVKAKGLVQISDSGAIETAVDEVLAENPAEVEAYRGGKTKLMSFFMGQVMRKTRGKANPAVVTGLLTEKLG
|
Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
|
Q30Y35
|
Q9SVM8
|
RBG2_ARATH
|
Small RNA binding protein 3
|
Arabidopsis
|
MAFCNKLGGLLRQNISSNGNVPVTSMLGSLRLMSTKLFIGGLSWGTDDASLRDAFAHFGDVVDAKVIVDRETGRSRGFGFVNFNDEGAATAAISEMDGKELNGRHIRVNPANDRPSAPRAYGGGGGYSGGGGGYGGGGGGYGGGGGGYGGGGDGGGGF
|
Promotes the cis-splicing and editing of several mitochondrial RNAs (including NAD5 transcripts) . Plays a role in RNA transcription or processing during stress. Binds RNAs and DNAs sequence with a preference to single-stranded nucleic acids. Displays strong affinity to poly(U) sequence. Exerts cold and freezing tolerance, probably by exhibiting an RNA chaperone activity during the cold and freezing adaptation process. Mediates cell-to-cell trafficking of RNA interference (RNAi) signals (small RNAs (sRNA), e.g. small interfering RNA (siRNA) and microRNA (miRNA)) which regulate growth and development, as well as responses to environmental inputs, including pathogen attack; can compromise zucchini yellow mosaic virus (ZYMV) and tobacco rattle virus (TRV) infections at the early stage .
|
Q9SVM8
|
B7L8B3
|
ILVD_ECO55
|
Dihydroxy-acid dehydratase
|
Escherichia
|
MPKYRSATTTHGRNMAGARALWRATGMTDADFGKPIIAVVNSFTQFVPGHVHLRDLGKLVAEQIEAAGGVAKEFNTIAVDDGIAMGHGGMLYSLPSRELIADSVEYMVNAHCADAMVCISNCDKITPGMLMASLRLNIPVIFVSGGPMEAGKTKLSDQIIKLDLVDAMIQGADPKVSDSQSDQVERSACPTCGSCSGMFTANSMNCLTEALGLSQPGNGSLLATHADRKQLFLNAGKRIVELTKRYYEQNDESALPRNIASKAAFENAMTLDIAMGGSTNTVLHLLAAAQEAEIDFTMSDIDKLSRKVPQLCKVAPSTQKYHMEDVHRAGGVIGILGELDRAGLLNRDVKNVLGLTLPQTLEQYDVMLTQDDAVKNMFRAGPAGIRTTQAFSQDCRWDSLDDDRANGCIRSLEHAYSKDGGLAVLYGNFAENGCIVKTAGVDDSILKFTGPAKVYESQDDAVEAILGGKVVAGDVVVIRYEGPKGGPGMQEMLYPTSFLKSMGLGKACALITDGRFSGGTSGLSIGHVSPEAASGGSIGLIEDGDLIAIDIPNRGIQLQVSDAELAARREAQDARGDKAWTPKNRERQVSFALRAYASLATSADKGAVRDKSKLGG
|
Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively.
|
B7L8B3
|
P08006
|
OPPC_SALTY
|
Oligopeptide transport system permease protein OppC
|
Salmonella
|
MMLSKKNSETLENFSEKLEVEGRSLWQDARRRFMHNRAAVASLIVLFLIALFVTVAPMLSQFTYFDTDWGMMSSAPDMASGHYFGTDSSGRDLLVRVAIGGRISLMVGIAAALVAVIVGTLYGSLSGYLGGKIDSVMMRLLEILNSFPFMFFVILLVTFFGQNILLIFVAIGMVSWLDMARIVRGQTLSLKRKEFIEAAQVGGVSTASIVIRHIVPNVLGVVVVYASLLVPSMILFESFLSFLGLGTQEPLSSWGALLSDGANSMEVSPWLLLFPAGFLVVTLFCFNFIGDGLRDALDPKDR
|
Part of the binding-protein-dependent transport system for oligopeptides; probably responsible for the translocation of the substrate across the membrane.
|
P08006
|
B7UM03
|
RLMF_ECO27
|
rRNA adenine N-6-methyltransferase
|
Escherichia
|
MSAQKPGLHPRNRHHSRYDLATLCQVNPELRQFLTLTPAGEQSVDFANPLAVKALNKALLAHFYAVANWDIPDGFLCPPVPGRADYIHHLADLLAEASGTIQANASILDIGVGANCIYPLIGVHEYGWRFTGSETSSQALSSAQAIISANPGLNRAIRLRRQKESGAIFNGIIHKNEQYDATLCNPPFHDSATAARAGSERKRRNLGLNKDDALNFGGQQQELWCEGGEVAFIKKMIEESKGFAKQVMWFTSLVSRGENLPPLYRALTDVGAVKVVKKEMAQGQKQSRFIAWTFMNDEQRRRFVNRQR
|
Specifically methylates the adenine in position 1618 of 23S rRNA.
|
B7UM03
|
C4Y459
|
GATB_CLAL4
|
Glutamyl-tRNA(Gln) amidotransferase subunit B, mitochondrial
|
Clavispora
|
MEEKSQVQLDSHIFNTTSSSSQYYPLNVMISRSIKGWRPEPGYPFKCGIEIHTQLKTKHKLFSLSKNSPGAAPNTCASYFDFGLPGTIPKLNPEALLLALRAAVALKSDISSISSFDRKHYFYMDQPLGYQITQHYQPLAKNGHLSLVPRLDDVEEAKTIHVEQIQLEQDTAKLNYNAYDGTVDIDHNRANVPLIEMVTKPDFSHLSELRAFVKKYISLMTHLGVCSGDMENGALRCDVNVSVAGGNRVEIKNLGSTSEIIAAAKYEYARQVQLLKHGKTPVEQETRSWDGTKTIRTRSKEDAIDYRYFPDVELPRIRLHPSIGKDLSQTLPELPEQLIQQLCEEPFLLEVKHARFLVENPDLYNYYKNLHHIIVDKHKLSYKVVNNWIIHEFIGAFNKLDIPVDVSVIDTEKLASLIIMVSEKKISITSAKLLLTQILQSPEDRELSIPDLIDAYDLGAVNDIHGDDLKEAIKEVCSEVIDSHPDVVTKIRNGKTKSINFLIGRAMKETQGKVDSKEFEKMFKKLIG
|
Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
|
C4Y459
|
P16591
|
FER_HUMAN
|
p94-Fer
|
Homo
|
MGFGSDLKNSHEAVLKLQDWELRLLETVKKFMALRIKSDKEYASTLQNLCNQVDKESTVQMNYVSNVSKSWLLMIQQTEQLSRIMKTHAEDLNSGPLHRLTMMIKDKQQVKKSYIGVHQQIEAEMIKVTKTELEKLKCSYRQLIKEMNSAKEKYKEALAKGKETEKAKERYDKATMKLHMLHNQYVLALKGAQLHQNQYYDITLPLLLDSLQKMQEEMIKALKGIFDEYSQITSLVTEEIVNVHKEIQMSVEQIDPSTEYNNFIDVHRTTAAKEQEIEFDTSLLEENENLQANEIMWNNLTAESLQVMLKTLAEELMQTQQMLLNKEEAVLELEKRIEESSETCEKKSDIVLLLSQKQALEELKQSVQQLRCTEAKFSAQKELLEQKVQENDGKEPPPVVNYEEDARSVTSMERKERLSKFESIRHSIAGIIRSPKSALGSSALSDMISISEKPLAEQDWYHGAIPRIEAQELLKKQGDFLVRESHGKPGEYVLSVYSDGQRRHFIIQYVDNMYRFEGTGFSNIPQLIDHHYTTKQVITKKSGVVLLNPIPKDKKWILSHEDVILGELLGKGNFGEVYKGTLKDKTSVAVKTCKEDLPQELKIKFLQEAKILKQYDHPNIVKLIGVCTQRQPVYIIMELVSGGDFLTFLRRKKDELKLKQLVKFSLDAAAGMLYLESKNCIHRDLAARNCLVGENNVLKISDFGMSRQEDGGVYSSSGLKQIPIKWTAPEALNYGRYSSESDVWSFGILLWETFSLGVCPYPGMTNQQAREQVERGYRMSAPQHCPEDISKIMMKCWDYKPENRPKFSELQKELTIIKRKLT
|
Tyrosine-protein kinase that acts downstream of cell surface receptors for growth factors and plays a role in the regulation of the actin cytoskeleton, microtubule assembly, lamellipodia formation, cell adhesion, cell migration and chemotaxis. Acts downstream of EGFR, KIT, PDGFRA and PDGFRB. Acts downstream of EGFR to promote activation of NF-kappa-B and cell proliferation. May play a role in the regulation of the mitotic cell cycle. Plays a role in the insulin receptor signaling pathway and in activation of phosphatidylinositol 3-kinase. Acts downstream of the activated FCER1 receptor and plays a role in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Plays a role in the regulation of mast cell degranulation. Plays a role in leukocyte recruitment and diapedesis in response to bacterial lipopolysaccharide (LPS). Plays a role in synapse organization, trafficking of synaptic vesicles, the generation of excitatory postsynaptic currents and neuron-neuron synaptic transmission. Plays a role in neuronal cell death after brain damage. Phosphorylates CTTN, CTNND1, PTK2/FAK1, GAB1, PECAM1 and PTPN11. May phosphorylate JUP and PTPN1. Can phosphorylate STAT3, but the biological relevance of this depends on cell type and stimulus.
|
P16591
|
Q9CJJ0
|
ADDB_LACLA
|
ATP-dependent helicase/nuclease RexB
|
Lactococcus
|
MEILYTEITQDLTEGLLEISLEELEKNRKVYYIVPSSMSFEKEKEILERLAKGSDSAVFDLLVTRFKQLPYYFDKREKATTKTELGTAGLSMLFRRVLRSFSKEEIPLYFSLQDSAGFLEMLIQLRTELLTANLSVENLPDSPKNQELKKILSRFEEKLANDYANYSEFGDFTSRLADGEFDFQLKDVTIVIDGYTRFSAEEELFIESIQDRVARFVIGTYSDENSLTAGSETIYISTSQMIGRFRSKFPVELRKMAFSSVNEVYNKLTKLLDLDSRFAISDQNIEINSADAKYFRIWEAENQKVEIEGVAKEIRQKISQGAFFKDFTVLVGDPAAYEITLKEIFELYEIPFFYAQEESMSQHPLVIFFESLLSIKKNNYGTDDVVNLLKSKVYTDVNLDEEVIDYFEYYVQKYKISGRKKFTEAFNESEFSKIELVNQLRENLLGNDSPLQVFLGTNRQKTGKKWVSDLQVLLENGNVMANMNTYFSEAESENKHQMADKHEQVWQMLISILNEFLAVFSDEKLKSVEFLDILLAGLKNAKYRQIPANVDVVNIKDYELVEPKTNKYIYAIGLSQTNFPRIKKNSTLLSDEERLEINQTTDENQFIEQLNVVNYQKNQFTVLSLVNSAKETLVLSMPQIMANEQGEFSPVFQLFLNHSDEKILQKIQEVNLFESLEHIGNSRSVISMIGKIERELVETEEKNDDKRVFWSSIFRILVKSNPDFQKILLDLAKDIDTVNLSQETLDQIYGDKLYASVSSFERFYNCEYQYFLETTLGLETFENIDINSKIVGNFFHEVFEKVMQEEALSAENFDEKLTKVLHDVDSNYSRYFTHDATARFTWTNLEEIVRQTATVLKETVSTDELKTLLTESSFGLPKSELGNFSVDDIYLRGRIDRLDQLSSDYLGAIDYKSSAHSFKLQDAYDGLSLQFMTYLDVIKEAFPNQKIWGALYLQFKNQPINLSEINHLSEIAGLLKESMRYDGLVLEEAADQIKAIENITVKKSNIYNQEEFEQLLKLNENHYQHAGQRLKSGQIAINPIMKRSEGIDQTGNVRGCRYCPLKSICRFEANVHMNDHSREIGQKSQAEILAELKGEGRNE
|
The heterodimer acts as both an ATP-dependent DNA helicase and an ATP-dependent, dual-direction single-stranded exonuclease. Recognizes the chi site generating a DNA molecule suitable for the initiation of homologous recombination. This subunit has 5' -> 3' nuclease activity.
|
Q9CJJ0
|
Q2IJ55
|
RL19_ANADE
|
50S ribosomal protein L19
|
Anaeromyxobacter
|
MLRKAIADIEAKYLRTDLPEMRAGDSVRVHTKIKEGDKERIQVFEGVVIAYRKGAPGSSMFTVRKVSYGVGVERMFPVHSPRIDKIEVVGHGGVRRSRLYFLRNLQGKAARLHQEEGPGAADAAHAAPTPA
|
This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site.
|
Q2IJ55
|
Q2P8Z6
|
PYRF_XANOM
|
OMP decarboxylase
|
Xanthomonas
|
MSRAPLPLAAHERLIFALDVPSHDEAIAWVDRLGDSVAFYKIGMELLASGEYFHVLDALAKRDKRVFVDLKFFDIPATVAGTIRRLAQWPVSYCTVHGWHAGMLQAAADANHGAMRLLAVTVLTSMGRPDLAAMGIDREPVDVVVERALAAEAAGIDGVIASGQEAGPIRRATGPAFSIVCPGIRPGGPVADDQQRIVGVAQAFTDGADAIVVGRPIRLAADPAAAAAAIQAEILAAVGQDRS
|
Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).
|
Q2P8Z6
|
A9WPN2
|
GATA_RENSM
|
Glutamyl-tRNA(Gln) amidotransferase subunit A
|
Renibacterium
|
MTELIKLSAAALAAKLASGEVTSVQVTQAYLDRIALVDGELNAFLHLNAEEALRVAAEVDADRAAGKELHELAGVPIAIKDLIVTKGQPTTAGSKILEGWISPYDATVIEKIRAAKMPILGKTNLDEFAMGSSTEHSAFGPTRNPWDLTRIPGGSGGGSAAAVAAFEAPLALGTDTGGSIRQPGAVTGTVGVKPTYGGVSRYGAIAMASSLDQIGPVSRTVLDAALLQEVIGGHDPKDSTSLVDPINGQTGCTGLADAARLGANGDLTGVRIGVVKELGGEGYQEGVEVRFRESLELLRGAGAEIVEVSCPSFGYALGAYYLIMPSEASSNLAKFDGVRFGLRKLPEDGPMTIERVMSATRAAGFGNEVKRRIILGAYALSAGYYDAYYGSAQKFRTLIQRDFEAAFAQADVLISPTAPTTAFKFGEKMADPLAMYLNDVATIPANLAGVPGMSLPNGLADEDGLPSGIQLLAPAREDALMYRVGAALEALHEAQWGGPILDRAPELGAASNATAVEGTK
|
Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
|
A9WPN2
|
Q8UGE7
|
RS6_AGRFC
|
30S ribosomal protein S6
|
Agrobacterium tumefaciens complex
|
MALYEHIFLARQDISAQQVDALVEQYKGVIESFGGKVGRVENWGLKSLTYRIKKNRKAHYALMDIDAPAAAVHEVERQMRINEDVLRYMTIAVEAHEEGPSAMMQKRDRDDRPRRDGDRPDRGPREDRGPRPPREGGFGDREDRPRRPREDRA
|
Binds together with S18 to 16S ribosomal RNA.
|
Q8UGE7
|
A6VMI0
|
DAPE_ACTSZ
|
N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase
|
Actinobacillus
|
MKHNIIELAQNLIRRPSVSPDDQGCQQMIAQRLEKLGFTIEWMPFNNTLNLWAKHGCGAPVIAFAGHTDVVPTGDKSQWVYPPFEAEIVDDMLYGRGAADMKGSLAAMVVAAEEYVKANPNHAGTIAFLITSDEEAAAKDGTVRVVETLMARGEKIDFCMVGEPSSSKTLGDIVKNGRRGSVTGNLYIEGVLGHVAYPHLAENPVHKALPFLQELTAYQWDNGNEFFPPTSLQIANIQAGTGSNNVIPGELYVQFNLRYCTEVTDEFIKNTVAEMLKKHGLAYRIEWNLSGKPFLTEPGKLVDAVVDSLESVAGVKPKLDTGGGTSDGRFIALMGAEVVELGPLNATIHKVDERVSVTDLVTLGAVYNQMLVNLLD
|
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.
|
A6VMI0
|
Q8S8N6
|
PLA2A_ARATH
|
Secretory phospholipase A2-alpha
|
Arabidopsis
|
MAAPIILFSFLLFFSVSVSALNVGVQLIHPSISLTKECSRKCESEFCSVPPFLRYGKYCGLLYSGCPGERPCDGLDSCCMKHDACVQSKNNDYLSQECSQKFINCMNNFSQKKQPTFKGNKCDADEVIDVISIVMEAALIAGKVLKKP
|
PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Releases lysophospholipids (LPLs) and free fatty acids (FFAs) from membrane phospholipids in response to hormones and other external stimuli. Modulates the trafficking of PIN proteins to the plasma membrane . Negatively regulates MYB30 transcriptional activity and hypersensitive response control .
|
Q8S8N6
|
Q8Y7I9
|
LUXS_LISMO
|
Autoinducer-2 production protein LuxS
|
Listeria
|
MAEKMNVESFNLDHTKVKAPFVRLAGTKVGVHGDEIYKYDVRFKQPNKEHMEMPALHSLEHLMAELARNHTDKLVDISPMGCQTGFYVSFINHSDYDDALEIIATTLTDVLVATEVPACNEVQCGWAASHSLEGAKALAEEFLAKRSEWKNVFGE
|
Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD).
|
Q8Y7I9
|
Q03QS9
|
DPO3_LEVBA
|
DNA polymerase III PolC-type
|
Levilactobacillus
|
MDEDRHALFEKLLQQLDLTSEADQPYFQTATVDRLTVHEQSRRWQFLLKLPSMLPFTAFVDFHNHLQVAFREIATVEATIEVDQPELTNRLLGDYWEWIVKNSGLTSNLIQELCQSQVPELDENNRVLLYAQNEVVKDFLSNQALGPIESAYRRAGFPKFNIHVMIDESKSQAKIDEFKARQEKTDAQLAQQAAAAIEKANQKRQSQGDTPAAEGPTQIGKAIKGDQPVTKMIDITQEERSVVVEGYVFEKEVRKLRSGRQLLTLKITDYTSSFAVKKFSRGAEDEAQFAGVEEGSWVKVRGNVQEDTYMHDLALNAYDINQVKHASRQDTAPEGEKRVELHLHTSMSQMDATNSIGDYVKQAKKWGMPALAITDHADVQGFPAAFNSAAKAGIKMLYGVEANLVDDGVPIGYNSAHVPLDGATYVVFDVETTGLSAIYDKVIELSAVKMEHQNVVDQFEEFIDPGFPLSEQTTNLTSITDDMVAGSKSEEEVFKLFREFCGDAIIVGHNVTFDVGFMNTGYQRHGMAEISNPIIDTLTLARFLYPTLKSYRLNTLAKRFHVSLEHHHRAVYDAESTGHLNYLFLKDAEDRYDIQYHDQLNDHMTDNDAYKHARPNHAILLAKTQAGLKNMFKLVSASNVDYYYRVPRVPRSVLEEYREGIIVGSACSSGEVFTAMMQKGQVEAAAKAKFYDYLEVQPSAAYQPLIDSGLIADRENMEEIVRNMVKLGHDLNKPVVATGDVHFLNPDDYIYRKILIHSQGGANPLNRQELPDVHFMTTDEMLTDFAYLGEETAKEIVVTNTQKIADDIDEVHPLKDKLYTPRMEGAEDEIRQRTMDTAHAMYGDPLPELVQHRVDRELKSIIGNGFSVIYLIAQRLVAKSNKDGYLVGSRGSVGSSLVATLTGITEVNPLPPHYRCPKCQYSHFYTKGEYSSGYDLPEKDCPECGTLMIGDGHNIPFETFLGFKGNKVPDIDLNFSGDYQPIAHNYTKVLFGEKNVYRAGTIGTVADKTAYGYVKAYERDTEQTFRGAEIDRLAKGATGVKRTTGQHPAGIIVVPDYMDIFDFTPIQYPADDQSAAWQTTHFDFHSIHDNILKIDILGHDDPTMIRTLQDLSGVDPTTIPMDDPGVMGLFSGTDSLGVTPEQIQSKTGTLGVPEFGTRFVRGMLEETHPQNYSQLLQISGLSHGTDVWLGNAEELIKNGTATIANVIGCRDNIMTDLINFGLDSETSFQVMEHVRKGRGIPDEWQEKMKATDCPDWYIDSCLKIKYMFPRAHAAAYVLMALRVAYFKVYFPIIYYAAYFSVRADDFDVVAMSQGKTAVKAAMKAINDQGMDASAKDKNLLTVLELANEMLERGFKFKMIDLEKSDAADWIIDGDTLIAPFKAAPGLGLNVAKQIVAARNDRPFISKEDLAKRGKVSKTLIDFMTENGVLAGLPDENQLSLFDDLM
|
Required for replicative DNA synthesis. This DNA polymerase also exhibits 3' to 5' exonuclease activity.
|
Q03QS9
|
B1VZW1
|
DNLJ2_STRGG
|
Polydeoxyribonucleotide synthase [NAD(+)] 2
| null |
MAGEDRVEQESSVPADVREKHALLAEQIEEHRFRYYVKDQPVVSDADFDRQLRSLEALEEEHPSLRTPDSPTQKVAGPYRTEFTSVEHRERMLSLDNAFDDEELAAWADRVAKDVGTPDHHFLCELKVDGLAVNLTYEHGRLTRAATRGDGRTGEDITPNVRTIAEIPHRLKGEDIPALVEIRGEVFFPMEDFEELNARLVAADDKPFANPRNAAAGSLRQKDPKVTATRPLHMVVHGIGAHEGLSIDRLSAAYDLLHTWGLPTARHNKVVDSLAGVREFIAHYGENRHSVEHEIDGVVVKLDEIPLQGRLGSTSRAPRWAIAWKYAPEEVNTKLVNIRVGVGRTGRVTPYAQVEPVEVAGSEVEFATLHNQNVVKAKGVLIGDTVVIRKAGEVIPEILGPVVDLRDGTEKAFEMPTHCPECGTELRPMKEADIDLRCPNARTCPAQLRERVFYLAGRKSLDIDHFGYVAAAALTRPLEPAEPVLKDESDLFSLTVEQLLPIRAYVLDQDSGLPKRDPKTGEEKIATVFANQQGEPKKNAVAMLEGIAAAKDAPLARVLTGLSIRHVGPVAAQELARQFRSIERIDEATEEELAAADGVGPTIAASVKQWFAEDWHREIVRKWREAGVRMADEGSDEDEGPRPLEGLTVVVTGTLAGHTRDGAKEALQALGAKVAGSVSKKTAFVVVGDNPGSKYDKAMQLKVPVLDEDGFAILLEQGPERAKEAALPVPEAAPAADPENSGE
|
DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
|
B1VZW1
|
Q5FNB7
|
MSCL_GLUOX
|
Large-conductance mechanosensitive channel
|
Gluconobacter
|
MSETKHTLHTPGWVSDFQKFIMRGNVLDLAVGVVIGAAFSAIVGSAVKDILTPFIGLITGGVDFSNLFITLKGPVKDTLAEAQKAGAVTVNIGVFLNAVIQFLIIAFFIFWLTRILSKLSRKQEAAPAAPPAPTKEEVLLTEIRDLLAQKNS
|
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.
|
Q5FNB7
|
Q80SY6
|
ADAL_MOUSE
|
Adenosine deaminase-like protein
|
Mus
|
MEAGQQWPGKTDFYLQLPKVELHAHLNGSISSSTMKKLIAKKPHLNVHGHMTMIDKGKKRTLQECFQMFQVIHQLTTSAEDILMVTKDVIKEFADDGVKYLELRSTPREENATGMTRKTYVESVLEGIKQCKQENLDIDVRYLMAIDRRGGPTIARETVELAKEFFLSTENTVLGLDLSGDPTIGQANDFLEPLLEAKKAGLKLALHLAEIPNREKENQMLLSLLPDRIGHGTFLSASEAGALDQVDFVRQHQIPLELCLTSNIKSQTVPSYDQHHFGFWYSIAHPSVICTDDKGVFATYLSQEYQLAAETFNLTPFQVWDLSYESINYIFACDNTRSELRKRWTHLKQKVLNCNEVNYF
|
Catalyzes the hydrolysis of the free cytosolic methylated adenosine nucleotide N(6)-methyl-AMP (N6-mAMP) to produce inositol monophosphate (IMP) and methylamine. Is required for the catabolism of cytosolic N6-mAMP, which is derived from the degradation of mRNA containing N6-methylated adenine (m6A).
|
Q80SY6
|
B0BVB7
|
ATPG_RICRO
|
F-ATPase gamma subunit
|
spotted fever group
|
MSNLKQLRTRIKSVKSTQKITKAMQLVSASKMAKIKSQIANSNFYIEAVSKMMSAILSIDMYELSIEEQKFFNTVPNKANLLIVMTSQRGLCGTFNYSIIQQVKNDIKELENKGEQIKLIIIGKKGYEALKRQYVNYIDSYFELPKIHDENLMLQVKQKIMSAVENLEVSNCVIYFNKFKNAMTQIMTRQQILPVAKYQDDSMIDNPIVNLVGFGYKERGAKPINNRSATSDIVGESKSIDYNYEYEGENLISNLINLYVNSQINYALLQSRASEEGARMTAMENATNNANDLISKLVLKLNRSRQAIITTELIEIIAGSEAV
|
Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
|
B0BVB7
|
A0KND9
|
PNP_AERHH
|
Polynucleotide phosphorylase
|
Aeromonas
|
MNPIVKSFQYGQHTVTLETGVMARQATAAVMVSMDDTCVFVTVVGKKEADHGRDFFPLTVNYQERTYAAGRIPGGFFRREGRPSEGETLISRLIDRPIRPLFPEGFLNEVQVVATVMSVNPAVSPDIVAMIGASAALAISGIPFGGPIGAARVGYMNGQYVLNPTTTELPQSDLDLVVAGTANAVLMVESEAAILSEEVMLGAVVFGHEQMQAVINAINEFAADVGTKPWNWTAPAVNEALKAKVAELATAELGEAYRITEKAVRYETIGAIKARVVEQVIASGVEEDAKKIGEEFHSLESRIVRGRVVRGEPRIDGRDPEMIRALSVATGVLPRAHGSALFTRGETQAMVVATLGTERDAQNIDELTGNRADRFMLHYNFPPYCVGETGMMGSPKRREIGHGRLAKRGVAAVMPSADEFPYVVRVVSEITESNGSSSMASVCGSSLALMDAGVPIKASVAGIAMGLVKEEEGFVVLSDILGDEDHLGDMDFKVAGTTEGVTALQMDIKIEGITKEIMEIALKQARGARLHILKVMDEAIQAPRAEISDFAPRIHTIKINPEKIKDVIGKGGSVIRALTEETGTNIELDDDGTVRIAAVDGDAAKEAIRRIEAITAEIEVNRIYEGKVVRLADFGAFVNILPGKDGLVHISQITDARVQNVADYLKIGDVVKVKVLEVDRQGRVRLSIKEANAPTEAAAEPAVAAVEEPAAE
|
Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
|
A0KND9
|
P59851
|
KAX2Z_CENLM
|
Potassium channel toxin alpha-KTx 02
|
Centruroides
|
TVIDVKCTSPKQCLPPCAKQ
|
Potent selective inhibitor of Kv1/KCNA voltage-gated potassium channels.
|
P59851
|
Q143I2
|
DCD_PARXL
|
Deoxycytidine triphosphate deaminase
|
Paraburkholderia
|
MTIKSDKWIRRMAESHKMIEPFAPDQVRVSEDGRKIVSYGTSSYGYDIRCADEFKIFTNINSTIVDPKNFDEKSFVDFKGDVCIIPPNSFALARTVEYFRIPRSVLTVCLGKSTYARCGIIVNVTPFEPEWEGHVTLEFSNTTPLPAKIYANEGVAQVLFFESDEICETSYADRGGKYQGQHGVTLPRT
|
Catalyzes the deamination of dCTP to dUTP.
|
Q143I2
|
Q9ZB21
|
UVRB_MYCPL
|
Excinuclease ABC subunit B
|
Mycoplasmopsis
|
MEEKFVLHSPFAPSGDQPEAIKALVDGIDEKKEHQVLLGVTGSGKTFTIANVIAQLNRPSLIISHNKTLASQLYSELKALFPDNRVEYFVSYFDFYKPEAYIPKSDLYIEKTSKNNKELEAMRMSAINALSIRKDTIVVASVAAIYGESNPKHYRQNFFPIEVGMQIDRKSLLLKLSQIGYERNRMELNKGQFDVKGDSIEICPGYVSDTNIRIDMFGNEIEAITLIDPLSKNVEGSRKNMTLFPATTYTVHENTIQNTVDLIKQELSERIEYFKSHDKLLEAQRIKDRTLNDLDSLLEFGYTSGIENYSRYLDGRAPGQRPYTLFDYLPDDSVIFIDESHLMIPQLHGMHNGDRARKLSLVEYGFRLPSALDNRPLRFEEFAEFKFPKIYISATPGDYELDLTHGEIVTQYIRPTGLLDPIIEIHSRDNQIEDIYDHLKEQIAKKERTLILTTTKKNAEELSLFLQEKKIKSAYIHDRFKIFERNEILKGLRMGKFDVVVGINLLKEGIDLPEVSLICVLNADSTGLMRDTRSLIQIVGRAARNDHGKVIFYANEITSSMRECIEDNLFKRKIQSEYNEKHNIIPKTIVKPIAPPIQNGILSEDHSKYYGEKDLSQMKHNKKFIDQMVRKMTQLAKANKFEEAIEIRDYLIEIGIELDK
|
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage.
|
Q9ZB21
|
P0DKV3
|
APOC1_ATEGE
|
Truncated apolipoprotein C-I
|
Ateles
|
MRLFLSLPVLVVVLLMILEGPGPAQGAPEALDTSSGLDKLKEFGNTLEDKVREFFNRVKESDIPAKTRNWFSETLQKVKEKLRIES
|
Inhibitor of lipoprotein binding to the low density lipoprotein (LDL) receptor, LDL receptor-related protein, and very low density lipoprotein (VLDL) receptor. Associates with high density lipoproteins (HDL) and the triacylglycerol-rich lipoproteins in the plasma and makes up about 10% of the protein of the VLDL and 2% of that of HDL. Appears to interfere directly with fatty acid uptake and is also the major plasma inhibitor of cholesteryl ester transfer protein (CETP). Binds free fatty acids and reduces their intracellular esterification. Modulates the interaction of APOE with beta-migrating VLDL and inhibits binding of beta-VLDL to the LDL receptor-related protein.
|
P0DKV3
|
Q1BXP1
|
ASTD_BURCA
|
Succinylglutamic semialdehyde dehydrogenase
|
Burkholderia cepacia complex
|
MTELFIDGAWVAGSGPVFASRNPGTDAVAWQGESASAADVDRAVASARRAFAGWSALDFEARCEIVKRFAALLTERKEAIATAIGRETGKPLWEARTEVASMAAKVGISIQAYQERTGEKRQDMADGVAVLRHRPHGVVAVFGPYNFPGHLPNGHIVPALIAGNTVVFKPSELAPGVARATVEVWQEAGLPAGVLNLVQGEKDTGIALANHRQIDGLFFTGSSDTGTLLHKQFGGRPEIVLALEMGGNNPLVIGEVEDIDAAVHHTIQSAFLSAGQRCTCARRIFVPQGAFGDRFLARFADVTSKITADVFDADPQPFMGAVISARAAAKLVDAQARLVEQGAKPIVAMAQRDPRLGFVNAAIVDVTGVANLPDEEHFGPLAQVVRYATFDEAIERANDTAFGLSAGLLADDAKVWEHFRRTIRAGIVNWNRPTNGASSAAPFGGTGRSGNHRPSAYYAADYCAYPMASVESTQLTLPASLSPGLHF
|
Catalyzes the NAD-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.
|
Q1BXP1
|
Q57M53
|
ARNE_SALCH
|
Undecaprenyl phosphate-aminoarabinose flippase subunit ArnE
|
Salmonella
|
MIGIVLVLASLLSVGGQLCQKQATRPLTTGRRRRHLMLWLGLALICMGAAMVLWLLVLQTLPVGIAYPMLSLNFVWVTLAAWKIWHEQVPPRHWLGVALIISGIIILGSAA
|
Translocates 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol (alpha-L-Ara4N-phosphoundecaprenol) from the cytoplasmic to the periplasmic side of the inner membrane.
|
Q57M53
|
P29642
|
CYB_ASTDO
|
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
|
Asthenes
|
FGSLLGICLMTQIITGLLMAMHYTADTTLAFTSVAHTCRNVQFGWLIRNLHANGASMFFICIYLHIGRGFYYGSYLFKETWNTGVILLLTLMATAFVGYVLPWGQMSFWGATVITNLFSAIPYIGQTLVEWAWGGFSVDNPMLTRFFALHFLLPFMIAGLTFIHLTFLHETGSNNPLGISSNCDKIPFHPYFSTKDILGFLAMLVPLTALAMFSPNLLGDPENFTPANPLVTPPHIKPEWYFLFAYAILRSIPNKLGGVLALAASVLILFLIPFLHKSKQRTMTFRPLSQLLFWILVTNLLILTWVGS
|
Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
|
P29642
|
P58719
|
PDXA_YERPE
|
4-(phosphohydroxy)-L-threonine dehydrogenase
|
Yersinia
|
MHNHNNRLVITPGEPAGVGPDLAITLAQQDWPVELVVCADPALLLARASQLNLPLQLREYQADQPAIAQQAGSLTILPVKTAVNVVPGKLDVGNSHYVVETLAKACDGAISGEFAALVTGPVQKSIINDAGIPFIGHTEFFADRSHCQRVVMMLATEELRVALATTHLPLLAVPGAITQASLHEVITILDNDLKTKFGITQPQIYVCGLNPHAGEGGHMGHEEIDTIIPALNTLRQQGINLIGPLPADTLFQPKYLQHADAVLAMYHDQGLPVLKYQGFGRAVNITLGLPFIRTSVDHGTALELAATGTADVGSFITALNLAIKMINNSNE
|
Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP).
|
P58719
|
Q1LIV1
|
MTGA_CUPMC
|
Peptidoglycan glycosyltransferase MtgA
|
Cupriavidus
|
MRWLAYLAGCLIVGVVAMQVYFFLQIAAWQVVNPSSTTFMRAERWRLCGFNFWSCPVQRQWVRYDEISRNIKRAVIASEDADFVNHPGYELDAMLDAWERNKQRGRIVRGGSTITQQLAKNLFLSSEQNYLRKGQELAITWMLELWLDKQRIFEIYLNSVEWGEGVFGVEAAAQHYFHTSASKLSVGQAARLAAALPAPKCFDKKQYCANVHVNFRVKASIIARRMGAATLPD
|
Peptidoglycan polymerase that catalyzes glycan chain elongation from lipid-linked precursors.
|
Q1LIV1
|
Q5HW21
|
ACCA_CAMJR
|
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha
|
Campylobacter
|
MASYLDFEKNIQQIDEDIINAQIKGDTEAVSILKKNLEKEISKTYKNLSDFQRLQLARHPDRPYALDYIELILNDAHEIHGDRAFRDDPAIVCFMGYLGEKKIIVIGEQKGRGTKDKIARNFGMPHPEGYRKALRVARLAEKFQIPILFLIDTPGAYPGIGAEERGQSEAIARNLYELSDLKIPTIAIVIGEGGSGGALAIGVADKLVMMKNSVFSVISPEGCAAILWNDPAKSEAATKAMKVTADDLKSQGLIDDVIDEPTNGAHRNKEAAAVAIADYVKKSLNELENIDVRELSANRMQKILKLGAYQEA
|
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.
|
Q5HW21
|
A1AQS8
|
NIKR_PELPD
|
Putative nickel-responsive regulator
|
Pelobacter
|
MGETIRFGISIDDKLLESFDQLIEHKGYANRSEALRDLIRASLIDVKWENGEEEMVGTVTLVFNHHVRDLSDKLTEHQHAYHHQIISALHVHLDAHNCLEVLVVRGKAREIKKIADELIGVKGVKHGKLVMTATGHDLH
|
Transcriptional regulator.
|
A1AQS8
|
A8FEQ8
|
SCPA_BACP2
|
Segregation and condensation protein A
|
Bacillus
|
MLEYQVKIDSFEGPLDLLLHLINRLEIDIYDIPVAKITEQYLLYVHTMRELELDVASEYLVMAATLLSIKSRMLLPKQEEELFDEDLLEEEEDPREELIGKLIEYRKYKDAAQELKEREEERQNAFTKPPSDLSEFAKESEAKDTNLHVTVYDMLGAFQKVLNRKKITKPAPSRITRQEIPIEDKMNEIMNHLRKTKKRTNFMTLFQHDQKEHLVVTFLAVLELMKSHQIMLEQEGNFEDIYIIGSETIHDA
|
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.
|
A8FEQ8
|
Subsets and Splits
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