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accession
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Full Name
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147
⌀
taxon
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46
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sequence
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2.75k
function
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5.51k
AlphaFoldDB
stringlengths
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10
A5DPE3
EF1A_PICGU
Elongation factor 1-alpha
Meyerozyma
MGKEKTHVNVVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAELGKGSFKYAWVLDKLKAERERGITIDIALWKFETPKYHVTVIDAPGHRDFIKNMITGTSQADCAILIIAGGTGEFEAGISKDGQTREHALLAYTLGVRQLIVAVNKMDSVKWDKNRFEEIIKETSNFVKKVGYNPKTVPFVPISGWNGDNMIEASTNCPWYKGWEKETKAGKSTGKTLLEAIDAIEPPQRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGIIKAGMVVTFAPAGVTTEVKSVEMHHEQLVEGVPGDNVGFNVKNVSVKEIRRGNVCGDSKNDPPKGCDSFTAQVIVLNHPGQISAGYSPVLDCHTAHIACKFDTLLEKIDRRTGKKMEDNPKFVKSGDASIVKMVPSKPMCVEAFTDYPPLGRFAVRDMRQTVAVGVIKSVEKSDKAGKVTKAAQKAAKK
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
A5DPE3
B8NM66
USTA_ASPFN
YAIG-XVI
Aspergillus subgen. Circumdati
MKLILTLLVSGLCALAAPAAKRDGVEDYAIGIDKRNSVEDYAIGIDKRNSVEDYAIGIDKRNSVEDYAIGIDKRNSVEDYAIGIDKRNTVEDYAIGIDKRNSVEDYAIGIDKRNTVEDYAIGIDKRNSVEDYAIGIDKRNSVEDYAIGIDKRGGSVEDYAIGIDKRNSVEDYAIGIDKRNSVEDYAIGIDKRGSVEDYAIGIDKKRGTVEDYAIGIDKRGGSVEDYAIGIDKRHGGH
Ribosomally synthesized cyclic peptide ustiloxin B precursor: Part of the gene cluster that mediates the biosynthesis of the secondary metabolite ustiloxin B, an antimitotic tetrapeptide . The ustA translated product contains a 16-fold repeated peptide embedding the tetrapeptide Tyr-Ala-Ile-Gly, that is converted into the cyclic moiety of ustiloxin B .
B8NM66
A4XLR9
RL24_CALS8
50S ribosomal protein L24
Caldicellulosiruptor
MPNKVHVKKGDTVVVISGKYKGKQGKVLTVLPKDKKVVVEGVNIVKKHVRPNPKMPQGGIITQEAPIWACKVMLVCPKCNKPTRIGHRFIQEGEEEKKVRTCKKCGEIID
One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.
A4XLR9
Q5Z620
CKX10_ORYSJ
Cytokinin oxidase 10
Oryza sativa
MMPRAQLTTFLIVTSFLSTVPYLRAPVHGGVLTSYDVSSLDIMSKIHTDHDATTKASSDFGHIVHATPNGVFRPTFPADIAALIRLSLSQPTPFTVAPRGKGHSSRGQAFAPGGIVVDMSALGDHGHHTSHRIDVSVDRMYVDAGGEQLWIDVLHTALKHGLTPRVWTDYLRITVGGTLSNAGIGGQAFRHGPQISNVHELDVVTGMGEMITCSPEVNSALFFAVLGGLGQFGVITRARIRLEPAPKRVKWVRIAYSDVHPFTTDQELLISKWASGSGFDYVEGQVQLNRTLTQGRRSSSFFSATDLARLTGLAIDTGSVAIYYIEGAMYYDDNTAASVDQKLDALLEELSFVRGFVFVRDASYVEFLDRVGREEQNLRSAGAWDVPHPWLNLFVPRSRILHFDAAVFKGILRNANPVGLILMYPMNKDMWDDRMTAMTPDEDVFYAVGLLRSAVAGGSGGDVEQLERENAAVLELCDLAGGGIGCRQYLPHHASRDGWRRHFGAKWGRVADLKARYDPRAILSPGQGIFPPPPPPSPPPPAAGEPITAS
Catalyzes the oxidation of cytokinins, a family of N(6)-substituted adenine derivatives that are plant hormones, where the substituent is an isopentenyl group.
Q5Z620
Q8CQD2
BUTA_STAES
Meso-2,3-butanediol dehydrogenase
Staphylococcus
MSKTAIITGAAGGLGKGIAERLANDGFNIVLQDINEALLLETEKEFKEKGYQAVAYKSDVSKKKEQEELVQFAVTEFGQLDVMVNNAGVDAVTPILEIGEEELSKLFNINVFGTLFGIQAAANQFIKQKSKGKIINACSIAGHESYEVLGTYSATKHSVRSFTQTAAKELADKGITVNAYCPGVAKTEMWDRIDEEMVKLDDSLEIGDAFEAFSSEIKLGRYQEPSDVANLVSFLASNDSDYITGQSILTDGGLVYR
Catalyzes the irreversible reduction of 2,3-butanediol to (S)-acetoin in the presence of NADH.
Q8CQD2
B2RV13
CF97D_HUMAN
CFAP97 domain-containing protein 1
Homo
MNNSLDYLAYPVIVSNHRQSTTFRKKLDFGHYVSHKNRIQIAKPTVDTKPPVAHTNHILKLSKLQGEQKKINKIEYENKQLCQKIANAHRGPAKVDCWNEYFSKSLNRETRNRELVRITMENQGILKRLVDRKPHYDRRASEIDWQNSRRYIRNTTRYLLSQNE
Required for male fertility through its role in axonemal doublet stabilization which is essential for sperm motility and fertilization.
B2RV13
A4JCN6
MOBA_BURVG
Molybdopterin-guanine dinucleotide synthase
Burkholderia cepacia complex
MPASVTPSITGLLLAGGRATRMDGADKGLQLLDGTPLALHVLRRLAGQVDEMVISANRNADRYAELGAPFGARVVPDETLDFAGPLAGLLAGMRAARAPLVVCAPCDTPSLPTDLVARLHAAFDAHRADIAMAVTVDAQHARSPQPTFALLRTSLADDLAAALAAGERKVRAWYARHKTVEVEFRDERAFYNANSWQELAALARR
Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
A4JCN6
Q9C8J7
TRO_ARATH
Protein ASH2 RELATIVE
Arabidopsis
MESLQSNSKIEEAEQNPKIEEAQVSVSLPEEPTGVLLPSELVDDSAPPESSDAVEESIETASEAEVSISLLEGTTTGTALLPSEENDLAPLESSGIIEEPIDTDLEKLDVVAMDVDQPGSDLKIESDSFSEEAPTTSSSDNPKSPKLDSVANQNGSAMEEDEGDEEQDDPPHKKLKQLDCLTSVAVKEEEEPEQVLPSEAMVVEEAATLVASAAKKSKSKKKNNNVWVTKSTRKGKKKSKANTPNPAAVEDKVLITPVPRFPDKGDDTPDLEICLSKVYKAEKVEISEDRLTAGSSKGYRMVRATRGVVEGAWYFEIKVLSLGETGHTRLGWSTDKGDLQAPVGYDGNSFGFRDIDGCKIHKALRETYAEEGYKEGDVIGFYINLPDGESFAPKPPHYVFYKGQRYICAPDAKEEPPKVVPGSEISFFKNGVCQGAAFTDIVGGRYYPAASMYTLPDQSNCLVKFNFGPSFEFFPEDFGGRATPRPMWEVPYHGFNGRLETNGSEDMKS
Trithorax-group gene homolog required for early embryogenesis . Required for the expression of FLC and FLC homologs and represses flowering . Required for proper leaf growth and development . Part of COMPASS-like complexes responsible for H3K4 trimethylation, but not for di- or mono-methylation of histone H3 'Lys-4' . Binds to target loci chromatin, increasing H3K4 trimethylation and causing activation of the gene . Involved in the transition from transcription initiation to transcription elongation .
Q9C8J7
Q2JT84
FOLD_SYNJA
Methenyltetrahydrofolate cyclohydrolase
unclassified Synechococcus
MSAKILDGKALAGRLQAEMAAQVQAWLPRVGRPPGLAVLRVGEDPASAAYVRGKERACERVGIASFGRHFSAQDSPAHLLDAIAQLNQDERVDGILVQLPLPPGWDPIPPLLAIDPAKDVDGLHPLNLGRLVRGEPGLRSCTPLGVMRLLQAEGIPIAGRKAVVVGRSLLVGKPLSLMLLAADATVTVAHSRTPNLAEVTRSADIVVMAVGRPRLLTADMVKPGAVVVDVGINRIQDPDGSEQLVGDVDYEAVKERAAAITPVPGGVGPMTVTMLLANTLESYKLRSHL
Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Q2JT84
P34721
MT1B_MORBO
Modification methylase MboIC
Moraxella
MRIKPYFESDDKNFNIYQGNCIDFMSHFQDNSIDMIFADPPYFLSNDGLTFKNSIIQSVNKGEWDKNDNEASIYNFNHEWIAQARQLLKDNGTIWISGTHHNIFTVGQVLKENNFKILNIITWEKPNPPPNFSCRYFTYSSEWIIWARKHSKIPHYFNYDLMKKLNGDKQQKDIWRLPAVGSWEKTQGKHPTQKPLGLLSRIILSSTQKDDLILDPFSGSGTTGIAGVLLDRNYIGIEQELEFLELSKRRYHEITPVLKNEFKQKIRKQISAI
A beta subtype methylase that recognizes the double-stranded sequence 5'-GATC-3', methylates A-2 on both strands, and protects the DNA from cleavage by the MboI endonuclease (Probable). This seems to be a weaker methylase than M1.MboI (Probable).
P34721
B4U194
CODY_STREM
GTP-sensing transcriptional pleiotropic repressor CodY
Streptococcus
MPNLLQKTRKITSILQRSVDSLETELPYNTMASRLADIIDCNACIINGGGSLLGYAMKYKTNTDRVEEFFETRQFPDAYVKAASRVYDTEANLSVENELTIFPVESKDIYPDGLTTIAPIYGGGMRLGTLIIWRNDNEFSDDDLVLVEISSTVVGIQLLNLQTENLEETIRKQTAVNMAINTLSYSEMKAVAAILSELDGNEGRLTASVIADRIGITRSVIVNALRKLESAGIIESRSLGMKGTYLKVINEGIFDKLKEF
DNA-binding protein that represses the expression of many genes that are induced as cells make the transition from rapid exponential growth to stationary phase. It is a GTP-binding protein that senses the intracellular GTP concentration as an indicator of nutritional limitations. At low GTP concentration it no longer binds GTP and stop to act as a transcriptional repressor.
B4U194
A6VHD2
RL3_METM7
50S ribosomal protein L3
Methanococcus
MGMKKSRPRRGSLAFSPRKRAKKLVPKIRSWPADKKVGLQAFPVYKAGTTHALLIENNPKSPNNGQEVFTPVTVLETPDVTVAGIRLYEKTTKGLKALTEVWAEQLDNDLGRKLTLVKKEEKKTADALDAVLEKATEVRVIVHTNPKTTGIPKKKPEVVEIRIGGSSVAERLAYAKEILGKTLAISDVFEAGEIIDTLAITKGKGFQGSVKRWGIKVQFGKHQRKGVGRHTGSIGPWRPRRVMWTVPLPGQMGFHQRTEYNKRILKLGSEGAEITPKGGFLNYGAVKNGYVVVKGTVQGPAKRLVVLRGSVRAAEDKFGLPEVAYISTESKQGN
One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.
A6VHD2
Q8KIX1
CH60_BUCTT
Chaperonin-60
Buchnera
MAAKEVKFGNDARAKMLRGVNVLADAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAREIELEDKFENMGTQMVKEVASKANDAAGDGTTTATVLAQSIITEGLKAVAAGMNPMDLKRGIDKAVIAAVEELRKLSVPCSDSKAIAQVGTISANSDLTVGKLIAEAMGKVGKEGVITVEEGTGLQDELDVVEGMQFDRGYLSPYFINKPESGAVELENPFILLADKKISNIRELLPILEAVAKAGKSLLIIAEDVEGEALATLIVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTGGTVISEEIGLELEKTILDDLGQAKRVVINKDTTIIIDGIGNEINIKGRIAQIHQQIEEATSDYVKEKLQERVAKLADGVAVIKVGAATEVELKEKKGRVEDALHATRAAVEEGVVAGGGVALIRVAGKISNLTGDNEDQNVGIKVALRAMESPLRQIVINAGEEASVIANNVKACEGSYGYNAYTEEYGDMISMGILDPTKVTRSALQYAASVAGLMITTECMITDLPKGETPDLNNSGGMGGGMGGGMGGMGGMM
Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.
Q8KIX1
A5F6Z2
FADR_VIBC3
Fatty acid metabolism regulator protein
Vibrio
MVIKAKSPAGFAEKYIIESIWNGRFPPGSILPAERELSELIGVTRTTLREVLQRLARDGWLTIQHGKPTKVNQFMETSGLHILDTLMTLDAENATSIVEDLLAARTNISPIFMRYAFKLNKESAERIMINVIESCEALVNAPSWDAFIAASPYAEKIQQHVKEDSEKDELKRQEILIAKTFNFYDYMLFQRLAFHSGNQIYGLIFNGLKKLYDRVGSYYFSNPQARELAMEFYRQLLAVCQSGEREHLPQVIRQYGIASGHIWNQMKMTLPSNFTEDDC
Multifunctional regulator of fatty acid metabolism.
A5F6Z2
Q96VT7
DAPB_ASPNG
Dipeptidyl-aminopeptidase B
Aspergillus subgen. Circumdati
MSSPRPSTSSTSSDSGLSVDTTAYPEESKYTSTAPGAGGLSDENRYRDVEEGEAGADEPFLPSAKKQAASGSRTSRLIWGLVILCVAGWLWGLVLFVTQNRSAQQSVSEALQSHESGAISGSSSSGKPVTLEQVLTGQWLPRSHAVSWIAGPNGEDGLLVEQGEDQGKGYLRVDDIRSRKGDATSQESRVLMEKAIVQVDGRTIFPVSTWPSPNLNKVLLLSEREKNWRHSFTGKYWIFDVATQTAQPLDPSNPDGRVQLAIWSPTSDMVAFVRDNNLYLRRLSSKEVVPITKDGGADLFYGIPDWVYEEEVFSGNSVTWWSGDGKYVAFLRTNETAVPEFPVQYYLSRPSGKRPPPGLEDYPEVREIKYPKAGAPNPVVSLQFYDVEKQEVFSIEAPDDFEDDDRIVIEIVWGTEGKILVRATNRESDVLKVFLFDTKARTSKLVRTENVADIDGGWVEPTQYTWFIPADPSNGRPHDGYLDTVIHEGYEHLGYFTPLDNSEPILLTQGEWEVVDAPTAVDLRKGIVYFISTKESPTERHLYQVNLDGSNLKPLTDTSKPGYYDVSFSHGTGYALLSYRGPSIPWQAIVNTETDELKYEETIEDNAGLARMVDSYALPTEIYQNVTIDGFTLQVVERRPPHFNPAKKYPVLFYLYNGPRSQTVDRKFSIDFQSYVASSLGYIVVTVDGRGTGFSGRKTRCIVRGNLGYYEAYDQITTANLWGEKPYVDETRMSIWGWSYGGFMTLKTLEQDAGQTFQYGMAVAPVTDWRHYDSIYTERYMHTPAHNPNGYDNTSITDMTALQQTVRFLVIHGASDDNVHIQNTLVLVDKLDLAGVQNYDLHFYPDSDHSINFHNAHRMVYERLSSWLVNAFNDEWHRIADPVPDDSMWEKVKRSLPMLVN
Type IV dipeptidyl-peptidase which removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline.
Q96VT7
B0T734
RPIA_CAUSK
Phosphoriboisomerase A
unclassified Caulobacter
MSADDQKRISGEAAAELVEAGMVVGLGTGSTAAWFVKALAARKLDIRGVPTSEATANLARELGIALTALDDVKSIDLTVDGADEIGPGLSLIKGGGAALLREKLVWEASKRCVVIADAAKHVKTLGKFPLPIEVVRFGHVHTGQRLADIAAEFDLLPPRLRMADRGVVVTDGGNVIYDMPSGVIAEPAALAAALKTVTGVVDHGLFLDLADEALLGTDQGVVKLVP
Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
B0T734
Q2LWU6
IF2_SYNAS
Translation initiation factor IF-2
Syntrophus
MSKKRVYELARELGIDNKELISRLEKLGIAVKSHSGTLEDSEVDRVTKEFHARGSREMVEQRIKTTVIRRRAVRVPEKEAVLEKVPVEMEKEMGKALPEEVPEKIAPSRETPPAKVVKPRPVVPEKKIPAAGEKPLAPPEKPAEPVAPPIAEILKQEKIQPPEKFAEEPLKKPAVIEPEKAAAAPKAVPGEAKPLPRTERVQEQGKPVPGRKEGRTPVSRRPAETRFPAKPAPQPEMARKQVVAAAPGRAVPQEKGAPKTEAEKPRKKIKLPDETRKGEQIPARKKTVLKKGPEKTDFRGTLEEEIIERAVRPPRWKEEKKAAPVKMKKTEITVPKAIKRRIRVGEAITVGDLAKKMGVKAGEVINKLMRMGLMATINQSIDFDAASLIATEFEYQVEPAGMEYDESMFKVESSVENLKPRAPVVTIMGHVDHGKTSLLDAIRKTRVTEGEAGGITQAIGAYRVNLKGREIVFLDTPGHEAFTAMRARGAQVTDIVVLVVAADDGVMDQTVEAINHSKIAGVPIIVAINKIDKPEADPGRIKQALTEYELVPEEWGGDTIFSEVSAKQKIGIEELLELILLQADVLELKADPDRPARGVVIEARLDRGRGPVATVLIQEGTLHEGDAFVSKTEYGRVRAMNDDQGRRIKEAGPATPVEVIGFSRVPQASAEFNAVEDEKKARSIGDYWMRKEREKELSATSKITLEQLYEKMKEGVKELNVILRADVQGSLEALSDALTKLSTDDIKLKVIHGSTGAITETDVMLASASNAIIIGFNVRPDARVAEIAEAEGVDIKLYDIIYNVIADVRAAMEGLLEPEYREVVLGRAEVRDLFRVPKVGTVAGSFVIDGKVTRKANVKLVRDGVVVFDGKIGSLKRFKDDVKEVLSGFECGIGIEGFNDLRMGDMIEAYINEKVERKL
One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex.
Q2LWU6
Q9H1E3
NUCKS_HUMAN
P1
Homo
MSRPVRNRKVVDYSQFQESDDADEDYGRDSGPPTKKIRSSPREAKNKRRSGKNSQEDSEDSEDKDVKTKKDDSHSAEDSEDEKEDHKNVRQQRQAASKAASKQREMLMEDVGSEEEQEEEDEAPFQEKDSGSDEDFLMEDDDDSDYGSSKKKNKKMVKKSKPERKEKKMPKPRLKATVTPSPVKGKGKVGRPTASKASKEKTPSPKEEDEEPESPPEKKTSTSPPPEKSGDEGSEDEAPSGED
Chromatin-associated protein involved in DNA repair by promoting homologous recombination (HR) . Binds double-stranded DNA (dsDNA) and secondary DNA structures, such as D-loop structures, but with less affinity than RAD51AP1 .
Q9H1E3
Q5PCV8
PDXB_SALPA
Erythronate-4-phosphate dehydrogenase
Salmonella
MKILVDENMPYARELFSRLGEVKAVPGRPIPVEELNHADALMVRSVTKVNESLLSGTPINFVGTATAGTDHVDEAWLKQAGIGFSAAPGCNAIAVVEYVFSALLMLAERDGFSLRDRTIGIVGVGNVGSRLQTRLEALGIRTLLCDPPRAARGDEGDFRTLDELVQEADVLTFHTPLYKDGPYKTLHLADETLIRRLKPGVILINACRGPVVDNAALLARLNAGQPLSVVLDVWEGEPDLNVALLEAVDIGTSHIAGYTLEGKARGTTQVFEAYSAFIGREQRVALETLLPAPEFDRITLHGPLDQPTLKRLAHLVYDVRRDDAPLRKVAGIPGEFDKLRKNYLERREWSSLYVMCDDETAAALLCKLGFNAVHHPAH
Catalyzes the oxidation of erythronate-4-phosphate to 3-hydroxy-2-oxo-4-phosphonooxybutanoate.
Q5PCV8
Q9NFL4
HCYG_APHSP
Hemocyanin G chain
unclassified Aphonopelma
MASIPEKQALILPLFEKLTSLTKETPPRAQWDPRLAGVGVLPRGTLFSCFHEKHLLEATKLFKVLYSPESFNDFLQLAREARVVVNEGLFAYAFSVAVIHRDDCKGVTLPPIQEVFPDRFVPSETINLAMKEAKNDPNSDIVVDVQETGNILDPEYKLAYFREDIGANAHHWYWHVVYPANWDAVFTGKTKDRKGELFYYMHQQMCARYDCERLSNGLTRMIPFHNFKEKLEGYAPHLTSLVSGLHYASRPAGLCLRDLSELEVQDVERWRDRILDAYHLNHVHDRENNDVVLDAEHGADILGAIIESSSDSVNRRFYGSLHNWGHVMMARMTDPDRSFEENPGVMSDTSTSLRDPIFYRWHRFVDNIFQEYKATLPSYTADDLNFPGLRIVSVQVNAKSQNRVRTFLKQEELVLSHGINFGTEHTVKVHYNHLDHEPFSYTINVDNSSGAVKHATVRIFLGPKCDELGNILEPNEQRRLFIELDKFHKELGPGLNTINRNSVESNVTVAHTYTFDELREGKLAPEDATEYCNCGWPRHMLIPKGTHRGMEFQLFVMLTDYTVDNPCGGAGKIVCADAVSYCGAKDQKYPDTKPMGFPFDRPTKIHTAEEILTPNMSLTDVVIQYVGHE
Hemocyanins are copper-containing oxygen carriers occurring freely dissolved in the hemolymph of many mollusks and arthropods.
Q9NFL4
Q0A4M2
ATP6_ALKEH
F-ATPase subunit 6
Alkalilimnicola
MSGNTALDYIQHHLTNLAVGEGYWTFHVDSLIMSFSLGALFCYLFWLGARRATAGVPSGLQNFVELMVEFVDQTTRETFQGKSRLIAPLALTIFCWIFLMNLMDLVPIDMVPSLMYAAGVDYFKILPTVDLNVTFALSISVFFLIIAYSFKGKGAGGFAKELLFHPFGPWLLPFNLILNIIELIAKPISLSLRLFGNMYAAELIFILISLLPWWIQWALGTPWAIFHILVIPLQAFIFMMLTVVYLSMANEHEEH
Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
Q0A4M2
B3EIU4
MIAA_CHLL2
Isopentenyl-diphosphate:tRNA isopentenyltransferase
Chlorobium
MTSGERQKPVLVILGPTASGKSALAMNIAGNLDAEIISADSRQIYRELTIGSAKPSEDDLRMVRHHFINEKTIGEPFTAGDFAEAAYARILDIHNRNKYAVVVGGSTLYLEGLLKGFGDLPPGDQEIRSRLTAELALAGGEKLFERLRKLDPIQAATLDPTKTRRLIRSLEIIEITGKTVTSLQEYRRIPALDYRIVGLSIARPILYGRIDTRVDEMIASGLVEEAEYLYKKHYSLLRTERNSALKTVGYQELFDFFEKKTDFDRAVTLIKQHTRNYAKRQLTFFKNRLNVTWMDAFGEHAAPDILRAACCRELAE
Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
B3EIU4
A4QQN1
M2DH_MAGO7
Mannitol 2-dehydrogenase
Pyricularia
MAFKLSTKHLADIGAQTEKSIRIPSYDRNDVKEGIVHVGVGGFHRAHLAVYVDKLMQSHGVRDYAICGVGLQPADASMRDVLASQDHMYTVIERSAAGSTAHVVGSIRNFLFAPDDREAVIAKMAHPDTHIVSLTITESGYYYNENTHELQSEHPDIQHDLDPANAAKPKTTFGFLYAAMVRRREQGLKPFTVLSCDNMLKNGSITRNMLQSFAKLKDPSMADWIAQYGGFPNAMVDRITPRTSDPDIKELADKFKIDDAWPVVTEPFMQWVVEDKFADGRPPFDLVGVQVVKDVKDVEQFEKHKLRLLNASHSAMGYPGQLAGFKYVHEVMEHPLYRKFIWQMMQEEVKPLLPEIPGVDIDAYCNTLMERFSNPTIMDQLPRIALNSSGKMPQFVMPSIAEAIWVTGPFRRLVFVAACWFRYVLGVDDKGNKFEVDDPMREELQSKAQAGGTKPHEILSIKSLFGDDLRGDERFLKEVTQAMEDIARDGVMATMPKFVNDA
Catalyzes the NAD(H)-dependent interconversion of D-fructose and D-mannitol in the mannitol metabolic pathway.
A4QQN1
Q3J8T7
RS4_NITOC
30S ribosomal protein S4
Nitrosococcus
MAKYTGPKLKQARREGTDLFLKSGVRPIDSKCKIEQVPGQHGAGARRARMSDYALQLREKQKLRRMYGVLERQFRRYYKEAARRKGSTGENLLKLLESRLDNVVYRMGFGSTRAEARQLINHKGVLVNGQGINIPSYQVRAEDVVAVREKAKRQDRIKFALELAQARAEAEWIEINAGKLEGVFKRVPERSELAPDIQENLVVELYSK
With S5 and S12 plays an important role in translational accuracy.
Q3J8T7
A9WNC6
ATPA_RENSM
F-ATPase subunit alpha
Renibacterium
MAELTINADDVRNALNEFAASYEPGNAERVEVGRVTTASDGIARVEGLPSVMANELLRFEDGTLGLAQNLDVREIGVIILGDFTGIEEGQEVHRTGEILSVPVGDQFLGRVVDPLGVPIDGLGEIQAETTRALELQAPGVTQRQSVKEPMQTGLKAIDAMIPIGRGQRQLIIGDRKTGKTAIAVDTILNQQANWASGDVKKQVRCIYVAIGQKASTIAEVRQTLEDNGALEYTTIVASPASDPAGFKYLAPYAGSAIGQHWMYSGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLERCAKLSDELGAGSMTGLPIIETKANDVGAFIPTNVVSITDGQIFLQSDLFNANQRPAVDVGISVSRVGGSAQVKSMKTVSGTLKLDLAQYRDMQAFAMFASDLDAASRQQLTRGSRLMELLKQPQYTPYPVEDQVVSIWAGTHGYLDEVPVEDILRFEREFLEHLRHSTEILTTLAQTNKLEDSTVEALKTSIVDFKKGFFGDGANHLVGAGHEEFDSLSEADVDQEKIVKQKR
Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
A9WNC6
Q6F8I7
PTH_ACIAD
Peptidyl-tRNA hydrolase
Acinetobacter
MSKISLIVGLGNPGAEYAQTRHNAGFWFVEQLADRYNITLKKDPKFHGFSGRGQIEGHDVRLLIPTTFMNRSGQSVVPFSKFYQISPEAILIAHDELDMDPGVIRLKTGGGHGGHNGLRDIVPHIGANFHRLRIGIGHPGSKDRVSGHVLGKAPQNEQTLMEDAIHHALSNTRLLVDGQIAQAMNQINAYKPK
The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Q6F8I7
Q9H8L6
MMRN2_HUMAN
EndoGlyx-1 p125/p140 subunit
Homo
MILSLLFSLGGPLGWGLLGAWAQASSTSLSDLQSSRTPGVWKAEAEDTGKDPVGRNWCPYPMSKLVTLLALCKTEKFLIHSQQPCPQGAPDCQKVKVMYRMAHKPVYQVKQKVLTSLAWRCCPGYTGPNCEHHDSMAIPEPADPGDSHQEPQDGPVSFKPGHLAAVINEVEVQQEQQEHLLGDLQNDVHRVADSLPGLWKALPGNLTAAVMEANQTGHEFPDRSLEQVLLPHVDTFLQVHFSPIWRSFNQSLHSLTQAIRNLSLDVEANRQAISRVQDSAVARADFQELGAKFEAKVQENTQRVGQLRQDVEDRLHAQHFTLHRSISELQADVDTKLKRLHKAQEAPGTNGSLVLATPGAGARPEPDSLQARLGQLQRNLSELHMTTARREEELQYTLEDMRATLTRHVDEIKELYSESDETFDQISKVERQVEELQVNHTALRELRVILMEKSLIMEENKEEVERQLLELNLTLQHLQGGHADLIKYVKDCNCQKLYLDLDVIREGQRDATRALEETQVSLDERRQLDGSSLQALQNAVDAVSLAVDAHKAEGERARAATSRLRSQVQALDDEVGALKAAAAEARHEVRQLHSAFAALLEDALRHEAVLAALFGEEVLEEMSEQTPGPLPLSYEQIRVALQDAASGLQEQALGWDELAARVTALEQASEPPRPAEHLEPSHDAGREEAATTALAGLARELQSLSNDVKNVGRCCEAEAGAGAASLNASLHGLHNALFATQRSLEQHQRLFHSLFGNFQGLMEANVSLDLGKLQTMLSRKGKKQQKDLEAPRKRDKKEAEPLVDIRVTGPVPGALGAALWEAGSPVAFYASFSEGTAALQTVKFNTTYINIGSSYFPEHGYFRAPERGVYLFAVSVEFGPGPGTGQLVFGGHHRTPVCTTGQGSGSTATVFAMAELQKGERVWFELTQGSITKRSLSGTAFGGFLMFKT
Inhibits endothelial cells motility and acts as a negative regulator of angiogenesis; it down-regulates KDR activation by binding VEGFA.
Q9H8L6
A9M5C1
CLPX_BRUC2
ATP-dependent Clp protease ATP-binding subunit ClpX
Brucella
MSKVSNGGGDSKNTLYCSFCGKSQHEVRKLIAGPTVFICDECVELCMDIIREENKSSMVKSREGVPTPQEIMAVLDDYVIGQKDAKRVLSVAVHNHYKRLAHQSKNSDIELAKSNILLVGPTGCGKTYLAQTLARIIDVPFIMADATTLTEAGYVGEDVENIILKLLQAADYNVERAQRGIVYIDEVDKISRKSDNPSITRDVSGEGVQQALLKIMEGTVASVPPQGGRKHPQQEFLQVDTTNILFICGGAFASLDRIISARGEKTSIGFGATVKSVDERRIGEVFKELEPEDLLKFGLIPEFVGRLPVIATLEDLDVDALVQILTEPKNALVKQYQRLFDMENVELVFHDDALRAIANKVVEHKTGARGLRSIMEKILLDTMFELPTLEGVREVVISGDVVDGSARPLYIYAERQDEKGNVSA
ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.
A9M5C1
A7FKS8
SSRP_YERP3
Small protein B
Yersinia
MTKKKAYKPGSATIAQNKRARHEYFIEEEFEAGLALQGWEVKSLRAGKANISDSYVMFKNGEAFLFGATITPLNVASTHVVCEPMRTRKLLLNKRELDSLFGRVNREGYTVVALSMYWKNAWVKVKIGVAKGKKDNDKRDDIRDREWKLDKARIMKHANR
Required for rescue of stalled ribosomes mediated by trans-translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to translate the ORF on the tmRNA; the nascent peptide is terminated with the 'tag peptide' encoded by the tmRNA and targeted for degradation. The ribosome is freed to recommence translation, which seems to be the essential function of trans-translation.
A7FKS8
Q5N7W3
RPN2_ORYSJ
Ribophorin-2
Oryza sativa
MAAAGGLPASATLLLLVIAAVAVAPLASAVRPVSDAHRSAAAELFAASPDGSFGDLETTYEAVRTFQILGVEKDKGLIGKACKFAAEKLASSSSSPAKDLFHAARISGVLKCSVDSGVYDDVATRLKAVIKDTNSLLELYYSVGGLLSIKEQGHNVVLPDADNTFHAIKALSQSDGRWRYDTNSAESSTFAAGIALEALSAVISLADSEVDSSMIAVVKNDIVKLFDTIKSYDDGTFYFDEKHVDAAEYKGPITTSASVVRGVTSFAAVASGKLNIPGEKILGLAKFFLGIGLPGSAKDCFNQIESLSFLENNRVFVPLVLSLPSKVFSLTSKDQLKVEVTTVFGSAAPPLRVNLVQVLGSDSKVITTETKELQFDLDNNVHYLDIAPLKIDVGKYSLVFEISLQEQEHETIYATGGTNTEAIFVTGLIKVDKAEIGISDNDAGTVESVQKIDLQKDTSVSLSANHLQKLRLSFQLSTPLGKTFKPHQVFLKLKHDESKVEHLFVVPGSARQFKIVLDFLGLVEKFYYLSGRYDLELAVGDAAMENSFLRALGHIELDLPEAPEKAPKPPAQAVDPFSKFGPKKEISHIFRSPEKRPPKELSFAFTGLTLLPIVGFLIGLMRLGVNLKNFPSLPAPAAFASLFHAGIGAVLLLYVLFWIKLDLFTTLKYLSFLGVFLVFVGHRALSYLSSTSAKQKTA
Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Q5N7W3
Q2G8X0
RL14_NOVAD
50S ribosomal protein L14
Novosphingobium
MIQMQSNLDVADNSGAKRVQCIKVLGGSKRRFAGVGDIIVVSVKEAQPRARVKKGDVHRAVIVRTKKDVRRTDGSVIRFDSNAAVLVGKNEEPIGTRIFGPVVRELRGKGFMKIISLAPEVL
Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome.
Q2G8X0
Q92765
SFRP3_HUMAN
FrzB-1
Homo
MVCGSPGGMLLLRAGLLALAALCLLRVPGARAAACEPVRIPLCKSLPWNMTKMPNHLHHSTQANAILAIEQFEGLLGTHCSPDLLFFLCAMYAPICTIDFQHEPIKPCKSVCERARQGCEPILIKYRHSWPENLACEELPVYDRGVCISPEAIVTADGADFPMDSSNGNCRGASSERCKCKPIRATQKTYFRNNYNYVIRAKVKEIKTKCHDVTAVVEVKEILKSSLVNIPRDTVNLYTSSGCLCPPLNVNEEYIIMGYEDEERSRLLLVEGSIAEKWKDRLGKKVKRWDMKLRHLGLSKSDSSNSDSTQSQKSGRNSNPRQARN
Soluble frizzled-related proteins (sFRPS) function as modulators of Wnt signaling through direct interaction with Wnts. They have a role in regulating cell growth and differentiation in specific cell types. SFRP3/FRZB appears to be involved in limb skeletogenesis. Antagonist of Wnt8 signaling. Regulates chondrocyte maturation and long bone development.
Q92765
Q8CWW3
RUVA_STRMU
Holliday junction ATP-dependent DNA helicase RuvA
Streptococcus
MYDYIKGNLTKITAKYIVLETGGLGYVINVANPYSFSNQINQAIQIYIHHVVREDAHLLYGFHTEDEKAVFLNLISVSGIGPTSALAIIAADDNEGLVKAIDHSDVNYLMKFPKIGKKTAQQMVLDLAGKFVDINEVSTDKSKVSTINNNQELEEAVEALLALGYKTNELKKIEKFFEGTTDTAENYIKSALKMLMK
The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB.
Q8CWW3
C4ZBF3
RBFA_AGARV
Ribosome-binding factor A
Lachnospiraceae incertae sedis
MRKNSIKNIRINEEVMRELSNIIRGEIKDPRINPMTSVVAVEVAPDLKTAKAYISVLGDKKSQADTLAGLKSAEGYIRRTLAKNINLRNTPAITFIIDQSIEYGVEMSKKIDEVTKNLKED
One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Associates with free 30S ribosomal subunits (but not with 30S subunits that are part of 70S ribosomes or polysomes). Required for efficient processing of 16S rRNA. May interact with the 5'-terminal helix region of 16S rRNA.
C4ZBF3
Q9XQN8
RPOA_SINAL
Plastid-encoded RNA polymerase subunit alpha
Sinapis
MVREKVKVSTRTLQWKCVESRRDSKRLYYGRFILSPLMKGQADTIGIAMARALLGEIEGTCITRAKSENIPHDYSNIVGIQESVHEILMNLNEIVLKSNLYGTRNPFICVQGPGYITARDIILPPSVEIVDNTQHIATLTEPINLCIGLKIERNRGYSLKMSNNFEDRSYPIDAVFMPVQNANHSIHSYGNGNEKQEILFIEIWTNGSLTPKEALYEASRNLINLFIPFLHVEEETFYLENNQHQVTLPVFPFHNKLVNLRQKKKELAFQYIFIDQLELPPRIYNCLKKSNIHTLLDLLNNSQEDLIKMEHFHIEDVKKLLDILEKK
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Q9XQN8
Q1CTU9
FOLD_HELPH
Methenyltetrahydrofolate cyclohydrolase
Helicobacter
MPNRGVVLLDGQALAYDIEKDLKNKIQTITAQTHKRPKLAVILVGKDPASITYVNMKIKACQRVGMDFDLKTLQEDITEAKLLSLIKDYNTDQNISGVLVQLPLPRHIDSKMVLEAIDPSKDVDGFHPLNIGKLCTQKESFLPATPMGVMRLLKHYHIEIKGKDVAIIGASNIIGKPLSMLMLNAGASVSVCHILTKDISFYTQNADIVCVGVGKPDLIKASMLKKGAVVVDIGINHLNDGRIVGDVDFNNAQKVAGFITPVPKGVGPMTIVSLLENTLIAFEKQQRKGF
Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Q1CTU9
Q3ZCC9
SEC13_BOVIN
SEC13-like protein 1
Bos
MVSVINTVDTSHEDMIHDAQMDYYGTRLATCSSDRSVKIFDVRNGGQILVADLRGHEGPVWQVAWAHPMYGNILASCSYDRKVIIWKEENGTWEKTHEHTGHDSSVNSVCWAPHDYGLILACGSSDGAISLLTYTGLGQWEVKKINNAHTIGCNAVSWAPAVVPGSLIDQPSGQKPNYIKKFASGGCDNLIKLWKEEEDGQWKEEQKLEAHSDWVRDVAWAPSIGLPTSTIASCSQDGRVFVWTCDDASGNTWSPKLLHKFNDVVWHVSWSITANILAVSGGDNKVTLWKESVDGQWVCISDVNKGQGPVSTSVTEGQQNDQ
As a component of the GATOR subcomplex GATOR2, functions within the amino acid-sensing branch of the TORC1 signaling pathway. Indirectly activates mTORC1 and the TORC1 signaling pathway through the inhibition of the GATOR1 subcomplex. It is negatively regulated by the upstream amino acid sensors SESN2 and CASTOR1.
Q3ZCC9
P83187
BRB_BASAL
Beta-basrubin
Basella
KIMAKPSKFYEQLRGR
Possesses antifungal activity against B.cinerea, M.arachidicola and F.oxysporum but not C.comatus and R.solani. Inhibits HIV-1 reverse transcriptase and cell-free translation.
P83187
Q3JNX1
UBIA_BURP1
4-HB polyprenyltransferase
pseudomallei group
MLARFPLYLRLIRMDKPIGSLLLLWPTLNALWIASDGHPAPSLVVIFALGTLLMRSAGCAINDYADRDFDRHVKRTAERPLTSGKIRAWEAIAIAVGLALVSFLLILPLNGLTKELSVVAVFVAATYPFMKRFFAIPQAYLGIAFGFGIPMAFAAVQDTVPMIAWAMLAANVFWSVAYDTAYAMVDRDDDLKIGMRTSAITFGRHDVLAIMLCYAAMLGIYVWLGAALHFGWPYWAGWAAAAGCSIYHYTLIKDRERMACFAAFRHNNWLGGVLFAGIAAHYALAVR
Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 3-octaprenyl-4-hydroxybenzoate.
Q3JNX1
Q0TE01
MUTH_ECOL5
Methyl-directed mismatch repair protein
Escherichia
MSQPRPLLSPPETEEQLLAQAQQLSGYTLGELAALAGLVTPENLKRDKGWIGVLLEIWLGASAGSKPEQDFAALGVELKTIPVDSLGRPLETTFVCVAPLTGNSGVTWETSHVRRKLKRVLWIPVEGERSIPLAKRRVGSPLLWSPNEEEDRQLREDWEELMDMIVLGQIERITARHGEYLQIRPKAANAKALTEAIGARGERILTLPRGFYLKKNFTSALLARHFLIQ
Sequence-specific endonuclease that cleaves unmethylated GATC sequences. It is involved in DNA mismatch repair.
Q0TE01
B3QL62
ATPG_CHLP8
F-ATPase gamma subunit
Chlorobaculum
MPTLKDIRIRLKGIKSTQQVTKAMKMVAAAKLRRAQDRAIQARPYAGKLKEMLASLSTKVDTSLNPLLSPREEVNKVLVVLVTSDRGLCGGFNANIMKLAQRVIHEDYAAQHAKGAVTMICAGTKGSDFFRKRGYNVTKAYPGVFQNLDFSSAKEIAELASQMYLKGEADKVILVYNEFKSVLAPNLRTEQLLPIAPEEGTEEAAGSEYLYEPSPEAIIDELVPKHLNTQVWRVMLESNAAEQAARMAAMDSATENAKELIRVLNISYNRARQAAITKELSEIVAGADALKQ
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.
B3QL62
Q6BPL7
ASA1_DEBHA
ASTRA-associated protein 1
Debaryomyces
MKPIELCTLRGHLNDITCTEPYYIGGKVSLVSADSNGWIIWWDINTRRPNCVWKGHDSNIVTLRQICNGLLLTHSKDSDIKIWDVENFKSGSREMPAEKYNNVQYFSIDRDGEEDNNVSKNELLEAFPLPENVVIPVNALNYCNVDYSNHHLITPATTDSNNFDLYSIFKPSHQTDESLEAKLNLKRVAANIDPWKLYKKTITQLNKEQGVEFEIGNENDILKRDKFGIMMKVLFVRDDLFYIGYESGHLIGYHIDFSGAINNENEGAKSDSVKPDKNVSGLAGLFGNKTKSFDKTIINKDPHIKMIYMNDSCSPYPIISLVYDNKENKIICGSAGKQLTFHKIPEEFSQFNDISDCKRYNLRHSGIQSVSINNSLLVVGFWDGLIKGYDLDLNELFKYCKRLPRIDVLESNSGQQQPREKQNSIKLCTVKLVIPNETDVVKSNDYKSLIKHKRDITTTNLLISSYYDGTITIFKV
Component of the ASTRA complex involved in chromatin remodeling.
Q6BPL7
Q6G2Z4
SYA_BARHE
Alanyl-tRNA synthetase
Bartonella
MNSVNSIRSTFLDYFQLNGHKIVSSSPLVPRNDPTLMFTNAGMVQFKNVFTGLEQRPYKQATTAQKCVRAGGKHNDLDNVGYTARHHTFFEMLGNFSFGDYFKEEAIFLSWNLLTKEFCLPEDKLLVTVYHNDDVSTELWRKISGLPDEKIVRIATADNFWAMGDTGPCGPCSEIFYDHGDEIWGGPPGSAYEDGDRFIEIWNLVFMQYEQVNKEKRVELPHPSIDTGMGLERIAAVLQGGHDNYDIDLFRALIAVSQEITGVKATGDFIASHRVIADHLRSSAFLIADGVLPSNEGRGYVLRRIMRRAMRHAHLLGAKEPLMWRLLPVLIHEMGQAYPELVRAESLISETLKLEEIRFRKTLERGLGLLSEASTDLKEGDHLNGEIAFKLYDTYGFPLDLTQDALRCRGISVDVAAFNKAMEGQKAKARANWSGSGETVTEAIWFSVRDQLGATEFLGYETEKSEGILTALVRDGEIVDDISSGQKAILVVNQTPFYGESGGQIGDSGTISGKNFVFEVHDTQKKADGVFIHIGEVKSGQARMSECVELTVDGVRRKKIRVNHSATHLLHEALRQVLGSHVTQKGSLVSPDRLRFDFSHPKSVSLEELEKIEDLANEIVLQNSEVTTRLMLVDDAISEGAMALFGEKYGDEVRVVSMGNRLEKGKLKSRWSIELCGGTHVERTGDIGLIHIVSESSVAAGVRRIEALTGTAARLYLSRQDARVHEIADLLKTSATDVEERVRILLEDRRKLEKELNDERKKSVLSGGIVKSDQEDITIINGISFMGRVVKNISPRDLKTLVDSGKKKIGSGVVAFIGVSEDGKGSAVLGVTDDLTHKLNAVDLVRILSGILGGQGGGGRPDMAQSGGPKGNKADEALAVLKASLEG
Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
Q6G2Z4
P95276
EPHB_MYCTO
Epoxide hydrolase B
Mycobacterium tuberculosis complex
MSQVHRILNCRGTRIHAVADSPPDQQGPLVVLLHGFPESWYSWRHQIPALAGAGYRVVAIDQRGYGRSSKYRVQKAYRIKELVGDVVGVLDSYGAEQAFVVGHDWGAPVAWTFAWLHPDRCAGVVGISVPFAGRGVIGLPGSPFGERRPSDYHLELAGPGRVWYQDYFAVQDGIITEIEEDLRGWLLGLTYTVSGEGMMAATKAAVDAGVDLESMDPIDVIRAGPLCMAEGARLKDAFVYPETMPAWFTEADLDFYTGEFERSGFGGPLSFYHNIDNDWHDLADQQGKPLTPPALFIGGQYDVGTIWGAQAIERAHEVMPNYRGTHMIADVGHWIQQEAPEETNRLLLDFLGGLRP
Could be involved in detoxification of extraneous host-cell epoxides. Catalyzes the hydrolysis of small aromatic epoxide-containing substrates such as trans-1,3-diphenylpropene oxide, trans and cis-stilbene oxide, and terpenoid epoxide.
P95276
Q3MAB1
PSBA2_TRIV2
Photosystem II Q(B) protein 2
Trichormus
MTATLQQRKSANVWEQFCEWITSTNNRLYIGWFGVLMIPTLLAATTCFIIAFIAAPPVDIDGIREPVAGSLIYGNNIISGAVVPSSNAIGLHFYPIWEAASLDEWLYNGGPYQLVIFHFLTGVFCYLGREWELSYRLGMRPWICLAFSAPVAAATAVFLIYPIGQGSFSDGMPLGISGTFNFMIVFQAEHNILMHPFHMLGVAGVFGGSLFSAMHGSLVTSSLVRETTENESQNYGYKFGQEEETYNIVAAHGYFGRLIFQYASFNNSRQLHFFLAAWPVIGIWFTALGVSTMAFNLNGFNFNQSIIDSQGRVINTWADIINRANLGMEVMHERNAHNFPLDLAAGEVAPVALTAPAING
Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbA) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors.
Q3MAB1
C5BNN0
PROA_TERTT
Glutamyl-gamma-semialdehyde dehydrogenase
Teredinibacter
MTVKDYMQQLGRQARAASRDMLAASTDDKNRALVAIADAITANRELIIQENARDLENGRANGLEPAMLDRLELTPARFDGMIEGLRQVAALPDPCGEISDLKYRPSGIQVGKMRVPLGVVGIIYESRPNVTIDAASLCLKSGNATILRGGSEAIHSNQAIAKCIAAGLESVGLPASAVQVVETTDRAAVGELITMAEYVDVIVPRGGRSLIERISNDAKVSVIKHLDGICHVFIDDDADLDKAFNIALNSKTHRYGVCNAMETLLVASSVAEKILPRLATAYAEKSVELRGCDRTLAILPNINAAKPEDWDTEYLAPILAIRVVDDMTAAMDHIAAHSSAHTESIVTENYTKARKFMALVDSASVMVNASTRFADGFQYGLGAEIGISTDKIHARGPVGLEGLTSQKWIVFGDGEILN
Catalyzes the NADPH-dependent reduction of L-glutamate 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate.
C5BNN0
A5GRD7
PNP_SYNR3
Polynucleotide phosphorylase
unclassified Synechococcus
MQGETRSISFDGREIRLTTRRYAPQAGGSVLIECGDTAVLVTATRANGREGIDFLPLTCDYEERLYAAGRIPGSFMRRESRPPERATLACRLIDRPIRPLFPSWMRDDLQIVATVMSVDERVPPDVLAVTGASLATLLAKIPFYGPMAAVRVGLLGDDFILNPSYREIERSELDLVVAGTAEGVVMVEAGAQQLPEEDMIEAIDFGYEAVLELIRHQKETIAELGIEQVVPEKPAEDTTVPDYLAKQCTKDIGAVLSQFTLTKAERDSQLDSIKAKAAEAIAALKETDAVRAAVSSNGKLLGNSFKALTKSMMRAQIVKDGKRVDGRSLDQVRPISAAAGVLPKRVHGSGLFQRGLTQVLSTATLGTPSDAQEMDDLNPSNEKHYLHHYNFPPYSVGETRPMRSPGRREIGHGALAERALLPVLPPKESFPYVLRVVSEVLSSNGSTSMGSVCGSTLALMDAGVPIAAPVAGAAMGLIREGSEVRVLTDIQGIEDFLGDMDFKVAGTEKGITALQMDMKITGLAMKTIGEAVTQARPARLHILEKMLEALDKPRDTMSPHAPRRLSFRIDPELIGTVIGPGGRTIKGITERTNTKIDIEDTGIVTVASHDGAAAEEAQKIIEGLTRRVSEGEYFDGKVTRVIPIGAFVEILPGKEGMIHISQLSDQRVEKVEDVVNVGDEVRVRVREIDNRGRINLTLRGVPQDGSDPQPTVILPIGES
Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
A5GRD7
P28480
TCPA_RAT
CCT-alpha
Rattus
MEGPLSVFGDRSTGEAIRSQNVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYINENLIINTDELGRDCLINAAKTSMSSKIIGINGDFFANMVVDAVLAVKYTDIRGQPRYPVNSVNILKAHGRSQIESMLINGYALNCVVGSQGMLKRIVNAKIACLDFSLQKTKMKLGVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRIAKASGASILSTLANLEGEETFEATMLGQAEEVVQERICDDELILIKNTKARTSASIILRGANDFMCDEMERSLHDALCVVKRVLESKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNEAQVNPERKNLKWIGLDLVHGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLIKLHPESKDDKHGGYENAVHSGALDD
Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin.
P28480
A0A2A5K5H4
AZG1_PAELB
Nucleobase transporter PlAzg1
Paenibacillus
MKGTFDVSRWETWFQLKERGTTWTTEILAGCTTFMTMVFILVVNPAILSDAGMDFNGVYVATVLVTLISTLIIALFGNFPFVIAPGMGINAFFAYSVVKAQGIPWQTALGSVFLAGTVFLVLALTRYRRFLLDAIPQSLKYAITAGTGLFICFVGLQNAKLVISSPDTLVTLGNLREPGTLLSIIGLAVTLLLMTYRIRGALFLGMIVTSVLAWIMGLMQLPSHFLSIPSGLAHTALQLDIDGVFNYDMLAVTFTFLLISVFETTGTMVSLAEQAGLMKEGRFPHSRSALLANAVGVTSGALLGTSPITTLVESGSGIAAGGRTGLTPIVTCILLVITMFFAPVAETLASTPFVTAPALVIVGFSMLEEMVHVEWKSFEEAFPSFLVMVTMPLTYSVSSAIGIGFIVYVLLKLFRGKAKEVHPALYFFALFFFIQLGFIHS
Transports adenine, hypoxanthine, xanthine and uracil. Transport is probably proton-dependent.
A0A2A5K5H4
Q9I1C8
METN1_PSEAE
Methionine import ATP-binding protein MetN 1
Pseudomonas
MTAMTVPPSLLPLEPFPTAPDTRASTPHIRLHGLGKRYPGGVQALREIDLEIRRGEVFGIIGRSGAGKSSLIRTLNRLERPSEGQVLIDDEDIGGYDGQRLVALRRRIGMIFQHFNLMSAKTVRQNIALPLRVAGVPRARIEERVAGLLQLVGLEEKRDAYPAQLSGGQKQRVGIARALVHQPQILLCDEATSALDPESTQAILALLRDINRRLGLTIVLITHEMAVIREICDRVVVLECGRIVEQGEVWEVFGDPRHAVTRSLLGSLRAALPADLQARLRQAPGAGDPVLLDLQYTGASRRVPDLLAIARAIGQRVDLLHGGIERIQGRALGRLLLQVGAPPGELPGVLAKAALVADKVEVLGHVAHA
Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system.
Q9I1C8
O84992
MACA1_RHOOP
Maleylacetate reductase I
Rhodococcus
MAERSSEFVFTGNPARVIFGAGRMRNVREEVERLGRGRVLLLGSENLREVCDQVQDLLGELFVNRYDGAAMHTPVEVTDIALAQLRTSEADCVVAIGGGSTTGLAKALAARTGVDQVILPTTYAGSEVTPVLGETVEGRKTTRSTLAVLPETVIYDVELSKNLPVPIAVASAVNALAHAVEAMYSPDANPVVDTWALEAAQALARGLRGLVSDPSCRRIRTDLLRGSWLAGMCLGSVGMAVHHKLCHTLGGAFGLPHAPTHTVVLPYAMSFNASEVPDVMDSLASAMNVSNAPAGVWDLIADAGGPTSLASLGLLQTDLDRAADLATEAPYRNPRQITRSGIRDLLQSAWEGNRPPE
Plays a major role in the degradation of chloroaromatic compounds by channeling maleylacetate and some of its substituted derivatives into the 3-oxoadipate pathway. This enzyme converts maleylacetate and 2-chloromaleylacetate with similar efficiencies.
O84992
Q9CQ20
M1IP1_MOUSE
Spot 14-related protein
Mus
MMQICDTYNQKHSLFNAMNRFIGAVNNMDQTVMVPSLLRDVPLSEPEIDEVSVEVGGSGGCLEERTTPAPSPGSANESFFAPSRDMYSHYVLLKSIRNDIEWGVLHQPSSPPAGSEESTWKPKDILVGLSHLESADAGEEDLEQQFHYHLRGLHTVLSKLTRKANILTNRYKQEIGFSNWGH
Plays a role in the regulation of lipogenesis in liver. Up-regulates ACACA enzyme activity. Required for efficient lipid biosynthesis, including triacylglycerol, diacylglycerol and phospholipid. Involved in stabilization of microtubules.
Q9CQ20
Q9VZE6
BRX1_DROME
Brix domain-containing protein 2 homolog
Sophophora
MGRKFQNKKKKAAPQLEIVPLDENPPLPPQRSSDDVVPKKARKEKWVNKQRVLVFSARGISHRDRHLMKDIKTLMPHHRPESKMERSKTLSVVNEMCEMKHCNKAMLFEGRRKRDLYMWISNTSGSTGPSAKFLIENIHTMAELKMTGNCLRGSRPLLSFDSKFDELPHLKLLKELFVQTYSVPNHHPKSQPFVDHVFTFTYLDKRIWFRNFQILSEDGGLSEVGPRYVMNPVKIFDGSFTGKTIWENPDYVSPSKQRQVLKKAAKDKYVNRVEQKVKHEATRPIRAYDGMDNDELFEDDDPVETAKILAAIAKKKKEEAAKQTPKSALTKKIKEKQLQAVKDVIERKKARTIKRVKKV
Required for biogenesis of the 60S ribosomal subunit.
Q9VZE6
Q820Y9
PNP_TROW8
Polynucleotide phosphorylase
Tropheryma
MQFSEGVIDNGRFGTRTIRFETGRLARQAQGSVVAYLDGETMLLSSTSVGKQPKEDCDFFPLTVDVEERSYAAGKIPGSYFRREGRPSTEAILACRLIDRPLRPSFNAGLRNEVQVIVTVLSIAPGEFYEALAINAASASTLVSGLPFSGPIGGVRLALIDGQWVAFPRYEDLSGAVFDLTVAGRVFVNESGKEDIAIMMVEAEATEPAWDLIHSHGAKKPNEEVIEEGIESAKVFIRTLCDIQRDLASKLSLSHTEPDLYPDYSDSVHSFVEGLVKSDLEKVYRGNHDSGYAPNALSASDEIKQKAYDAFHDAVLSGRFDQDSLSQFPHAYKAVLKDVVRTCVLEGFARMDGRGLSDIRPLDAEVQVVPRVHGSAVFQRGETQVLGVTTLNMLKMEQQIDSLAPIVSKRYIHHYNFPPYSTGEVGRVGSPKRREIGHGFLAERALVPVLPSREDFPYAIRQVSEALGSNGSTSMGSVCASTLSLLNAGVPLRAPVAGIAMGLISGRVDGEMRYVTLTDISGSEDALGDMDFKVAGTSDFITALQLDTKLDGIPAHVLSEALAHARSARLAILDVLTRVIDSPDQMSEYAPRVVRVKIPVQKIGELIGPKGKVINSIQDETGAEISIEDDGTVYIGSSQADSSEKAVAMVNSIVNPVEPCVGSQFLGTVVKNMPFGSFISLVPGKDGLLHISEIRKMVDGRHLESVDEVLSVGQKVLVEVSKIDDRGKLCLVAVK
Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Q820Y9
A7NJG1
BCHL_ROSCS
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Roseiflexus
MSLTLAIYGKGGIGKSTTSSNLSAALALKGAKVLQIGCDPKHDSTFALTGMLQPTVIDVLTEVDFHHEEVSVEDVVHTGFAGVDTLESGGPPAGSGCGGYVVGETVKLLHEFGLYDKYDVIVFDVLGDVVCGGFSAPLNYADYGVIIACNDFDSIFAANRLCLAIKQKSARYRVELAGIIANRVDYELGGGTTLLEQFAETVGTQIIGRVPYHDLIRRSRLMGKTLFEMEGPGKEECTTPFLEMAEYLLNRPRSTVPKPMGDREIFNVIGGWR
Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The L component serves as a unique electron donor to the NB-component of the complex, and binds Mg-ATP.
A7NJG1
B7MWP9
COBS_ECO81
Cobalamin-5'-phosphate synthase
Escherichia
MSKLFWAMLSFITRLPVPRRWSQGLDFEHYSRGIITFPLIGLLLGAISGLVFMVLQAWCGAPLAALFSVLVLVLMTGGFHLDGLADTCDGVFSARSRDRMLEIMRDSRLGTHGGLALIFVVLAKILVLSELALRGESILASLAAACAVSRGTAALLMYRHRYAREEGLGNVFIGKIDGRQTCVTLGLAAIFAAVLLPGMHGVAAMVVTMVAIFILGQLLKRTLGGQTGDTLGAAIELGELVFLLALL
Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
B7MWP9
Q5HE48
PTMCB_STAAC
PTS system mannitol-specific EIIB component
Staphylococcus
MSQTEEKKGIGRRVQAFGSFLSSMIMPNIGAFIAWGFIAAIFIDNGWLPNKDLATLAGPMITYLIPLLIAFSGGRLIYDLRGGIIAATATMGVIVALPDTPMLLGAMIMGPLVGWLMKKTDQLIQPRTPQGFEMLFNNFSAGILGFIMTIAGFKILAPLMKFIMHILSVAVEALVHAHLLPLVSILVEPAKIVFLNNAINHGVFTPLGADQAAKAGQSILYTIESNPGPGLGILLAYMIFGKGTAKTTSYGAGIIHFLGGIHEIYFPYVLMRPLLFIAVILGGMTGVATYQATGFGFKSPASPGSFIVYCLNAPRGEFLHMLLGVFLAALVSFVVAALIMKFTREPKQDLEAATAQMENTKGKKSSVASKLVSSDKNVNTEENASGNVSETSSSDDDPEALLDNYNTEDVDAHNYNNINHVIFACDAGMGSSAMGASMLRNKFKKAGINDITVTNTAINQLPKDAQLVITQKKLTDRAIKQTPNAIHISVDNFLNSPRYEELLNNLKKDDQA
The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II CmtAB PTS system is involved in D-mannitol transport.
Q5HE48
Q8LKI3
ALB32_CHLRE
Inner membrane ALBINO3-like protein 2, chloroplastic
Chlamydomonas
MALQMKQSPSMGVRRASQPVLPPRPIVHRGVGSVSRRPAVVVKASLLDAASAASAVDAVHHATQLYTLAEGGPIDVLAQFFEFVLQTLDEGLESAKIPYSYGFAIIALTVLVKVATFPLTQKQVESTLSLQALQPRVKELQAKYADDPENLQLETARLYKEAGVNPLAGCFPTLATIPVFIGLYNALSNAAKEGLLTEGFFWIPSLGGPTTIGGGLEWLVPFENGAPPVGWANAAAYLVMPVLLVASQYASQKIISSQNNQDPSQQQAQAILKFLPLMIGWFSLNVPSGLTLYWFVNNLLSTGQQLYLKATVKVNIPEAIKAPATAGSSTPIVKPKEERVKKVTGKELGSRKKRRNDDGEEVEDVEVEVVSSGSSSSSGSNGASGRKGEKFRALKAREAAAKAASTVSAGAGGSEEGKDNSA
Required for the insertion of some light-harvesting complexes (LHC) proteins into the chloroplast thylakoid membrane. Essential for the assembly and activity of LHC I and II. Its function is probably partly distinct from that of ALB3.1.
Q8LKI3
Q3T0L7
RL28_BOVIN
60S ribosomal protein L28
Bos
MSAHLQWMVVRNCSSFLIKRNKQTYSTEPNNLKARNSFRYNGLIHRKTVGVEPAADGKGVVVVMKRRSGQRKPATSYVRTTINKNARATLSSIRHMIRKNKYRPDLRMAAIRRASAILRSQKPVMVKRKPSRPTKSS
Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Q3T0L7
C4LDX4
EFP_TOLAT
Elongation factor P
Tolumonas
MKIAQEIRVGNVIMIGKDPMVVLKTEFNKSGRNSAVVKMKMKNLLSGAGAETVFKADDKLDTVQLERKECTYSYFADPMYVFMDTEYNQYDIEKENLGDVLNYLIDGMEDICEVTFYDGKAISMELPITIVREVEYTEPSVRGDTSGKVMKPAKLKGTDATISVADFVKIGDKIEIDTRTGEFKRRV
Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
C4LDX4
Q9LN86
DRE1F_ARATH
Dehydration-responsive element-binding protein 1F
Arabidopsis
MNNDDIILAEMRPKKRAGRRVFKETRHPVYRGIRRRNGDKWVCEVREPTHQRRIWLGTYPTADMAARAHDVAVLALRGRSACLNFADSAWRLPVPESNDPDVIRRVAAEAAEMFRPVDLESGITVLPCAGDDVDLGFGSGSGSGSGSEERNSSSYGFGDYEEVSTTMMRLAEGPLMSPPRSYMEDMTPTNVYTEEEMCYEDMSLWSYRY
Transcriptional activator that binds specifically to the DNA sequence 5'-[AG]CCGAC-3'. Binding to the C-repeat/DRE element mediates cold or dehydration-inducible transcription. CBF/DREB1 factors play a key role in freezing tolerance and cold acclimation.
Q9LN86
Q2LCR5
NDUS2_DICCI
NADH dehydrogenase subunit 7
Dictyostelium
MLNISKIFEEVKVMKNFTLNFGPQHPAAHGVLRLIVELESENVVRVEPHIGLLHRGTEKLIEGKTYTQALPYFDRLDYVSMNVQEHAYSLAVERLYLDSLDIELEIPQRAKVIRVLFSEITRVLNHIMATTTHAMDVGALTPFLWAFEEREKLMEFYERVSGARMHAAYIRPGGVAFDLPMNISEDIYKFVIQYRKRLEEIEDMLINNRIWKQRLVDIGIVSAEEALNYGFTGPLLRGAGIVYDIRKNYPYDDYDKYDFKIIIGEENNSYTRFIIRMKEMYQSLAIIEQALNNLRPGLIKLEGVNITAPDRAFVKKDMESCINHFKFFSEGFIIPANENYTIVEAPKGEFGIYLNANDTAKPYRCRIKAPGFLHLQGLNMMSKDHLLADVVTLIGTQDIVFGEVDR
Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Q2LCR5
Q8GYS8
LTG17_ARATH
Non-specific lipid transfer protein GPI-anchored 17
Arabidopsis
MKIGVVLVLLTVFVVVMSSTSVSAQSDEDECLKETGQMQLNCFPYLTDNRIHTPSFACCSEVYTVGKTYVDCFCQFINNGGPSFGIVVSQKLLDLPELCGVYGACGNGKNFKNTSL
Probable lipid transfer protein.
Q8GYS8
A5CQ60
ATPB_CLAM3
F-ATPase subunit beta
Clavibacter
MTDTATAPVASDSVAGVGRIVRVTGPVVDIEFPHDSIPPVYNALKTTITIGEESTEITLEIALHLGDDVVRAIALKPTDGLVRGQEVRDTGAAISVPVGDITKGKVFNVTGDILNNEGGEPIEITERWPIHRKPPMFDQLESKTQLFETGIKVIDLLTPYVQGGKIGLFGGAGVGKTVLIQEMIQRVAQDHGGVSVFAGVGERTREGNDLIMEMEEAGVFDKTALVFGQMDEPPGTRLRVALSALTMAEYFRDVKNQDVLLFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLADEMGVLQERITSTRGHSITSLQAIYVPADDYTDPAPATTFAHLDATTELSREIASRGLYPAVDPLTSTSRILDPRYLGQAHYDTATRVKAILQKNKELQEIIAILGVDELSEEDKVTVSRARRIQQFLSQNTYMAKKFTGVEGSTVPLKNTIESFSKIADGDYDHVAEQAFFNVGDLDDVERRWSEIQKENG
Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
A5CQ60
Q1MQE1
HSLV_LAWIP
ATP-dependent protease subunit HslV
Lawsonia
MEIRGTTILAVRHKGHVALAGDGQVTLGQSVVMKHTAKKVRRMYKNQVIAGFAGTTADAFTLFERFDNYLEETNGNLVRAAVELAKEWRKDKYLRRLEAMLLVVDKDHTFVLSGTGDVIEPDDGIAAIGSGGLYAVAAARALVAHSELSAAEIARESMRITAEICVFTNLNLTLETL
Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
Q1MQE1
Q9SXA5
SCAM5_ARATH
Secretory carrier-associated membrane protein 5
Arabidopsis
MGGRYDRNTFDEQDEVNPFANPGSVPAASNSRLSPLPPEPAGFGYGRTVDIPLDRPGSGAQDLKKKEKELQAKEADLRRREQDLKRKQDAAARAGIVIEAKNWPTFFPLIHHDIANEILVRLQRLQYIAFATYLGLVLALFWNIIAVTTAWIKGEGVTIWLLAVIYFISGVPGGYVLWYRPLYRAFRSDSAFNFGWFFLFYMLHILFCLFAAVAPPIVFKGKSLAGILPAIDVLSAQALVGIFYFIGFGLFCLESVVSIWVIQQVYMYFRGSGKADDMRRDAARGAMRAAI
Probably involved in membrane trafficking.
Q9SXA5
Q11DD7
ATPA_CHESB
F-ATPase subunit alpha
unclassified Chelativorans
MDIRAAEISAILKDQIKNFGKEAEVSEVGQVLSVGDGIARVYGLDNVQAGEMVEFPGGIRGMALNLEVDNVGVVIFGADRDIKEGDTVKRTGAIVEVPVGPGLLGRVVDALGNPIDGKGPIQATERRRVDVKAPGIIPRKSVHEPMSTGLKAIDALIPIGRGQRELIIGDRQTGKTAIILDTFLNQKPLNDGDDESQKLYCIYVAVGQKRSTVAQFVKVLEERGALEYSIVVAATASDPAPMQFLAPFAGCAMGEYFRDNGKHAVIAYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDDNGSGSLTALPVIETQANDVSAYIPTNVISITDGQIFLETNLFFQGVRPAVNVGLSVSRVGSAAQVKAMKQVAGSIKGELAQYREMAAFAQFGSDLDAATQRLLNRGARLTELLKQPQFSPLKTEEQVVVIFAGVNGYLDALALRDVGRFEQGLLTHMRSEGKEILDAIRVEKALSDDLRAKLKAEIDAYAKNFS
Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
Q11DD7
Q8PBY7
TIG_XANCP
PPIase
Xanthomonas
MQASIESTGNLERRLTFTLPQERLETHVGGRLRELARTTRIKGFRPGKVPTKVIEQRFGQQVRAEAMEGLLRETFDSAVREHSLRLAGNPRIDQGESDFDFVATFEVVPDFGDIDVTNLSVVRHTAEVTDADIDQMIENLRLQRRTWNPVERGAQVGDLVALETWSQAGNERLPAEGVETGSSVLGSGVMFDQIEKGLEGLSKGEDKALSIDFPADWRVPQLAGKTVQVHVKAVEVSEPVLPEVNKEFIKSFGVKSGDAEQFRADIRTNLERELKGALMNRLRREVGEQLIAAYAHVEMPPRLVENEAGSMLAQQVDQMRRSGRNPGEIPADAHQGFMDAAAKRVLVGLLVGEVARRNELRLESKRVSETLRLIASTYEEPEQVIEMYRNDPQLMSGLQSRVMEEQVIDWIAERAKHTEQSLSFQDAIRV
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.
Q8PBY7
A9VM93
RECF_BACMK
DNA replication and repair protein RecF
Bacillus cereus group
MFITEIQLKNYRNYEHLELSFEDKVNVIIGENAQGKTNLMEAIYVLAMAKSHRTSNDRELIRWDEDYGNIKGRLQRRNSSISLELNISKKGKKAKLNQLEQQKLSQYIGEMNVVMFAPEDLNLVKGSPQVRRRFLDMELGQIAPVYLYELSQYQKVLTQRNHLLKKMQGNSKNEETMLDVFTLQLIEHGAKILRKRFEFLHLLQEWAAPIHRGISRGLEELEIVYKPSVDVSESMDLSKIKEVYYESFQSVKQREIFRGTTLLGPHRDDLQFFVNSKNVQVFGSQGQQRTTALSLKLAEIELIYSEVKEYPILLLDDVLSELDDYRQSHLLNTIQGKVQTFVTTTSVEGIEHETLKEAKTIHVTNGTVDCEIDRK
The RecF protein is involved in DNA metabolism; it is required for DNA replication and normal SOS inducibility. RecF binds preferentially to single-stranded, linear DNA. It also seems to bind ATP.
A9VM93
B2RKW6
PANC_PORG3
Pantoate-activating enzyme
Porphyromonas
MEIFNTVASLKNFVAHARAERKTIGLVPTMGALHRGHISLIHRAVAECDICVASVFVNPTQFNDKRDLECYPRTPEADAAVLAEAGCHAVFMPSVEEVYPEPDTRVFDLGSVAEVMEGKHRPGHFNGVAQVVSKLFMMVEPDKAYFGEKDFQQIAVIRSMVNLLGLPVTIVACPIIREEDGLALSSRNVRLGSEERAIAPSIARILGQSRTLRPAHTPEAVTRWVTESLNALPHLQVEYFEIVDGNSLQRIDNWQDTDHAVGCITVYCGEVRLIDNIKYED
Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
B2RKW6
P07178
HARS1_MESAU
Histidyl-tRNA synthetase
Mesocricetus
MASPALEELVLNSRHRLVRGLKQQKASADQIEEEVAKLLKLKAQLGHDESKQKFVLKTPKGTRDYSPRQMAVREKVFDVIICCFKRHGAEVIDTPVFELKETLMGKYGQDCKLIYDLKDQGGELLSLRYDLTVPFGRYLAMNNLTNIKRYHIAKVYRRDNPAMTRGRYLNSITVDFDIAGQFDPMIPDAECLKIMCEILSSLQIGKFLVKVNDRRILDGMFAVCGVPDSKFRTICSSVDKLDKVSWEEVKNEMVGEKGLAPEVADRIGDYVQQHGEVCLVEQLLQDPKLSQNKQAVEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYVAVLLQMPTGAGEEPWCGQCGCWRRYDGLVGMFDPKGRKVPCVGLSIGVERIFSIVEQRLEALEEKVRTTETQVLVASAQKKLAGGETKACLQLWDAGIKAELLYKKNPKLLNQLQYCEETGIPLVAIIGEQELKDGVIKLRSVASREEVDVRREDLVEEIRRRTNQPLYVC
Catalyzes the ATP-dependent ligation of histidine to the 3'-end of its cognate tRNA, via the formation of an aminoacyl-adenylate intermediate (His-AMP). Plays a role in axon guidance.
P07178
Q3KPK4
BORE1_XENLA
Dasra-B
Xenopus
MASGKKKTSRKPKNRSVKNEKLASFIKDFDSQVKIITEEMKASVVNILKEVDSQYNIEIIKLPMAIREMCWLDYIAKGGSQKALEAAATVKVDMEEITSTVTKTPFKADKKVKKGKCKPDDETVELNPLKSVIRTKTKAKVAAKKPSTARRTRASVGNVANTSKRTSKRGRATPSASKQAETSLLGYTPAATPRIDTSIFKTPALRTPCMQEPVYTFSANGSPLAGMDELFINVPARDGKIIRLLASEVDGLDINRLDQQAFENIKLLSSRLERLCKKLK
Component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Contributes to CPC function by facilitating loading of the CPC onto chromosomes.
Q3KPK4
P70447
NGN2_MOUSE
Protein atonal homolog 4
Mus
MFVKSETLELKEEEEVLMLLGSASPASATLTPMSSSADEEEDEELRRPGSARGQRGAEAEQGVQGSPASGAGGCRPGRLLGLMHECKRRPSRSRAVSRGAKTAETVQRIKKTRRLKANNRERNRMHNLNAALDALREVLPTFPEDAKLTKIETLRFAHNYIWALTETLRLADHCAGAGGLQGALFTEAVLLSPGAALGASGDSPSPPSSWSCTNSPASSSNSTSPYSCTLSPASPGSDVDYWQPPPPEKHRYAPHLPLARDCI
Transcriptional regulator. Involved in neuronal differentiation. Activates transcription by binding to the E box (5'-CANNTG-3').
P70447
A8G9L5
LSPA_SERP5
Signal peptidase II
Serratia
MSKPICSTGLRWLWLVVVVLVLDFASKQWILGNFVLGQSQPLIPSFNLFYARNYGAAFSFLADHGGWQRWFFAGIAVAIVAVLLVMMYRSSAQQKLNNIAYAFIIGGALGNLFDRLWHGFVVDFIDFYVGNWHYPTFNLADSFICVGAAMIVLEGFLSPANKSAKSKGE
This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
A8G9L5
B4HR78
KTU_DROSE
PP1-interacting protein 20
Sophophora
MSASRSRNKQSKLCDDERLDISKDEFNRFQEAFGQEEFRKLFFDYVDEIQDPENRKIYEAEITQLEKERGVEVRFIHPKPGFVIKTALDGELKCFINIASSEEIERPKNEVATDPSSGSRGLNWSIPMAQTTSRDDFDAKNNHCKVFDVVFHPDALHLAMRNKQFRQCLIDTALDAVEREYKVSLDRANLKFPKLDYKGIPRPTVIRKMSDNPTAEEQEPHPLAHMFPTKPPAPGKPEPRVLPMKTKPTPVPEFTVPRYTIKHSHDVDLSEYTDELDAKLHVTVPRSLVVEIELPLLRSTAECQLDVTSKSVYLFSERQGAKYRLKLDLPFIVDDKAGRARFDTDMRRLSITLPVVRKSVQEQAQMHETLRHFSREDSGVELHSNSESPVEEDPDGELSDSKADISKTSSPTVVRNANSPFLKSSVHYQLPSKFDCNVLDNVMAFVLHVPNVQPDSIEQLREQRSLHLKFATIGSGYYPTHYAFYVELSADHEDSAIESAEAEAWDNNVVLKLYLNSQSETPAGYLAGLDATELKEYPVHGQYHVKSKEKVNAKKENAPLDVEFERNQEGHALKVTIRPGTKEEEEEEEDKENQDQKPESDQQQQQQVQNKKSGKKQRKRNKKERSLSESACADMVLQEPLAKSNELQPRATFKLPPQRKQRSYSESNDSTGRSHRGILKRFSRYGPRPSMSDSCSSIDDSSSYSCSVDASGASLFSQSFGGIPEEDRSDAGLSESCKKTVRFNDHIMKQVFRLDSSILGQRKKNQKRRDLKLRAQQRRLSEGDSVDYEETRGSALKQKENPSRNCTDSGLDLTGAAGAHSNNNESDAKNAMMFEMDD
Required for cytoplasmic pre-assembly of axonemal dyneins, thereby playing a central role in motility in cilia and flagella. Involved in pre-assembly of dynein arm complexes in the cytoplasm before intraflagellar transport loads them for the ciliary compartment.
B4HR78
B2TRH8
RSMG_CLOBB
16S rRNA 7-methylguanosine methyltransferase
Clostridium
MKFYDLMCKAAQDVGLELSKEQYEKFIIYKNLLQEWNEKVNLTAITEDEEIIKKHFIDSIKAFKRDEFKEAKTLIDVGTGAGFPGIPVAIMNENIQVTLLDSLNKRVNFLNLVTEKLGLKNVVAIHSRAEDGARQKNLRESFDIATSRAVANMSVLSEFCLPYVKINGHFIALKGPAVEEEIKDSDKAITTLGGQLLDICEVEIEDTELKHNLVVVKKIKECPKAYPRKAGNVTKKPIK
Specifically methylates the N7 position of a guanine in 16S rRNA.
B2TRH8
P07737
PROF1_HUMAN
Profilin I
Homo
MAGWNAYIDNLMADGTCQDAAIVGYKDSPSVWAAVPGKTFVNITPAEVGVLVGKDRSSFYVNGLTLGGQKCSVIRDSLLQDGEFSMDLRTKSTGGAPTFNVTVTKTDKTLVLLMGKEGVHGGLINKKCYEMASHLRRSQY
Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG. Inhibits androgen receptor (AR) and HTT aggregation and binding of G-actin is essential for its inhibition of AR.
P07737
P74521
GLGA1_SYNY3
Starch [bacterial glycogen] synthase 1
unclassified Synechocystis
MKILFVAAEVSPLAKVGGMGDVVGSLPKVLHQLGHDVRVFMPYYGFIGDKIDVPKEPVWKGEAMFQQFAVYQSYLPDTKIPLYLFGHPAFDSRRIYGGDDEAWRFTFFSNGAAEFAWNHWKPEIIHCHDWHTGMIPVWMHQSPDIATVFTIHNLAYQGPWRGLLETMTWCPWYMQGDNVMAAAIQFANRVTTVSPTYAQQIQTPAYGEKLEGLLSYLSGNLVGILNGIDTEIYNPAEDRFISNVFDADSLDKRVKNKIAIQEETGLEINRNAMVVGIVARLVEQKGIDLVIQILDRFMSYTDSQLIILGTGDRHYETQLWQMASRFPGRMAVQLLHNDALSRRVYAGADVFLMPSRFEPCGLSQLMAMRYGCIPIVRRTGGLVDTVSFYDPINEAGTGYCFDRYEPLDCFTAMVRAWEGFRFKADWQKLQQRAMRADFSWYRSAGEYIKVYKGVVGKPEELSPMEEEKIAELTASYR
Synthesizes alpha-1,4-glucan chains using ADP-glucose.
P74521
B0BRX2
ATPB_ACTPJ
F-ATPase subunit beta
Actinobacillus
MATGKIVQIIGAVIDVEFPQDAVPKVYDALKVESGLTLEVQQQLGGGLVRCIALGTSDGLKRGLKVENTGNPIQVPVGTKTLGRIMNVLGEPIDEKGPIGEEARWDIHRAAPSYEEQSNSTELLETGIKVIDLICPFAKGGKVGLFGGAGVGKTVNMMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMTDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATTFAHLDSTVVLSRNIASLGIYPAVDPLDSTSRQLDPLVVGEEHYNVARGVQGTLQRYKELKDIIAILGMDELSEDDKLVVARARKIERFLSQPFFVAEVFTGSQGKYVSLKDTIRGFKGILEGEFDHIPEQAFYMAGSIDEVVERASKM
Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
B0BRX2
A0Q5C7
FETP_FRATN
Probable Fe(2+)-trafficking protein
Francisella
MTKVFCKKYHQELDAIPFQPLPGELGKKIHNEISNKAWQAWLAHQTILINEYRLNLIEPKAKEFLKEEMHKFLFEGKEEKPEQFSEI
Could be a mediator in iron transactions between iron acquisition and iron-requiring processes, such as synthesis and/or repair of Fe-S clusters in biosynthetic enzymes.
A0Q5C7
B0U418
CH60_XYLFM
Chaperonin-60
Xylella
MAAKEIIFSEKARSRMVYGVNLLANAVKATLGPKGRNVVLDKNFGSPIITKDGVSVAKEIELADKFENMGAQMLKEVASKTNDHAGDGTTTATVLAQALIREGCKAVAAGMNPMDLKRGIDKAVIAAVTELKKISKPTSDDKAIAQVATISANSDESIGNIIAEAMKKVGKEGVITIEEGTTLENELDVVEGMQFDRGYSSPYFINNQQSQIVELDNPYILLHDKKISNVRDLLTVLDAVAKESKQLLIVAEEVEGEALATLVVNNIRGIIKVCAVKAPGFGDRRKAMLEDMAVLTGGTVISEEVGLSLEKATTSHLGKAKKVRVSKENTTIIDGMGDNDAINGRVKQIKTQIEETTSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVDDALLATRAAVEEGVIPGGGVALIRVITAISNLKGANEDQTHGIQIALRAMEAPLREIVANAGEEPSVILNKVKEGKGNFGYNAATGEFGDMVNFGILDPTKVTRSALQNAASIAGLMITTEAMIAEAPKKDEPTPPAAGGGMGGMGGMDF
Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.
B0U418
B0UHP4
THIG_METS4
Thiazole synthase
Methylobacterium
MTTPTPLAPDGDDPLVIAGTPLRSRLLIGTAGYPTQAIMAEAVRASGAEIATVSIRRVSLRGHGSDTVSLLAGHRFLPNTAGCETARDAVMTAELAREALGTAWIKVEVIGDRETLYPDVAETLEATRQLVDAGFVVLPYCNDDPVVCARLADLGAAAVMPMGSLIGSGMGVANPANLELICRRSPVPVIVDAGIGTASDAVIAMELGAAAVLLNTAVAKADDPVRMARAMRHAVEAGRLAHGAGRIPRRARAEPSSPQLGLVGS
Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S.
B0UHP4
Q8ZQ47
HPCH_SALTY
4-hydroxy-2-ketoheptane-1,7-dioate aldolase
Salmonella
MKNAFKDALKAGRPQIGLWLGLANSYSAELLAGAGFDWLLIDGEHAPNNVQTVLTQLQAIAPYPSQPVVRPSWNDPVQIKQLLDVGAQTLLIPMVQNADEARNAVAATRYPPAGIRGVGSALARASRWNRIPEYLHLANDAMCVLVQIETREAMSNLASILDVDGIDGVFIGPADLSADMGFAGNPQHPEVQAAIENAIVQIRAAGKAPGILMANEALAKRYLELGALFVAVGVDTTLLARGAEALAARFGVEKKLSGASGVY
Catalyzes the reversible retro-aldol cleavage of 4-hydroxy-2-ketoheptane-1,7-dioate (HKHD) to pyruvate and succinic semialdehyde.
Q8ZQ47
D2Y2D0
H20A3_CYRHA
Peptide F8-26.11
Haplopelma
MKSATLLALSFLLIASCFLICEAEHSRYEEHEILEENMGDVVNLEQRSCAKPGEMCMRIKCCDGQCGCNRGTGRCFCK
Putative ion channel inhibitor.
D2Y2D0
Q8GZP5
AOS3_SOLLC
Cytochrome P450 CYP74D1
Solanum subgen. Lycopersicon
MANTKDSYHIITMDTKESSIPSLPMKEIPGDYGVPFFGAIKDRYDFHYNQGADEFFRSRMKKYDSTVFRTNVPPGPFNARNSKVVVLVDAVSYPILFDNSQVDKENYFEGTFMSSPSFNGGYKVCGFLGTSDPKHTTLKGLFLSTLTRLHDKFIPIFTTSITSMFTSLEKELSEKGTSYFNPIGDNLSFEFLFRLFCEGKNPIDTSVGPNGPKIVDKWVFLQLAPLISLGLKFVPNFLEDLVLHTFPLPYILVKRDHQKLYNAFYNSMKDILDEAEKLGVKRDEACHNFVFLAGFNSYGGLKVFFPSLIKWIGTSGPSLHARLVKEIRTAVKEAGGVTLSAIDKMPLVKSVVYETLRMDPPVPFQTVKARKNIIITNHESSFLIKKDELIFGYQPLATKDSKVFKNAEEFNPDRFVGGGEKLLKYVYWSNGKEIDNPSVNDKQCPGKDLIVLMGRLLVVEFFMRYDTFEVEFGKLLLGSKVTFKSLTKATS
Cytochrome P450 metabolizing both 13- and 9-hydroperoxides of linoleic and linolenic acids, but with a marked preference for 9-hydroperoxy fatty acids . Has no activity toward 13S-hydroperoxy-9(Z),11(E),15(Z)-octadecatrienoic acid (13-HPOT) . Catalyzes not only the synthesis of allene oxide, but also its hydrolysis and cyclization . The first step is the synthesis of (12Z)-9,10-epoxyoctadeca-10,12-dienoic acid (9,10-EOD) and the final products are (9R)-alpha-ketol and the racemic cis-10-oxo-11-phytoenoic acid . The cyclase activity possesses regiospecificity and (9Z)-12,13-epoxyoctadeca-9,11-dienoic acid (12,13-EOD) is significantly less efficient as a substrate for cyclopentenone production than 9,10-EOD . Has no hydroperoxide lyase activity . May play a defensive role against soil-borne pests that affect roots or juvenile tissues as they emerge from the germinating seed .
Q8GZP5
B5ZZ10
ALLA_RHILW
Ureidoglycolatase
Rhizobium
MPEFLDIRPLTSAAFAAFGEVIEADPASMRLINGGTTERFHALAAAEAAGEGARVIINLFRGQPRNFPYDVDMMERHPFGSQSFSPVSGRPFLVVVSEDESGRPGRPQVFLARGDQGVNYRRNVWHHPLMALGEVSDFLVVDRDGAGNNLEEFFFETPYIIKEPAL
Catalyzes the catabolism of the allantoin degradation intermediate (S)-ureidoglycolate, generating urea and glyoxylate. Involved in the utilization of allantoin as nitrogen source.
B5ZZ10
A7H8F4
APT_ANADF
Adenine phosphoribosyltransferase
unclassified Anaeromyxobacter
MVMSAAMEAVRARIRDVPDFPQKGIVFKDITPVLADPTTFREVIDAFVARWKDERISKVVGIESRGFLFAAPLAYALGAGLTIARKPGKLPWETIREVYSLEYGENSLELHIDAVKAGERVLVVDDVLATGGTADAVGRLVTRQGATLVAYSFLVELGFLGGAKRLGREHVHALLSY
Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
A7H8F4
Q7CZN9
CTAA_AGRFC
Cytochrome aa3-controlling protein
Agrobacterium tumefaciens complex
MANGSVDMVVEAALQKQEKDRRLLRIWLRVVLFTLFCLVLVGGATRLTESGLSITEWKPIHGAIPPLSVAEWEEEFQLYKRIPQYQEINKGMSLDEFKTIFWWEWAHRLLARTIGLVFALPLAFFWLTGRVEKRLRLPLVGLLALGGFQGFVGWWMVSSGLVNRTDVSQYRLATHLTIACLIFAGCMWILRGLSHHSPDAADERTGRGFAALLTVLCLFQIYLGALVAGLNAGLSYNTWPLMDGSLVPGDLFLQQPWWINLFENPKTVQFVHRLGAYTLFAATLWHMVSMARALPGTPHARRAVLFFVLISVQAGLGITTLLMHVDIHVALAHQGMALILLGFSVAHWRGFIGEYPAPVAVEVRD
Catalyzes the conversion of heme O to heme A by two successive hydroxylations of the methyl group at C8. The first hydroxylation forms heme I, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme A.
Q7CZN9
A6Q4C9
FMT_NITSB
Methionyl-tRNA formyltransferase
unclassified Nitratiruptor
MRIVFMGTPDYATTILEGLLEKFEVVGVFTQPDKPVGRKQVVTPPHVKKFLIEKNVDIPIFQPSTLKSEEVYEQLHTLAPDFIVVAAYGQILPKEILQLAPCINLHASLLPKYRGASPIQHALLNGDTVTGVTAMLMDEGLDTGDILAYDVIDIQNSDNAITLFEKLSHLAKELTPKVLQSFENIAPIAQHDVDASYCKKIRKQDGQIRFSDAKVIWNKYRAFIVWPGIFLENGLKLKEIDLVETDNTHEEGKILEISDAGVVVGCRRGSICIKSVQPPSKKAMEAVAYLRGKRLKVGDTFF
Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
A6Q4C9
P13251
SP2D_BACAM
Stage II sporulation protein D
Bacillus amyloliquefaciens group
MKPIVFLLSGLCVLILLVPTILVLPFQAEKGAAVNREPGHKTAHTIRETKGAEPTLKESPVSVPVYRTSNHSVENIPLEEYVIGVVASEMPVEFKPEALKAQALAARTFIVRLMVANSASRPRKGSLVDDTQMFQVYKSKSQLKKEWGSDYAQNLKKITNAVAGTQGKILTYENKPIEASFFSTSNGYTENAEAYWTSAIPYLKSVKSPWDKKSPKYLATRTFSVPEFQQKLGVQLAGQDTVGQITARTPGHQVATAVINGKKLKGRDIREKLGLRSADFEWKRNGGTITITTKGFGHGVGMSQYGANYMAEQGKSVTDIVKHYYQGVDISEADSFLSKYMAKK
May act at the level of sigma-G activity or its stability. SpoIID is probably required for engulfment.
P13251
Q62KD8
OTCC_BURMA
Ornithine carbamoyltransferase, catabolic
pseudomallei group
MSFNLHNRNLLSLIHHNARELRYLLDLARDLKRAKYSGTEQPRLLRKNIALIFEKTSTRTRCAFEVAAYDQGANVTYIDPASSQIGHKESMRDTARVLGRMYDAIEYRGFSQEIVEELAHHAGVPVFNGLTDEYHPTQMLADVMTMREHSDKPLHDIRYAYLGDARNNMGNSLLLIGAKLGMDVRIGAPKSLWPAADFIAQCEAFAAESGARLTLTEDPYEAVKGVDFIHTDVWVSMGEPVEAWDERINALLPYQVNRKLIESTGNPRTRFMHCLPSFHNCETKVGKQIAERYPHLQDGIEVTDEVFESPRCIAFEQAENRMHTIKAVLVSTLGGI
Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline.
Q62KD8
B6JJQ2
Y7544_AFIC5
Nucleoid-associated protein OCAR_7544/OCA5_c05960
Afipia
MADFLGMMKQAAQLQSKMKEMQEQLDQVEVEGSAGGSMVTVRMTAKMELKAVSIDPSLMKPEEREVLEDLLVAAQNDARRKAEEAMQERMKALTGGLSIPGLGLG
Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection.
B6JJQ2
A9GZW9
HIS6_GLUDA
ImGP synthase subunit HisF
Gluconacetobacter
MLKLRVIPCLDVKNGRVVKGVNFVSLRDAGDPVEQAAVYDAAGADELTFLDITASHENRDTILDVVSRTAERIFLPLTVGGGVRTTDDMRRLLLAGADKCAMNSAAVARPDLVSEAARKFGSQCVVVAVDARSDGHGSWEVYTHGGRTPTGRNVIDWCREVVERGAGEILLTSMDRDGTGSGFDLDLLCAACTAVRVPIVASGGVGTLEHFVEGARAGATGLLAASVFHFGQFTIPQVKQALADAGLPVRHTPAHPVP
IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit.
A9GZW9
Q8Y3Y6
KTHY_LISMO
dTMP kinase
Listeria
MKAIFITLEGPDGSGKTTVGTLLNQKMTEAGIDFIKTREPGGSPISEKVRNIVLGIGNEEMDPKTEVLLIAGARRQHVVETIRPALAAGKSVLCDRFMDSSLAYQGAGRDMNMEQVLQVNLYAIEDTLPDRTYYLDVPAEVGLARIAANKGREVNRLDKEDITYHEKVQAGYEKVINMFPERFMRVDATKTPEEITETILADILRQLA
Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Q8Y3Y6
Q7CWX3
RUTD_AGRFC
Aminohydrolase
Agrobacterium tumefaciens complex
MHFEVHGRTDAEAPTILLSSGLGGSSAYWLPQIEALSDHFRIVTYDHRGTGRTGGEVPTEGGISAMADDVLEIVSALNLEKFHFMGHALGGLIGLDIALRQPRLIDRLVLINAWSKADPHSGRCFDVRIELLEKSGVDAFVKAQPLFLYPAAWMSEHQERLARDDAHGVAHFQGKTNVLRRIAALRAFDIDARLGEIGNPVLVVATKDDLLVPYTRSLRLAEGLPQSELCLLDFGAHAVNITEPDLFNTRLLQFLLPADQT
Involved in pyrimidine catabolism. May facilitate the hydrolysis of carbamate, a reaction that can also occur spontaneously.
Q7CWX3
P25195
NODM_RHIML
Nodulation protein M
Sinorhizobium
MCGIVGIVGHQPVSERLVEALEPLEYRGYDSAGVATMDAGTLQRRRAEGKLGNLREKLKEAPLSGTIGIAHTRWATHGAPTERNAHPHFTEGVAVVHNGIIENFAELKDELAAGGAEFQTETDTEVVAHLLAKYRRDGLGRREAMHAMLKRVKGAYALAVLFEDDPSTIMAARTGPLAIGHGNGEMFLGSDAIALAPFTNEITYLIDGDWAVIGKTGVHIFDFDGNVVERPRQISTAAAFLVDKGNHRHFMEKEIYEQPEVIAIALGHYVNVIDKSCRSDSDAIDFAGVESLAISCCGTAYLAGLIGKYWFERYARLPVEIAVASEFRYREIPLSPQSALFISQSGETADTLASLRYCKAHGLRIGAVVNARESTMARESDAVFPILAGPEIGVARTKAFTCQLAVLAALRAGAGKARGTISGDEEQALIKSLAEMPAIMGQVLNSIQPEIEVLSRELSNCRDVLYLGRGTSFPLAMEGALKLKEISYIQPKSYAAGQLKHGPYALIDENMPVIVIAPHDRFFDKTVTNMQEVARGGRIILITDEKGAAASKLDTMHTIVLPEVDEIIAPMIFSLPLQLLAYHTAVFMGTDVDQPRNLAKSVTVE
Involved in the production of the root hair deformation (HAD) factor specifically on medicago.
P25195
Q3SX23
LONP2_BOVIN
Peroxisomal Lon protease
Bos
MSSVSPIQIPSRLPLLLTHEGVLLPGSTMRTSVDSARNLQLVRSRLLKGTSLQSTILGVIPNTPDPASDAQDLPPLHRIGTAALAVQVVGSNWPKPHYTLLITGLCRFQITQVVREKPYPVAEVEQLDRLEEFPNTCKTREELGELSEQFYKYAVQLVEMLDMSVPAVAKLRRLLDSLPREALPDILTSIIRTSNKEKLQILDAVSLEERFKMTIPLLVRQIEGLKLLQKTRKHKQDDDKRVIAIRPMRRITHVPGALADEDEDEDNDDIVMLEKKIRTSSMPEQAHKVCVKEIKRLKKMPQSMPEYALTRNYLELMVELPWNKSTTDRLDIRAARVLLDNDHYAMEKLKKRVLEYLAVRQLKNNLKGPILCFVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQGDPAAALLEVLDPEQNHNFTDHYLNVAFDLSQVLFIATANTTASIPPALLDRMEIIQVPGYTQEEKIEIAHRHLIPKQLEQHGLTPQQIQIPQVTTLDIITRYTREAGVRSLDRKLGAICRAVAVKVAEGQHREAKLDRPDVAEGEGCKEHLLEDGKSDPVSDTTDLALPPEMPILIDFHALKDILGPPMYEMEVSERLSQPGVAIGLAWTPLGGEIMFVEASRMDGEGQLTLTGQLGNVMKESAHLAISWLRSNAKKYHLTNASGSFDLLENTDIHLHFPAGAVTKDGPSAGVTIATCLASLFSGRLVRSDVAMTGEITLRGLVLPVGGIKDKALAAHRAGLKRVIIPQRNEKDLEEIPANVRQDLSFITASCLDEVLNAAFDGGFTVKARPGLLNSKL
ATP-dependent serine protease that mediates the selective degradation of misfolded and unassembled polypeptides in the peroxisomal matrix. Necessary for type 2 peroxisome targeting signal (PTS2)-containing protein processing and facilitates peroxisome matrix protein import. May indirectly regulate peroxisomal fatty acid beta-oxidation through degradation of the self-processed forms of TYSND1.
Q3SX23
Q5HJ90
ESAA_STAAC
Type VII secretion system accessory factor EsaA
Staphylococcus
MKKKNWIYALIVTLIIIIAIVSMIFFVQTKYGDQSEKGSQSVSNKNNKIHIAIVNEDQPTTYNGKKVELGQAFIKRLANEKNYKFETVTRNVAESGLKNGGYQVMIVIPENFSKLAMQLDAKTPSKISLQYKTAVGQKEEVAKNTEKVVSNVLNDFNKNLVEIYLTSIIDNLHNAQKNVGAIMTREHGVNSKFSNYLLNPINDFPELFTDTLVNSISANKDITKWFQTYNKSLLSANSDTFRVNTDYNVSTLIEKQNSLFDEHNTAMDKMLQDYKSQKDSVELDNYINALKQMDSQIDQQSSMQDTGKEEYKQTVKENLDKLREIIQSQESPFSKGMIEDYRKQLTESLQDELANNKDLQDALNSIKMNNAQFAENLEKQLHDDIVKEPDTDTTFIYNMSKQDFIAAGLNEGEANKYEAIVKEAKRYKNEYNLKKPLAEHINLTDYDNQVAQDTSSLINDGVKVQRTETIKSNDINQLTVATDPHFNFEGDIKINGKKYDIKDQSVQLDTSNKEYKVEVNGVAKLKKDAEKDFLKDKTMHLQLLFGQANRQDEPNDKKATSVVDVTLNHNLDGRLSKDALSQQLSALSRFDAHYKMYTDTKGREDKPFDNKRLIDMMVDQVINDMESFKDDKVAVLHQIDSMEENSDKLIDDILNNKKNTTKNKEDISKLIDQLENVKKTFAEEPQEPKIDKGKNDEFNTMSSNLDKEISRISEKSTQLLSDTQESKSIADSVSGQLNQVDNNVNKLHATGRALGVRANDLNRQMAKNDKDNELFAKEFKKVLQNSKDGDRQNQALKAFMSNPVQKKNLENVLANNGNTDVISPTLFVLLMYLLSMITAYIFYSYERAKGQMNFIKDDYSSKNHLWNNVITSGVIGTTGLVEGLIVGLIAMNKFHVLAGYRAKFILMVILTMMVFVLINTYLLRQVKSIGMFLMIAALGLYFVAMNNLKAAGQGVTNKISPLSYIDNMFFNYLNAEHPIGLVLVILTVLVIIGFVLNMFIKHFKKERLI
Component of the type VII secretion system (Ess). Provides together with EssB and other components such as EssC and EssE a secretion platform across the cytoplasmic membrane in the host.
Q5HJ90
A8AZ72
HUTG_STRGC
Formiminoglutamate hydrolase
Streptococcus
MLEDYYQLDNSYYQRGVEDNLYAAKWGMVIEFLNLNDPNLKPVEGVNFALIGFKSDKGVYINHGRVGAVEGPQSIRTQLAKLPWHLGRNVHVFDVGDIDGPNRSLEQLQSSLAKAVKRLRELNLRPIVLGGGHETAYGNYLGLKSSLKPEQELAVINMDAHFDLRPYDQTGPNSGTGFRQMFDETLAQKQVFNYLILGIQEHNNNLFLFDFVAKSKAIQFLTGLDIYQMGHKEVCKVVDAFLADKEQVYLTIDIDCFAAGAAPGVSAIQSLGVDPNLAVLVFQHIAASGKLIGFDVVEVSPPHDIDNHTANLAASFIFYLTQVWAQIHD
Catalyzes the conversion of N-formimidoyl-L-glutamate to L-glutamate and formamide.
A8AZ72
Q81T85
NORM_BACAN
Multidrug-efflux transporter
Bacillus cereus group
MKETNSFSQKLKQFVLLFFPIFVTQMSLFAMSFFDTTMSGHASPIDLAGVAIGTSIWIPVSTGLTGILMATTPIVAQLVGSKKKEDVPHVIIQAVYLAICASFVVILIGLFTVTPILNGMRLEEPVERIAAQFLSIIAIGIIPLFTYTVLRGFIDALGKTRTTMIITLLSLPINVVLNYVLIFGNFGFPKLGGVGAAIASAATYWCILIITVMIIRTKEPFASFNIFKQLYRPSLSSWKEFLKLGVPIGFAIFFETSIFAAVTLMMSNFSTTTIAAHQAAMNFASLLYMTPLSLAMAMTIAVGFEVGAKRYNNAKQYGFIGIGLALAFALLYSILLYFFDDEIASIYTTDIQVHHLAKEFLIFAILFQISDAIATPVQGALRGYKDVNVALIMTLIAYWVIGLPLGYILATYTDWAAKGYWIGLIIGLAFGATFLLIRLFQVQRKYTTQNSRS
Multidrug efflux pump.
Q81T85