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
|
|---|---|---|---|---|---|---|
Q8CV64
|
RECX_OCEIH
|
Regulatory protein RecX
|
Oceanobacillus
|
MKKIARITTQKKHKNRYNIFLQTPDGGDAYGFSVDEAILIEYRLSKGMELEDEMISILEQKDTLHKAYTLTIHFLSYRMRSEKEVSDYLQKKEVDEEHIAEIIKRLKKEKWVDDQQFAEMFVRSRINSSSKGPKMIQQELFEKGVDGSKITSALEQYPVEEQKQKVEKLISKKLQSKSKDSHQKRIDQIKQNLMQKGFDSGVISMVIQQMDTTEDTDREWEVLQLQGEKLLYKYQKKHSGFALKQKVMEGLYRKGFSFDMINQFIDQSLQDE
|
Modulates RecA activity.
|
Q8CV64
|
Q5HC05
|
RPOB_EHRRW
|
Transcriptase subunit beta
|
Ehrlichia
|
MSSSVTSKYVLNSFSSVPRLSYAKSIDIKDSLTDLIKIQRDSYNAFIGIDQDVDSGIKNIFQSMFPIQDLLGRAVLQFVSYSIGEPQYDEYECIKRGITYSVPIRIVLRFIVWKVQEVSFKEVKYVVDEETSEKSIKYIKEQEVSIGDLPTMTSYGTFIINGVERVIVSQMHRSPGVFFDSDKGKTYSSGKLIYLARIIPYRGSWLDFEFDIKDILYFRIDRKRKLPVSLLLRALGLSNSEILDTFYDKIRYERCENGWVVPFVVDRFRGVRLSYDLVDIDGNVLVKANTRITLRLAKKLASDGLKKYLVPFAEIQGLFIANDLVDPASNVMIMCAGESITSEHINKLKLFDINEIFILNIDFLTVGPYILNTLFLDKNISYEDALFEIYKVLRSGESPSLDTMKAFFDGLFFEKERYDLSTVGRIKLNDHLGLDISEDVTVLTKDDIIHVIKKLVLLRDGEGFVDDIDHLGNRRVRSVGEFIENQFRIGILRLERMIMDYMSSVNFDNAMPCDFVNPKVLATVLKDFFSSSQLSQFMDQTNPLSEVTHKRRLSALGPGGLTRERAGFEVRDVHPTHYGRICPIETPEGQNIGLISSLAIYARINKHGFIESPYRKVDNGVVTDKVEYLLAMQESNYYIADASATLDENNRFVDDMLYCRHDGNFVMVKREQVDYIDVSPKQIVSVAASLIPFLENNDANRALMGSNMQRQAVPLLKADAPLVGTGMESIVAAGSGTVVLAKRSGIVHRVDGLYIVIRAFDKEKNEYLGVDIYNLRKFQRSNHNTCINQKPLVKPGDYVRENDVIADGSAIDQGELALGKNVLVAFMSWQGYNFEDSIVISSEVVKKDVFTSIHIEEFECVVRDTALGPEKIMRSIPDVNEDSLSHLDDVGIVNVGAEVSAGDILVGKVTPRPPVSLPPETKLLVTIFGEKVFDCVDSSLYLPIDVEGTVVDVHVFVRRGVEENDRSLLIKQNEINGFIKERDYEIDVVSEYFYDELKRVLVNTNTEYNNQNIEDYLKSIPQKSWWDIKLSDESVLSQISDLKEKFDSMIENAHSKFDQKIDKLNYGYDLPQGVLCIVKVFVAVKHNLQPGDKMAGRHGNKGVISRIVPVEDMPYLEDGTPVDIILNSLGVPSRMNVGQILETHLGWASVNLGKKIGNILDNIDELTIAHLRNFLDQVYDGQDLKYSIRSMSDDDLLAFAERLRDGVPMAAPVFEGPKDNQISNLLKLADLDVSGQVDLYDGRIGEKFDRKVTVGYIYMLKLHHLVDDKIHARSVGPYGLVTQQPLGGKSHFGGQRFGEMECWALQAYGAAYTLQEMLTVKSDDIVGRVKIYESIIKGDSNFECGIPESFNVMVKELRSLCLDVALKQDKDFLHDRKINN
|
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
|
Q5HC05
|
A9HDX7
|
DCUP_GLUDA
|
Uroporphyrinogen decarboxylase
|
Gluconacetobacter
|
MTDTGKPLLRVLQGEAVWPPPIWLMRQAGRYLPEFRALRDQADFITRCMTPDLATEITLQPIRRYAMDGAILFSDILILPWAMGQSLDFVAGKGPILGAIRSEADLARLDPKRVPDATAPVMETLSRLRAILDGPDPIGAAQGGRVTLLGFAGAPFTVACYMVEGHGSREFDATRGMAYSDPLLFDRLMATLTQATADMLVAQIDAGAEAVMLFDSWSGLLPPAQFRRHVIAPTRAIVQEIQARRPGVPVIGFPRLAGIMAAEYARETGLRVMALDTGADMAAMAGLLPPGMTVQGNLDPLLLLAGGDAMAQEARAIRDAMKGRPHVFNLGHGVVPPTPPEHVGDLVRTVREV
|
Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
|
A9HDX7
|
Q87KN8
|
TRMA_VIBPA
|
tmRNA (uracil(341)-C(5))-methyltransferase
|
Vibrio
|
MATLDVNPQRYQEQLAEKVERLTDMFAPYNVPELEVFESPEQHYRMRAEFRVWHEGEDLYYIMFNQETREKYRVDQFPAASRLINDLMPLLVEAMKDNESLRRKLFQVDFLSTLSGEILVSLLYHRQLDEEWIENAKALKQRLNDEGFNLNIIGRARKMKIILDRDYVIEKLDVNGQSYIYQQVENSFTQPNGKVAEKMLEWAVDCTQESTGDLLELYCGNGNFSLALAQNFDRVLATELAKPSVESAQYNIAANKIDNVQIIRMSAEEFTEAMEGKREFRRLKDNGVDLKSYNCNTIFVDPPRAGMDVDTCKMVQGYERIMYISCNPETLKENLDILSETHNVTRFALFDQFPYTHHMEAGVLLERKA
|
Dual-specificity methyltransferase that catalyzes the formation of 5-methyluridine at position 54 (m5U54) in all tRNAs, and that of position 341 (m5U341) in tmRNA (transfer-mRNA).
|
Q87KN8
|
Q8C522
|
ENDD1_MOUSE
|
Endonuclease domain-containing 1 protein
|
Mus
|
MGCARWLALGGLLALAGLLQARLLLPQQAGFGECDRFFYKGTPPAGLATEAHVRICQRFAGSERFATLYSPGHRIPVFSAFRAARPASRSAEQRGLLEPQIDDPDSNLEEVIDEANALTSVDNLGSKQALNADYIDSDYEIGQLYPFPLNSDLQMATFPLTNSVPMTQSFRERWHMNLNSLMDRALIPHCSEGKDLYILTGAVPSEHRVKGKVTIPEFVWLAACCAVPGEGWAMGFIKHTQDIDVIEDVMLRDLEKLLPHKPQLFQDNCGEMEQDTEKMKKILEVVNQVQDEERSLQSQERMSPLASTQSQRSALLSPEAPPEGGSSFLGQVLGFLATPFIKLFQLIYYLVTAVLRNIVHLLWLVAKQAINTVESCLYHLGEATVSYLVAIGQELVSIPWKVLKVVAKVIRAFLRILCCLLKAVCRALSIPLRVLVDVATFPVYTVGAIPIVCKDIAVGLGGTLSLLFDTAFGTVGGLFQIVFSVFKRIGYKVTLDNSGEF
|
May act as a DNase and a RNase. Plays a role in the modulation of innate immune signaling through the cGAS-STING pathway by interacting with RNF26.
|
Q8C522
|
B1YVL0
|
PLSX_BURA4
|
Phosphate-acyl-ACP acyltransferase
|
Burkholderia cepacia complex
|
MTVKLTIDCMGGDHGPSVTVPAAVKFVRAHPDAHLMLVGIESAIRAQLKKLKALDDPALTIVPATEVVAMDDPVEVALRKKKDSSMRVALNQVKEGAAQACISAGNTGALMAVSRYVLKTLPGIERPAIAFALPNPTGYTMMLDLGANVDCEPQHLLQFAEMGHALVAALEGKERPTIGLLNIGEEVIKGNETIKRAGELLRASTLNFRGNVEGNDIYKGTVDVIVCDGFVGNVALKTSEGLAQMLSDIIREEFGRSLMSKLMALLALPVLMRFKKRVDHRQYNGAALLGLKGLVIKSHGSADAYAFEWAIKRGYDAVKNGVLERLARAMADNSVSLGDGGHDAGGAGTASPAPGHHAEPSAAQSSKA
|
Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
|
B1YVL0
|
I6Y3V5
|
IPDE1_MYCTU
|
5OH-HIP-CoA dehydrogenase alpha subunit
|
Mycobacterium tuberculosis complex
|
MQDVEEFRAQVRGWLADNLAGEFAALKGLGGPGREHEAFEERRAWNQRLAAAGLTCLGWPEEHGGRGLSTAHRVAFYEEYARADAPDKVNHFGEELLGPTLIAFGTPQQQRRFLPRIRDVTELWCQGYSEPGAGSDLASVATTAELDGDQWVINGQKVWTSLAHLSQWCFVLARTEKGSQRHAGLSYLLVPLDQPGVQIRPIVQITGTAEFNEVFFDDARTDADLVVGAPGDGWRVAMATLTFERGVSTLGQQIVYARELSNLVELARRTAAADDPLIRERLTRAWTGLRAMRSYALATMEGPAVEQPGQDNVSKLLWANWHRNLGELAMDVIGKPGMTMPDGEFDEWQRLYLFTRADTIYGGSNEIQRNIIAERVLGLPREAKG
|
Involved in cholesterol degradation. Catalyzes the dehydrogenation of 5OH-HIP-CoA to 5OH-HIPE-CoA . Can also use octanoyl-CoA and dihydroferuloyl-CoA, with lower efficiency. Cannot use 3-oxo-4-pregnene-20-carboxyl-CoA (3-OPC-CoA) .
|
I6Y3V5
|
Q5E2G4
|
GPH_ALIF1
|
Phosphoglycolate phosphatase
|
Aliivibrio
|
MFEDIKLIAFDLDGTLLDSVPDLARAVDLAMQDMGYPRVTLEQASHWIGNGADVLVSRALSQNYIVKDDLDAELIKQARARLDQHYHDGGHQLSHLYPDVKDTLERLHQQGYTLALVTNKPSQFVPELLEQHQLTHLFSEVIGGDTFAEKKPNPFALNWLLDKHGLTAPQMLMVGDSKNDIQAAQAAGCHSFALTYGYNHGEPISDSQPDVVSDEFKYLLAVLSMAR
|
Specifically catalyzes the dephosphorylation of 2-phosphoglycolate. Is involved in the dissimilation of the intracellular 2-phosphoglycolate formed during the DNA repair of 3'-phosphoglycolate ends, a major class of DNA lesions induced by oxidative stress.
|
Q5E2G4
|
Q979K2
|
RL13_THEVO
|
50S ribosomal protein L13
|
Thermoplasma
|
MKIIDASNTVYGRLSAYVAKQLLNGEEVVIVNASKAVITGDRKFIIDKFKQRLDIGSVRKGPYYPKTPENILRRSIGDMLPKKITRGKEALSRCKVYRNLPKNVSSEKIEKVDDVMTDKVVGIITLEELSKELGGM
|
This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly.
|
Q979K2
|
P32731
|
RBFA_BACSU
|
Ribosome-binding factor A
|
Bacillus
|
MSMRANRVGEQMKKELGDIISRKLKDPRIGFLTVTDVRVSGDLQIAKVYISVLGDEKKREEALKGLAKAKGFIRSEIGSRIRLRKTPEIEFEFDESIDYGNRIETLIHELHSEKPSE
|
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.
|
P32731
|
P97484
|
LIRB3_MOUSE
|
Paired immunoglobulin-like receptor B
|
Mus
|
MSCTFTALLRLGLTLSLWIPVLTGSLPKPILRVQPDSVVSRRTKVTFLCEETIGANEYRLYKDGKLYKTVTKNKQKPENKAEFSFSNVDLSNAGQYRCSYSTQYKSSGYSDLLELVVTGHYWTPSLLAQASPVVTSGGYVTLQCESWHNDHKFILTVEGPQKLSWTQDSQYNYSTRKYHALFSVGPVTPNQRWICRCYSYDRNRPYVWSPPSESVELLVSGNLQKPTIKAEPGSVITSKRAMTIWCQGNLDAEVYFLHNEKSQKTQSTQTLQEPGNKGKFFIPSVTLQHAGQYRCYCYGSAGWSQPSDTLELVVTGIYEYYEPRLSVLPSPVVTAGGNMTLHCASDFPYDKFILTKEDKKFGNSLDTEHISSSGQYRALFIIGPTTPTHTGAFRCYGYYKNAPQLWSVPSALQQILISGLSKKPSLLTHQGHILDPGMTLTLQCFSDINYDRFALHKVGGADIMQHSSQQTDTGFSVANFTLGYVSSSTGGQYRCYGAHNLSSEWSASSEPLDILITGQLPLTPSLSVQPNHTVHSGETVSLLCWSMDSVDTFILSKEGSAQQPLRLKSKSHDQQSQAEFSMSAVTSHLSGTYRCYGAQDSSFYLLSSASAPVELTVSGPIETSTPPPTMSMPLGGLHMYLKALIGVSVAFILFLFIFIFILLRRRHRGKFRKDVQKEKDLQLSSGAEEPITRKGELQKRPNPAAATQEESLYASVEDMQTEDGVELNSWTPPEEDPQGETYAQVKPSRLRKAGHVSPSVMSREQLNTEYEQAEEGQGANNQAAESGESQDVTYAQLCSRTLRQGAAASPLSQAGEAPEEPSVYATLAAARPEAVPKDMEQ
|
May act as receptor for class I MHC antigens. Becomes activated upon coligation of LILRB3 and immune receptors, such as FCGR2B and the B-cell receptor. Down-regulates antigen-induced B-cell activation by recruiting phosphatases to its immunoreceptor tyrosine-based inhibitor motifs (ITIM).
|
P97484
|
B2A8M8
|
THII_NATTJ
|
tRNA 4-thiouridine synthase
|
Natranaerobius
|
MYNYLLIRYGEIGLKGKNRSYFEKSLVKNMQSALKDLEIGKIKSTQGRMYIPLSGSSDELTRVLDRVTRVFGIETVSPAVKVESDLEVIKKTALQVFKNHMDSISPQNQVSFKVDCRRADKLFSKNSMEMNQILGAHILDHVPGLKVDVKQPQILLQVEIREDGTYIFTEKIPGHGGLPIGTTGKGVLMLSGGIDSPVAGWLAMKRGIQVVGLHFHSYPFTSQRALKKVEDISQVLSRYGTGPTGGFKLITNHFTDIQKAIQNYCSESMWVTVMRRFMFYIANRMAQKEQAMTVVTGENVGQVASQTLESMHAVSQDVVNLPILRPLAGLDKKEIMSKAETIGTYDISIRPYEDCCTLFLPKNPKTRPSLEQTKREISKLNFEELVEESLEKTEIKYFEPYQDITEEELTFDV
|
Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS.
|
B2A8M8
|
P19579
|
CAPA_BACAN
|
Capsule biosynthesis protein CapA
|
Bacillus cereus group
|
MRRKLTFQEKLLIFIKKTKKKNPRYVAIVLPLIAVILIAATWVQRTEAVAPVKHRENEKLTMTMVGDIMMGRHVKEIVNRYGTDYVFRHVSPYLKNSDYVSGNFEHPVLLEDKKNYQKADKNIHLSAKEETVKAVKEAGFTVLNLANNHMTDYGAKGTKDTIKAFKEADLDYVGAGENFKDVKNIVYQNVNGVRVATLGFTDAFVAGAIATKEQPGSLSMNPDVLLKQISKAKDPKKGNADLVVVNTHWGEEYDNKPSPRQEALAKAMVDAGADIIVGHHPHVLQSFDVYKQGIIFYSLGNFVFDQGWTRTKDSALVQYHLRDNGTAILDVVPLNIQEGSPKPVTSALDKNRVYRQLTKDTSKGALWSKKDDKLEIKLNHKHVIEKMKKREKQEHQDKQEKENQVSVETTT
|
Essential for the synthesis of the polyglutamate capsule of B.anthracis which is one of the principal virulence factors during anthrax infection. May form a polyglutamyl synthetase complex together with proteins CapB and CapC.
|
P19579
|
C0QAY0
|
FOLD_DESAH
|
Methenyltetrahydrofolate cyclohydrolase
|
Desulforapulum
|
MAEVLKGKPVADALKAELTKNIEALKKDKGITPKLGIIRVGARPDDLFYEGGAKKTCAAVGMDCEIFEYPEDIDQASFEKAVTEVGAKKDVNGILMFSPLPKNLDERKIRTLIPVEKDVDCLTTGGAAKVFTDDATGFPPCTPTACMEMLHFYDIPIKGKKCVVVGRSLVVGKPLAMLLLREHGTVTICHSRTENLPGVCQDADILIAAVGRAKMVKADFVKKGQIVIDVGINADPDRPGKYCGDVDFETVEPVVTKITPVPAGVGSVTTSVLCKQTFMACQMQNA
|
Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
|
C0QAY0
|
O42668
|
TPR1_SCHPO
|
Tetratricopeptide repeat protein 1
|
Schizosaccharomyces
|
MEGFTLETHASRIIEVPLLGQEDQSVEIDCSSLPSDATELCEILVNEQAPREFWTKFAHEYYIRGLREQAILILKSGLETLKDSESLCILNANIAAIYLSMAREAMLKKDTDLRDEQLRNVRTYLEAANNIDSKSEINVLLHGIYRILLNPTDKESLENAARCFDFVLQKSGGNILGFLGKARILYAKGNYRSALKLYQRALVSNPQFKPDPRIGIGLCFWNLDMKTDALSAWTRVQQLDPKNTVVDTYIGLYYYDLAFQNVNNDSFVQNYGKALQHIQRAFKTRNNDPVASSILERYVYSKKNYEGCIKLAENVIQNSFSSSLIADGYYWMGRAYHQMGNNEKAMASYQKAKAADDRHLLSSVGIGQIQILQNDLTSAKLTFERIAEQNQSCFEALVVLGCLHASDSKPDLTKARMLLDRAFNLVGSSKLPRVVDSDLYITQARLWEKEDTKKSLGFLTRALDFLESAHMSVGPELLNNIAVLQYHLGLIPEAHGNIIKAKSVLPDANPELSLLLDYNLARCEEELGNTSVASEAYVSILEKHPSFIDARIRKCLLQLSNPNEETFKEIRHIMNADSQNLEVRAFFGWYLSKQKRRPVEDPEVRHCSQTLRHWHDDIYSLVQLGNAYMRQAREFRVHNDREKLKRQKLYIKAIQSYDQAIKFDPKNAHAAQGIAIILAQNRQFSKALLILSKVREAIKDATTLINIGNCLAELKQFSRAIEVFETVYSSTGESDTYGVLSCLGRVWLQRGRESKNVDYLKESVRYATLALEKNPENPSLLFNVAFVQFQLCELIRQKPENSRTVEDLNFAMQQLDASIETFTKLVSVEHPPYSPTSIEQRAKMAKNTTKRQLERAIQAQIEYEKSVAAKLEDARIQREKEKARRLAEEEALLKEKQERERQLQEERQKMQEEVLEWRKSQQKASEDDMSLSDDEEKQSGKKKKKDRKKRKSKSKQESSDSGVSEDDEIPLSDARNKTKKRRVNRRVISEEYTFDQDSDAEGNQEEEVSRTIEEKQDNDITDNQDDNKELNLFSEEDEE
|
Involved in promoting potassiumm ion uptake.
|
O42668
|
Q5L0U5
|
PYRC_GEOKA
|
Dihydroorotase
|
Geobacillus thermoleovorans group
|
MGVWLKNGMSFNKDGELMRTHIKIEHGTIAAILYEQPLEANEEDVIDVGGRLIVPGLIDLHVHLREPGGEAKETIETGTLAAAKGGFTTVAAMPNTNPAPDRKEQMEWLQARIRETARVNVLPYAAITIGQKGEELTDFAALKEAGAFAFTDDGVGVQSAGMMFEAMKQAAALDMAIVAHCEDDTLTNGGAVHDGEFARRYGLRGIPSVCEAVHIARDVLLAEAAGCHYHVCHISTKESVRVVRDAKRAGIRVTAEVTPHHLLLCDEDIPGLDANYKMNPPLRSREDRDALIEGLLDGTIDFIATDHAPHTAAEKAKGIEAAPFGIVGLETAFPLLYTHFVKTGVFTLKQLVDWLTIKPAQCFGLKAGRLAVGAPADIAVIDLETEEAIDPETFASKGKNTPFAGWVCQGWPVMTFVGGTLVWEKGRA
|
Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
|
Q5L0U5
|
Q8U9K6
|
RUVB_AGRFC
|
Holliday junction ATP-dependent DNA helicase RuvB
|
Agrobacterium tumefaciens complex
|
MSDADRLITPEKRGEDIDTTLRPQSLDDFTGQAEARANLKVFIEAAKNRGEALDHVLFVGPPGLGKTTLAQIMAKELGVNFKSTSGPVIAKAGDLAALLTNLEERDVLFIDEIHRLNPAVEEILYPAMEDFQLDLIIGEGPAARSVKIDLSKFTLVAATTRLGLLTTPLRDRFGIPVRLAFYTVDELELIVRRGARLMGLNMTDGGAREIARRARGTPRIAGRLLRRVRDFAEVARAEAVTREIADEALTRLLVDNMGLDQLDMRYLTMIAVNFGGGPVGIETIAAGLSEPRDAIEDIIEPYMIQQGFIQRTPRGRILTATAWKHLGLQPPKDLEAAQFRLTLEDD
|
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.
|
Q8U9K6
|
Q9Y708
|
CGR1_EMENI
|
rRNA-processing protein cgrA
|
Aspergillus subgen. Nidulantes
|
MSSAAPAPSTHAAKSIRKNGKNWHDNKKPFRPNGGLTSYTKRAAARKEQEAIKEYEKELREEREAERQAHIQRIKERRAAKEEKERYEKMAEKMHRKRVERLKKREKRNKLLNS
|
Involved in nucleolar integrity and required for processing of the pre-rRNA for the 60S ribosome subunit.
|
Q9Y708
|
Q0HYA3
|
CYSC_SHESR
|
Adenosine-5'-phosphosulfate kinase
|
Shewanella
|
MSNIVWHQHSVDQADRAKLKGQNPVLLWFTGLSGAGKSTLAGALERALFDAGFHTYLLDGDNVRHGLCKDLGFSVADRDENLRRVGEVAKLMVDAGLVVLSAFISPTREERDSIRARFPEGQFIEVHVSTPLSICEQRDPKGLYVKARRGEISNFTGISSPYEAPLSAELTIDTSKGDLASQVRALIDYLTAIEVINPSRLTASA
|
Catalyzes the synthesis of activated sulfate.
|
Q0HYA3
|
Q7SZ73
|
FXL15_XENLA
|
F-box/LRR-repeat protein 15
|
Xenopus
|
MAKDEDNSRVHLLDLPWEDVLVPHILSYLPLRHILSLQRVSKPFHSLVHIYLCNCRHFDSTQLGPQLPKTTFSELLKNNTVLQKLDLQSCSDWLTDKELLPIIGQNHHLTYINLNSCGQLTRQSLVAISLSCPHLQNICLGHCDWVDCLSMRSLADHCKCLEAIDLTACRQLKDDAISYLVQKSTRLKSLSLAVNANISDIAVEETAKSCRDLEHLDLTGCLRVKNDSIRTLAEYCNNLKSLKVKHCHNVTESSLGNLRKREVVLDVEPPLQRALVLLQDVVGFAPFINLQI
|
Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Acts as a positive regulator of the BMP signaling pathway). Required for dorsal/ventral pattern formation (By similarity.
|
Q7SZ73
|
Q4L7Y6
|
ATPA_STAHJ
|
F-ATPase subunit alpha
|
Staphylococcus
|
MAIKAEEISALLRSQIENYESEMSVTDVGTVLQIGDGIALIHGLNDCMAGELVEFSNGVLGLAQNLEESNVGVVILGPYTEITEGDEVRRTGRIMEVPVGEELIGRVVNPLGQPIDGQGPINTTKTRPVEQKATGVMARKSVDEPLQTGIKAIDALVPIGRGQRELIIGDRQTGKTTIGIDTILNQKGLDTICIYVAIGQKDSTVRANVEKLRQAGALDYTIVVSASASEPSPLLYIAPYSGVTMGEEFMFNGKHVLIVYDDLTKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLNDDLGGGSITALPIIETQAGDISAYVPTNVISITDGQIFLQSDLFFSGVRPAINAGQSVSRVGGSAQIKAMKKVAGTLRLDLASYRELESFAQFGSDLDEFTARKLERGKRTVEVLKQDQNKPLPVENQVLIIYALTKGYLDDIPVEDITRFEDELNSWTKSNGSDLLNEIRETGGLPSDDKFEATINEFKKSFSKSE
|
Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
|
Q4L7Y6
|
A4YCR6
|
EF1A_METS5
|
Elongation factor Tu
|
Metallosphaera
|
MSQKPHLNLIVIGHVDHGKSTLVGRLLMDRGFLDEKTIKEAEEAAKKLGKESEKYAFLLDRLKEERERGVTINLTFMRFETKKYFFTIIDAPGHRDFVKNMITGASQADAAILAVSARKGEFESGMSLEGQTREHIILAKTMGLNQVIVAITKMDVAEPPYDQKRYNEIKETIEKFMKSFGFDMSKVKFIPIVSITGENVTKRSENMKWYNGPTLEEALDMLEIPPKPVDKPLRLPIQEVYSISGVGTVPVGRVESGVMKVGDKIVFMPAGKSAEVRSIETHHTKLEKAEPGDNIGFNVRGIDKKDVKRGDVVGHTTNPPTVAEEFTARVIVVWHPTALAVGYTPVVHVHTASIACRVSEIVARLDPKTGKEAEKNPQFIKQGESAIVKFKPIKPLCVEKFSDFPPLGRFAMRDMGKTVGVGVINDVKPSKIEIK
|
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
|
A4YCR6
|
Q8DST2
|
MURE_STRMU
|
UDP-N-acetylmuramyl-tripeptide synthetase
|
Streptococcus
|
MITIETVLTILKNNANFREIIDGKHYQYKYSNPEVAFHHISYDSRDIKASTLFFVKGATFKKEFLEKAIESGLTFYVAEKDYQVGIPLILVNNIKNAMCLIAKEFYDNPQDKLKTLAFTGTKGKTTAAYFAYHILKQGYRPAMISTMNTTLDGKTFFKSKLTTPESLDLFKMMAQAVANGMTHLIMEVSSQAYLVGRVYGLTFDVGVFLNISPDHIGPIEHPTFEDYFYHKRLLLKHSRYVIVNSQMNHFALIKEQVADQPHDFYGKYSDNQIINSKAFSFDLTGKLAGHYDIQLTGSFNQENAVAAALACLQLGASQTDIQKGIVQTTVPGRMEVLIQKNGAKVFVDYAHNGDSLEKLLSVVEEHQKGTLILILGAPGNKGESRRADFGYVINAHPELQVILTADDPNNEDPQLISQEIAHHIKRPVNIIVDRKQAIQKAMSLTQSENDAVIIAGKGADAFQIIKGKRTAYAGDIEVARKYL
|
Catalyzes the addition of L-lysine to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan.
|
Q8DST2
|
P80859
|
6PGD_BACSU
|
GNTZII
|
Bacillus
|
MSKQQIGVIGLAVMGKNLALNIESRGFSVSVYNRSSSKTEEFLQEAKGKNVVGTYSIEEFVQSLETPRKILLMVKAGTATDATIQSLLPHLEKDDILIDGGNTYYKDTQRRNKELAESGIHFIGTGVSGGEEGALKGPSIMPGGQKEAHELVKPILEAISAKVDGEPCTTYIGPDGAGHYVKMVHNGIEYGDMQLISESYFILKQVLGLSADELHEVFAEWNKGELDSYLIEITADIFTKKDEETGKPLVDVILDKAGQKGTGKWTSQSALDLGVPLPIITESVFARFISAMKEERVKASGLLSGPEVKPVTENKEELIEAVRKALFMSKICSYAQGFAQMKAASEEYNWDLKYGEIAMIFRGGCIIRAAFLQKIKEAYDREPELDNLLLDSYFKNIVESYQGALRQVISLAVAQGVPVPSFSSALAYYDSYRTAVLPANLIQAQRDYFGAHTYERTDKEGIFHTEWMK
|
Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH. Is the predominant 6-P-gluconate dehydrogenase isoenzyme in B.subtilis during growth on glucose and gluconate.
|
P80859
|
Q9RYZ2
|
Y2861_DEIRA
|
Uncharacterized protein DR_A0161
|
Deinococcus
|
MSAGSLGGRSRLDEQLERMTADFLSMQDTLAGQLRALQAAFAQGDTSVREEVERLDRDIDAANARIEGEALHLLARQSPVAHDLKLTLLILQSTPDLERAGDYAKHVARRLSALRAGTAGHPSEFAQALALLLQMATTLRAASSPMNAALAHEVRALDDQVDALYDRAVEQVLAGRPDAALADTLEASHAWRAAERLGDHLVNVAQRTERLLARPAPSDAPA
|
Not known; probably involved in phosphate transport and/or metabolism.
|
Q9RYZ2
|
A1UK02
|
KHSE_MYCSK
|
Homoserine kinase
|
unclassified Mycobacterium
|
MTQTLPAGLTATATVAASSANLGPGFDSLGLALSLYDEIVVETVDSGLTVTVEGEGAGQVALDSSHLVVRAIEAGLRATGCIAPGLVVRCRNDIPHSRGLGSSAAAVVGGLAAANGLVSQTDWTPLTVEQLIQLSSAFEGHPDNAAAAVLGGAVVTWTDGAGAQARYAAAPLRVHPDIHLFPAIPQQRSSTAETRVLLPDTVSHTDARFNLSRAALLVVALTERPDLLMAATEDVLHQPQRAAAMPASAEFLRVLRGCGVAAVLSGAGPAVIALSTEPVLPAEAVEFGIANGFTIAEMAVGDGVRWSTGVAAGR
|
Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
|
A1UK02
|
A0KF22
|
RL4_AERHH
|
50S ribosomal protein L4
|
Aeromonas
|
MELVMKDAKSALEVSETTFGREFNEALVHQVVVAYAAGARQGTRAQLTRSEVSGGGKKPWRQKGTGRARAGSIRSPIWRSGGVTFAAKPQDHSQKVNKKMYRGAIRSILSELVRQERLIVVEKFGIEAPKTKELIAKLKEMELTDVLIVTAEVDENLFLAARNLYKVDVRDVAGIDPVSLIAFDKVLMTADAVKQIEEMLA
|
Forms part of the polypeptide exit tunnel.
|
A0KF22
|
P18949
|
METC_SALTY
|
Cysteine-S-conjugate beta-lyase
|
Salmonella
|
MTDKQLDTKLVNAGRSKKYTLGSVNSVIQRASSLVFDTVEAKKHATRNLANGELFYGRRGTLTHFSLQEAMCELEGGAGCALFPCGAAAVANTILAFVEQGDHILMTNTAYEPSQDFCSKILGKLGVTTSWFDPLIGADITQHIQPNTKVVFLESPGSITMEVHDIPSIVSAVRRVAPEAVIMIDNTWAAGVLFKALEFDIDISIQAGTKYLIGHSDAMVGTAVANARCWEQLRENAYLMGQMLDADTAYMTSRGLRTLGVRLRQHQESSLKIAAWLANHPQVARVNHPALPGSKGHAFWKRDFTGSSGLFSFVLNKKLTEAELSAYLDNFSLFSMAYSWGGYESLIIANQPEQIAAIRPAGGVDFTGTLVRVHIGLESVDDLIADLAAGFARIV
|
Catalyzes the cleavage of cystathionine to homocysteine, pyruvate and ammonia during methionine biosynthesis.
|
P18949
|
Q3K3L2
|
RPOB_STRA1
|
Transcriptase subunit beta
|
Streptococcus
|
MAGHEVQYGKHRTRRSFSRIKEVLDLPNLIEIQTDSFQDFLDAGLKEVFEDVLPISNFTDTMDLEFVGYELKEPKYTLEEARIHDASYSAPIFVTFRLVNKETGEIKTQEVFFGDFPIMTEMGTFIINGGERIIVSQLVRSPGVYFNDKVDKNGKVGYGSTVIPNRGAWLELETDAKDIAYTRIDRTRKIPFTTLVRALGFSGDDEIVDIFGDSELVRNTIEKDIHKNPSDSRTDEALKEIYERLRPGEPKTADSSRSLLVARFFDPRRYDLAAVGRYKINKKLNLKTRLLNQTIAENLVDGETGEILVEAGTVMTRDVIDSIAEHIDGDLNKFVYTPNDYAVVTEPVILQKFKVVAPTDPDRVVTIVGNSNPEDKVRALTPADILAEMSYFLNLAEGIGKVDDIDHLGNRRIRAVGELLANQFRIGLARMERNVRERMSVQDNEVLTPQQIINIRPVTAAVKEFFGSSQLSQFMDQHNPLSELSHKRRLSALGPGGLTRDRAGYEVRDVHYTHYGRMCPIETPEGPNIGLINNLSSFGHLNKYGFIQTPYRKVDRSTGAVTNEIVWLTADEEDEFTVAQANSKLNEDGTFAEEIVMGRHQGNNQEFPSSIVDFVDVSPKQVVAVATACIPFLENDDSNRALMGANMQRQAVPLIDPKAPYVGTGMEYQAAHDSGAAVIAKHDGRVIFSDAEKVEVRREDGSLDVYHVQKFRRSNSGTAYNQRTLVKVGDLVEKGDFIADGPSMENGEMALGQNPVVAYMTWEGYNFEDAVIMSERLVKEDVYTSVHLEEFESETRDTKLGPEEITREIPNVGEDSLRDLDEMGIIRIGAEVKEGDILVGKVTPKGEKDLSAEERLLHAIFGDKSREVRDTSLRVPHGGDGVVRDVKIFTRANGDELQSGVNMLVRVYIAQKRKIKVGDKMAGRHGNKGVVSRIVPVEDMPYLPDGTPVDIMLNPLGVPSRMNIGQVMELHLGMAARNLGIHIATPVFDGASSEDLWETVQEAGMDSDAKTVLYDGRTGEPFDNRVSVGVMYMIKLHHMVDDKLHARSVGPYSLVTQQPLGGKAQFGGQRFGEMEVWALEAYGASNVLQEILTYKSDDVTGRLKAYEAITKGKPIPKPGVPESFRVLVKELQSLGLDMRVLDEDDNEVELRDLDEGEDDDVMHVDDLEKARVKQEAEEKQAEQVSEVVQED
|
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
|
Q3K3L2
|
A6T4I7
|
RSMA_KLEP7
|
S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase
|
Klebsiella
|
MNNRVHQGHLARKRFGQNFLNDQFVIDSIVSAINPQKGQAMVEIGPGLAALTEPVGERLDQLTVIELDRDLAARLQTHPFLGPKLTIYQQDAMTMNFGELAEKMGQPLRVFGNLPYNISTPLMFHLFSYTDAIADMHFMLQKEVVNRLVAGPNSKAYGRLSVMAQYYCQVIPVLEVPPSAFTPPPKVDSAVVRLVPHSTMPYPVKEIRVLSRITTEAFNQRRKTIRNSLGNLFSVEVLTELGIDPAMRAENISVAQYCLMANWLSDNLPTKES
|
Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
|
A6T4I7
|
B5XQ71
|
MINC_KLEP3
|
Probable septum site-determining protein MinC
|
Klebsiella
|
MSNTPIELKGSSFTLSVVHLHDANPEVIRQALEDKIAQAPAFLRHAPVVVNIASVEEEVEWRAINEAIAATGLRIMGVSGCKIPRLKTEIDRAGIPLLTEGKEKAPRPAPSEPTPPPPPVANQITKTRLIDQPVRSGQRIYAPHCDLIVTNHVSAGAELIADGNIHVYGMMRGRALAGAGGDRDAQIFCTHLAAELVSIAGEYWLSDNIPAEFYGKAARLRLGESALTVQPLN
|
Cell division inhibitor that blocks the formation of polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings. Prevents FtsZ polymerization.
|
B5XQ71
|
Q83I04
|
RL19_TROW8
|
50S ribosomal protein L19
|
Tropheryma
|
MHALDALDALSIKADIPDFSPGDTVRVYVNITEGDRSRVQVFQGVVIARRGFGVRQTFTVRKISFQVGVERIFPLHSPSINRIEVVTKGSVRRAKLYYIRKLRGKKAKVKQKREL
|
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.
|
Q83I04
|
P0C0X3
|
TFB5_CANAL
|
RNA polymerase II transcription factor B subunit 5
|
Candida
|
MLVASKGVLVQCDPSIKALIIQIDSSSSGIILEELDETHLLIQHDKVNFVKSELNRLLSKNIYNPFEEE
|
Component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to TFIIK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module TFIIK controls the initiation of transcription.
|
P0C0X3
|
A1VT30
|
COAX_POLNA
|
Pantothenic acid kinase
|
Polaromonas
|
MTFLALDVGNTRLKWAQYDAPVVGAKLLAHGAVFLENIDRLAENDWHGMPEPSAILGCVVAGDAIKRRVAEQMEIWDVLPRWVHSSPQEAGLTNGYDHPARLGSDRWVAMIGAYHRLLARGIRKPCLVVMVGTAVTVEAIDASGKFLGGIILPGHGIMLRALESGTAGLHVPTGDVRDFPTNTSDALTSGGTFAIAGAVQRMVDNITRHCGEAPECIMTGGAAWKMAPSMSVKVELVETLIFDGLLEIASRRFKP
|
Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
|
A1VT30
|
Q9QY17
|
PACN2_RAT
|
Syndapin-II
|
Rattus
|
MSVTYDDSVGVEVSSDSFWEVGNYKRTVKRIDDGHRLCGDLMNCLHERARIEKAYAQQLTEWARRWRQLVEKGPQYGTVEKAWMAVMSEAERVSELHLEVKASLMNEDFEKIKNWQKEAFHKQMMGGFKETKEAEDGFRKAQKPWAKKLKEVDAAKKAHHTACKEEKLAVSREANSKADPSLNPEQLKKLQDKIEKCKQDVLKTKDKYEKALKELDQTTPQYMENMEQVFEQCQQFEEKRLRFFREVLLEVQKHLDLSNVASYKGIYRELEQSIKAADAVEDLRWFRANHGPGMAMNWPQFEDEEWSADLNRTLSRREKKKAADGVTLTGINQTGDQSGQNKPSSNLSVPSNPAQSTQLQSSYNPFEDEDDTGSSVSEKEDIKAKNVSSYEKTQNYPADWSDDESNNPFSSTDANGDSNPFDEDTTSGTEVRVRALYDYEGQEHDELSFKAGDELTKIEDEDEQGWCKGRLDSGQVGLYPANYVEAIQ
|
Regulates the morphogenesis and endocytosis of caveolae . Lipid-binding protein that is able to promote the tubulation of the phosphatidic acid-containing membranes it preferentially binds. Plays a role in intracellular vesicle-mediated transport. Involved in the endocytosis of cell-surface receptors like the EGF receptor, contributing to its internalization in the absence of EGF stimulus.
|
Q9QY17
|
Q3SVD0
|
ISPG_NITWN
|
1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase
|
Nitrobacter
|
MNKLESPSEIDVAGPSPRHKTTQVMVGNVAVGGGAPIVVQSMTNTDTADIEGTIAQVAALSRAGSEMVRMTVDRDEAAAAVPHIRDGLRKRGITTPLIGDFHYIGHKLLADHPSCAEALDKYRINPGNVGFKDKRDKQFTDIVETAIKYGKAVRIGANWGSLDQELLTHLMEENANSAAPLDARAVTREAMVQSALLSAKRAEEIGLPKTRMVLSAKVSAVQDLIAVYQTLASRSDYAIHLGLTEAGMGSKGIVASSAALGILLQQGIGDTIRISLTPEPGGDRTLEVQVAQELLQTMGFRTFVPLVAACPGCGRTTSTTFQELARSIQDFIRDEMPNWKTQYPGVEQLNVAVMGCIVNGPGESKHADIGISLPGTGEAPAAPVFVDGKKFKTLRGPAIAQDFKALVIDYIEQRYGDAAKARAEAVSAAE
|
Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.
|
Q3SVD0
|
Q8DZK7
|
NADK_STRA5
|
ATP-dependent NAD kinase
|
Streptococcus
|
MTQMNFTDRATRVAIIANGKYQSKRVASKLFAAFKHDPDFYLSKKDPDIVISIGGDGMLLSAFHMYEKQLDKVRFVGVHTGHLGFYTDYRDFEVDTLINNLKNDKGEQISYPILKVTITLEDGRVIRARALNESTIKRIEKTMVADVVINQVVFERFRGDGILVSTPTGSTAYNKSLGGAVLHPTIEALQLTEISSLNNRVYRTLGSSVIIPKKDAIEIVPKRVGVYTISIDNKTVHYKNVTKIEYSIDEKSINFVSTPSHTSFWERVNDAFIGEPEH
|
Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
|
Q8DZK7
|
Q46631
|
AMSA_ERWAM
|
Amylovoran biosynthesis membrane-associated protein AmsA
|
Erwinia
|
MKSKIEEPSANGGEAIRFELAHLLGQLLDHRWMIVAVSVLFTLMGTLYSLFATPIYSADAMVQVEQKNANTVLNDISQMMPNAQPASAAEIEIITSRMVLGKTVADLGLDVLVQQDHFPLIGAGLSRIIGQKAQQIAVSRLKVPTLWDKRELSVEVDGPDSYTVSKDGNELFKGKVGQFEQHGDVTMLVNSIEADAGTRFTVSKLNNLQAIKMISNNLVVADMGKDTGVLGLTYSGEDPVQISRVLDQVINNYLYQNIARKSEEAEKSIQFLAQQLPDVRAKLDQAEDKLNVFRRKHDSVDMSLEAKSALDSSVSIQTQLNALTFREAEVSQLFKKDHPTYRALLEKRQTLDEQQKQLNGKISQMPQTQQEIVRLTRDVQAGQEIYMQLLNRQQELNISKASTVGDVRIIDHAETAAKPVAPKSILIVAGSLILGLVVSVGLVLMKALFHHGIDNPEQLEELGLNVYASVPLSEWQRKKDQETLLKRKLDARTDPHNRLLALGNPTDLSIEAIRSLRTSLHFAMMDAQNNILMITGASPGIGKTFVCANLATLVAKTGEKVLFIDGDMRRGYTHELLGAESKTGLSDILSGKLPFNTDLVQRGDYGFDFIARGQVPPNPSELLMNSRMKELVHWASQNYDLVLIDTPPILAVTDASIIGKLAGTSLMVARFETNTVKEVEISYKRFIQNGIDIKGIILNAVVRKSANNYGYGYDYYDYSYQQGEKS
|
Involved in the biosynthesis of amylovoran which functions as a virulence factor.
|
Q46631
|
A5GQF7
|
NU3C_SYNR3
|
NDH-1 subunit 3
|
unclassified Synechococcus
|
MFVLPGYDAFLGFLLIAAAVPVLALITNAVLAPRSRQGERRLTYESGMEPVGGAWIQFNIRYYMFALVFVIFDVETVFLYPWAVAFHRLGLLAFIEALVFIAILVVALAYAWRKGALEWS
|
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.
|
A5GQF7
|
P19486
|
EF1A_THEAC
|
Elongation factor Tu
|
Thermoplasma
|
MASQKPHLNLITIGHVDHGKSTLVGRLLYEHGEIPAHIIEEYRKEAEQKGKATFEFAWVMDRFKEERERGVTIDLAHRKFETDKYYFTLIDAPGHRDFVKNMITGTSQADAAILVISAREGEGVMEQTREHAFLARTLGVPQMVVAINKMDATSPPYSEKRYNEVKADAEKLLRSIGFKDISFVPISGYKGDNVTKPSPNMPWYKGPTLLQALDAFKVPEKPINKPLRIPVEDVYSITGIGTVPVGRVETGVLKPGDKVIFLPADKQGDVKSIEMHHEPLQQAEPGDNIGFNVRGIAKNDIKRGDVCGHLDTPPTVVKAFTAQIIVLNHPSVIAPGYKPVFHVHTAQVACRIDEIVKTLNPKDGTTLKEKPDFIKNGDVAIVKVIPDKPLVIEKVSEIPQLGRFAVRDMGQTVAAGQCIDLEKR
|
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
|
P19486
|
Q96AJ1
|
CLUA1_HUMAN
|
Qilin
|
Homo
|
MSFRDLRNFTEMMRALGYPRHISMENFRTPNFGLVSEVLLWLVKRYEPQTDIPPDVDTEQDRVFFIKAIAQFMATKAHIKLNTKKLYQADGYAVKELLKITSVLYNAMKTKGMEGSEIVEEDVNKFKFDLGSKIADLKAARQLASEITSKGASLYDLLGMEVELREMRTEAIARPLEINETEKVMRIAIKEILTQVQKTKDLLNNVASDEANLEAKIEKRKLELERNRKRLETLQSVRPCFMDEYEKTEEELQKQYDTYLEKFQNLTYLEQQLEDHHRMEQERFEEAKNTLCLIQNKLKEEEKRLLKSGSNDDSDIDIQEDDESDSELEERRLPKPQTAMEMLMQGRPGKRIVGTMQGGDSDDNEDSEESEIDMEDDDDEDDDLEDESISLSPTKPNRRVRKSEPLDESDNDF
|
Required for cilia biogenesis. Appears to function within the multiple intraflagellar transport complex B (IFT-B). Key regulator of hedgehog signaling.
|
Q96AJ1
|
Q9SKJ5
|
CESAA_ARATH
|
Probable cellulose synthase A catalytic subunit 10 [UDP-forming]
|
Arabidopsis
|
MVAGSYRRYEFVRNRDDSDDGLKPLKDLNGQICQICGDDVGLTKTGNVFVACNECGFPLCQSCYEYERKDGSQCCPQCKARFRRHNGSPRVEVDEKEDDVNDIENEFDYTQGNNKARLPHRAEEFSSSSRHEESLPVSLLTHGHPVSGEIPTPDRNATLSPCIDPQLPGIYQLLLLPVRILDPSKDLNSYGLVNVDWKKRIQGWKLKQDKNMIHMTGKYHEGKGGEFEGTGSNGDELQMVDDARLPMSRVVHFPSARMTPYRIVIVLRLIILGVFLHYRTTHPVKDAYALWLTSVICEIWFAFSWLLDQFPKWYPINRETFLDRLALRYDRDGEPSQLAPVDVFVSTVDPMKEPPLVTANTVLSILAVDYPVDKVACYVSDDGSAMLTFEALSETAEFSKKWVPFCKKFNIEPRAPEFYFSQKIDYLKDKIQPSFVKERRAMKREYEEFKVRINILVAKAQKIPEDGWTMEDGTSWPGNNPRDHPGMIQVFLGHSGGLDTDGNELPRLIYVSREKRPGFQHHKKAGAMNALIRVSAVLTNGAYLLNVDCDHYFNNSKAIKEAMCFMMDPAIGKKCCYVQFPQRFDGIDLHDRYANRNTVFFDINLKGLDGIQGPVYVGTGCCFNRQALYGYDPVLTEEDLEPNIIVKSCFGSRKKGKSRKIPNYEDNRSIKRSDSNVPLFNMEDIDEDVEGYEDEMSLLVSQKRLEKRFGQSPVFIAATFMEQGGLPSTTNPLTLLKEAIHVISCGYEAKTDWGKEIGWIYGSVTEDILTGFKMHARGWISIYCVPSRPAFKGSAPINLSDRLNQVLRWALGSIEILLSRHCPIWYGYNGRLKLLERIAYINTIVYPITSIPLLAYCMLPAFCLITNTFIIPEISNLASLCFMLLFASIYASAILELKWSDVALEDWWRNEQFWVIGGTSAHLFAVFQGLLKVFAGIDTNFTVTSKASDEDGDFAELYVFKWTSLLIPPTTILLVNLVGIVAGVSYAINSGYQSWGPLMGKLLFAFWVVAHLYPFLKGLLGRQNRTPTIVIVWSALLASIFSLLWVRINPFVSTTGVMSNSFMGE
|
Probable catalytic subunit of cellulose synthase terminal complexes ('rosettes'), required for beta-1,4-glucan microfibril crystallization, a major mechanism of the cell wall formation.
|
Q9SKJ5
|
Q133W8
|
MRAY_RHOPS
|
UDP-MurNAc-pentapeptide phosphotransferase
|
Rhodopseudomonas
|
MLYWLIDLSSSIPAFNVFRYITFRTGGAVVTGALFVFLCGPWIINNLRLRQGKGQPIRSDGPQSHLVTKKGTPTMGGLMILSGLTVGTVLWANPVNPYVWIVLAVTLGFGFVGFYDDYMKVTKQTHAGISGRTRLLIEFAIAGAACFALVWLGRSSLSSSLVIPFFKEVVLNLGWYFVIFGAFVIVGAGNAVNLTDGLDGLAIVPVMIAAASFGLIAYLAGNAVFADYLQINYVAGTGELAVLCGALLGAGLGFLWFNAPPASIFMGDTGSLALGGMLGSIAVAVKHEIVLAVIGGLFVLEAVSVIVQVASFKLTGKRVFRMAPIHHHFEQKGWTEPQIVIRFWIIAVMLALAGLATLKLR
|
Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
|
Q133W8
|
Q04806
|
GTO3_YEAST
|
Glutathione S-transferase omega-like 3
|
Saccharomyces
|
MSEKSASNNKAEFKRQSSPFREIISADHPIYKPAKGRYWLYVALPCPWAQRTLITRALKGLAPIIGCSVAHWHLDDKGWRFLEEGDGKTNERHWFDIAGGISSVNLNTSTPVANIPNNAHRLLVDGTDEPHYGYKRLSDFYFKTKPDYKGRFTVPVLWDLETCTIVNNESSDIIGIMNSAAFDEFVGEEYRQVRLVPRSLEAQITEFNSWVYDKINNGVYKAGFAECAEVYEREVTSLFQYLDKLENLLDKKYTDLEAEYGKNNKDKILDRYFAIGDTLTEADVRLYPTIVRFDVVYHQHFKCNLATIRDDYSRIHTWLKNIYWRHEAFQRTTDFTHIKLGYTRSQPRVNPIGITPLGPKPDIRPP
|
Active as '1-Cys' thiol transferase against beta-hydroxyethyl disulfide (HED), as dehydroascorbate reductase and as dimethylarsinic acid reductase, while not active against the standard GST substrate 1-chloro-2,4-dinitrobenzene (CDNB).
|
Q04806
|
Q6XGD4
|
CAPE_ECOLX
|
Patatin-like phospholipase
|
Escherichia
|
MTYSVSPSSLLTEYGNDNICRVLALDGGGAKGFYTLGVLKEIEAMLGCPLYKRFDLVFGTSTGAIIAALIALGYEVDQIHALYTEHVPRVMSSRSAAARTMALQDLAKEVFQDKTFEDVLMGIGIVATRWMTERPMIFKGNVVQAHGRKGTFSPGFGVSIADAVQASCSAYPFFERKVIVTAAGDKVELIDGGYCANNPTLFAIADATVALKKDHKDIRVINVGVGIYPEPKPGLLMRIAKKWLAVQLLQKTLEINTQSMDQLRDILFKDIPTIRISDTFERPEMATDLLEYNLDKLNTLRQRGRESFGAREAQLREFLI
|
Phospholipase that is activated upon binding to the cyclic dinucleotide (CDN) second messenger 3',3'-cyclic UMP-AMP (3',3'-cUAMP).
|
Q6XGD4
|
Q56K04
|
CRIP1_BOVIN
|
Cysteine-rich protein 1
|
Bos
|
MPKCPKCSKEVYFAERVTSLGKDWHRPCLKCEKCGKTLTSGGHAEHEGKPYCNHPCYAAMFGPKGFGRGGAESHTFK
|
Seems to have a role in zinc absorption and may function as an intracellular zinc transport protein.
|
Q56K04
|
B2VGW6
|
ARGR_ERWT9
|
Arginine repressor
|
Erwinia
|
MRNSSKQEDLIKAFKALLKEEKFSSQGEIVNALQEEGFENINQSKVSRMLTKFGAVRTRNAKMEMVYCLPAELGVPTTTSPLKNLVLDIDFNDALVVIHTSPGAAQLIARLLDSLGKAEGILGTIAGDDTIFITPARSFTVKQLHDAILVLFEQEL
|
Regulates arginine biosynthesis genes.
|
B2VGW6
|
P0C2B4
|
PEPO_LACLC
|
Endopeptidase O
|
Lactococcus
|
MTRIQDDLFATVNAEWLENAEIPADKPRISAFDELVLKNEKNLAKDLADLSQNLPTDNPELLEAIKFYNKAGDWQAREKADFSAVKNELAKVETLNTFEDFKNNLTQLVFHSQAPLPFSFSVEPDMKDAIHYSLGFSGPGLILPDTTYYNDEHPRKKELLDFWAKNTSEILKTFDVENAEEIAKSALKFDALLVPSANTSEEWAKYAELYHPISTDSFVSKVKNLDLKSLIKDLVKTEPDKVIVYEDRFYESFDSLINEENWSLIKAWMLTKIARGATSFFNEDLRILGGAYGRFLSNVQEARSQEKHQLDLTESYFSQVIGLFYGKKYFGEAGKADVKRMVTAMIKVYQARLSKNEWLSQETAEKAIEKLDAITPFIGFPDKLPEIYSRLKTTSGSLYEDALKFDEILTARTFEKFSEDVDKTSWHMPAHMVNAYYSPDSNTIVFPAAILQAPFYSLEQSSSQNYGGIGTVIAHEISHAFDNNGAQFDKEGNLNKWWLDEDYEAFEEKQKEMIALFDGVETEAGPANGKLIVSENIADQGGITAALTAAKDEKDVDLKAFFSQWAKIWRMKASKEFQQMLLSMDFHAPAKLRANIPPTNLEEFYDTFDVKETDKMYRAPENRLKIW
|
Endopeptidase with broad substrate specificity for several oligopeptides.
|
P0C2B4
|
B0T8A6
|
LGT_CAUSK
|
Phosphatidylglycerol--prolipoprotein diacylglyceryl transferase
|
unclassified Caulobacter
|
MIFPNIDPIVHIGPWALQWGPLALRWYALAYVVGILLGWRYAVMLVRDAKLWGGHKPTATPLQIDDLVLWITLGIILGGRIGYVLFYMMLNEGQRAGLAEHPFDVFKIWEGGMSFHGGFLGVCAAIVLFARQQKIDMLKLGDLIAPVAPIGLFFGRCANFINGELWGRETTHPWGMIFCNETIQKANQGGCPAGHLPRHPSQLYEAALEGVLLFLILNFAAHKLKWLQRRGALVATFLICYGLFRVSLEGVRNPDHGMPNFPLGLTMGMILSIPMLAVGVWLLWRALREPVPPPLAEDHEPA
|
Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
|
B0T8A6
|
Q2MY55
|
PATD3_SOLTU
|
Patatin group D-3
|
Solanum
|
MATTKSFLILIVMILATTSSTFASLEEMVTVLSIDGGGIKGIIPGTILEFLEGQLQKMDNNADARLADYFDVIGGTSTGGLLTSMITTPNENNRPFAAANEIVPFFFEHGPHIFNSSTGQFFGPKYDGKYLMQVLQENLGETRVHQALTEVAISSLDIKTNKPVIFTKSNLAKSPELDAKMYDICYSTAAAPTYFPPHYFTTNTINGDKYEFNLVDGAVATVADPALLSISVATRLAEKDPAFASIRSLNYKKMLLLSLGTGTTSEFDKTYTAEETAKWGAIQWMLVIQRMTDAASSYMTDYYLSTVFQAQNSQKNYLRVQENALTGTTTEMDDASEANMESLVQVGENLLKKPVSKDNPETYEEALKRFAKLLSDRKKLRANKASY
|
Probable lipolytic acyl hydrolase (LAH), an activity which is thought to be involved in the response of tubers to pathogens.
|
Q2MY55
|
Q0THN1
|
ASR_ECOL5
|
Acid shock protein
|
Escherichia
|
MKKVLALVVAAAMGLSSAAFAAETATTPAPTATTTKAAPAKTTHHKKQHKAAPAQKAQAAKKHHKNAKAEQKAPEQKAQAAKKHAKKHSHQQPAKPAAQPAA
|
Required for growth and/or survival at acidic conditions.
|
Q0THN1
|
Q1QV43
|
SYS_CHRSD
|
Seryl-tRNA(Ser/Sec) synthetase
|
Chromohalobacter
|
MLDPKLLRSDLPLVAERLARRGFTLDTARLEALESRRRELQTETERLQNERNTRSKAIGQAKASGEDIQPLLDEVSDLGERLDAAKARLAEVQAEWDESVAALPNLPHDSVPQGLDEADNVELHRWGTPGTFDFEVRDHVDLGAKFGYLDFEMAAKLTGSRFAVMRGPIARLHRALAQFMLDKQTREHGYEECYVPYIVNDASLTGTGQLPKFGEDLFKLEGDHDFYLIPTAEVPLTNIAREQIFTPAELPLKLTAHTPCFRSEAGAYGRDTRGMIRQHQFDKVEMVQIVDPATSYDALESMRGHAEAILQALELPYRVVTLCAGDMGFGAAKTYDLEVWLPSQETYREISSISNCEDFQARRMQARMRHPEQKKPQLVHTLNGSGLAVGRCLLAVLENCQQADGSIVIPEVLRGYMDGVERINA
|
Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).
|
Q1QV43
|
O49741
|
GATA2_ARATH
|
GATA transcription factor 2
|
Arabidopsis
|
MDVYGLSSPDLLRIDDLLDFSNEDIFSASSSGGSTAATSSSSFPPPQNPSFHHHHLPSSADHHSFLHDICVPSDDAAHLEWLSQFVDDSFADFPANPLGGTMTSVKTETSFPGKPRSKRSRAPAPFAGTWSPMPLESEHQQLHSAAKFKPKKEQSGGGGGGGGRHQSSSSETTEGGGMRRCTHCASEKTPQWRTGPLGPKTLCNACGVRFKSGRLVPEYRPASSPTFVLTQHSNSHRKVMELRRQKEVMRQPQQVQLHHHHHPF
|
Transcriptional activator that specifically binds 5'-GATA-3' or 5'-GAT-3' motifs within gene promoters. May be involved in the regulation of some light-responsive genes.
|
O49741
|
O66131
|
GLPK_THETH
|
Glycerokinase
|
Thermus
|
MNQYMLAIDQGTTSSRAILFNQKGEIVHMAQKEFTQYFPQPGWVEHNANEIWGSVLAVIASVLSEAQVKPEQVAGIGITNQRETTVVWEKDTGNPIYNAIVWQSRQTAGICDELKAKGYDPLFRKKTGLLIDAYFSGTKVKWILDHVDGARERAERGELLFGTIDTWLIWKLSGGRVHVTDYSNASRTLMFNIHTLEWDDELLDILGVPKAMLPEVRPSSEVYAKTAPYHFFGVEVPIAGAAGDQQAALFGQACFTEGMAKNTYGTGCFMLMNTGEKAVASKHGLLTTIAWGIDGKVEYALEGSIFVAGSAIQWLRDGLRMIKTAADSETYAEKVESTDGVYVVPAFIGLGTPYWDSEVRGAVFGLTRGTTKEHFIRATLESLAYQTKDVLAVMEADSGISLTTLRVDGGAVKNNFLMQFQSDLLAVPVERPVVNETTALGAAYLAGLAVGYWNSRDDIAAQWQLERRFEPKMDDDKRTMLYDGWKKAVRAAMAFK
|
Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate.
|
O66131
|
B7GH89
|
ISPG_ANOFW
|
1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase
|
Anoxybacillus
|
MSEIIHRSKTRPVRVGNITIGGNNEVVIQSMTTTKTHDVDATVAQIHRLEEAGCQIVRVACPDERAADAIAEIKKRINIPLVVDIHFDYRLALKAIENGADKIRINPGNIGKREKVEAVVKAAKERGVPIRIGVNAGSLEKRILDKYGYPTADGMVESALHHIRILEDLDFQDIIVSLKASDVRLAIEAYEKAARAFDYPLHLGITESGTLFAGTVKSAAGLGAILSKGIGNTVRVSLSADPVEEVKVARELLKAFGLAANAATLISCPTCGRIEIDLISIANEIEEYIAQIKAPIKVAVLGCAVNGPGEAREADIGIAGARGEGLLFRHGKIVRKVPEETMVEELKKEIDKLAEEYASKGKQK
|
Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.
|
B7GH89
|
P0DMJ0
|
AMP4_HETSP
|
Antimicrobial peptide HsAp4
|
Heterometrus
|
MSRRRILILVLVTMLVKTMAGMESKWVETTYEIKKRSGTSEKERESGRLLGVVKRLIVGFRSPFRGRRAISEQT
|
Possesses antimicrobial activity against both Gram-negative and Gram-positive bacteria, as well as against the fungus C.tropicalis. Also possesses a relatively high hemolytic activity.
|
P0DMJ0
|
Q8NER1
|
TRPV1_HUMAN
|
Vanilloid receptor 1
|
Homo
|
MKKWSSTDLGAAADPLQKDTCPDPLDGDPNSRPPPAKPQLSTAKSRTRLFGKGDSEEAFPVDCPHEEGELDSCPTITVSPVITIQRPGDGPTGARLLSQDSVAASTEKTLRLYDRRSIFEAVAQNNCQDLESLLLFLQKSKKHLTDNEFKDPETGKTCLLKAMLNLHDGQNTTIPLLLEIARQTDSLKELVNASYTDSYYKGQTALHIAIERRNMALVTLLVENGADVQAAAHGDFFKKTKGRPGFYFGELPLSLAACTNQLGIVKFLLQNSWQTADISARDSVGNTVLHALVEVADNTADNTKFVTSMYNEILMLGAKLHPTLKLEELTNKKGMTPLALAAGTGKIGVLAYILQREIQEPECRHLSRKFTEWAYGPVHSSLYDLSCIDTCEKNSVLEVIAYSSSETPNRHDMLLVEPLNRLLQDKWDRFVKRIFYFNFLVYCLYMIIFTMAAYYRPVDGLPPFKMEKTGDYFRVTGEILSVLGGVYFFFRGIQYFLQRRPSMKTLFVDSYSEMLFFLQSLFMLATVVLYFSHLKEYVASMVFSLALGWTNMLYYTRGFQQMGIYAVMIEKMILRDLCRFMFVYIVFLFGFSTAVVTLIEDGKNDSLPSESTSHRWRGPACRPPDSSYNSLYSTCLELFKFTIGMGDLEFTENYDFKAVFIILLLAYVILTYILLLNMLIALMGETVNKIAQESKNIWKLQRAITILDTEKSFLKCMRKAFRSGKLLQVGYTPDGKDDYRWCFRVDEVNWTTWNTNVGIINEDPGNCEGVKRTLSFSLRSSRVSGRHWKNFALVPLLREASARDRQSAQPEEVYLRQFSGSLKPEDAEVFKSPAASGEK
|
Ligand-activated non-selective calcium permeant cation channel involved in detection of noxious chemical and thermal stimuli. Seems to mediate proton influx and may be involved in intracellular acidosis in nociceptive neurons. Involved in mediation of inflammatory pain and hyperalgesia. Sensitized by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases, which involves PKC isozymes and PCL. Activation by vanilloids, like capsaicin, and temperatures higher than 42 degrees Celsius, exhibits a time- and Ca(2+)-dependent outward rectification, followed by a long-lasting refractory state. Mild extracellular acidic pH (6.5) potentiates channel activation by noxious heat and vanilloids, whereas acidic conditions (pH <6) directly activate the channel. Can be activated by endogenous compounds, including 12-hydroperoxytetraenoic acid and bradykinin. Acts as ionotropic endocannabinoid receptor with central neuromodulatory effects. Triggers a form of long-term depression (TRPV1-LTD) mediated by the endocannabinoid anandamine in the hippocampus and nucleus accumbens by affecting AMPA receptors endocytosis.
|
Q8NER1
|
A8LE19
|
METK_FRASN
|
Methionine adenosyltransferase
|
unclassified Frankia
|
MATRLFTSESVTEGHPDKIADQVSDSILDAMLKDDPKSRVAVETMITTGQVHVAGEVTTKTYVDIASVVRERILEIGYDSSKKGFDGASCGVSVSIGSQSPDIAQGVDTAHEARVEGSTEDDLDRQGAGDQGLMFGFACDETPELMPLPIALAHRLARRLSAVRKDGQVGYLRPDGKTQVTIEYEDGKPVRLDTVVVSSQHAADIDLDTLLAPDVAEYVVEPELALLEISTEGRRLLVNPTGRFEIGGPMGDAGLTGRKIIVDTYGGYARHGGGAFSGKDPSKVDRSAAYAMRWVAKNVVAAGLASRCEVQVAYAIGKAHPVGLFVETFGTGKVPDAQIQDAVTQVFDLRPAAIVRDLDLLRPIYAQTAAYGHFGRPELDFTWEATSRADALTAAVKG
|
Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme.
|
A8LE19
|
Q5F6I7
|
NADA_NEIG1
|
Quinolinate synthase
|
Neisseria
|
MQTAARRSFDYDMPLIQTPTSACQIRQAWAKVADTPDHETAGRLKDEIKVLLKRKNAVLVAHYYVDPLIQDLALETGGCVGDSLEMARFGAEHEAGTLVVAGVRFMGESAKILCPEKTVLMPDLEAECSLDLGCPEEAFSAFCDQHPDRTVAVYANTSAAVKARADWVVTSSVALEIVSYLKSRGEKLIWGPDRHLGDYIRRETGADMLLWQGSCIVHNEFKGQELAALKAEHPDAVVLVHPESPQSVIELGDVVGSTSKLLKAAVSRPEKKFIVATDLGILHEMQKQAPDKEFIAAPTAGNGGSCKSCAFCPWMAMNSLGGIKHALTGGRNEILLDRKLGEAAKLPLQRMLDFAAGLKRGDVFNGMGPA
|
Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate.
|
Q5F6I7
|
Q0K9V9
|
ALR_CUPNH
|
Alanine racemase
|
Cupriavidus
|
MPRPIHAVIHQPALANNLDIIRGKAPESRIWAVVKANAYGHGIRRVFAALRGADGFGLLDLNEAVLLRDLGWQGPILLLEGFFQPQDVAVIEQYRLTTAIHCDEQLRMLESARAKGPLAIQLKLNTGMNRLGFHPAAYRTAWERARAMPCVGSIVHMTHFSDADSARGVAHQIEAFDAATANLPGEASLSNSAAVLWHPQAHRAWVRPGIILYGASPTGRDADIAGTGLQPAMSLHSELISVQDLQPGDTVGYGSLFTAERPMRIGVVACGYADGYPRHASGWGEQRAPVLVDGVRTELVGRVSMDMLCVDLTPCPKARVGSPVTLWGQGLPIDEVAQASGTVGYELMCALAPRVPTSVATITASDSAAPAVA
|
Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
|
Q0K9V9
|
O75817
|
POP7_HUMAN
|
Ribonucleases P/MRP protein subunit POP7 homolog
|
Homo
|
MAENREPRGAVEAELDPVEYTLRKRLPSRLPRRPNDIYVNMKTDFKAQLARCQKLLDGGARGQNACSEIYIHGLGLAINRAINIALQLQAGSFGSLQVAANTSTVELVDELEPETDTREPLTRIRNNSAIHIRVFRVTPK
|
Component of ribonuclease P, a ribonucleoprotein complex that generates mature tRNA molecules by cleaving their 5'-ends . Also a component of the MRP ribonuclease complex, which cleaves pre-rRNA sequences .
|
O75817
|
A0A0G3F8Z3
|
TBO1_TIBOB
|
Omega-Tbo-IT1
|
Tibellus
|
MKKTFCFILILVCIVLKSVNAEEEDNFEESSLEMETARCASKNERCGNALYGTKGPGCCNGKCICRTVPRKGVNSCRCM
|
Insect-specific toxin that probably acts as an inhibitor of presynaptic insect calcium channels, presumably Cav2 subtype. In vivo, induces immediate paralysis on insects, followed by death when high doses are injected.
|
A0A0G3F8Z3
|
F9UT68
|
LPDD_LACPL
|
Gallate decarboxylase subunit D
|
Lactiplantibacillus
|
MATFTTEQAGYQMQAILQVIGYDLLIVVTGGTNPHIGDVTTLTASTVPETVKFPSHDGRFHKDNFISERMAKRIQRYLAGSCTITAGIHVNQITKAQIAAAAPMTDDLSRQIISWLQAHPVQAEKPEYYGQDEQPR
|
Probably involved in tannin degradation, however the precise biochemical function in metabolism of gallate is unknown.
|
F9UT68
|
Q849R0
|
SEPB_PSEP1
|
Probable efflux pump membrane transporter SepB
|
Pseudomonas
|
MSRFFIDRPIFAWVLAIIAMLAGALSLTKMPISQYPNIAAPAVSIQVVYPGASAKTVQDTVVQVIEQQLNGLDGFRYMAAESASDGSMNIIVTFEQGTNPDIAQVQVQNKLQLATPRLPEEVQRQGLRVVKYQMNFFMVVGLVDKTGKMTNFDLGNLIASQLQDPISRINGVGDFLLFGSPYAMRIWLDPGKLNSYQLTPGDVAQAIREQNVQVSSGQLGGLPTRSGVQLNATVVGKTRMTTPAEFEEILVKVKADGSQVRVKDLGRVVLASENFAISAKYRGQDSAGLGLRLASGGNLLETVKAVKAELEKQKAYLPEGVEVIYPYDTSPVVEASIDSVVHTILEAVVLVFLVMFLFLQSLRATIIPTLAVPVVLLAAFALLPYFGISINVLTMYAMVLAIGLLVDDAIVVVENVERLMHDEGLSPLEATRKSMGQISGALVGIGMVLSAVFVPMAFFGGSAGIIYKQFAVTIVICMSLSVLVALIFTPALCATILKAPENDAHHEKKGFFGWFNRSFDRNSARFERGVGGILKHRGRYLLIFALITAGTGYLFTQIPKAFLPSEDQGLMMTEVRMPLNASAERTEVVLQEVKDYLLKEEGQLVDHVMTVNGFNFAGRGQNSGLVLVVLKDWAARQAAGEDVLSVAERANARFARIKDATVMAFVPPAVLEMGNAMGFDLYLQDNLGLGHESLMAARNQFLELAAENPSLRAVRPNGKDDEPQFQVKIDDEKARALQVSIASINDTMSAAWGSMYVNDFIDLGRVKRVYIQGVDSSRIAPEDFDKWYVRNALGEMVPFSAFATGEWIHGSPKLERYGGISAVNILGEPAPGFSTGDAMIAIAQIMQQLPSGIGLSYNGLSYEEIRTGDQAPMLYALTVLIVFLCLAALYESWSVPMSVILVVPLGIFGAVLATLWRGLEADVYFQVGLMTTVGLSAKNAILIIEFAKELYEKEGVPLVKAAIEAARLRLRPIIMTSLAFTFGVLPMARATGAGAGSQHSIATGVVGGMITATVLAVFFVPLFYVVVVKVFERNKKPAALAEEELA
|
Probable membrane transporter component of the SepABC efflux pump with unknown specificity.
|
Q849R0
|
Q0TKN7
|
ACPH_ECOL5
|
Acyl carrier protein phosphodiesterase
|
Escherichia
|
MNFLAHLHLAHLAESSLSGNLLADFVRGNPEESFPPDVVAGIHMHRRIDVLTDNLPEVREAREWFRNETRRVAPITLDVMWDHFLSRHWSQLSPDFPLQEFTCYAREQVMTILPDSPPRFINLNNYLWSERWLVRYRDMDFIQSVLNGMASRRPRLDALRDSWYDLDAHYDALETRFWQFYPRMMEQASRKAL
|
Converts holo-ACP to apo-ACP by hydrolytic cleavage of the phosphopantetheine prosthetic group from ACP.
|
Q0TKN7
|
B1L1I1
|
G6PI_CLOBM
|
Phosphohexose isomerase
|
Clostridium
|
MKNSLSLDLTKTKPYVEEHEIQYLESIIREMDNTLGKKTGPGNKFLGWMDLPINYNKEEFARIKKAAEKIKNTCDVFIVIGIGGSYLGSRAAIEMISNTFYNNLDKSQRKVPQIYFAGNNISSTYMADLLELVKDKDICVNVISKSGTTTEPAIAFRIFKELLENKYGKEGAKERIFATTDAAKGALRTLADSEGYETFVIPDDVGGRFSVLTPVGLLPIAASGIDIDEMMKGAADARQEYSSDNIEKNHVYRYVAVRNALYRKGKTTEMLVNFEPCLHYFGEWWKQLYGESEGKDGKGIFPAAADFSTDLHSMGQYIQEGLRNIFETFINVENPRKSIMIKEDKENLDGLNFLAEKDMDYVNHQALRGTVLAHNDGGVPAIVLNVPELSAYYFGQLVYFFEKACGISGYLQGVNPFDQPGVEAYKKNMFALLGKPGHEDMKATLEERLK
|
Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
|
B1L1I1
|
Q43883
|
NIFB_TRIAZ
|
Radical SAM assemblase NifB
|
Trichormus
|
MTPPVTGSSVTESTPTKAKSGGCGCDTSTTVEMDEKLQERIAKHPCYSEEAHHHYARMHVAVAPACNIQCNYCNRKYDCANESRPGVVSELLTPEEAAHKVLVIAGKIPQMTVLGIAGPGDPLANPEKTFRTFELIADKAPDIKLCLSTNGLMLPEYVDRIKQLNIDHVTITLNTIDPEIGAQIYSWVHYKRRRYRGAEGARILLEKQMEGLQALREADILCKVNSVMIPGINDQHLVEVNKMIREQGAFLHNIMPLISAPEHGTHFGLTGQRGPSQKELKSVQDQCSGNMKMMRHCRQCRADAVGLLGEDRSQEFTKDKFLEMAPEYDFDKRQEVHEGIEKFRVELKVAKEKVLAGKEKTASNPKILVAIATKGGGLVNQHFGHAKEFQVYEVDGSEVRFVSHRKVDHYCQGGYGEEATFDNIVKTIADCKAVLVSKIGESPKEKLLQAGIQTVEAYDVIEKVALEFYEQWNKG
|
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.
|
Q43883
|
Q2P4Y6
|
PQQB_XANOM
|
Pyrroloquinoline quinone biosynthesis protein B
|
Xanthomonas
|
MRIIVLGSAAGGGHPQWNCHTPASLRAWQQADGAQRRTQASIAVSADGERWVLINASPDFRQQILATPALWPQQGLRHSPIKAVLLTSGEIDHIAGLLSMRESQPFALHASRRVLDLLAQNPIFDAVNPQYVSRQPFTLNAPLTVSGLQLTPFSVPGKVPLFMESRSGGDLAGSQEETLGLTIDDSQHRVHYIPGCAAMTDALRARLHGAELVFFDGTLWRDDEMVQLGISQKTGQRMGHMSIDGPEGTIAAFAPLNVARKIFIHLNTTNPVLNTQSPEFATARASGWEVAHDGLEIAL
|
May be involved in the transport of PQQ or its precursor to the periplasm.
|
Q2P4Y6
|
O54820
|
PAPS1_CAVPO
|
Adenylylsulfate 3'-phosphotransferase
|
Cavia
|
MELPGSLCKKAKLGHGAQSWGMQRATNVTYQAHHVSRNKRGQVVGTRGGFRGCTVWLTGLSGAGKTTVSMALGEHLVCHGIPCYTLDGDNIRQGLNKNLGFSPEDREENVRRIAEVAKLFADAGLVCITSFISPYTQDRNNARQIHEGASLPFFEVFVDAPLHVCEQRDVKGLYKKARAGEIKGFTGIDSEYEKPEAPELVLKTDACDVNDCVQQVVELLQERDIVPVDASYEVKELYVPENKLHLAKTDAESLPALQINKVDMQWVQVLAEGWATPLGGFMREREYLQCLHFDCLLDGGVINLSVPIVLTATEEDKERLDGCTAFALIYEGRRVAILRNPEFFEHRKEERCARQWGTTCKSHPYIKMVMEQGDWLIGGDLQVLDRIYWNDGLDQYRLTPTELKQKFKDMNADAVFAFQLRNPVHNGHALLMQDTHRQLLERGYRRPVLLLHPLGGWTKDDDVPLMWRMKQHAAVLEEGILNPESTVVAIFPSPMMYAGPTGVQWHCRARMVAGANFYIVGRDPAGMPHPETGKDLYKPTHGAKVLTMAPGLITLEIVPFRVAAYNKRKKRMDYYDAEHHEDFEFISGTRMRRLAREGQKPPEGFMAPTAWAVLAEYYKALEKA
|
Bifunctional enzyme with both ATP sulfurylase and APS kinase activity, which mediates two steps in the sulfate activation pathway. The first step is the transfer of a sulfate group to ATP to yield adenosine 5'-phosphosulfate (APS), and the second step is the transfer of a phosphate group from ATP to APS yielding 3'-phosphoadenylylsulfate (PAPS: activated sulfate donor used by sulfotransferase). In mammals, PAPS is the sole source of sulfate; APS appears to be only an intermediate in the sulfate-activation pathway. Required for normal biosynthesis of sulfated L-selectin ligands in endothelial cells.
|
O54820
|
P60105
|
RL11_VIBVY
|
50S ribosomal protein L11
|
Vibrio
|
MAKKVEAYIKLQVAAGMANPSPPVGPALGQRGVNIMEFCKAFNAKTESMEKGLPVPVVITVYSDRSFTFVTKTPPAAVLLKKAAGIKSGSGRPNTEKVGTVTDAQIQEIAEAKAADMTGADIEAMKRSIAGTARSMGLVVEG
|
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
|
P60105
|
A1U126
|
RECR_MARN8
|
Recombination protein RecR
|
Marinobacter
|
MAFSPLVDELVESLRCLPGVGQKTAQRMAFHLLERGRSGGTRLAAALNHAMDGVRRCDSCQNFSDTEICQICEKPERRNGTLCVVESPSDLLAIEQAGDYKGSYFVLMGHLSPIDGVGPEEIGIERLLDRVRREGVTELILATNPTVEGEATAHYIADRLDGQNILITRLAHGIPVGGELGYVDGFTLTHAFRGRKPLSE
|
May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO.
|
A1U126
|
P53545
|
GSC_CHICK
|
Homeobox protein goosecoid
|
Gallus
|
MPASMFSIDNILAARPRCKDSVLLPPSAPVVFPSLHGDSLYGAASDYGGFYSRAVAPGSALPAVGRSRLGYNNYYYGQLHVATSPVGPSCCGAVPPLGAQQCSCVPPAGYEGAGSVLMSPVPHQMLPYMNVGTLSRTELQLLNQLHCRRKRRHRTIFTDEQLEALENLFQETKYPDVGTREQLARKVHLREEKVEVWFKNRRAKWRRQKRSSSEESENAQKWNKASKTSPEKRQEDGKSDLDSDS
|
Involved in the development of the organizer region in the gastrula (Hensen node in chicken).
|
P53545
|
Q661E2
|
RL4_BORGP
|
50S ribosomal protein L4
|
Borreliella
|
MERKVFSKDGKEIGTINLDDRVFNIEISHGSIYNAIKNELSNLRVGTSSTKTRSEVRGSSKKPWKQKGTGRARVGTKRNPIWIGGGIALGPKPRDYSYRLPKKVKRLAFKSVLSLRAADENNFKVVENFNIESGKTKDLALIIKNFASFNGKVVILLGNDDQMIKRAGKNIRDLKILSFNKLRVVDLFYAKNLIALESAVNKLNEFYVK
|
Forms part of the polypeptide exit tunnel.
|
Q661E2
|
Q1Q8S2
|
RNPH_PSYCK
|
tRNA nucleotidyltransferase
|
Psychrobacter
|
MRIDNRELNQLRSISFERHYTKHAEGSVLVSFGDTKVLCTASVESGVPRWLKGKGKGWITAEYGMLPRATNTRNQREAARGKQSGRTQEIQRLIGRSLRAMIDLSKLGENTIYLDCDVLQADGGTRTASVTGAAIALIDALESIQKTKKLKADPLIGLVAAVSVGMKDGKAYLDLNYEEDASCDTDLNVVMTQKGEFIELQGTAEEKPFTRAQADDMLILAEKGIAELIAMQKTALGW
|
Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation.
|
Q1Q8S2
|
P28635
|
METQ_ECOLI
|
D-methionine-binding lipoprotein MetQ
|
Escherichia
|
MAFKFKTFAAVGALIGSLALVGCGQDEKDPNHIKVGVIVGAEQQVAEVAQKVAKDKYGLDVELVTFNDYVLPNEALSKGDIDANAFQHKPYLDQQLKDRGYKLVAVGNTFVYPIAGYSKKIKSLDELQDGSQVAVPNDPTNLGRSLLLLQKVGLIKLKDGVGLLPTVLDVVENPKNLKIVELEAPQLPRSLDDAQIALAVINTTYASQIGLTPAKDGIFVEDKESPYVNLIVTREDNKDAENVKKFVQAYQSDEVYEAANKVFNGGAVKGW
|
This protein is a component of a D-methionine permease, a binding protein-dependent, ATP-driven transport system.
|
P28635
|
B8CNX5
|
CMOA_SHEPW
|
Carboxy-S-adenosyl-L-methionine synthase
|
Shewanella
|
MKSSQDDLYAKPYQQVSDFQFDNKVAGVFNDMIRRSVPGYGQIINTIGDLAQKYATPNSKIYDLGCSLGAATLSVRRRVEGRNCQIIAVDNSESMIERCKENLSAYVSETPVKLVCGDIRDIEIENASLVILNFTMQFLAPEHRQSLLKKIYDGLQPGGLLVLSEKLYFEQDKIQSTLDDLHLDFKRANGYSELEISQKRSSLEHVMKPDTLEQHKIRIKQQGFSQFSVWFQCFNFASMVAIK
|
Catalyzes the conversion of S-adenosyl-L-methionine (SAM) to carboxy-S-adenosyl-L-methionine (Cx-SAM).
|
B8CNX5
|
Q473Q7
|
UREF_CUPPJ
|
Urease accessory protein UreF
|
Cupriavidus
|
MTPLRQLISLLHLASPALPIGGFSYSQGLEAAIDIGCVRDADTAERWIRDSLLYVQAQCEAPLWLLLHRGWQAMDVDAVREWNGWFHATRETAELRLETEQMGWSLAKLVGQMGWGGDALREHLAVISPVCLPTAFAATCVALEIDEREGLAAYCFNWAENQVAAAIKAVPLGQVAGQHMLRRLHEAVLMTVDEAVQRAAETPPRLSTFSPMLGLLSSRHETQYSRLFRS
|
Required for maturation of urease via the functional incorporation of the urease nickel metallocenter.
|
Q473Q7
|
Q4PSE6
|
LRX7_ARATH
|
Cell wall hydroxyproline-rich glycoprotein
|
Arabidopsis
|
MRIYQPTLLIFTTVVLLSISAVAPGGSRQLLYTRDDPITIPPYLIFENVRLERAYVALQAWKRAMISDPWNLTTNWFGSRVCDYNGVVCSESLDDPLVKTVSGVDLNQGDIAGHLPEELGLLTDIALFHVNSNRFCGTLPVGFSQLSLLFELDLSNNRFAGKFPEVVIGLPKLKYLDLRYNEFEGELPESLFDKDLDALFLNSNRFRSKIPVNMGNSPVSVLVLASNRFEGCIPPSFGKMGKTLNEIILMDNGLQSCIPNDMGLLQNVTVLDISYNWLVGELPKSMGQMENLEVLNVERNMLSGLIPDELCSLEKLRDFRYGSNYFTGEPATCRYLENYNYTMNCFKDVRDQRSMMECKMFLSKPVDCDSFKCSPGSSCFSPPPSQISPSSQPLAPAPSPTSPPLSTPPPARPCPPVYSPPPPPPLSLAPSMN
|
Modulates cell morphogenesis by regulating cell wall formation and assembly, and/or growth polarization.
|
Q4PSE6
|
Q66HD3
|
NASP_RAT
|
Nuclear autoantigenic sperm protein
|
Rattus
|
MATESTATAAIAAELVSADKVEDAPAPSTSADKMESLDVDSEAKKLLGLGQKHLVMGDIPAAVNAFQEAASLLGKKYGETANECGEAFFFYGKSLLELARMENGVLGNALEGVHVEEEEGEKTEDESLVENNDNVDEEAREELREQVYDAMGEKEAKKAEGQSLTKPETDKEQESEVEKGGREDMDISEPAEKLQEKVESTSKQLTESSEEAKEAAIPGLNEDEVTSGKTEQESLCTEEGKSISGVYVQNKEFREAVPQEEGEEMISLEKKPKETSEDQTIGAPEKQDTLMKVVEIEAEIDSEVKSVDVGGEEPKDQGAISESELGKAVLMQLSGQDVEVSPVVAAEAGSEVSEKPGQEITVLPNNGPVVGQSSAGDQTPSEPQNSAERLSETKDGASVEEVKAELVPEQEEAMPPVEESEAAGDGVETKVAQRATEKAPEDKFKIAANEETQERDEQMKEGEETEGSEEEDKENDKAEETTNESVLEKKTLQENEEEEIGNLELAWDMLDLAKIIFKRQETKEAQLYAAQAHLKLGEVSVESENYIQAVEEFQACLSLQEQYLEAHDRLLAETHYQLGLAYGYNSQYDEAVAQFGKSIDVIEKRMAVLLEQMKEAEGSFTEYEKEIEELKELLPEIREKIEDAKESQRSGNVAELALKATLVESSTSGFTPSGAGASVSMIASRKPTDGASSSNCVTDISHLVRKKRKPEEESPRKDDAKKAKPEPEVNGGSGDAVSSGNEVSENMEAEAENQAESQTTAEGTVDSAATVKSTAC
|
Required for DNA replication, normal cell cycle progression and cell proliferation. Forms a cytoplasmic complex with HSP90 and H1 linker histones and stimulates HSP90 ATPase activity. NASP and H1 histone are subsequently released from the complex and translocate to the nucleus where the histone is released for binding to DNA.
|
Q66HD3
|
A5GJG7
|
ACCA_SYNPW
|
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha
|
unclassified Synechococcus
|
MPRRPLLEFEKPLVELEQQIEQIRQRARDSEVDVSPQLHQLETLAARRREEIFKSLTPAQKIQVARHPHRPSTLDYIQMLCDDWVELHGDRRGSDDQALIGGIGRLGDRAVLLIGHQKGRDTKENVARNFGMATPGGYRKALRLMDHANRFGLPILSFIDTPGAYAGLLAEEQGQGEAIAVNLREMFRFRVPIIATVIGEGGSGGALGIGVADKLLMFEHSVYTVASPEACASILWRDAGKASEAASALKITGPDLLSLGVVDEVLPEPVGGNHWAPLEAGEILKEALTRNLEGLLQLSEDALREQRYRKFRAMGQFLDDLSPEALMAE
|
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.
|
A5GJG7
|
A8AF95
|
FLIT_CITK8
|
Flagellar protein FliT
|
Citrobacter
|
MTNFIPSLTDWHALHALSITMLDLAHSGKWDELIEQEMNYVQLVEGIARNPISPGNTFLINQAKEILNAVLRNEAELKTLLQHRMEELRQLIDQTGKQQSVSTTYGNLAGNILFPSNLNQ
|
Dual-function protein that regulates the transcription of class 2 flagellar operons and that also acts as an export chaperone for the filament-capping protein FliD. As a transcriptional regulator, acts as an anti-FlhDC factor; it directly binds FlhC, thus inhibiting the binding of the FlhC/FlhD complex to class 2 promoters, resulting in decreased expression of class 2 flagellar operons. As a chaperone, effects FliD transition to the membrane by preventing its premature polymerization, and by directing it to the export apparatus.
|
A8AF95
|
A6VH00
|
RS8_METM7
|
30S ribosomal protein S8
|
Methanococcus
|
MSLMDPLANALNHVSNCESVGKNVAYLKPASKLIGRVLNVMQDQGYIGNFEYIEDGKAGVYKVDLIGQINKCGAVKPRFAVKNHDFEKFEKRYLPAKGFGLLIVSTPKGLMTHDEARNAGVGGRLISYIY
|
One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit.
|
A6VH00
|
B7NEP6
|
SELA_ECOLU
|
Selenocysteinyl-tRNA(Sec) synthase
|
Escherichia
|
MTTETRSLYSQLPAIDRLLRDSSFLSLRDTYGHTRVVELLRQMLDEAREVIRDSQTLPAWCENWAQEVDARLTKEAQSALRPVINLTGTVLHTNLGRALQAEAAVEAVAQAMRSPVTLEYDLDDAGRGHRDRALAQLLCRITGAEDACIVNNNAAAVLLMLAATASGKEVVVSRGELVEIGGAFRIPDVMRQAGCTLHEVGTTNRTHANDYRQAVNENTALLMKVHTSNYSIQGFTKAIDEAELVALGKELDIPVVTDLGSGSLVDLSQYGLPKEPMPQELIAAGVSLVSFSGDKLLGGPQAGIIVGKKEMIARLQSHPLKRALRADKMTLAALEATVRLYLHPEALSEKLPTLRLLTRSAEVIQIQAQRLQAPLAAHYGAEFAVQVMPCLSQIGSGSLPVDRLPSAALTFTPHDGRGSHLESLAARWRELPVPVIGRIYDGRLWLDLRCLEDEQRFLEMLLK
|
Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis.
|
B7NEP6
|
Q137A8
|
QUEA_RHOPS
|
Queuosine biosynthesis protein QueA
|
Rhodopseudomonas
|
MRTELFDFDLPASSIALRPVSPRDAARMLVVRPGATLEDRAVRDLPALLQPGDQLVVNDTRVIAAQLTGRRIGRATEPRIEATLIKRLDGSRWQALVKPAKKLAEGDVVRFGHDGRVCLLGHLDATVEAKGDAGEVTLAFTFHGPALDQAIAELGATPLPPYIASKRTPDDQDAADYQTMFAANEGAVAAPTAGLHFTPELDAALKARGVTLHRLTLHVGAGTFLPVKVDDTAEHKMHAEWGTISEATADALNAARAQGGRIVAVGTTSLRLLESAAREDGTIAPFADETAIFITPGYRFRAVDALMTNFHLPRSTLFMLVSAFCGLETMQAAYRHAIDSGYRFYSYGDASLLFREPASR
|
Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
|
Q137A8
|
Q8TRS3
|
KAD_METAC
|
Adenylate monophosphate kinase
|
Methanosarcina
|
MNIILFGPPGAGKGTQAKKLVDFYGIPQISTGDILRANVREGTELGLAAKAYMDKGELVPDQVLIGIIKNRLNEADCEKGFILDGYPRTVPQADALEAILDEIEKPIDVVLNLEVPDEVLVGRISGRLMCKCGASYHIISNPPKKDNVCDICGGEVFQRADDTAEAVQNRLDVYKKQTQPLINYYKEKGILVTLDGTKEIDVVFEDLKAILAKFA
|
Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
|
Q8TRS3
|
C6E585
|
APT_GEOSM
|
Adenine phosphoribosyltransferase
|
unclassified Geobacter
|
MEDLKSIIRNIPDFPKKGILFKDITTLLGDAKSFQRMVDLLSHRYVGQKIDKVVGVEARGFIIGAALAYKLGAGIVLVRKPGKLPSQTRSKTYDLEYGTDTLEIHTDAFNKGDRVLIADDLLATGGTMAAVVDLISSMDVELVECCFMAELEFLEGGKKLPEGKVFSLLKF
|
Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
|
C6E585
|
Q0DIV0
|
HEMH2_ORYSJ
|
Protoheme ferro-lyase 2
|
Oryza sativa
|
MWSSSQASTRGVIEVGRVEAGPSHFPKRPAPRNSSRVNLSRTYAIKSCSVSSRTGLCLGQCYHKKSSACKCKLGWSSQPLSSLRHHLRVHSSASEAVLTSQSDFTKLLVGNEKIGVLLLNLGGPETLDDVQPFLFNLFADPDIIRLPRLFRFLQKPLAQFISVVRAPKSKEGYASIGGGSPLRQITDAQAEALRKALCDKDIPAKVYVGMRYWHPFTEEAIEQIKRDGITKLVVLPLYPQFSISTSGSSLRLLEGIFREDEYLVNMQHTVIPSWYQREGYIKAMATLIEKELRTFSEPQKVMIFFSAHGVPLAYVEEAGDPYKAEMEECVDLIMEELEKRGITNSCTLAYQSRVGPVEWLRPYTDETIIELGQKGVKSLLAVPISFVSEHIETLEEIDVEYKELALESGIKHWGRVPALGCEPTFITDLADAVIESLPYVGAMAVSNLEARQPLVPLGSVEELLAAYDSKRDELPPPVTVWEWGWTKSAETWNGRAAMLAVLALLVLEVTTGEGFLHQWGILPLFH
|
Catalyzes the ferrous insertion into protoporphyrin IX.
|
Q0DIV0
|
Q6G5A8
|
COAE_BARHE
|
Dephosphocoenzyme A kinase
|
Bartonella
|
MKIIGLTGSIAMGKSTVADFFRQAGISVFSADEAVYKLYKSEPTLSLIEYKFPGVFENGKVNRQKLSEILINDNEKLQTLEKIIHPLVQEKEKKFIDTARQQGEKLVVLDIPLLLETKGEKRVDSVVVVSAPLAIQKERAMIRQNMSEKKFAFINGRQMSDEKKRARADFIIDTGKDLENTREQVLFVIKSLLKN
|
Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
|
Q6G5A8
|
A3MRU1
|
RL11_BURM7
|
50S ribosomal protein L11
|
pseudomallei group
|
MAKKIVGFIKLQIPAGKANPSPPVGPALGQRGLNIMEFCKAFNAQTQGMEPGLPVPVVITAYADKSFTFVMKTPPATVLIKKAAKVDKGSSKPHTDKVGKITRAQAEEIAKTKMPDLTAADLDAAVRTIAGSARSMGITVEGV
|
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
|
A3MRU1
|
Q5RDJ2
|
ZMYM2_PONAB
|
Zinc finger protein 198
|
Pongo
|
MDTSSVGGLELTDQTPVLLGSTAMATSLTNVGNSFSGPANPLVSRSNKFQNSSVEDDDDVVFIEPVQPPPPSVPVVADQRTITFTSSKNEELQGNDSKITPSSKELASQKGSVSETIVIDDEEDMETNQGQEKNSSNFIERRPPETKNRTNDVDFSTSSFSRSKVNAGMGNSGITTEPDSEIQIANVTTLETGVSSVNDGQLENTDGRDMNLMITHVTSLQNTNLGDVSNGLQSSNFGVNIQTYTPSLTSQTKTGVGPFNPGRMNVAGDVFQNGESATHHNPDSWISQSASFPRNQKQPGVDSLSPVASLPKQIFQPSAQQQPTKPVKVTCANCKKPLQKGQTAYQRKGSAHLFCSTTCLSSFSHKPAPKKLCVMCKKDITTMKGTIVAQVDSSESFQEFCSTSCLSLYEDKQNPTKGALNKSRCTICGKLTEIRHEVSFKNMTHKLCSDHCFNRYRMANGLIMNCCEQCGEYLPSKGAGNNVLVIDGQQKRFCCQSCVSEYKQVGSHPSFLKEVRDHMQDSFLMQPEKYGKLTTCTGCRTQCRFFDMTQCIGPNGYMEPYCSTACMNSHKTKYAKSQSLGIICHFCKRNSLPQYQTTMPDGKLYNFCNSSCVAKFQALSMQSSPNGQFVAPSDIQLKCNYCKNSFCSKPEILEWENKVHQFCSKTCSDDYKKLHCIVTYCEYCQEEKTLHETVNFSGVKRPFCSEGCKLLYKQDFARRLGLRCVTCNYCSQLCKKGATKELDGVVRDFCSEDCCKKFQDWYYKAARCDCCKSQGTLKERVQWRGEMKHFCDQHCLLRFYCQQNEPNMTTQKGPENLHYDQGCQTSRTKMTGSAPPPSPTPNKEMKNKAVLCKPLTMTKATYCKPHMQTKSCQTDDTWKTEYVPVPIPVPVYIPVPMHMYSQNIPVPTTVPVPVPVPVFLPAPLDSSEKIPAAIEELKSKVSSDALDTELLTMTDMMSEDEGKTETTNINSVIIETDIIGSDLLKNSDPETQSSMPDVPYEPDLDIEIDFPRAAEELDMENEFLLPPVFGEEYEEQPRPRSKKKGAKRKAVSGYQSHDDSSDNSECSFPFKYTYGVNAWKHWVKTRQLDEDLLVLDELKSSKSVKLKEDLLSHTTAELNYGLAHFVNEIRRPNGENYAPDSIYYLCLGIQEYLCGSNRKDNIFIDPGYQTFEQELNKILRSWQPSILPDGSIFSRVEEDYLWRIKQLGSHSPVALLNTLFYFNTKYFGLKTVEQHLRLSFGTVFRHWKKNPLTMENKACLRYQVSSLCGTDNEDKITTGKRKHEDDEPVFEQIENTANPSRCPVKMFECYLSKSPQNLNQRMDVFYLQPECSSSTDSPVWYTSTSLDRNTLENMLVRVLLVKDIYDKDNYELDEDTD
|
May function as a transcription factor.
|
Q5RDJ2
|
O05137
|
MASZ_PSEFL
|
Malate synthase G
|
Pseudomonas
|
MTEHVQVGGLQVAKVLFDFVNNEAIPGTGITADQFWAGADKVIHDLAPKNKALLAKRDDFQARIDTWHQTHAGQAHDPVAYKAFLQDIGYLLPEAADFQASTQNVDDEIARMAGPQLVVPVMNARFALNASNARWGSLYDALYGTDAISEADGAEKGKGYNKVRGDKVIAFARAFLDEAAPLSAGSHVDSTGYKIADGKLIVSLKGGSNSGLRDDAQLIGFQGPAAQPIAILLKHNGLHFEIQIDASTPVGQTDAAGVKDVLMEAALTTIMDCEDSVAAVDADDKVVIYRNWLGLMKGDLAEEVAKGGKTFTRTMNPDRVYTGVDGQDVTLHGRSLLFVRNVGHLMTIDAILDKAGNEVPEGILDGLLTSLAAIHSLNGNSSRKNSRTGSVYIVKPKMHGPEEAAFTNELFGRIEDVLNLPRNTLKVGIMDEERRTTVNLKACIKAASERVVFINTGFLDRTGDEIHTSMEAGAMVRKAAMKTEKWIGAYENWNVDIGLSTGLQGRAQIGKGMWAMPDLMAAMLEQKIAHPLAGANTAWVPSPTAAALHALHYHKVDVFARQAELAKRERASVDDILTIPLAKNTDWSEEEIRNELDNNAQGILGYVVRWIDQGVGCSKVPDINDVGLMEDRATLRISSQHIANWLRHGVVTQDQVMESLKRMAPVVDRQNAGDALYRPLAPDFDSNIAFQAAVELVIEGTKQPNGYTEPVLHRKRREFKAKNGL
|
Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form malate and CoA.
|
O05137
|
O05940
|
DLDH_RHIEC
|
ORF-E3
|
Rhizobium
|
MAESYDVIIIGSGPGGYVAAIRASQLGLKTAIVEREHMGGICLNWGCIPTKALLRSAEVLDHANHFKDFGLVLEGSVKPDAKAVVGRSRAVSARLNAGVGFLMKKNKIDIIWGEAKLTKPGEIVVGKSSKPVVEPQHPLPKNVKGEGTYTAKHIIIATGARPRALPGIEPDGKLIWTYFEALKPDALPKSLIVMGSGAIGIEFASFYRSMGVDVTVVEVMPTIMPVEDAEITAIARKQLEKRGLKIFTSAKVTKVEKGAGSITAHVETSDGKVQQITADRMISAVGVQGNIENLGLEALGVKTDRGCVVADGYGKTNVAGIYAIGDVAGPPMLAHKAEHEGVVCVEKIAGLPNVHPTDKGKVPGCTYCNPQVASVGLTEAKAKELGRDIRVGRFSFAANGKAIALGEDQGMVKVIFDKKTGELLGAHMVGAEVTELIQGFVVAMNLETTEEELMHTIFPHPTVSETMKEAVLDAYGRVLNA
|
Lipoamide dehydrogenase is a component of the alpha-ketoacid dehydrogenase complexes.
|
O05940
|
Q0T8F9
|
CAIE_SHIF8
|
Carnitine operon protein CaiE
|
Shigella
|
MSYYAFEGLIPVVHPTAFVHPSAVLIGDVIVGAGVYIGPLASLRGDYGRLIVQAGANIQDGCIMHGYCDTDTIVGENGHIGHGAILHGCVIGRDALVGMNSVIMDGAVIGEESIVAAMSFVKAGFSGEKRQLLMGTPARAVRSVSDDELHWKRLNTKEYQDLVGRCHASLHETQPLRQMEENRPRLQGTTDVTPKR
|
Overproduction of CaiE stimulates the activity of CaiB and CaiD.
|
Q0T8F9
|
Q7ZAP3
|
PHNX_SALTY
|
Phosphonoacetaldehyde phosphonohydrolase
|
Salmonella
|
MNRIHAVILDWAGTTVDFGSFAPTQIFVEAFRQAFDVEITLAEARVPMGLGKWQHIEALGKLPAVDARWQAKFGRSMSAADIDAIYAAFMPLQIAKVVDFSSPIAGVIDTIAALRAEGIKIGSCSGYPRAVMERLVPAAAGHGYRPDHWVATDDLAAGGRPGPWMALQNVIALGIDAVAHCVKVDDAAPGISEGLNAGMWTVGLAVSGNEFGATWDAYQTMSKEDVAVRREHAASKLYAAGAHYVVDSLADLPGVIAHINARLAQGERP
|
Involved in phosphonate degradation.
|
Q7ZAP3
|
Q8IZ69
|
TRM2A_HUMAN
|
mRNA (uracil-5-)-methyltransferase TRMT2A
|
Homo
|
MSENLDNEGPKPMESCGQESSSALSCPTVSVPPAAPAALEEVEKEGAGAATGPGPQPGLYSYIRDDLFTSEIFKLELQNVPRHASFSDVRRFLGRFGLQPHKTKLFGQPPCAFVTFRSAAERDKALRVLHGALWKGRPLSVRLARPKADPMARRRRQEGESEPPVTRVADVVTPLWTVPYAEQLERKQLECEQVLQKLAKEIGSTNRALLPWLLEQRHKHNKACCPLEGVRPSPQQTEYRNKCEFLVGVGVDGEDNTVGCRLGKYKGGTCAVAAPFDTVHIPEATKQVVKAFQEFIRSTPYSAYDPETYTGHWKQLTVRTSRRHQAMAIAYFHPQKLSPEELAELKTSLAQHFTAGPGRASGVTCLYFVEEGQRKTPSQEGLPLEHVAGDRCIHEDLLGLTFRISPHAFFQVNTPAAEVLYTVIQDWAQLDAGSMVLDVCCGTGTIGLALARKVKRVIGVELCPEAVEDARVNAQDNELSNVEFHCGRAEDLVPTLVSRLASQHLVAILDPPRAGLHSKVILAIRRAKNLRRLLYVSCNPRAAMGNFVDLCRAPSNRVKGIPFRPVKAVAVDLFPQTPHCEMLILFERVEHPNGTGVLGPHSPPAQPTPGPPDNTLQETGTFPSS
|
S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the formation of 5-methyl-uridine in tRNAs and some mRNAs . Mainly catalyzes the methylation of uridine at position 54 (m5U54) in cytosolic tRNAs . Also able to mediate the formation of 5-methyl-uridine in some mRNAs .
|
Q8IZ69
|
Q74CG7
|
PANC_GEOSL
|
Pantoate-activating enzyme
|
Geobacter
|
MRIIDSVADMQAFSRDARRSGKTIALVPTMGYLHDGHASLMREGRTRADILVVSIFVNPTQFGPNEDFTTYPRDLERDLQVAEAAGADVIFAPRADDMYPAGFQTYVDVEKVTLPLCGASRPGHFRGVTTVVAKLFNIVMPHTAFFGKKDFQQLAVIRRMVADLNMDLSIVGMPIIREPDGLAMSSRNAYLGPQERTNALCLNRSLAAARTLFTDGERSVARLRDTVLRILTEVPGAAIDYADFRDSETLEPVEAANEKTLLALAVKIGTTRLIDNCVLGEEQ
|
Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
|
Q74CG7
|
A5CWV5
|
HTPG_VESOH
|
High temperature protein G
|
Candidatus Vesicomyosocius
|
MTIKQTHSFQTEVSQLLHLMIHSLYSNKEIFLRELISNASDAVDKLKFKSLSDDTLIEGKEALQIHIDVNKDANTITITDNGIGMSEVEVNKNIGTIANSGTKKFLKSLNETQAQDSNLIGQFGVGFYSSFIVSDKVEIITRKAGSKSKKGTKWASTGKGKYSIESIDRPDFGTSVILHIKKDEKEFLDDYRLRNIISKYSDHITVPIMMVKVSEDNKDIEYERINKANAFWAQDKQDLKQKDYDEFYKSLTYDLEAPLTQLHNRVEGNIDYTSLLFIPSKSPFDIWEPKRKGGIKLYAKRVFIMEDNEALMPLYLRFVKGVIDTADLSLNLSREILQDNKVIKAIRKASVKRILSVLEKMAKNKPEDYATFWQEFGMLMKEGVVEDTINKDKIAKLLRFTTNKSKNATQTVTLEHYIKNIQKDQKAIYYITAETYETAKGSPHLENFNQKNIEVLLLSDRVDEWMVSNFREFDGIQLKSIAKGNLEDFDSKEEKKAKEEVAKNFEIVIEKMQKILDSQVKEIKISSRLSESPSCLVADENEMGGNMERIMKSLGQDIPDTKPILEINPTHSLVKKLKTKIDEDLVKVLFDQAVLSEGGQLKDPAEFVKRINKLIN
|
Molecular chaperone. Has ATPase activity.
|
A5CWV5
|
Q62280
|
SSXT_MOUSE
|
Synovial sarcoma-associated Ss18-alpha
|
Mus
|
MSVAFAAPRQRGKGEITPAAIQKMLDENNHLIQCIMDYQNKGKASECSQYQQILHTNLVYLATIADSNQNMQSLLPAPPTQTMPMGPGGMSQSGPPPPPRSHNMPSDGMVGGGPPAPHMQNQMNGQMPGPNHMPMQGPGPSQLSMTNSSMNMPSSSHGSMGGYNHSVPSSQSMPVQNQMTMSQGQPMGNYGPRPNMNMQPNQGPMMHQQPPSQQYNMPPGGAQHYQGQQAPMGLMGQVNQGSHMMGQRQMPPYRPPQQGPPQQYSGQEDYYGDQYSHGGQGPPEGMNQQYYPDGHNDYGYQQPSYPEQGYDRPYEDSSQHYYEGGNSQYGQQQDAYQGPPPQQGYPPQQQQYPGQQGYPGQQQSYGPSQGGPGPQYPNYPQGQGQQYGGYRPTQPGPPQPPQQRPYGYDQGQYGNYQQ
|
Appears to function synergistically with RBM14 as a transcriptional coactivator. Component of SWI/SNF chromatin remodeling subcomplex GBAF that carries out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner.
|
Q62280
|
Q9ERJ6
|
GLHA_MERUN
|
Thyrotropin alpha chain
|
Meriones
|
MDYDRRYAAVILVVLSMFLHILHSLPDGDFIIQGCPECKLKENKYFSKGGAPIYQCMGCCFSRAYPTPARSKKTMLVPKNITSEATCCVAKSFTKATVMGNARVENHTECHCSTCYYHKS
|
Shared alpha chain of the active heterodimeric glycoprotein hormones thyrotropin/thyroid stimulating hormone/TSH, lutropin/luteinizing hormone/LH and follitropin/follicle stimulating hormone/FSH. These hormones bind specific receptors on target cells that in turn activate downstream signaling pathways.
|
Q9ERJ6
|
O42837
|
MTA1_SORMK
|
Mating type protein SmtA-1
|
Sordaria
|
MSSVDQIVKTFAKLPEGERNAAVNAILAMMPPGPGPVRQIPEPVSQAPAPKKKVNGFMGFRSYYSPLFSQFPQKARSPFMTILWQHDPFHNEWDFMCSVYSSIRNYLEQSNAQREKKITLQYWLHFAVPVMGVLGRENYLPTLGWDLVTMPNGTIDLMRIAMPLFRKNLQPMNGLCLFTKCQEGGLQVDNQHLVIAKLSDPSYDMIWFNKRPHYQQRHAVQADSSELGVSALFPRNHAVAAEADDVATLQLPHWMQQGDFGTESGYSPQFETLLGSILENGNATSNDSYNMALAMDVPMMGFNGGA
|
Required for mating.
|
O42837
|
Subsets and Splits
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