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
|
|---|---|---|---|---|---|---|
Q1LNM2
|
SSUD_CUPMC
|
FMNH2-dependent aliphatic sulfonate monooxygenase
|
Cupriavidus
|
MQVLWFIPTHGDSRYLGTSEGAREVSFDYLKQVAVAADTLGYDGVLIPTGRSCEDPWVVASALAAVTRKLRFLVALRPGLMTPTLAARMAATFDRVSNGRLLVNLVTGGDVAELEGDGLFLNHAERYEASAEFIRVWRDLLAASHENGEISFEGKHVTVKGARVLYPPIQRPHPPVYFGGSSEAAHDLAAEQVETYLTWGEPPADVAKKIADVRARAAKHGRTVRFGIRLHVIVRETDAAAWAAADELISKLDDQTVARAQAVFAKMDSEGQRRMAALHAGGTRRTREALEISPNLWAGVGLVRGGAGTALVGDPKTVAARIEEYAALGIDTFVLSGYPHLEEAYRFAELVFPLLPRKVRDKLPGQVLSGPFGEVMATGIVPIASQS
|
Catalyzes the desulfonation of aliphatic sulfonates.
|
Q1LNM2
|
A9SS00
|
MTND2_PHYPA
|
Acireductone dioxygenase (Ni(2+)-requiring) 2
|
Physcomitrium
|
MQVQRPPLEAWYMNDSEEDQRLPHHRNPPEYVTLEKLAALGVIHWVLDADNHETDPELSIIRKDRGYNYTDVITVCPEMLPSYEAKIKSFYEEHIHMDEEIRYCLDGSGYFDVRDPEDHWIRIWVRKGDMIVLPAGCYHRFTLDEHNYIMAMRLFVGEPIWTPYNRPQDEHPVRKGYVHQFLQPELLDVDMSISA
|
Catalyzes 2 different reactions between oxygen and the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) depending upon the metal bound in the active site. Fe-containing acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4-methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine in the methionine recycle pathway. Ni-containing acireductone dioxygenase (Ni-ARD) produces methylthiopropionate, carbon monoxide and formate, and does not lie on the methionine recycle pathway.
|
A9SS00
|
Q3J8Q8
|
RPOC_NITOC
|
Transcriptase subunit beta'
|
Nitrosococcus
|
MRDLLNLLKQQNQVEEFDSIRIGLASPDMIRAWSYGEVKKPETINYRTFKPERDGLFCAKIFGPVKDYECLCGKYKRLKHRGVICEKCGVEVTLAKVRRERMGHIELASPVAHIWFLKSLPSRISLLLDMTLRDIERVLYFEASVVIDPGMTPLERGQLLADEAYLQAIEEYGDEFDARMGAEAVQKMLKTLDLKGEAIRLREEITGTNSDTKIKKFSKRLKLIEAFIDSGNRSEWMILEVLPVLPPDLRPLVPLEGGRFATSDLNDLYRRVINRNNRLKRLLDLNAPDIIVRNEKRMLQESVDALLDNGRRGRAITGTNKLPLKSLADMIKGKQGRFRQNLLGKRVDYSGRSVIVVGPTLKLHQCGLPKKMALELFKPFIFGKLERAGLATTIKAAKKLVEREGPEVWDVLEEVIREHPVMLNRAPTLHRLGIQAFEPVLIEGKAIQLHPLVCVAFNADFDGDQMAVHVPLSLEAQLEARALMMSTNNILSPANGEPIIVPTQDVVLGLYYMTCERVNAKGEGMLFADINEVRRAYETSIAELHAKISVRITEIDPSKPEGEGETTRLVNTTVGRALLSELLPPGLPFELANKNMTKKEISRLVNICYRRLGLKTSVVFADRLMYLGFRQATLSGISIGVNDMVVPKEKQAILADAEEEVKEIEDQYASGLVTNGERYNKVVDIWSHTNDQVAKAMMERLGSEEVYDAKGNVVKQQTFNSIYMMADSGARGSAAQIRQLAGMRGLMAKPDGSIIETPITANFREGLDVLQYFISTHGARKGLADTALKTANSGYLTRRLVDVAQDLVVTKDDCGTTRGINITPFVEGGDVVEPLRERVLGRVLALNVYVPGSNEVAIPASTLLDESWVDYLETLGIDAVKVRSPITCETRYGICAACYGRDLGRGYRINIGEAIGVIAAQSIGEPGTQLTMRTFHIGGAASRTVTTDRIEVKYKGNIRLHNVKIVQHDSGKYVAVSRSGEVHIVDEQGRERERYKIPYGAELSAGDGDTVESGQVIATWAPHTHPVITEVAGKVRLQDFLEGSTVERQADEVTGLTSLTVLDPKQRGAAVKELRPMVKLVDETGSDLCLAGTDIPAHYYLPAGAVVSVEDEAMVGVGDVLARLPQESSKTRDITGGLPRVADLFEARKPKDPAVLAEISGTVSFGKETKGKQRLIITGSDGERHEELIPKWRQVNVFEGEHVEKGEAIVDGPPVPHDILRLRGVEELTYYIVNEVQEVYRLQGVKINDKHIEVIICQMLRKVEIIEPGDTSFLKGEQIDKPRLLEENEKMEKEDKLPARFEPVLLGITKASLATESFISAASFQETTRVLTEAAVTGKCDELRGLKENVIVGRLIPAGTGLAYHSERRRKRRMLEQPESLTADTGTSHYGEDEISESGAATA
|
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
|
Q3J8Q8
|
Q3AQ17
|
GCST_CHLCH
|
Glycine cleavage system T protein
|
Chlorobium
|
MKKTALYPCHEQSGAKIIDFGGYLMPVQYAGIIAEHKAVRSAAGLFDVSHMGNFFVKGSRALEFLQFVTTNDLAKVVDGQAQYNLMLYPSGGIVDDLIIYRMSADTFFLIVNASNADKDFAWLQQHIDQFEGVTLEDHTERLSLIALQGPLALSILNRLFPSIDGEALGSFHFCSASFNGFDVIIARTGYTGEKGVEMCVPNEAAIALWEALMAAGAADGIQPIGLGARDTLRLEMGYSLYGHEINQDTNPLEARLKWVVKMDKGHFIGKEACEQAMQHPQRTVIGFSLEGRALPRQGFTLYNSDRQAIGVVCSGTLSPTLQEPVGTCSVLREYGKPGTPILVEVRGAFHAGIIRSLPFVTNTSLA
|
The glycine cleavage system catalyzes the degradation of glycine.
|
Q3AQ17
|
P37754
|
6PGD9_ECOLX
|
6-phosphogluconate dehydrogenase, decarboxylating
|
Escherichia
|
MSKQQIGVVGMAVMGRNLALNIESRGYTVSVFNRSREKTEEVIAENPGKKLVPYYTVQEFVESLETPRRILLMVKAGSGTDSAIDSLKPYLDKGDIIIDGGNTFFQDTIRRNRELSAEGFNFIGTGVSGGEEGALKGPSIMPGGQKEAYELVAPILKQIAAVAEDGEPCVTYIGADGAGHYVKMVHNGIEYGDMQLIAEAYALLKGGLTLSNEELAQTFTEWNEGELSSYLYDITKDIFTKKDEEGKYLVDVILDEAANKGTGKWTSQSSLDLGEPLSLITESVFPRYISSLKDQRVAASKVLSGPQAQPAGDKAEFIEKVRRALYLGKIVSYAQGFSQLRAASDEYNWELNYAEIAKIFRAGCIIRAQFLQKITDAYAQNAGIANLLLAPYFKQIADDYQQALRDVVAYAVQNGIRVPTFSAAIAYYDSYRSAVLPANLIQAQRDYFGAHTYKRTDKEGVFHTEWLE
|
Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH.
|
P37754
|
A1RLU3
|
RLMM_SHESW
|
23S rRNA 2'-O-ribose methyltransferase RlmM
|
Shewanella
|
MKNLFLFCRAGFEKECAAEIQQRAGELNVGGFVKANNNDAYVVYQCFEDDAADTLVKQLPLDSLIFARQMFAASDLLVDLPENDRISPIVAALSDVSKAGEVRVETPDTNEAKELSAFCRKFTVPLRQHLKKSGSLLAQENPKRPIIHVCFIGPGRAYVGYSYSNNSSPHFMGIPRLKMAADAPSRSSLKLDEAFGQFVPKEEQEERIRSGMNAVDLGACPGGWTYQLVRRGMFVSAVDNGPMDEKLMETGQVKHYREDGFRFEPQRKNIYWLVCDMVEKPARVAELIEAWAINGWFKEAIFNLKLPMKSRYKEVTAILETMQTILKENGVTDFKVQCKHLYHDRDEVTVHLWLRPNTAWN
|
Catalyzes the 2'-O-methylation at nucleotide C2498 in 23S rRNA.
|
A1RLU3
|
P22186
|
MRAZ_ECOLI
|
Transcriptional regulator MraZ
|
Escherichia
|
MFRGATLVNLDSKGRLSVPTRYREQLLENAAGQMVCTIDIYHPCLLLYPLPEWEIIEQKLSRLSSMNPVERRVQRLLLGHASECQMDGAGRLLIAPVLRQHAGLTKEVMLVGQFNKFELWDETTWHQQVKEDIDAEQLATGDLSERLQDLSL
|
Negatively regulates its own expression and that of the subsequent genes in the proximal part of the division and cell wall (dcw) gene cluster. Acts by binding directly to DNA. May also regulate the expression of genes outside the dcw cluster.
|
P22186
|
P53843
|
IST1_YEAST
|
Increased sodium tolerance protein 1
|
Saccharomyces
|
MAPSMIPFTIKLKTCLKMCIQRLRYAQEKQQAIAKQSRRQVAQLLLTNKEQKAHYRVETLIHDDIHIELLEILELYCELLLARVQVINDISTEEQLVKEHMDDGINEAIRSLIYAILFVDEVKELSQLKDLMAWKINVEFVNGVIADHIDVPEKIIKKCSPSVPKEELVDLYLKEIAKTYDVPYSKLENSLSSSSSNISSDFSDPSGDIEDNDEEKPILALDNDDNDNADAKHPITVKKPRQNSENIKNELKIPKDIKKEVIEKKQSEKKTTKRKTKKEQENDELDELKKRFDALRRK
|
Involved in a late step in sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles. The lumenal sequestrated membrane proteins are targeted into the vacuole after fusion of the endosome with the vacuole. Regulates the recruitment of VPS4 to the ESCRT-III complex, probably in conjunction with DID2, and VPS4 catalyzes the disassembly of the ESCRT-III complex.
|
P53843
|
B2VH43
|
RF3_ERWT9
|
Peptide chain release factor 3
|
Erwinia
|
MSNAPFMQEVARRRTFAIISHPDAGKTTITEKVLLFGQAIQTAGTVKGRGSNQHAKSDWMEMEKQRGISITTSVMQFPYRGSLVNLLDTPGHEDFSEDTYRTLTAVDCCLMVIDAAKGVEDRTRKLMEVTRLRDTPILTFMNKLDRDIRDPMEVMDEVESELKIACAPITWPVGCGKLFKGVYHLYKDETYLYQSGKGHTIQEVRIVKGLGNPELDAAIGDELAAQLRDELELVQGASHEFDRDAFLNGKLSPVFFGTALGNFGVDHMLDGLVEWAPSPMPRNTDLRTVTATDEKFTGFVFKIQANMDPKHRDRVAFMRVVSGKYEKGMKLRQVRTGKDVVIADALTFMAGDRSHVEEAYPGDIIGLHNHGTIQIGDTFTQGENMKFTGIPNFAPELFRRIRLRDPLKQKQLLKGLVQLSEEGAVQVFRPVHNNDLIVGAVGVLQFDVVVARLKSEYNVEAIYEAINVSTARWVECDDVKKFDEFQRKNEINLALDGGDNLTYIAPTMVNLNITQERYPDVVFRKTREH
|
Increases the formation of ribosomal termination complexes and stimulates activities of RF-1 and RF-2. It binds guanine nucleotides and has strong preference for UGA stop codons. It may interact directly with the ribosome. The stimulation of RF-1 and RF-2 is significantly reduced by GTP and GDP, but not by GMP.
|
B2VH43
|
Q47LI8
|
RS12_THEFY
|
30S ribosomal protein S12
|
Thermobifida
|
MPTIQQLVRKGRKTKVSKNKTPALKGSPQRRGVCTRVYTTTPKKPNSALRKVARVRLSSQIEVTAYIPGVGHNLQEHSIVLVRGGRVKDLPGVRYRIVRGALDTQGVRNRKQARSRYGAKKEK
|
Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit.
|
Q47LI8
|
Q13TI1
|
RL24_PARXL
|
50S ribosomal protein L24
|
Paraburkholderia
|
MNKIRKGDEVIVITGKDKGKRGVVLSVGEGKVIVEGINLVKKHVKPNPMKGTTGGVEAKTMPLQISNVALVDANGKASRVGIKVEGDKKIRFLKTTGAELSA
|
One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.
|
Q13TI1
|
A1JMV3
|
MGSA_YERE8
|
Methylglyoxal synthase
|
Yersinia
|
MELTTRTIAARKHIALVSHDHCKKSLLEWVMQNRDLLSQHELYATGTTGNLVQKATGIDVHCLLSGPMGGDQEVGALISEKKIDILIFFWDPLNAVPHDPDVKALLRLATVWNIPVATNRSTADFLIDSALFSGEVTIAIPNYDRYLQQRLK
|
Catalyzes the formation of methylglyoxal from dihydroxyacetone phosphate.
|
A1JMV3
|
P35056
|
PEX5_YEAST
|
Peroxisomal protein PAS10
|
Saccharomyces
|
MDVGSCSVGNNPLAQLHKHTQQNKSLQFNQKNNGRLNESPLQGTNKPGISEAFISNVNAISQENMANMQRFINGEPLIDDKRRMEIGPSSGRLPPFSNVHSLQTSANPTQIKGVNDISHWSQEFQGSNSIQNRNADTGNSEKAWQRGSTTASSRFQYPNTMMNNYAYASMNSLSGSRLQSPAFMNQQQSGRSKEGVNEQEQQPWTDQFEKLEKEVSENLDINDEIEKEENVSEVEQNKPETVEKEEGVYGDQYQSDFQEVWDSIHKDAEEVLPSELVNDDLNLGEDYLKYLGGRVNGNIEYAFQSNNEYFNNPNAYKIGCLLMENGAKLSEAALAFEAAVKEKPDHVDAWLRLGLVQTQNEKELNGISALEECLKLDPKNLEAMKTLAISYINEGYDMSAFTMLDKWAETKYPEIWSRIKQQDDKFQKEKGFTHIDMNAHITKQFLQLANNLSTIDPEIQLCLGLLFYTKDDFDKTIDCFESALRVNPNDELMWNRLGASLANSNRSEEAIQAYHRALQLKPSFVRARYNLAVSSMNIGCFKEAAGYLLSVLSMHEVNTNNKKGDVGSLLNTYNDTVIETLKRVFIAMNRDDLLQEVKPGMDLKRFKGEFSF
|
Binds to the C-terminal PTS1-type tripeptide peroxisomal targeting signal (SKL-type) and plays an essential role in peroxisomal protein import.
|
P35056
|
Q1WUF0
|
HRCA_LIGS1
|
Heat-inducible transcription repressor HrcA
|
Ligilactobacillus
|
MLTERQLLILETIIRDYTDLGQPIGSKTLQEQLPIRVSSATIRNEMAVLEKQGFITKEHSSSGRIPSLKGYRYYVDNLVKPVKIDSKSVRSIQSLFGNEYRRVDEIIEMSAKILSDLTNYTAITLRPEASDLKLEGFRMVPLGNGQVMVILVASDGSVESQIYNLPNNIDGESLEAVIRLINDKLVGSSLSEVTSKLQELQPLLTKYIEKSDGFIDVFGGILDKAIKEQFYIGGRRNLLNFANGNNLEQIKSLYSLIDDESDKIGGLVDNTTNPHDHHGISVKIGDEMSDRLLLDYSLVSATYNVGSHGRGMIAILGPTNMPYSKMIGLVEVFQKELTKKLIDYYRNFDK
|
Negative regulator of class I heat shock genes (grpE-dnaK-dnaJ and groELS operons). Prevents heat-shock induction of these operons.
|
Q1WUF0
|
A4FZL0
|
AMPPA_METM5
|
Nucleoside monophosphate phosphorylase
|
Methanococcus
|
MLFLNAKFIDLDLGENAVIVNEEDLKGTSYYPQDRVLIESHAGSVIGNIYSTKTMVNKGEVGMLVSELAEISISEGEEVKLRHAEKPESIPFIKKKMDGQVLNPHEIRTIIDEIVSKKLSNIELSAFVSSTYINGMNMDEISEMTKRIAETGDMIAWEKSLVVDIHSIGGVPGNKYALLSIPILAAAGITVPKTSSRAITSPAGTADVMEVLTNVELKEEEIKRIVKTTNGCLAWGGGVNLAPADDIIINVERPVSIDPQPQLLASVMAKKIATGIKYTVIDIPVGKGVKIKNEAEGAKLARKFIELGESLNIKVECVLTYGGQPLGRAIGPALEAREAIEALQDPKNAPKSLIEKALSLAGILLELGGAAQIGEGQNLAWEILESGKALEKFNQIITEQGGTPKKPEEIELGDYVEEILAPIDGYITDISNTAITNVVKEAGAPRDKKAGILLNSKIGNKVKQGDVLYTIYSGSEERLVSAINLARRVYPVKVEGMLIERISKF
|
Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO.
|
A4FZL0
|
P27095
|
ACSA_METSH
|
Acyl-activating enzyme
|
Methanothrix
|
MLKLAGKEDKKLKTTVFQDETRIFNPPKELVEKSIVMQWMKKKGFKTEKEMRAWCSSDEHYLEFWDEMAKTYVDWHKPYTKVMDDSEMPYFHWFTGGEINITYNAVDRHAKGAKKDKVAYIWIPEPTDQPVQKITYGDLYKEVNKFANGLKSLGLKKGDRVSIYMPMIPQLPIAMLACAKLGVSHIVVFSGFSSKGLMDRAAHCGSRAIITVDGFYRRGKPVPLKPNADEAAGGAPSVEKIIVYKRAGVDVSMKEGRDVWWHDLVKGQSEECEPVWVDPEHRLYILYTSGTTGKPKGIEHATGGNAVGPAQTLHWVFDLKDDDVWWCTADIGWVTGHSYIVYAPLILGMTSLMYEGAADYPDFGRWWKNIQDHKVTVLYTAPTAVRMFMKQGAEWPDKYDLSSLRLLGSVGEPINPEAWMWYREHIGRGELQIMDTWWQTETGTFLNSPLPITPLKPGSCTFPLPGYDISILDEEGNEVPLGSGGNIVALKPYPSMLRAFWGDKERFMKEYWQFYWDVPGRRGVYLAGDKAQRDKDGYFFIQGRIDDVLSVAGHRIANAEVESALVAHPKIAEAAVVGKPDEVKGESIVAFVILRVGNEPSPELAKDAIAFVRKTLGPVAAPTEVHFVNDLPKTRSGKIMRRVVKARALGNPVGDISTLMNPEAVDGIPKIV
|
Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA.
|
P27095
|
B4EU19
|
RISB_PROMH
|
6,7-dimethyl-8-ribityllumazine synthase
|
Proteus
|
MNVIKGVVAAPNARVAIAIARFNNFINDSLLEGAVDALERIGQVSSENITVVWVPGAYELPLTVKALVESDKYDAVIALGTVIRGGTAHFEYVAGECSSGLSHVAMQSEIPVTFGVLTTESIEQAIERAGTKAGNKGAEAAMTALEMINVLKAIKG
|
Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
|
B4EU19
|
P30338
|
ARSR_STAAU
|
Arsenical resistance operon repressor
|
Staphylococcus
|
MSYKELSTILKILSDSSRLEILDLLSCGELCACDLLEHFQFSQPTLSHHMKSLVDNELVTTRKDGNKHWYQLNHAILDDIIQNLNIINTSNQRCVCKNVKSGDC
|
Transcriptional repressor for the ars operon. ArsR is a trans-acting regulatory protein which controls its own expression. The repressive effect of ArsR is alleviated by oxyions of +III oxidation state of arsenic, antimony, and bismuth, as well as arsenate (As(V)).
|
P30338
|
C5D367
|
ISPE_GEOSW
|
4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase
|
unclassified Geobacillus
|
MRLLVKAPAKINLSLDVLHKRPDGYHEVKMVMTTIDLADRIELIPQMDDTIQIISKNRFVPDDHRNLAYQAAKLLKDTFAIKQGIAISITKNIPVAAGLAGGSSDAAATLRGLNKLWNLGLTLDELAELGAKIGSDVSFCVYGGTAIATGRGEKITPIPAPPPCWVILAKPSIGVSTAEVYRNLKVDEIPHPDVDGMVEAIYRQDYAAICKLVGNVLEEVTLKKYPEVAHIKEQMKRFGADAVLMSGSGPTVFGLVQHDSRLQRIYNGLRGFCDQVFAVRILGERHSLD
|
Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
|
C5D367
|
Q1ACH0
|
PETD_CHAVU
|
17 kDa polypeptide
|
Chara
|
MGVTKKPDLTDPILRAKLAKGMGHNYYGEPAWPNDLLYIFPVVILGTIACTIGLAVLDPSMIGEPANPFATPLEILPEWYFFPVFQILRTVPNKLLGVLLMASVPVGLLTVPFLENVNKFQNPFRRPVATTVFLIGTAVAIWLGIGAALPIDKSLTLGLF
|
Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
|
Q1ACH0
|
Q3MIV0
|
KR221_HUMAN
|
Keratin-associated protein 22-1
|
Homo
|
MSFDNNYHGGQGYAKGGLGCSYGCGLSGYGYACYCPWCYERSWFSGCF
|
In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins.
|
Q3MIV0
|
Q608L6
|
GLGC_METCA
|
ADP-glucose synthase
|
Methylococcus
|
MPESMHASSRFVSRLTRQTLALILAGGRGSRLQKLTEWRAKPAVPFGGKFRIIDFPLSNCVNSGIRQVGVLTQYKADSLIRHIQQGWGFLRGELGEFIDIMPAQQRLQESWYAGTADAVYQNLDIIRQRDPEFIMILAGDHVYKMDYGLMLAYHVERKADLTIGCMEVPLADAKAFGVMQMDGEQRIRKFVEKPSDPPPMPNRPDHAAASMGIYIFNTAFLFEQLIKDADTPGSNHDFGMDIIPQVIQKYRVFAYRFRNAQSGVQAYWRDVGTVDSYWAANMELIGVDPELNLYDQEWPIWTYQAQTPPAKFVFDDDDRRGMAVDSMVSGGCIISGAEVRHSLLFSNVRVNSFSRVLDSVILPDVNIGRHCRISRAVIDKGCNIPPNTVIGENLEDDRKRFYVSPEGIVLVTPDCLGQRLHFHR
|
Involved in the biosynthesis of ADP-glucose, a building block required for the elongation reactions to produce glycogen. Catalyzes the reaction between ATP and alpha-D-glucose 1-phosphate (G1P) to produce pyrophosphate and ADP-Glc.
|
Q608L6
|
Q51404
|
FUMC2_PSEAE
|
Iron-independent fumarase 2
|
Pseudomonas
|
MTDTRIERDSMGELAVPATALYGAQTQRAVNNFPVSGQRMPQAFVRALLLAKAAAARANVSLQQLDAPMGEAIADTCLQLLQEDFMQHFPVDVFQTGSGTSSNMNANEVVATLASRRLGGKVNPNDHVNCGQSSNDIIPSTIHISAALEISERLLPALRHLEQTIQSKAGEVHAYVKTGRTHLMDAMPVRMSQVLGGWAQQVRQAGVHIESVLPALQQLAQGGTAVGTGINAHPRFAERFSQELNDLTGLAFRPGDDFFALIGSQDTAVAASGQLKTLAVTLMKLANDLRWMNSGPLAGLGEIELEALQPGSSIMPGKVNPVIPEATAMVAAQVIGNDAAIAVAGQSGNFELNVMLPLVADNLLHSIQLLANVSRLLADKAIASFKVNQGKLSEALARNPILVTALNPIIGYQKAAEIAKQAYREGRPIIDVALENTDLDRARLEVLLDPEKLTAGGL
|
Involved in the TCA cycle. Catalyzes the stereospecific interconversion of fumarate to L-malate.
|
Q51404
|
Q68XK6
|
NUSB_RICTY
|
Antitermination factor NusB
|
typhus group
|
MSTNKINKKSIARIAAVQALYQNILQNNYDMYDIMQNILACYHSNSIDLPKNFKISLSISHFKMLVKSVFENINKLDEIIDNHLTNDKDPVHMPILLRALLRVSICELLFCSTTPAKVVINEYTDIANDLLNEHEIGFVNSILDKIAQENNKIS
|
Involved in transcription antitermination. Required for transcription of ribosomal RNA (rRNA) genes. Binds specifically to the boxA antiterminator sequence of the ribosomal RNA (rrn) operons.
|
Q68XK6
|
Q8KIY4
|
CH10_STROR
|
Chaperonin-10
|
Streptococcus
|
MLKPLGDRVVLKIEEKEQTVGGFVLAGSAQEKTKTAQVVATGQGVRTLNGDLVAPSVKPGDRVLVEAHAGIDVKDGDEKYIIVGEANILAIIEE
|
Together with the chaperonin GroEL, 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. GroES binds to the apical surface of the GroEL ring, thereby capping the opening of the GroEL channel.
|
Q8KIY4
|
P29432
|
YIDD_BUCAP
|
Putative membrane protein insertion efficiency factor
|
Buchnera
|
MVKLSTIVVFCLTFFVSIYQNYISFFMPSNCRFYPTCSTYMILSLRKFGVIKGIILTILRLFKCHPLHQGGEDLVPLKIKDKSEY
|
Could be involved in insertion of integral membrane proteins into the membrane.
|
P29432
|
Q6AY80
|
NQO2_RAT
|
Quinone reductase 2
|
Rattus
|
MAGKKVLLVYAHQEPKSFNGSMKQVAVEELSKQGCTVTVSDLYTMNFEPRATRNDVTGALSNPEVFKYGIEAYEAYKKKALTSDILEEQRKVQEADLVIFQFPLYWFSVPAILKGWMDRVLCQGFAFDVPGFYDSGFLKDKLALLSFTTGGTAEMYTKAGVNGDFRYFLWPLQHGTLHFCGFKVLAPQISFGPEVSSEEQRKVMLASWVQRLKSIWKEEPIHCTPSWYFQG
|
The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinones involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis.
|
Q6AY80
|
Q13QI0
|
MHPA_PARXL
|
3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase
|
Paraburkholderia
|
MPASNDPVAASRRCETVSADVAIIGAGPVGLMIANYLGLQGVRVVVLEKLEQIIDYPRAIGLDDEALRVFQSVGLADVLLPHTTPDHWMRFVTHTGHCFASIEPRTDEFGWSRRNAFIQPLADRVLYEGLRRFPHVQVLFGTSVSGFTQDPAGVTIEADDEKGGRRTVRASYMVGADGGNSFVRRLLDVPFEGRTKPNQWIVVDVRNDPIGSPHIYMHCDPQRPYVSAALPHGIRRFEFMVMPGETEEELSKPENMAALIRKVVADPQKVDYIRKRVYTHNARLASTFRVDRVLLAGDAAHIMPVWQGQGYNSGIRDASNLGWKLAMVVKQLAGDALLDTYTAERRAHARSMIHLSEVAGDIFAPTSRFGIKFRDAFVRTFNVVPAMKRYFVEMRFKPMPRYETGVVLLAERKRKHGVMARVLERSGHSAPGRLLGLMSEKRESLLGRLVYGRDPSCHSPVGRMFIQPRVRTAEGSVVRLDDVLGSRFAIIGWGSDPTFGLSPLARETWQRLGGCFVLAKPDNQLDFHDDVPAGVIAIGDVQGRLKEWFARVPESVVLLRPDRFVAGMCTPQQVSDCIGELALKLSLKPAEQPAVKLAVPERAVAPESVAGVAAVAAVATRA
|
Catalyzes the insertion of one atom of molecular oxygen into position 2 of the phenyl ring of 3-(3-hydroxyphenyl)propionate (3-HPP) and hydroxycinnamic acid (3HCI).
|
Q13QI0
|
Q97BX2
|
RL22_THEVO
|
50S ribosomal protein L22
|
Thermoplasma
|
MKGYSMSVDENNARARIVEADISLKDAVNIAHHIRGMKLDYAKQILEDVVSKKYAIPYFRYLDSVSHRPGKGPGRYPVKAAKVFIDLLSNVENNAEFKGMNTDSLIIKHVAANKGRMIKKYTPKAYGRAGANFKDLINLEVIVTEGDQ
|
The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome.
|
Q97BX2
|
A8H8U2
|
PPNP_SHEPA
|
Xanthosine phosphorylase
|
Shewanella
|
MLAVNEYFEGQVKSISFAGADKPASVGVMEAGEYEFGTAAPEVMQVISGALTVLLPGQAEWQTFSAGEQFDVIGDAKFQVKVATQTAYLCIYG
|
Catalyzes the phosphorolysis of diverse nucleosides, yielding D-ribose 1-phosphate and the respective free bases. Can use uridine, adenosine, guanosine, cytidine, thymidine, inosine and xanthosine as substrates. Also catalyzes the reverse reactions.
|
A8H8U2
|
A5H453
|
PER42_MAIZE
|
Plasma membrane-bound peroxidase 3-1
|
Zea
|
MATSSGSCLIISLLVVVVAAALSASTASAQLSSTFYDTSCPSAMSTISSGVNSAVAQQARVGASLLRLHFHDCFIQGCDASILLNDTSGEQTQPPNLTLNPRAFDVVNSIKAQVEAACPGVVSCADILAVAARDGVVALGGPSWTVLLGRRDSTGSFPSQTSDLPPPTSSLQALLAAYSKKNLDATDMVALSGAHTIGQAQCSSFNGHIYNDTNINAAFATSLKANCPMSGGSSLAPLDTMTPTVFGNDYYKNLLSQKGLLHSDQELFNNGSTDSTVSNFASSSAAFTSAFTAAMVKMGNLGPLTGTSGQIRLTCWKLNSS
|
Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
|
A5H453
|
Q48965
|
PYRG_MYCCT
|
UTP--ammonia ligase
|
Mycoplasma
|
MAKFIFVTGGVVSGLGKGITASSIGALLKASGLKVFMQKFDPYLNVDPGTMSPYQHGEVFVTKDGGETDLDLGHYERFIDEELTKLSSTTSGKIYLSVIKGERKGDTSGKTIQVVPHITDAIKNKVYQAAKQSQADVIISEIGGTVGDIESQPFIEAIRQIRLEQGKENVMFVHVVLLLWLAASKEYKTKPIQNSVKAMASLGIQPDVIVCRSDSSSPKDIKEKISLFCNVPITNIIDAIDQDSIYRVPLALAKQNLQDIIIEQLQLKANAIDLTSWKQFNKKIDSSSQEIEISFVGKYIELQDAYLSVLESLKIAGWEFNKKIKIRWIQAETLNESNYNEILKNSQGILVPGGFGKRGIEGMMLASRYARDNDIPYLGICLGMQIATISIARDLLNWTDADSTEFNKNTTHPIFDYIKGIDRDNIGGTLRLGTMVTKLEKDSLVSKLYNSDVALERHRHRYEFNNKYKKDLESVGLRFSGIYEEKNLVEVIEMPSLKFFVASQFHPEFTSRPNKPTPLFKGFIKAIIENNK
|
Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.
|
Q48965
|
P30345
|
MERT_STRLI
|
Mercury ion transport protein
|
Streptomyces
|
MTPPPTQPGDRRGGLLGTLAVVGVALLPIICCAGPVLLASGALAGLGGVLVSPWLLAPAAVLLAGALTWWLRRRRTGNGDACCLPAPRTDQHDRDLLRKQ
|
Involved in mercuric transport. Passes a mercury ion from the MerP protein to the mercuric reductase MerA.
|
P30345
|
Q0C627
|
AROB_HYPNA
|
3-dehydroquinate synthase
|
Hyphomonas
|
MKTSSPLETVRVELGARAYDILVGHGALSELGPRLSQMLKRPRAFVLTDETVARHHKDALEAAVKSAGIRLDWLSLPPGEKTKSFSQLEGVLDWLLAGGADRGDTLIAFGGGVIGDMGGLAASLMKRGMGFVQVPTTLLAQVDSSVGGKTAVNTPRGKNLIGAFYQPRLVIADTALLATLPARELKAGYAEIVKYGLINDAAFFDWLAVNGQKVLALEPEAARYAVARSCAAKAAIVAEDETETGVRQLLNLGHTFGHAFEAANEYRENLLHGEAVALGMALAFRYGAASGITPAADAARVTEVLGASGLPVSLEGFDPARFAADRLAALMQQDKKARAGRVPLILARGIGAAYVHPDADLASVERFLASELA
|
Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
|
Q0C627
|
Q8FUL4
|
RECF_COREF
|
DNA replication and repair protein RecF
|
Corynebacterium
|
MYIRSLELRDFRSWPELKVELKPGITIFIGRNGFGKTNIVEAIGYLAHLSSHRVSTDAPLVRANAGDARISAVAVNQGRELAAHLLIKPHAANQGQINRTRVKSPRELLGVIKTVLFAPEDLALVRGEPAERRRYLDDIIATRRPRMAGVKADYDKVLKQRNALLKTATIALRRGYGTEEGAAALATLDTWDGQLARLGAEVMAARFALVQDLSSQIRDAYQTIAPESRPAAVNYKTTIDQGLAQFGEFDAGIIEATLLTELAAKRQREIERGMSLVGPHRDDLELHLGGQPAKGFASHGETWSFALSMRIAEFNLLRSDGTDPILILDDVFSELDAGRREKLVGIARDAEQVIITAAVSDDLPANLADAITARHTVTVRDTDAGRISLLDEQPDTQP
|
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.
|
Q8FUL4
|
A0Q2L2
|
TIG_CLONN
|
PPIase
|
Clostridium
|
MNTKIERVENNVVKLEITVEKEKFNEAIKKAYKKNVKRFNVPGFRKGKAPMNIITRYYGEGVFYEDAINTCCEEAYPMAVEEHNLQPVDYPKIDIVEIGSGKDFVFTAEVVTRPEVKLENYKGVEAKKNTYEVTDEDVEKQLNAMLEKNARIITKEEGAAVQKNDIAIIDFKGFVDGKAFEGGEATDYSLEIGTGTFIDNFEDQLVGLKVGEEKEVNVNFPEQYGREELNGKPAKFEVKIKEIKVKELPALDDEFAKEVSEFDTVDALKADLKTKLEEANKNREKVEYEEAVIEEVCNRAEVEIPEVMIEKEIDMMLKDLEMRLGYQGLDLASYYQYTNSSEAKVREYMKETAEKKVKTELVLEKIVKDEKIEATEEEIKERAKEMAQQYGGGQDADKLVEAIVGAQREVLARQLANEKAIDFLVENSKEIA
|
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.
|
A0Q2L2
|
O82233
|
IF4G2_ARATH
|
Eukaryotic translation initiation factor isoform 4G-2
|
Arabidopsis
|
MQQQGEPSVLSLRPGGGGGKSRLFVPRFSSSSSFDLTNGGSEETPFPVKRENSGERVRFSREEILQHRESVQVSDEILRRCKEIAVELFGEEQSWGNHAAESKITNHTQHRHTETDNRDWHSRSQIPTSGKEWLRDDPREAKSTWQGSGPTPVLIKAEVPWSAKRGALSDKDRVVKSVKGILNKLTPEKYELLKGQLIDAGITSADILKEVIQLIFENAILQPTFCEMYALLCFDINGQLPSFPSEEPGGKEITFKRVLLNNCQEAFEGAGKLKEEIRQMTNPDQEMERMDKEKMAKLRTLGNIRLIGELLKQKMVPEKIVHHIVQELLGDDTKACPAEGDVEALCQFFITIGKQLDDSPRSRGINDTYFGRLKELARHPQLELRLRFMVQNVVDLRANKWVPRREEVKAKKINEIHSEAERNLGMRPGAMASMRNNNNNRAAVSGAADGMGLGNILGRPGTGGMMPGMPGTRVMPMDEDGWEMARTRSMPRGNRQTVQQPRFQPPPAINKSLSVNSRLLPQGSGGLLNGGGRPSPLLQGNGSSSAPQASKPIPTVEKPQPRSQPQPQPQAAPLANSLNAGELERKTKSLLEEYFSIRLVDEALQCVEELKSPSYHPELVKETISLGLEKNPPLVEPIAKLLKHLISKNVLTSKDLGAGCLLYGSMLDDIGIDLPKAPNSFGEFLGELVSAKVLDFELVRDVLKKMEDEWFRKTVLNAVIKSVRECPSGQSVLDSQAVEVEACQSLL
|
Plays a role in the accumulation of some potyvirus during viral infection.
|
O82233
|
O08333
|
PFP_STRCO
|
Pyrophosphate-dependent 6-phosphofructose-1-kinase
|
Streptomyces albidoflavus group
|
MKVGVLTGGGDCPGLNAVIRAVVRKGVQEYGYDFTGFRDGWRGPLEGDTVPLDIPAVRGILPRGGTVLGSSRTNPLKQRDGIRRIKDNLAALGVEALITIGGEDTLGVATRLADEYGVPCVGVPKTIDNDLSATDYTFGFDTAVGIATEAIDRLHTTAESHMRVLVVEVMGRHAGWIALHSGLAGGANVILIPEQRFDVEQVCSWVTSRFRASYAPIVVVAEGAMPRDGDMVLKDESLDSYGHVRLSGVGEWLAKQIEKRTGNEARTTVLGHVQRGGTPSAFDRWLATRFGLHAVDCVHDGDFGKMVALRGTDIVRVPIAEATARLKTVDPALYEEVGVFFG
|
Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.
|
O08333
|
Q7NRZ0
|
RL9_CHRVO
|
50S ribosomal protein L9
|
Chromobacterium
|
MQIILLEKVANLGQLGDVVNVKNGFARNFLIPQGKAKRATEANLKEFDARRAELEAKQAEILADAKVRAEKLNEAVITIAQKAGVDGRLFGSVTNVDVAEAVTAFGVQIKRHEVRLPNGPFKAIGEYDIEIALHHDVVTPIKIVVVGEA
|
Binds to the 23S rRNA.
|
Q7NRZ0
|
Q60803
|
TRAF3_MOUSE
|
RING-type E3 ubiquitin transferase TRAF3
|
Mus
|
MESSKKMDAAGTLQPNPPLKLQPDRGAGSVLVPEQGGYKEKFVKTVEDKYKCEKCRLVLCNPKQTECGHRFCESCMAALLSSSSPKCTACQESIIKDKVFKDNCCKREILALQVYCRNEGRGCAEQLTLGHLLVHLKNECQFEELPCLRADCKEKVLRKDLRDHVEKACKYREATCSHCKSQVPMIKLQKHEDTDCPCVVVSCPHKCSVQTLLRSELSAHLSECVNAPSTCSFKRYGCVFQGTNQQIKAHEASSAVQHVNLLKEWSNSLEKKVSLLQNESVEKNKSIQSLHNQICSFEIEIERQKEMLRNNESKILHLQRVIDSQAEKLKELDKEIRPFRQNWEEADSMKSSVESLQNRVTELESVDKSAGQAARNTGLLESQLSRHDQMLSVHDIRLADMDLRFQVLETASYNGVLIWKIRDYKRRKQEAVMGKTLSLYSQPFYTGYFGYKMCARVYLNGDGMGKGTHLSLFFVIMRGEYDALLPWPFKQKVTLMLMDQGSSRRHLGDAFKPDPNSSSFKKPTGEMNIASGCPVFVAQTVLENGTYIKDDTIFIKVIVDTSDLPDP
|
Cytoplasmic E3 ubiquitin ligase that regulates various signaling pathways, such as the NF-kappa-B, mitogen-activated protein kinase (MAPK) and interferon regulatory factor (IRF) pathways, and thus controls a lot of biological processes in both immune and non-immune cell types . In TLR and RLR signaling pathways, acts as an E3 ubiquitin ligase promoting the synthesis of 'Lys-63'-linked polyubiquitin chains on several substrates such as ASC that lead to the activation of the type I interferon response or the inflammasome . Following the activation of certain TLRs such as TLR4, acts as a negative NF-kappa-B regulator, possibly to avoid unregulated inflammatory response, and its degradation via 'Lys-48'-linked polyubiquitination is required for MAPK activation and production of inflammatory cytokines . Alternatively, when TLR4 orchestrates bacterial expulsion, TRAF3 undergoes 'Lys-33'-linked polyubiquitination and subsequently binds to RALGDS, mobilizing the exocyst complex to rapidly expel intracellular bacteria back for clearance. Acts also as a constitutive negative regulator of the alternative NF-kappa-B pathway, which controls B-cell survival and lymphoid organ development . Required for normal antibody isotype switching from IgM to IgG . Plays a role T-cell dependent immune responses . Down-regulates proteolytic processing of NFKB2, and thereby inhibits non-canonical activation of NF-kappa-B. Promotes ubiquitination and proteasomal degradation of MAP3K14.
|
Q60803
|
Q0AEI0
|
DXR_NITEC
|
2-C-methyl-D-erythritol 4-phosphate synthase
|
Nitrosomonas
|
MTPIRHLTILGSTGSIGESTLDVVARHPDRFQAVALTADKNVEKMFEQCKRFYPSYAVMLNAQSAEQLEAKLRVAGLGTMVLSGIESLEKVASLPEIDTVMAAIVGAAGIRPTLSAAQAGKHILLANKETLVMAGRIFMDTIRQYHATLLPIDSEHNAIFQSLPQHYNGDLISSGVRRILLTASGGPFHKADLQTLSTVTPEQACAHPNWVMGRKISVDSATMMNKGLEVIEAHWLFNVEPEKIQVVVHPQSVIHSMVEYIDGSVLAQLGNPDMRTPIAHALGYPERIESGVQSMDIFKIAQLNFEAPDFERFPCLRLAYEALSKGGNMPAVLNAANEVAVEVFLAGKIPFTVIPAIIEHVMESIDRQEITDLEDVLAADLRARETARKWLDTQAWQRGQSGAPLFRAEQWNG
|
Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).
|
Q0AEI0
|
P30719
|
CH10_CLOAB
|
Chaperonin-10
|
Clostridium
|
MKIRPLGDRVVIKRLEAEETTKSGIVLPSSAKEKPQMAEVVAVGPGGVVDGKEIQMQVKTGDKVFFSKYSGTEIKVDNEELLILRQDDILGIVEE
|
Together with the chaperonin GroEL, 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. GroES binds to the apical surface of the GroEL ring, thereby capping the opening of the GroEL channel.
|
P30719
|
P04483
|
TETR2_ECOLX
|
Tetracycline repressor protein class B from transposon Tn10
|
Escherichia
|
MSRLDKSKVINSALELLNEVGIEGLTTRKLAQKLGVEQPTLYWHVKNKRALLDALAIEMLDRHHTHFCPLEGESWQDFLRNNAKSFRCALLSHRDGAKVHLGTRPTEKQYETLENQLAFLCQQGFSLENALYALSAVGHFTLGCVLEDQEHQVAKEERETPTTDSMPPLLRQAIELFDHQGAEPAFLFGLELIICGLEKQLKCESGS
|
TetR is the repressor of the tetracycline resistance element; its N-terminal region forms a helix-turn-helix structure and binds DNA. Binding of tetracycline to TetR reduces the repressor affinity for the tetracycline resistance gene (tetA) promoter operator sites.
|
P04483
|
Q00G37
|
KSL7_ORYSI
|
Ent-kaurene synthase-like 7
|
Oryza sativa
|
MMLLGSPSSGGYGGKFAGASPAGGTTTMAPSAKQPSSRAPPPGITGGRNDLRILSPAAAAAAVGGLEMKKPEAEGIAESLQATHRKELEASIRKQLQGVELSPSPYDTAWVAMVPLRGSSHNPSFPQCVDWILENQWDDGSWSIDGSISTANKDVLSSTLACVLALNKWNVGREHIRRGLSFIGRNFSIAMDDQAVAPIGFGITFPAMLTLANGSGLEVPVRQNDIDSLNHLREMKIQREAGNHSRGRKAYMAYLAEGFGNLLEWDEIMMFQRKNGSLFNCPSSTAGALANYHDDKALQYLQSLVNKFDGVVPTLYPLNIYCQLSMVDALENMGISQYFASEIKSILDMTYSSWLGRDEEIMLDVTTCAMAFRLLRMNGYDVSSDELSHVAGASGFRDSLQGYLNDRKSVLEVYKTSKHSISENDLILDSIGSWSGSLLKEMLCSNGIQGTPGREEIEFALKYPFYSTLERLVHRKNIVLFDAKGSQMLKTECMPVHDSQDFLALAVDDFCISQSNYQNELNYLESWVKDNRLDQLHFARQKITYCYLSGAATTFRPEMGYARTSWARTAWLTAVIDDLFDVGGLEQEQENLLALMEKWEEPGEDEYYSEDVKIVFQALYNTVNEIGAKASALQGHDVTKYLVDVWLHVVRCMKVEAEWQRSQHLPTFEEYMESGMVSLGQGATVMSALFLIGEKLPEGVVELEEYDEMFRLMGTCGRLLNDIRGIEREESDGKMTNGVSLLVHASGGSMSVDEAKTEVMKRIDASRRKLLSLVVGEQEGPIPRPCKQLFWKMCKILHLFYYQTDGFSSPKEMVSAVDAVIKEPLQLRSL
|
Involved in phytocassane phytoalexins biosynthesis. Catalyzes the conversion of ent-copalyl diphosphate to the phytoalexin precursor ent-cassa-12,15-diene.
|
Q00G37
|
P47397
|
RL3_MYCGE
|
50S ribosomal protein L3
|
Mycoplasma
|
MDVRGIFGVKVGMSQIFTEQNECLPITIVYCEANQVAGIKTIAKDNYNATLLSFQTVDEKQLNKPKQGFFSKLKLEPHKYLREIRKMQGFELGKKITPQELFKIGEYVDVTSLTKGRGFTGAIKRWNFKIGPLGHGAGYPHRFQGSVQAGRGGSSAQRVFKGKKMSGHYGHEQVTIQNLFIVGFDEINKLVLVSGAIAGPEGGIVLIKTAKKKTGKIKDIKLAVQTVKAPQLKAPKKQKTKVETNQVNPKIEEEKTK
|
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.
|
P47397
|
A8Y9G4
|
ATPI_LOLPR
|
F-ATPase subunit IV
|
Lolium
|
MNIIPCSIKTLKGLYDISGVEVGQHFYWQIGSFQIHAQVLITSWVVITILLGSVVIAVRNPQTVPMDGQNFFEYVLEFIRDLSKTQIGEEYGPWVPFIGTMFLFIFVSNWSGALLPWKIIELPHGELAAPTNDINTTVALALLTSAAYFYAGLSKKGLSYFEKYIKPTPILLPINILEDFTKPLSLSFRLFGNILADELVVVVLVSLVPLVVPIPVMFLGLFTSGIQALIFATLAAAYIGESMEGHH
|
Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
|
A8Y9G4
|
Q8CHJ0
|
PIGU_CRIGR
|
GPI transamidase component PIG-U
|
Cricetulus
|
MAAPLALVLVVAVTVRAALFRSSLAEFISERVEVVSPLSSWKRVVEGLSLLDLGVSPYSGAVFHETPLIIYLFHFLIDYAELVFMITDALTAIALYFAIQDFNKVVFKKQKLLLELDQYAPDVAELIRTPMEMRYIPLKVALFYLLNPYTILSCVAKSTCAINNTLIAFFILTTIKGSVFLSAIFLALATYQTLYPVTLFAPGLLYLLQRQYIPVKVKSKAFWIFSWEYAMMYIGSLVVIVCLSFFLLSSWDFIPAVYGFILSVPDLTPNIGLFWYFFAEMFEHFSLFFVCVFQINVFFYTVPLAIKLKEHPIFFMFIQIAIISIFKSYPTVGDVALYMAFFPVWNHLYRFLRNVFVLTCIIVVCSLLFPVLWHLWIYAGSANSNFFYAITLTFNVGQILLISDYFYAFLRREYYLTHGLYLTAKDGTEAMLVLK
|
Component of the GPI transamidase complex. May be involved in the recognition of either the GPI attachment signal or the lipid portion of GPI.
|
Q8CHJ0
|
Q32A65
|
FDHD_SHIDS
|
Sulfur carrier protein FdhD
|
Shigella
|
MKKTQQKEIENVTNITGVRQIELWRRDDLQHPRLDEVAEEVPVALVYNGISHVVMMASPKDLEYFALGFSLSEGIIESPRDIFGMDVVPSCNGLEVQIELSSRRFMGLKERRRALAGRTGCGVCGVEQLNDIGKPVQPLPFTQTFDLNKLDDALRHLNDFQPVGQLTSCTHAAAWMLPSGELVGGHEDVGRHVALDKLLGRRSQEGESWQQGAVLVSSRASYEMVQKSAMCGVEILFAVSAATTLAVEVAERCNLTLVGFCKPGRATVYTHPQRLSN
|
Required for formate dehydrogenase (FDH) activity. Acts as a sulfur carrier protein that transfers sulfur from IscS to the molybdenum cofactor prior to its insertion into FDH.
|
Q32A65
|
Q85FV4
|
RR17_CYAM1
|
30S ribosomal protein S17, chloroplastic
|
Cyanidioschyzon
|
MKKLLGLVVSCRMQKTVIVEVKTQVKHALYGKRIMKKKRYAVHDPEKKASLGELIWIRTCRPISKTKKWIYDSSANASQSSR
|
One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.
|
Q85FV4
|
A5V5Y5
|
RS5_RHIWR
|
30S ribosomal protein S5
|
Rhizorhabdus
|
MADETEIQAAAPAEAAPGAEGQGERRGRGGRGRGGNDRGGDRGRGRDGRGRRDDRRGSEEQGEELIEKLVHINRVSKTVKGGKRFGFAALVVVGDGKGRAGFGHGKAREVPEAISKATAAAKKAMVRVPLREGRTLHHDGNGHFGAGRVTVRTAPPGTGIIAGGPMRAIFESLGVADVVTKSVGTSNPYNMIRATFEALKDQTSPKSVSQRRGKKIADLLGRGGASAPVAEAEAAAITE
|
Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body.
|
A5V5Y5
|
B3Q851
|
LEUC_RHOPT
|
Isopropylmalate isomerase
|
Rhodopseudomonas
|
MSAKPTTLYDKIWNDHLVHEAEDGTCLLYIDRHLVHEVTSPQAFEGLRTAGRKVHAPEKTLAVVDHNVPTTDRSKPNPDPESAEQIAALAENARDFGITYYNEFDKRQGVVHVIGPEQGFTLPGTTIVCGDSHTSTHGAFGALAHGIGTSEVEHVLATQTLIQKKAKNMRVTVDGQLPDGVTAKDVILAIIGEIGTAGGTGYVLEYAGDAIRSLSMEGRMTVCNMSIEGGARAGLIAPDAKAYEFLKGRPLAPKGEAWDAALRYWETLRSDDGAHFDHELKLDAAALPPIVTWGTSPEDVISVTGRVPNPADIADEAKRLSKERALAYMGLTPGTKITDIKIDRMFIGSCTNGRIEDLRAAAKVAEGKTVNANVNAIIVPGSGLVKEQAEAEGLDKIFIKAGFEWREPGCSMCLAMNPDKLAPEERCASTSNRNFEGRQGFKGRTHLVSPAMAAAAAIAGHFVDIRDWH
|
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
|
B3Q851
|
Q47XB5
|
HIS5_COLP3
|
ImGP synthase subunit HisH
|
Colwellia
|
MTSAKNVIVDTGCANLSSVKFAVERLGFEVTITDDITIIQQAEKVIFPGVGSAKHAMKNIKAKNLEAALQGLTQPVLGFCLGMQLMTESSTEGKKSSTEGNNDDNTSHIVPCLNLIPTNVEPLKAQGNRLPHMGWNTLTQVSNHPIFKGISEGDYFYFVHSFAAPISEYTIASCEYGSTFSAAIAKDNFIGCQFHPERSSALGSKIIQNFLELDSTELNQELVNL
|
IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF.
|
Q47XB5
|
Q4K688
|
PTH_PSEF5
|
Peptidyl-tRNA hydrolase
|
Pseudomonas
|
MTAIKLIVGLGNPGTEYEQTRHNAGALFVERIAEKQGINLVADRKYFGLTGRFSHQGQDIRLLIPTTYMNRSGQAVAALAGFFRIKPEEILVAHDELDLPPGVAKLKTGGGHGGHNGLRDIIAQLGNQNTFHRLRLGIGHPGVASMVSNFVLGRAPRAEQEKLDASIDFALGVLPDIFAGEWNRAMKNLHSQKA
|
The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
|
Q4K688
|
A7GVN2
|
RL9_BACCN
|
50S ribosomal protein L9
|
Bacillus cereus group
|
MKVIFLKDVKGKGKKGEIKNVPDGYANNFLLKQGLAAEANNSNMKTLEAQKRKEEKEAAAELENAKKLKETLEKLTVELKAKSGEGGRLFGSITSKQIVDELQKTHKIKLDKRKFEMEDAIRSLGYTNVTVKLHPQVTATVKVHVSEQ
|
Binds to the 23S rRNA.
|
A7GVN2
|
Q54S02
|
3HAO_DICDI
|
3-hydroxyanthranilic acid dioxygenase
|
Dictyostelium
|
MLPPININKWIEENKSLLQPPVGAKLLYTDIDSTFVVMIVGGPNQRTDYHVNETDEFFYQFKGDMILKIVDKDGSFRDINIREGETFILPGNTPHSPQRYRDTIGLVIEKKRSSENIDKLLWFCDNKDCRKLLFSRSFHVDDLDLGKQLTPIINEFYGNEENRTCKHCNHISQKPTVNDYIQ
|
Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate.
|
Q54S02
|
A0A0M3KKZ0
|
GTF3_STRA6
|
Glucosyltransferase 3
|
Streptococcus
|
MRTYITNLNGHSITSTAQIAQNMVTDIAVSLGFRELGIHSYPIDTDSPEEMSKRLDGICSGLRKNDIVIFQTPTWNTTTFDEKLFHKLKIFGVKIVIFIHDVVPLMFDGNFYLMDRTIAYYNEADVLIAPSQAMVDKLQSYGLTVKKILVQGMWDHPTNITLQAVNHKKLVHFPGNPERFNFIKNWRIPTELHVYTDHNMQLPTTVVKEPYQSDEQLIMKMSEGGYGLVWMDDRDKQYQSLYCPYKLGAYIAAGIPVIIQKGIANQDIIEKNNLGFIIEKIDDISNIVESTTEEEYMEIVSDVRRFNPLVRQGYFTRKLLTDAVFSALNSM
|
Required for polymorphic O-glycosylation of the serine-rich repeat protein Srr2. Catalyzes the second step in glycosylation of the serine-rich repeat protein in this bacteria. Transfers glucose from UDP-glucose to the terminal GlcNAc moiety of 3-O-(N-acetyl-alpha-D-glucosaminyl)-L-seryl-[protein] which results from the first glycosylation step of Srr2; does not use other sugar nucleotides as substrates . Complements deletion of the gtf3 gene from S.parasanguinis strain FW213 .
|
A0A0M3KKZ0
|
P29189
|
ACP_GUITH
|
Acyl carrier protein
|
Guillardia
|
MNEQEIFEKVQTIISEQLGVDKSQVTKDANFANDLGADSLDTVELVMAIEEAFNIEIPDDAAEQISNLQQAVDFISQKVAA
|
Carrier of the growing fatty acid chain in fatty acid biosynthesis.
|
P29189
|
Q0V254
|
DML1_PHANO
|
Protein DML1
|
Parastagonospora
|
MREIVTLQFGERSNYLGTHFWNTQESYFTYPPEAESPVNHDILFRPGIAPDGSDTFTPRALIYDLKGAFGSMRKINALYEPEDDRSILDQPGVWPSKPIVQRTQPIPPSTYQEHLDNGLDPPALNISSVRYWSDYSRVFYHPKSIAQLSEFDVNDTLMPFEKWEVGKGLFEKLEREVDLVDRDLRPFVEECDGIQGLQIFTGVDDAWGGWASGWIERLRDEYGKMSIWTWGLGDQGANAAVGRERRLQQMVNASQSLQTLGEQSSVYIPISNSPTKTPSYLSLDATSLWHVGALQAIGLESMTISSRLRTSVGGRGNLQDLEDTINSTGKRRIGKFEMSIADPEVLSENYSKEMAQAEKTGSMTSRRTSEDDEELSSFDIDVFTRDYRAVSRSGKKEHVFGRAEVSRGDWNLTDDNEARDPHNRFNQGPTLQRYTAPILFPLLDSYPTSIFDVGSGLGTKLAVHAGLTTSTAVAGQIRAVEQIVKRLVGIEEREALCNGLQVLAEEYDEGWDSGTDSDDDG
|
Involved in the partitioning of the mitochondrial organelle and mitochondrial DNA (mtDNA) inheritance.
|
Q0V254
|
C6DHY7
|
PTH_PECCP
|
Peptidyl-tRNA hydrolase
|
Pectobacterium
|
MSSIKLIVGLANPGAEYAATRHNAGAWFVDRLADAYRQPLKEESKFFGYTSRLNLAGQDVRLLVPTTFMNLSGKAVAAMATFYRIQPDEILVAHDELDLLPGIAKLKLGGGHGGHNGLKDIISKLGNNPNFHRLRIGIGHPGDKSKVTGFVLGKPPTSEQTLIDDAIDEAVRCTEILMKEDMIKAMNRLHAFKPA
|
The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
|
C6DHY7
|
P0DD49
|
TRUB_STRPQ
|
tRNA-uridine isomerase
|
Streptococcus
|
MINGIINLKKEAGMTSHDAVFKLRKLLQEKKIGHGGTLDPDVVGVLPIAVGKATRVIEYMTEAGKVYEGQVTLGYSTTTEDASGEVVARSSLPAVLTEELVDQTMTTFLGKITQTPPMYSAVKVNGRKLYEYARAGESVERPRREVTISLFERTSPLNFTEDGLCRFSFKVACGKGTYVRTLAVDLGRALGVESHMSFLQRSASAGLTLETAYTLGEIADMVSKQEMSFLLPIEYGVADLPKMVIDDTELTEISFGRRLSLPSQEPLLAAFHGEKVIAILEKRDQEYKPKKVLI
|
Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
|
P0DD49
|
B0RDZ1
|
SYP_CLAMS
|
Prolyl-tRNA synthetase
|
Clavibacter
|
MSTRLSKLFVRTLREDPVDAEVASHRLLVRAGYIRRQAPGIFAWLPLGLRVKNKVEAIVREEMERIGAQEVHFPALLPAEPYQATGRYDEYGPGMFRLEDRKRAPMVLAPTHEEFFALLVKDLYSSYKDLPLSIYQIQDKYRDEARPRAGILRGREFTMKDAYSFDHTDAGLAVSYQAQRDAYERIFQRLGLEYVIVAADAGAMGGSKSEEFLHPTPIGEDTFVRSPGGYAANVEAFTTLVPESIPIEGQPAARVFDSPDTPTIQTLVDLANAREPREDGRAWTAADTLKNIVLALTHLDGTRELVVVGIPGDRDIDLKRAEVAFFPAEVEAANDGDLAKNPGLVKGYIGPWSPEGPVLGSTSSTKVRYVVDPRVVDGSSWITGANVAGKHVLSLVAGRDFTPDGVVEAADVRDGDPAPDGSGPISTARGTEIGHVFELGRKYAEALGLKVLDENGKLVTVTMGSYGIGITRNLALVAEATQDGRGLLWPASISPFDVHVVMTGKDPAVGTAAEELVDALDAAGLDVLFDDRPKVSPGVKFGDAELIGVPTVVIVGRGAVDGMAELWDRRTNERTPVALADVAGALTAAR
|
Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS.
|
B0RDZ1
|
Q2M1D1
|
UFSP2_DROPS
|
Probable Ufm1-specific protease 2
|
Sophophora
|
MLPKLKISAFLLKRLERVKQQSSGCLYGVFYGDGTLLLLSFNLSNVGQLNYEQIQHRFPAELDLCGLVKFGDCTDAEAHLNEVIKSVDITDNPILLKCELGTLVGMRASFFVHGKLEEVPYDVMDSEQLYNDFCFTRLQCGFYLQTAATPECVAKEMHVLRKRVADGNLVFKVPHTNIYIHSCGPMDNKLRGESRINDLVQAIPIPSGKENVVADKKKSKTAAQTQLAKHFGATGCEYDLINIDVMRIRTRDLLARDSPPHPALSIAVTTEEQTRAQVPLEIEAMAMLCKNTKLQRLYDVLIESICRALRLFEQSLNEHLAESEGGSLAVPRSHHFYPQGFGHFLSCAYLEGLGDDEPIMQERRKRLHRQFSLPVTRPYFRRANQCHFQGEVDDAPWTPLLNTHVGVRPSAVTDGKEYLVNGNYHYYHYLQQQVQDKGWGCAYRSLQTICSWFVLQGYTNAPIPTHLEVQKYLHKINDKPSSFVGSSQWIGSTEISMCLQGFLKVDSKILHVSSGAELPTIASELAMHFQTQGTPVMIGGGVLAHTIIGVDYCVQSGEVKFLILDPHYTGADELATIQIKGWCGWKSMDFWSKGSYYNLCMPQRPILY
|
Thiol protease which recognizes and hydrolyzes the peptide bond at the C-terminal Gly of UFM1, a ubiquitin-like modifier protein bound to a number of target proteins. Does not hydrolyze SUMO1 or ISG15 ubiquitin-like proteins.
|
Q2M1D1
|
Q8WW12
|
PCNP_HUMAN
|
PEST proteolytic signal-containing nuclear protein
|
Homo
|
MADGKAGDEKPEKSQRAGAAGGPEEEAEKPVKTKTVSSSNGGESSSRSAEKRSAEEEAADLPTKPTKISKFGFAIGSQTTKKASAISIKLGSSKPKETVPTLAPKTLSVAAAFNEDEDSEPEEMPPEAKMRMKNIGRDTPTSAGPNSFNKGKHGFSDNQKLWERNIKSHLGNVHDQDN
|
May be involved in cell cycle regulation.
|
Q8WW12
|
Q5HSH9
|
RF1_CAMJR
|
Peptide chain release factor 1
|
Campylobacter
|
MLASKLDPFLKRFEELNSLLSSSDIINDISKMTTLSKEQKNLEPIVLKAKEYLKTLDNIEENKALLNDPELGELAKEELKTLEELKPKLEEEIKILLLPKDPNDERNIFLEIRAGAGGDEASLFVGDLVKAYARYAENRGYKLEIVSSSEGSVGGFKEIIMLVKGTGAYSRLKYEGGTHRVQRVPQTESQGRVHTSAITVAVMPEVDDIEIEINPNDLKVDVMRSSGHGGQSVNTTDSAVRITHIPTGIVVVNQDGKSQHKNKESAMKVLKARLYEMQESERLAKESEARKSQVGSGDRSERIRTYNFPQNRISDHRINLTLYRLDAIMQDGLFDEIIEPLITHHQAQALQEQNL
|
Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
|
Q5HSH9
|
Q5YTQ0
|
Y3593_NOCFA
|
Nucleotide-binding protein NFA_35930
|
Nocardia
|
MTRVESNNTASQAPPSGAGTLEQQVEVVIVTGLSGAGRGTAAKVLEDLGWYVADNLPPELIGRMVELGAAADPPIRRLALVMDVRSRFFTGDLSVVADQLRALGLRTRVLFLEASDDVLIRRFGFARRRHPLQSESADGTLSAGIAVERVRLAGVKAAADLVIDTTELSIHQLHRKLEEAYGGGAPAALQLTVQSFGFKYGVPLDADMVLDVRFLPNPHWIPELREHSGQETVVSEYVLSRPGAQDYLHTCHHLVDLTTSGYRQEGKRYMTVAVGCTGGKHRSVAIAEALGELIGADTSAESADVVRVVHRDLGRE
|
Displays ATPase and GTPase activities.
|
Q5YTQ0
|
Q7VYS2
|
ISPH_BORPE
|
4-hydroxy-3-methylbut-2-enyl diphosphate reductase
|
Bordetella
|
MTAEVTAADAEVLLAQPRGFCAGVDRAIDIVERALELHGAPIYVRHEIVHNRYVVEDLRGKGAVFIDELDQAPAGAIVVFSAHGVSQAVRGEAEARGLRVFDATCPLVTKVHIEVARMRAAGREIVMIGHKGHPEVEGTLGQAQGGMYLVETVEDVAALQVSDPGNLAYVTQTTLSVDDAAAVAGALKARFPGIVEPKKSDICYATQNRQDAVKLLAPECDLVLVVGSTNSSNSNRLREVAERKGVAAYLIDGAHAIDPAWLQGRRSIGITAGASAPEVLVQQVVERVRELGAVSVRTMPGLEESVAFPLPKGLSRKIAQTESLE
|
Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
|
Q7VYS2
|
B7GIA3
|
MUTL_ANOFW
|
DNA mismatch repair protein MutL
|
Anoxybacillus
|
MGKIRKLDDALANKIAAGEVVERPASVVKELVENAIDAHSTIIEVELEEAGLAKIRVVDNGDGFEEEDCFLAFERHATSKIKDEADLFRIRTLGFRGEALPSIASVSHLELKTSTGEGPGTWLVLKGGELVQHGRTSSRKGTDITVSHLFFNTPARLKYMKTIHTELGHVVDVINRLALAHPHISFRLTHNGKQLFYTNGNGDVRQVLAAIYGLDVAKKMIAIHAETLDFTIDGYVALPEVTRASRNYMTTIVNGRYIKNYSLYKAIEEGYHTLLPIGRHPITFLNIMMDPLLIDVNVHPAKLEVRFSKETELNELVQQTIRQSFQKKTLIPEVTAPRVEKTKAEQQTFSFEHIVKESNTMSPRVTEIHRDQEKKTEERIVLEKSDEHVRDQDVTLLDVESVVPSEHVTGEMDQERIPPLYPIGQMHGTYILAQNENGLYIIDQHAAQERIKYEYFREKLATVTNELQPLLIPLTLTYSSSEYLLIESYRDQLAACGVFLEPFGHNSFIVRSHPQWFPKGEEVAIIEEMIKQVLEMKKVDMKQLREKAAIMMSCKQSIKANQFLRNDEIFALLESLRKTSDPFTCPHGRPIIIHFSTYELEKMFKRVM
|
This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex.
|
B7GIA3
|
Q3A413
|
SYE_SYNC1
|
Glutamyl-tRNA synthetase
|
Syntrophotalea
|
MSKLRVRFAPSPTGYLHIGGARTALFNFLLARKEQGTFVLRIEDTDVARSTQESVDAILQAMDWLGMSCDEGPIYQSDRFDLYRAKIDQLVEQGKAYRCYCTAEELEKKREAAMQDGRKPKYDGTCRQLQEVCDDKPYVIRFKAPQEGATTFHDRIKGDITFQNEELDDLIIQRTDGTPTYNFVVVVDDAEMGINLVLRGDDHINNTPRQIMLYKALGYPVPDFAHVPMILGADKSRLSKRHGATSVMAYKEMGYLPEALVNYLVRLGWSHGDQEIFTQDELTQLFSLDNIGKSASVFNPEKLIWLNSHYIKTGNPGRLAQLLAGHLAADGIDVANIADLEPIVVALQDRSKTLVDMAQQARCFFADDIQFDEKAAAKFLIEDNRFVFEALSAALESCDDWKEDILDGVFKGVLEATGLKFGKLAQPARVALVGGTTGPSICLIMQILGREKTLARLQGAMSRLGQ
|
Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
|
Q3A413
|
Q9LNC2
|
PLA18_ARATH
|
Phospholipase A1-IIalpha
|
Arabidopsis
|
MVEGIPKRWKVLSGQNKWKGLLDPLDPDLRRYIIHYGEMSQVGYDAFNWDRKSRYAGDCYYSKNRLLARTGFLKANPFRYKVTKYIYATASIKLPISFIVKSLSKDASRVQTNWMGYIAVATDQGKAMLGRRDIVVAWRGTLQPYEWANDFDFPLEPAISVFPVTDPKDNPRIGSGWLDIYTASDSRSPYDTTSAQEQVQGELKRLLELYKDEEISITFTGHSLGAVMSVLSAADLVYGKKNNININLQKKQVPITVFAFGSPRIGDHNFKNVVDSLQPLNILRIVNVPDVAPHYPLLLYSEIGEVLEINTLNSTYLKRSLNFRNYHNLEIYLHGMAGMQDTDGVFKLEIGRDISLVNKGLDALKDEYLVPSTWRCLANKGMLQMDDGTWKLDVHRRDHDDDVDADDNDDSSTSNQLQELNTD
|
Acylhydrolase that catalyzes the hydrolysis of phospholipids at the sn-1 position.
|
Q9LNC2
|
Q1QSW3
|
SSRP_CHRSD
|
Small protein B
|
Chromohalobacter
|
MAKKKGNLGSSTIAQNKKARFEYHIDETFEAGLSLAGWEVKSLRAGKAQLTDTYILIKNGEAWLLGSHITPLNTVSTHVVADPSRTRKLLLHRKEIAKIFSRTQDKGHTCVPLKLYWKKNLVKCELALVRGKKLHDKRATEKARDWNREKARIMRAH
|
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.
|
Q1QSW3
|
A5GTX8
|
KATG_SYNR3
|
Peroxidase/catalase
|
unclassified Synechococcus
|
MSMAEMRCPFSGHGAATTPASATTNQHWWPEQINLGLLHQHNPAANPLGSNFDYRQAFNSLDLNAVKADLMALMTDSQSWWPADWGHYGGLFIRMAWHSAGTYRLADGRGGAGHGNQRFAPLNSWPDNTNLDKARRLLWPIKAKYGSNLSWADLIILAGNCALESMGLPTAGFAGGREDIWEPEDDIYWGSETSWLSDERHDNDGAIESPLAATEMGLIYVNPEGPHGEPDPVASGREVRDTFARMGMNNEETVALVAGGHTFGKAHGAAPSAHLGADPEGAALEQLGLGWQNTYASGCGADTITSGIEGAWKPNPTRWDQGYFEMLFGYEWELHQSPAGAWQWHPKDVKAEHMIPDAHVPGRSAPPMMTTADLSLRFDPVYEPIARRFLGDPQAFGNAFAQAWFKLTHRDLGPRSCYLGADVPEAVMSWQDPLPTTSHPTIDAPAVDALKQELLNTGLSHGELISTAWASAASFRQSDRRGGANGARLRLQPQCNWELNNPEQLKRVLSVLEAVQMRFNQQHQGGMQVSLADLIVLSGSAAVEQAMAATGQRCRVRFTPGRVDASAEQTDNASFNALKPIADGFRNYLRSDLPLKAEQLLVDRAQQLHLSAPEMTALIGGFRVLGLNWDGSDIGVFTSRPGQFSNDFFVNLLDMSTQWSPVEGHSNLYQGIDTETKQPRWRASRVDLVFGSHAQLRAIAEVYGQAGGSARLAADFSAAWSKVMELDRFDLL
|
Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity.
|
A5GTX8
|
Q46LE5
|
ACCD_PROMT
|
Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta
|
Prochlorococcus
|
MSLFDWFADRRKGQFVGKVTQESEESDGLWEKCPECGQVVYRKDLIDNCSVCSNCGHHNRIDSKERIRLISDPNTFKSINNHLTPVDPLGFKDRRAYADRLRESQAGTGLKDGVLTGTCEVNSIPMALAVMDFRFMGGSMGSVVGEKITRLIEHSTKEKLPLLIVCASGGARMQEGMLSLMQMAKISGALERHRDAQLLYMPLLTHPTTGGVTASFAMLGDLILAEPKALIGFAGRRVIEQTLREKLPDNFQTAEYLQDHGFVDTIVPRTELKETLAKILRLHKTQVVKLQTNA
|
Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.
|
Q46LE5
|
P22367
|
MSAS_PENPA
|
6-methylsalicylic acid synthase
|
Penicillium
|
MHSAATSTYPSGKTSPAPVGTPGTEYSEYEFSNDVAVVGMACRVAGGNHNPELLWQSLLSQKSAMGEIPPMRWEPYYRRDARNEKFLKNTTSRGYFLDRLEDFDCQFFGISPKEAEQMDPQQRVSLEVASEALEDAGIPAKSLSGSDTAVFWGVNSDDYSKLVLEDLPNVEAWMGIGTAYCGVPNRISYHLNLMGPSTAVDAACASSLVAIHHGVQAIRLGESKVAIVGGVNALCGPGLTRVLDKAGAISSDGSCKSFDDDAHGYARGEGAGALVLKSLHRALLDHDNVLAVIKGSAVCQDGKTNGIMAPNSVAQQLAANNALSAANIDPHTVRYVEAHATSTPLGDPTEISAIASVYGADRPADDPCYIGSIKPNIGHLEAGAGVMGFIKAVLAIQKGVLPPQANLTKLNSRIDWKTAGVKVVQEATPWPESDPIRRAGVCSYGYGGTVSHAVIEEFSPILQPDPLGNGAVSGPGLLLLSGPQEKRLALQAKTLRDWMTAEGKDHNLSDILTTLATRRDHHDYRAALVVDDYRDAEQVLQSLANGVDHTFTTQSRVLGSDISKDVVWVFSGHGAQWPDMGKQLIHNPVFFAAIQPLDELIQAEIGLSPIELLRTGDFESSDRVQILTYVMQIGLSALLQSNGITPQAVIGHSVGEIAASVVAGALSPAEGALIVTRRALLYRQVMGKGGMILVNLPSAETEEILGSRSDLVVAIDSSPSSCVVAGDKELVAETAEALKARGVKTFTVKSDIAFHSPTLNGLVDPLRDVLAETLSPVSPNVKLYSTALADPRGQDLRDVEYWAGNMVNRVRLTSAVKAAVEDGYRLFLEVSTHPVVSHSINETLMDAGMEDFAVIPTLLRKKPTEKHILHSIAQLHCRGAEVNWAAQMPGRWATGVPTTTWMHKPIWRKIETAPLHTGLTHDVEKHTLLGQRIPVPGTDTYVYTTRLDNDTKPFPGSHPLHGTEIVPAAGLINTFLKGTGGQMLQNVVLRVPVAINAPRSVQVVVQQDQVKVVSRLIPSEPSQLDDDASWVTHTTAYWDRKVAGSEDRIDFAAVKSRLVTKLADNFSIDYLDKVGVSAMGFPWAVTEHYRNDKEMLARVDVNPAISGDAPLPWDSSSWAPVLDAATSVGSTIFPTPALRMPAQIERVEVFTSQDPPKISWLYVQEASDSVPTSHVSVVSEAGEVLAKFTAMRFSEIEGTPGVSGSMESLVHQIAWPPATPAEEPLSIETVILVSPDATTRALYAASLPTRVNSFQFSSTQEFFSNASSLPLEKGTVVTYIPGEVASLAEVPAASESFTWNLLELIKFTVNGSLPIKVFTLTANIGEGQTPTALAQSPLYGLARVIASEHPDLGTLIDVEEPVIPLSTMRYIQGADIIRINDGIARTSRFRSLPRNKLLPASEGPRLLPRPEGTYLITGGLGVLGLEVADFLVEKGARRLLLISRRALPPRRTWDQVSEDLQPTIAKIRLLESRGASVHVLPLDITKPDAVEQLTTALDRLSLPSVQGVVHAAGVLDNELVMQTTRDAFNRVLAPKIAGALALHEVFPPKSVDFFVMFSSCGNLVGFTGQASYGSGNAFLDTLATHRARLGDAAVSFQWTSWRGLGMGASTDFINAELESKGITDVTRDEAFAAWQHLAKYDMDHGVVLRSRAFEDGEPIPVSILNDIAVRRVGTVSNTSPAAAGSSDAVPTSGPELKAYLDEKIRGCVAKVLQMTAEDVDSKAALADLGVDSVMTVTLRRQLQLTLKIAVPPTLTWSHPTVSHLAVWFAEKLAK
|
This multifunctional enzyme is a polyketide synthase. It catalyzes a total of 11 steps by seven different component enzymes, in the biosynthesis of the antibiotic patulin.
|
P22367
|
Q54I71
|
AARA_DICDI
|
Suppressor of amiB protein 16
|
Dictyostelium
|
MNDCGSLFNKKLFKMNLLFKHLKLQQHLKLQQKPLLNNSSINNNINNNNNNNNNNNSNNDSNNTNTNIFNNSFLNSDLIERLIIKFTIGYLKNNITEDYIEQILLENQNNFIKSTTTSNYILEENNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNSSSSSSSILSKFNKLEEDNELELQKKQKQQLEQQEEELFNQFNFLEGIEDQNDFLSEQETIQKIKFLIKMTAKSMSNYSSPNTLIPSVSKTYISPFGLSSNGSTNNHNNNNNNNHHHHSNNGNLIESSNNVNNQLNVSNYNNNNSNHYDENNQFDIFLIPTEMLVHLLSFLSANDLWRISLTCKRIWYIVDVFKFWELLFEQTCPRIYYAMQFNSRWSNPTSFQSKMILCYIDRLPTDNYKNFDKSDESGQIKKIIGVMNENLHNPMILRETCYILKRLSYRQRKEDEHESLIARYGGISLILQAMKNHPYDAGVQEDACGALGNLTCDSPNNMGLYSNDNYLSVVEQGGIQLILQAMKNHMMNPGVQYNTSFVLRNLARNDVSESRVAIEGGIQSIATAMKNHPNHIGIQTQGCGALRNLGCNDSNKVLSAKEGGIGLILRAMRSFSSHPDLQLNGCGALRNLARNEDNKNMISRQNGIQLVLGAMSNHPDDPDVQDEGCAALINLAYQDEANEETIAREGGINLILKAMRNHPFHSGVQMQGRGALKNLSCNPKNKLTIARSGGIELMNIAMQNHPNFANRFLELSRILQVALEDGNI
|
Required to regulate pattern formation during multi-cellular stages of development and for the formation of adherens junctions. Plays a structural role during the regulation of stalk formation. Involved in cell signaling. Required for spore-cell differentiation. Overexpression increases number and size of cell junctions and reduces spore-cell formation.
|
Q54I71
|
B2A524
|
NADK_NATTJ
|
ATP-dependent NAD kinase
|
Natranaerobius
|
MRSVGLIPNIQKDQVAEITSRMYKILSEHDIDVYLTHEGADLIGTESAGVSSDVMGEVAEMIIILGGDGTILKAAREYAPYDIPLLGINLGKMGFLAEIEANEVMAYLESLLTGNYTIEERMMLDATVLRDRKEITTFSALNDVIIAKGPFSRIIEVETKVGGNYLETYPGDGLIVTSPTGSTGYSFSAGGPIISSNLEVMMITPICPHLMHNRSVIISSDEVVTAKMKTNYAVVVLTVDGQQGFTLQDGDEIKVKKSNYKTKLVKLRRRSFYQLLNEKLTGGQEV
|
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.
|
B2A524
|
Q15YR1
|
RLMG_PSEA6
|
rRNA (guanine-N(2)-)-methyltransferase RlmG
|
Pseudoalteromonas
|
MKTELTLLDHSYELLRYPAENQHVSWQAWDSADEYLMEYVAQNITDLNGLNIHIYNDDFGALGVWFATNNAPLWISDSFVAHKALALNLERNHLPIENVNVQNSLYKANQKADLVLIKVPKTLALLEQQLIDLQSSVTPETRIIAAGKANAIQKSTLALFEKHLGLTTTSLAKKKSRLIFCQYDGVKQSVSPYPTKWKTDNTQFIMSNLANVFSRQQLDIGARVLLAHLPDANHKCIVDLGCGNGVLGLHVLHKSPGAHVIFVDESFMAIASAKMNIEQNMPDKLDQCKFIVSNCLDECLSSGENEATVDIVLCNPPFHQQNTITDHIALQMFKDSKRILKHAGELRVVGNRHLDYPQTIKRLFGHYKVLASDRKFSILSAIKK
|
Specifically methylates the guanine in position 1835 (m2G1835) of 23S rRNA.
|
Q15YR1
|
Q3K2R2
|
RLMN_STRA1
|
tRNA m2A37 methyltransferase
|
Streptococcus
|
MPKKTDTPDYKPSIYSLTRDELIAWAIEHGEKKFRASQIWDWLYKKRVQSFDEMTNISKDFIALLNENFVVNPLKQRIVQESADGTVKYLFELPDGMLIETVLMRQHYGLSVCVTTQVGCNIGCTFCASGLIKKQRDLNNGEITAQIMLVQKYFDERGQGERVSHIVVMGIGEPFDNYTNVLKFLRTVNDDNGLAIGARHITVSTSGLAHKIREFANEGVQVNLAVSLHAPNNELRSSIMRINRSFPLEKLFAAIEYYIETTNRRVTFEYIMLNGVNDTPENAQELADLTKKIRKLSYVNLIPYNPVSEHDQYSRSPKERVEAFYDVLKKNGVNCVVRQEHGTDIDAACGQLRSNTMKRDRQKAKVGQ
|
Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs.
|
Q3K2R2
|
Q9M158
|
STR4_ARATH
|
Sulfurtransferase 4
|
Arabidopsis
|
MEALKTATFSPMSVLSEKRSEPRKPFSLPNLFPPKSQRPISQESFLKRFNGGLALLTSVLSSATAPAKSLTYEEALQQSMTTSSSFDSDGLIEGISNFVTDNPLVIAGGVAALAVPFVLSQVLNKKPKSWGVESAKNAYTKLGTDDNAQLLDIRATADFRQVGSPNIKGLGKKAVSTVYNGEDKPGFLKKLSLKFKDPENTTLYILDKFDGNSELVAELVALNGFKSAYAIKDGAEGPRGWLNSSLPWIEPKKTLSLDLSSLTDSISGVFGESSDGVSVALGVAAAAGLSVFAFTEIETILQLLGSAALVQLAGKKLLFAEDRKQTLKQVDEFLNTKVAPKELVDELKEIGKALLPQSTSNKALPAPATVTAEAESATATTTTVDKPVPEPETVAATTTTVDKPVPEPEPVPEPVPVPAIEAAVAAQVITEPTETEAKPKPHSRPLSPYASYPDLKPPSSPMPSQP
|
Rhodanese domain-containing protein required for anchoring ferredoxin--NADP reductase to the thylakoid membranes and sustaining efficient linear electron flow (LEF).
|
Q9M158
|
B9E8F4
|
UPP_MACCJ
|
UPRTase
|
Macrococcus
|
MAKVHVFDHPLIQHKLSYIREESTGTKEFRELVDEVGMLMAYEVTRDLELDDVQIKTPVTEMTAKRLSGKKIAVVPILRAGLGMTEGVLKMIPAARVGHIGLYRDPETLQPVEYFAKMPQDIEERDFIVVDPMLATGGSAIEAINSLKKRGAVKIRFMCLVAAPEGVEALQKAHPDVDIYIAGLDEKLNDHGYIVPGLGDAGDRLFGTK
|
Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
|
B9E8F4
|
B8DE40
|
PRMA_LISMH
|
Ribosomal protein L11 methyltransferase
|
Listeria
|
MEWSEVEVHTTNEAVEPVANVLTEFGAAGVSIEDVADFLREREDKFGEIYALKREDYPEDGVIIKAYFLKTSEFVEQIPEIEQTLKNLTTFDIPLGKFQFVVNDVDDEEWATAWKKYYHPVQITDRITIVPSWESYTPSANEIIIELDPGMAFGTGTHPTTQLCIRALSDYLQPGDEVIDVGTGSGVLSIASAKLGAKSILATDLDEIATRAAEENITLNKTEHIITVKQNNLLQDINKTNVDIVVANILAEVILLFPEDVYRALKPGGIFIASGIIEDKAKVVEEALKNAGLIIEKIEQQGDWVAIISKRGVE
|
Methylates ribosomal protein L11.
|
B8DE40
|
Q9XZ56
|
4EBP_DROME
|
4E-binding protein Thor
|
Sophophora
|
MSASPTARQAITQALPMITRKVVISDPIQMPEVYSSTPGGTLYSTTPGGTKLIYERAFMKNLRGSPLSQTPPSNVPSCLLRGTPRTPFRKCVPVPTELIKQTKSLKIEDQEQFQLDL
|
Repressor of translation initiation that regulates eIF4E1 activity by preventing its assembly into the eIF4F complex . Hypophosphorylated form competes with eIF4G1 and strongly binds to eIF4E1, leading to repress translation . In contrast, hyperphosphorylated form dissociates from eIF4E1, allowing interaction between eIF4G1 and eIF4E1, leading to initiation of translation . Acts as a regulator of various biological processes, such as innate immunity, cell growth or synaptic transmission . Acts downstream of phosphoinositide-3-kinase (PI3K) to regulate cell growth . Extends lifespan upon dietary restriction by regulating the mitochondrial translation . Acts as a regulator of lifespan in response to cold by regulating the mitochondrial translation . Acts as a negative regulator of presynaptic release of neurotransmitter in motor neurons: Thor expression is induced in response to insulin signaling, leading to prevent of translation of complexin (cpx), a protein known to regulate the exocytosis of synaptic vesicles . Acts as a negative regulator of synaptic strength at the neuromuscular junction: Thor expression in response to acute fasting prevents translation, thereby suppressing retrograde synaptic enhancement .
|
Q9XZ56
|
A8FE66
|
ODO1_BACP2
|
Alpha-ketoglutarate dehydrogenase
|
Bacillus
|
MFQNDVKQPLSWEEFHGPNLGYVLELYDQYVQDPTSVDEDLRGIFDELGAPPSEMKEEIGKKENSVVTSEQIQKIASVVKLAEDIRTYGHLNASVNPLRKEKELQELFPLKEYGLTEEDVKNIPISIISPDAPKHISNGIEAINHLRNTYKRTISFEFDHVHDFEERNWLSKSIESGELFKKKPADKLVSVFKRLTEVEQFEQFLHKTFVGQKRFSIEGLDALVPVLDEIISESVTQGTSNINIGMAHRGRLNVLAHVLGKPYEIIFSEFQHAPNKELVPSEGSIGISYGWTGDVKYHLGADRQIKDEDTKSARVTLANNPSHLEFIDPIIEGSTRAAQELRTQKGYPAQDVEKALAILIHGDAAFPGEGIVAETLNLSQLVGYQVGGTIHIIANNMIGFTTESNESRSTKYASDLAKGFEIPIVHVNADDPEACLAAVQLAVEYRKRFKKDFLIDLIGYRRYGHNEMDEPSTTQPMLYDAVRKHKTVKNIFADKLVSEGLLTKEQREEIEQAVATRIEEAYQKVPSKKEHTIQEIELPEPVSNGFPAVDTSVEFDVLRKLNEELISWPDDFQVFGKLKRILEKRAKVFTDDRKVEWSLGEALAFASILKDGTPIRMTGQDSERGTFAQRNLVLHDSQTGNEFIALHELSDANASFTVHNSPLSEGSVIGFEYGYNVYSPETLVIWEAQFGDFANAAQVYFDQFISAGRAKWGQKSGLVMLLPHGYEGQGPEHSSGRTERFLQSAAENNWTVANLTSAAQYFHILRRQAKMLLREEIRPLVIMTPKSLLRNPNSLSEVQELTDGQFQPVLEQPGLVHDHEKVSRLVLSSGKVSIDISDRFTQMEEPKDWLHIARVEQLYPFPAKDIKAILSKLTNLEEIVWTQEEPQNMGAWGYIEPYLREIAPEKVKVRYIGRRRRSSTAEGDPTVHKKEQERIVSDSLTRKN
|
E1 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the decarboxylation of 2-oxoglutarate, the first step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2).
|
A8FE66
|
B7LK48
|
YIDC_ESCF3
|
Membrane protein YidC
|
Escherichia
|
MDSQRNLLVIALLFVSFMIWQAWEQDKNPQPQAQQTTQTTTTAAGSAADQGVPASGQGKLISVKTDVLDLTINTRGGDVEQALLPAYPKELNSTQPFQLLETSPQFIYQAQSGLTGRDGPDNPANGPRPLYNVEKDAYVLAEGQNELQVPMTYTDAAGNTFTKTFILKRGDYAVNVNYNVQNAGEKPLEISTFGQLKQSITLPPYLDTGSSNFALHTFRGAAYSTPDEKYEKYKFDTIADNENLNISSKGGWVAMLQQYFATAWIPHNDGTNNFYTANLGNGIAAIGYKSQPVLVQPGQTGAMNSTLWVGPEIQDKMAAVAPHLDLTVDYGWLWFISQPLFKLLKWIHSFVGNWGFSIIIITFIVRGIMYPLTKAQYTSMAKMRMLQPKIQAMRERLGDDKQRISQEMMALYKAEKVNPLGGCFPLLIQMPIFLALYYMLMGSVELRQAPFALWIHDLSAQDPYYILPILMGVTMFFIQKMSPTTVTDPMQQKIMTFMPVIFTVFFLWFPSGLVLYYIVSNLVTIIQQQLIYRGLEKRGLHSREKKKS
|
Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins.
|
B7LK48
|
A4XHY7
|
GATC_CALS8
|
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C
|
Caldicellulosiruptor
|
MITRNDVEYVANLARLTLTEEEIEKMTKELGAIIEFANKLSDLDTEGIEPTAHVLNLYNVFRSDEVKPSYPREEILKNAPSHDDVCIKVPKIVE
|
Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
|
A4XHY7
|
Q28540
|
IL7_SHEEP
|
Interleukin-7
|
Ovis
|
MFHVSFRYIFGIPPLILVLLPVASSDCDFSGKDGGAYQNVLMVSIDDLDNMINFDSNCLNNEPNFFKKHSCDDNKEASFLNRAARKLKQFLKMNISDDFKLHLSTVSQGTLTLLNCTSKGKGRKPPSLGEAQPTKNLEENKSLKEQRKQNDLCFLKILLQKIKTCWNKILRGITEH
|
Hematopoietic cytokine that plays an essential role in the development, expansion, and survival of naive and memory T-cells and B-cells thereby regulating the number of mature lymphocytes and maintaining lymphoid homeostasis. Mechanistically, exerts its biological effects through a receptor composed of IL7RA subunit and the cytokine receptor common subunit gamma/CSF2RG. Binding to the receptor leads to activation of various kinases including JAK1 or JAK3 depending on the cell type and subsequently propagation of signals through activation of several downstream signaling pathways including the PI3K/Akt/mTOR or the JAK-STAT5.
|
Q28540
|
A5N8N4
|
PAND_CLOK5
|
Aspartate 1-decarboxylase alpha chain
|
Clostridium
|
MQLNMLKSKIHRATVTEANLNYVGSITIDRELMESAHIIEYEKIQVVDIDNGNRLETYVIAGEKGSKVICLNGAAARHVQPGDKVILMTYCQMDEEEAKIHKPIVIFLDENNSIFQITDYEKHGQVK
|
Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
|
A5N8N4
|
P10410
|
TOXK_CYBMR
|
Killer toxin HM-1
|
Cyberlindnera
|
MKFSFVYGLTGFLAATSSALPSEILSTGYERSALEKRGDGYLIMCKNCDPNTGSCDWKQNWNTCVGIGANVHWMVTGGSTDGKQGCATIWEGSGCVGRSTTMCCPANTCCNINTGFYIRSYRRVE
|
This toxin kills sensitive strains of yeast. It inhibits beta-1,3-glucan synthesis.
|
P10410
|
Q3K4M4
|
ARGB_PSEPF
|
NAG kinase
|
Pseudomonas
|
MTLERDAAANTAKVLSEALPYIRRYVGKTLVIKYGGNAMESEELKTGFARDIVLMKAVGINPVVVHGGGPQIGDLLKRLSIESHFVDGMRVTDAATMDVVEMVLGGQVNKSIVNLINRHGGSAIGLTGKDAGLIRAKKLTVTRQTPEMTQPEIIDIGHVGEVVGINTELLNLLVKGNFIPVIAPIGVGENGESYNINADLVAGKVAEALKAEKLMLLTNIAGLMDKSGTVLTGLSTQQVDDLIADGTIYGGMLPKIRCALEAVQGGVGSSLIIDGRVPNAILLEIFTDTGVGTLISNRKRP
|
Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
|
Q3K4M4
|
Q96VP3
|
CYC_COCLU
|
Cytochrome c
|
Curvularia
|
MGFEQGDAKKGANLFKTRCAQCHTLKAGEGNKIGPELHGLFGRKTGSVAGYSYTDANKQKGIEWNHDTLFEYLENPKKYIPGTKMAFGGLKKPKDRNDLITFLEQETK
|
Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.
|
Q96VP3
|
A4QKB3
|
RBL_BARVE
|
Ribulose bisphosphate carboxylase large chain
|
Barbarea
|
MSPQTETKASVGFKAGVKEYKLTYYTPEYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVPGEETQFIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALAALRLEDLRIPPAYTKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKSQAETGEIKGHYLNATAGTCEEMIKRAVFARELGVRIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRLSGGDHIHAGTVVGKLEGDRESTLGFVDLLRDDYVEKDRSRGIFFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLAIEGNEIIREACKWSPELAAACEVWKEIRFNFPTIDKLDGQA
|
RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.
|
A4QKB3
|
Q9LXU0
|
CLE40_ARATH
|
CLE40p
|
Arabidopsis
|
MAAMKYKGSVFIILVILLLSSSLLAHSSSTKSFFWLGETQDTKAMKKEKKIDGGTANEVEERQVPTGSDPLHHKHIPFTP
|
Extracellular signal peptide secreted by differentiated root cells that regulates root cell fate. Acts with ACR4 as a ligand-receptor pair in a signal transduction pathway, coordinating movement of the root tip and organization of cell divisions in the root meristem. Promotes cell differentiation in the distal root meristem in a dose-dependent manner, especially the transition from columella stem cells (CSC) daughters into columella cells (CCs). Induces ACR4 expression in root quiescent center (QC). Involved in WUX5 QC-specific expression pattern regulation. Regulates the transition of protophloem cells from proliferation to differentiation, thus impinging on postembryonic growth capacity of the root meristem; this signaling pathway requires CRN and CLV2 .
|
Q9LXU0
|
Q49ZB2
|
MDEP_STAS1
|
Staphylococcal efflux pump A
|
Staphylococcus
|
MKYLRYLLTTLIVLSVFIISGAIFLTFLGFGLYGLSRILIYFHLAYFGYNKSFYDNLIYYGSYIVLGYFNLFIVENLMDYFRKKLPENLYFQGLTFQLITFSVTTLLFYFIVHIHYTYIDIDFWVIVLIIGVLFICKEIFYPDSKNLNQKNK
|
Involved in multidrug efflux.
|
Q49ZB2
|
Q9TKX2
|
PSBZ_NEPOL
|
Photosystem II reaction center protein Z
|
Nephroselmis
|
MTFIFQLALFALVALSFLLVVGVPVAFAAPEGWNVTKGYVFQGVSAWFALVFTVGVLNSLVA
|
Controls the interaction of photosystem II (PSII) cores with the light-harvesting antenna.
|
Q9TKX2
|
A0A075B6J6
|
LV322_HUMAN
|
Immunoglobulin lambda variable 3-22
|
Homo
|
MAWATLLLPLLNLYTGSVASYELTQLPSVSVSPGQTARITCSGDVLGENYADWYQQKPGQAPELVIYEDSERYPGIPERFSGSTSGNTTTLTISRVLTEDEADYYCLSGDEDNPS
|
V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition . Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens . The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen .
|
A0A075B6J6
|
B2INF6
|
TRMD_STRPS
|
tRNA [GM37] methyltransferase
|
Streptococcus
|
MKIDILTLFPEMFSPLEHSIVGKAREKGLLDIQYHNFRENAEKARHVDDEPYGGGQGMLLRVQPIFDSFDAIEKKNPRVILLDPAGKQFDQAYAEDLAQEEELIFICGHYEGYDERIKTLVTDEISLGDYVLTGGELAAMTMIDATVRLIPEVIGKESSHQDDSFSSGLLEYPQYTRPYDYRGMVVPDVLMSGHHEKIRQWRLYESLKKTYERRPDLLEHYQLTVEEEKMLAEIKENKE
|
Specifically methylates guanosine-37 in various tRNAs.
|
B2INF6
|
A6LPB1
|
DNAA_CLOB8
|
Chromosomal replication initiator protein DnaA
|
Clostridium
|
MDADLKNLWDKTLDIIKSELSEVSFNTWIKSCEPLSISSNTLKISVPNSFTQDILDKRYKDLVANSIKAVCSKLYTIEFIIMSEIYEKEEIKSSSNQKSKAIVVNDEMSSTLNPKYTFNSFVIGNSNRFAHAASLAVAESPAKAYNPLFIYGGVGLGKTHLMHAIGHYILDGNPNAKVVYVSSEKFTNELINAIKDDKNEEFRNKYRNVDILLIDDIQFIAGKERTQEEFFHTFNALHDANKQIILSSDRPPKEIPTLEDRLRSRFEWGLIADIQVPDFETRMAILKKKADVENLNVANEVMGYIATKIKSNIRELEGALIRIIAYSSLTNREVTVDLATEALKDIISKKQGKHVTIDLIQDVVSSYFNLRVEDLKSQRRTRNVAYPRQIAMYLSRKLTDMSLPKIGEEFGGRDHTTVIHAYEKISENLKTDDSLQSTVNDITKKLTQN
|
Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids.
|
A6LPB1
|
P22397
|
PSPC_CANLF
|
Pulmonary surfactant-associated proteolipid SPL(Val)
|
Canis
|
GIPCFPSSLKRLLIIVVVIVLVVVVIVGALLMGL
|
Pulmonary surfactant associated proteins promote alveolar stability by lowering the surface tension at the air-liquid interface in the peripheral air spaces.
|
P22397
|
P52710
|
CBPY_KOMPG
|
Carboxypeptidase YSCY
|
Komagataella
|
MILHTYIILSLLTIFPKAIGLSLQMPMALEASYASLVEKATLAVGQEIDAIQKGIQQGWLEVETRFPTIVSQLSYSTGPKFAIKKKDATFWDFYVESQELPNYRLRVKRNNPEVLKVDFTKQYSGYLDVEADDKHFFYWFFESRNDPQNDPIILWLNGGPGCSSLTGLFFELGSSRINENLKPIFNPYSWNGNASIIYLDQPVNVGFSYSSSSVSNTVVAGEDVYAFLQLFFQHFPEYQTNDFHIAGESYAGHYIPVFADEILSQKNRNFNLTSVLIGNGLTDPLTQYRYYEPMACGEGGAPSVLPADECENMLVTQDKCLSLIQACYDSQSAFTCAPAAIYCNNAQMGPYQRTGKNVYDIRKECDGGSLCYKDLEFIDTYLNQKFVQDALGAEVDTYESCNFEINRNFLFAGDWMKPYHEHVSSLLNKGLPVLIYAGDKDFICNWLGNRAWTDVLPWVDADGFEKAEVQDWLVNGRKAGEFKNYSNFTYLRVYDAGHMAPYDQPENSHEMVNRWISGDFSFH
|
Involved in degradation of small peptides.
|
P52710
|
Q8XBJ8
|
CYSA_ECO57
|
Sulfate-transporting ATPase
|
Escherichia
|
MSIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQHYALFRHMTVFDNIAFGLTVLPRRERPNAAAIKAKVTKLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDQVWREPATRFVLEFMGEVNRLQGTIRGGQFHVGAHRWPLGYTPAYQGPVDLFLRPWEVDISRRTSLDSPLPVQVLEASPKGHYTQLVVQPLGWYNEPLTVVMHGDDAPQRGERLFVGLQHARLYNGDERIEPRDEELALAQSA
|
Part of the ABC transporter complex CysAWTP involved in sulfate/thiosulfate import. Responsible for energy coupling to the transport system.
|
Q8XBJ8
|
Q95083
|
PSA5_DROME
|
Proteasome subunit alpha type-5
|
Sophophora
|
MFLTRSEYDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGICTPEGVVLAVEKRITSPLMVPSTVEKIVEVDKHIGCATSGLMADARTLIERARVECQNHWFVYNERMSIESCAQAVSTLAIQFGDSGDSDGAAAMSRPFGVAILFAGIEAGQPQLWHMDPSGTFVRHGAKAIGSGSEGAQQNLQDLFRPDLTLDEAIDISLNTLKQVMEEKLNSTNVEVMTMTKEREFYMFTKEEVEQHIKNIA
|
The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.
|
Q95083
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.